{
 "cells": [
  {
   "cell_type": "markdown",
   "metadata": {},
   "source": [
    "# Automated Ligand Design Pipeline\n",
    "\n",
    "> ### In this tutorial we will cover:\n",
    "> - how we can use BuildAMol to randomly assemble fragments from a library into larger molecules\n",
    "> - how we can use BuildAMol in an automated ligand design framework"
   ]
  },
  {
   "cell_type": "markdown",
   "metadata": {},
   "source": [
    "Automated design for protein ligands is a very active field of research. Many dedicated software solutions exist, leveraging machine learning, deep learning, fragment-based assembly, graph-based, SMILES-based, diffusion-based, and all kinds of techniques in order to produce structures of small molecules that hopefully bind a specific protein target. \n",
    "\n",
    "BuildAmol can be used in automated setups to generate molecules. However, it is not designed to perform any kind of analysis on proteins and alike. In this tutorial we will develop a pipeline that will use BuildAmol to generate molecular candidate structures and then forwards these to the library `dockstring`[https://github.com/dockstring/dockstring/tree/main] which will evaluate the docking potential of a given candidate.\n",
    "Using these two primary tools we will make a simple ligand-design system.\n",
    "\n",
    "As a disclaimer at the start, this tutorial does **not** produce a fully-fledged production ready ligand-design tool! It merely provides some insight and inspiration of how one might use BuildAMol in such a context! Nothing that we will be developing in this tutorial is extensively tested or optimized for performance, so keep this in mind while following along. Actually, since dockstring only works with SMILES the whole code will technically perform a bunch of conversions back-and-forth that would be totally unnecessary, but that's just a side note..."
   ]
  },
  {
   "cell_type": "code",
   "execution_count": 1,
   "metadata": {},
   "outputs": [],
   "source": [
    "import buildamol as bam\n",
    "import numpy as np"
   ]
  },
  {
   "cell_type": "markdown",
   "metadata": {},
   "source": [
    "## Getting a fragment library\n",
    "Ligands are assembled from fragments such as individual benzene rings or ethanol in hopes of finding a combination of fragments that will suite the requirements. In this tutorial we will load a fragment library that was prepared in BuildAMol before. If you are curious how that was done, check out the \"Fragment Library\" tutorial in the documentation! "
   ]
  },
  {
   "cell_type": "code",
   "execution_count": 2,
   "metadata": {},
   "outputs": [
    {
     "data": {
      "text/plain": [
       "201"
      ]
     },
     "execution_count": 2,
     "metadata": {},
     "output_type": "execute_result"
    }
   ],
   "source": [
    "library = bam.read_compounds(\"./files/fragments.json\")\n",
    "len(library)"
   ]
  },
  {
   "cell_type": "markdown",
   "metadata": {},
   "source": [
    "Great! So we have loaded a small fragment library of 96 fragments. Let's look at one of them:"
   ]
  },
  {
   "cell_type": "code",
   "execution_count": 3,
   "metadata": {},
   "outputs": [
    {
     "data": {
      "image/png": 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",
      "text/plain": [
       "<PIL.PngImagePlugin.PngImageFile image mode=RGB size=1000x500>"
      ]
     },
     "execution_count": 3,
     "metadata": {},
     "output_type": "execute_result"
    }
   ],
   "source": [
    "library.get(list(library.ids)[20]).chem2dview().draw()"
   ]
  },
  {
   "cell_type": "markdown",
   "metadata": {},
   "source": [
    "## Making molecules from fragments\n",
    "\n",
    "Now that we have a bunch of fragments to work with we can start thinking about how to combine them into ligands. For this purpose, let's define a class called the `MoleculeSampler`. This class will keep track of the fragment database and will be able to assemble a molecule from a numerical array input. Why do we need an array input? Well, machine learning works with numerical data. If we want to use any kind of automated optimization algorithm we will need to find a way of \"encoding\" our ligand molecules into an array with some numbers.\n",
    "\n",
    "### Encoding \"instructions\" to build a molecule in numpy\n",
    "The most important first decision we need to make is how to encode our molecules of interest into numpy arrays. We cannot directly use atom coordinates because we don't know what atoms the ligands will include or how many atoms are in each fragment. What we can know, however, is which fragments to attach to each other. We can also know which atoms to use when attaching different fragments. How do we \"encode\" this kind of data? Here's one possibility:\n",
    "\n",
    "```\n",
    "[incoming_fragment_global_index, incoming_atom_index, target_fragment_atom]\n",
    "```\n",
    "\n",
    "We can use the indices of fragments within our database to identify fragments and we can use indices for each fragment to identify the atoms that should be used for connecting different fragments. In this case we make the simple assumption that each fragment will always be connected to the previous fragment. So the second fragment attaches to the first, the third to the second, and so on... \n",
    "\n",
    "Let's look at an example:\n",
    "```\n",
    "array([[159,  -1,  -1],\n",
    "       [128,   4,   5],\n",
    "       [195,   1,   1]])\n",
    "```\n",
    "The matrix above states the following: \"Start with the fragment nr. 159 in the database (first line, the rest of the line can be ignored). Then get the next fragment, which is nr. 128 in the database, and connect it via its fifth atom to the first fragment in the molecule via its sixth atom (remember that indices start at 0, so index 4 = entry 5). Finally, get the last fragment, which is nr. 195 in the database, and connect it via its second atom to the second fragment again via its second atom.\"\n",
    "Sounds bulky, right? Maybe it will be a bit clearer when we implement the whole system in code..."
   ]
  },
  {
   "cell_type": "code",
   "execution_count": 4,
   "metadata": {},
   "outputs": [],
   "source": [
    "class MoleculeSampler:\n",
    "    def __init__(self, fragments: list):\n",
    "\n",
    "        # we need to maintain a per-fragment database of possible atom-sites where another fragment can be attached\n",
    "        # we also need to maintain a per-fragment database of atom-ids to make linkages\n",
    "        attachment_points = []\n",
    "        atom_ids = []\n",
    "\n",
    "        # let's browse through all fragments and identify the attachment points\n",
    "        # also, filter out any fragments without any attachment points (good practice)\n",
    "        to_drop = []\n",
    "        for fdx, fragment in enumerate(fragments):\n",
    "            \n",
    "            # we define all non-Hydrogen atoms as potential attachment points\n",
    "            # but only those that have a hydrogen neighbor that can be removed\n",
    "            # will be considered as attachment points\n",
    "            n_atoms = sum(1 for i in fragment.get_atoms() if i.element != \"H\")\n",
    "            a = []\n",
    "            for adx, atom in enumerate(fragment.get_atoms()):\n",
    "                if atom.element == \"H\":\n",
    "                    continue\n",
    "                if fragment.get_hydrogen(atom):\n",
    "                    a.append(adx)\n",
    "            if len(a) == 0:\n",
    "                to_drop.append(fdx)\n",
    "                continue\n",
    "            attachment_points.append(a)\n",
    "            atom_ids.append([atom.id for atom in fragment.get_atoms()])\n",
    "        \n",
    "        for fragment in to_drop:\n",
    "            del fragments[fragment]\n",
    "\n",
    "        self.fragments = fragments\n",
    "        self.attachment_points = attachment_points\n",
    "        self.atom_ids = atom_ids\n",
    "\n",
    "\n",
    "    def random(self, n_fragments: int):\n",
    "        \"\"\"\n",
    "        Make a random matrix encoding for a molecule assembled from fragments.\n",
    "        \"\"\"\n",
    "        # we could literally just use a single line here of np.random here, but then we run the risk of \n",
    "        # making invalid matrices where attachment_points are referenced more than once so we make a more intricate \n",
    "        # method here to ensure our \"random\" matrices are valid\n",
    "\n",
    "        matrix = np.full((n_fragments, 3), -1, dtype=int)\n",
    "        matrix[0, 0] = np.random.choice(len(self.fragments))\n",
    "\n",
    "        # we maintain a chache to keep track over which attachment points have been used already\n",
    "        # on which fragments\n",
    "        _used_atoms = {i : set() for i in range(n_fragments)}\n",
    "        for i in range(1, n_fragments):\n",
    "\n",
    "            # choose an incoming fragment from the database\n",
    "            matrix[i, 0] = np.random.choice(len(self.fragments))\n",
    "\n",
    "            # choose an attachment point on the incoming fragment that was not used already\n",
    "            while matrix[i, 1] == -1:\n",
    "                atom = np.random.choice(self.attachment_points[matrix[i, 0]])\n",
    "                if atom not in _used_atoms[i]:\n",
    "                    matrix[i, 1] = atom   \n",
    "                    _used_atoms[i].add(atom)\n",
    "            \n",
    "            # choose a target fragment in the molecule\n",
    "            # and choose an attachment point in the target that was not used already\n",
    "            target = i-1\n",
    "            while matrix[i, 2] == -1:\n",
    "                available = [i for i in self.attachment_points[matrix[target, 0]] if i not in _used_atoms[target]]\n",
    "                if len(available) > 0:\n",
    "                    matrix[i, 2] = np.random.choice(available)\n",
    "                    _used_atoms[target].add(matrix[i, 2])\n",
    "                    \n",
    "        return matrix\n",
    "    \n",
    "    def make_molecule(self, matrix):\n",
    "        \"\"\"\n",
    "        Assemble a molecule based on an instruction matrix\n",
    "        \"\"\"\n",
    "        _used_atoms = {i : set() for i in range(len(matrix))}\n",
    "\n",
    "        # we start by copying the first fragment\n",
    "        mol = self.fragments[matrix[0, 0]].copy()\n",
    "\n",
    "        # we then attach all other fragments        \n",
    "        for i in range(1, len(matrix)):\n",
    "            source, source_atom, target_atom = matrix[i, :]\n",
    "            target = i-1\n",
    "            # sanity checking to ensure we are not trying to attach to the same atom twice\n",
    "            if target_atom in _used_atoms[target]:\n",
    "                raise ValueError(\"Target atom already used\")\n",
    "            if source_atom in _used_atoms[i]:\n",
    "                raise ValueError(\"Source atom already used\")\n",
    "\n",
    "            # make a linkage and attach the fragment\n",
    "            link = bam.linkage(self.atom_ids[matrix[target, 0]][target_atom], self.atom_ids[source][source_atom])\n",
    "            mol.attach(self.fragments[source], link, at_residue=int(target+1))\n",
    "\n",
    "            _used_atoms[target].add(target_atom)\n",
    "            _used_atoms[i].add(source_atom)\n",
    "\n",
    "        return mol"
   ]
  },
  {
   "cell_type": "markdown",
   "metadata": {},
   "source": [
    "Okey, so that's done. It is a bit of a clunk but it should do the trick. Let's test out what our example array from above actually yields:"
   ]
  },
  {
   "cell_type": "code",
   "execution_count": 5,
   "metadata": {},
   "outputs": [
    {
     "data": {
      "image/png": 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     },
     "execution_count": 5,
     "metadata": {},
     "output_type": "execute_result"
    }
   ],
   "source": [
    "# make a sampler with our fragment library\n",
    "sampler = MoleculeSampler([library.get(i) for i in library.ids])\n",
    "\n",
    "# make the matrix from the example above\n",
    "matrix = np.array([\n",
    "       [159,  -1,  -1],\n",
    "       [128,   4,   5],\n",
    "       [195,   1,   1]])\n",
    "\n",
    "# and make the molecule\n",
    "mol = sampler.make_molecule(matrix)\n",
    "mol.chem2dview().draw()  "
   ]
  },
  {
   "cell_type": "markdown",
   "metadata": {},
   "source": [
    "Cool! So apparently we can make molecules from numpy arrays now! With that taken care of we can start thinking about or actual goal of finding \n",
    "ligand generation. "
   ]
  },
  {
   "cell_type": "markdown",
   "metadata": {},
   "source": [
    "## The docking procedure\n",
    "\n",
    "We will use *dockstring* which is a library that works with RDKit, Openbabel, and Autodock Vina to dock a molecule onto a protein. The system is relatively simple. One loads a protein target and then passes SMILES for the possible ligand to the `Target.dock` method, which will return a docking score. Regrettably, we cannot directly pass an RDKit molecule to dockstring so there will be a lot of back-and-forth computation going on but that can't be helped right now...  "
   ]
  },
  {
   "cell_type": "code",
   "execution_count": 6,
   "metadata": {},
   "outputs": [],
   "source": [
    "import dockstring as ds\n",
    "\n",
    "# we will work with the exact same setup that the authors of dockstring have used in their basic tutorial\n",
    "# which was to use the DRD2 (dopamine receptor D2) target protein from the PDB\n",
    "target_id = \"DRD2\"\n",
    "target = ds.load_target(target_id)"
   ]
  },
  {
   "cell_type": "markdown",
   "metadata": {},
   "source": [
    "Now we can test our example molecule's docking score:"
   ]
  },
  {
   "cell_type": "code",
   "execution_count": 7,
   "metadata": {},
   "outputs": [
    {
     "name": "stderr",
     "output_type": "stream",
     "text": [
      "/Users/noahhk/anaconda3/envs/glyco2/lib/python3.11/site-packages/dockstring/utils.py:77: DockstringWarning: Although Mac use is supported, docking scores on Mac do not always perfectly match scores from Linux. Therefore, extra care should be taken when comparing results to other platforms. In particular, the baselines in the DOCKSTRING paper were computed on Linux, so please do not directly compare your docking scores to the scores reported on the paper.\n",
      "  warnings.warn(\n"
     ]
    },
    {
     "name": "stdout",
     "output_type": "stream",
     "text": [
      "-7.4\n"
     ]
    }
   ],
   "source": [
    "score, aux = target.dock(mol.to_smiles())\n",
    "print(score)"
   ]
  },
  {
   "cell_type": "markdown",
   "metadata": {},
   "source": [
    "In fact, dockstring even provides us with an RDKit molecule for the algined ligand which can be found in the `aux` dictionary. It actually contains 10 conformers that were evaluated, we are only interested in the best one (which is the first one):"
   ]
  },
  {
   "cell_type": "code",
   "execution_count": 8,
   "metadata": {},
   "outputs": [
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    }
   ],
   "source": [
    "def get_ligand(rdkit_ligand):\n",
    "    # remove the other conformers (since we cannot import multi-conformer RDKit molecules directly into BuildAMol)\n",
    "    conf = rdkit_ligand.GetConformer(0)\n",
    "    for i in range(1, 10):\n",
    "        rdkit_ligand.RemoveConformer(i)\n",
    "\n",
    "    ligand = bam.Molecule.from_rdkit(rdkit_ligand)\n",
    "    return ligand\n",
    "\n",
    "aligned = get_ligand(aux[\"ligand\"])    \n",
    "aligned.py3dmol().show()"
   ]
  },
  {
   "cell_type": "markdown",
   "metadata": {},
   "source": [
    "## Making a pipeline \n",
    "\n",
    "Okey, now that we know that everything works we can start to actually design a pipeline that will actually put all the pieces together in order to generate some possible ligands. Since this tutorial should illustrate the general workflow and provide some inspiration rather than present a full-fledged finished product, we will not be implementing anything overly fancy. We will simply write a scoring function to make and dock a molecule using *dockstring* and then pass that to `scipy.optimize.minimize` and see what happens... Ideally we would like to have multiple candidate ligands, so we will run our pipeline a few times to get some hits..."
   ]
  },
  {
   "cell_type": "code",
   "execution_count": 9,
   "metadata": {},
   "outputs": [],
   "source": [
    "from warnings import filterwarnings\n",
    "filterwarnings(\"ignore\")\n",
    "ds.setup_logger(level=\"ERROR\")\n",
    "\n",
    "# let's try to find a ligand from 4 fragments\n",
    "n_fragments = 4\n",
    "starting = sampler.random(n_fragments)\n",
    "\n",
    "# we will set up a dictionary that allows us to store a few more of the \"best\" ligands along the way...\n",
    "metadata = {\"best_score\" : np.inf, \"ligand\" : None}\n",
    "\n",
    "# we define our scoring function that will evaluate the ligand\n",
    "def score(matrix):\n",
    "    # we need to reshape since the matrix is 2D but the optimizer will pass it as a 1D array\n",
    "    matrix = matrix.reshape(starting.shape).astype(int)\n",
    "    \n",
    "    # we use try-except since we cannot be sure that the matrix will be valid at all times\n",
    "    try:\n",
    "        smiles = sampler.make_molecule(matrix).to_smiles()\n",
    "        score, aux = target.dock(smiles)\n",
    "        new_best = min(metadata[\"best_score\"], score)\n",
    "        if score == new_best:\n",
    "            metadata[\"best_score\"] = score\n",
    "            metadata[\"ligand\"] = aux[\"ligand\"]  \n",
    "        return score\n",
    "    except:\n",
    "        return np.inf"
   ]
  },
  {
   "cell_type": "markdown",
   "metadata": {},
   "source": [
    "We can now test out if we can \"optimize\" for a ligand here with our scoring function. Let's see if we get an output..."
   ]
  },
  {
   "cell_type": "code",
   "execution_count": 19,
   "metadata": {},
   "outputs": [
    {
     "name": "stdout",
     "output_type": "stream",
     "text": [
      "-11.6\n"
     ]
    },
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      ]
     },
     "metadata": {},
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    }
   ],
   "source": [
    "from scipy import optimize\n",
    "# we will use the Nelder-Mead method since it is simple and does not require gradients\n",
    "# and we will do only a small test-run with 5 iterations\n",
    "out = optimize.minimize(score, starting.flatten(), method=\"Nelder-Mead\", options={\"maxiter\" : 5})\n",
    "\n",
    "# the results should be stored in the metadata dictionary now\n",
    "print(metadata[\"best_score\"])\n",
    "ligand = get_ligand(metadata[\"ligand\"])\n",
    "ligand.to_pdb(\"./files/DRD2_ligand.pdb\")\n",
    "ligand.py3dmol().show()"
   ]
  },
  {
   "cell_type": "markdown",
   "metadata": {},
   "source": [
    "And let's also check out the ligand and protein together:"
   ]
  },
  {
   "cell_type": "code",
   "execution_count": 21,
   "metadata": {},
   "outputs": [
    {
     "data": {
      "application/3dmoljs_load.v0": "<div id=\"3dmolviewer_1716802976377794\"  style=\"position: relative; width: 800px; height: 600px;\">\n        <p id=\"3dmolwarning_1716802976377794\" style=\"background-color:#ffcccc;color:black\">You appear to be running in JupyterLab (or JavaScript failed to load for some other reason).  You need to install the 3dmol extension: <br>\n        <tt>jupyter labextension install jupyterlab_3dmol</tt></p>\n        </div>\n<script>\n\nvar loadScriptAsync = function(uri){\n  return new Promise((resolve, reject) => {\n    //this is to ignore the existence of requirejs amd\n    var savedexports, savedmodule;\n    if (typeof exports !== 'undefined') savedexports = exports;\n    else exports = {}\n    if (typeof module !== 'undefined') savedmodule = module;\n    else module = {}\n\n    var tag = document.createElement('script');\n    tag.src = uri;\n    tag.async = true;\n    tag.onload = () => {\n        exports = savedexports;\n        module = savedmodule;\n        resolve();\n    };\n  var firstScriptTag = document.getElementsByTagName('script')[0];\n  firstScriptTag.parentNode.insertBefore(tag, firstScriptTag);\n});\n};\n\nif(typeof $3Dmolpromise === 'undefined') {\n$3Dmolpromise = null;\n  $3Dmolpromise = loadScriptAsync('https://cdnjs.cloudflare.com/ajax/libs/3Dmol/2.0.3/3Dmol-min.js');\n}\n\nvar viewer_1716802976377794 = null;\nvar warn = document.getElementById(\"3dmolwarning_1716802976377794\");\nif(warn) {\n    warn.parentNode.removeChild(warn);\n}\n$3Dmolpromise.then(function() {\nviewer_1716802976377794 = $3Dmol.createViewer(document.getElementById(\"3dmolviewer_1716802976377794\"),{backgroundColor:\"white\"});\nviewer_1716802976377794.zoomTo();\n\tviewer_1716802976377794.addModels(\"HEADER    MEMBRANE PROTEIN                        02-MAR-18   6CM4              \\nTITLE     STRUCTURE OF THE D2 DOPAMINE RECEPTOR BOUND TO THE ATYPICAL           \\nTITLE    2 ANTIPSYCHOTIC DRUG RISPERIDONE                                       \\nCOMPND    MOL_ID: 1;                                                            \\nCOMPND   2 MOLECULE: D(2) DOPAMINE RECEPTOR, ENDOLYSIN CHIMERA;                 \\nCOMPND   3 CHAIN: A;                                                            \\nCOMPND   4 SYNONYM: DOPAMINE D2 RECEPTOR, LYSIS PROTEIN, LYSOZYME, MURAMIDASE,  \\nCOMPND   5 DOPAMINE D2 RECEPTOR;                                                \\nCOMPND   6 EC: 3.2.1.17;                                                        \\nCOMPND   7 ENGINEERED: YES                                                      \\nSOURCE    MOL_ID: 1;                                                            \\nSOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, ENTEROBACTERIA PHAGE T4;          \\nSOURCE   3 ORGANISM_COMMON: HUMAN, BACTERIOPHAGE T4;                            \\nSOURCE   4 ORGANISM_TAXID: 9606, 10665;                                         \\nSOURCE   5 GENE: DRD2, E, T4TP126;                                              \\nSOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            \\nSOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             \\nSOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;                                       \\nSOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          \\nSOURCE  10 EXPRESSION_SYSTEM_PLASMID: PFASTBAC1-HM                              \\nKEYWDS    GPCR, D2, DOPAMINE RECEPTOR, ANTIPSYCHOTIC, RISPERIDONE, MEMBRANE     \\nKEYWDS   2 PROTEIN                                                              \\nEXPDTA    X-RAY DIFFRACTION                                                     \\nAUTHOR    S.WANG,T.CHE,A.LEVIT,B.K.SHOICHET,D.WACKER,B.L.ROTH                   \\nREVDAT   6   04-OCT-23 6CM4    1       REMARK                                   \\nREVDAT   5   27-NOV-19 6CM4    1       REMARK                                   \\nREVDAT   4   20-FEB-19 6CM4    1       REMARK                                   \\nREVDAT   3   11-APR-18 6CM4    1       DBREF                                    \\nREVDAT   2   21-MAR-18 6CM4    1       JRNL                                     \\nREVDAT   1   14-MAR-18 6CM4    0                                                \\nSPRSDE     14-MAR-18 6CM4      6C38                                             \\nJRNL        AUTH   S.WANG,T.CHE,A.LEVIT,B.K.SHOICHET,D.WACKER,B.L.ROTH          \\nJRNL        TITL   STRUCTURE OF THE D2 DOPAMINE RECEPTOR BOUND TO THE ATYPICAL  \\nJRNL        TITL 2 ANTIPSYCHOTIC DRUG RISPERIDONE.                              \\nJRNL        REF    NATURE                        V. 555   269 2018              \\nJRNL        REFN                   ESSN 1476-4687                               \\nJRNL        PMID   29466326                                                     \\nJRNL        DOI    10.1038/NATURE25758                                          \\nREMARK   2                                                                      \\nREMARK   2 RESOLUTION.    2.87 ANGSTROMS.                                       \\nREMARK   3                                                                      \\nREMARK   3 REFINEMENT.                                                          \\nREMARK   3   PROGRAM     : PHENIX (1.12_2829: ???)                              \\nREMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            \\nREMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           \\nREMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            \\nREMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              \\nREMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               \\nREMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           \\nREMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  \\nREMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  \\nREMARK   3                                                                      \\nREMARK   3    REFINEMENT TARGET : ML                                            \\nREMARK   3                                                                      \\nREMARK   3  DATA USED IN REFINEMENT.                                            \\nREMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.87                           \\nREMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.55                          \\nREMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.360                          \\nREMARK   3   COMPLETENESS FOR RANGE        (%) : 95.2                           \\nREMARK   3   NUMBER OF REFLECTIONS             : 12814                          \\nREMARK   3                                                                      \\nREMARK   3  FIT TO DATA USED IN REFINEMENT.                                     \\nREMARK   3   R VALUE     (WORKING + TEST SET) : 0.227                           \\nREMARK   3   R VALUE            (WORKING SET) : 0.226                           \\nREMARK   3   FREE R VALUE                     : 0.249                           \\nREMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.850                           \\nREMARK   3   FREE R VALUE TEST SET COUNT      : 622                             \\nREMARK   3                                                                      \\nREMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           \\nREMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        \\nREMARK   3     1 29.5504 -  4.5475    0.98     3287   157  0.2103 0.2188        \\nREMARK   3     2  4.5475 -  3.6116    0.99     3151   170  0.2090 0.2511        \\nREMARK   3     3  3.6116 -  3.1556    0.99     3111   162  0.2730 0.3034        \\nREMARK   3     4  3.1556 -  2.8674    0.84     2643   133  0.3166 0.3214        \\nREMARK   3                                                                      \\nREMARK   3  BULK SOLVENT MODELLING.                                             \\nREMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       \\nREMARK   3   SOLVENT RADIUS     : 1.11                                          \\nREMARK   3   SHRINKAGE RADIUS   : 0.90                                          \\nREMARK   3   K_SOL              : NULL                                          \\nREMARK   3   B_SOL              : NULL                                          \\nREMARK   3                                                                      \\nREMARK   3  ERROR ESTIMATES.                                                    \\nREMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.390            \\nREMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.640           \\nREMARK   3                                                                      \\nREMARK   3  B VALUES.                                                           \\nREMARK   3   FROM WILSON PLOT           (A**2) : NULL                           \\nREMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           \\nREMARK   3   OVERALL ANISOTROPIC B VALUE.                                       \\nREMARK   3    B11 (A**2) : NULL                                                 \\nREMARK   3    B22 (A**2) : NULL                                                 \\nREMARK   3    B33 (A**2) : NULL                                                 \\nREMARK   3    B12 (A**2) : NULL                                                 \\nREMARK   3    B13 (A**2) : NULL                                                 \\nREMARK   3    B23 (A**2) : NULL                                                 \\nREMARK   3                                                                      \\nREMARK   3  TWINNING INFORMATION.                                               \\nREMARK   3   FRACTION: NULL                                                     \\nREMARK   3   OPERATOR: NULL                                                     \\nREMARK   3                                                                      \\nREMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       \\nREMARK   3                 RMSD          COUNT                                  \\nREMARK   3   BOND      :  0.003           3283                                  \\nREMARK   3   ANGLE     :  0.516           4483                                  \\nREMARK   3   CHIRALITY :  0.037            544                                  \\nREMARK   3   PLANARITY :  0.003            549                                  \\nREMARK   3   DIHEDRAL  : 10.862           1928                                  \\nREMARK   3                                                                      \\nREMARK   3  TLS DETAILS                                                         \\nREMARK   3   NUMBER OF TLS GROUPS  : 3                                          \\nREMARK   3   TLS GROUP : 1                                                      \\nREMARK   3    SELECTION: CHAIN 'A' AND (RESID 36 THROUGH 222 )                  \\nREMARK   3    ORIGIN FOR THE GROUP (A):   7.6595   9.9883   1.8227              \\nREMARK   3    T TENSOR                                                          \\nREMARK   3      T11:   0.3906 T22:   0.3948                                     \\nREMARK   3      T33:   0.4097 T12:  -0.0409                                     \\nREMARK   3      T13:   0.0298 T23:   0.0323                                     \\nREMARK   3    L TENSOR                                                          \\nREMARK   3      L11:   4.8704 L22:   2.9655                                     \\nREMARK   3      L33:   4.7317 L12:   0.7811                                     \\nREMARK   3      L13:   2.8181 L23:   1.4507                                     \\nREMARK   3    S TENSOR                                                          \\nREMARK   3      S11:   0.0593 S12:  -0.1051 S13:   0.0093                       \\nREMARK   3      S21:   0.1418 S22:  -0.1464 S23:   0.1356                       \\nREMARK   3      S31:   0.4299 S32:  -0.3974 S33:  -0.0137                       \\nREMARK   3   TLS GROUP : 2                                                      \\nREMARK   3    SELECTION: CHAIN 'A' AND (RESID 1002 THROUGH 1161 )               \\nREMARK   3    ORIGIN FOR THE GROUP (A):  32.7700  -7.7446  36.3658              \\nREMARK   3    T TENSOR                                                          \\nREMARK   3      T11:   0.6968 T22:   0.5198                                     \\nREMARK   3      T33:   0.5000 T12:   0.0363                                     \\nREMARK   3      T13:   0.0872 T23:   0.1084                                     \\nREMARK   3    L TENSOR                                                          \\nREMARK   3      L11:   6.6697 L22:   6.8821                                     \\nREMARK   3      L33:   6.4568 L12:   1.6541                                     \\nREMARK   3      L13:   1.9941 L23:   1.4205                                     \\nREMARK   3    S TENSOR                                                          \\nREMARK   3      S11:  -0.2551 S12:   0.1211 S13:  -0.2547                       \\nREMARK   3      S21:  -0.3908 S22:  -0.0566 S23:  -0.4642                       \\nREMARK   3      S31:   0.4711 S32:   0.2364 S33:   0.3147                       \\nREMARK   3   TLS GROUP : 3                                                      \\nREMARK   3    SELECTION: CHAIN 'A' AND (RESID 384 THROUGH 460 )                 \\nREMARK   3    ORIGIN FOR THE GROUP (A):   9.8885  -1.6530  -1.3224              \\nREMARK   3    T TENSOR                                                          \\nREMARK   3      T11:   0.6392 T22:   0.3770                                     \\nREMARK   3      T33:   0.5276 T12:   0.0087                                     \\nREMARK   3      T13:  -0.0908 T23:   0.0140                                     \\nREMARK   3    L TENSOR                                                          \\nREMARK   3      L11:   6.0244 L22:   5.3813                                     \\nREMARK   3      L33:   6.7255 L12:   0.3578                                     \\nREMARK   3      L13:   1.1698 L23:   0.5209                                     \\nREMARK   3    S TENSOR                                                          \\nREMARK   3      S11:  -0.0948 S12:   0.3307 S13:   0.0832                       \\nREMARK   3      S21:  -0.4022 S22:   0.2772 S23:  -0.0581                       \\nREMARK   3      S31:   1.2902 S32:  -0.0417 S33:  -0.2847                       \\nREMARK   3                                                                      \\nREMARK   3  NCS DETAILS                                                         \\nREMARK   3   NUMBER OF NCS GROUPS : NULL                                        \\nREMARK   3                                                                      \\nREMARK   3  OTHER REFINEMENT REMARKS: NULL                                      \\nREMARK   4                                                                      \\nREMARK   4 6CM4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         \\nREMARK 100                                                                      \\nREMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-MAR-18.                  \\nREMARK 100 THE DEPOSITION ID IS D_1000232947.                                   \\nREMARK 200                                                                      \\nREMARK 200 EXPERIMENTAL DETAILS                                                 \\nREMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  \\nREMARK 200  DATE OF DATA COLLECTION        : 13-AUG-17                          \\nREMARK 200  TEMPERATURE           (KELVIN) : 100                                \\nREMARK 200  PH                             : NULL                               \\nREMARK 200  NUMBER OF CRYSTALS USED        : 1                                  \\nREMARK 200                                                                      \\nREMARK 200  SYNCHROTRON              (Y/N) : Y                                  \\nREMARK 200  RADIATION SOURCE               : APS                                \\nREMARK 200  BEAMLINE                       : 23-ID-B                            \\nREMARK 200  X-RAY GENERATOR MODEL          : NULL                               \\nREMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  \\nREMARK 200  WAVELENGTH OR RANGE        (A) : 1.033                              \\nREMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL CRYO-COOLED         \\nREMARK 200                                   SI(111)                            \\nREMARK 200  OPTICS                         : NULL                               \\nREMARK 200                                                                      \\nREMARK 200  DETECTOR TYPE                  : PIXEL                              \\nREMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER X 16M                \\nREMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000                           \\nREMARK 200  DATA SCALING SOFTWARE          : HKL-3000                           \\nREMARK 200                                                                      \\nREMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 12826                              \\nREMARK 200  RESOLUTION RANGE HIGH      (A) : 2.867                              \\nREMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             \\nREMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               \\nREMARK 200                                                                      \\nREMARK 200 OVERALL.                                                             \\nREMARK 200  COMPLETENESS FOR RANGE     (%) : 97.3                               \\nREMARK 200  DATA REDUNDANCY                : 5.500                              \\nREMARK 200  R MERGE                    (I) : 0.13400                            \\nREMARK 200  R SYM                      (I) : NULL                               \\nREMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.2000                            \\nREMARK 200                                                                      \\nREMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     \\nREMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90                     \\nREMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.99                     \\nREMARK 200  COMPLETENESS FOR SHELL     (%) : 86.9                               \\nREMARK 200  DATA REDUNDANCY IN SHELL       : 2.50                               \\nREMARK 200  R MERGE FOR SHELL          (I) : 0.73800                            \\nREMARK 200  R SYM FOR SHELL            (I) : NULL                               \\nREMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.000                              \\nREMARK 200                                                                      \\nREMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              \\nREMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        \\nREMARK 200 SOFTWARE USED: PHASER                                                \\nREMARK 200 STARTING MODEL: PDB ENTRIES 5WIU & 2RH1                              \\nREMARK 200                                                                      \\nREMARK 200 REMARK: NULL                                                         \\nREMARK 280                                                                      \\nREMARK 280 CRYSTAL                                                              \\nREMARK 280 SOLVENT CONTENT, VS   (%): 57.13                                     \\nREMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.87                     \\nREMARK 280                                                                      \\nREMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM TRIS-HCL, PH 7.8, 230 MM          \\nREMARK 280  LITHIUM NITRATE, 25% PEG400, 4% 1,3-BUTANEDIOL, LIPIDIC CUBIC       \\nREMARK 280  PHASE, TEMPERATURE 293K                                             \\nREMARK 290                                                                      \\nREMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            \\nREMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       \\nREMARK 290                                                                      \\nREMARK 290      SYMOP   SYMMETRY                                                \\nREMARK 290     NNNMMM   OPERATOR                                                \\nREMARK 290       1555   X,Y,Z                                                   \\nREMARK 290       2555   -X+1/2,-Y,Z+1/2                                         \\nREMARK 290       3555   -X,Y+1/2,-Z+1/2                                         \\nREMARK 290       4555   X+1/2,-Y+1/2,-Z                                         \\nREMARK 290                                                                      \\nREMARK 290     WHERE NNN -> OPERATOR NUMBER                                     \\nREMARK 290           MMM -> TRANSLATION VECTOR                                  \\nREMARK 290                                                                      \\nREMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            \\nREMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             \\nREMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                \\nREMARK 290 RELATED MOLECULES.                                                   \\nREMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            \\nREMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            \\nREMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            \\nREMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       25.48950            \\nREMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            \\nREMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       75.65350            \\nREMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            \\nREMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       36.26150            \\nREMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       75.65350            \\nREMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       25.48950            \\nREMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       36.26150            \\nREMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            \\nREMARK 290                                                                      \\nREMARK 290 REMARK: NULL                                                         \\nREMARK 300                                                                      \\nREMARK 300 BIOMOLECULE: 1                                                       \\nREMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                \\nREMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  \\nREMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               \\nREMARK 300 BURIED SURFACE AREA.                                                 \\nREMARK 350                                                                      \\nREMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           \\nREMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                \\nREMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          \\nREMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          \\nREMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               \\nREMARK 350                                                                      \\nREMARK 350 BIOMOLECULE: 1                                                       \\nREMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         \\nREMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  \\nREMARK 350 SOFTWARE USED: PISA                                                  \\nREMARK 350 TOTAL BURIED SURFACE AREA: 1850 ANGSTROM**2                          \\nREMARK 350 SURFACE AREA OF THE COMPLEX: 20460 ANGSTROM**2                       \\nREMARK 350 CHANGE IN SOLVENT FREE ENERGY: 12.0 KCAL/MOL                         \\nREMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     \\nREMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            \\nREMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            \\nREMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            \\nREMARK 465                                                                      \\nREMARK 465 MISSING RESIDUES                                                     \\nREMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       \\nREMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               \\nREMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                \\nREMARK 465                                                                      \\nREMARK 465   M RES C SSSEQI                                                     \\nREMARK 465     MET A   140                                                      \\nREMARK 465     LEU A   141                                                      \\nREMARK 465     TYR A   142                                                      \\nREMARK 465     ASN A   143                                                      \\nREMARK 465     LYS A   362                                                      \\nREMARK 465     LEU A   363                                                      \\nREMARK 465     CYS A   443                                                      \\nREMARK 470                                                                      \\nREMARK 470 MISSING ATOM                                                         \\nREMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           \\nREMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          \\nREMARK 470 I=INSERTION CODE):                                                   \\nREMARK 470   M RES CSSEQI  ATOMS                                                \\nREMARK 470     ASN A  35    CG   OD1  ND2                                       \\nREMARK 470     TYR A  36    CG   CD1  CD2  CE1  CE2  CZ   OH                    \\nREMARK 470     LEU A  43    CG   CD1  CD2                                       \\nREMARK 470     GLU A  62    CG   CD   OE1  OE2                                  \\nREMARK 470     LYS A  63    CG   CD   CE   NZ                                   \\nREMARK 470     VAL A  96    CG1  CG2                                            \\nREMARK 470     GLU A  99    CG   CD   OE1  OE2                                  \\nREMARK 470     LYS A 101    CG   CD   CE   NZ                                   \\nREMARK 470     THR A 144    OG1  CG2                                            \\nREMARK 470     ARG A 145    CG   CD   NE   CZ   NH1  NH2                        \\nREMARK 470     SER A 147    OG                                                  \\nREMARK 470     LYS A 149    CG   CD   CE   NZ                                   \\nREMARK 470     ARG A 150    CG   CD   NE   CZ   NH1  NH2                        \\nREMARK 470     ASN A 176    CG   OD1  ND2                                       \\nREMARK 470     ASP A 178    CG   OD1  OD2                                       \\nREMARK 470     GLN A 179    CG   CD   OE1  NE2                                  \\nREMARK 470     ASN A 180    CG   OD1  ND2                                       \\nREMARK 470     LYS A 211    CE   NZ                                             \\nREMARK 470     ARG A 217    CG   CD   NE   CZ   NH1  NH2                        \\nREMARK 470     ARG A 218    CG   CD   NE   CZ   NH1  NH2                        \\nREMARK 470     LYS A 221    CG   CD   CE   NZ                                   \\nREMARK 470     ARG A 222    CG   CD   NE   CZ   NH1  NH2                        \\nREMARK 470     LYS A1016    CG   CD   CE   NZ                                   \\nREMARK 470     LYS A1019    CG   CD   CE   NZ                                   \\nREMARK 470     GLU A1022    CG   CD   OE1  OE2                                  \\nREMARK 470     LEU A1032    CG   CD1  CD2                                       \\nREMARK 470     LEU A1033    CG   CD1  CD2                                       \\nREMARK 470     LYS A1035    CG   CD   CE   NZ                                   \\nREMARK 470     SER A1036    OG                                                  \\nREMARK 470     SER A1038    OG                                                  \\nREMARK 470     ASN A1040    CG   OD1  ND2                                       \\nREMARK 470     SER A1044    OG                                                  \\nREMARK 470     GLU A1045    CG   CD   OE1  OE2                                  \\nREMARK 470     LYS A1048    CG   CD   CE   NZ                                   \\nREMARK 470     ILE A1050    CG1  CG2  CD1                                       \\nREMARK 470     ASN A1053    CG   OD1  ND2                                       \\nREMARK 470     THR A1054    OG1  CG2                                            \\nREMARK 470     ASN A1055    CG   OD1  ND2                                       \\nREMARK 470     VAL A1057    CG1  CG2                                            \\nREMARK 470     LYS A1060    CG   CD   CE   NZ                                   \\nREMARK 470     LYS A1065    CG   CD   CE   NZ                                   \\nREMARK 470     ARG A1080    CG   CD   NE   CZ   NH1  NH2                        \\nREMARK 470     LYS A1083    CG   CD   CE   NZ                                   \\nREMARK 470     LYS A1085    CG   CD   CE   NZ                                   \\nREMARK 470     ASN A1116    CG   OD1  ND2                                       \\nREMARK 470     ASP A1127    CG   OD1  OD2                                       \\nREMARK 470     VAL A1131    CG1  CG2                                            \\nREMARK 470     LYS A1135    CG   CD   CE   NZ                                   \\nREMARK 470     ARG A1137    CG   CD   NE   CZ   NH1  NH2                        \\nREMARK 470     GLN A1141    CG   CD   OE1  NE2                                  \\nREMARK 470     LYS A1147    CG   CD   CE   NZ                                   \\nREMARK 470     THR A1157    OG1  CG2                                            \\nREMARK 470     SER A 364    OG                                                  \\nREMARK 470     GLN A 365    CG   CD   OE1  NE2                                  \\nREMARK 470     GLN A 366    CG   CD   OE1  NE2                                  \\nREMARK 470     LYS A 367    CG   CD   CE   NZ                                   \\nREMARK 470     LYS A 369    CG   CD   CE   NZ                                   \\nREMARK 470     LYS A 370    CG   CD   CE   NZ                                   \\nREMARK 470     ILE A 394    CG1  CG2  CD1                                       \\nREMARK 470     HIS A 398    CG   ND1  CD2  CE1  NE2                             \\nREMARK 470     ASP A 400    CG   OD1  OD2                                       \\nREMARK 470     VAL A 406    CG1  CG2                                            \\nREMARK 470     LEU A 407    CG   CD1  CD2                                       \\nREMARK 470     ILE A 431    CG1  CG2  CD1                                       \\nREMARK 470     GLU A 432    CG   CD   OE1  OE2                                  \\nREMARK 470     ARG A 434    CG   CD   NE   CZ   NH1  NH2                        \\nREMARK 470     LYS A 435    CG   CD   CE   NZ                                   \\nREMARK 470     LEU A 438    CG   CD1  CD2                                       \\nREMARK 470     LYS A 439    CG   CD   CE   NZ                                   \\nREMARK 470     HIS A 442    CG   ND1  CD2  CE1  NE2                             \\nREMARK 500                                                                      \\nREMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         \\nREMARK 500 SUBTOPIC: TORSION ANGLES                                             \\nREMARK 500                                                                      \\nREMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            \\nREMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               \\nREMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             \\nREMARK 500                                                                      \\nREMARK 500 STANDARD TABLE:                                                      \\nREMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    \\nREMARK 500                                                                      \\nREMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           \\nREMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            \\nREMARK 500                                                                      \\nREMARK 500  M RES CSSEQI        PSI       PHI                                   \\nREMARK 500    GLN A  66       70.23   -104.22                                   \\nREMARK 500    VAL A  87      -52.46   -121.67                                   \\nREMARK 500    PHE A 198      -60.72   -124.56                                   \\nREMARK 500    ASN A1055       17.81     58.75                                   \\nREMARK 500    PHE A1114       49.44    -89.78                                   \\nREMARK 500    ASP A 400       11.47     57.92                                   \\nREMARK 500    LEU A 441       33.98    -88.55                                   \\nREMARK 500                                                                      \\nREMARK 500 REMARK: NULL                                                         \\nREMARK 610                                                                      \\nREMARK 610 MISSING HETEROATOM                                                   \\nREMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           \\nREMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          \\nREMARK 610 I=INSERTION CODE):                                                   \\nREMARK 610   M RES C SSEQI                                                      \\nREMARK 610     OLA A 2005                                                       \\nREMARK 610     OLA A 2006                                                       \\nDBREF  6CM4 A   35   222  UNP    P14416   DRD2_HUMAN      35    222             \\nDBREF  6CM4 A 1002  1161  UNP    D9IEF7   D9IEF7_BPT4      2    161             \\nDBREF  6CM4 A  362   443  UNP    P14416   DRD2_HUMAN     362    443             \\nSEQADV 6CM4 ALA A  122  UNP  P14416    ILE   122 CONFLICT                       \\nSEQADV 6CM4 THR A 1054  UNP  D9IEF7    CYS    54 CONFLICT                       \\nSEQADV 6CM4 ALA A 1097  UNP  D9IEF7    CYS    97 CONFLICT                       \\nSEQADV 6CM4 ALA A  375  UNP  P14416    LEU   375 CONFLICT                       \\nSEQADV 6CM4 ALA A  379  UNP  P14416    LEU   379 CONFLICT                       \\nSEQRES   1 A  430  ASN TYR TYR ALA THR LEU LEU THR LEU LEU ILE ALA VAL\\nSEQRES   2 A  430  ILE VAL PHE GLY ASN VAL LEU VAL CYS MET ALA VAL SER\\nSEQRES   3 A  430  ARG GLU LYS ALA LEU GLN THR THR THR ASN TYR LEU ILE\\nSEQRES   4 A  430  VAL SER LEU ALA VAL ALA ASP LEU LEU VAL ALA THR LEU\\nSEQRES   5 A  430  VAL MET PRO TRP VAL VAL TYR LEU GLU VAL VAL GLY GLU\\nSEQRES   6 A  430  TRP LYS PHE SER ARG ILE HIS CYS ASP ILE PHE VAL THR\\nSEQRES   7 A  430  LEU ASP VAL MET MET CYS THR ALA SER ALA LEU ASN LEU\\nSEQRES   8 A  430  CYS ALA ILE SER ILE ASP ARG TYR THR ALA VAL ALA MET\\nSEQRES   9 A  430  PRO MET LEU TYR ASN THR ARG TYR SER SER LYS ARG ARG\\nSEQRES  10 A  430  VAL THR VAL MET ILE SER ILE VAL TRP VAL LEU SER PHE\\nSEQRES  11 A  430  THR ILE SER CYS PRO LEU LEU PHE GLY LEU ASN ASN ALA\\nSEQRES  12 A  430  ASP GLN ASN GLU CYS ILE ILE ALA ASN PRO ALA PHE VAL\\nSEQRES  13 A  430  VAL TYR SER SER ILE VAL SER PHE TYR VAL PRO PHE ILE\\nSEQRES  14 A  430  VAL THR LEU LEU VAL TYR ILE LYS ILE TYR ILE VAL LEU\\nSEQRES  15 A  430  ARG ARG ARG ARG LYS ARG ASN ILE PHE GLU MET LEU ARG\\nSEQRES  16 A  430  ILE ASP GLU GLY LEU ARG LEU LYS ILE TYR LYS ASP THR\\nSEQRES  17 A  430  GLU GLY TYR TYR THR ILE GLY ILE GLY HIS LEU LEU THR\\nSEQRES  18 A  430  LYS SER PRO SER LEU ASN ALA ALA LYS SER GLU LEU ASP\\nSEQRES  19 A  430  LYS ALA ILE GLY ARG ASN THR ASN GLY VAL ILE THR LYS\\nSEQRES  20 A  430  ASP GLU ALA GLU LYS LEU PHE ASN GLN ASP VAL ASP ALA\\nSEQRES  21 A  430  ALA VAL ARG GLY ILE LEU ARG ASN ALA LYS LEU LYS PRO\\nSEQRES  22 A  430  VAL TYR ASP SER LEU ASP ALA VAL ARG ARG ALA ALA LEU\\nSEQRES  23 A  430  ILE ASN MET VAL PHE GLN MET GLY GLU THR GLY VAL ALA\\nSEQRES  24 A  430  GLY PHE THR ASN SER LEU ARG MET LEU GLN GLN LYS ARG\\nSEQRES  25 A  430  TRP ASP GLU ALA ALA VAL ASN LEU ALA LYS SER ARG TRP\\nSEQRES  26 A  430  TYR ASN GLN THR PRO ASN ARG ALA LYS ARG VAL ILE THR\\nSEQRES  27 A  430  THR PHE ARG THR GLY THR TRP ASP ALA TYR LYS LEU SER\\nSEQRES  28 A  430  GLN GLN LYS GLU LYS LYS ALA THR GLN MET ALA ALA ILE\\nSEQRES  29 A  430  VAL ALA GLY VAL PHE ILE ILE CYS TRP LEU PRO PHE PHE\\nSEQRES  30 A  430  ILE THR HIS ILE LEU ASN ILE HIS CYS ASP CYS ASN ILE\\nSEQRES  31 A  430  PRO PRO VAL LEU TYR SER ALA PHE THR TRP LEU GLY TYR\\nSEQRES  32 A  430  VAL ASN SER ALA VAL ASN PRO ILE ILE TYR THR THR PHE\\nSEQRES  33 A  430  ASN ILE GLU PHE ARG LYS ALA PHE LEU LYS ILE LEU HIS\\nSEQRES  34 A  430  CYS\\nHET    8NU  A2001      30                                                       \\nHET    PEG  A2002       7                                                       \\nHET    PEG  A2003       7                                                       \\nHET    PEG  A2004       7                                                       \\nHET    OLA  A2005      13                                                       \\nHET    OLA  A2006      12                                                       \\nHET    OLA  A2007      20                                                       \\nHETNAM     8NU 3-[2-[4-(6-FLUORANYL-1,2-BENZOXAZOL-3-YL)PIPERIDIN-1-            \\nHETNAM   2 8NU  YL]ETHYL]-2-METHYL-6,7,8,9-TETRAHYDROPYRIDO[1,2-                \\nHETNAM   3 8NU  A]PYRIMIDIN-4-ONE                                               \\nHETNAM     PEG DI(HYDROXYETHYL)ETHER                                            \\nHETNAM     OLA OLEIC ACID                                                       \\nFORMUL   2  8NU    C23 H27 F N4 O2                                              \\nFORMUL   3  PEG    3(C4 H10 O3)                                                 \\nFORMUL   6  OLA    3(C18 H34 O2)                                                \\nFORMUL   9  HOH   *16(H2 O)                                                     \\nHELIX    1   1 ASN A   35  GLU A   62  1                                  28\\nHELIX    2   2 LYS A   63  GLN A   66  1                                   4\\nHELIX    3   3 THR A   67  LEU A   86  1                                  20\\nHELIX    4   4 VAL A   87  GLY A   98  1                                  12\\nHELIX    5   5 SER A  103  MET A  138  1                                  36\\nHELIX    6   6 TYR A  146  CYS A  168  1                                  23\\nHELIX    7   7 PRO A  169  ASN A  176  1                                   8\\nHELIX    8   8 CYS A  182  ASN A  186  1                                   5\\nHELIX    9   9 ALA A  188  VAL A  196  1                                   9\\nHELIX   10  10 PHE A  198  GLU A 1011  1                                  35\\nHELIX   11  11 SER A 1038  GLY A 1051  1                                  14\\nHELIX   12  12 THR A 1059  ASN A 1081  1                                  23\\nHELIX   13  13 LEU A 1084  LEU A 1091  1                                   8\\nHELIX   14  14 ASP A 1092  ALA A 1112  1                                  21\\nHELIX   15  15 PHE A 1114  GLN A 1123  1                                  10\\nHELIX   16  16 ARG A 1125  ALA A 1134  1                                  10\\nHELIX   17  17 SER A 1136  GLN A 1141  1                                   6\\nHELIX   18  18 THR A 1142  GLY A 1156  1                                  15\\nHELIX   19  19 GLU A  368  CYS A  399  1                                  32\\nHELIX   20  20 PRO A  404  ASN A  418  1                                  15\\nHELIX   21  21 VAL A  421  PHE A  429  1                                   9\\nHELIX   22  22 ASN A  430  LEU A  441  1                                  12\\nSHEET    1   1 1 ARG A1014  LYS A1019  0\\nSHEET    2   2 1 TYR A1025  GLY A1028  0\\nSHEET    3   3 1 HIS A1031  THR A1034  0\\nSSBOND   1 CYS A  107    CYS A  182                          1555   1555  2.03\\nSSBOND   2 CYS A  399    CYS A  401                          1555   1555  2.04\\nCRYST1   50.979   72.523  151.307  90.00  90.00  90.00 P 21 21 21    4          \\nORIGX1      1.000000  0.000000  0.000000        0.00000                         \\nORIGX2      0.000000  1.000000  0.000000        0.00000                         \\nORIGX3      0.000000  0.000000  1.000000        0.00000                         \\nSCALE1      0.019616  0.000000  0.000000        0.00000                         \\nSCALE2      0.000000  0.013789  0.000000        0.00000                         \\nSCALE3      0.000000  0.000000  0.006609        0.00000                         \\nATOM      1  N   ASN A  35      -5.317  -8.666 -16.658  1.00108.95           N\\nATOM      2  CA  ASN A  35      -3.999  -9.279 -16.550  1.00112.41           C\\nATOM      3  C   ASN A  35      -3.770  -9.829 -15.148  1.00103.98           C\\nATOM      4  O   ASN A  35      -4.596  -9.642 -14.253  1.00111.14           O\\nATOM      5  CB  ASN A  35      -2.903  -8.271 -16.904  1.00115.88           C\\nATOM      6  N   TYR A  36      -2.640 -10.512 -14.962  1.00122.79           N\\nANISOU    6  N   TYR A  36    17290  13079  16284  -1997  -3163  -3043       N\\nATOM      7  CA  TYR A  36      -2.284 -11.046 -13.653  1.00105.49           C\\nANISOU    7  CA  TYR A  36    15314  10451  14315  -2168  -3210  -2776       C\\nATOM      8  C   TYR A  36      -1.522 -10.036 -12.804  1.00100.38           C\\nANISOU    8  C   TYR A  36    14564  10022  13555  -2013  -2870  -2480       C\\nATOM      9  O   TYR A  36      -1.767  -9.933 -11.597  1.00 95.60           O\\nANISOU    9  O   TYR A  36    13979   9308  13038  -2297  -2774  -2120       O\\nATOM     10  CB  TYR A  36      -1.455 -12.323 -13.811  1.00 98.01           C\\nANISOU   10  CB  TYR A  36    14721   8957  13564  -1967  -3571  -3071       C\\nATOM     11  N   TYR A  37      -0.606  -9.280 -13.416  1.00105.86           N\\nANISOU   11  N   TYR A  37    15140  11047  14036  -1589  -2687  -2627       N\\nATOM     12  CA  TYR A  37       0.202  -8.334 -12.652  1.00101.50           C\\nANISOU   12  CA  TYR A  37    14496  10678  13392  -1434  -2394  -2372       C\\nATOM     13  C   TYR A  37      -0.596  -7.105 -12.233  1.00 97.18           C\\nANISOU   13  C   TYR A  37    13669  10521  12732  -1638  -2109  -2055       C\\nATOM     14  O   TYR A  37      -0.269  -6.474 -11.221  1.00 92.55           O\\nANISOU   14  O   TYR A  37    13035   9983  12145  -1663  -1908  -1774       O\\nATOM     15  CB  TYR A  37       1.435  -7.931 -13.459  1.00105.43           C\\nANISOU   15  CB  TYR A  37    14938  11423  13698   -962  -2294  -2627       C\\nATOM     16  CG  TYR A  37       2.442  -9.052 -13.603  1.00112.39           C\\nANISOU   16  CG  TYR A  37    16060  11928  14715   -688  -2547  -2949       C\\nATOM     17  CD1 TYR A  37       2.745  -9.880 -12.528  1.00116.25           C\\nANISOU   17  CD1 TYR A  37    16804  11893  15472   -778  -2740  -2820       C\\nATOM     18  CD2 TYR A  37       3.084  -9.291 -14.814  1.00112.70           C\\nANISOU   18  CD2 TYR A  37    16070  12145  14606   -332  -2615  -3395       C\\nATOM     19  CE1 TYR A  37       3.662 -10.907 -12.650  1.00117.63           C\\nANISOU   19  CE1 TYR A  37    17203  11682  15808   -489  -3027  -3136       C\\nATOM     20  CE2 TYR A  37       4.002 -10.320 -14.944  1.00114.52           C\\nANISOU   20  CE2 TYR A  37    16488  12042  14980    -35  -2866  -3754       C\\nATOM     21  CZ  TYR A  37       4.287 -11.123 -13.860  1.00116.82           C\\nANISOU   21  CZ  TYR A  37    17037  11766  15584    -99  -3089  -3627       C\\nATOM     22  OH  TYR A  37       5.200 -12.147 -13.987  1.00116.76           O\\nANISOU   22  OH  TYR A  37    17222  11387  15756    236  -3393  -4004       O\\nATOM     23  N   ALA A  38      -1.639  -6.750 -12.985  1.00 96.22           N\\nANISOU   23  N   ALA A  38    13359  10676  12525  -1764  -2113  -2120       N\\nATOM     24  CA  ALA A  38      -2.506  -5.655 -12.566  1.00 90.24           C\\nANISOU   24  CA  ALA A  38    12324  10255  11709  -1946  -1899  -1864       C\\nATOM     25  C   ALA A  38      -3.348  -6.039 -11.356  1.00 93.14           C\\nANISOU   25  C   ALA A  38    12686  10447  12255  -2375  -1898  -1620       C\\nATOM     26  O   ALA A  38      -3.625  -5.191 -10.500  1.00 89.27           O\\nANISOU   26  O   ALA A  38    12015  10164  11737  -2476  -1673  -1375       O\\nATOM     27  CB  ALA A  38      -3.409  -5.222 -13.721  1.00 92.04           C\\nANISOU   27  CB  ALA A  38    12349  10812  11811  -1948  -1956  -2018       C\\nATOM     28  N   THR A  39      -3.759  -7.307 -11.265  1.00101.53           N\\nANISOU   28  N   THR A  39    13946  11141  13491  -2646  -2152  -1687       N\\nATOM     29  CA  THR A  39      -4.521  -7.761 -10.105  1.00 98.62           C\\nANISOU   29  CA  THR A  39    13594  10616  13261  -3121  -2155  -1423       C\\nATOM     30  C   THR A  39      -3.673  -7.706  -8.839  1.00 94.46           C\\nANISOU   30  C   THR A  39    13228   9915  12749  -3111  -2033  -1154       C\\nATOM     31  O   THR A  39      -4.127  -7.220  -7.795  1.00 90.19           O\\nANISOU   31  O   THR A  39    12545   9551  12174  -3363  -1831   -884       O\\nATOM     32  CB  THR A  39      -5.041  -9.178 -10.345  1.00 96.91           C\\nANISOU   32  CB  THR A  39    13602   9983  13235  -3430  -2502  -1538       C\\nATOM     33  OG1 THR A  39      -5.673  -9.242 -11.631  1.00 99.65           O\\nANISOU   33  OG1 THR A  39    13821  10489  13554  -3372  -2644  -1841       O\\nATOM     34  CG2 THR A  39      -6.044  -9.566  -9.272  1.00 85.14           C\\nANISOU   34  CG2 THR A  39    12068   8436  11847  -4016  -2487  -1245       C\\nATOM     35  N   LEU A  40      -2.434  -8.202  -8.915  1.00 91.92           N\\nANISOU   35  N   LEU A  40    13187   9271  12469  -2807  -2162  -1251       N\\nATOM     36  CA  LEU A  40      -1.537  -8.138  -7.766  1.00 89.55           C\\nANISOU   36  CA  LEU A  40    13043   8803  12179  -2751  -2081  -1015       C\\nATOM     37  C   LEU A  40      -1.335  -6.702  -7.304  1.00 83.76           C\\nANISOU   37  C   LEU A  40    12038   8512  11276  -2605  -1722   -856       C\\nATOM     38  O   LEU A  40      -1.301  -6.429  -6.098  1.00 87.36           O\\nANISOU   38  O   LEU A  40    12497   8987  11709  -2775  -1584   -580       O\\nATOM     39  CB  LEU A  40      -0.191  -8.777  -8.104  1.00 87.94           C\\nANISOU   39  CB  LEU A  40    13114   8249  12051  -2357  -2285  -1222       C\\nATOM     40  CG  LEU A  40      -0.166 -10.273  -8.417  1.00 86.57           C\\nANISOU   40  CG  LEU A  40    13274   7524  12094  -2433  -2707  -1405       C\\nATOM     41  CD1 LEU A  40       1.260 -10.798  -8.334  1.00 81.27           C\\nANISOU   41  CD1 LEU A  40    12855   6507  11518  -2029  -2890  -1557       C\\nATOM     42  CD2 LEU A  40      -1.085 -11.041  -7.480  1.00 87.43           C\\nANISOU   42  CD2 LEU A  40    13549   7331  12340  -3007  -2857  -1101       C\\nATOM     43  N   LEU A  41      -1.202  -5.770  -8.248  1.00 77.53           N\\nANISOU   43  N   LEU A  41    11027   8075  10356  -2302  -1588  -1023       N\\nATOM     44  CA  LEU A  41      -1.025  -4.372  -7.871  1.00 83.20           C\\nANISOU   44  CA  LEU A  41    11504   9166  10941  -2162  -1296   -879       C\\nATOM     45  C   LEU A  41      -2.242  -3.847  -7.120  1.00 91.88           C\\nANISOU   45  C   LEU A  41    12365  10511  12032  -2501  -1145   -694       C\\nATOM     46  O   LEU A  41      -2.101  -3.145  -6.111  1.00 94.79           O\\nANISOU   46  O   LEU A  41    12646  11017  12354  -2528   -951   -503       O\\nATOM     47  CB  LEU A  41      -0.739  -3.520  -9.108  1.00 84.35           C\\nANISOU   47  CB  LEU A  41    11487   9616  10946  -1830  -1231  -1064       C\\nATOM     48  CG  LEU A  41       0.684  -3.615  -9.668  1.00 84.82           C\\nANISOU   48  CG  LEU A  41    11682   9604  10941  -1449  -1257  -1222       C\\nATOM     49  CD1 LEU A  41       0.863  -2.686 -10.856  1.00 82.66           C\\nANISOU   49  CD1 LEU A  41    11233   9703  10473  -1206  -1167  -1345       C\\nATOM     50  CD2 LEU A  41       1.708  -3.304  -8.588  1.00 84.95           C\\nANISOU   50  CD2 LEU A  41    11768   9527  10981  -1340  -1134  -1042       C\\nATOM     51  N   THR A  42      -3.447  -4.187  -7.587  1.00 91.95           N\\nANISOU   51  N   THR A  42    12247  10603  12085  -2760  -1237   -778       N\\nATOM     52  CA  THR A  42      -4.651  -3.758  -6.883  1.00 87.42           C\\nANISOU   52  CA  THR A  42    11395  10312  11509  -3092  -1095   -650       C\\nATOM     53  C   THR A  42      -4.741  -4.405  -5.507  1.00 89.21           C\\nANISOU   53  C   THR A  42    11759  10370  11767  -3467  -1059   -402       C\\nATOM     54  O   THR A  42      -5.141  -3.757  -4.533  1.00 90.48           O\\nANISOU   54  O   THR A  42    11720  10805  11853  -3617   -841   -252       O\\nATOM     55  CB  THR A  42      -5.894  -4.085  -7.708  1.00 81.63           C\\nANISOU   55  CB  THR A  42    10483   9703  10829  -3302  -1229   -812       C\\nATOM     56  OG1 THR A  42      -5.719  -3.600  -9.045  1.00 80.89           O\\nANISOU   56  OG1 THR A  42    10326   9737  10673  -2956  -1306  -1030       O\\nATOM     57  CG2 THR A  42      -7.122  -3.427  -7.095  1.00 73.78           C\\nANISOU   57  CG2 THR A  42     9102   9107   9822  -3566  -1057   -743       C\\nATOM     58  N   LEU A  43      -4.372  -5.685  -5.408  1.00 89.32           N\\nANISOU   58  N   LEU A  43    12123   9933  11882  -3624  -1291   -363       N\\nATOM     59  CA  LEU A  43      -4.291  -6.324  -4.100  1.00 89.41           C\\nANISOU   59  CA  LEU A  43    12339   9733  11900  -3975  -1300    -78       C\\nATOM     60  C   LEU A  43      -3.297  -5.599  -3.203  1.00 85.76           C\\nANISOU   60  C   LEU A  43    11923   9332  11330  -3737  -1117     75       C\\nATOM     61  O   LEU A  43      -3.540  -5.429  -2.003  1.00 86.73           O\\nANISOU   61  O   LEU A  43    12007   9591  11355  -4009   -965    311       O\\nATOM     62  CB  LEU A  43      -3.907  -7.795  -4.254  1.00 92.73           C\\nANISOU   62  CB  LEU A  43    13182   9571  12480  -4106  -1657    -74       C\\nATOM     63  N   LEU A  44      -2.173  -5.155  -3.773  1.00 83.60           N\\nANISOU   63  N   LEU A  44    11715   8995  11055  -3246  -1124    -66       N\\nATOM     64  CA  LEU A  44      -1.214  -4.375  -3.000  1.00 85.11           C\\nANISOU   64  CA  LEU A  44    11914   9267  11155  -3006   -957     53       C\\nATOM     65  C   LEU A  44      -1.839  -3.078  -2.502  1.00 85.13           C\\nANISOU   65  C   LEU A  44    11557   9754  11035  -3039   -660    109       C\\nATOM     66  O   LEU A  44      -1.633  -2.688  -1.347  1.00 86.93           O\\nANISOU   66  O   LEU A  44    11776  10082  11172  -3118   -515    286       O\\nATOM     67  CB  LEU A  44       0.031  -4.082  -3.838  1.00 87.56           C\\nANISOU   67  CB  LEU A  44    12295   9491  11483  -2502  -1005   -135       C\\nATOM     68  CG  LEU A  44       1.048  -3.125  -3.207  1.00 86.61           C\\nANISOU   68  CG  LEU A  44    12129   9496  11281  -2230   -831    -46       C\\nATOM     69  CD1 LEU A  44       1.618  -3.719  -1.930  1.00 87.91           C\\nANISOU   69  CD1 LEU A  44    12554   9391  11458  -2363   -905    175       C\\nATOM     70  CD2 LEU A  44       2.164  -2.764  -4.177  1.00 83.34           C\\nANISOU   70  CD2 LEU A  44    11712   9091  10864  -1783   -849   -246       C\\nATOM     71  N   ILE A  45      -2.611  -2.400  -3.356  1.00 82.86           N\\nANISOU   71  N   ILE A  45    10974   9766  10745  -2965   -594    -59       N\\nATOM     72  CA  ILE A  45      -3.287  -1.172  -2.940  1.00 83.78           C\\nANISOU   72  CA  ILE A  45    10732  10317  10784  -2961   -364    -56       C\\nATOM     73  C   ILE A  45      -4.154  -1.429  -1.715  1.00 85.75           C\\nANISOU   73  C   ILE A  45    10876  10734  10969  -3402   -243     98       C\\nATOM     74  O   ILE A  45      -4.169  -0.633  -0.767  1.00 85.46           O\\nANISOU   74  O   ILE A  45    10685  10954  10832  -3395    -44    165       O\\nATOM     75  CB  ILE A  45      -4.118  -0.594  -4.101  1.00 80.09           C\\nANISOU   75  CB  ILE A  45     9986  10096  10350  -2847   -391   -260       C\\nATOM     76  CG1 ILE A  45      -3.232  -0.296  -5.309  1.00 82.72           C\\nANISOU   76  CG1 ILE A  45    10426  10322  10681  -2446   -492   -386       C\\nATOM     77  CG2 ILE A  45      -4.845   0.666  -3.657  1.00 71.03           C\\nANISOU   77  CG2 ILE A  45     8464   9363   9163  -2807   -205   -292       C\\nATOM     78  CD1 ILE A  45      -3.998   0.221  -6.511  1.00 85.25           C\\nANISOU   78  CD1 ILE A  45    10525  10865  11002  -2340   -563   -559       C\\nATOM     79  N   ALA A  46      -4.887  -2.544  -1.711  1.00 89.24           N\\nANISOU   79  N   ALA A  46    11398  11053  11455  -3812   -363    150       N\\nATOM     80  CA  ALA A  46      -5.719  -2.875  -0.560  1.00 84.99           C\\nANISOU   80  CA  ALA A  46    10762  10712  10819  -4309   -240    325       C\\nATOM     81  C   ALA A  46      -4.868  -3.120   0.678  1.00 86.02           C\\nANISOU   81  C   ALA A  46    11172  10680  10833  -4395   -199    583       C\\nATOM     82  O   ALA A  46      -5.201  -2.653   1.773  1.00 82.61           O\\nANISOU   82  O   ALA A  46    10575  10580  10232  -4584     19    688       O\\nATOM     83  CB  ALA A  46      -6.581  -4.096  -0.869  1.00 77.37           C\\nANISOU   83  CB  ALA A  46     9868   9590   9938  -4771   -418    360       C\\nATOM     84  N   VAL A  47      -3.758  -3.841   0.522  1.00 84.11           N\\nANISOU   84  N   VAL A  47    11343   9946  10669  -4238   -419    662       N\\nATOM     85  CA  VAL A  47      -2.894  -4.117   1.664  1.00 83.65           C\\nANISOU   85  CA  VAL A  47    11575   9696  10512  -4292   -436    908       C\\nATOM     86  C   VAL A  47      -2.272  -2.829   2.191  1.00 82.63           C\\nANISOU   86  C   VAL A  47    11279   9847  10269  -3948   -212    871       C\\nATOM     87  O   VAL A  47      -2.139  -2.644   3.406  1.00 89.41           O\\nANISOU   87  O   VAL A  47    12171  10845  10957  -4107    -91   1051       O\\nATOM     88  CB  VAL A  47      -1.826  -5.156   1.281  1.00 85.45           C\\nANISOU   88  CB  VAL A  47    12252   9322  10892  -4129   -768    941       C\\nATOM     89  CG1 VAL A  47      -0.873  -5.397   2.438  1.00 84.04           C\\nANISOU   89  CG1 VAL A  47    12375   8931  10627  -4135   -829   1190       C\\nATOM     90  CG2 VAL A  47      -2.490  -6.457   0.863  1.00 89.97           C\\nANISOU   90  CG2 VAL A  47    13015   9574  11594  -4506  -1029    979       C\\nATOM     91  N   ILE A  48      -1.893  -1.915   1.294  1.00 78.76           N\\nANISOU   91  N   ILE A  48    10618   9450   9859  -3495   -165    645       N\\nATOM     92  CA  ILE A  48      -1.320  -0.643   1.730  1.00 77.79           C\\nANISOU   92  CA  ILE A  48    10338   9559   9659  -3180     16    603       C\\nATOM     93  C   ILE A  48      -2.344   0.158   2.522  1.00 82.81           C\\nANISOU   93  C   ILE A  48    10623  10681  10158  -3375    261    582       C\\nATOM     94  O   ILE A  48      -2.025   0.749   3.560  1.00 85.46           O\\nANISOU   94  O   ILE A  48    10924  11187  10359  -3347    400    647       O\\nATOM     95  CB  ILE A  48      -0.797   0.158   0.525  1.00 76.69           C\\nANISOU   95  CB  ILE A  48    10090   9420   9628  -2722     -7    395       C\\nATOM     96  CG1 ILE A  48       0.350  -0.582  -0.162  1.00 81.09           C\\nANISOU   96  CG1 ILE A  48    10957   9571  10283  -2498   -216    373       C\\nATOM     97  CG2 ILE A  48      -0.339   1.535   0.969  1.00 73.83           C\\nANISOU   97  CG2 ILE A  48     9552   9290   9212  -2449    157    360       C\\nATOM     98  CD1 ILE A  48       0.859   0.105  -1.411  1.00 83.26           C\\nANISOU   98  CD1 ILE A  48    11128   9896  10613  -2110   -227    183       C\\nATOM     99  N   VAL A  49      -3.590   0.189   2.047  1.00 85.62           N\\nANISOU   99  N   VAL A  49    10696  11290  10545  -3560    309    458       N\\nATOM    100  CA  VAL A  49      -4.628   0.950   2.736  1.00 86.41           C\\nANISOU  100  CA  VAL A  49    10399  11901  10530  -3713    539    369       C\\nATOM    101  C   VAL A  49      -5.028   0.256   4.033  1.00 86.76           C\\nANISOU  101  C   VAL A  49    10505  12094  10367  -4215    646    582       C\\nATOM    102  O   VAL A  49      -5.154   0.896   5.083  1.00 84.97           O\\nANISOU  102  O   VAL A  49    10110  12216   9958  -4262    848    578       O\\nATOM    103  CB  VAL A  49      -5.837   1.166   1.811  1.00 85.12           C\\nANISOU  103  CB  VAL A  49     9887  11980  10477  -3747    531    151       C\\nATOM    104  CG1 VAL A  49      -7.004   1.745   2.592  1.00 88.42           C\\nANISOU  104  CG1 VAL A  49     9863  12953  10781  -3956    756     30       C\\nATOM    105  CG2 VAL A  49      -5.456   2.084   0.662  1.00 80.88           C\\nANISOU  105  CG2 VAL A  49     9274  11370  10087  -3251    439    -34       C\\nATOM    106  N   PHE A  50      -5.229  -1.063   3.980  1.00 87.95           N\\nANISOU  106  N   PHE A  50    10908  11980  10529  -4611    497    773       N\\nATOM    107  CA  PHE A  50      -5.635  -1.794   5.177  1.00 89.88           C\\nANISOU  107  CA  PHE A  50    11255  12333  10561  -5041    554   1009       C\\nATOM    108  C   PHE A  50      -4.604  -1.654   6.289  1.00 92.06           C\\nANISOU  108  C   PHE A  50    11792  12524  10663  -4962    580   1197       C\\nATOM    109  O   PHE A  50      -4.957  -1.394   7.445  1.00 93.62           O\\nANISOU  109  O   PHE A  50    11871  13085  10613  -5087    752   1242       O\\nATOM    110  CB  PHE A  50      -5.857  -3.269   4.846  1.00 88.37           C\\nANISOU  110  CB  PHE A  50    11370  11743  10463  -5313    300   1176       C\\nATOM    111  CG  PHE A  50      -6.166  -4.119   6.048  1.00 91.54           C\\nANISOU  111  CG  PHE A  50    11945  12184  10651  -5658    293   1438       C\\nATOM    112  CD1 PHE A  50      -7.465  -4.232   6.518  1.00 92.88           C\\nANISOU  112  CD1 PHE A  50    11823  12793  10672  -5976    452   1419       C\\nATOM    113  CD2 PHE A  50      -5.157  -4.805   6.708  1.00 90.81           C\\nANISOU  113  CD2 PHE A  50    12302  11702  10500  -5665    108   1698       C\\nATOM    114  CE1 PHE A  50      -7.752  -5.011   7.623  1.00 96.10           C\\nANISOU  114  CE1 PHE A  50    12394  13265  10853  -6335    441   1672       C\\nATOM    115  CE2 PHE A  50      -5.439  -5.583   7.816  1.00 94.85           C\\nANISOU  115  CE2 PHE A  50    12982  12260  10797  -6003     73   1952       C\\nATOM    116  CZ  PHE A  50      -6.737  -5.688   8.272  1.00 98.38           C\\nANISOU  116  CZ  PHE A  50    13146  13159  11074  -6358    245   1949       C\\nATOM    117  N   GLY A  51      -3.324  -1.822   5.959  1.00 89.17           N\\nANISOU  117  N   GLY A  51    11775  11692  10415  -4731    395   1283       N\\nATOM    118  CA  GLY A  51      -2.301  -1.796   6.988  1.00 84.51           C\\nANISOU  118  CA  GLY A  51    11458  10976   9676  -4664    370   1475       C\\nATOM    119  C   GLY A  51      -2.075  -0.415   7.573  1.00 79.23           C\\nANISOU  119  C   GLY A  51    10517  10705   8881  -4366    607   1313       C\\nATOM    120  O   GLY A  51      -1.800  -0.278   8.767  1.00 79.21           O\\nANISOU  120  O   GLY A  51    10593  10866   8639  -4497    694   1454       O\\nATOM    121  N   ASN A  52      -2.183   0.626   6.746  1.00 74.87           N\\nANISOU  121  N   ASN A  52     9661  10300   8487  -3969    686   1017       N\\nATOM    122  CA  ASN A  52      -1.869   1.971   7.213  1.00 72.04           C\\nANISOU  122  CA  ASN A  52     9081  10223   8066  -3641    847    847       C\\nATOM    123  C   ASN A  52      -3.057   2.680   7.841  1.00 76.56           C\\nANISOU  123  C   ASN A  52     9223  11393   8475  -3813   1107    674       C\\nATOM    124  O   ASN A  52      -2.860   3.566   8.681  1.00 76.05           O\\nANISOU  124  O   ASN A  52     9026  11599   8272  -3672   1243    574       O\\nATOM    125  CB  ASN A  52      -1.305   2.809   6.069  1.00 68.61           C\\nANISOU  125  CB  ASN A  52     8565   9624   7879  -3132    768    642       C\\nATOM    126  CG  ASN A  52       0.113   2.416   5.715  1.00 79.96           C\\nANISOU  126  CG  ASN A  52    10362  10592   9427  -2882    569    754       C\\nATOM    127  OD1 ASN A  52       1.065   2.835   6.370  1.00 77.35           O\\nANISOU  127  OD1 ASN A  52    10144  10206   9041  -2704    566    802       O\\nATOM    128  ND2 ASN A  52       0.261   1.600   4.681  1.00 80.13           N\\nANISOU  128  ND2 ASN A  52    10547  10294   9604  -2861    393    767       N\\nATOM    129  N   VAL A  53      -4.286   2.318   7.468  1.00 82.38           N\\nANISOU  129  N   VAL A  53     9715  12360   9224  -4106   1170    606       N\\nATOM    130  CA  VAL A  53      -5.441   2.817   8.209  1.00 86.81           C\\nANISOU  130  CA  VAL A  53     9853  13535   9597  -4309   1419    435       C\\nATOM    131  C   VAL A  53      -5.398   2.300   9.643  1.00 91.28           C\\nANISOU  131  C   VAL A  53    10607  14230   9845  -4566   1474    633       C\\nATOM    132  O   VAL A  53      -5.768   3.009  10.588  1.00 98.44           O\\nANISOU  132  O   VAL A  53    11273  15582  10548  -4528   1653    471       O\\nATOM    133  CB  VAL A  53      -6.751   2.433   7.494  1.00 83.17           C\\nANISOU  133  CB  VAL A  53     9126  13231   9243  -4473   1406    307       C\\nATOM    134  CG1 VAL A  53      -7.949   2.691   8.387  1.00 78.74           C\\nANISOU  134  CG1 VAL A  53     8217  13227   8475  -4616   1596    143       C\\nATOM    135  CG2 VAL A  53      -6.893   3.217   6.198  1.00 79.84           C\\nANISOU  135  CG2 VAL A  53     8453  12777   9107  -4129   1341     45       C\\nATOM    136  N   LEU A  54      -4.923   1.065   9.827  1.00 86.53           N\\nANISOU  136  N   LEU A  54    10442  13233   9201  -4813   1292    968       N\\nATOM    137  CA  LEU A  54      -4.726   0.529  11.172  1.00 88.26           C\\nANISOU  137  CA  LEU A  54    10891  13520   9123  -5054   1288   1196       C\\nATOM    138  C   LEU A  54      -3.747   1.383  11.968  1.00 86.94           C\\nANISOU  138  C   LEU A  54    10787  13428   8817  -4810   1356   1171       C\\nATOM    139  O   LEU A  54      -4.002   1.722  13.130  1.00 94.33           O\\nANISOU  139  O   LEU A  54    11611  14759   9469  -4901   1496   1127       O\\nATOM    140  CB  LEU A  54      -4.224  -0.914  11.097  1.00 90.28           C\\nANISOU  140  CB  LEU A  54    11637  13240   9427  -5281   1006   1548       C\\nATOM    141  CG  LEU A  54      -5.198  -2.030  10.729  1.00 92.89           C\\nANISOU  141  CG  LEU A  54    11990  13500   9806  -5638    909   1650       C\\nATOM    142  CD1 LEU A  54      -4.459  -3.354  10.614  1.00 97.20           C\\nANISOU  142  CD1 LEU A  54    13055  13428  10449  -5757    575   1961       C\\nATOM    143  CD2 LEU A  54      -6.301  -2.128  11.763  1.00 96.43           C\\nANISOU  143  CD2 LEU A  54    12213  14478   9948  -5990   1090   1654       C\\nATOM    144  N   VAL A  55      -2.613   1.737  11.356  1.00 84.36           N\\nANISOU  144  N   VAL A  55    10638  12737   8678  -4508   1252   1188       N\\nATOM    145  CA  VAL A  55      -1.593   2.518  12.053  1.00 89.47           C\\nANISOU  145  CA  VAL A  55    11371  13417   9208  -4276   1291   1178       C\\nATOM    146  C   VAL A  55      -2.164   3.838  12.551  1.00 92.31           C\\nANISOU  146  C   VAL A  55    11279  14347   9446  -4112   1550    831       C\\nATOM    147  O   VAL A  55      -1.801   4.314  13.634  1.00 95.44           O\\nANISOU  147  O   VAL A  55    11689  14966   9606  -4066   1624    802       O\\nATOM    148  CB  VAL A  55      -0.374   2.741  11.133  1.00 85.96           C\\nANISOU  148  CB  VAL A  55    11134  12447   9082  -3803   1074   1151       C\\nATOM    149  CG1 VAL A  55       0.679   3.587  11.829  1.00 76.85           C\\nANISOU  149  CG1 VAL A  55    10045  11292   7864  -3476   1063   1092       C\\nATOM    150  CG2 VAL A  55       0.217   1.408  10.697  1.00 86.37           C\\nANISOU  150  CG2 VAL A  55    11619  11948   9251  -3934    799   1439       C\\nATOM    151  N   CYS A  56      -3.075   4.442  11.786  1.00 85.56           N\\nANISOU  151  N   CYS A  56    10018  13731   8759  -3998   1660    538       N\\nATOM    152  CA  CYS A  56      -3.627   5.737  12.175  1.00 80.56           C\\nANISOU  152  CA  CYS A  56     8941  13592   8075  -3762   1850    148       C\\nATOM    153  C   CYS A  56      -4.603   5.598  13.334  1.00 86.48           C\\nANISOU  153  C   CYS A  56     9514  14821   8522  -4005   1984     66       C\\nATOM    154  O   CYS A  56      -4.495   6.313  14.337  1.00 84.77           O\\nANISOU  154  O   CYS A  56     9186  14923   8102  -3899   2089   -102       O\\nATOM    155  CB  CYS A  56      -4.301   6.398  10.975  1.00 67.26           C\\nANISOU  155  CB  CYS A  56     6920  11917   6720  -3468   1818   -150       C\\nATOM    156  SG  CYS A  56      -3.139   6.859   9.688  1.00 71.11           S\\nANISOU  156  SG  CYS A  56     7652  11761   7605  -2939   1540   -134       S\\nATOM    157  N   MET A  57      -5.565   4.680  13.217  1.00 89.30           N\\nANISOU  157  N   MET A  57     9839  15250   8838  -4343   1978    170       N\\nATOM    158  CA  MET A  57      -6.547   4.508  14.283  1.00 99.11           C\\nANISOU  158  CA  MET A  57    10893  16987   9777  -4621   2115     99       C\\nATOM    159  C   MET A  57      -5.891   4.028  15.570  1.00100.31           C\\nANISOU  159  C   MET A  57    11370  17145   9601  -4843   2094    365       C\\nATOM    160  O   MET A  57      -6.282   4.448  16.665  1.00109.98           O\\nANISOU  160  O   MET A  57    12410  18838  10541  -4909   2235    210       O\\nATOM    161  CB  MET A  57      -7.633   3.529  13.845  1.00106.16           C\\nANISOU  161  CB  MET A  57    11719  17920  10695  -4975   2095    198       C\\nATOM    162  CG  MET A  57      -8.458   4.012  12.672  1.00104.93           C\\nANISOU  162  CG  MET A  57    11195  17843  10830  -4777   2113    -94       C\\nATOM    163  SD  MET A  57      -9.729   2.811  12.239  1.00106.23           S\\nANISOU  163  SD  MET A  57    11291  18073  11000  -5226   2085     28       S\\nATOM    164  CE  MET A  57      -8.718   1.360  11.965  1.00104.77           C\\nANISOU  164  CE  MET A  57    11736  17203  10870  -5491   1838    545       C\\nATOM    165  N   ALA A  58      -4.891   3.151  15.458  1.00 91.70           N\\nANISOU  165  N   ALA A  58    10761  15535   8547  -4945   1896    749       N\\nATOM    166  CA  ALA A  58      -4.253   2.590  16.647  1.00 94.86           C\\nANISOU  166  CA  ALA A  58    11502  15887   8653  -5159   1819   1033       C\\nATOM    167  C   ALA A  58      -3.578   3.673  17.478  1.00 93.98           C\\nANISOU  167  C   ALA A  58    11323  16005   8380  -4887   1912    851       C\\nATOM    168  O   ALA A  58      -3.795   3.769  18.691  1.00 97.13           O\\nANISOU  168  O   ALA A  58    11671  16787   8447  -5049   2002    828       O\\nATOM    169  CB  ALA A  58      -3.240   1.521  16.244  1.00 92.30           C\\nANISOU  169  CB  ALA A  58    11700  14899   8471  -5223   1532   1429       C\\nATOM    170  N   VAL A  59      -2.740   4.492  16.841  1.00 96.30           N\\nANISOU  170  N   VAL A  59    11619  16077   8895  -4483   1883    717       N\\nATOM    171  CA  VAL A  59      -2.102   5.595  17.551  1.00 91.92           C\\nANISOU  171  CA  VAL A  59    10983  15733   8211  -4197   1959    504       C\\nATOM    172  C   VAL A  59      -3.144   6.585  18.045  1.00 91.74           C\\nANISOU  172  C   VAL A  59    10460  16322   8077  -4097   2177     56       C\\nATOM    173  O   VAL A  59      -2.990   7.184  19.117  1.00 99.07           O\\nANISOU  173  O   VAL A  59    11313  17573   8756  -4030   2251   -105       O\\nATOM    174  CB  VAL A  59      -1.062   6.271  16.638  1.00 84.96           C\\nANISOU  174  CB  VAL A  59    10179  14491   7608  -3805   1881    441       C\\nATOM    175  CG1 VAL A  59      -0.446   7.484  17.318  1.00 88.37           C\\nANISOU  175  CG1 VAL A  59    10505  15150   7923  -3491   1949    173       C\\nATOM    176  CG2 VAL A  59       0.009   5.267  16.235  1.00 77.23           C\\nANISOU  176  CG2 VAL A  59     9704  12913   6729  -3889   1637    864       C\\nATOM    177  N   SER A  60      -4.229   6.759  17.291  1.00 95.26           N\\nANISOU  177  N   SER A  60    10557  16933   8706  -4072   2257   -169       N\\nATOM    178  CA  SER A  60      -5.247   7.733  17.658  1.00 98.05           C\\nANISOU  178  CA  SER A  60    10416  17831   9007  -3917   2417   -638       C\\nATOM    179  C   SER A  60      -6.057   7.307  18.875  1.00104.36           C\\nANISOU  179  C   SER A  60    11113  19121   9420  -4286   2535   -633       C\\nATOM    180  O   SER A  60      -6.732   8.148  19.479  1.00107.43           O\\nANISOU  180  O   SER A  60    11125  20003   9691  -4157   2661  -1033       O\\nATOM    181  CB  SER A  60      -6.183   7.974  16.473  1.00 97.14           C\\nANISOU  181  CB  SER A  60     9973  17730   9205  -3784   2427   -864       C\\nATOM    182  OG  SER A  60      -7.148   8.967  16.770  1.00 99.99           O\\nANISOU  182  OG  SER A  60     9859  18573   9559  -3574   2531  -1349       O\\nATOM    183  N   ARG A  61      -6.003   6.030  19.255  1.00 98.78           N\\nANISOU  183  N   ARG A  61    10729  18286   8518  -4738   2478   -202       N\\nATOM    184  CA  ARG A  61      -6.880   5.512  20.291  1.00103.46           C\\nANISOU  184  CA  ARG A  61    11212  19353   8745  -5156   2589   -162       C\\nATOM    185  C   ARG A  61      -6.159   4.772  21.410  1.00107.55           C\\nANISOU  185  C   ARG A  61    12131  19803   8928  -5464   2513    219       C\\nATOM    186  O   ARG A  61      -6.808   4.395  22.392  1.00117.52           O\\nANISOU  186  O   ARG A  61    13311  21498   9842  -5828   2609    262       O\\nATOM    187  CB  ARG A  61      -7.937   4.590  19.664  1.00104.53           C\\nANISOU  187  CB  ARG A  61    11265  19502   8951  -5497   2593    -37       C\\nATOM    188  CG  ARG A  61      -8.730   5.267  18.557  1.00 96.67           C\\nANISOU  188  CG  ARG A  61     9865  18588   8277  -5209   2647   -407       C\\nATOM    189  CD  ARG A  61     -10.016   4.534  18.248  1.00108.57           C\\nANISOU  189  CD  ARG A  61    11174  20320   9758  -5564   2702   -387       C\\nATOM    190  NE  ARG A  61      -9.801   3.362  17.409  1.00109.71           N\\nANISOU  190  NE  ARG A  61    11662  19943  10079  -5797   2536     11       N\\nATOM    191  CZ  ARG A  61     -10.778   2.566  16.987  1.00115.93           C\\nANISOU  191  CZ  ARG A  61    12357  20800  10890  -6123   2537     93       C\\nATOM    192  NH1 ARG A  61     -12.034   2.820  17.330  1.00116.46           N\\nANISOU  192  NH1 ARG A  61    11988  21459  10801  -6264   2710   -185       N\\nATOM    193  NH2 ARG A  61     -10.501   1.519  16.223  1.00119.11           N\\nANISOU  193  NH2 ARG A  61    13096  20686  11475  -6303   2354    434       N\\nATOM    194  N   GLU A  62      -4.853   4.558  21.301  1.00 96.97           N\\nANISOU  194  N   GLU A  62    11215  17953   7675  -5333   2333    491       N\\nATOM    195  CA  GLU A  62      -4.083   3.859  22.320  1.00101.43           C\\nANISOU  195  CA  GLU A  62    12192  18393   7956  -5580   2207    858       C\\nATOM    196  C   GLU A  62      -3.184   4.851  23.046  1.00102.22           C\\nANISOU  196  C   GLU A  62    12307  18603   7928  -5257   2227    678       C\\nATOM    197  O   GLU A  62      -2.426   5.591  22.409  1.00 92.57           O\\nANISOU  197  O   GLU A  62    11100  17116   6955  -4842   2178    531       O\\nATOM    198  CB  GLU A  62      -3.246   2.737  21.703  1.00100.84           C\\nANISOU  198  CB  GLU A  62    12621  17618   8074  -5678   1928   1315       C\\nATOM    199  N   LYS A  63      -3.269   4.854  24.378  1.00108.00           N\\nANISOU  199  N   LYS A  63    13040  19738   8259  -5463   2293    691       N\\nATOM    200  CA  LYS A  63      -2.467   5.770  25.183  1.00106.16           C\\nANISOU  200  CA  LYS A  63    12820  19652   7864  -5180   2305    504       C\\nATOM    201  C   LYS A  63      -0.976   5.535  24.970  1.00 98.83           C\\nANISOU  201  C   LYS A  63    12367  18125   7059  -4996   2054    800       C\\nATOM    202  O   LYS A  63      -0.243   6.439  24.552  1.00 90.24           O\\nANISOU  202  O   LYS A  63    11250  16879   6157  -4571   2024    584       O\\nATOM    203  CB  LYS A  63      -2.833   5.616  26.660  1.00114.28           C\\nANISOU  203  CB  LYS A  63    13807  21206   8408  -5502   2401    526       C\\nATOM    204  N   ALA A  64      -0.510   4.312  25.239  1.00108.15           N\\nANISOU  204  N   ALA A  64    13988  18956   8148  -5308   1844   1286       N\\nATOM    205  CA  ALA A  64       0.917   4.011  25.200  1.00103.75           C\\nANISOU  205  CA  ALA A  64    13892  17853   7678  -5142   1563   1569       C\\nATOM    206  C   ALA A  64       1.513   4.169  23.805  1.00 99.33           C\\nANISOU  206  C   ALA A  64    13405  16779   7558  -4812   1452   1552       C\\nATOM    207  O   ALA A  64       2.735   4.041  23.649  1.00 84.58           O\\nANISOU  207  O   ALA A  64    11875  14464   5799  -4615   1215   1732       O\\nATOM    208  CB  ALA A  64       1.164   2.590  25.719  1.00103.60           C\\nANISOU  208  CB  ALA A  64    14310  17538   7516  -5540   1320   2073       C\\nATOM    209  N   LEU A  65       0.685   4.450  22.798  1.00 91.85           N\\nANISOU  209  N   LEU A  65    12140  15902   6858  -4745   1606   1334       N\\nATOM    210  CA  LEU A  65       1.126   4.676  21.429  1.00 92.45           C\\nANISOU  210  CA  LEU A  65    12233  15560   7334  -4450   1535   1288       C\\nATOM    211  C   LEU A  65       1.071   6.143  21.021  1.00 91.55           C\\nANISOU  211  C   LEU A  65    11741  15700   7344  -4047   1715    824       C\\nATOM    212  O   LEU A  65       1.216   6.447  19.835  1.00 98.95           O\\nANISOU  212  O   LEU A  65    12606  16387   8603  -3825   1705    736       O\\nATOM    213  CB  LEU A  65       0.282   3.842  20.465  1.00 91.67           C\\nANISOU  213  CB  LEU A  65    12087  15284   7459  -4662   1529   1402       C\\nATOM    214  CG  LEU A  65       0.533   2.337  20.472  1.00 96.52           C\\nANISOU  214  CG  LEU A  65    13133  15448   8091  -4973   1266   1854       C\\nATOM    215  CD1 LEU A  65      -0.389   1.627  19.490  1.00101.66           C\\nANISOU  215  CD1 LEU A  65    13694  15972   8962  -5162   1269   1895       C\\nATOM    216  CD2 LEU A  65       1.987   2.059  20.143  1.00 88.49           C\\nANISOU  216  CD2 LEU A  65    12531  13837   7256  -4733    974   2071       C\\nATOM    217  N   GLN A  66       0.870   7.056  21.966  1.00 97.64           N\\nANISOU  217  N   GLN A  66    12271  16951   7878  -3940   1858    509       N\\nATOM    218  CA  GLN A  66       0.729   8.476  21.643  1.00 91.59           C\\nANISOU  218  CA  GLN A  66    11125  16421   7256  -3531   1991      9       C\\nATOM    219  C   GLN A  66       2.014   9.220  22.003  1.00 88.27           C\\nANISOU  219  C   GLN A  66    10883  15873   6783  -3219   1872    -76       C\\nATOM    220  O   GLN A  66       2.081  10.015  22.940  1.00 95.43           O\\nANISOU  220  O   GLN A  66    11654  17116   7488  -3077   1921   -364       O\\nATOM    221  CB  GLN A  66      -0.488   9.060  22.354  1.00 94.21           C\\nANISOU  221  CB  GLN A  66    11011  17366   7418  -3569   2200   -377       C\\nATOM    222  CG  GLN A  66      -1.806   8.615  21.747  1.00 90.38           C\\nANISOU  222  CG  GLN A  66    10255  17032   7053  -3778   2313   -412       C\\nATOM    223  CD  GLN A  66      -3.010   9.067  22.544  1.00 98.45           C\\nANISOU  223  CD  GLN A  66    10853  18690   7865  -3861   2497   -767       C\\nATOM    224  OE1 GLN A  66      -2.887   9.506  23.689  1.00102.35           O\\nANISOU  224  OE1 GLN A  66    11295  19524   8070  -3847   2548   -921       O\\nATOM    225  NE2 GLN A  66      -4.187   8.960  21.941  1.00101.41           N\\nANISOU  225  NE2 GLN A  66    10914  19243   8376  -3945   2588   -913       N\\nATOM    226  N   THR A  67       3.049   8.942  21.221  1.00 81.40           N\\nANISOU  226  N   THR A  67    10313  14420   6193  -3058   1648    159       N\\nATOM    227  CA  THR A  67       4.366   9.523  21.416  1.00 80.16           C\\nANISOU  227  CA  THR A  67    10341  13928   6189  -2690   1412    112       C\\nATOM    228  C   THR A  67       4.724  10.396  20.219  1.00 81.81           C\\nANISOU  228  C   THR A  67    10385  13739   6959  -2223   1303   -122       C\\nATOM    229  O   THR A  67       4.047  10.388  19.187  1.00 83.11           O\\nANISOU  229  O   THR A  67    10366  13821   7392  -2189   1372   -182       O\\nATOM    230  CB  THR A  67       5.424   8.430  21.618  1.00 74.28           C\\nANISOU  230  CB  THR A  67    10089  12752   5384  -2838   1150    588       C\\nATOM    231  OG1 THR A  67       5.732   7.823  20.359  1.00 77.15           O\\nANISOU  231  OG1 THR A  67    10579  12565   6169  -2749   1000    784       O\\nATOM    232  CG2 THR A  67       4.909   7.358  22.566  1.00 76.90           C\\nANISOU  232  CG2 THR A  67    10631  13398   5190  -3391   1228    928       C\\nATOM    233  N   THR A  68       5.803  11.165  20.370  1.00 86.60           N\\nANISOU  233  N   THR A  68    11062  14111   7731  -1884   1119   -244       N\\nATOM    234  CA  THR A  68       6.274  11.984  19.259  1.00 81.90           C\\nANISOU  234  CA  THR A  68    10353  13120   7646  -1492    990   -405       C\\nATOM    235  C   THR A  68       6.614  11.116  18.055  1.00 76.38           C\\nANISOU  235  C   THR A  68     9828  11956   7236  -1519    883    -94       C\\nATOM    236  O   THR A  68       6.157  11.379  16.939  1.00 74.99           O\\nANISOU  236  O   THR A  68     9479  11652   7360  -1401    915   -182       O\\nATOM    237  CB  THR A  68       7.490  12.816  19.681  1.00 80.77           C\\nANISOU  237  CB  THR A  68    10291  12786   7611  -1198    788   -526       C\\nATOM    238  OG1 THR A  68       8.582  11.948  20.014  1.00 75.97           O\\nANISOU  238  OG1 THR A  68    10037  11917   6911  -1290    604   -182       O\\nATOM    239  CG2 THR A  68       7.155  13.692  20.878  1.00 83.25           C\\nANISOU  239  CG2 THR A  68    10436  13561   7636  -1147    872   -884       C\\nATOM    240  N   THR A  69       7.412  10.066  18.270  1.00 78.37           N\\nANISOU  240  N   THR A  69    10426  11955   7395  -1662    733    255       N\\nATOM    241  CA  THR A  69       7.811   9.195  17.168  1.00 78.88           C\\nANISOU  241  CA  THR A  69    10662  11578   7732  -1656    605    503       C\\nATOM    242  C   THR A  69       6.596   8.584  16.482  1.00 78.27           C\\nANISOU  242  C   THR A  69    10482  11594   7664  -1890    759    558       C\\nATOM    243  O   THR A  69       6.522   8.550  15.247  1.00 73.15           O\\nANISOU  243  O   THR A  69     9763  10702   7330  -1761    732    539       O\\nATOM    244  CB  THR A  69       8.748   8.097  17.676  1.00 76.37           C\\nANISOU  244  CB  THR A  69    10733  11000   7285  -1777    388    839       C\\nATOM    245  OG1 THR A  69       9.982   8.680  18.112  1.00 72.19           O\\nANISOU  245  OG1 THR A  69    10268  10338   6821  -1513    212    771       O\\nATOM    246  CG2 THR A  69       9.035   7.083  16.582  1.00 74.02           C\\nANISOU  246  CG2 THR A  69    10604  10273   7247  -1776    252   1050       C\\nATOM    247  N   ASN A  70       5.625   8.114  17.269  1.00 82.86           N\\nANISOU  247  N   ASN A  70    11039  12561   7884  -2256    925    618       N\\nATOM    248  CA  ASN A  70       4.436   7.496  16.698  1.00 81.91           C\\nANISOU  248  CA  ASN A  70    10800  12565   7757  -2530   1069    672       C\\nATOM    249  C   ASN A  70       3.562   8.494  15.947  1.00 81.00           C\\nANISOU  249  C   ASN A  70    10269  12649   7860  -2327   1221    314       C\\nATOM    250  O   ASN A  70       2.805   8.084  15.063  1.00 74.10           O\\nANISOU  250  O   ASN A  70     9290  11736   7128  -2431   1271    335       O\\nATOM    251  CB  ASN A  70       3.629   6.801  17.798  1.00 79.20           C\\nANISOU  251  CB  ASN A  70    10505  12647   6942  -3020   1221    832       C\\nATOM    252  CG  ASN A  70       4.333   5.581  18.348  1.00 78.28           C\\nANISOU  252  CG  ASN A  70    10856  12250   6638  -3286   1014   1268       C\\nATOM    253  OD1 ASN A  70       5.224   5.030  17.706  1.00 74.09           O\\nANISOU  253  OD1 ASN A  70    10588  11183   6379  -3127    762   1443       O\\nATOM    254  ND2 ASN A  70       3.941   5.152  19.542  1.00 73.15           N\\nANISOU  254  ND2 ASN A  70    10308  11972   5512  -3692   1103   1439       N\\nATOM    255  N   TYR A  71       3.640   9.786  16.274  1.00 84.07           N\\nANISOU  255  N   TYR A  71    10427  13227   8291  -2033   1261    -20       N\\nATOM    256  CA  TYR A  71       2.933  10.782  15.475  1.00 77.80           C\\nANISOU  256  CA  TYR A  71     9275  12516   7768  -1780   1321   -352       C\\nATOM    257  C   TYR A  71       3.632  11.001  14.143  1.00 70.85           C\\nANISOU  257  C   TYR A  71     8477  11134   7310  -1497   1135   -290       C\\nATOM    258  O   TYR A  71       2.978  11.216  13.117  1.00 65.56           O\\nANISOU  258  O   TYR A  71     7626  10422   6864  -1416   1148   -386       O\\nATOM    259  CB  TYR A  71       2.809  12.094  16.246  1.00 74.68           C\\nANISOU  259  CB  TYR A  71     8632  12431   7314  -1540   1370   -746       C\\nATOM    260  CG  TYR A  71       1.783  12.035  17.350  1.00 80.29           C\\nANISOU  260  CG  TYR A  71     9123  13772   7611  -1796   1612   -924       C\\nATOM    261  CD1 TYR A  71       0.690  11.189  17.253  1.00 82.22           C\\nANISOU  261  CD1 TYR A  71     9248  14311   7681  -2164   1796   -825       C\\nATOM    262  CD2 TYR A  71       1.912  12.814  18.492  1.00 84.10           C\\nANISOU  262  CD2 TYR A  71     9504  14589   7861  -1688   1658  -1202       C\\nATOM    263  CE1 TYR A  71      -0.250  11.123  18.258  1.00 91.89           C\\nANISOU  263  CE1 TYR A  71    10236  16183   8495  -2441   2045   -986       C\\nATOM    264  CE2 TYR A  71       0.976  12.756  19.503  1.00 85.39           C\\nANISOU  264  CE2 TYR A  71     9439  15406   7599  -1932   1905  -1392       C\\nATOM    265  CZ  TYR A  71      -0.103  11.907  19.381  1.00 94.33           C\\nANISOU  265  CZ  TYR A  71    10434  16859   8548  -2320   2110  -1275       C\\nATOM    266  OH  TYR A  71      -1.045  11.839  20.381  1.00 99.85           O\\nANISOU  266  OH  TYR A  71    10911  18103   8926  -2541   2275  -1429       O\\nATOM    267  N   LEU A  72       4.963  10.950  14.139  1.00 66.28           N\\nANISOU  267  N   LEU A  72     8155  10205   6825  -1355    960   -134       N\\nATOM    268  CA  LEU A  72       5.688  10.938  12.880  1.00 65.47           C\\nANISOU  268  CA  LEU A  72     8142   9678   7057  -1158    810    -34       C\\nATOM    269  C   LEU A  72       5.520   9.612  12.156  1.00 66.26           C\\nANISOU  269  C   LEU A  72     8411   9590   7173  -1363    790    218       C\\nATOM    270  O   LEU A  72       5.755   9.545  10.947  1.00 70.26           O\\nANISOU  270  O   LEU A  72     8925   9843   7928  -1232    713    248       O\\nATOM    271  CB  LEU A  72       7.166  11.237  13.129  1.00 68.98           C\\nANISOU  271  CB  LEU A  72     8763   9860   7585   -964    640     32       C\\nATOM    272  CG  LEU A  72       7.464  12.668  13.586  1.00 71.02           C\\nANISOU  272  CG  LEU A  72     8861  10200   7924   -721    600   -231       C\\nATOM    273  CD1 LEU A  72       8.795  12.745  14.308  1.00 68.45           C\\nANISOU  273  CD1 LEU A  72     8719   9732   7557   -638    454   -157       C\\nATOM    274  CD2 LEU A  72       7.449  13.618  12.399  1.00 69.98           C\\nANISOU  274  CD2 LEU A  72     8565   9884   8138   -488    531   -351       C\\nATOM    275  N   ILE A  73       5.112   8.562  12.866  1.00 69.01           N\\nANISOU  275  N   ILE A  73     8906  10062   7254  -1697    844    397       N\\nATOM    276  CA  ILE A  73       4.844   7.288  12.214  1.00 67.68           C\\nANISOU  276  CA  ILE A  73     8907   9691   7118  -1917    795    618       C\\nATOM    277  C   ILE A  73       3.522   7.340  11.460  1.00 71.94           C\\nANISOU  277  C   ILE A  73     9183  10422   7728  -2023    929    489       C\\nATOM    278  O   ILE A  73       3.411   6.809  10.350  1.00 75.02           O\\nANISOU  278  O   ILE A  73     9617  10582   8307  -2015    856    546       O\\nATOM    279  CB  ILE A  73       4.880   6.148  13.249  1.00 69.17           C\\nANISOU  279  CB  ILE A  73     9379   9898   7006  -2275    759    894       C\\nATOM    280  CG1 ILE A  73       6.327   5.743  13.542  1.00 66.13           C\\nANISOU  280  CG1 ILE A  73     9319   9150   6659  -2128    522   1069       C\\nATOM    281  CG2 ILE A  73       4.072   4.944  12.777  1.00 68.47           C\\nANISOU  281  CG2 ILE A  73     9386   9730   6900  -2615    755   1076       C\\nATOM    282  CD1 ILE A  73       6.453   4.548  14.461  1.00 67.07           C\\nANISOU  282  CD1 ILE A  73     9782   9188   6514  -2462    402   1387       C\\nATOM    283  N   VAL A  74       2.507   7.996  12.029  1.00 70.79           N\\nANISOU  283  N   VAL A  74     8739  10720   7436  -2102   1115    280       N\\nATOM    284  CA  VAL A  74       1.244   8.128  11.308  1.00 74.58           C\\nANISOU  284  CA  VAL A  74     8921  11407   8009  -2166   1221    118       C\\nATOM    285  C   VAL A  74       1.392   9.116  10.161  1.00 73.54           C\\nANISOU  285  C   VAL A  74     8633  11099   8211  -1776   1127    -73       C\\nATOM    286  O   VAL A  74       0.708   8.995   9.137  1.00 75.63           O\\nANISOU  286  O   VAL A  74     8769  11334   8631  -1776   1112   -121       O\\nATOM    287  CB  VAL A  74       0.095   8.527  12.256  1.00 73.62           C\\nANISOU  287  CB  VAL A  74     8477  11862   7633  -2350   1446    -95       C\\nATOM    288  CG1 VAL A  74       0.133   7.692  13.523  1.00 69.23           C\\nANISOU  288  CG1 VAL A  74     8110  11512   6684  -2747   1535    127       C\\nATOM    289  CG2 VAL A  74       0.126  10.011  12.581  1.00 69.08           C\\nANISOU  289  CG2 VAL A  74     7641  11478   7130  -1988   1471   -451       C\\nATOM    290  N   SER A  75       2.276  10.106  10.306  1.00 69.43           N\\nANISOU  290  N   SER A  75     8129  10455   7797  -1464   1043   -169       N\\nATOM    291  CA  SER A  75       2.644  10.933   9.164  1.00 66.75           C\\nANISOU  291  CA  SER A  75     7729   9871   7764  -1146    912   -253       C\\nATOM    292  C   SER A  75       3.278  10.082   8.075  1.00 68.29           C\\nANISOU  292  C   SER A  75     8151   9714   8082  -1158    801    -30       C\\nATOM    293  O   SER A  75       3.025  10.291   6.882  1.00 67.91           O\\nANISOU  293  O   SER A  75     8025   9564   8214  -1048    739    -65       O\\nATOM    294  CB  SER A  75       3.595  12.044   9.605  1.00 65.59           C\\nANISOU  294  CB  SER A  75     7599   9627   7697   -876    823   -350       C\\nATOM    295  OG  SER A  75       4.148  12.722   8.492  1.00 65.64           O\\nANISOU  295  OG  SER A  75     7609   9355   7975   -636    678   -344       O\\nATOM    296  N   LEU A  76       4.099   9.107   8.470  1.00 69.61           N\\nANISOU  296  N   LEU A  76     8600   9702   8145  -1281    755    185       N\\nATOM    297  CA  LEU A  76       4.653   8.169   7.503  1.00 70.39           C\\nANISOU  297  CA  LEU A  76     8904   9490   8352  -1284    641    344       C\\nATOM    298  C   LEU A  76       3.555   7.304   6.898  1.00 71.56           C\\nANISOU  298  C   LEU A  76     9015   9685   8488  -1514    675    369       C\\nATOM    299  O   LEU A  76       3.587   6.994   5.700  1.00 67.72           O\\nANISOU  299  O   LEU A  76     8556   9030   8146  -1442    597    372       O\\nATOM    300  CB  LEU A  76       5.725   7.307   8.170  1.00 71.65           C\\nANISOU  300  CB  LEU A  76     9365   9437   8421  -1339    541    534       C\\nATOM    301  CG  LEU A  76       6.488   6.311   7.296  1.00 73.93           C\\nANISOU  301  CG  LEU A  76     9872   9386   8833  -1283    387    648       C\\nATOM    302  CD1 LEU A  76       7.050   6.993   6.057  1.00 66.82           C\\nANISOU  302  CD1 LEU A  76     8859   8395   8135  -1003    352    542       C\\nATOM    303  CD2 LEU A  76       7.598   5.643   8.104  1.00 66.32           C\\nANISOU  303  CD2 LEU A  76     9178   8218   7804  -1274    247    796       C\\nATOM    304  N   ALA A  77       2.567   6.918   7.708  1.00 76.17           N\\nANISOU  304  N   ALA A  77     9525  10531   8886  -1810    794    379       N\\nATOM    305  CA  ALA A  77       1.468   6.103   7.203  1.00 75.85           C\\nANISOU  305  CA  ALA A  77     9422  10562   8836  -2078    825    401       C\\nATOM    306  C   ALA A  77       0.603   6.875   6.217  1.00 76.40           C\\nANISOU  306  C   ALA A  77     9182  10781   9066  -1929    853    183       C\\nATOM    307  O   ALA A  77       0.034   6.277   5.295  1.00 74.94           O\\nANISOU  307  O   ALA A  77     8980  10529   8965  -2027    802    189       O\\nATOM    308  CB  ALA A  77       0.618   5.589   8.364  1.00 77.54           C\\nANISOU  308  CB  ALA A  77     9590  11086   8784  -2476    967    470       C\\nATOM    309  N   VAL A  78       0.484   8.192   6.395  1.00 72.57           N\\nANISOU  309  N   VAL A  78     8462  10479   8634  -1687    898    -17       N\\nATOM    310  CA  VAL A  78      -0.263   9.001   5.438  1.00 73.72           C\\nANISOU  310  CA  VAL A  78     8340  10714   8956  -1502    861   -213       C\\nATOM    311  C   VAL A  78       0.492   9.092   4.118  1.00 73.77           C\\nANISOU  311  C   VAL A  78     8495  10392   9143  -1286    699   -137       C\\nATOM    312  O   VAL A  78      -0.108   9.025   3.037  1.00 75.36           O\\nANISOU  312  O   VAL A  78     8606  10583   9444  -1265    631   -185       O\\nATOM    313  CB  VAL A  78      -0.556  10.391   6.030  1.00 69.67           C\\nANISOU  313  CB  VAL A  78     7563  10433   8477  -1281    899   -460       C\\nATOM    314  CG1 VAL A  78      -1.042  11.346   4.951  1.00 67.83           C\\nANISOU  314  CG1 VAL A  78     7129  10169   8475  -1016    769   -625       C\\nATOM    315  CG2 VAL A  78      -1.591  10.281   7.138  1.00 54.88           C\\nANISOU  315  CG2 VAL A  78     5447   9002   6402  -1505   1086   -609       C\\nATOM    316  N   ALA A  79       1.819   9.239   4.180  1.00 71.40           N\\nANISOU  316  N   ALA A  79     8408   9854   8865  -1136    637    -25       N\\nATOM    317  CA  ALA A  79       2.617   9.243   2.959  1.00 72.25           C\\nANISOU  317  CA  ALA A  79     8642   9715   9095   -969    515     48       C\\nATOM    318  C   ALA A  79       2.382   7.976   2.148  1.00 78.12           C\\nANISOU  318  C   ALA A  79     9512  10348   9824  -1122    472    118       C\\nATOM    319  O   ALA A  79       2.254   8.030   0.919  1.00 82.23           O\\nANISOU  319  O   ALA A  79    10005  10818  10420  -1035    394     87       O\\nATOM    320  CB  ALA A  79       4.097   9.398   3.301  1.00 67.24           C\\nANISOU  320  CB  ALA A  79     8191   8894   8464   -836    476    149       C\\nATOM    321  N   ASP A  80       2.306   6.826   2.820  1.00 70.96           N\\nANISOU  321  N   ASP A  80     8756   9392   8812  -1362    499    214       N\\nATOM    322  CA  ASP A  80       2.041   5.580   2.113  1.00 74.85           C\\nANISOU  322  CA  ASP A  80     9387   9736   9318  -1522    420    263       C\\nATOM    323  C   ASP A  80       0.578   5.468   1.707  1.00 70.40           C\\nANISOU  323  C   ASP A  80     8610   9377   8763  -1703    452    165       C\\nATOM    324  O   ASP A  80       0.275   4.919   0.641  1.00 75.04           O\\nANISOU  324  O   ASP A  80     9225   9874   9413  -1725    358    129       O\\nATOM    325  CB  ASP A  80       2.453   4.386   2.975  1.00 85.13           C\\nANISOU  325  CB  ASP A  80    10957  10859  10529  -1735    379    424       C\\nATOM    326  CG  ASP A  80       3.955   4.316   3.193  1.00 91.73           C\\nANISOU  326  CG  ASP A  80    12008  11459  11389  -1526    293    497       C\\nATOM    327  OD1 ASP A  80       4.707   4.814   2.326  1.00 90.12           O\\nANISOU  327  OD1 ASP A  80    11774  11187  11279  -1257    253    424       O\\nATOM    328  OD2 ASP A  80       4.383   3.762   4.231  1.00 93.76           O\\nANISOU  328  OD2 ASP A  80    12452  11616  11555  -1644    259    631       O\\nATOM    329  N   LEU A  81      -0.340   5.974   2.535  1.00 74.65           N\\nANISOU  329  N   LEU A  81     8912  10218   9233  -1827    580     91       N\\nATOM    330  CA  LEU A  81      -1.751   5.961   2.159  1.00 71.55           C\\nANISOU  330  CA  LEU A  81     8249  10074   8865  -1978    612    -40       C\\nATOM    331  C   LEU A  81      -2.001   6.765   0.893  1.00 74.65           C\\nANISOU  331  C   LEU A  81     8488  10471   9406  -1709    505   -178       C\\nATOM    332  O   LEU A  81      -2.886   6.418   0.105  1.00 69.21           O\\nANISOU  332  O   LEU A  81     7680   9851   8766  -1803    444   -254       O\\nATOM    333  CB  LEU A  81      -2.611   6.504   3.297  1.00 69.87           C\\nANISOU  333  CB  LEU A  81     7752  10250   8545  -2106    782   -153       C\\nATOM    334  CG  LEU A  81      -3.075   5.485   4.331  1.00 74.99           C\\nANISOU  334  CG  LEU A  81     8452  11043   8999  -2544    901    -27       C\\nATOM    335  CD1 LEU A  81      -3.852   6.179   5.437  1.00 74.69           C\\nANISOU  335  CD1 LEU A  81     8087  11477   8814  -2632   1099   -186       C\\nATOM    336  CD2 LEU A  81      -3.924   4.409   3.669  1.00 73.03           C\\nANISOU  336  CD2 LEU A  81     8197  10767   8785  -2854    842     14       C\\nATOM    337  N   LEU A  82      -1.237   7.838   0.678  1.00 69.87           N\\nANISOU  337  N   LEU A  82     7892   9789   8867  -1397    460   -196       N\\nATOM    338  CA  LEU A  82      -1.409   8.637  -0.529  1.00 65.99           C\\nANISOU  338  CA  LEU A  82     7299   9280   8492  -1167    327   -272       C\\nATOM    339  C   LEU A  82      -0.757   7.982  -1.740  1.00 70.21           C\\nANISOU  339  C   LEU A  82     8057   9596   9025  -1131    218   -180       C\\nATOM    340  O   LEU A  82      -1.178   8.231  -2.875  1.00 71.57           O\\nANISOU  340  O   LEU A  82     8160   9794   9239  -1047    101   -233       O\\nATOM    341  CB  LEU A  82      -0.848  10.040  -0.313  1.00 59.37           C\\nANISOU  341  CB  LEU A  82     6407   8421   7728   -892    291   -300       C\\nATOM    342  CG  LEU A  82      -1.644  10.851   0.706  1.00 62.33           C\\nANISOU  342  CG  LEU A  82     6510   9044   8130   -856    360   -482       C\\nATOM    343  CD1 LEU A  82      -1.091  12.261   0.855  1.00 55.10           C\\nANISOU  343  CD1 LEU A  82     5564   8044   7327   -570    267   -530       C\\nATOM    344  CD2 LEU A  82      -3.114  10.883   0.314  1.00 64.42           C\\nANISOU  344  CD2 LEU A  82     6475   9550   8451   -907    325   -667       C\\nATOM    345  N   VAL A  83       0.261   7.147  -1.524  1.00 71.76           N\\nANISOU  345  N   VAL A  83     8510   9592   9162  -1179    238    -64       N\\nATOM    346  CA  VAL A  83       0.813   6.355  -2.620  1.00 69.53           C\\nANISOU  346  CA  VAL A  83     8414   9139   8867  -1147    140    -43       C\\nATOM    347  C   VAL A  83      -0.238   5.394  -3.158  1.00 73.89           C\\nANISOU  347  C   VAL A  83     8937   9715   9422  -1353     76   -116       C\\nATOM    348  O   VAL A  83      -0.404   5.247  -4.375  1.00 79.13           O\\nANISOU  348  O   VAL A  83     9606  10373  10087  -1289    -32   -185       O\\nATOM    349  CB  VAL A  83       2.078   5.608  -2.159  1.00 61.51           C\\nANISOU  349  CB  VAL A  83     7653   7900   7818  -1130    147     49       C\\nATOM    350  CG1 VAL A  83       2.537   4.623  -3.222  1.00 56.33           C\\nANISOU  350  CG1 VAL A  83     7164   7084   7153  -1094     37      1       C\\nATOM    351  CG2 VAL A  83       3.187   6.592  -1.827  1.00 55.01           C\\nANISOU  351  CG2 VAL A  83     6836   7065   7001   -921    189    106       C\\nATOM    352  N   ALA A  84      -0.973   4.732  -2.264  1.00 63.07           N\\nANISOU  352  N   ALA A  84     7532   8393   8036  -1628    136   -100       N\\nATOM    353  CA  ALA A  84      -1.979   3.777  -2.713  1.00 68.51           C\\nANISOU  353  CA  ALA A  84     8190   9097   8744  -1877     65   -159       C\\nATOM    354  C   ALA A  84      -3.109   4.458  -3.475  1.00 67.78           C\\nANISOU  354  C   ALA A  84     7803   9251   8701  -1831     21   -306       C\\nATOM    355  O   ALA A  84      -3.668   3.871  -4.408  1.00 63.21           O\\nANISOU  355  O   ALA A  84     7217   8653   8146  -1911   -101   -386       O\\nATOM    356  CB  ALA A  84      -2.540   3.003  -1.520  1.00 70.03           C\\nANISOU  356  CB  ALA A  84     8393   9327   8888  -2241    149    -72       C\\nATOM    357  N   THR A  85      -3.449   5.692  -3.108  1.00 59.88           N\\nANISOU  357  N   THR A  85     6561   8463   7726  -1685     85   -362       N\\nATOM    358  CA  THR A  85      -4.630   6.368  -3.632  1.00 70.05           C\\nANISOU  358  CA  THR A  85     7536   9994   9087  -1632     16   -521       C\\nATOM    359  C   THR A  85      -4.329   7.352  -4.758  1.00 73.23           C\\nANISOU  359  C   THR A  85     7938  10354   9531  -1316   -140   -540       C\\nATOM    360  O   THR A  85      -5.144   7.493  -5.674  1.00 73.60           O\\nANISOU  360  O   THR A  85     7844  10501   9619  -1283   -285   -640       O\\nATOM    361  CB  THR A  85      -5.355   7.103  -2.501  1.00 66.86           C\\nANISOU  361  CB  THR A  85     6829   9873   8704  -1660    148   -625       C\\nATOM    362  OG1 THR A  85      -4.432   7.958  -1.812  1.00 68.22           O\\nANISOU  362  OG1 THR A  85     7080   9977   8864  -1454    215   -567       O\\nATOM    363  CG2 THR A  85      -5.948   6.109  -1.519  1.00 61.69           C\\nANISOU  363  CG2 THR A  85     6117   9358   7964  -2054    299   -604       C\\nATOM    364  N   LEU A  86      -3.186   8.043  -4.718  1.00 62.95           N\\nANISOU  364  N   LEU A  86     6792   8914   8211  -1106   -129   -431       N\\nATOM    365  CA  LEU A  86      -2.875   9.074  -5.699  1.00 69.96           C\\nANISOU  365  CA  LEU A  86     7691   9770   9119   -857   -279   -398       C\\nATOM    366  C   LEU A  86      -1.823   8.663  -6.718  1.00 73.74           C\\nANISOU  366  C   LEU A  86     8430  10102   9484   -805   -327   -290       C\\nATOM    367  O   LEU A  86      -1.627   9.386  -7.700  1.00 78.44           O\\nANISOU  367  O   LEU A  86     9050  10709  10044   -662   -458   -237       O\\nATOM    368  CB  LEU A  86      -2.400  10.356  -5.000  1.00 71.90           C\\nANISOU  368  CB  LEU A  86     7888   9995   9438   -669   -260   -361       C\\nATOM    369  CG  LEU A  86      -3.358  11.015  -4.012  1.00 70.39           C\\nANISOU  369  CG  LEU A  86     7407   9983   9357   -640   -226   -527       C\\nATOM    370  CD1 LEU A  86      -2.805  12.358  -3.572  1.00 66.08           C\\nANISOU  370  CD1 LEU A  86     6851   9355   8902   -408   -280   -511       C\\nATOM    371  CD2 LEU A  86      -4.735  11.169  -4.633  1.00 73.10           C\\nANISOU  371  CD2 LEU A  86     7488  10505   9781   -625   -371   -694       C\\nATOM    372  N   VAL A  87      -1.137   7.538  -6.512  1.00 71.08           N\\nANISOU  372  N   VAL A  87     8285   9640   9081   -916   -240   -262       N\\nATOM    373  CA  VAL A  87      -0.068   7.087  -7.395  1.00 73.29           C\\nANISOU  373  CA  VAL A  87     8777   9820   9251   -840   -268   -222       C\\nATOM    374  C   VAL A  87      -0.364   5.702  -7.963  1.00 77.64           C\\nANISOU  374  C   VAL A  87     9430  10309   9760   -973   -330   -334       C\\nATOM    375  O   VAL A  87      -0.313   5.497  -9.179  1.00 73.98           O\\nANISOU  375  O   VAL A  87     9018   9892   9199   -916   -433   -399       O\\nATOM    376  CB  VAL A  87       1.295   7.094  -6.673  1.00 71.74           C\\nANISOU  376  CB  VAL A  87     8723   9494   9039   -769   -152   -126       C\\nATOM    377  CG1 VAL A  87       2.408   6.688  -7.635  1.00 74.66           C\\nANISOU  377  CG1 VAL A  87     9249   9829   9290   -667   -171   -133       C\\nATOM    378  CG2 VAL A  87       1.561   8.458  -6.054  1.00 66.12           C\\nANISOU  378  CG2 VAL A  87     7914   8818   8388   -656   -114    -33       C\\nATOM    379  N   MET A  88      -0.666   4.743  -7.091  1.00 80.11           N\\nANISOU  379  N   MET A  88     9788  10515  10136  -1166   -284   -354       N\\nATOM    380  CA  MET A  88      -0.910   3.374  -7.543  1.00 77.27           C\\nANISOU  380  CA  MET A  88     9560  10025   9773  -1313   -382   -456       C\\nATOM    381  C   MET A  88      -2.014   3.257  -8.587  1.00 74.77           C\\nANISOU  381  C   MET A  88     9120   9842   9447  -1377   -521   -585       C\\nATOM    382  O   MET A  88      -1.856   2.434  -9.508  1.00 75.54           O\\nANISOU  382  O   MET A  88     9351   9858   9492  -1370   -641   -704       O\\nATOM    383  CB  MET A  88      -1.213   2.478  -6.335  1.00 80.86           C\\nANISOU  383  CB  MET A  88    10082  10339  10303  -1575   -337   -400       C\\nATOM    384  CG  MET A  88      -0.060   2.322  -5.349  1.00 81.25           C\\nANISOU  384  CG  MET A  88    10311  10211  10350  -1521   -256   -278       C\\nATOM    385  SD  MET A  88       1.427   1.569  -6.040  1.00 83.45           S\\nANISOU  385  SD  MET A  88    10860  10245  10603  -1297   -355   -350       S\\nATOM    386  CE  MET A  88       0.780   0.002  -6.622  1.00 86.55           C\\nANISOU  386  CE  MET A  88    11408  10421  11056  -1493   -560   -493       C\\nATOM    387  N   PRO A  89      -3.134   3.998  -8.521  1.00 73.85           N\\nANISOU  387  N   PRO A  89     8745   9932   9382  -1424   -534   -603       N\\nATOM    388  CA  PRO A  89      -4.103   3.930  -9.629  1.00 74.48           C\\nANISOU  388  CA  PRO A  89     8707  10146   9448  -1448   -704   -735       C\\nATOM    389  C   PRO A  89      -3.480   4.213 -10.985  1.00 73.67           C\\nANISOU  389  C   PRO A  89     8725  10074   9192  -1237   -816   -758       C\\nATOM    390  O   PRO A  89      -3.834   3.559 -11.972  1.00 74.04           O\\nANISOU  390  O   PRO A  89     8817  10141   9174  -1277   -962   -893       O\\nATOM    391  CB  PRO A  89      -5.142   4.990  -9.248  1.00 73.14           C\\nANISOU  391  CB  PRO A  89     8221  10200   9368  -1431   -703   -747       C\\nATOM    392  CG  PRO A  89      -5.085   5.041  -7.779  1.00 71.74           C\\nANISOU  392  CG  PRO A  89     7982  10016   9258  -1543   -514   -680       C\\nATOM    393  CD  PRO A  89      -3.645   4.834  -7.418  1.00 67.98           C\\nANISOU  393  CD  PRO A  89     7787   9325   8719  -1455   -417   -550       C\\nATOM    394  N   TRP A  90      -2.552   5.170 -11.056  1.00 69.93           N\\nANISOU  394  N   TRP A  90     8302   9624   8643  -1037   -753   -630       N\\nATOM    395  CA  TRP A  90      -1.831   5.402 -12.301  1.00 70.06           C\\nANISOU  395  CA  TRP A  90     8440   9716   8463   -885   -824   -623       C\\nATOM    396  C   TRP A  90      -0.927   4.229 -12.652  1.00 73.43           C\\nANISOU  396  C   TRP A  90     9074  10033   8794   -879   -795   -740       C\\nATOM    397  O   TRP A  90      -0.713   3.948 -13.836  1.00 80.52           O\\nANISOU  397  O   TRP A  90    10046  11036   9511   -815   -885   -849       O\\nATOM    398  CB  TRP A  90      -0.996   6.677 -12.206  1.00 72.68           C\\nANISOU  398  CB  TRP A  90     8778  10094   8744   -730   -758   -431       C\\nATOM    399  CG  TRP A  90      -1.743   7.924 -11.827  1.00 78.23           C\\nANISOU  399  CG  TRP A  90     9301  10853   9571   -681   -825   -337       C\\nATOM    400  CD1 TRP A  90      -2.061   8.338 -10.567  1.00 78.70           C\\nANISOU  400  CD1 TRP A  90     9229  10858   9814   -696   -738   -319       C\\nATOM    401  CD2 TRP A  90      -2.229   8.939 -12.716  1.00 88.37           C\\nANISOU  401  CD2 TRP A  90    10523  12253  10801   -588  -1022   -264       C\\nATOM    402  NE1 TRP A  90      -2.729   9.539 -10.616  1.00 79.87           N\\nANISOU  402  NE1 TRP A  90     9218  11075  10052   -589   -872   -284       N\\nATOM    403  CE2 TRP A  90      -2.844   9.929 -11.925  1.00 85.91           C\\nANISOU  403  CE2 TRP A  90    10036  11918  10690   -521  -1067   -232       C\\nATOM    404  CE3 TRP A  90      -2.213   9.101 -14.106  1.00 93.09           C\\nANISOU  404  CE3 TRP A  90    11205  12978  11187   -553  -1185   -228       C\\nATOM    405  CZ2 TRP A  90      -3.436  11.064 -12.476  1.00 91.05           C\\nANISOU  405  CZ2 TRP A  90    10603  12614  11379   -398  -1303   -166       C\\nATOM    406  CZ3 TRP A  90      -2.801  10.229 -14.651  1.00 88.71           C\\nANISOU  406  CZ3 TRP A  90    10584  12483  10637   -467  -1412   -117       C\\nATOM    407  CH2 TRP A  90      -3.404  11.195 -13.838  1.00 91.05           C\\nANISOU  407  CH2 TRP A  90    10716  12700  11179   -380  -1486    -87       C\\nATOM    408  N   VAL A  91      -0.382   3.540 -11.646  1.00 69.25           N\\nANISOU  408  N   VAL A  91     8640   9297   8374   -930   -690   -736       N\\nATOM    409  CA  VAL A  91       0.555   2.453 -11.912  1.00 71.26           C\\nANISOU  409  CA  VAL A  91     9090   9406   8578   -872   -701   -873       C\\nATOM    410  C   VAL A  91      -0.181   1.188 -12.341  1.00 81.86           C\\nANISOU  410  C   VAL A  91    10506  10626   9969  -1010   -867  -1076       C\\nATOM    411  O   VAL A  91       0.272   0.468 -13.239  1.00 84.97           O\\nANISOU  411  O   VAL A  91    11020  11005  10261   -913   -961  -1279       O\\nATOM    412  CB  VAL A  91       1.447   2.203 -10.683  1.00 66.23           C\\nANISOU  412  CB  VAL A  91     8549   8562   8051   -856   -583   -782       C\\nATOM    413  CG1 VAL A  91       2.331   0.984 -10.905  1.00 66.75           C\\nANISOU  413  CG1 VAL A  91     8812   8434   8116   -769   -652   -961       C\\nATOM    414  CG2 VAL A  91       2.295   3.427 -10.395  1.00 71.66           C\\nANISOU  414  CG2 VAL A  91     9171   9373   8685   -712   -442   -614       C\\nATOM    415  N   VAL A  92      -1.320   0.890 -11.713  1.00 76.99           N\\nANISOU  415  N   VAL A  92     9808   9938   9507  -1247   -911  -1047       N\\nATOM    416  CA  VAL A  92      -2.100  -0.267 -12.139  1.00 83.11           C\\nANISOU  416  CA  VAL A  92    10641  10591  10346  -1426  -1092  -1225       C\\nATOM    417  C   VAL A  92      -2.714  -0.014 -13.513  1.00 85.39           C\\nANISOU  417  C   VAL A  92    10837  11112  10496  -1365  -1232  -1373       C\\nATOM    418  O   VAL A  92      -2.760  -0.914 -14.362  1.00 87.20           O\\nANISOU  418  O   VAL A  92    11179  11274  10677  -1366  -1396  -1596       O\\nATOM    419  CB  VAL A  92      -3.160  -0.626 -11.077  1.00 86.97           C\\nANISOU  419  CB  VAL A  92    11035  10994  11015  -1752  -1083  -1133       C\\nATOM    420  CG1 VAL A  92      -4.059   0.557 -10.774  1.00 88.40           C\\nANISOU  420  CG1 VAL A  92    10916  11464  11208  -1788   -990  -1030       C\\nATOM    421  CG2 VAL A  92      -3.984  -1.823 -11.526  1.00 90.14           C\\nANISOU  421  CG2 VAL A  92    11495  11253  11500  -1988  -1291  -1301       C\\nATOM    422  N   TYR A  93      -3.173   1.217 -13.762  1.00 86.77           N\\nANISOU  422  N   TYR A  93    10817  11548  10602  -1298  -1201  -1261       N\\nATOM    423  CA  TYR A  93      -3.600   1.598 -15.106  1.00 83.84           C\\nANISOU  423  CA  TYR A  93    10389  11409  10056  -1209  -1354  -1357       C\\nATOM    424  C   TYR A  93      -2.477   1.379 -16.111  1.00 80.40           C\\nANISOU  424  C   TYR A  93    10133  11042   9375  -1017  -1359  -1466       C\\nATOM    425  O   TYR A  93      -2.706   0.878 -17.219  1.00 74.40           O\\nANISOU  425  O   TYR A  93     9423  10381   8465   -997  -1517  -1669       O\\nATOM    426  CB  TYR A  93      -4.062   3.059 -15.102  1.00 86.78           C\\nANISOU  426  CB  TYR A  93    10567  11993  10412  -1130  -1345  -1178       C\\nATOM    427  CG  TYR A  93      -4.289   3.683 -16.465  1.00 96.56           C\\nANISOU  427  CG  TYR A  93    11788  13469  11430  -1012  -1516  -1193       C\\nATOM    428  CD1 TYR A  93      -5.528   3.603 -17.096  1.00 94.66           C\\nANISOU  428  CD1 TYR A  93    11412  13349  11207  -1088  -1737  -1310       C\\nATOM    429  CD2 TYR A  93      -3.274   4.383 -17.106  1.00 98.40           C\\nANISOU  429  CD2 TYR A  93    12135  13829  11423   -849  -1468  -1073       C\\nATOM    430  CE1 TYR A  93      -5.739   4.185 -18.334  1.00 95.59           C\\nANISOU  430  CE1 TYR A  93    11537  13682  11100   -983  -1926  -1302       C\\nATOM    431  CE2 TYR A  93      -3.475   4.965 -18.343  1.00 97.04           C\\nANISOU  431  CE2 TYR A  93    11974  13889  11007   -780  -1636  -1042       C\\nATOM    432  CZ  TYR A  93      -4.707   4.864 -18.952  1.00 96.39           C\\nANISOU  432  CZ  TYR A  93    11785  13900  10937   -837  -1876  -1153       C\\nATOM    433  OH  TYR A  93      -4.903   5.446 -20.182  1.00 95.53           O\\nANISOU  433  OH  TYR A  93    11712  14022  10562   -771  -2074  -1102       O\\nATOM    434  N   LEU A  94      -1.250   1.724 -15.722  1.00 88.56           N\\nANISOU  434  N   LEU A  94    11244  12051  10355   -879  -1185  -1358       N\\nATOM    435  CA  LEU A  94      -0.090   1.590 -16.592  1.00 90.25           C\\nANISOU  435  CA  LEU A  94    11571  12398  10320   -698  -1144  -1470       C\\nATOM    436  C   LEU A  94       0.187   0.143 -16.984  1.00 86.74           C\\nANISOU  436  C   LEU A  94    11276  11802   9879   -668  -1251  -1798       C\\nATOM    437  O   LEU A  94       0.806  -0.096 -18.027  1.00 79.60           O\\nANISOU  437  O   LEU A  94    10426  11091   8726   -524  -1274  -1999       O\\nATOM    438  CB  LEU A  94       1.131   2.192 -15.893  1.00 91.19           C\\nANISOU  438  CB  LEU A  94    11704  12504  10440   -587   -935  -1297       C\\nATOM    439  CG  LEU A  94       2.362   2.481 -16.745  1.00 96.59           C\\nANISOU  439  CG  LEU A  94    12420  13445  10836   -422   -839  -1342       C\\nATOM    440  CD1 LEU A  94       1.952   3.241 -17.987  1.00 95.48           C\\nANISOU  440  CD1 LEU A  94    12233  13639  10407   -435   -921  -1281       C\\nATOM    441  CD2 LEU A  94       3.366   3.277 -15.931  1.00 94.01           C\\nANISOU  441  CD2 LEU A  94    12057  13105  10556   -364   -648  -1120       C\\nATOM    442  N   GLU A  95      -0.244  -0.827 -16.175  1.00 91.64           N\\nANISOU  442  N   GLU A  95    11967  12086  10767   -809  -1328  -1863       N\\nATOM    443  CA  GLU A  95      -0.007  -2.228 -16.505  1.00 89.73           C\\nANISOU  443  CA  GLU A  95    11897  11617  10578   -779  -1491  -2179       C\\nATOM    444  C   GLU A  95      -1.104  -2.803 -17.392  1.00 87.68           C\\nANISOU  444  C   GLU A  95    11631  11388  10293   -904  -1724  -2391       C\\nATOM    445  O   GLU A  95      -0.812  -3.568 -18.317  1.00 89.77           O\\nANISOU  445  O   GLU A  95    12002  11667  10441   -784  -1865  -2717       O\\nATOM    446  CB  GLU A  95       0.121  -3.065 -15.229  1.00 87.59           C\\nANISOU  446  CB  GLU A  95    11758  10917  10607   -899  -1515  -2120       C\\nATOM    447  CG  GLU A  95       0.439  -4.539 -15.480  1.00 93.67           C\\nANISOU  447  CG  GLU A  95    12747  11357  11487   -851  -1741  -2438       C\\nATOM    448  CD  GLU A  95       1.851  -4.758 -16.002  1.00102.62           C\\nANISOU  448  CD  GLU A  95    13952  12557  12482   -504  -1707  -2681       C\\nATOM    449  OE1 GLU A  95       2.722  -3.902 -15.740  1.00104.20           O\\nANISOU  449  OE1 GLU A  95    14062  12957  12571   -357  -1484  -2527       O\\nATOM    450  OE2 GLU A  95       2.093  -5.788 -16.670  1.00107.64           O\\nANISOU  450  OE2 GLU A  95    14717  13056  13125   -376  -1910  -3051       O\\nATOM    451  N   VAL A  96      -2.362  -2.449 -17.129  1.00 78.94           N\\nANISOU  451  N   VAL A  96    10382  10316   9297  -1131  -1774  -2245       N\\nATOM    452  CA  VAL A  96      -3.462  -2.952 -17.947  1.00 80.52           C\\nANISOU  452  CA  VAL A  96    10543  10563   9488  -1267  -2011  -2444       C\\nATOM    453  C   VAL A  96      -3.331  -2.439 -19.375  1.00 85.05           C\\nANISOU  453  C   VAL A  96    11087  11511   9717  -1081  -2072  -2578       C\\nATOM    454  O   VAL A  96      -3.404  -3.209 -20.340  1.00 82.90           O\\nANISOU  454  O   VAL A  96    10906  11266   9327  -1037  -2258  -2893       O\\nATOM    455  CB  VAL A  96      -4.816  -2.561 -17.328  1.00 77.18           C\\nANISOU  455  CB  VAL A  96     9907  10166   9251  -1538  -2032  -2265       C\\nATOM    456  N   VAL A  97      -3.117  -1.130 -19.528  1.00 87.40           N\\nANISOU  456  N   VAL A  97    11271  12099   9836   -979  -1932  -2336       N\\nATOM    457  CA  VAL A  97      -2.995  -0.529 -20.854  1.00 88.86           C\\nANISOU  457  CA  VAL A  97    11446  12664   9653   -847  -1994  -2384       C\\nATOM    458  C   VAL A  97      -1.719  -0.983 -21.554  1.00 90.16           C\\nANISOU  458  C   VAL A  97    11752  12956   9548   -647  -1919  -2608       C\\nATOM    459  O   VAL A  97      -1.694  -1.122 -22.783  1.00 92.93           O\\nANISOU  459  O   VAL A  97    12140  13588   9583   -572  -2028  -2817       O\\nATOM    460  CB  VAL A  97      -3.061   1.005 -20.740  1.00 86.80           C\\nANISOU  460  CB  VAL A  97    11060  12617   9305   -817  -1897  -2025       C\\nATOM    461  CG1 VAL A  97      -2.893   1.659 -22.106  1.00 88.76           C\\nANISOU  461  CG1 VAL A  97    11335  13252   9139   -721  -1981  -2009       C\\nATOM    462  CG2 VAL A  97      -4.372   1.434 -20.086  1.00 86.16           C\\nANISOU  462  CG2 VAL A  97    10792  12448   9495   -970  -1990  -1884       C\\nATOM    463  N   GLY A  98      -0.650  -1.230 -20.800  1.00 88.15           N\\nANISOU  463  N   GLY A  98    11562  12531   9400   -550  -1740  -2596       N\\nATOM    464  CA  GLY A  98       0.613  -1.604 -21.402  1.00 89.34           C\\nANISOU  464  CA  GLY A  98    11789  12846   9310   -334  -1652  -2837       C\\nATOM    465  C   GLY A  98       1.360  -0.469 -22.059  1.00 91.48           C\\nANISOU  465  C   GLY A  98    11987  13570   9202   -247  -1473  -2660       C\\nATOM    466  O   GLY A  98       2.307  -0.717 -22.810  1.00 93.59           O\\nANISOU  466  O   GLY A  98    12270  14114   9177    -92  -1395  -2892       O\\nATOM    467  N   GLU A  99       0.962   0.772 -21.797  1.00 93.52           N\\nANISOU  467  N   GLU A  99    12159  13918   9455   -352  -1418  -2264       N\\nATOM    468  CA  GLU A  99       1.609   1.938 -22.378  1.00 95.54           C\\nANISOU  468  CA  GLU A  99    12373  14557   9372   -328  -1286  -2022       C\\nATOM    469  C   GLU A  99       1.259   3.151 -21.529  1.00 92.97           C\\nANISOU  469  C   GLU A  99    11976  14105   9244   -422  -1241  -1593       C\\nATOM    470  O   GLU A  99       0.253   3.163 -20.815  1.00 85.82           O\\nANISOU  470  O   GLU A  99    11021  12937   8648   -506  -1345  -1519       O\\nATOM    471  CB  GLU A  99       1.181   2.153 -23.835  1.00 94.86           C\\nANISOU  471  CB  GLU A  99    12308  14866   8868   -355  -1437  -2092       C\\nATOM    472  N   TRP A 100       2.110   4.174 -21.614  1.00 89.68           N\\nANISOU  472  N   TRP A 100    11539  13894   8642   -414  -1089  -1330       N\\nATOM    473  CA  TRP A 100       1.871   5.446 -20.932  1.00 88.27           C\\nANISOU  473  CA  TRP A 100    11308  13606   8625   -483  -1080   -935       C\\nATOM    474  C   TRP A 100       0.892   6.302 -21.742  1.00 91.37           C\\nANISOU  474  C   TRP A 100    11702  14149   8867   -556  -1315   -744       C\\nATOM    475  O   TRP A 100       1.217   7.382 -22.236  1.00 95.09           O\\nANISOU  475  O   TRP A 100    12204  14809   9115   -605  -1334   -453       O\\nATOM    476  CB  TRP A 100       3.188   6.177 -20.702  1.00 86.77           C\\nANISOU  476  CB  TRP A 100    11107  13540   8322   -471   -861   -729       C\\nATOM    477  CG  TRP A 100       4.148   5.471 -19.784  1.00 92.86           C\\nANISOU  477  CG  TRP A 100    11859  14140   9283   -376   -663   -888       C\\nATOM    478  CD1 TRP A 100       4.731   4.252 -19.983  1.00 99.53           C\\nANISOU  478  CD1 TRP A 100    12726  15011  10078   -261   -605  -1253       C\\nATOM    479  CD2 TRP A 100       4.655   5.958 -18.534  1.00 93.04           C\\nANISOU  479  CD2 TRP A 100    11841  13932   9577   -369   -533   -700       C\\nATOM    480  NE1 TRP A 100       5.558   3.944 -18.928  1.00 99.78           N\\nANISOU  480  NE1 TRP A 100    12740  14828  10345   -179   -465  -1286       N\\nATOM    481  CE2 TRP A 100       5.530   4.975 -18.027  1.00 94.10           C\\nANISOU  481  CE2 TRP A 100    11981  13965   9809   -254   -408   -944       C\\nATOM    482  CE3 TRP A 100       4.449   7.125 -17.792  1.00 92.42           C\\nANISOU  482  CE3 TRP A 100    11726  13714   9675   -431   -538   -373       C\\nATOM    483  CZ2 TRP A 100       6.198   5.125 -16.811  1.00 92.35           C\\nANISOU  483  CZ2 TRP A 100    11733  13525   9830   -217   -285   -845       C\\nATOM    484  CZ3 TRP A 100       5.114   7.273 -16.583  1.00 87.83           C\\nANISOU  484  CZ3 TRP A 100    11114  12928   9330   -397   -398   -300       C\\nATOM    485  CH2 TRP A 100       5.977   6.279 -16.107  1.00 90.94           C\\nANISOU  485  CH2 TRP A 100    11517  13244   9792   -299   -271   -522       C\\nATOM    486  N   LYS A 101      -0.329   5.791 -21.877  1.00 95.15           N\\nANISOU  486  N   LYS A 101    12148  14527   9477   -577  -1521   -906       N\\nATOM    487  CA  LYS A 101      -1.365   6.446 -22.678  1.00 96.45           C\\nANISOU  487  CA  LYS A 101    12300  14824   9522   -619  -1798   -787       C\\nATOM    488  C   LYS A 101      -2.121   7.498 -21.869  1.00 98.53           C\\nANISOU  488  C   LYS A 101    12457  14876  10104   -621  -1907   -529       C\\nATOM    489  O   LYS A 101      -3.351   7.502 -21.813  1.00100.15           O\\nANISOU  489  O   LYS A 101    12553  15004  10495   -628  -2120   -595       O\\nATOM    490  CB  LYS A 101      -2.319   5.405 -23.251  1.00 91.01           C\\nANISOU  490  CB  LYS A 101    11597  14158   8826   -638  -1991  -1116       C\\nATOM    491  N   PHE A 102      -1.377   8.397 -21.223  1.00 92.76           N\\nANISOU  491  N   PHE A 102    11736  14060   9449   -605  -1768   -264       N\\nATOM    492  CA  PHE A 102      -1.943   9.593 -20.620  1.00 93.22           C\\nANISOU  492  CA  PHE A 102    11716  13947   9756   -575  -1904    -18       C\\nATOM    493  C   PHE A 102      -1.857  10.735 -21.628  1.00 91.71           C\\nANISOU  493  C   PHE A 102    11641  13918   9287   -599  -2119    289       C\\nATOM    494  O   PHE A 102      -1.422  10.558 -22.768  1.00103.07           O\\nANISOU  494  O   PHE A 102    13204  15642  10313   -665  -2138    313       O\\nATOM    495  CB  PHE A 102      -1.202   9.983 -19.340  1.00 94.22           C\\nANISOU  495  CB  PHE A 102    11808  13862  10129   -551  -1677     95       C\\nATOM    496  CG  PHE A 102      -0.815   8.827 -18.469  1.00 91.97           C\\nANISOU  496  CG  PHE A 102    11490  13455  10000   -556  -1432   -141       C\\nATOM    497  CD1 PHE A 102      -1.737   8.243 -17.618  1.00 88.34           C\\nANISOU  497  CD1 PHE A 102    10903  12822   9841   -574  -1444   -314       C\\nATOM    498  CD2 PHE A 102       0.483   8.344 -18.477  1.00 88.17           C\\nANISOU  498  CD2 PHE A 102    11097  13037   9364   -553  -1204   -181       C\\nATOM    499  CE1 PHE A 102      -1.375   7.184 -16.805  1.00 84.23           C\\nANISOU  499  CE1 PHE A 102    10394  12156   9452   -611  -1257   -481       C\\nATOM    500  CE2 PHE A 102       0.849   7.286 -17.667  1.00 83.36           C\\nANISOU  500  CE2 PHE A 102    10485  12270   8917   -538  -1037   -386       C\\nATOM    501  CZ  PHE A 102      -0.082   6.706 -16.830  1.00 81.83           C\\nANISOU  501  CZ  PHE A 102    10213  11865   9014   -578  -1075   -513       C\\nATOM    502  N   SER A 103      -2.265  11.924 -21.210  1.00 88.70           N\\nANISOU  502  N   SER A 103    11226  13356   9120   -550  -2299    526       N\\nATOM    503  CA  SER A 103      -1.855  13.135 -21.896  1.00 82.43           C\\nANISOU  503  CA  SER A 103    10589  12620   8110   -603  -2476    904       C\\nATOM    504  C   SER A 103      -0.586  13.661 -21.237  1.00 83.13           C\\nANISOU  504  C   SER A 103    10732  12623   8230   -660  -2230   1106       C\\nATOM    505  O   SER A 103      -0.135  13.148 -20.210  1.00 83.31           O\\nANISOU  505  O   SER A 103    10661  12526   8466   -622  -1957    945       O\\nATOM    506  CB  SER A 103      -2.969  14.182 -21.869  1.00 79.20           C\\nANISOU  506  CB  SER A 103    10137  12018   7939   -498  -2879   1043       C\\nATOM    507  OG  SER A 103      -3.335  14.521 -20.542  1.00 76.16           O\\nANISOU  507  OG  SER A 103     9579  11344   8016   -372  -2840    955       O\\nATOM    508  N   ARG A 104       0.009  14.689 -21.845  1.00 84.27           N\\nANISOU  508  N   ARG A 104    11037  12833   8148   -776  -2344   1478       N\\nATOM    509  CA  ARG A 104       1.252  15.212 -21.290  1.00 80.60           C\\nANISOU  509  CA  ARG A 104    10612  12312   7701   -868  -2123   1679       C\\nATOM    510  C   ARG A 104       1.025  15.830 -19.921  1.00 77.44           C\\nANISOU  510  C   ARG A 104    10113  11518   7794   -740  -2150   1682       C\\nATOM    511  O   ARG A 104       1.913  15.783 -19.064  1.00 78.86           O\\nANISOU  511  O   ARG A 104    10250  11620   8096   -755  -1890   1666       O\\nATOM    512  CB  ARG A 104       1.881  16.231 -22.235  1.00 80.66           C\\nANISOU  512  CB  ARG A 104    10815  12469   7362  -1078  -2266   2114       C\\nATOM    513  CG  ARG A 104       3.382  16.383 -22.031  1.00 90.20           C\\nANISOU  513  CG  ARG A 104    12038  13815   8417  -1248  -1948   2260       C\\nATOM    514  CD  ARG A 104       3.766  17.736 -21.446  1.00101.17           C\\nANISOU  514  CD  ARG A 104    13504  14894  10041  -1329  -2089   2624       C\\nATOM    515  NE  ARG A 104       3.451  18.831 -22.359  1.00106.68           N\\nANISOU  515  NE  ARG A 104    14414  15562  10556  -1484  -2476   3046       N\\nATOM    516  CZ  ARG A 104       2.650  19.849 -22.059  1.00108.76           C\\nANISOU  516  CZ  ARG A 104    14758  15416  11150  -1381  -2885   3220       C\\nATOM    517  NH1 ARG A 104       2.092  19.927 -20.857  1.00104.63           N\\nANISOU  517  NH1 ARG A 104    14088  14533  11136  -1126  -2918   2984       N\\nATOM    518  NH2 ARG A 104       2.417  20.795 -22.961  1.00112.28           N\\nANISOU  518  NH2 ARG A 104    15433  15822  11408  -1532  -3275   3626       N\\nATOM    519  N   ILE A 105      -0.160  16.392 -19.688  1.00 79.98           N\\nANISOU  519  N   ILE A 105    10379  11613   8397   -597  -2469   1666       N\\nATOM    520  CA  ILE A 105      -0.435  17.000 -18.394  1.00 78.38           C\\nANISOU  520  CA  ILE A 105    10057  11079   8646   -452  -2502   1613       C\\nATOM    521  C   ILE A 105      -0.797  15.939 -17.359  1.00 74.85           C\\nANISOU  521  C   ILE A 105     9401  10617   8423   -355  -2239   1232       C\\nATOM    522  O   ILE A 105      -0.422  16.063 -16.189  1.00 73.96           O\\nANISOU  522  O   ILE A 105     9211  10343   8549   -307  -2066   1171       O\\nATOM    523  CB  ILE A 105      -1.528  18.076 -18.534  1.00 77.26           C\\nANISOU  523  CB  ILE A 105     9910  10715   8730   -308  -2966   1710       C\\nATOM    524  CG1 ILE A 105      -1.691  18.858 -17.227  1.00 76.93           C\\nANISOU  524  CG1 ILE A 105     9750  10345   9133   -142  -3017   1643       C\\nATOM    525  CG2 ILE A 105      -2.847  17.465 -18.989  1.00 71.80           C\\nANISOU  525  CG2 ILE A 105     9083  10142   8055   -199  -3143   1458       C\\nATOM    526  CD1 ILE A 105      -0.522  19.761 -16.903  1.00 63.79           C\\nANISOU  526  CD1 ILE A 105     8244   8504   7489   -248  -2982   1938       C\\nATOM    527  N   HIS A 106      -1.425  14.862 -17.789  1.00 78.10           N\\nANISOU  527  N   HIS A 106     9732  11194   8747   -350  -2214    984       N\\nATOM    528  CA  HIS A 106      -1.751  13.780 -16.889  1.00 72.04           C\\nANISOU  528  CA  HIS A 106     8805  10412   8157   -326  -1967    668       C\\nATOM    529  C   HIS A 106      -0.480  13.081 -16.470  1.00 75.28           C\\nANISOU  529  C   HIS A 106     9289  10863   8451   -409  -1617    644       C\\nATOM    530  O   HIS A 106      -0.345  12.663 -15.351  1.00 70.37           O\\nANISOU  530  O   HIS A 106     8580  10125   8032   -389  -1418    503       O\\nATOM    531  CB  HIS A 106      -2.690  12.806 -17.558  1.00 69.03           C\\nANISOU  531  CB  HIS A 106     8344  10182   7701   -344  -2050    426       C\\nATOM    532  CG  HIS A 106      -4.109  13.257 -17.558  1.00 86.66           C\\nANISOU  532  CG  HIS A 106    10420  12382  10122   -239  -2375    359       C\\nATOM    533  ND1 HIS A 106      -4.497  14.469 -17.043  1.00 93.53           N\\nANISOU  533  ND1 HIS A 106    11265  13098  11175   -109  -2634    518       N\\nATOM    534  CD2 HIS A 106      -5.234  12.662 -18.003  1.00 92.54           C\\nANISOU  534  CD2 HIS A 106    11011  13228  10921   -235  -2507    125       C\\nATOM    535  CE1 HIS A 106      -5.801  14.602 -17.170  1.00 95.16           C\\nANISOU  535  CE1 HIS A 106    11292  13325  11539     -1  -2912    369       C\\nATOM    536  NE2 HIS A 106      -6.273  13.520 -17.751  1.00 94.46           N\\nANISOU  536  NE2 HIS A 106    11111  13409  11371    -89  -2829    134       N\\nATOM    537  N   CYS A 107       0.459  12.953 -17.384  1.00 74.40           N\\nANISOU  537  N   CYS A 107     9326  10942   8001   -501  -1547    768       N\\nATOM    538  CA  CYS A 107       1.750  12.355 -17.073  1.00 74.41           C\\nANISOU  538  CA  CYS A 107     9366  11008   7898   -548  -1239    725       C\\nATOM    539  C   CYS A 107       2.520  13.220 -16.082  1.00 69.26           C\\nANISOU  539  C   CYS A 107     8705  10174   7436   -541  -1146    902       C\\nATOM    540  O   CYS A 107       3.036  12.718 -15.076  1.00 62.15           O\\nANISOU  540  O   CYS A 107     7754   9173   6688   -508   -936    780       O\\nATOM    541  CB  CYS A 107       2.542  12.149 -18.368  1.00 77.98           C\\nANISOU  541  CB  CYS A 107     9930  11782   7918   -646  -1190    790       C\\nATOM    542  SG  CYS A 107       4.200  11.445 -18.193  1.00 79.49           S\\nANISOU  542  SG  CYS A 107    10119  12137   7945   -673   -832    689       S\\nATOM    543  N   ASP A 108       2.590  14.530 -16.341  1.00 68.64           N\\nANISOU  543  N   ASP A 108     8692  10029   7359   -576  -1335   1195       N\\nATOM    544  CA  ASP A 108       3.289  15.433 -15.430  1.00 67.61           C\\nANISOU  544  CA  ASP A 108     8561   9699   7427   -578  -1293   1358       C\\nATOM    545  C   ASP A 108       2.673  15.405 -14.037  1.00 65.65           C\\nANISOU  545  C   ASP A 108     8180   9208   7557   -435  -1270   1167       C\\nATOM    546  O   ASP A 108       3.393  15.362 -13.033  1.00 66.27           O\\nANISOU  546  O   ASP A 108     8226   9190   7765   -423  -1086   1133       O\\nATOM    547  CB  ASP A 108       3.280  16.856 -15.990  1.00 70.02           C\\nANISOU  547  CB  ASP A 108     8985   9912   7707   -648  -1582   1705       C\\nATOM    548  CG  ASP A 108       4.274  17.047 -17.124  1.00 81.41           C\\nANISOU  548  CG  ASP A 108    10562  11623   8747   -867  -1532   1967       C\\nATOM    549  OD1 ASP A 108       5.293  16.329 -17.150  1.00 84.41           O\\nANISOU  549  OD1 ASP A 108    10904  12225   8943   -940  -1226   1879       O\\nATOM    550  OD2 ASP A 108       4.043  17.922 -17.986  1.00 86.93           O\\nANISOU  550  OD2 ASP A 108    11397  12326   9305   -971  -1808   2260       O\\nATOM    551  N   ILE A 109       1.341  15.424 -13.956  1.00 63.48           N\\nANISOU  551  N   ILE A 109     7808   8870   7442   -332  -1455   1030       N\\nATOM    552  CA  ILE A 109       0.665  15.365 -12.662  1.00 61.96           C\\nANISOU  552  CA  ILE A 109     7449   8532   7562   -218  -1412    821       C\\nATOM    553  C   ILE A 109       1.015  14.072 -11.937  1.00 63.72           C\\nANISOU  553  C   ILE A 109     7629   8811   7771   -268  -1106    623       C\\nATOM    554  O   ILE A 109       1.341  14.076 -10.743  1.00 59.23           O\\nANISOU  554  O   ILE A 109     7010   8137   7359   -241   -960    564       O\\nATOM    555  CB  ILE A 109      -0.856  15.511 -12.845  1.00 58.03           C\\nANISOU  555  CB  ILE A 109     6805   8039   7204   -115  -1656    674       C\\nATOM    556  CG1 ILE A 109      -1.212  16.937 -13.262  1.00 58.42           C\\nANISOU  556  CG1 ILE A 109     6896   7940   7362    -12  -2018    855       C\\nATOM    557  CG2 ILE A 109      -1.588  15.133 -11.573  1.00 56.04           C\\nANISOU  557  CG2 ILE A 109     6336   7761   7197    -50  -1535    405       C\\nATOM    558  CD1 ILE A 109      -2.681  17.131 -13.524  1.00 59.89           C\\nANISOU  558  CD1 ILE A 109     6917   8142   7695    126  -2302    693       C\\nATOM    559  N   PHE A 110       0.949  12.945 -12.648  1.00 61.78           N\\nANISOU  559  N   PHE A 110     7422   8717   7335   -338  -1034    516       N\\nATOM    560  CA  PHE A 110       1.250  11.658 -12.031  1.00 58.79           C\\nANISOU  560  CA  PHE A 110     7039   8336   6961   -385   -808    335       C\\nATOM    561  C   PHE A 110       2.679  11.622 -11.510  1.00 63.91           C\\nANISOU  561  C   PHE A 110     7771   8939   7574   -390   -613    414       C\\nATOM    562  O   PHE A 110       2.921  11.236 -10.361  1.00 59.44           O\\nANISOU  562  O   PHE A 110     7180   8260   7146   -384   -476    340       O\\nATOM    563  CB  PHE A 110       0.997  10.530 -13.034  1.00 61.38           C\\nANISOU  563  CB  PHE A 110     7419   8803   7098   -442   -823    194       C\\nATOM    564  CG  PHE A 110       1.692   9.234 -12.700  1.00 68.94           C\\nANISOU  564  CG  PHE A 110     8447   9728   8016   -477   -636     42       C\\nATOM    565  CD1 PHE A 110       1.579   8.662 -11.444  1.00 75.18           C\\nANISOU  565  CD1 PHE A 110     9204  10361   8999   -508   -525    -42       C\\nATOM    566  CD2 PHE A 110       2.437   8.573 -13.660  1.00 71.59           C\\nANISOU  566  CD2 PHE A 110     8887  10201   8115   -474   -595    -28       C\\nATOM    567  CE1 PHE A 110       2.216   7.472 -11.150  1.00 77.40           C\\nANISOU  567  CE1 PHE A 110     9585  10560   9264   -531   -416   -161       C\\nATOM    568  CE2 PHE A 110       3.070   7.383 -13.372  1.00 74.90           C\\nANISOU  568  CE2 PHE A 110     9372  10553   8534   -462   -477   -203       C\\nATOM    569  CZ  PHE A 110       2.960   6.833 -12.116  1.00 77.70           C\\nANISOU  569  CZ  PHE A 110     9724  10690   9110   -489   -407   -255       C\\nATOM    570  N   VAL A 111       3.641  12.034 -12.340  1.00 65.60           N\\nANISOU  570  N   VAL A 111     8072   9264   7587   -416   -603    568       N\\nATOM    571  CA  VAL A 111       5.043  11.987 -11.930  1.00 66.54           C\\nANISOU  571  CA  VAL A 111     8228   9388   7667   -424   -420    620       C\\nATOM    572  C   VAL A 111       5.288  12.924 -10.757  1.00 60.65           C\\nANISOU  572  C   VAL A 111     7442   8452   7150   -393   -417    727       C\\nATOM    573  O   VAL A 111       6.026  12.590  -9.822  1.00 56.21           O\\nANISOU  573  O   VAL A 111     6872   7814   6670   -370   -270    674       O\\nATOM    574  CB  VAL A 111       5.960  12.317 -13.119  1.00 69.81           C\\nANISOU  574  CB  VAL A 111     8700  10035   7791   -499   -401    765       C\\nATOM    575  CG1 VAL A 111       7.405  12.336 -12.671  1.00 60.98           C\\nANISOU  575  CG1 VAL A 111     7563   8955   6651   -512   -214    801       C\\nATOM    576  CG2 VAL A 111       5.758  11.308 -14.235  1.00 72.95           C\\nANISOU  576  CG2 VAL A 111     9130  10652   7937   -508   -394    597       C\\nATOM    577  N   THR A 112       4.669  14.106 -10.784  1.00 59.23           N\\nANISOU  577  N   THR A 112     7242   8180   7083   -374   -610    861       N\\nATOM    578  CA  THR A 112       4.789  15.036  -9.664  1.00 65.31           C\\nANISOU  578  CA  THR A 112     7970   8754   8090   -319   -646    910       C\\nATOM    579  C   THR A 112       4.286  14.407  -8.371  1.00 66.52           C\\nANISOU  579  C   THR A 112     8031   8833   8410   -256   -532    693       C\\nATOM    580  O   THR A 112       4.970  14.440  -7.343  1.00 76.31           O\\nANISOU  580  O   THR A 112     9268   9991   9734   -241   -417    676       O\\nATOM    581  CB  THR A 112       4.019  16.321  -9.963  1.00 64.71           C\\nANISOU  581  CB  THR A 112     7889   8561   8139   -269   -933   1031       C\\nATOM    582  OG1 THR A 112       4.645  17.010 -11.052  1.00 63.73           O\\nANISOU  582  OG1 THR A 112     7888   8484   7843   -379  -1048   1304       O\\nATOM    583  CG2 THR A 112       3.995  17.223  -8.744  1.00 62.38           C\\nANISOU  583  CG2 THR A 112     7534   8052   8116   -171   -994    998       C\\nATOM    584  N   LEU A 113       3.086  13.825  -8.407  1.00 61.29           N\\nANISOU  584  N   LEU A 113     7289   8219   7778   -245   -569    534       N\\nATOM    585  CA  LEU A 113       2.533  13.195  -7.214  1.00 68.29           C\\nANISOU  585  CA  LEU A 113     8081   9085   8780   -248   -453    353       C\\nATOM    586  C   LEU A 113       3.348  11.975  -6.799  1.00 67.53           C\\nANISOU  586  C   LEU A 113     8081   8983   8595   -321   -257    312       C\\nATOM    587  O   LEU A 113       3.573  11.752  -5.604  1.00 68.67           O\\nANISOU  587  O   LEU A 113     8216   9064   8811   -332   -149    267       O\\nATOM    588  CB  LEU A 113       1.075  12.808  -7.454  1.00 70.65           C\\nANISOU  588  CB  LEU A 113     8249   9477   9119   -266   -536    201       C\\nATOM    589  CG  LEU A 113       0.073  13.960  -7.517  1.00 65.91           C\\nANISOU  589  CG  LEU A 113     7497   8872   8673   -146   -751    162       C\\nATOM    590  CD1 LEU A 113      -1.287  13.451  -7.958  1.00 61.41           C\\nANISOU  590  CD1 LEU A 113     6776   8439   8118   -174   -840      2       C\\nATOM    591  CD2 LEU A 113      -0.016  14.648  -6.165  1.00 61.76           C\\nANISOU  591  CD2 LEU A 113     6853   8287   8324    -59   -710     69       C\\nATOM    592  N   ASP A 114       3.794  11.174  -7.768  1.00 63.91           N\\nANISOU  592  N   ASP A 114     7718   8590   7975   -359   -233    311       N\\nATOM    593  CA  ASP A 114       4.598   9.999  -7.445  1.00 66.05           C\\nANISOU  593  CA  ASP A 114     8086   8820   8191   -384   -102    240       C\\nATOM    594  C   ASP A 114       5.885  10.392  -6.734  1.00 66.08           C\\nANISOU  594  C   ASP A 114     8124   8760   8225   -333    -12    324       C\\nATOM    595  O   ASP A 114       6.262   9.778  -5.730  1.00 69.96           O\\nANISOU  595  O   ASP A 114     8658   9151   8773   -337     64    278       O\\nATOM    596  CB  ASP A 114       4.901   9.208  -8.720  1.00 75.01           C\\nANISOU  596  CB  ASP A 114     9296  10059   9148   -388   -118    174       C\\nATOM    597  CG  ASP A 114       5.951   8.133  -8.509  1.00 75.49           C\\nANISOU  597  CG  ASP A 114     9451  10063   9168   -352    -25     76       C\\nATOM    598  OD1 ASP A 114       5.746   7.255  -7.648  1.00 74.37           O\\nANISOU  598  OD1 ASP A 114     9364   9766   9125   -388     -9     -2       O\\nATOM    599  OD2 ASP A 114       6.981   8.161  -9.214  1.00 76.15           O\\nANISOU  599  OD2 ASP A 114     9549  10268   9116   -291     20     74       O\\nATOM    600  N   VAL A 115       6.568  11.421  -7.235  1.00 71.45           N\\nANISOU  600  N   VAL A 115     8790   9494   8864   -306    -41    464       N\\nATOM    601  CA  VAL A 115       7.809  11.865  -6.610  1.00 70.24           C\\nANISOU  601  CA  VAL A 115     8641   9297   8749   -279     30    542       C\\nATOM    602  C   VAL A 115       7.535  12.461  -5.234  1.00 69.24           C\\nANISOU  602  C   VAL A 115     8477   9030   8802   -253     19    542       C\\nATOM    603  O   VAL A 115       8.282  12.220  -4.279  1.00 70.91           O\\nANISOU  603  O   VAL A 115     8710   9175   9059   -230     93    521       O\\nATOM    604  CB  VAL A 115       8.536  12.862  -7.531  1.00 65.07           C\\nANISOU  604  CB  VAL A 115     7975   8750   7999   -319     -9    719       C\\nATOM    605  CG1 VAL A 115       9.683  13.529  -6.804  1.00 60.52           C\\nANISOU  605  CG1 VAL A 115     7374   8118   7505   -321     36    809       C\\nATOM    606  CG2 VAL A 115       9.043  12.156  -8.778  1.00 62.56           C\\nANISOU  606  CG2 VAL A 115     7676   8649   7446   -346     53    680       C\\nATOM    607  N   MET A 116       6.454  13.232  -5.103  1.00 72.12           N\\nANISOU  607  N   MET A 116     8773   9364   9266   -239    -88    539       N\\nATOM    608  CA  MET A 116       6.164  13.889  -3.832  1.00 68.31           C\\nANISOU  608  CA  MET A 116     8226   8792   8936   -191   -103    487       C\\nATOM    609  C   MET A 116       5.814  12.877  -2.746  1.00 67.37           C\\nANISOU  609  C   MET A 116     8106   8685   8808   -232     19    357       C\\nATOM    610  O   MET A 116       6.435  12.860  -1.677  1.00 67.14           O\\nANISOU  610  O   MET A 116     8105   8604   8802   -221     83    349       O\\nATOM    611  CB  MET A 116       5.031  14.896  -4.005  1.00 66.63           C\\nANISOU  611  CB  MET A 116     7912   8564   8843   -129   -269    455       C\\nATOM    612  CG  MET A 116       4.669  15.602  -2.718  1.00 65.54           C\\nANISOU  612  CG  MET A 116     7676   8370   8856    -46   -291    332       C\\nATOM    613  SD  MET A 116       3.209  16.636  -2.880  1.00 73.08           S\\nANISOU  613  SD  MET A 116     8464   9323   9980     85   -509    199       S\\nATOM    614  CE  MET A 116       3.000  17.178  -1.184  1.00 75.15           C\\nANISOU  614  CE  MET A 116     8597   9592  10365    186   -462    -23       C\\nATOM    615  N   MET A 117       4.820  12.023  -3.000  1.00 57.68           N\\nANISOU  615  N   MET A 117     6854   7527   7535   -303     36    271       N\\nATOM    616  CA  MET A 117       4.373  11.084  -1.977  1.00 63.01           C\\nANISOU  616  CA  MET A 117     7536   8218   8187   -406    135    188       C\\nATOM    617  C   MET A 117       5.457  10.093  -1.578  1.00 71.53           C\\nANISOU  617  C   MET A 117     8783   9196   9201   -439    202    236       C\\nATOM    618  O   MET A 117       5.388   9.526  -0.482  1.00 77.20           O\\nANISOU  618  O   MET A 117     9549   9888   9894   -524    260    225       O\\nATOM    619  CB  MET A 117       3.132  10.337  -2.457  1.00 61.50           C\\nANISOU  619  CB  MET A 117     7283   8115   7968   -518    120    103       C\\nATOM    620  CG  MET A 117       1.975  11.258  -2.770  1.00 64.85           C\\nANISOU  620  CG  MET A 117     7509   8654   8476   -463     28     19       C\\nATOM    621  SD  MET A 117       1.790  12.509  -1.489  1.00 62.59           S\\nANISOU  621  SD  MET A 117     7071   8409   8301   -354     37    -66       S\\nATOM    622  CE  MET A 117       0.518  13.548  -2.206  1.00 56.74           C\\nANISOU  622  CE  MET A 117     6109   7754   7697   -221   -153   -189       C\\nATOM    623  N   CYS A 118       6.449   9.867  -2.434  1.00 70.60           N\\nANISOU  623  N   CYS A 118     8747   9036   9042   -373    183    282       N\\nATOM    624  CA  CYS A 118       7.576   9.023  -2.062  1.00 70.67           C\\nANISOU  624  CA  CYS A 118     8885   8946   9021   -346    211    289       C\\nATOM    625  C   CYS A 118       8.689   9.813  -1.387  1.00 68.27           C\\nANISOU  625  C   CYS A 118     8564   8615   8761   -260    228    351       C\\nATOM    626  O   CYS A 118       9.435   9.249  -0.578  1.00 62.32           O\\nANISOU  626  O   CYS A 118     7898   7774   8009   -239    233    351       O\\nATOM    627  CB  CYS A 118       8.121   8.295  -3.295  1.00 71.86           C\\nANISOU  627  CB  CYS A 118     9091   9112   9101   -295    188    239       C\\nATOM    628  SG  CYS A 118       6.974   7.093  -4.021  1.00 68.74           S\\nANISOU  628  SG  CYS A 118     8755   8698   8664   -398    132    131       S\\nATOM    629  N   THR A 119       8.819  11.105  -1.703  1.00 71.90           N\\nANISOU  629  N   THR A 119     8925   9128   9267   -218    203    409       N\\nATOM    630  CA  THR A 119       9.769  11.947  -0.985  1.00 68.93           C\\nANISOU  630  CA  THR A 119     8523   8711   8956   -165    196    461       C\\nATOM    631  C   THR A 119       9.300  12.212   0.440  1.00 62.52           C\\nANISOU  631  C   THR A 119     7704   7861   8191   -175    201    411       C\\nATOM    632  O   THR A 119      10.125  12.295   1.357  1.00 61.89           O\\nANISOU  632  O   THR A 119     7656   7732   8127   -144    202    417       O\\nATOM    633  CB  THR A 119       9.981  13.271  -1.728  1.00 67.89           C\\nANISOU  633  CB  THR A 119     8314   8606   8874   -156    129    558       C\\nATOM    634  OG1 THR A 119      10.268  13.009  -3.105  1.00 63.88           O\\nANISOU  634  OG1 THR A 119     7808   8202   8260   -182    139    610       O\\nATOM    635  CG2 THR A 119      11.148  14.045  -1.129  1.00 64.40           C\\nANISOU  635  CG2 THR A 119     7848   8113   8507   -132    108    616       C\\nATOM    636  N   ALA A 120       7.987  12.343   0.642  1.00 61.79           N\\nANISOU  636  N   ALA A 120     7547   7824   8105   -218    203    341       N\\nATOM    637  CA  ALA A 120       7.457  12.486   1.992  1.00 59.49           C\\nANISOU  637  CA  ALA A 120     7220   7579   7805   -246    240    258       C\\nATOM    638  C   ALA A 120       7.815  11.283   2.852  1.00 61.28           C\\nANISOU  638  C   ALA A 120     7585   7779   7919   -337    300    286       C\\nATOM    639  O   ALA A 120       8.114  11.433   4.041  1.00 62.06           O\\nANISOU  639  O   ALA A 120     7711   7891   7976   -343    316    271       O\\nATOM    640  CB  ALA A 120       5.943  12.676   1.947  1.00 60.06           C\\nANISOU  640  CB  ALA A 120     7153   7780   7886   -287    251    145       C\\nATOM    641  N   SER A 121       7.784  10.080   2.268  1.00 59.91           N\\nANISOU  641  N   SER A 121     7518   7552   7694   -409    305    325       N\\nATOM    642  CA  SER A 121       8.208   8.889   2.998  1.00 65.17           C\\nANISOU  642  CA  SER A 121     8361   8120   8282   -489    296    378       C\\nATOM    643  C   SER A 121       9.662   9.003   3.431  1.00 68.85           C\\nANISOU  643  C   SER A 121     8900   8486   8775   -361    241    416       C\\nATOM    644  O   SER A 121      10.014   8.643   4.561  1.00 69.48           O\\nANISOU  644  O   SER A 121     9088   8521   8792   -399    214    457       O\\nATOM    645  CB  SER A 121       8.013   7.640   2.137  1.00 61.09           C\\nANISOU  645  CB  SER A 121     7954   7505   7753   -550    254    383       C\\nATOM    646  OG  SER A 121       6.661   7.485   1.747  1.00 71.73           O\\nANISOU  646  OG  SER A 121     9221   8952   9081   -688    290    343       O\\nATOM    647  N   ALA A 122      10.522   9.500   2.544  1.00 66.20           N\\nANISOU  647  N   ALA A 122     8498   8140   8516   -228    219    409       N\\nATOM    648  CA  ALA A 122      11.932   9.632   2.882  1.00 64.09           C\\nANISOU  648  CA  ALA A 122     8247   7817   8288   -115    169    424       C\\nATOM    649  C   ALA A 122      12.144  10.731   3.911  1.00 67.35           C\\nANISOU  649  C   ALA A 122     8599   8264   8729    -99    162    428       C\\nATOM    650  O   ALA A 122      12.870  10.544   4.893  1.00 67.60           O\\nANISOU  650  O   ALA A 122     8699   8245   8739    -68    109    438       O\\nATOM    651  CB  ALA A 122      12.746   9.905   1.621  1.00 62.95           C\\nANISOU  651  CB  ALA A 122     8005   7723   8189    -24    175    411       C\\nATOM    652  N   LEU A 123      11.511  11.886   3.707  1.00 62.65           N\\nANISOU  652  N   LEU A 123     7879   7737   8186   -107    182    403       N\\nATOM    653  CA  LEU A 123      11.661  12.982   4.654  1.00 64.73           C\\nANISOU  653  CA  LEU A 123     8084   8013   8499    -71    145    360       C\\nATOM    654  C   LEU A 123      11.002  12.677   5.993  1.00 68.58           C\\nANISOU  654  C   LEU A 123     8623   8569   8865   -134    179    297       C\\nATOM    655  O   LEU A 123      11.397  13.259   7.008  1.00 65.26           O\\nANISOU  655  O   LEU A 123     8197   8165   8435    -96    140    244       O\\nATOM    656  CB  LEU A 123      11.095  14.271   4.056  1.00 60.03           C\\nANISOU  656  CB  LEU A 123     7361   7429   8020    -42    106    331       C\\nATOM    657  CG  LEU A 123      12.060  15.137   3.236  1.00 62.40           C\\nANISOU  657  CG  LEU A 123     7610   7663   8437    -13     31    421       C\\nATOM    658  CD1 LEU A 123      12.857  14.325   2.223  1.00 59.85           C\\nANISOU  658  CD1 LEU A 123     7308   7374   8057    -33     81    508       C\\nATOM    659  CD2 LEU A 123      11.293  16.248   2.540  1.00 58.42           C\\nANISOU  659  CD2 LEU A 123     7032   7125   8039     -7    -54    431       C\\nATOM    660  N   ASN A 124      10.015  11.778   6.022  1.00 64.20           N\\nANISOU  660  N   ASN A 124     8115   8078   8200   -253    250    303       N\\nATOM    661  CA  ASN A 124       9.452  11.343   7.295  1.00 68.55           C\\nANISOU  661  CA  ASN A 124     8724   8742   8580   -376    301    282       C\\nATOM    662  C   ASN A 124      10.430  10.450   8.047  1.00 72.49           C\\nANISOU  662  C   ASN A 124     9424   9133   8985   -402    229    393       C\\nATOM    663  O   ASN A 124      10.617  10.600   9.260  1.00 78.80           O\\nANISOU  663  O   ASN A 124    10273  10006   9661   -433    215    382       O\\nATOM    664  CB  ASN A 124       8.129  10.616   7.067  1.00 63.03           C\\nANISOU  664  CB  ASN A 124     8004   8152   7791   -549    391    281       C\\nATOM    665  CG  ASN A 124       6.940  11.540   7.141  1.00 59.12           C\\nANISOU  665  CG  ASN A 124     7283   7866   7312   -543    463    113       C\\nATOM    666  OD1 ASN A 124       6.864  12.399   8.016  1.00 58.74           O\\nANISOU  666  OD1 ASN A 124     7141   7941   7236   -481    474    -16       O\\nATOM    667  ND2 ASN A 124       6.000  11.373   6.218  1.00 59.97           N\\nANISOU  667  ND2 ASN A 124     7292   8020   7473   -588    490     83       N\\nATOM    668  N   LEU A 125      11.062   9.508   7.343  1.00 66.29           N\\nANISOU  668  N   LEU A 125     8756   8179   8253   -373    162    480       N\\nATOM    669  CA  LEU A 125      12.084   8.682   7.972  1.00 65.46           C\\nANISOU  669  CA  LEU A 125     8836   7929   8106   -343     35    565       C\\nATOM    670  C   LEU A 125      13.243   9.524   8.477  1.00 65.97           C\\nANISOU  670  C   LEU A 125     8840   7991   8234   -191    -37    522       C\\nATOM    671  O   LEU A 125      13.922   9.139   9.436  1.00 61.15           O\\nANISOU  671  O   LEU A 125     8360   7325   7547   -177   -149    572       O\\nATOM    672  CB  LEU A 125      12.583   7.629   6.988  1.00 62.70           C\\nANISOU  672  CB  LEU A 125     8578   7397   7847   -276    -48    593       C\\nATOM    673  CG  LEU A 125      11.555   6.553   6.663  1.00 64.43           C\\nANISOU  673  CG  LEU A 125     8919   7557   8006   -451    -38    646       C\\nATOM    674  CD1 LEU A 125      12.089   5.633   5.597  1.00 62.96           C\\nANISOU  674  CD1 LEU A 125     8802   7188   7932   -337   -140    608       C\\nATOM    675  CD2 LEU A 125      11.214   5.779   7.920  1.00 61.82           C\\nANISOU  675  CD2 LEU A 125     8799   7183   7505   -650   -100    783       C\\nATOM    676  N   CYS A 126      13.482  10.673   7.849  1.00 67.22           N\\nANISOU  676  N   CYS A 126     8812   8199   8530    -94      0    444       N\\nATOM    677  CA  CYS A 126      14.522  11.568   8.333  1.00 68.85           C\\nANISOU  677  CA  CYS A 126     8945   8402   8814     11    -78    401       C\\nATOM    678  C   CYS A 126      14.084  12.257   9.617  1.00 71.84           C\\nANISOU  678  C   CYS A 126     9323   8885   9086    -30    -78    330       C\\nATOM    679  O   CYS A 126      14.848  12.331  10.588  1.00 74.42           O\\nANISOU  679  O   CYS A 126     9709   9205   9362      8   -177    320       O\\nATOM    680  CB  CYS A 126      14.866  12.592   7.257  1.00 64.79           C\\nANISOU  680  CB  CYS A 126     8252   7891   8474     72    -60    375       C\\nATOM    681  SG  CYS A 126      16.409  13.441   7.561  1.00 69.06           S\\nANISOU  681  SG  CYS A 126     8693   8402   9146    160   -175    353       S\\nATOM    682  N   ALA A 127      12.849  12.762   9.642  1.00 60.58           N\\nANISOU  682  N   ALA A 127     7817   7582   7618    -95     24    250       N\\nATOM    683  CA  ALA A 127      12.322  13.375  10.854  1.00 61.10           C\\nANISOU  683  CA  ALA A 127     7852   7809   7555   -121     44    122       C\\nATOM    684  C   ALA A 127      12.220  12.369  11.990  1.00 65.12           C\\nANISOU  684  C   ALA A 127     8538   8411   7794   -256     52    201       C\\nATOM    685  O   ALA A 127      12.407  12.729  13.158  1.00 65.71           O\\nANISOU  685  O   ALA A 127     8640   8603   7724   -258     16    127       O\\nATOM    686  CB  ALA A 127      10.957  13.996  10.570  1.00 60.25           C\\nANISOU  686  CB  ALA A 127     7585   7843   7462   -141    147    -17       C\\nATOM    687  N   ILE A 128      11.925  11.108  11.673  1.00 64.09           N\\nANISOU  687  N   ILE A 128     8546   8221   7582   -384     77    357       N\\nATOM    688  CA  ILE A 128      11.829  10.083  12.705  1.00 61.38           C\\nANISOU  688  CA  ILE A 128     8417   7924   6982   -558     46    492       C\\nATOM    689  C   ILE A 128      13.184   9.868  13.370  1.00 64.99           C\\nANISOU  689  C   ILE A 128     9025   8241   7426   -455   -148    563       C\\nATOM    690  O   ILE A 128      13.286   9.807  14.600  1.00 69.74           O\\nANISOU  690  O   ILE A 128     9740   8959   7800   -534   -198    591       O\\nATOM    691  CB  ILE A 128      11.271   8.779  12.108  1.00 62.32           C\\nANISOU  691  CB  ILE A 128     8673   7934   7072   -722     61    653       C\\nATOM    692  CG1 ILE A 128       9.772   8.923  11.836  1.00 63.83           C\\nANISOU  692  CG1 ILE A 128     8711   8345   7195   -888    252    582       C\\nATOM    693  CG2 ILE A 128      11.548   7.604  13.028  1.00 64.88           C\\nANISOU  693  CG2 ILE A 128     9290   8172   7190   -886    -69    860       C\\nATOM    694  CD1 ILE A 128       9.120   7.668  11.294  1.00 68.59           C\\nANISOU  694  CD1 ILE A 128     9440   8852   7770  -1092    259    730       C\\nATOM    695  N   SER A 129      14.244   9.756  12.565  1.00 66.20           N\\nANISOU  695  N   SER A 129     9164   8178   7810   -278   -262    578       N\\nATOM    696  CA  SER A 129      15.586   9.611  13.121  1.00 63.02           C\\nANISOU  696  CA  SER A 129     8848   7658   7438   -147   -463    607       C\\nATOM    697  C   SER A 129      15.949  10.799  13.998  1.00 65.47           C\\nANISOU  697  C   SER A 129     9055   8109   7713    -86   -487    474       C\\nATOM    698  O   SER A 129      16.527  10.629  15.078  1.00 65.88           O\\nANISOU  698  O   SER A 129     9234   8177   7619    -82   -631    506       O\\nATOM    699  CB  SER A 129      16.603   9.467  11.995  1.00 65.36           C\\nANISOU  699  CB  SER A 129     9050   7784   7998     39   -538    582       C\\nATOM    700  OG  SER A 129      16.749  10.693  11.302  1.00 65.87           O\\nANISOU  700  OG  SER A 129     8871   7922   8235    114   -445    460       O\\nATOM    701  N   ILE A 130      15.624  12.011  13.546  1.00 64.82           N\\nANISOU  701  N   ILE A 130     8755   8106   7766    -35   -383    319       N\\nATOM    702  CA  ILE A 130      15.959  13.208  14.313  1.00 68.76           C\\nANISOU  702  CA  ILE A 130     9156   8695   8276     36   -439    156       C\\nATOM    703  C   ILE A 130      15.205  13.216  15.636  1.00 70.22           C\\nANISOU  703  C   ILE A 130     9425   9110   8144    -76   -395     92       C\\nATOM    704  O   ILE A 130      15.775  13.502  16.695  1.00 76.17           O\\nANISOU  704  O   ILE A 130    10235   9933   8773    -45   -514     30       O\\nATOM    705  CB  ILE A 130      15.668  14.473  13.488  1.00 69.26           C\\nANISOU  705  CB  ILE A 130     9002   8739   8574    105   -379     19       C\\nATOM    706  CG1 ILE A 130      16.553  14.504  12.241  1.00 65.51           C\\nANISOU  706  CG1 ILE A 130     8440   8094   8355    174   -420    103       C\\nATOM    707  CG2 ILE A 130      15.878  15.716  14.329  1.00 65.28           C\\nANISOU  707  CG2 ILE A 130     8415   8293   8097    175   -469   -180       C\\nATOM    708  CD1 ILE A 130      16.380  15.745  11.402  1.00 62.56           C\\nANISOU  708  CD1 ILE A 130     7895   7673   8203    202   -405     32       C\\nATOM    709  N   ASP A 131      13.909  12.904  15.595  1.00 70.28           N\\nANISOU  709  N   ASP A 131     9426   9280   7998   -221   -219     94       N\\nATOM    710  CA  ASP A 131      13.155  12.749  16.833  1.00 71.28           C\\nANISOU  710  CA  ASP A 131     9617   9702   7763   -378   -141     50       C\\nATOM    711  C   ASP A 131      13.708  11.611  17.677  1.00 75.20           C\\nANISOU  711  C   ASP A 131    10397  10170   8008   -506   -269    283       C\\nATOM    712  O   ASP A 131      13.639  11.660  18.910  1.00 73.14           O\\nANISOU  712  O   ASP A 131    10222  10134   7432   -599   -289    255       O\\nATOM    713  CB  ASP A 131      11.678  12.515  16.525  1.00 70.71           C\\nANISOU  713  CB  ASP A 131     9449   9834   7586   -540     79     22       C\\nATOM    714  CG  ASP A 131      10.820  12.477  17.775  1.00 76.68           C\\nANISOU  714  CG  ASP A 131    10201  10991   7942   -727    206    -66       C\\nATOM    715  OD1 ASP A 131      10.819  13.472  18.528  1.00 78.05           O\\nANISOU  715  OD1 ASP A 131    10254  11363   8039   -619    204   -327       O\\nATOM    716  OD2 ASP A 131      10.140  11.455  18.001  1.00 79.31           O\\nANISOU  716  OD2 ASP A 131    10647  11456   8030   -996    304    118       O\\nATOM    717  N   ARG A 132      14.264  10.581  17.036  1.00 72.55           N\\nANISOU  717  N   ARG A 132    10215   9556   7796   -504   -380    502       N\\nATOM    718  CA  ARG A 132      14.921   9.521  17.791  1.00 74.39           C\\nANISOU  718  CA  ARG A 132    10739   9679   7847   -579   -584    726       C\\nATOM    719  C   ARG A 132      16.221  10.003  18.417  1.00 74.84           C\\nANISOU  719  C   ARG A 132    10811   9673   7954   -388   -804    656       C\\nATOM    720  O   ARG A 132      16.614   9.507  19.479  1.00 74.70           O\\nANISOU  720  O   ARG A 132    11012   9686   7686   -458   -973    778       O\\nATOM    721  CB  ARG A 132      15.175   8.307  16.894  1.00 71.71           C\\nANISOU  721  CB  ARG A 132    10547   9024   7674   -578   -687    923       C\\nATOM    722  CG  ARG A 132      13.976   7.378  16.715  1.00 69.10           C\\nANISOU  722  CG  ARG A 132    10338   8727   7188   -858   -567   1086       C\\nATOM    723  CD  ARG A 132      13.493   6.832  18.055  1.00 75.91           C\\nANISOU  723  CD  ARG A 132    11433   9782   7627  -1155   -591   1269       C\\nATOM    724  NE  ARG A 132      12.518   7.717  18.686  1.00 77.94           N\\nANISOU  724  NE  ARG A 132    11497  10480   7636  -1291   -337   1099       N\\nATOM    725  CZ  ARG A 132      12.271   7.756  19.990  1.00 77.58           C\\nANISOU  725  CZ  ARG A 132    11552  10740   7186  -1484   -317   1141       C\\nATOM    726  NH1 ARG A 132      12.931   6.960  20.822  1.00 76.41           N\\nANISOU  726  NH1 ARG A 132    11728  10477   6827  -1585   -559   1394       N\\nATOM    727  NH2 ARG A 132      11.366   8.602  20.464  1.00 79.78           N\\nANISOU  727  NH2 ARG A 132    11599  11452   7261  -1565    -71    912       N\\nATOM    728  N   TYR A 133      16.902  10.960  17.786  1.00 73.32           N\\nANISOU  728  N   TYR A 133    10393   9395   8070   -171   -822    476       N\\nATOM    729  CA  TYR A 133      18.124  11.492  18.379  1.00 72.55           C\\nANISOU  729  CA  TYR A 133    10271   9257   8037    -13  -1032    389       C\\nATOM    730  C   TYR A 133      17.813  12.311  19.624  1.00 76.41           C\\nANISOU  730  C   TYR A 133    10753  10016   8263    -65  -1020    228       C\\nATOM    731  O   TYR A 133      18.475  12.161  20.658  1.00 82.66           O\\nANISOU  731  O   TYR A 133    11685  10852   8869    -54  -1214    255       O\\nATOM    732  CB  TYR A 133      18.894  12.340  17.365  1.00 65.57           C\\nANISOU  732  CB  TYR A 133     9133   8238   7542    169  -1045    254       C\\nATOM    733  CG  TYR A 133      20.160  12.957  17.931  1.00 69.03           C\\nANISOU  733  CG  TYR A 133     9504   8648   8079    305  -1262    149       C\\nATOM    734  CD1 TYR A 133      21.367  12.268  17.901  1.00 73.59           C\\nANISOU  734  CD1 TYR A 133    10124   9075   8760    424  -1482    232       C\\nATOM    735  CD2 TYR A 133      20.148  14.224  18.502  1.00 67.30           C\\nANISOU  735  CD2 TYR A 133     9162   8546   7862    326  -1271    -61       C\\nATOM    736  CE1 TYR A 133      22.526  12.825  18.419  1.00 73.44           C\\nANISOU  736  CE1 TYR A 133    10011   9052   8839    539  -1690    123       C\\nATOM    737  CE2 TYR A 133      21.303  14.789  19.022  1.00 69.25           C\\nANISOU  737  CE2 TYR A 133     9341   8760   8209    429  -1488   -164       C\\nATOM    738  CZ  TYR A 133      22.488  14.084  18.977  1.00 74.54           C\\nANISOU  738  CZ  TYR A 133    10039   9309   8975    524  -1689    -64       C\\nATOM    739  OH  TYR A 133      23.637  14.640  19.490  1.00 78.51           O\\nANISOU  739  OH  TYR A 133    10443   9800   9586    618  -1914   -178       O\\nATOM    740  N   THR A 134      16.813  13.190  19.544  1.00 70.79           N\\nANISOU  740  N   THR A 134     9871   9496   7530   -102   -814     34       N\\nATOM    741  CA  THR A 134      16.526  14.064  20.674  1.00 74.84           C\\nANISOU  741  CA  THR A 134    10337  10284   7814   -106   -805   -201       C\\nATOM    742  C   THR A 134      16.021  13.276  21.876  1.00 73.81           C\\nANISOU  742  C   THR A 134    10425  10433   7188   -319   -780    -82       C\\nATOM    743  O   THR A 134      16.266  13.672  23.021  1.00 83.45           O\\nANISOU  743  O   THR A 134    11696  11863   8150   -318   -870   -208       O\\nATOM    744  CB  THR A 134      15.517  15.137  20.270  1.00 81.04           C\\nANISOU  744  CB  THR A 134    10877  11199   8715    -61   -617   -471       C\\nATOM    745  OG1 THR A 134      14.231  14.541  20.084  1.00 85.24           O\\nANISOU  745  OG1 THR A 134    11407  11920   9060   -236   -387   -405       O\\nATOM    746  CG2 THR A 134      15.945  15.803  18.969  1.00 80.96           C\\nANISOU  746  CG2 THR A 134    10697  10893   9169     91   -653   -505       C\\nATOM    747  N   ALA A 135      15.341  12.151  21.642  1.00 74.49           N\\nANISOU  747  N   ALA A 135    10655  10530   7120   -527   -674    172       N\\nATOM    748  CA  ALA A 135      14.858  11.340  22.756  1.00 76.81           C\\nANISOU  748  CA  ALA A 135    11182  11087   6918   -800   -658    350       C\\nATOM    749  C   ALA A 135      16.008  10.654  23.480  1.00 76.81           C\\nANISOU  749  C   ALA A 135    11471  10921   6791   -787   -978    571       C\\nATOM    750  O   ALA A 135      15.979  10.505  24.707  1.00 82.26           O\\nANISOU  750  O   ALA A 135    12330  11871   7053   -935  -1044    623       O\\nATOM    751  CB  ALA A 135      13.849  10.307  22.259  1.00 69.76           C\\nANISOU  751  CB  ALA A 135    10373  10203   5930  -1063   -492    588       C\\nATOM    752  N   VAL A 136      17.029  10.233  22.739  1.00 76.95           N\\nANISOU  752  N   VAL A 136    11539  10534   7164   -603  -1189    688       N\\nATOM    753  CA  VAL A 136      18.154   9.535  23.350  1.00 82.31           C\\nANISOU  753  CA  VAL A 136    12472  11024   7777   -545  -1537    878       C\\nATOM    754  C   VAL A 136      19.136  10.524  23.967  1.00 82.04           C\\nANISOU  754  C   VAL A 136    12325  11053   7795   -336  -1708    644       C\\nATOM    755  O   VAL A 136      19.554  10.367  25.120  1.00 81.48           O\\nANISOU  755  O   VAL A 136    12446  11103   7411   -382  -1911    704       O\\nATOM    756  CB  VAL A 136      18.839   8.630  22.309  1.00 77.31           C\\nANISOU  756  CB  VAL A 136    11904   9961   7508   -406  -1706   1045       C\\nATOM    757  CG1 VAL A 136      20.246   8.278  22.755  1.00 77.43           C\\nANISOU  757  CG1 VAL A 136    12049   9764   7606   -210  -2095   1106       C\\nATOM    758  CG2 VAL A 136      18.017   7.366  22.083  1.00 72.64           C\\nANISOU  758  CG2 VAL A 136    11557   9266   6777   -655  -1667   1340       C\\nATOM    759  N   ALA A 137      19.501  11.568  23.224  1.00 77.79           N\\nANISOU  759  N   ALA A 137    11484  10437   7637   -128  -1644    384       N\\nATOM    760  CA  ALA A 137      20.609  12.434  23.603  1.00 80.22           C\\nANISOU  760  CA  ALA A 137    11669  10715   8097     69  -1852    182       C\\nATOM    761  C   ALA A 137      20.209  13.605  24.491  1.00 87.12           C\\nANISOU  761  C   ALA A 137    12440  11898   8765     54  -1780   -115       C\\nATOM    762  O   ALA A 137      21.094  14.243  25.073  1.00 87.55           O\\nANISOU  762  O   ALA A 137    12447  11955   8861    179  -1994   -277       O\\nATOM    763  CB  ALA A 137      21.304  12.975  22.349  1.00 74.40           C\\nANISOU  763  CB  ALA A 137    10663   9730   7877    260  -1849     74       C\\nATOM    764  N   MET A 138      18.922  13.910  24.616  1.00 85.65           N\\nANISOU  764  N   MET A 138    12198  11978   8368    -81  -1504   -224       N\\nATOM    765  CA  MET A 138      18.517  15.099  25.348  1.00 91.36           C\\nANISOU  765  CA  MET A 138    12776  12989   8948    -40  -1439   -587       C\\nATOM    766  C   MET A 138      17.450  14.760  26.377  1.00 93.65           C\\nANISOU  766  C   MET A 138    13184  13730   8670   -264  -1268   -595       C\\nATOM    767  O   MET A 138      16.648  13.844  26.169  1.00 90.32           O\\nANISOU  767  O   MET A 138    12865  13389   8064   -478  -1095   -353       O\\nATOM    768  CB  MET A 138      18.001  16.181  24.387  1.00 94.18           C\\nANISOU  768  CB  MET A 138    12839  13259   9687     83  -1276   -847       C\\nATOM    769  CG  MET A 138      19.095  16.769  23.500  1.00 98.65           C\\nANISOU  769  CG  MET A 138    13264  13452  10767    263  -1446   -874       C\\nATOM    770  SD  MET A 138      18.521  18.077  22.402  1.00105.80           S\\nANISOU  770  SD  MET A 138    13881  14215  12101    371  -1319  -1121       S\\nATOM    771  CE  MET A 138      20.031  18.481  21.533  1.00105.56           C\\nANISOU  771  CE  MET A 138    13744  13805  12559    477  -1542  -1039       C\\nATOM    772  N   PRO A 139      17.425  15.482  27.515  1.00104.46           N\\nANISOU  772  N   PRO A 139    14532  15425   9735   -241  -1315   -880       N\\nATOM    773  CA  PRO A 139      16.509  15.224  28.635  1.00105.59           C\\nANISOU  773  CA  PRO A 139    14765  16095   9259   -469  -1152   -923       C\\nATOM    774  C   PRO A 139      15.042  15.103  28.221  1.00104.65           C\\nANISOU  774  C   PRO A 139    14492  16238   9033   -630   -782   -969       C\\nATOM    775  O   PRO A 139      14.317  16.097  28.261  1.00106.02           O\\nANISOU  775  O   PRO A 139    14394  16653   9234   -519   -617  -1385       O\\nATOM    776  CB  PRO A 139      16.714  16.446  29.535  1.00103.32           C\\nANISOU  776  CB  PRO A 139    14347  16058   8852   -301  -1242  -1390       C\\nATOM    777  CG  PRO A 139      18.112  16.868  29.263  1.00100.62           C\\nANISOU  777  CG  PRO A 139    14009  15289   8934    -72  -1575  -1406       C\\nATOM    778  CD  PRO A 139      18.340  16.603  27.805  1.00 97.12           C\\nANISOU  778  CD  PRO A 139    13483  14389   9030     -4  -1545  -1193       C\\nATOM    779  N   THR A 144       8.716  17.350  27.929  1.00103.31           N\\nANISOU  779  N   THR A 144    12885  17966   8400   -718    631  -2535       N\\nATOM    780  CA  THR A 144       7.590  18.233  28.208  1.00111.55           C\\nANISOU  780  CA  THR A 144    13533  19499   9351   -578    832  -3111       C\\nATOM    781  C   THR A 144       6.396  17.895  27.318  1.00111.78           C\\nANISOU  781  C   THR A 144    13322  19627   9521   -685   1084  -3075       C\\nATOM    782  O   THR A 144       6.556  17.666  26.122  1.00115.16           O\\nANISOU  782  O   THR A 144    13802  19541  10411   -631   1006  -2812       O\\nATOM    783  CB  THR A 144       7.971  19.712  28.006  1.00112.47           C\\nANISOU  783  CB  THR A 144    13477  19327   9931   -104    597  -3618       C\\nATOM    784  N   ARG A 145       5.198  17.868  27.907  1.00112.87           N\\nANISOU  784  N   ARG A 145    13181  20279   9425   -824   1334  -3251       N\\nATOM    785  CA  ARG A 145       4.002  17.509  27.151  1.00114.09           C\\nANISOU  785  CA  ARG A 145    13078  20551   9719   -950   1551  -3212       C\\nATOM    786  C   ARG A 145       3.581  18.596  26.170  1.00118.73           C\\nANISOU  786  C   ARG A 145    13352  20930  10830   -531   1477  -3651       C\\nATOM    787  O   ARG A 145       2.846  18.305  25.221  1.00119.01           O\\nANISOU  787  O   ARG A 145    13234  20913  11072   -582   1585  -3578       O\\nATOM    788  CB  ARG A 145       2.846  17.198  28.104  1.00118.50           C\\nANISOU  788  CB  ARG A 145    13396  21689   9937  -1221   1786  -3270       C\\nATOM    789  N   TYR A 146       4.024  19.834  26.375  1.00121.59           N\\nANISOU  789  N   TYR A 146    13630  21133  11434   -123   1259  -4089       N\\nATOM    790  CA  TYR A 146       3.700  20.948  25.491  1.00117.64           C\\nANISOU  790  CA  TYR A 146    12880  20335  11482    295   1102  -4485       C\\nATOM    791  C   TYR A 146       4.829  21.280  24.526  1.00108.31           C\\nANISOU  791  C   TYR A 146    11951  18428  10772    498    805  -4303       C\\nATOM    792  O   TYR A 146       4.573  21.530  23.344  1.00100.71           O\\nANISOU  792  O   TYR A 146    10911  17078  10275    638    718  -4241       O\\nATOM    793  CB  TYR A 146       3.345  22.185  26.325  1.00124.08           C\\nANISOU  793  CB  TYR A 146    13429  21323  12394    606    974  -5030       C\\nATOM    794  CG  TYR A 146       3.156  23.462  25.533  1.00125.41           C\\nANISOU  794  CG  TYR A 146    13400  21084  13165   1062    702  -5422       C\\nATOM    795  CD1 TYR A 146       1.920  23.794  24.993  1.00128.22           C\\nANISOU  795  CD1 TYR A 146    13405  21556  13758   1181    740  -5641       C\\nATOM    796  CD2 TYR A 146       4.211  24.347  25.345  1.00125.84           C\\nANISOU  796  CD2 TYR A 146    13634  20614  13563   1355    362  -5554       C\\nATOM    797  CE1 TYR A 146       1.746  24.966  24.276  1.00131.82           C\\nANISOU  797  CE1 TYR A 146    13721  21595  14769   1588    432  -5955       C\\nATOM    798  CE2 TYR A 146       4.047  25.515  24.631  1.00128.03           C\\nANISOU  798  CE2 TYR A 146    13776  20456  14413   1732     64  -5846       C\\nATOM    799  CZ  TYR A 146       2.815  25.821  24.099  1.00132.64           C\\nANISOU  799  CZ  TYR A 146    14037  21147  15214   1852     92  -6034       C\\nATOM    800  OH  TYR A 146       2.656  26.988  23.388  1.00136.93           O\\nANISOU  800  OH  TYR A 146    14484  21222  16320   2213   -261  -6277       O\\nATOM    801  N   SER A 147       6.076  21.287  25.005  1.00108.97           N\\nANISOU  801  N   SER A 147    12336  18257  10810    490    611  -4125       N\\nATOM    802  CA  SER A 147       7.206  21.602  24.138  1.00104.01           C\\nANISOU  802  CA  SER A 147    11926  16901  10691    633    308  -3860       C\\nATOM    803  C   SER A 147       7.407  20.541  23.065  1.00103.85           C\\nANISOU  803  C   SER A 147    12083  16559  10818    407    370  -3277       C\\nATOM    804  O   SER A 147       7.842  20.861  21.953  1.00 99.45           O\\nANISOU  804  O   SER A 147    11570  15480  10738    539    199  -3123       O\\nATOM    805  CB  SER A 147       8.481  21.758  24.972  1.00101.67           C\\nANISOU  805  CB  SER A 147    11877  16479  10273    647     99  -3814       C\\nATOM    806  N   SER A 148       7.103  19.279  23.375  1.00100.58           N\\nANISOU  806  N   SER A 148    11778  16447   9991     56    598  -2950       N\\nATOM    807  CA  SER A 148       7.325  18.214  22.404  1.00 97.98           C\\nANISOU  807  CA  SER A 148    11636  15794   9798   -147    625  -2427       C\\nATOM    808  C   SER A 148       6.273  18.239  21.303  1.00 88.88           C\\nANISOU  808  C   SER A 148    10254  14611   8905   -117    745  -2472       C\\nATOM    809  O   SER A 148       6.602  18.071  20.125  1.00 80.56           O\\nANISOU  809  O   SER A 148     9283  13109   8218    -74    646  -2217       O\\nATOM    810  CB  SER A 148       7.339  16.858  23.106  1.00103.00           C\\nANISOU  810  CB  SER A 148    12497  16702   9935   -541    771  -2055       C\\nATOM    811  OG  SER A 148       6.089  16.599  23.719  1.00106.17           O\\nANISOU  811  OG  SER A 148    12692  17721   9926   -754   1057  -2228       O\\nATOM    812  N   LYS A 149       5.003  18.446  21.667  1.00 92.05           N\\nANISOU  812  N   LYS A 149    10349  15519   9108   -139    955  -2812       N\\nATOM    813  CA  LYS A 149       3.946  18.506  20.661  1.00 84.26           C\\nANISOU  813  CA  LYS A 149     9110  14536   8369    -93   1046  -2895       C\\nATOM    814  C   LYS A 149       4.192  19.638  19.673  1.00 88.93           C\\nANISOU  814  C   LYS A 149     9627  14634   9529    289    781  -3067       C\\nATOM    815  O   LYS A 149       3.943  19.488  18.470  1.00 93.01           O\\nANISOU  815  O   LYS A 149    10125  14862  10350    308    742  -2887       O\\nATOM    816  CB  LYS A 149       2.585  18.670  21.333  1.00 79.97           C\\nANISOU  816  CB  LYS A 149     8188  14678   7518   -142   1299  -3315       C\\nATOM    817  N   ARG A 150       4.688  20.778  20.160  1.00 87.49           N\\nANISOU  817  N   ARG A 150     9416  14340   9487    578    575  -3405       N\\nATOM    818  CA  ARG A 150       5.060  21.865  19.261  1.00 81.69           C\\nANISOU  818  CA  ARG A 150     8671  13071   9295    893    273  -3505       C\\nATOM    819  C   ARG A 150       6.223  21.474  18.359  1.00 80.21           C\\nANISOU  819  C   ARG A 150     8786  12341   9349    799    130  -2998       C\\nATOM    820  O   ARG A 150       6.317  21.964  17.230  1.00 82.46           O\\nANISOU  820  O   ARG A 150     9071  12222  10039    928    -38  -2909       O\\nATOM    821  CB  ARG A 150       5.411  23.117  20.063  1.00 80.33           C\\nANISOU  821  CB  ARG A 150     8437  12868   9215   1187     52  -3965       C\\nATOM    822  N   ARG A 151       7.111  20.595  18.831  1.00 78.36           N\\nANISOU  822  N   ARG A 151     8802  12110   8862    578    185  -2672       N\\nATOM    823  CA  ARG A 151       8.234  20.166  18.003  1.00 72.71           C\\nANISOU  823  CA  ARG A 151     8328  10937   8361    507     62  -2239       C\\nATOM    824  C   ARG A 151       7.780  19.202  16.916  1.00 79.91           C\\nANISOU  824  C   ARG A 151     9266  11777   9319    342    198  -1915       C\\nATOM    825  O   ARG A 151       8.310  19.226  15.799  1.00 80.42           O\\nANISOU  825  O   ARG A 151     9410  11464   9683    376     87  -1687       O\\nATOM    826  CB  ARG A 151       9.319  19.528  18.870  1.00 74.01           C\\nANISOU  826  CB  ARG A 151     8732  11123   8264    367     34  -2034       C\\nATOM    827  CG  ARG A 151      10.576  19.134  18.110  1.00 82.30           C\\nANISOU  827  CG  ARG A 151     9986  11745   9540    333   -108  -1658       C\\nATOM    828  CD  ARG A 151      11.637  18.577  19.045  1.00 87.06           C\\nANISOU  828  CD  ARG A 151    10798  12374   9905    242   -184  -1509       C\\nATOM    829  NE  ARG A 151      11.097  17.537  19.917  1.00 91.56           N\\nANISOU  829  NE  ARG A 151    11463  13317  10010     18     -7  -1413       N\\nATOM    830  CZ  ARG A 151      11.047  16.249  19.600  1.00 88.57           C\\nANISOU  830  CZ  ARG A 151    11241  12910   9500   -194     83  -1059       C\\nATOM    831  NH1 ARG A 151      10.538  15.370  20.453  1.00 83.32           N\\nANISOU  831  NH1 ARG A 151    10680  12574   8402   -440    216   -953       N\\nATOM    832  NH2 ARG A 151      11.506  15.837  18.428  1.00 87.56           N\\nANISOU  832  NH2 ARG A 151    11174  12429   9667   -175     27   -816       N\\nATOM    833  N   VAL A 152       6.797  18.350  17.218  1.00 81.56           N\\nANISOU  833  N   VAL A 152     9402  12365   9221    140    437  -1897       N\\nATOM    834  CA  VAL A 152       6.288  17.429  16.204  1.00 81.36           C\\nANISOU  834  CA  VAL A 152     9394  12272   9245    -25    549  -1623       C\\nATOM    835  C   VAL A 152       5.564  18.196  15.104  1.00 80.65           C\\nANISOU  835  C   VAL A 152     9093  12045   9504    168    481  -1785       C\\nATOM    836  O   VAL A 152       5.709  17.888  13.915  1.00 78.73           O\\nANISOU  836  O   VAL A 152     8921  11517   9474    149    431  -1543       O\\nATOM    837  CB  VAL A 152       5.377  16.364  16.843  1.00 80.98           C\\nANISOU  837  CB  VAL A 152     9312  12669   8787   -333    803  -1562       C\\nATOM    838  CG1 VAL A 152       5.106  15.241  15.863  1.00 82.24           C\\nANISOU  838  CG1 VAL A 152     9570  12682   8997   -541    871  -1224       C\\nATOM    839  CG2 VAL A 152       6.004  15.810  18.104  1.00 83.35           C\\nANISOU  839  CG2 VAL A 152     9819  13145   8703   -511    831  -1443       C\\nATOM    840  N   THR A 153       4.781  19.211  15.482  1.00 84.22           N\\nANISOU  840  N   THR A 153     9285  12700  10015    371    455  -2213       N\\nATOM    841  CA  THR A 153       4.057  20.004  14.492  1.00 78.54           C\\nANISOU  841  CA  THR A 153     8369  11830   9642    587    332  -2387       C\\nATOM    842  C   THR A 153       5.011  20.696  13.525  1.00 75.61           C\\nANISOU  842  C   THR A 153     8160  10910   9657    737     57  -2208       C\\nATOM    843  O   THR A 153       4.738  20.779  12.322  1.00 76.21           O\\nANISOU  843  O   THR A 153     8221  10766   9967    773    -25  -2073       O\\nATOM    844  CB  THR A 153       3.168  21.031  15.195  1.00 80.46           C\\nANISOU  844  CB  THR A 153     8306  12365   9901    832    300  -2933       C\\nATOM    845  OG1 THR A 153       2.144  20.354  15.937  1.00 82.11           O\\nANISOU  845  OG1 THR A 153     8305  13162   9733    652    595  -3096       O\\nATOM    846  CG2 THR A 153       2.527  21.976  14.186  1.00 77.79           C\\nANISOU  846  CG2 THR A 153     7796  11785   9977   1109     80  -3121       C\\nATOM    847  N   VAL A 154       6.141  21.193  14.030  1.00 73.65           N\\nANISOU  847  N   VAL A 154     8065  10459   9460    799    -90  -2194       N\\nATOM    848  CA  VAL A 154       7.112  21.843  13.156  1.00 71.40           C\\nANISOU  848  CA  VAL A 154     7922   9692   9516    880   -337  -2000       C\\nATOM    849  C   VAL A 154       7.787  20.821  12.246  1.00 67.73           C\\nANISOU  849  C   VAL A 154     7638   9069   9028    675   -255  -1548       C\\nATOM    850  O   VAL A 154       8.007  21.079  11.057  1.00 61.81           O\\nANISOU  850  O   VAL A 154     6927   8041   8515    690   -370  -1361       O\\nATOM    851  CB  VAL A 154       8.137  22.627  13.993  1.00 65.37           C\\nANISOU  851  CB  VAL A 154     7244   8781   8811    974   -518  -2127       C\\nATOM    852  CG1 VAL A 154       9.256  23.154  13.108  1.00 56.93           C\\nANISOU  852  CG1 VAL A 154     6321   7254   8055    968   -742  -1864       C\\nATOM    853  CG2 VAL A 154       7.453  23.767  14.722  1.00 60.75           C\\nANISOU  853  CG2 VAL A 154     6475   8294   8312   1228   -654  -2627       C\\nATOM    854  N   MET A 155       8.122  19.645  12.784  1.00 69.04           N\\nANISOU  854  N   MET A 155     7921   9413   8899    483    -75  -1374       N\\nATOM    855  CA  MET A 155       8.784  18.630  11.972  1.00 68.64           C\\nANISOU  855  CA  MET A 155     8035   9207   8837    329    -24  -1003       C\\nATOM    856  C   MET A 155       7.875  18.134  10.856  1.00 64.55           C\\nANISOU  856  C   MET A 155     7452   8706   8368    269     63   -905       C\\nATOM    857  O   MET A 155       8.316  17.979   9.712  1.00 59.62           O\\nANISOU  857  O   MET A 155     6898   7863   7894    252      8   -690       O\\nATOM    858  CB  MET A 155       9.241  17.467  12.851  1.00 72.37           C\\nANISOU  858  CB  MET A 155     8663   9833   9001    158     94   -859       C\\nATOM    859  CG  MET A 155      10.407  17.803  13.768  1.00 80.64           C\\nANISOU  859  CG  MET A 155     9815  10814  10011    208    -29   -884       C\\nATOM    860  SD  MET A 155      11.031  16.373  14.674  1.00 89.65           S\\nANISOU  860  SD  MET A 155    11184  12069  10810     19     37   -657       S\\nATOM    861  CE  MET A 155      12.405  17.110  15.553  1.00 99.07           C\\nANISOU  861  CE  MET A 155    12443  13153  12047    140   -171   -742       C\\nATOM    862  N   ILE A 156       6.602  17.886  11.166  1.00 67.34           N\\nANISOU  862  N   ILE A 156     7652   9352   8582    227    200  -1075       N\\nATOM    863  CA  ILE A 156       5.685  17.372  10.156  1.00 68.91           C\\nANISOU  863  CA  ILE A 156     7773   9590   8821    157    271  -1001       C\\nATOM    864  C   ILE A 156       5.469  18.403   9.059  1.00 69.08           C\\nANISOU  864  C   ILE A 156     7705   9384   9158    345     81  -1053       C\\nATOM    865  O   ILE A 156       5.484  18.072   7.867  1.00 70.31           O\\nANISOU  865  O   ILE A 156     7916   9392   9407    300     52   -852       O\\nATOM    866  CB  ILE A 156       4.357  16.945  10.806  1.00 70.36           C\\nANISOU  866  CB  ILE A 156     7765  10184   8786     48    458  -1197       C\\nATOM    867  CG1 ILE A 156       4.590  15.773  11.761  1.00 67.02           C\\nANISOU  867  CG1 ILE A 156     7488   9956   8020   -215    628  -1044       C\\nATOM    868  CG2 ILE A 156       3.332  16.571   9.742  1.00 64.85           C\\nANISOU  868  CG2 ILE A 156     6940   9528   8171     -3    496  -1169       C\\nATOM    869  CD1 ILE A 156       3.333  15.249  12.401  1.00 60.59           C\\nANISOU  869  CD1 ILE A 156     6493   9587   6942   -411    838  -1180       C\\nATOM    870  N   SER A 157       5.271  19.668   9.439  1.00 67.59           N\\nANISOU  870  N   SER A 157     7393   9155   9133    558    -76  -1325       N\\nATOM    871  CA  SER A 157       5.081  20.719   8.446  1.00 66.91           C\\nANISOU  871  CA  SER A 157     7261   8799   9364    734   -321  -1352       C\\nATOM    872  C   SER A 157       6.261  20.789   7.488  1.00 65.20           C\\nANISOU  872  C   SER A 157     7252   8247   9275    664   -437  -1006       C\\nATOM    873  O   SER A 157       6.079  20.905   6.271  1.00 70.97           O\\nANISOU  873  O   SER A 157     8005   8831  10130    658   -531   -845       O\\nATOM    874  CB  SER A 157       4.876  22.064   9.138  1.00 53.19           C\\nANISOU  874  CB  SER A 157     5403   7001   7805    983   -525  -1706       C\\nATOM    875  OG  SER A 157       3.770  22.013  10.019  1.00 59.25           O\\nANISOU  875  OG  SER A 157     5930   8154   8428   1059   -395  -2076       O\\nATOM    876  N   ILE A 158       7.481  20.701   8.019  1.00 63.38           N\\nANISOU  876  N   ILE A 158     7159   7930   8993    600   -428   -895       N\\nATOM    877  CA  ILE A 158       8.662  20.757   7.168  1.00 62.29           C\\nANISOU  877  CA  ILE A 158     7167   7544   8955    516   -512   -595       C\\nATOM    878  C   ILE A 158       8.684  19.577   6.207  1.00 66.42           C\\nANISOU  878  C   ILE A 158     7754   8134   9350    369   -356   -352       C\\nATOM    879  O   ILE A 158       9.069  19.717   5.042  1.00 76.92           O\\nANISOU  879  O   ILE A 158     9134   9324  10767    323   -426   -148       O\\nATOM    880  CB  ILE A 158       9.935  20.815   8.030  1.00 62.52           C\\nANISOU  880  CB  ILE A 158     7286   7519   8948    483   -529   -568       C\\nATOM    881  CG1 ILE A 158       9.969  22.114   8.833  1.00 61.54           C\\nANISOU  881  CG1 ILE A 158     7112   7280   8990    635   -734   -823       C\\nATOM    882  CG2 ILE A 158      11.177  20.683   7.165  1.00 56.51           C\\nANISOU  882  CG2 ILE A 158     6625   6594   8253    369   -564   -273       C\\nATOM    883  CD1 ILE A 158      11.102  22.178   9.819  1.00 68.44           C\\nANISOU  883  CD1 ILE A 158     8055   8136   9811    610   -764   -846       C\\nATOM    884  N   VAL A 159       8.260  18.399   6.670  1.00 61.58           N\\nANISOU  884  N   VAL A 159     7145   7737   8515    280   -157   -371       N\\nATOM    885  CA  VAL A 159       8.270  17.217   5.808  1.00 61.95           C\\nANISOU  885  CA  VAL A 159     7267   7816   8456    152    -40   -177       C\\nATOM    886  C   VAL A 159       7.403  17.448   4.578  1.00 58.47           C\\nANISOU  886  C   VAL A 159     6754   7353   8111    173    -97   -152       C\\nATOM    887  O   VAL A 159       7.847  17.270   3.437  1.00 64.62           O\\nANISOU  887  O   VAL A 159     7599   8038   8915    129   -128     32       O\\nATOM    888  CB  VAL A 159       7.811  15.973   6.589  1.00 61.71           C\\nANISOU  888  CB  VAL A 159     7270   7984   8194     28    136   -202       C\\nATOM    889  CG1 VAL A 159       7.571  14.812   5.641  1.00 58.85           C\\nANISOU  889  CG1 VAL A 159     6974   7622   7763    -90    212    -53       C\\nATOM    890  CG2 VAL A 159       8.840  15.593   7.634  1.00 64.69           C\\nANISOU  890  CG2 VAL A 159     7772   8351   8457     -6    154   -157       C\\nATOM    891  N   TRP A 160       6.156  17.865   4.792  1.00 55.67           N\\nANISOU  891  N   TRP A 160     6244   7112   7797    249   -122   -357       N\\nATOM    892  CA  TRP A 160       5.209  17.964   3.688  1.00 61.87           C\\nANISOU  892  CA  TRP A 160     6946   7902   8658    275   -191   -352       C\\nATOM    893  C   TRP A 160       5.414  19.222   2.854  1.00 68.14           C\\nANISOU  893  C   TRP A 160     7758   8458   9675    394   -447   -287       C\\nATOM    894  O   TRP A 160       5.155  19.201   1.645  1.00 72.46           O\\nANISOU  894  O   TRP A 160     8331   8951  10250    369   -527   -148       O\\nATOM    895  CB  TRP A 160       3.778  17.893   4.226  1.00 54.20           C\\nANISOU  895  CB  TRP A 160     5762   7176   7654    313   -130   -618       C\\nATOM    896  CG  TRP A 160       3.447  16.528   4.729  1.00 59.47           C\\nANISOU  896  CG  TRP A 160     6436   8074   8087    111    106   -599       C\\nATOM    897  CD1 TRP A 160       3.428  16.111   6.027  1.00 64.43           C\\nANISOU  897  CD1 TRP A 160     7047   8894   8538     21    258   -694       C\\nATOM    898  CD2 TRP A 160       3.129  15.380   3.933  1.00 65.48           C\\nANISOU  898  CD2 TRP A 160     7253   8873   8755    -53    190   -456       C\\nATOM    899  NE1 TRP A 160       3.105  14.776   6.089  1.00 64.83           N\\nANISOU  899  NE1 TRP A 160     7153   9080   8400   -211    420   -586       N\\nATOM    900  CE2 TRP A 160       2.917  14.305   4.817  1.00 67.13           C\\nANISOU  900  CE2 TRP A 160     7487   9263   8758   -251    374   -455       C\\nATOM    901  CE3 TRP A 160       2.997  15.161   2.558  1.00 66.76           C\\nANISOU  901  CE3 TRP A 160     7455   8935   8975    -62    110   -331       C\\nATOM    902  CZ2 TRP A 160       2.575  13.030   4.371  1.00 70.04           C\\nANISOU  902  CZ2 TRP A 160     7926   9666   9019   -454    457   -337       C\\nATOM    903  CZ3 TRP A 160       2.659  13.895   2.117  1.00 69.12           C\\nANISOU  903  CZ3 TRP A 160     7807   9302   9154   -239    209   -252       C\\nATOM    904  CH2 TRP A 160       2.451  12.846   3.021  1.00 68.25           C\\nANISOU  904  CH2 TRP A 160     7727   9325   8880   -431    370   -257       C\\nATOM    905  N   VAL A 161       5.874  20.317   3.463  1.00 67.95           N\\nANISOU  905  N   VAL A 161     7737   8280   9802    507   -599   -373       N\\nATOM    906  CA  VAL A 161       6.140  21.520   2.680  1.00 69.19           C\\nANISOU  906  CA  VAL A 161     7952   8155  10182    576   -883   -262       C\\nATOM    907  C   VAL A 161       7.379  21.323   1.823  1.00 65.64           C\\nANISOU  907  C   VAL A 161     7665   7597   9678    402   -867     76       C\\nATOM    908  O   VAL A 161       7.447  21.799   0.684  1.00 71.00           O\\nANISOU  908  O   VAL A 161     8411   8144  10420    354  -1023    278       O\\nATOM    909  CB  VAL A 161       6.273  22.747   3.599  1.00 68.92           C\\nANISOU  909  CB  VAL A 161     7883   7953  10351    740  -1087   -473       C\\nATOM    910  CG1 VAL A 161       6.754  23.958   2.810  1.00 55.10           C\\nANISOU  910  CG1 VAL A 161     6251   5845   8841    751  -1414   -291       C\\nATOM    911  CG2 VAL A 161       4.941  23.041   4.271  1.00 68.37           C\\nANISOU  911  CG2 VAL A 161     7604   8033  10340    947  -1123   -858       C\\nATOM    912  N   LEU A 162       8.370  20.607   2.346  1.00 57.34           N\\nANISOU  912  N   LEU A 162     6669   6627   8492    302   -683    137       N\\nATOM    913  CA  LEU A 162       9.567  20.343   1.562  1.00 62.34           C\\nANISOU  913  CA  LEU A 162     7399   7226   9060    152   -640    403       C\\nATOM    914  C   LEU A 162       9.274  19.375   0.424  1.00 64.44           C\\nANISOU  914  C   LEU A 162     7686   7633   9165     68   -521    527       C\\nATOM    915  O   LEU A 162       9.756  19.565  -0.698  1.00 73.70           O\\nANISOU  915  O   LEU A 162     8910   8787  10307    -32   -568    735       O\\nATOM    916  CB  LEU A 162      10.668  19.803   2.467  1.00 66.33           C\\nANISOU  916  CB  LEU A 162     7929   7786   9485    111   -507    389       C\\nATOM    917  CG  LEU A 162      12.083  19.741   1.909  1.00 71.44           C\\nANISOU  917  CG  LEU A 162     8616   8419  10108    -16   -484    596       C\\nATOM    918  CD1 LEU A 162      12.409  21.020   1.165  1.00 63.78           C\\nANISOU  918  CD1 LEU A 162     7665   7275   9293    -96   -691    765       C\\nATOM    919  CD2 LEU A 162      13.044  19.530   3.061  1.00 75.47           C\\nANISOU  919  CD2 LEU A 162     9125   8941  10610      0   -439    519       C\\nATOM    920  N   SER A 163       8.481  18.334   0.691  1.00 62.39           N\\nANISOU  920  N   SER A 163     7390   7531   8786     86   -371    399       N\\nATOM    921  CA  SER A 163       8.099  17.410  -0.371  1.00 64.81           C\\nANISOU  921  CA  SER A 163     7718   7951   8957     15   -289    475       C\\nATOM    922  C   SER A 163       7.384  18.143  -1.499  1.00 65.90           C\\nANISOU  922  C   SER A 163     7840   8039   9160     33   -467    552       C\\nATOM    923  O   SER A 163       7.634  17.874  -2.680  1.00 71.94           O\\nANISOU  923  O   SER A 163     8662   8855   9817    -51   -466    710       O\\nATOM    924  CB  SER A 163       7.213  16.302   0.193  1.00 64.78           C\\nANISOU  924  CB  SER A 163     7674   8087   8852      4   -146    321       C\\nATOM    925  OG  SER A 163       7.785  15.740   1.357  1.00 61.15           O\\nANISOU  925  OG  SER A 163     7254   7650   8329    -18    -31    269       O\\nATOM    926  N   PHE A 164       6.497  19.078  -1.153  1.00 60.59           N\\nANISOU  926  N   PHE A 164     7089   7277   8655    156   -639    427       N\\nATOM    927  CA  PHE A 164       5.825  19.887  -2.164  1.00 61.72           C\\nANISOU  927  CA  PHE A 164     7234   7322   8893    201   -880    505       C\\nATOM    928  C   PHE A 164       6.833  20.691  -2.972  1.00 65.16           C\\nANISOU  928  C   PHE A 164     7806   7601   9350     94  -1027    793       C\\nATOM    929  O   PHE A 164       6.879  20.597  -4.203  1.00 65.92           O\\nANISOU  929  O   PHE A 164     7974   7746   9327    -10  -1074    992       O\\nATOM    930  CB  PHE A 164       4.803  20.813  -1.496  1.00 57.42           C\\nANISOU  930  CB  PHE A 164     6564   6683   8568    400  -1076    267       C\\nATOM    931  CG  PHE A 164       4.135  21.779  -2.443  1.00 61.42           C\\nANISOU  931  CG  PHE A 164     7089   7023   9226    488  -1405    340       C\\nATOM    932  CD1 PHE A 164       3.067  21.374  -3.232  1.00 63.79           C\\nANISOU  932  CD1 PHE A 164     7317   7446   9476    519  -1453    302       C\\nATOM    933  CD2 PHE A 164       4.563  23.097  -2.528  1.00 60.79           C\\nANISOU  933  CD2 PHE A 164     7109   6640   9350    534  -1703    451       C\\nATOM    934  CE1 PHE A 164       2.450  22.259  -4.099  1.00 64.22           C\\nANISOU  934  CE1 PHE A 164     7400   7336   9667    615  -1799    378       C\\nATOM    935  CE2 PHE A 164       3.946  23.988  -3.393  1.00 65.28           C\\nANISOU  935  CE2 PHE A 164     7729   7008  10065    614  -2062    545       C\\nATOM    936  CZ  PHE A 164       2.889  23.566  -4.178  1.00 64.54           C\\nANISOU  936  CZ  PHE A 164     7564   7051   9906    666  -2113    510       C\\nATOM    937  N   THR A 165       7.667  21.477  -2.285  1.00 60.91           N\\nANISOU  937  N   THR A 165     7302   6899   8944     90  -1100    820       N\\nATOM    938  CA  THR A 165       8.590  22.366  -2.984  1.00 68.08           C\\nANISOU  938  CA  THR A 165     8326   7648   9893    -59  -1264   1109       C\\nATOM    939  C   THR A 165       9.585  21.592  -3.836  1.00 67.06           C\\nANISOU  939  C   THR A 165     8237   7731   9511   -266  -1055   1321       C\\nATOM    940  O   THR A 165      10.068  22.114  -4.846  1.00 74.56           O\\nANISOU  940  O   THR A 165     9269   8666  10395   -439  -1158   1596       O\\nATOM    941  CB  THR A 165       9.335  23.256  -1.988  1.00 72.21           C\\nANISOU  941  CB  THR A 165     8862   7963  10613    -43  -1373   1067       C\\nATOM    942  OG1 THR A 165      10.064  22.439  -1.068  1.00 84.36           O\\nANISOU  942  OG1 THR A 165    10343   9656  12055    -52  -1111    946       O\\nATOM    943  CG2 THR A 165       8.362  24.133  -1.215  1.00 69.54           C\\nANISOU  943  CG2 THR A 165     8475   7415  10531    191  -1616    813       C\\nATOM    944  N   ILE A 166       9.898  20.352  -3.455  1.00 69.64           N\\nANISOU  944  N   ILE A 166     8506   8267   9687   -255   -775   1193       N\\nATOM    945  CA  ILE A 166      10.825  19.548  -4.247  1.00 72.15           C\\nANISOU  945  CA  ILE A 166     8831   8805   9778   -397   -585   1317       C\\nATOM    946  C   ILE A 166      10.150  19.043  -5.520  1.00 72.60           C\\nANISOU  946  C   ILE A 166     8918   9016   9653   -435   -578   1379       C\\nATOM    947  O   ILE A 166      10.751  19.045  -6.601  1.00 74.34           O\\nANISOU  947  O   ILE A 166     9167   9388   9690   -588   -548   1564       O\\nATOM    948  CB  ILE A 166      11.383  18.389  -3.402  1.00 64.44           C\\nANISOU  948  CB  ILE A 166     7804   7945   8737   -337   -355   1141       C\\nATOM    949  CG1 ILE A 166      12.401  18.911  -2.386  1.00 65.09           C\\nANISOU  949  CG1 ILE A 166     7859   7927   8946   -345   -368   1133       C\\nATOM    950  CG2 ILE A 166      12.008  17.326  -4.294  1.00 61.90           C\\nANISOU  950  CG2 ILE A 166     7469   7861   8189   -405   -177   1168       C\\nATOM    951  CD1 ILE A 166      12.979  17.825  -1.505  1.00 55.41           C\\nANISOU  951  CD1 ILE A 166     6604   6788   7663   -276   -195    979       C\\nATOM    952  N   SER A 167       8.896  18.605  -5.414  1.00 66.08           N\\nANISOU  952  N   SER A 167     8070   8185   8852   -311   -603   1216       N\\nATOM    953  CA  SER A 167       8.168  18.066  -6.554  1.00 69.77           C\\nANISOU  953  CA  SER A 167     8557   8794   9156   -335   -616   1237       C\\nATOM    954  C   SER A 167       7.500  19.138  -7.404  1.00 70.97           C\\nANISOU  954  C   SER A 167     8769   8841   9355   -354   -900   1407       C\\nATOM    955  O   SER A 167       7.132  18.860  -8.553  1.00 69.63           O\\nANISOU  955  O   SER A 167     8642   8809   9005   -415   -942   1493       O\\nATOM    956  CB  SER A 167       7.104  17.078  -6.070  1.00 67.68           C\\nANISOU  956  CB  SER A 167     8226   8582   8907   -228   -531    989       C\\nATOM    957  OG  SER A 167       6.153  17.737  -5.251  1.00 68.82           O\\nANISOU  957  OG  SER A 167     8295   8591   9261   -104   -663    859       O\\nATOM    958  N   CYS A 168       7.324  20.345  -6.871  1.00 72.75           N\\nANISOU  958  N   CYS A 168     9009   8812   9819   -293  -1126   1446       N\\nATOM    959  CA  CYS A 168       6.648  21.393  -7.631  1.00 73.51           C\\nANISOU  959  CA  CYS A 168     9186   8743  10001   -284  -1466   1607       C\\nATOM    960  C   CYS A 168       7.347  21.747  -8.942  1.00 77.62           C\\nANISOU  960  C   CYS A 168     9848   9341  10301   -524  -1540   1966       C\\nATOM    961  O   CYS A 168       6.638  22.045  -9.918  1.00 81.68           O\\nANISOU  961  O   CYS A 168    10442   9849  10744   -540  -1760   2098       O\\nATOM    962  CB  CYS A 168       6.478  22.640  -6.754  1.00 74.94           C\\nANISOU  962  CB  CYS A 168     9371   8593  10510   -158  -1727   1556       C\\nATOM    963  SG  CYS A 168       5.411  23.906  -7.472  1.00 83.98           S\\nANISOU  963  SG  CYS A 168    10608   9450  11852    -51  -2231   1669       S\\nATOM    964  N   PRO A 169       8.683  21.755  -9.044  1.00 78.38           N\\nANISOU  964  N   PRO A 169     9970   9541  10269   -727  -1380   2136       N\\nATOM    965  CA  PRO A 169       9.296  22.005 -10.360  1.00 83.73           C\\nANISOU  965  CA  PRO A 169    10752  10394  10669   -996  -1410   2471       C\\nATOM    966  C   PRO A 169       8.894  21.001 -11.428  1.00 84.95           C\\nANISOU  966  C   PRO A 169    10900  10878  10501  -1015  -1280   2429       C\\nATOM    967  O   PRO A 169       8.857  21.362 -12.611  1.00 84.19           O\\nANISOU  967  O   PRO A 169    10915  10894  10178  -1189  -1413   2692       O\\nATOM    968  CB  PRO A 169      10.799  21.935 -10.063  1.00 82.55           C\\nANISOU  968  CB  PRO A 169    10540  10383  10443  -1178  -1179   2547       C\\nATOM    969  CG  PRO A 169      10.912  22.332  -8.645  1.00 76.42           C\\nANISOU  969  CG  PRO A 169     9712   9325   9998  -1032  -1220   2380       C\\nATOM    970  CD  PRO A 169       9.698  21.762  -7.973  1.00 74.69           C\\nANISOU  970  CD  PRO A 169     9435   9030   9916   -740  -1219   2057       C\\nATOM    971  N   LEU A 170       8.584  19.755 -11.051  1.00 79.08           N\\nANISOU  971  N   LEU A 170    10044  10281   9723   -856  -1047   2113       N\\nATOM    972  CA  LEU A 170       8.270  18.731 -12.044  1.00 73.43           C\\nANISOU  972  CA  LEU A 170     9322   9863   8714   -871   -932   2033       C\\nATOM    973  C   LEU A 170       7.035  19.090 -12.860  1.00 76.56           C\\nANISOU  973  C   LEU A 170     9801  10208   9081   -835  -1215   2109       C\\nATOM    974  O   LEU A 170       6.917  18.677 -14.020  1.00 77.86           O\\nANISOU  974  O   LEU A 170    10015  10626   8942   -927  -1211   2171       O\\nATOM    975  CB  LEU A 170       8.080  17.380 -11.356  1.00 67.28           C\\nANISOU  975  CB  LEU A 170     8435   9155   7972   -710   -697   1684       C\\nATOM    976  CG  LEU A 170       9.176  16.975 -10.366  1.00 66.79           C\\nANISOU  976  CG  LEU A 170     8297   9091   7988   -692   -470   1577       C\\nATOM    977  CD1 LEU A 170       8.737  15.773  -9.563  1.00 66.74           C\\nANISOU  977  CD1 LEU A 170     8235   9057   8068   -536   -332   1276       C\\nATOM    978  CD2 LEU A 170      10.488  16.689 -11.074  1.00 61.58           C\\nANISOU  978  CD2 LEU A 170     7607   8724   7065   -840   -287   1659       C\\nATOM    979  N   LEU A 171       6.108  19.856 -12.280  1.00 72.91           N\\nANISOU  979  N   LEU A 171     9340   9439   8925   -685  -1477   2076       N\\nATOM    980  CA  LEU A 171       4.945  20.322 -13.024  1.00 75.80           C\\nANISOU  980  CA  LEU A 171     9768   9727   9306   -622  -1806   2146       C\\nATOM    981  C   LEU A 171       5.311  21.339 -14.094  1.00 79.71           C\\nANISOU  981  C   LEU A 171    10460  10190   9637   -830  -2066   2561       C\\nATOM    982  O   LEU A 171       4.541  21.531 -15.041  1.00 84.88           O\\nANISOU  982  O   LEU A 171    11203  10874  10173   -833  -2320   2673       O\\nATOM    983  CB  LEU A 171       3.917  20.942 -12.075  1.00 74.05           C\\nANISOU  983  CB  LEU A 171     9460   9199   9478   -376  -2034   1961       C\\nATOM    984  CG  LEU A 171       2.918  20.015 -11.385  1.00 69.74           C\\nANISOU  984  CG  LEU A 171     8717   8733   9050   -185  -1900   1574       C\\nATOM    985  CD1 LEU A 171       2.056  20.807 -10.416  1.00 68.86           C\\nANISOU  985  CD1 LEU A 171     8486   8373   9305     44  -2112   1385       C\\nATOM    986  CD2 LEU A 171       2.059  19.311 -12.420  1.00 65.45           C\\nANISOU  986  CD2 LEU A 171     8160   8395   8313   -188  -1959   1520       C\\nATOM    987  N   PHE A 172       6.460  21.995 -13.967  1.00 68.04           N\\nANISOU  987  N   PHE A 172     9054   8656   8140  -1028  -2027   2807       N\\nATOM    988  CA  PHE A 172       6.795  23.074 -14.882  1.00 78.77           C\\nANISOU  988  CA  PHE A 172    10620   9942   9366  -1280  -2310   3252       C\\nATOM    989  C   PHE A 172       8.096  22.777 -15.619  1.00 85.91           C\\nANISOU  989  C   PHE A 172    11542  11237   9862  -1615  -2028   3473       C\\nATOM    990  O   PHE A 172       9.011  23.607 -15.641  1.00 88.20           O\\nANISOU  990  O   PHE A 172    11911  11460  10141  -1873  -2078   3779       O\\nATOM    991  CB  PHE A 172       6.876  24.399 -14.118  1.00 84.73           C\\nANISOU  991  CB  PHE A 172    11461  10224  10509  -1254  -2621   3391       C\\nATOM    992  CG  PHE A 172       5.617  24.738 -13.360  1.00 85.93           C\\nANISOU  992  CG  PHE A 172    11551  10035  11063   -893  -2895   3113       C\\nATOM    993  CD1 PHE A 172       4.602  25.461 -13.964  1.00 86.94           C\\nANISOU  993  CD1 PHE A 172    11803   9937  11293   -793  -3356   3232       C\\nATOM    994  CD2 PHE A 172       5.447  24.323 -12.046  1.00 83.56           C\\nANISOU  994  CD2 PHE A 172    11054   9673  11022   -654  -2699   2721       C\\nATOM    995  CE1 PHE A 172       3.443  25.769 -13.275  1.00 83.30           C\\nANISOU  995  CE1 PHE A 172    11232   9212  11208   -436  -3605   2923       C\\nATOM    996  CE2 PHE A 172       4.288  24.629 -11.350  1.00 82.96           C\\nANISOU  996  CE2 PHE A 172    10876   9366  11280   -334  -2919   2431       C\\nATOM    997  CZ  PHE A 172       3.286  25.353 -11.967  1.00 83.10           C\\nANISOU  997  CZ  PHE A 172    10978   9179  11417   -212  -3367   2511       C\\nATOM    998  N   GLY A 173       8.179  21.592 -16.224  1.00 92.00           N\\nANISOU  998  N   GLY A 173    12224  12431  10302  -1618  -1741   3296       N\\nATOM    999  CA  GLY A 173       9.333  21.223 -17.023  1.00 99.29           C\\nANISOU  999  CA  GLY A 173    13120  13810  10797  -1900  -1463   3431       C\\nATOM   1000  C   GLY A 173      10.629  21.114 -16.255  1.00105.40           C\\nANISOU 1000  C   GLY A 173    13746  14661  11642  -1983  -1167   3370       C\\nATOM   1001  O   GLY A 173      11.703  21.225 -16.853  1.00109.34           O\\nANISOU 1001  O   GLY A 173    14209  15498  11836  -2275   -998   3563       O\\nATOM   1002  N   LEU A 174      10.558  20.899 -14.940  1.00100.46           N\\nANISOU 1002  N   LEU A 174    13015  13761  11393  -1742  -1102   3100       N\\nATOM   1003  CA  LEU A 174      11.734  20.873 -14.068  1.00103.35           C\\nANISOU 1003  CA  LEU A 174    13246  14141  11880  -1788   -879   3034       C\\nATOM   1004  C   LEU A 174      12.539  22.163 -14.183  1.00110.64           C\\nANISOU 1004  C   LEU A 174    14250  14960  12828  -2107  -1028   3434       C\\nATOM   1005  O   LEU A 174      13.746  22.179 -13.930  1.00113.38           O\\nANISOU 1005  O   LEU A 174    14470  15481  13128  -2273   -823   3467       O\\nATOM   1006  CB  LEU A 174      12.615  19.654 -14.361  1.00 97.67           C\\nANISOU 1006  CB  LEU A 174    12350  13885  10875  -1796   -492   2806       C\\nATOM   1007  CG  LEU A 174      13.534  19.118 -13.264  1.00 92.37           C\\nANISOU 1007  CG  LEU A 174    11502  13215  10381  -1682   -254   2560       C\\nATOM   1008  CD1 LEU A 174      12.928  19.339 -11.890  1.00 88.80           C\\nANISOU 1008  CD1 LEU A 174    11078  12307  10354  -1450   -387   2419       C\\nATOM   1009  CD2 LEU A 174      13.792  17.638 -13.505  1.00 90.06           C\\nANISOU 1009  CD2 LEU A 174    11076  13252   9891  -1525     22   2210       C\\nATOM   1010  N   ASN A 175      11.863  23.254 -14.556  1.00127.08           N\\nANISOU 1010  N   ASN A 175    16542  16739  15004  -2196  -1417   3738       N\\nATOM   1011  CA  ASN A 175      12.511  24.539 -14.814  1.00131.09           C\\nANISOU 1011  CA  ASN A 175    17185  17092  15530  -2547  -1637   4178       C\\nATOM   1012  C   ASN A 175      13.737  24.358 -15.706  1.00135.52           C\\nANISOU 1012  C   ASN A 175    17627  18169  15696  -2875  -1339   4267       C\\nATOM   1013  O   ASN A 175      14.777  24.991 -15.516  1.00141.49           O\\nANISOU 1013  O   ASN A 175    18317  18930  16514  -3096  -1295   4368       O\\nATOM   1014  CB  ASN A 175      12.876  25.244 -13.504  1.00127.19           C\\nANISOU 1014  CB  ASN A 175    16665  16177  15484  -2475  -1748   4122       C\\nATOM   1015  CG  ASN A 175      11.656  25.790 -12.774  1.00121.37           C\\nANISOU 1015  CG  ASN A 175    16035  14913  15169  -2144  -2109   3974       C\\nATOM   1016  OD1 ASN A 175      10.689  26.228 -13.400  1.00120.30           O\\nANISOU 1016  OD1 ASN A 175    16064  14605  15041  -2092  -2430   4105       O\\nATOM   1017  ND2 ASN A 175      11.697  25.764 -11.445  1.00115.08           N\\nANISOU 1017  ND2 ASN A 175    15127  13886  14713  -1906  -2061   3672       N\\nATOM   1018  N   ASN A 176      13.611  23.469 -16.686  1.00138.51           N\\nANISOU 1018  N   ASN A 176    17960  19005  15662  -2893  -1141   4194       N\\nATOM   1019  CA  ASN A 176      14.702  23.139 -17.593  1.00128.90           C\\nANISOU 1019  CA  ASN A 176    16590  18346  14041  -3148   -837   4194       C\\nATOM   1020  C   ASN A 176      14.143  23.135 -19.012  1.00130.29           C\\nANISOU 1020  C   ASN A 176    16893  18756  13854  -3256   -934   4312       C\\nATOM   1021  O   ASN A 176      13.054  23.656 -19.280  1.00128.25           O\\nANISOU 1021  O   ASN A 176    16856  18174  13701  -3186  -1280   4456       O\\nATOM   1022  CB  ASN A 176      15.347  21.804 -17.188  1.00114.40           C\\nANISOU 1022  CB  ASN A 176    14490  16909  12066  -3004   -416   3849       C\\nATOM   1023  N   ALA A 177      14.888  22.541 -19.940  1.00131.35           N\\nANISOU 1023  N   ALA A 177    16876  19466  13564  -3410   -639   4223       N\\nATOM   1024  CA  ALA A 177      14.518  22.512 -21.354  1.00133.06           C\\nANISOU 1024  CA  ALA A 177    17193  19978  13388  -3547   -695   4324       C\\nATOM   1025  C   ALA A 177      13.850  21.175 -21.665  1.00139.43           C\\nANISOU 1025  C   ALA A 177    17953  21060  13966  -3279   -543   3999       C\\nATOM   1026  O   ALA A 177      14.499  20.218 -22.087  1.00134.42           O\\nANISOU 1026  O   ALA A 177    17113  20932  13028  -3260   -210   3722       O\\nATOM   1027  CB  ALA A 177      15.744  22.740 -22.230  1.00132.82           C\\nANISOU 1027  CB  ALA A 177    17018  20431  13018  -3895   -487   4415       C\\nATOM   1028  N   ASP A 178      12.535  21.113 -21.456  1.00139.56           N\\nANISOU 1028  N   ASP A 178    18147  20737  14141  -3057   -814   4002       N\\nATOM   1029  CA  ASP A 178      11.738  19.985 -21.927  1.00140.00           C\\nANISOU 1029  CA  ASP A 178    18203  21034  13957  -2843   -761   3735       C\\nATOM   1030  C   ASP A 178      10.328  20.465 -22.235  1.00139.46           C\\nANISOU 1030  C   ASP A 178    18375  20618  13994  -2746  -1185   3897       C\\nATOM   1031  O   ASP A 178       9.372  20.082 -21.554  1.00142.64           O\\nANISOU 1031  O   ASP A 178    18808  20766  14622  -2479  -1336   3761       O\\nATOM   1032  CB  ASP A 178      11.711  18.857 -20.894  1.00137.06           C\\nANISOU 1032  CB  ASP A 178    17675  20675  13728  -2556   -547   3368       C\\nATOM   1033  N   GLN A 179      10.191  21.295 -23.270  1.00143.02           N\\nANISOU 1033  N   GLN A 179    18983  21074  14284  -2960  -1392   4178       N\\nATOM   1034  CA  GLN A 179       8.987  22.105 -23.424  1.00133.33           C\\nANISOU 1034  CA  GLN A 179    17987  19403  13269  -2879  -1859   4383       C\\nATOM   1035  C   GLN A 179       7.753  21.243 -23.675  1.00128.51           C\\nANISOU 1035  C   GLN A 179    17406  18844  12578  -2605  -1987   4153       C\\nATOM   1036  O   GLN A 179       6.787  21.279 -22.902  1.00124.40           O\\nANISOU 1036  O   GLN A 179    16911  17946  12410  -2345  -2237   4071       O\\nATOM   1037  CB  GLN A 179       9.188  23.117 -24.553  1.00132.56           C\\nANISOU 1037  CB  GLN A 179    18056  19342  12970  -3191  -2041   4737       C\\nATOM   1038  N   ASN A 180       7.766  20.455 -24.749  1.00126.77           N\\nANISOU 1038  N   ASN A 180    17160  19104  11903  -2656  -1831   4014       N\\nATOM   1039  CA  ASN A 180       6.565  19.780 -25.230  1.00115.92           C\\nANISOU 1039  CA  ASN A 180    15839  17790  10414  -2448  -2017   3825       C\\nATOM   1040  C   ASN A 180       6.535  18.292 -24.886  1.00111.57           C\\nANISOU 1040  C   ASN A 180    15109  17542   9741  -2253  -1745   3379       C\\nATOM   1041  O   ASN A 180       5.949  17.498 -25.625  1.00103.18           O\\nANISOU 1041  O   ASN A 180    14050  16740   8415  -2166  -1771   3154       O\\nATOM   1042  CB  ASN A 180       6.419  19.972 -26.739  1.00115.56           C\\nANISOU 1042  CB  ASN A 180    15926  18028   9952  -2620  -2110   3964       C\\nATOM   1043  N   GLU A 181       7.135  17.896 -23.764  1.00104.62           N\\nANISOU 1043  N   GLU A 181    14065  16578   9107  -2156  -1490   3195       N\\nATOM   1044  CA  GLU A 181       7.136  16.494 -23.369  1.00106.80           C\\nANISOU 1044  CA  GLU A 181    14149  16965   9465  -1902  -1204   2656       C\\nATOM   1045  C   GLU A 181       6.948  16.366 -21.867  1.00100.72           C\\nANISOU 1045  C   GLU A 181    13266  15721   9281  -1661  -1157   2456       C\\nATOM   1046  O   GLU A 181       7.211  17.295 -21.099  1.00102.83           O\\nANISOU 1046  O   GLU A 181    13557  15677   9838  -1708  -1233   2688       O\\nATOM   1047  CB  GLU A 181       8.426  15.780 -23.782  1.00111.20           C\\nANISOU 1047  CB  GLU A 181    14562  18052   9639  -2014   -799   2478       C\\nATOM   1048  CG  GLU A 181       8.455  15.363 -25.237  1.00118.18           C\\nANISOU 1048  CG  GLU A 181    15491  19499   9912  -2150   -768   2439       C\\nATOM   1049  CD  GLU A 181       9.558  14.373 -25.529  1.00125.80           C\\nANISOU 1049  CD  GLU A 181    16244  20936  10620  -2119   -359   2054       C\\nATOM   1050  OE1 GLU A 181       9.649  13.356 -24.809  1.00127.00           O\\nANISOU 1050  OE1 GLU A 181    16258  20997  10999  -1858   -200   1630       O\\nATOM   1051  OE2 GLU A 181      10.339  14.618 -26.473  1.00132.18           O\\nANISOU 1051  OE2 GLU A 181    16999  22090  11133  -2311   -210   2123       O\\nATOM   1052  N   CYS A 182       6.490  15.185 -21.461  1.00 85.77           N\\nANISOU 1052  N   CYS A 182    11262  13784   7544  -1421  -1042   2020       N\\nATOM   1053  CA  CYS A 182       6.326  14.886 -20.051  1.00 85.01           C\\nANISOU 1053  CA  CYS A 182    11057  13309   7934  -1219   -963   1809       C\\nATOM   1054  C   CYS A 182       7.659  15.034 -19.325  1.00 85.25           C\\nANISOU 1054  C   CYS A 182    10998  13354   8038  -1280   -699   1848       C\\nATOM   1055  O   CYS A 182       8.737  14.991 -19.927  1.00 87.66           O\\nANISOU 1055  O   CYS A 182    11266  14030   8011  -1441   -506   1910       O\\nATOM   1056  CB  CYS A 182       5.770  13.473 -19.864  1.00 85.07           C\\nANISOU 1056  CB  CYS A 182    10980  13320   8021  -1022   -869   1364       C\\nATOM   1057  SG  CYS A 182       5.430  13.056 -18.147  1.00 88.55           S\\nANISOU 1057  SG  CYS A 182    11313  13325   9006   -826   -793   1143       S\\nATOM   1058  N   ILE A 183       7.575  15.222 -18.009  1.00 86.69           N\\nANISOU 1058  N   ILE A 183    11127  13162   8650  -1153   -694   1796       N\\nATOM   1059  CA  ILE A 183       8.782  15.505 -17.243  1.00 88.06           C\\nANISOU 1059  CA  ILE A 183    11221  13307   8931  -1209   -498   1856       C\\nATOM   1060  C   ILE A 183       9.631  14.253 -17.070  1.00 90.76           C\\nANISOU 1060  C   ILE A 183    11430  13873   9183  -1113   -193   1518       C\\nATOM   1061  O   ILE A 183      10.856  14.349 -16.944  1.00 89.70           O\\nANISOU 1061  O   ILE A 183    11199  13916   8966  -1199     -1   1550       O\\nATOM   1062  CB  ILE A 183       8.428  16.141 -15.888  1.00 82.65           C\\nANISOU 1062  CB  ILE A 183    10529  12169   8706  -1098   -610   1893       C\\nATOM   1063  CG1 ILE A 183       9.689  16.703 -15.236  1.00 81.90           C\\nANISOU 1063  CG1 ILE A 183    10377  12044   8696  -1203   -475   2026       C\\nATOM   1064  CG2 ILE A 183       7.755  15.134 -14.972  1.00 80.02           C\\nANISOU 1064  CG2 ILE A 183    10121  11657   8626   -869   -543   1542       C\\nATOM   1065  CD1 ILE A 183      10.562  17.486 -16.201  1.00 77.13           C\\nANISOU 1065  CD1 ILE A 183     9815  11711   7778  -1501   -472   2363       C\\nATOM   1066  N   ILE A 184       9.020  13.066 -17.078  1.00 86.05           N\\nANISOU 1066  N   ILE A 184    10817  13266   8612   -938   -167   1182       N\\nATOM   1067  CA  ILE A 184       9.808  11.848 -16.945  1.00 81.50           C\\nANISOU 1067  CA  ILE A 184    10141  12849   7978   -818     61    843       C\\nATOM   1068  C   ILE A 184      10.649  11.603 -18.187  1.00 77.44           C\\nANISOU 1068  C   ILE A 184     9566  12848   7010   -918    205    786       C\\nATOM   1069  O   ILE A 184      11.589  10.802 -18.148  1.00 77.18           O\\nANISOU 1069  O   ILE A 184     9408  13014   6904   -822    403    514       O\\nATOM   1070  CB  ILE A 184       8.907  10.636 -16.645  1.00 80.64           C\\nANISOU 1070  CB  ILE A 184    10060  12549   8030   -635      7    515       C\\nATOM   1071  CG1 ILE A 184       9.694   9.574 -15.876  1.00 78.25           C\\nANISOU 1071  CG1 ILE A 184     9688  12171   7873   -478    168    222       C\\nATOM   1072  CG2 ILE A 184       8.346  10.052 -17.932  1.00 83.92           C\\nANISOU 1072  CG2 ILE A 184    10523  13226   8137   -643    -67    367       C\\nATOM   1073  CD1 ILE A 184       8.861   8.383 -15.456  1.00 80.33           C\\nANISOU 1073  CD1 ILE A 184    10011  12185   8326   -346     90    -54       C\\nATOM   1074  N   ALA A 185      10.335  12.279 -19.291  1.00 80.23           N\\nANISOU 1074  N   ALA A 185     9999  13442   7044  -1105     98   1028       N\\nATOM   1075  CA  ALA A 185      11.162  12.234 -20.487  1.00 83.51           C\\nANISOU 1075  CA  ALA A 185    10349  14420   6960  -1262    251   1031       C\\nATOM   1076  C   ALA A 185      12.352  13.177 -20.411  1.00 83.75           C\\nANISOU 1076  C   ALA A 185    10288  14647   6887  -1499    393   1327       C\\nATOM   1077  O   ALA A 185      13.207  13.143 -21.301  1.00 89.61           O\\nANISOU 1077  O   ALA A 185    10921  15924   7202  -1661    576   1320       O\\nATOM   1078  CB  ALA A 185      10.320  12.565 -21.723  1.00 73.89           C\\nANISOU 1078  CB  ALA A 185     9279  13403   5395  -1401     57   1201       C\\nATOM   1079  N   ASN A 186      12.425  14.011 -19.384  1.00 87.95           N\\nANISOU 1079  N   ASN A 186    10846  14788   7782  -1536    315   1567       N\\nATOM   1080  CA  ASN A 186      13.545  14.931 -19.235  1.00 90.37           C\\nANISOU 1080  CA  ASN A 186    11066  15232   8039  -1784    421   1852       C\\nATOM   1081  C   ASN A 186      14.781  14.156 -18.795  1.00 93.04           C\\nANISOU 1081  C   ASN A 186    11153  15806   8392  -1671    718   1526       C\\nATOM   1082  O   ASN A 186      14.734  13.472 -17.765  1.00 90.82           O\\nANISOU 1082  O   ASN A 186    10830  15214   8462  -1399    737   1252       O\\nATOM   1083  CB  ASN A 186      13.200  16.017 -18.220  1.00 86.22           C\\nANISOU 1083  CB  ASN A 186    10651  14175   7934  -1820    209   2150       C\\nATOM   1084  CG  ASN A 186      14.162  17.185 -18.259  1.00 89.29           C\\nANISOU 1084  CG  ASN A 186    11013  14659   8255  -2152    225   2537       C\\nATOM   1085  OD1 ASN A 186      15.380  17.008 -18.241  1.00 95.97           O\\nANISOU 1085  OD1 ASN A 186    11655  15837   8971  -2255    479   2464       O\\nATOM   1086  ND2 ASN A 186      13.616  18.393 -18.314  1.00 87.60           N\\nANISOU 1086  ND2 ASN A 186    10997  14142   8145  -2325    -71   2943       N\\nATOM   1087  N   PRO A 187      15.895  14.232 -19.527  1.00 95.07           N\\nANISOU 1087  N   PRO A 187    11229  16621   8273  -1873    941   1541       N\\nATOM   1088  CA  PRO A 187      17.095  13.486 -19.110  1.00 94.27           C\\nANISOU 1088  CA  PRO A 187    10845  16765   8209  -1726   1203   1183       C\\nATOM   1089  C   PRO A 187      17.587  13.857 -17.721  1.00 93.98           C\\nANISOU 1089  C   PRO A 187    10749  16330   8627  -1662   1185   1242       C\\nATOM   1090  O   PRO A 187      18.317  13.067 -17.109  1.00 94.56           O\\nANISOU 1090  O   PRO A 187    10638  16436   8855  -1433   1319    896       O\\nATOM   1091  CB  PRO A 187      18.127  13.845 -20.190  1.00 87.30           C\\nANISOU 1091  CB  PRO A 187     9769  16534   6867  -2026   1406   1271       C\\nATOM   1092  CG  PRO A 187      17.630  15.128 -20.784  1.00 81.91           C\\nANISOU 1092  CG  PRO A 187     9311  15710   6102  -2368   1189   1793       C\\nATOM   1093  CD  PRO A 187      16.135  15.035 -20.737  1.00 89.48           C\\nANISOU 1093  CD  PRO A 187    10552  16349   7098  -2256    952   1890       C\\nATOM   1094  N   ALA A 188      17.198  15.020 -17.198  1.00 89.90           N\\nANISOU 1094  N   ALA A 188    10393  15427   8337  -1837    994   1648       N\\nATOM   1095  CA  ALA A 188      17.621  15.462 -15.877  1.00 87.20           C\\nANISOU 1095  CA  ALA A 188    10012  14708   8411  -1788    952   1704       C\\nATOM   1096  C   ALA A 188      16.681  15.017 -14.764  1.00 83.84           C\\nANISOU 1096  C   ALA A 188     9732  13727   8396  -1473    795   1536       C\\nATOM   1097  O   ALA A 188      16.983  15.253 -13.591  1.00 75.80           O\\nANISOU 1097  O   ALA A 188     8687  12406   7707  -1395    761   1530       O\\nATOM   1098  CB  ALA A 188      17.750  16.987 -15.848  1.00 80.85           C\\nANISOU 1098  CB  ALA A 188     9302  13764   7654  -2142    804   2201       C\\nATOM   1099  N   PHE A 189      15.554  14.386 -15.094  1.00 80.92           N\\nANISOU 1099  N   PHE A 189     9504  13244   7997  -1314    698   1400       N\\nATOM   1100  CA  PHE A 189      14.640  13.936 -14.051  1.00 78.27           C\\nANISOU 1100  CA  PHE A 189     9281  12440   8018  -1065    570   1248       C\\nATOM   1101  C   PHE A 189      15.276  12.851 -13.193  1.00 80.35           C\\nANISOU 1101  C   PHE A 189     9430  12648   8450   -824    697    901       C\\nATOM   1102  O   PHE A 189      15.128  12.856 -11.964  1.00 75.11           O\\nANISOU 1102  O   PHE A 189     8806  11626   8105   -710    633    876       O\\nATOM   1103  CB  PHE A 189      13.335  13.437 -14.671  1.00 80.58           C\\nANISOU 1103  CB  PHE A 189     9715  12675   8225   -983    445   1165       C\\nATOM   1104  CG  PHE A 189      12.426  12.754 -13.693  1.00 85.91           C\\nANISOU 1104  CG  PHE A 189    10465  12965   9214   -760    358    965       C\\nATOM   1105  CD1 PHE A 189      11.690  13.490 -12.780  1.00 86.83           C\\nANISOU 1105  CD1 PHE A 189    10658  12708   9625   -749    203   1115       C\\nATOM   1106  CD2 PHE A 189      12.306  11.375 -13.683  1.00 84.50           C\\nANISOU 1106  CD2 PHE A 189    10274  12804   9028   -575    421    619       C\\nATOM   1107  CE1 PHE A 189      10.853  12.861 -11.873  1.00 82.22           C\\nANISOU 1107  CE1 PHE A 189    10115  11841   9283   -588    152    936       C\\nATOM   1108  CE2 PHE A 189      11.471  10.742 -12.779  1.00 79.97           C\\nANISOU 1108  CE2 PHE A 189     9777  11887   8720   -435    339    479       C\\nATOM   1109  CZ  PHE A 189      10.745  11.486 -11.874  1.00 75.49           C\\nANISOU 1109  CZ  PHE A 189     9262  11015   8404   -457    224    645       C\\nATOM   1110  N   VAL A 190      15.990  11.913 -13.820  1.00 82.64           N\\nANISOU 1110  N   VAL A 190     9581  13296   8524   -736    857    620       N\\nATOM   1111  CA  VAL A 190      16.608  10.825 -13.066  1.00 79.80           C\\nANISOU 1111  CA  VAL A 190     9129  12855   8338   -476    921    274       C\\nATOM   1112  C   VAL A 190      17.619  11.375 -12.070  1.00 73.96           C\\nANISOU 1112  C   VAL A 190     8263  12038   7801   -501    965    362       C\\nATOM   1113  O   VAL A 190      17.647  10.963 -10.905  1.00 69.81           O\\nANISOU 1113  O   VAL A 190     7780  11184   7561   -328    899    257       O\\nATOM   1114  CB  VAL A 190      17.246   9.799 -14.024  1.00 76.29           C\\nANISOU 1114  CB  VAL A 190     8531  12834   7621   -350   1058    -85       C\\nATOM   1115  CG1 VAL A 190      18.329   8.997 -13.321  1.00 73.98           C\\nANISOU 1115  CG1 VAL A 190     8071  12543   7496   -111   1121   -401       C\\nATOM   1116  CG2 VAL A 190      16.181   8.863 -14.570  1.00 70.22           C\\nANISOU 1116  CG2 VAL A 190     7922  11973   6787   -219    957   -292       C\\nATOM   1117  N   VAL A 191      18.449  12.327 -12.502  1.00 74.89           N\\nANISOU 1117  N   VAL A 191     8232  12459   7764   -745   1062    574       N\\nATOM   1118  CA  VAL A 191      19.440  12.910 -11.603  1.00 69.99           C\\nANISOU 1118  CA  VAL A 191     7472  11783   7337   -800   1089    659       C\\nATOM   1119  C   VAL A 191      18.756  13.666 -10.472  1.00 71.73           C\\nANISOU 1119  C   VAL A 191     7882  11494   7879   -818    904    880       C\\nATOM   1120  O   VAL A 191      19.167  13.580  -9.308  1.00 74.22           O\\nANISOU 1120  O   VAL A 191     8168  11584   8449   -696    866    802       O\\nATOM   1121  CB  VAL A 191      20.401  13.820 -12.387  1.00 69.86           C\\nANISOU 1121  CB  VAL A 191     7256  12216   7071  -1128   1224    873       C\\nATOM   1122  CG1 VAL A 191      21.588  14.210 -11.518  1.00 61.69           C\\nANISOU 1122  CG1 VAL A 191     6014  11194   6229  -1167   1269    875       C\\nATOM   1123  CG2 VAL A 191      20.860  13.135 -13.669  1.00 71.25           C\\nANISOU 1123  CG2 VAL A 191     7250  12975   6848  -1136   1419    651       C\\nATOM   1124  N   TYR A 192      17.698  14.409 -10.792  1.00 73.30           N\\nANISOU 1124  N   TYR A 192     8269  11519   8064   -952    769   1133       N\\nATOM   1125  CA  TYR A 192      17.008  15.209  -9.786  1.00 69.49           C\\nANISOU 1125  CA  TYR A 192     7937  10591   7877   -952    585   1300       C\\nATOM   1126  C   TYR A 192      16.386  14.323  -8.714  1.00 69.05           C\\nANISOU 1126  C   TYR A 192     7966  10230   8040   -683    540   1063       C\\nATOM   1127  O   TYR A 192      16.743  14.407  -7.534  1.00 70.50           O\\nANISOU 1127  O   TYR A 192     8135  10210   8443   -602    510   1018       O\\nATOM   1128  CB  TYR A 192      15.946  16.079 -10.460  1.00 70.53           C\\nANISOU 1128  CB  TYR A 192     8235  10616   7948  -1102    419   1566       C\\nATOM   1129  CG  TYR A 192      15.223  17.022  -9.524  1.00 71.79           C\\nANISOU 1129  CG  TYR A 192     8522  10343   8412  -1083    204   1704       C\\nATOM   1130  CD1 TYR A 192      15.814  18.212  -9.114  1.00 72.52           C\\nANISOU 1130  CD1 TYR A 192     8604  10305   8647  -1251    105   1926       C\\nATOM   1131  CD2 TYR A 192      13.943  16.733  -9.066  1.00 75.40           C\\nANISOU 1131  CD2 TYR A 192     9093  10543   9014   -904     92   1589       C\\nATOM   1132  CE1 TYR A 192      15.157  19.082  -8.265  1.00 72.60           C\\nANISOU 1132  CE1 TYR A 192     8724   9917   8942  -1200   -114   1996       C\\nATOM   1133  CE2 TYR A 192      13.275  17.600  -8.217  1.00 78.40           C\\nANISOU 1133  CE2 TYR A 192     9549  10580   9658   -860    -96   1656       C\\nATOM   1134  CZ  TYR A 192      13.887  18.772  -7.820  1.00 72.16           C\\nANISOU 1134  CZ  TYR A 192     8758   9648   9013   -988   -206   1843       C\\nATOM   1135  OH  TYR A 192      13.226  19.632  -6.973  1.00 63.34           O\\nANISOU 1135  OH  TYR A 192     7711   8188   8168   -909   -415   1853       O\\nATOM   1136  N   SER A 193      15.457  13.449  -9.114  1.00 72.61           N\\nANISOU 1136  N   SER A 193     8511  10659   8417   -566    526    916       N\\nATOM   1137  CA  SER A 193      14.715  12.654  -8.139  1.00 77.34           C\\nANISOU 1137  CA  SER A 193     9213  10968   9205   -382    469    746       C\\nATOM   1138  C   SER A 193      15.615  11.681  -7.386  1.00 75.22           C\\nANISOU 1138  C   SER A 193     8884  10678   9019   -217    535    524       C\\nATOM   1139  O   SER A 193      15.294  11.286  -6.260  1.00 76.80           O\\nANISOU 1139  O   SER A 193     9170  10614   9397   -116    473    460       O\\nATOM   1140  CB  SER A 193      13.580  11.897  -8.830  1.00 79.11           C\\nANISOU 1140  CB  SER A 193     9536  11195   9327   -336    430    640       C\\nATOM   1141  OG  SER A 193      14.075  10.934  -9.741  1.00 69.99           O\\nANISOU 1141  OG  SER A 193     8324  10300   7968   -274    524    442       O\\nATOM   1142  N   SER A 194      16.739  11.283  -7.980  1.00 71.25           N\\nANISOU 1142  N   SER A 194     8226  10467   8381   -186    646    398       N\\nATOM   1143  CA  SER A 194      17.664  10.407  -7.271  1.00 72.26           C\\nANISOU 1143  CA  SER A 194     8279  10561   8614      6    663    171       C\\nATOM   1144  C   SER A 194      18.401  11.166  -6.177  1.00 76.18           C\\nANISOU 1144  C   SER A 194     8709  10947   9290    -29    635    286       C\\nATOM   1145  O   SER A 194      18.423  10.741  -5.014  1.00 72.02           O\\nANISOU 1145  O   SER A 194     8263  10164   8939     99    550    218       O\\nATOM   1146  CB  SER A 194      18.661   9.784  -8.246  1.00 72.31           C\\nANISOU 1146  CB  SER A 194     8087  10955   8432     84    784    -57       C\\nATOM   1147  OG  SER A 194      17.998   9.092  -9.286  1.00 80.43           O\\nANISOU 1147  OG  SER A 194     9180  12101   9277    122    797   -194       O\\nATOM   1148  N   ILE A 195      19.005  12.300  -6.530  1.00 77.08           N\\nANISOU 1148  N   ILE A 195     8687  11249   9349   -226    688    474       N\\nATOM   1149  CA  ILE A 195      19.847  13.021  -5.580  1.00 70.51           C\\nANISOU 1149  CA  ILE A 195     7763  10342   8685   -272    652    555       C\\nATOM   1150  C   ILE A 195      18.988  13.748  -4.552  1.00 66.52           C\\nANISOU 1150  C   ILE A 195     7438   9466   8370   -304    511    708       C\\nATOM   1151  O   ILE A 195      19.129  13.541  -3.341  1.00 74.63           O\\nANISOU 1151  O   ILE A 195     8511  10286   9557   -186    438    633       O\\nATOM   1152  CB  ILE A 195      20.787  13.987  -6.321  1.00 68.49           C\\nANISOU 1152  CB  ILE A 195     7299  10412   8313   -520    744    715       C\\nATOM   1153  CG1 ILE A 195      21.784  13.200  -7.177  1.00 66.22           C\\nANISOU 1153  CG1 ILE A 195     6764  10568   7828   -459    911    488       C\\nATOM   1154  CG2 ILE A 195      21.510  14.892  -5.337  1.00 63.89           C\\nANISOU 1154  CG2 ILE A 195     6643   9700   7932   -613    668    829       C\\nATOM   1155  CD1 ILE A 195      22.738  14.064  -7.971  1.00 56.97           C\\nANISOU 1155  CD1 ILE A 195     5348   9813   6484   -752   1041    642       C\\nATOM   1156  N   VAL A 196      18.073  14.597  -5.019  1.00 62.66           N\\nANISOU 1156  N   VAL A 196     7052   8902   7854   -450    454    905       N\\nATOM   1157  CA  VAL A 196      17.332  15.463  -4.105  1.00 67.97           C\\nANISOU 1157  CA  VAL A 196     7847   9264   8715   -469    309   1012       C\\nATOM   1158  C   VAL A 196      16.343  14.656  -3.269  1.00 67.07           C\\nANISOU 1158  C   VAL A 196     7868   8944   8670   -296    275    861       C\\nATOM   1159  O   VAL A 196      16.268  14.814  -2.046  1.00 61.49           O\\nANISOU 1159  O   VAL A 196     7206   8054   8102   -231    210    818       O\\nATOM   1160  CB  VAL A 196      16.626  16.582  -4.888  1.00 64.23           C\\nANISOU 1160  CB  VAL A 196     7440   8750   8216   -643    212   1244       C\\nATOM   1161  CG1 VAL A 196      15.849  17.474  -3.945  1.00 52.97           C\\nANISOU 1161  CG1 VAL A 196     6116   7001   7009   -610     37   1287       C\\nATOM   1162  CG2 VAL A 196      17.638  17.392  -5.674  1.00 71.96           C\\nANISOU 1162  CG2 VAL A 196     8304   9935   9102   -883    238   1445       C\\nATOM   1163  N   SER A 197      15.571  13.778  -3.911  1.00 68.31           N\\nANISOU 1163  N   SER A 197     8091   9151   8712   -244    315    780       N\\nATOM   1164  CA  SER A 197      14.505  13.073  -3.211  1.00 64.29           C\\nANISOU 1164  CA  SER A 197     7706   8466   8256   -150    280    676       C\\nATOM   1165  C   SER A 197      14.986  11.839  -2.460  1.00 64.86           C\\nANISOU 1165  C   SER A 197     7819   8478   8346    -22    301    516       C\\nATOM   1166  O   SER A 197      14.304  11.401  -1.528  1.00 71.84           O\\nANISOU 1166  O   SER A 197     8812   9202   9284      7    262    476       O\\nATOM   1167  CB  SER A 197      13.401  12.668  -4.191  1.00 64.34           C\\nANISOU 1167  CB  SER A 197     7768   8525   8155   -175    281    661       C\\nATOM   1168  OG  SER A 197      12.416  13.677  -4.297  1.00 65.40           O\\nANISOU 1168  OG  SER A 197     7921   8583   8345   -241    188    775       O\\nATOM   1169  N   PHE A 198      16.134  11.265  -2.824  1.00 56.65           N\\nANISOU 1169  N   PHE A 198     6693   7571   7259     50    348    422       N\\nATOM   1170  CA  PHE A 198      16.563  10.006  -2.225  1.00 61.84           C\\nANISOU 1170  CA  PHE A 198     7413   8131   7953    205    308    258       C\\nATOM   1171  C   PHE A 198      17.951  10.080  -1.597  1.00 66.94           C\\nANISOU 1171  C   PHE A 198     7945   8814   8677    293    283    207       C\\nATOM   1172  O   PHE A 198      18.076   9.853  -0.391  1.00 63.30           O\\nANISOU 1172  O   PHE A 198     7574   8170   8306    352    191    202       O\\nATOM   1173  CB  PHE A 198      16.518   8.887  -3.269  1.00 62.27           C\\nANISOU 1173  CB  PHE A 198     7477   8279   7904    290    331     91       C\\nATOM   1174  CG  PHE A 198      16.836   7.525  -2.714  1.00 71.87           C\\nANISOU 1174  CG  PHE A 198     8800   9318   9188    461    226    -82       C\\nATOM   1175  CD1 PHE A 198      15.889   6.822  -1.986  1.00 73.26           C\\nANISOU 1175  CD1 PHE A 198     9194   9229   9414    432    130    -54       C\\nATOM   1176  CD2 PHE A 198      18.074   6.944  -2.927  1.00 66.14           C\\nANISOU 1176  CD2 PHE A 198     7955   8695   8481    641    204   -273       C\\nATOM   1177  CE1 PHE A 198      16.173   5.566  -1.481  1.00 70.07           C\\nANISOU 1177  CE1 PHE A 198     8932   8611   9079    560    -15   -171       C\\nATOM   1178  CE2 PHE A 198      18.365   5.687  -2.423  1.00 70.55           C\\nANISOU 1178  CE2 PHE A 198     8637   9036   9134    826     45   -436       C\\nATOM   1179  CZ  PHE A 198      17.412   4.997  -1.700  1.00 69.64           C\\nANISOU 1179  CZ  PHE A 198     8787   8602   9070    775    -79   -363       C\\nATOM   1180  N   TYR A 199      18.996  10.380  -2.373  1.00 67.17           N\\nANISOU 1180  N   TYR A 199     7766   9103   8654    290    360    166       N\\nATOM   1181  CA  TYR A 199      20.356  10.230  -1.861  1.00 67.05           C\\nANISOU 1181  CA  TYR A 199     7598   9159   8719    402    329     58       C\\nATOM   1182  C   TYR A 199      20.656  11.224  -0.746  1.00 67.17           C\\nANISOU 1182  C   TYR A 199     7604   9058   8859    323    261    193       C\\nATOM   1183  O   TYR A 199      21.379  10.897   0.202  1.00 60.26           O\\nANISOU 1183  O   TYR A 199     6716   8098   8082    445    161    112       O\\nATOM   1184  CB  TYR A 199      21.367  10.375  -2.997  1.00 71.88           C\\nANISOU 1184  CB  TYR A 199     7935  10155   9221    380    457    -32       C\\nATOM   1185  CG  TYR A 199      21.372   9.197  -3.942  1.00 81.30           C\\nANISOU 1185  CG  TYR A 199     9102  11489  10299    540    498   -275       C\\nATOM   1186  CD1 TYR A 199      21.185   7.907  -3.469  1.00 86.13           C\\nANISOU 1186  CD1 TYR A 199     9871  11856  10998    769    359   -463       C\\nATOM   1187  CD2 TYR A 199      21.545   9.374  -5.307  1.00 83.10           C\\nANISOU 1187  CD2 TYR A 199     9165  12088  10320    449    652   -315       C\\nATOM   1188  CE1 TYR A 199      21.177   6.825  -4.325  1.00 85.63           C\\nANISOU 1188  CE1 TYR A 199     9799  11878  10859    933    355   -719       C\\nATOM   1189  CE2 TYR A 199      21.538   8.297  -6.171  1.00 80.51           C\\nANISOU 1189  CE2 TYR A 199     8809  11905   9875    615    680   -585       C\\nATOM   1190  CZ  TYR A 199      21.352   7.026  -5.674  1.00 76.43           C\\nANISOU 1190  CZ  TYR A 199     8448  11104   9487    871    522   -803       C\\nATOM   1191  OH  TYR A 199      21.344   5.950  -6.531  1.00 69.70           O\\nANISOU 1191  OH  TYR A 199     7579  10355   8547   1053    510  -1106       O\\nATOM   1192  N   VAL A 200      20.116  12.435  -0.831  1.00 65.74           N\\nANISOU 1192  N   VAL A 200     7439   8856   8685    133    281    383       N\\nATOM   1193  CA  VAL A 200      20.375  13.434   0.206  1.00 71.58           C\\nANISOU 1193  CA  VAL A 200     8173   9468   9555     66    193    476       C\\nATOM   1194  C   VAL A 200      19.616  13.076   1.483  1.00 70.25           C\\nANISOU 1194  C   VAL A 200     8210   9046   9435    156     95    445       C\\nATOM   1195  O   VAL A 200      20.203  13.156   2.571  1.00 66.48           O\\nANISOU 1195  O   VAL A 200     7736   8490   9035    213      0    407       O\\nATOM   1196  CB  VAL A 200      20.038  14.854  -0.281  1.00 71.46           C\\nANISOU 1196  CB  VAL A 200     8129   9461   9562   -148    192    671       C\\nATOM   1197  CG1 VAL A 200      20.109  15.848   0.873  1.00 70.31           C\\nANISOU 1197  CG1 VAL A 200     8017   9123   9575   -187     60    720       C\\nATOM   1198  CG2 VAL A 200      20.992  15.264  -1.393  1.00 67.72           C\\nANISOU 1198  CG2 VAL A 200     7444   9277   9011   -300    285    742       C\\nATOM   1199  N   PRO A 201      18.333  12.691   1.432  1.00 68.63           N\\nANISOU 1199  N   PRO A 201     8167   8739   9171    150    111    459       N\\nATOM   1200  CA  PRO A 201      17.717  12.147   2.655  1.00 67.01           C\\nANISOU 1200  CA  PRO A 201     8135   8363   8962    204     43    424       C\\nATOM   1201  C   PRO A 201      18.416  10.898   3.166  1.00 63.12           C\\nANISOU 1201  C   PRO A 201     7712   7811   8461    342    -32    331       C\\nATOM   1202  O   PRO A 201      18.541  10.711   4.383  1.00 64.72           O\\nANISOU 1202  O   PRO A 201     8019   7903   8669    376   -131    332       O\\nATOM   1203  CB  PRO A 201      16.275  11.860   2.217  1.00 66.92           C\\nANISOU 1203  CB  PRO A 201     8227   8319   8879    142     97    446       C\\nATOM   1204  CG  PRO A 201      16.022  12.833   1.137  1.00 66.63           C\\nANISOU 1204  CG  PRO A 201     8086   8379   8852     55    144    523       C\\nATOM   1205  CD  PRO A 201      17.319  12.916   0.383  1.00 66.70           C\\nANISOU 1205  CD  PRO A 201     7946   8542   8857     61    178    525       C\\nATOM   1206  N   PHE A 202      18.884  10.041   2.258  1.00 56.10           N\\nANISOU 1206  N   PHE A 202     6771   6992   7551    435    -11    238       N\\nATOM   1207  CA  PHE A 202      19.593   8.829   2.655  1.00 63.87           C\\nANISOU 1207  CA  PHE A 202     7821   7882   8566    610   -137    119       C\\nATOM   1208  C   PHE A 202      20.816   9.156   3.509  1.00 70.36           C\\nANISOU 1208  C   PHE A 202     8539   8718   9475    697   -242     86       C\\nATOM   1209  O   PHE A 202      20.977   8.621   4.613  1.00 72.54           O\\nANISOU 1209  O   PHE A 202     8969   8826   9768    771   -400     91       O\\nATOM   1210  CB  PHE A 202      19.992   8.047   1.402  1.00 62.85           C\\nANISOU 1210  CB  PHE A 202     7591   7872   8416    726    -97    -41       C\\nATOM   1211  CG  PHE A 202      20.499   6.659   1.671  1.00 70.17           C\\nANISOU 1211  CG  PHE A 202     8620   8639   9403    941   -273   -200       C\\nATOM   1212  CD1 PHE A 202      20.468   6.114   2.942  1.00 73.47           C\\nANISOU 1212  CD1 PHE A 202     9254   8795   9864    982   -462   -139       C\\nATOM   1213  CD2 PHE A 202      21.014   5.899   0.638  1.00 76.10           C\\nANISOU 1213  CD2 PHE A 202     9257   9501  10156   1108   -271   -423       C\\nATOM   1214  CE1 PHE A 202      20.939   4.847   3.177  1.00 78.88           C\\nANISOU 1214  CE1 PHE A 202    10067   9279  10625   1182   -682   -264       C\\nATOM   1215  CE2 PHE A 202      21.485   4.628   0.866  1.00 75.62           C\\nANISOU 1215  CE2 PHE A 202     9296   9248  10187   1343   -483   -603       C\\nATOM   1216  CZ  PHE A 202      21.447   4.100   2.137  1.00 79.28           C\\nANISOU 1216  CZ  PHE A 202    10003   9395  10724   1380   -707   -507       C\\nATOM   1217  N   ILE A 203      21.692  10.031   3.011  1.00 69.89           N\\nANISOU 1217  N   ILE A 203     8223   8871   9462    667   -169     66       N\\nATOM   1218  CA  ILE A 203      22.931  10.333   3.726  1.00 70.07           C\\nANISOU 1218  CA  ILE A 203     8101   8940   9583    743   -275      9       C\\nATOM   1219  C   ILE A 203      22.628  10.977   5.074  1.00 68.51           C\\nANISOU 1219  C   ILE A 203     8043   8585   9403    671   -375    114       C\\nATOM   1220  O   ILE A 203      23.185  10.584   6.106  1.00 61.96           O\\nANISOU 1220  O   ILE A 203     7279   7659   8605    783   -545     72       O\\nATOM   1221  CB  ILE A 203      23.843  11.227   2.870  1.00 67.00           C\\nANISOU 1221  CB  ILE A 203     7390   8840   9226    648   -158     -7       C\\nATOM   1222  CG1 ILE A 203      24.189  10.534   1.555  1.00 68.52           C\\nANISOU 1222  CG1 ILE A 203     7420   9264   9349    728    -43   -152       C\\nATOM   1223  CG2 ILE A 203      25.111  11.566   3.623  1.00 62.39           C\\nANISOU 1223  CG2 ILE A 203     6625   8319   8761    704   -276    -75       C\\nATOM   1224  CD1 ILE A 203      24.882  11.438   0.566  1.00 75.16           C\\nANISOU 1224  CD1 ILE A 203     7956  10453  10148    555    118   -121       C\\nATOM   1225  N   VAL A 204      21.738  11.974   5.082  1.00 68.09           N\\nANISOU 1225  N   VAL A 204     8035   8512   9324    499   -292    232       N\\nATOM   1226  CA  VAL A 204      21.439  12.706   6.313  1.00 64.98           C\\nANISOU 1226  CA  VAL A 204     7739   8013   8938    443   -378    276       C\\nATOM   1227  C   VAL A 204      20.881  11.767   7.375  1.00 65.55           C\\nANISOU 1227  C   VAL A 204     8061   7945   8902    504   -469    277       C\\nATOM   1228  O   VAL A 204      21.332  11.764   8.527  1.00 66.60           O\\nANISOU 1228  O   VAL A 204     8259   8027   9017    550   -610    260       O\\nATOM   1229  CB  VAL A 204      20.471  13.865   6.027  1.00 56.49           C\\nANISOU 1229  CB  VAL A 204     6664   6928   7872    291   -296    354       C\\nATOM   1230  CG1 VAL A 204      19.900  14.399   7.325  1.00 59.98           C\\nANISOU 1230  CG1 VAL A 204     7227   7276   8289    274   -375    333       C\\nATOM   1231  CG2 VAL A 204      21.185  14.972   5.267  1.00 55.27           C\\nANISOU 1231  CG2 VAL A 204     6299   6869   7831    182   -275    403       C\\nATOM   1232  N   THR A 205      19.886  10.960   7.005  1.00 66.29           N\\nANISOU 1232  N   THR A 205     8302   7982   8903    478   -403    312       N\\nATOM   1233  CA  THR A 205      19.340   9.991   7.947  1.00 66.07           C\\nANISOU 1233  CA  THR A 205     8524   7824   8753    475   -492    356       C\\nATOM   1234  C   THR A 205      20.407   9.003   8.395  1.00 73.22           C\\nANISOU 1234  C   THR A 205     9501   8627   9694    637   -693    319       C\\nATOM   1235  O   THR A 205      20.450   8.611   9.567  1.00 73.97           O\\nANISOU 1235  O   THR A 205     9780   8626   9698    635   -843    376       O\\nATOM   1236  CB  THR A 205      18.162   9.258   7.313  1.00 64.13           C\\nANISOU 1236  CB  THR A 205     8398   7536   8434    391   -397    399       C\\nATOM   1237  OG1 THR A 205      17.159  10.210   6.937  1.00 70.05           O\\nANISOU 1237  OG1 THR A 205     9065   8385   9167    268   -244    415       O\\nATOM   1238  CG2 THR A 205      17.567   8.265   8.291  1.00 59.18           C\\nANISOU 1238  CG2 THR A 205     8038   6780   7668    317   -492    485       C\\nATOM   1239  N   LEU A 206      21.282   8.594   7.476  1.00 71.22           N\\nANISOU 1239  N   LEU A 206     9095   8407   9557    784   -714    211       N\\nATOM   1240  CA  LEU A 206      22.343   7.663   7.839  1.00 69.37           C\\nANISOU 1240  CA  LEU A 206     8891   8070   9395    992   -940    126       C\\nATOM   1241  C   LEU A 206      23.325   8.302   8.810  1.00 67.69           C\\nANISOU 1241  C   LEU A 206     8584   7907   9228   1046  -1074    104       C\\nATOM   1242  O   LEU A 206      23.847   7.629   9.705  1.00 63.83           O\\nANISOU 1242  O   LEU A 206     8237   7281   8736   1166  -1318    106       O\\nATOM   1243  CB  LEU A 206      23.069   7.177   6.586  1.00 68.74           C\\nANISOU 1243  CB  LEU A 206     8603   8086   9429   1162   -911    -54       C\\nATOM   1244  CG  LEU A 206      24.254   6.253   6.864  1.00 66.60           C\\nANISOU 1244  CG  LEU A 206     8300   7728   9276   1438  -1170   -212       C\\nATOM   1245  CD1 LEU A 206      23.779   4.999   7.577  1.00 68.61           C\\nANISOU 1245  CD1 LEU A 206     8929   7645   9495   1492  -1416   -131       C\\nATOM   1246  CD2 LEU A 206      24.981   5.908   5.578  1.00 65.91           C\\nANISOU 1246  CD2 LEU A 206     7933   7826   9284   1614  -1102   -453       C\\nATOM   1247  N   LEU A 207      23.592   9.597   8.647  1.00 71.05           N\\nANISOU 1247  N   LEU A 207     8784   8507   9703    951   -950     91       N\\nATOM   1248  CA  LEU A 207      24.489  10.279   9.572  1.00 68.27           C\\nANISOU 1248  CA  LEU A 207     8336   8199   9405    979  -1088     58       C\\nATOM   1249  C   LEU A 207      23.856  10.418  10.949  1.00 68.21           C\\nANISOU 1249  C   LEU A 207     8586   8088   9244    897  -1186    154       C\\nATOM   1250  O   LEU A 207      24.552  10.352  11.967  1.00 66.32           O\\nANISOU 1250  O   LEU A 207     8392   7815   8989    976  -1395    132       O\\nATOM   1251  CB  LEU A 207      24.875  11.645   9.012  1.00 63.44           C\\nANISOU 1251  CB  LEU A 207     7441   7765   8897    855   -953     35       C\\nATOM   1252  CG  LEU A 207      25.757  11.605   7.765  1.00 58.28           C\\nANISOU 1252  CG  LEU A 207     6481   7306   8356    900   -859    -62       C\\nATOM   1253  CD1 LEU A 207      25.869  12.987   7.135  1.00 58.28           C\\nANISOU 1253  CD1 LEU A 207     6266   7458   8418    685   -713     -2       C\\nATOM   1254  CD2 LEU A 207      27.133  11.057   8.115  1.00 60.06           C\\nANISOU 1254  CD2 LEU A 207     6537   7593   8688   1106  -1049   -219       C\\nATOM   1255  N   VAL A 208      22.536  10.604  11.000  1.00 65.76           N\\nANISOU 1255  N   VAL A 208     8427   7760   8800    740  -1039    244       N\\nATOM   1256  CA  VAL A 208      21.850  10.728  12.283  1.00 70.01           C\\nANISOU 1256  CA  VAL A 208     9179   8279   9143    643  -1090    309       C\\nATOM   1257  C   VAL A 208      21.897   9.408  13.042  1.00 72.90           C\\nANISOU 1257  C   VAL A 208     9821   8505   9370    686  -1284    405       C\\nATOM   1258  O   VAL A 208      22.211   9.371  14.237  1.00 72.29           O\\nANISOU 1258  O   VAL A 208     9878   8422   9167    690  -1459    437       O\\nATOM   1259  CB  VAL A 208      20.403  11.205  12.072  1.00 62.31           C\\nANISOU 1259  CB  VAL A 208     8243   7366   8066    475   -875    344       C\\nATOM   1260  CG1 VAL A 208      19.616  11.100  13.361  1.00 57.35           C\\nANISOU 1260  CG1 VAL A 208     7821   6784   7185    363   -898    391       C\\nATOM   1261  CG2 VAL A 208      20.388  12.634  11.560  1.00 55.34           C\\nANISOU 1261  CG2 VAL A 208     7134   6567   7324    438   -769    263       C\\nATOM   1262  N   TYR A 209      21.584   8.304  12.360  1.00 67.17           N\\nANISOU 1262  N   TYR A 209     9206   7651   8663    711  -1285    458       N\\nATOM   1263  CA  TYR A 209      21.578   7.010  13.032  1.00 62.85           C\\nANISOU 1263  CA  TYR A 209     8966   6907   8008    728  -1515    581       C\\nATOM   1264  C   TYR A 209      22.975   6.598  13.468  1.00 67.38           C\\nANISOU 1264  C   TYR A 209     9528   7379   8695    962  -1822    518       C\\nATOM   1265  O   TYR A 209      23.130   5.942  14.504  1.00 76.08           O\\nANISOU 1265  O   TYR A 209    10894   8346   9666    963  -2077    640       O\\nATOM   1266  CB  TYR A 209      20.960   5.946  12.126  1.00 60.49           C\\nANISOU 1266  CB  TYR A 209     8784   6452   7749    710  -1483    623       C\\nATOM   1267  CG  TYR A 209      19.452   5.927  12.179  1.00 66.56           C\\nANISOU 1267  CG  TYR A 209     9685   7270   8334    437  -1286    750       C\\nATOM   1268  CD1 TYR A 209      18.788   5.544  13.335  1.00 66.30           C\\nANISOU 1268  CD1 TYR A 209     9921   7223   8047    229  -1351    931       C\\nATOM   1269  CD2 TYR A 209      18.693   6.292  11.078  1.00 67.85           C\\nANISOU 1269  CD2 TYR A 209     9692   7530   8559    372  -1040    687       C\\nATOM   1270  CE1 TYR A 209      17.408   5.526  13.397  1.00 71.51           C\\nANISOU 1270  CE1 TYR A 209    10651   7990   8531    -39  -1153   1024       C\\nATOM   1271  CE2 TYR A 209      17.312   6.271  11.129  1.00 67.87           C\\nANISOU 1271  CE2 TYR A 209     9776   7601   8410    135   -874    776       C\\nATOM   1272  CZ  TYR A 209      16.675   5.892  12.292  1.00 73.98           C\\nANISOU 1272  CZ  TYR A 209    10778   8387   8944    -71   -920    933       C\\nATOM   1273  OH  TYR A 209      15.301   5.875  12.350  1.00 78.65           O\\nANISOU 1273  OH  TYR A 209    11400   9107   9378   -325   -736    998       O\\nATOM   1274  N   ILE A 210      24.002   6.972  12.702  1.00 65.59           N\\nANISOU 1274  N   ILE A 210     8989   7235   8698   1151  -1815    332       N\\nATOM   1275  CA  ILE A 210      25.373   6.731  13.144  1.00 66.53           C\\nANISOU 1275  CA  ILE A 210     9020   7316   8943   1384  -2102    228       C\\nATOM   1276  C   ILE A 210      25.669   7.536  14.402  1.00 68.90           C\\nANISOU 1276  C   ILE A 210     9347   7706   9128   1318  -2205    265       C\\nATOM   1277  O   ILE A 210      26.296   7.036  15.343  1.00 66.82           O\\nANISOU 1277  O   ILE A 210     9234   7337   8820   1429  -2518    299       O\\nATOM   1278  CB  ILE A 210      26.368   7.053  12.015  1.00 68.77           C\\nANISOU 1278  CB  ILE A 210     8898   7760   9473   1556  -2020      2       C\\nATOM   1279  CG1 ILE A 210      26.237   6.043  10.879  1.00 66.91           C\\nANISOU 1279  CG1 ILE A 210     8656   7435   9331   1685  -1991    -87       C\\nATOM   1280  CG2 ILE A 210      27.792   7.062  12.545  1.00 69.56           C\\nANISOU 1280  CG2 ILE A 210     8822   7898   9711   1774  -2291   -139       C\\nATOM   1281  CD1 ILE A 210      27.237   6.254   9.771  1.00 66.26           C\\nANISOU 1281  CD1 ILE A 210     8158   7579   9440   1852  -1900   -335       C\\nATOM   1282  N   LYS A 211      25.221   8.797  14.439  1.00 68.09           N\\nANISOU 1282  N   LYS A 211     9108   7786   8977   1147  -1974    247       N\\nATOM   1283  CA  LYS A 211      25.368   9.607  15.645  1.00 72.77           C\\nANISOU 1283  CA  LYS A 211     9739   8468   9442   1077  -2066    245       C\\nATOM   1284  C   LYS A 211      24.551   9.044  16.798  1.00 75.75           C\\nANISOU 1284  C   LYS A 211    10492   8790   9501    949  -2158    418       C\\nATOM   1285  O   LYS A 211      24.918   9.225  17.965  1.00 75.16           O\\nANISOU 1285  O   LYS A 211    10526   8758   9275    949  -2353    430       O\\nATOM   1286  CB  LYS A 211      24.956  11.053  15.367  1.00 72.52           C\\nANISOU 1286  CB  LYS A 211     9503   8598   9455    934  -1825    165       C\\nATOM   1287  CG  LYS A 211      26.059  11.921  14.784  1.00 76.74           C\\nANISOU 1287  CG  LYS A 211     9682   9223  10251    997  -1830     21       C\\nATOM   1288  CD  LYS A 211      27.081  12.304  15.845  1.00 80.50           C\\nANISOU 1288  CD  LYS A 211    10106   9734  10746   1072  -2092    -66       C\\nATOM   1289  N   ILE A 212      23.444   8.363  16.492  1.00 76.82           N\\nANISOU 1289  N   ILE A 212    10821   8858   9510    813  -2022    555       N\\nATOM   1290  CA  ILE A 212      22.634   7.738  17.534  1.00 75.49           C\\nANISOU 1290  CA  ILE A 212    11004   8670   9009    629  -2092    753       C\\nATOM   1291  C   ILE A 212      23.351   6.523  18.110  1.00 78.85           C\\nANISOU 1291  C   ILE A 212    11697   8862   9401    741  -2475    889       C\\nATOM   1292  O   ILE A 212      23.426   6.348  19.332  1.00 81.23           O\\nANISOU 1292  O   ILE A 212    12234   9186   9445    664  -2673   1015       O\\nATOM   1293  CB  ILE A 212      21.244   7.368  16.983  1.00 72.94           C\\nANISOU 1293  CB  ILE A 212    10775   8353   8584    420  -1838    858       C\\nATOM   1294  CG1 ILE A 212      20.367   8.618  16.858  1.00 72.24           C\\nANISOU 1294  CG1 ILE A 212    10488   8519   8442    291  -1522    738       C\\nATOM   1295  CG2 ILE A 212      20.575   6.319  17.861  1.00 71.22           C\\nANISOU 1295  CG2 ILE A 212    10941   8062   8058    211  -1961   1112       C\\nATOM   1296  CD1 ILE A 212      18.962   8.339  16.351  1.00 65.08           C\\nANISOU 1296  CD1 ILE A 212     9627   7664   7437     90  -1276    811       C\\nATOM   1297  N   TYR A 213      23.890   5.666  17.237  1.00 80.40           N\\nANISOU 1297  N   TYR A 213    11866   8833   9849    936  -2607    855       N\\nATOM   1298  CA  TYR A 213      24.609   4.484  17.706  1.00 74.91           C\\nANISOU 1298  CA  TYR A 213    11423   7857   9182   1095  -3032    956       C\\nATOM   1299  C   TYR A 213      25.796   4.871  18.580  1.00 76.60           C\\nANISOU 1299  C   TYR A 213    11566   8127   9414   1272  -3314    873       C\\nATOM   1300  O   TYR A 213      26.091   4.197  19.574  1.00 75.58           O\\nANISOU 1300  O   TYR A 213    11741   7846   9129   1288  -3670   1037       O\\nATOM   1301  CB  TYR A 213      25.070   3.642  16.515  1.00 69.47           C\\nANISOU 1301  CB  TYR A 213    10637   6949   8811   1339  -3122    828       C\\nATOM   1302  CG  TYR A 213      25.850   2.401  16.899  1.00 82.87           C\\nANISOU 1302  CG  TYR A 213    12578   8305  10605   1567  -3612    881       C\\nATOM   1303  CD1 TYR A 213      25.198   1.248  17.317  1.00 88.00           C\\nANISOU 1303  CD1 TYR A 213    13681   8643  11110   1422  -3838   1153       C\\nATOM   1304  CD2 TYR A 213      27.237   2.376  16.828  1.00 83.04           C\\nANISOU 1304  CD2 TYR A 213    12370   8305  10877   1924  -3876    656       C\\nATOM   1305  CE1 TYR A 213      25.906   0.107  17.664  1.00 88.45           C\\nANISOU 1305  CE1 TYR A 213    13945   8382  11281   1597  -4262   1171       C\\nATOM   1306  CE2 TYR A 213      27.955   1.241  17.174  1.00 84.14           C\\nANISOU 1306  CE2 TYR A 213    12701   8139  11130   2144  -4318    655       C\\nATOM   1307  CZ  TYR A 213      27.286   0.109  17.589  1.00 88.74           C\\nANISOU 1307  CZ  TYR A 213    13713   8432  11572   1950  -4461    892       C\\nATOM   1308  OH  TYR A 213      27.998  -1.023  17.933  1.00 93.97           O\\nANISOU 1308  OH  TYR A 213    14524   8828  12351   2091  -4813    843       O\\nATOM   1309  N   ILE A 214      26.491   5.955  18.226  1.00 79.22           N\\nANISOU 1309  N   ILE A 214    11503   8668   9929   1388  -3184    634       N\\nATOM   1310  CA  ILE A 214      27.667   6.368  18.988  1.00 79.71           C\\nANISOU 1310  CA  ILE A 214    11448   8796  10043   1553  -3456    525       C\\nATOM   1311  C   ILE A 214      27.278   6.769  20.407  1.00 82.99           C\\nANISOU 1311  C   ILE A 214    12112   9325  10094   1359  -3536    663       C\\nATOM   1312  O   ILE A 214      27.993   6.468  21.373  1.00 77.18           O\\nANISOU 1312  O   ILE A 214    11526   8534   9267   1459  -3903    709       O\\nATOM   1313  CB  ILE A 214      28.405   7.505  18.256  1.00 74.49           C\\nANISOU 1313  CB  ILE A 214    10301   8350   9651   1642  -3272    259       C\\nATOM   1314  CG1 ILE A 214      28.993   6.995  16.944  1.00 73.37           C\\nANISOU 1314  CG1 ILE A 214     9897   8156   9825   1855  -3239    102       C\\nATOM   1315  CG2 ILE A 214      29.508   8.085  19.125  1.00 79.54           C\\nANISOU 1315  CG2 ILE A 214    10802   9091  10328   1753  -3532    141       C\\nATOM   1316  CD1 ILE A 214      29.840   8.022  16.221  1.00 79.87           C\\nANISOU 1316  CD1 ILE A 214    10233   9224  10891   1906  -3079   -130       C\\nATOM   1317  N   VAL A 215      26.138   7.447  20.558  1.00 80.48           N\\nANISOU 1317  N   VAL A 215    11834   9193   9553   1092  -3207    710       N\\nATOM   1318  CA  VAL A 215      25.693   7.866  21.883  1.00 80.01           C\\nANISOU 1318  CA  VAL A 215    11978   9313   9108    905  -3241    790       C\\nATOM   1319  C   VAL A 215      25.303   6.658  22.722  1.00 86.31           C\\nANISOU 1319  C   VAL A 215    13235   9978   9582    774  -3480   1098       C\\nATOM   1320  O   VAL A 215      25.668   6.557  23.900  1.00 89.76           O\\nANISOU 1320  O   VAL A 215    13882  10466   9758    750  -3755   1189       O\\nATOM   1321  CB  VAL A 215      24.532   8.868  21.764  1.00 69.82           C\\nANISOU 1321  CB  VAL A 215    10575   8272   7681    685  -2829    710       C\\nATOM   1322  CG1 VAL A 215      23.873   9.073  23.115  1.00 70.46           C\\nANISOU 1322  CG1 VAL A 215    10891   8582   7299    474  -2833    787       C\\nATOM   1323  CG2 VAL A 215      25.035  10.188  21.201  1.00 70.96           C\\nANISOU 1323  CG2 VAL A 215    10323   8520   8117    791  -2692    435       C\\nATOM   1324  N   LEU A 216      24.556   5.722  22.131  1.00 88.27           N\\nANISOU 1324  N   LEU A 216    13660  10047   9830    664  -3400   1278       N\\nATOM   1325  CA  LEU A 216      24.129   4.539  22.870  1.00 81.42           C\\nANISOU 1325  CA  LEU A 216    13257   9014   8666    480  -3641   1616       C\\nATOM   1326  C   LEU A 216      25.314   3.682  23.294  1.00 84.21           C\\nANISOU 1326  C   LEU A 216    13802   9063   9129    728  -4180   1700       C\\nATOM   1327  O   LEU A 216      25.268   3.046  24.353  1.00 81.69           O\\nANISOU 1327  O   LEU A 216    13836   8687   8514    577  -4427   1947       O\\nATOM   1328  CB  LEU A 216      23.148   3.725  22.025  1.00 83.40           C\\nANISOU 1328  CB  LEU A 216    13629   9094   8967    318  -3470   1765       C\\nATOM   1329  CG  LEU A 216      21.846   4.440  21.657  1.00 89.34           C\\nANISOU 1329  CG  LEU A 216    14218  10142   9584     56  -2973   1707       C\\nATOM   1330  CD1 LEU A 216      21.017   3.625  20.676  1.00 88.79           C\\nANISOU 1330  CD1 LEU A 216    14221   9881   9633    -62  -2839   1814       C\\nATOM   1331  CD2 LEU A 216      21.046   4.736  22.911  1.00 97.88           C\\nANISOU 1331  CD2 LEU A 216    15482  11550  10159   -274  -2870   1850       C\\nATOM   1332  N   ARG A 217      26.382   3.651  22.492  1.00 81.94           N\\nANISOU 1332  N   ARG A 217    13237   8618   9279   1094  -4322   1464       N\\nATOM   1333  CA  ARG A 217      27.561   2.877  22.871  1.00 83.41           C\\nANISOU 1333  CA  ARG A 217    13486   8566   9641   1348  -4750   1435       C\\nATOM   1334  C   ARG A 217      28.345   3.556  23.985  1.00 85.61           C\\nANISOU 1334  C   ARG A 217    13711   9042   9775   1403  -4934   1364       C\\nATOM   1335  O   ARG A 217      28.952   2.873  24.816  1.00 80.30           O\\nANISOU 1335  O   ARG A 217    13221   8234   9057   1442  -5229   1443       O\\nATOM   1336  CB  ARG A 217      28.460   2.641  21.658  1.00 74.00           C\\nANISOU 1336  CB  ARG A 217    11946   7228   8942   1710  -4789   1141       C\\nATOM   1337  N   ARG A 218      28.347   4.891  24.021  1.00 77.47           N\\nANISOU 1337  N   ARG A 218    12427   8320   8687   1399  -4771   1198       N\\nATOM   1338  CA  ARG A 218      28.948   5.589  25.152  1.00 79.95           C\\nANISOU 1338  CA  ARG A 218    12725   8839   8812   1411  -4955   1127       C\\nATOM   1339  C   ARG A 218      28.170   5.328  26.435  1.00 82.04           C\\nANISOU 1339  C   ARG A 218    13403   9226   8543   1087  -4970   1402       C\\nATOM   1340  O   ARG A 218      28.765   5.243  27.517  1.00 84.60           O\\nANISOU 1340  O   ARG A 218    13838   9600   8707   1097  -5207   1432       O\\nATOM   1341  CB  ARG A 218      29.022   7.089  24.868  1.00 75.14           C\\nANISOU 1341  CB  ARG A 218    11692   8536   8320   1397  -4623    823       C\\nATOM   1342  N   ARG A 219      26.847   5.179  26.326  1.00 85.99           N\\nANISOU 1342  N   ARG A 219    14111   9803   8758    785  -4704   1599       N\\nATOM   1343  CA  ARG A 219      26.016   4.885  27.490  1.00 84.46           C\\nANISOU 1343  CA  ARG A 219    14260   9795   8035    425  -4645   1858       C\\nATOM   1344  C   ARG A 219      26.340   3.511  28.066  1.00 86.08           C\\nANISOU 1344  C   ARG A 219    14765   9710   8230    380  -4920   2118       C\\nATOM   1345  O   ARG A 219      26.501   3.361  29.283  1.00 90.06           O\\nANISOU 1345  O   ARG A 219    15467  10337   8414    256  -5076   2247       O\\nATOM   1346  CB  ARG A 219      24.539   4.978  27.102  1.00 85.75           C\\nANISOU 1346  CB  ARG A 219    14494  10127   7961    100  -4243   1970       C\\nATOM   1347  CG  ARG A 219      23.566   4.985  28.270  1.00 97.90           C\\nANISOU 1347  CG  ARG A 219    16277  12019   8900   -302  -4086   2160       C\\nATOM   1348  CD  ARG A 219      22.137   5.191  27.780  1.00103.51           C\\nANISOU 1348  CD  ARG A 219    16923  12951   9455   -597  -3619   2177       C\\nATOM   1349  NE  ARG A 219      22.015   6.380  26.940  1.00103.98           N\\nANISOU 1349  NE  ARG A 219    16513  13152   9842   -422  -3259   1780       N\\nATOM   1350  CZ  ARG A 219      21.746   7.599  27.400  1.00102.81           C\\nANISOU 1350  CZ  ARG A 219    16138  13388   9536   -439  -3032   1497       C\\nATOM   1351  NH1 ARG A 219      21.567   7.793  28.700  1.00112.25           N\\nANISOU 1351  NH1 ARG A 219    17509  14920  10223   -616  -3093   1534       N\\nATOM   1352  NH2 ARG A 219      21.656   8.624  26.563  1.00 90.07           N\\nANISOU 1352  NH2 ARG A 219    14137  11821   8266   -282  -2765   1173       N\\nATOM   1353  N   ARG A 220      26.443   2.493  27.205  1.00 85.93           N\\nANISOU 1353  N   ARG A 220    14788   9305   8558    483  -5002   2177       N\\nATOM   1354  CA  ARG A 220      26.753   1.145  27.680  1.00 92.53           C\\nANISOU 1354  CA  ARG A 220    15922   9808   9426    451  -5313   2391       C\\nATOM   1355  C   ARG A 220      28.118   1.092  28.355  1.00 98.18           C\\nANISOU 1355  C   ARG A 220    16600  10438  10265    730  -5700   2278       C\\nATOM   1356  O   ARG A 220      28.296   0.384  29.353  1.00 99.06           O\\nANISOU 1356  O   ARG A 220    17008  10452  10178    616  -5960   2492       O\\nATOM   1357  CB  ARG A 220      26.686   0.149  26.522  1.00 94.83           C\\nANISOU 1357  CB  ARG A 220    16221   9701  10109    561  -5350   2378       C\\nATOM   1358  CG  ARG A 220      25.281  -0.055  25.969  1.00100.75           C\\nANISOU 1358  CG  ARG A 220    17071  10487  10720    234  -5015   2543       C\\nATOM   1359  CD  ARG A 220      25.299  -0.715  24.596  1.00102.73           C\\nANISOU 1359  CD  ARG A 220    17220  10409  11403    417  -5011   2417       C\\nATOM   1360  NE  ARG A 220      23.971  -0.712  23.986  1.00105.76           N\\nANISOU 1360  NE  ARG A 220    17640  10872  11673    124  -4663   2533       N\\nATOM   1361  CZ  ARG A 220      23.743  -0.876  22.687  1.00111.13           C\\nANISOU 1361  CZ  ARG A 220    18166  11401  12658    249  -4533   2393       C\\nATOM   1362  NH1 ARG A 220      24.756  -1.052  21.850  1.00115.91           N\\nANISOU 1362  NH1 ARG A 220    18552  11801  13687    664  -4699   2115       N\\nATOM   1363  NH2 ARG A 220      22.500  -0.857  22.220  1.00109.07           N\\nANISOU 1363  NH2 ARG A 220    17943  11230  12267    -44  -4223   2509       N\\nATOM   1364  N   LYS A 221      29.096   1.832  27.826  1.00 87.90           N\\nANISOU 1364  N   LYS A 221    14922   9183   9293   1081  -5746   1943       N\\nATOM   1365  CA  LYS A 221      30.396   1.903  28.485  1.00 91.01           C\\nANISOU 1365  CA  LYS A 221    15227   9552   9800   1332  -6088   1803       C\\nATOM   1366  C   LYS A 221      30.311   2.643  29.815  1.00 92.81           C\\nANISOU 1366  C   LYS A 221    15563  10123   9576   1152  -6111   1881       C\\nATOM   1367  O   LYS A 221      31.080   2.348  30.738  1.00 97.14           O\\nANISOU 1367  O   LYS A 221    16229  10626  10054   1227  -6434   1922       O\\nATOM   1368  CB  LYS A 221      31.420   2.575  27.569  1.00 88.24           C\\nANISOU 1368  CB  LYS A 221    14391   9229   9907   1702  -6082   1409       C\\nATOM   1369  N   ARG A 222      29.386   3.599  29.935  1.00 89.90           N\\nANISOU 1369  N   ARG A 222    15156  10111   8890    923  -5782   1877       N\\nATOM   1370  CA  ARG A 222      29.220   4.328  31.190  1.00 91.86           C\\nANISOU 1370  CA  ARG A 222    15494  10740   8669    746  -5774   1897       C\\nATOM   1371  C   ARG A 222      28.375   3.544  32.190  1.00 96.10           C\\nANISOU 1371  C   ARG A 222    16450  11352   8712    379  -5763   2271       C\\nATOM   1372  O   ARG A 222      28.677   3.536  33.390  1.00100.34           O\\nANISOU 1372  O   ARG A 222    17145  12050   8928    306  -5948   2359       O\\nATOM   1373  CB  ARG A 222      28.596   5.698  30.923  1.00 87.62           C\\nANISOU 1373  CB  ARG A 222    14726  10572   7995    668  -5443   1670       C\\nATOM   1374  N   ASN A1002      27.322   2.874  31.712  1.00 85.72           N\\nANISOU 1374  N   ASN A1002    12716   9421  10431    154  -1889   1403       N\\nATOM   1375  CA  ASN A1002      26.456   2.104  32.601  1.00 78.54           C\\nANISOU 1375  CA  ASN A1002    11488   8720   9636    336  -1772   1042       C\\nATOM   1376  C   ASN A1002      27.206   0.951  33.259  1.00 74.17           C\\nANISOU 1376  C   ASN A1002    10829   8409   8943    253  -1283    980       C\\nATOM   1377  O   ASN A1002      26.974   0.646  34.435  1.00 77.99           O\\nANISOU 1377  O   ASN A1002    11066   9013   9552    361  -1151    748       O\\nATOM   1378  CB  ASN A1002      25.242   1.584  31.828  1.00 72.27           C\\nANISOU 1378  CB  ASN A1002    10694   8018   8747    370  -1959    956       C\\nATOM   1379  CG  ASN A1002      24.296   2.693  31.414  1.00 85.39           C\\nANISOU 1379  CG  ASN A1002    12363   9440  10641    548  -2522    954       C\\nATOM   1380  OD1 ASN A1002      24.569   3.871  31.643  1.00 91.93           O\\nANISOU 1380  OD1 ASN A1002    13249   9977  11701    641  -2774   1033       O\\nATOM   1381  ND2 ASN A1002      23.179   2.324  30.796  1.00 95.12           N\\nANISOU 1381  ND2 ASN A1002    13533  10764  11844    599  -2763    857       N\\nATOM   1382  N   ILE A1003      28.104   0.295  32.520  1.00 69.88           N\\nANISOU 1382  N   ILE A1003    10476   7942   8134     67  -1017   1180       N\\nATOM   1383  CA  ILE A1003      28.844  -0.824  33.094  1.00 75.25           C\\nANISOU 1383  CA  ILE A1003    11058   8796   8739     40   -607   1126       C\\nATOM   1384  C   ILE A1003      29.846  -0.336  34.137  1.00 79.70           C\\nANISOU 1384  C   ILE A1003    11473   9334   9474     69   -527   1154       C\\nATOM   1385  O   ILE A1003      30.117  -1.035  35.121  1.00 81.90           O\\nANISOU 1385  O   ILE A1003    11597   9734   9788    131   -334   1048       O\\nATOM   1386  CB  ILE A1003      29.526  -1.644  31.981  1.00 76.66           C\\nANISOU 1386  CB  ILE A1003    11445   9056   8624   -116   -342   1259       C\\nATOM   1387  CG1 ILE A1003      30.131  -2.927  32.553  1.00 83.23           C\\nANISOU 1387  CG1 ILE A1003    12171  10007   9446    -76     25   1164       C\\nATOM   1388  CG2 ILE A1003      30.599  -0.830  31.276  1.00 75.86           C\\nANISOU 1388  CG2 ILE A1003    11492   8897   8434   -279   -312   1524       C\\nATOM   1389  CD1 ILE A1003      30.765  -3.812  31.509  1.00 89.05           C\\nANISOU 1389  CD1 ILE A1003    13083  10813   9939   -170    311   1194       C\\nATOM   1390  N   PHE A1004      30.403   0.862  33.954  1.00 72.73           N\\nANISOU 1390  N   PHE A1004    10657   8281   8697      0   -708   1309       N\\nATOM   1391  CA  PHE A1004      31.300   1.419  34.961  1.00 72.86           C\\nANISOU 1391  CA  PHE A1004    10523   8260   8901      1   -698   1302       C\\nATOM   1392  C   PHE A1004      30.561   1.658  36.271  1.00 75.78           C\\nANISOU 1392  C   PHE A1004    10709   8641   9442    194   -837   1009       C\\nATOM   1393  O   PHE A1004      31.045   1.293  37.349  1.00 75.51           O\\nANISOU 1393  O   PHE A1004    10525   8740   9424    231   -703    911       O\\nATOM   1394  CB  PHE A1004      31.920   2.718  34.446  1.00 74.85           C\\nANISOU 1394  CB  PHE A1004    10908   8273   9256   -164   -904   1525       C\\nATOM   1395  CG  PHE A1004      32.831   3.387  35.431  1.00 80.49           C\\nANISOU 1395  CG  PHE A1004    11471   8921  10192   -205   -951   1497       C\\nATOM   1396  CD1 PHE A1004      34.093   2.876  35.685  1.00 79.31           C\\nANISOU 1396  CD1 PHE A1004    11166   8951  10018   -317   -675   1584       C\\nATOM   1397  CD2 PHE A1004      32.429   4.533  36.100  1.00 83.97           C\\nANISOU 1397  CD2 PHE A1004    11907   9110  10888   -118  -1297   1351       C\\nATOM   1398  CE1 PHE A1004      34.938   3.492  36.589  1.00 82.95           C\\nANISOU 1398  CE1 PHE A1004    11465   9368  10684   -377   -769   1550       C\\nATOM   1399  CE2 PHE A1004      33.269   5.154  37.007  1.00 85.07           C\\nANISOU 1399  CE2 PHE A1004    11928   9181  11215   -183  -1370   1289       C\\nATOM   1400  CZ  PHE A1004      34.525   4.633  37.251  1.00 84.25           C\\nANISOU 1400  CZ  PHE A1004    11666   9282  11062   -331  -1119   1402       C\\nATOM   1401  N   GLU A1005      29.376   2.270  36.194  1.00 75.34           N\\nANISOU 1401  N   GLU A1005    10654   8467   9503    325  -1114    852       N\\nATOM   1402  CA  GLU A1005      28.576   2.488  37.395  1.00 80.23           C\\nANISOU 1402  CA  GLU A1005    11062   9155  10266    516  -1188    504       C\\nATOM   1403  C   GLU A1005      28.115   1.169  38.000  1.00 86.02           C\\nANISOU 1403  C   GLU A1005    11656  10202  10825    527   -889    366       C\\nATOM   1404  O   GLU A1005      28.046   1.030  39.227  1.00 90.45           O\\nANISOU 1404  O   GLU A1005    12070  10923  11372    580   -788    167       O\\nATOM   1405  CB  GLU A1005      27.375   3.375  37.076  1.00 77.92           C\\nANISOU 1405  CB  GLU A1005    10741   8676  10189    694  -1544    334       C\\nATOM   1406  CG  GLU A1005      27.742   4.831  36.890  1.00 84.80           C\\nANISOU 1406  CG  GLU A1005    11751   9159  11311    720  -1903    409       C\\nATOM   1407  CD  GLU A1005      28.491   5.393  38.081  1.00 89.89           C\\nANISOU 1407  CD  GLU A1005    12315   9761  12076    724  -1883    248       C\\nATOM   1408  OE1 GLU A1005      27.991   5.262  39.219  1.00 89.61           O\\nANISOU 1408  OE1 GLU A1005    12069   9916  12064    880  -1796   -120       O\\nATOM   1409  OE2 GLU A1005      29.591   5.949  37.880  1.00 88.50           O\\nANISOU 1409  OE2 GLU A1005    12285   9394  11947    539  -1944    483       O\\nATOM   1410  N   MET A1006      27.798   0.187  37.153  1.00 78.13           N\\nANISOU 1410  N   MET A1006    10736   9284   9667    448   -755    474       N\\nATOM   1411  CA  MET A1006      27.337  -1.104  37.657  1.00 72.09           C\\nANISOU 1411  CA  MET A1006     9881   8748   8762    410   -494    376       C\\nATOM   1412  C   MET A1006      28.381  -1.755  38.553  1.00 75.65           C\\nANISOU 1412  C   MET A1006    10336   9295   9114    362   -262    468       C\\nATOM   1413  O   MET A1006      28.038  -2.402  39.549  1.00 76.42           O\\nANISOU 1413  O   MET A1006    10345   9565   9126    348   -119    363       O\\nATOM   1414  CB  MET A1006      26.994  -2.033  36.497  1.00 63.48           C\\nANISOU 1414  CB  MET A1006     8926   7661   7531    307   -419    476       C\\nATOM   1415  CG  MET A1006      26.279  -3.292  36.913  1.00 70.23           C\\nANISOU 1415  CG  MET A1006     9703   8684   8298    231   -215    360       C\\nATOM   1416  SD  MET A1006      26.609  -4.663  35.798  1.00 70.93           S\\nANISOU 1416  SD  MET A1006    10037   8714   8198     86    -29    502       S\\nATOM   1417  CE  MET A1006      25.235  -5.747  36.183  1.00 79.60           C\\nANISOU 1417  CE  MET A1006    11010   9948   9288    -46     55    311       C\\nATOM   1418  N   LEU A1007      29.660  -1.591  38.223  1.00 74.32           N\\nANISOU 1418  N   LEU A1007    10257   9030   8951    321   -234    678       N\\nATOM   1419  CA  LEU A1007      30.716  -2.231  38.992  1.00 72.19           C\\nANISOU 1419  CA  LEU A1007     9955   8841   8633    310    -74    777       C\\nATOM   1420  C   LEU A1007      31.310  -1.346  40.078  1.00 77.91           C\\nANISOU 1420  C   LEU A1007    10574   9585   9442    343   -217    715       C\\nATOM   1421  O   LEU A1007      31.846  -1.881  41.054  1.00 81.18           O\\nANISOU 1421  O   LEU A1007    10944  10120   9781    352   -154    740       O\\nATOM   1422  CB  LEU A1007      31.835  -2.718  38.066  1.00 71.02           C\\nANISOU 1422  CB  LEU A1007     9882   8633   8470    261     76    992       C\\nATOM   1423  CG  LEU A1007      31.556  -4.102  37.475  1.00 67.80           C\\nANISOU 1423  CG  LEU A1007     9585   8237   7941    251    288   1010       C\\nATOM   1424  CD1 LEU A1007      30.727  -4.015  36.198  1.00 65.13           C\\nANISOU 1424  CD1 LEU A1007     9386   7844   7514    183    249    974       C\\nATOM   1425  CD2 LEU A1007      32.848  -4.848  37.236  1.00 68.79           C\\nANISOU 1425  CD2 LEU A1007     9698   8348   8090    287    481   1140       C\\nATOM   1426  N   ARG A1008      31.232  -0.018  39.954  1.00 81.15           N\\nANISOU 1426  N   ARG A1008    10972   9855  10007    355   -447    635       N\\nATOM   1427  CA  ARG A1008      31.610   0.793  41.106  1.00 79.83           C\\nANISOU 1427  CA  ARG A1008    10721   9701   9912    383   -602    485       C\\nATOM   1428  C   ARG A1008      30.583   0.693  42.224  1.00 79.95           C\\nANISOU 1428  C   ARG A1008    10660   9903   9815    473   -581    181       C\\nATOM   1429  O   ARG A1008      30.878   1.089  43.357  1.00 82.62           O\\nANISOU 1429  O   ARG A1008    10953  10337  10104    486   -655     22       O\\nATOM   1430  CB  ARG A1008      31.814   2.257  40.711  1.00 75.25           C\\nANISOU 1430  CB  ARG A1008    10178   8848   9565    361   -878    461       C\\nATOM   1431  CG  ARG A1008      30.548   3.009  40.384  1.00 84.73           C\\nANISOU 1431  CG  ARG A1008    11405   9893  10893    488  -1070    258       C\\nATOM   1432  CD  ARG A1008      30.759   4.502  40.562  1.00 91.79           C\\nANISOU 1432  CD  ARG A1008    12342  10481  12053    509  -1399    147       C\\nATOM   1433  NE  ARG A1008      30.802   4.870  41.973  1.00 97.78           N\\nANISOU 1433  NE  ARG A1008    12996  11338  12815    587  -1451   -187       N\\nATOM   1434  CZ  ARG A1008      29.731   5.209  42.684  1.00100.58           C\\nANISOU 1434  CZ  ARG A1008    13254  11756  13206    785  -1504   -595       C\\nATOM   1435  NH1 ARG A1008      28.534   5.231  42.111  1.00 94.43           N\\nANISOU 1435  NH1 ARG A1008    12420  10935  12522    941  -1541   -707       N\\nATOM   1436  NH2 ARG A1008      29.857   5.526  43.966  1.00105.64           N\\nANISOU 1436  NH2 ARG A1008    13834  12529  13777    825  -1520   -917       N\\nATOM   1437  N   ILE A1009      29.394   0.171  41.926  1.00 74.25           N\\nANISOU 1437  N   ILE A1009     9910   9267   9034    507   -473     81       N\\nATOM   1438  CA  ILE A1009      28.416  -0.151  42.956  1.00 75.30           C\\nANISOU 1438  CA  ILE A1009     9929   9661   9019    531   -350   -186       C\\nATOM   1439  C   ILE A1009      28.680  -1.535  43.536  1.00 78.79           C\\nANISOU 1439  C   ILE A1009    10438  10305   9194    403   -107     -8       C\\nATOM   1440  O   ILE A1009      28.534  -1.752  44.743  1.00 85.17           O\\nANISOU 1440  O   ILE A1009    11227  11348   9787    355    -20   -120       O\\nATOM   1441  CB  ILE A1009      26.996  -0.039  42.373  1.00 72.07           C\\nANISOU 1441  CB  ILE A1009     9394   9267   8722    603   -364   -387       C\\nATOM   1442  CG1 ILE A1009      26.670   1.415  42.030  1.00 73.75           C\\nANISOU 1442  CG1 ILE A1009     9547   9243   9230    783   -675   -591       C\\nATOM   1443  CG2 ILE A1009      25.968  -0.620  43.332  1.00 70.49           C\\nANISOU 1443  CG2 ILE A1009     9027   9408   8349    556   -136   -634       C\\nATOM   1444  CD1 ILE A1009      25.423   1.572  41.190  1.00 76.17           C\\nANISOU 1444  CD1 ILE A1009     9730   9499   9713    890   -796   -718       C\\nATOM   1445  N   ASP A1010      29.079  -2.490  42.694  1.00 72.06           N\\nANISOU 1445  N   ASP A1010     9694   9350   8336    343     -7    269       N\\nATOM   1446  CA  ASP A1010      29.286  -3.870  43.127  1.00 72.56           C\\nANISOU 1446  CA  ASP A1010     9858   9501   8210    243    179    457       C\\nATOM   1447  C   ASP A1010      30.708  -4.106  43.629  1.00 75.95           C\\nANISOU 1447  C   ASP A1010    10352   9894   8612    272    117    675       C\\nATOM   1448  O   ASP A1010      30.908  -4.550  44.763  1.00 79.91           O\\nANISOU 1448  O   ASP A1010    10905  10541   8916    226    124    730       O\\nATOM   1449  CB  ASP A1010      28.966  -4.834  41.979  1.00 68.87           C\\nANISOU 1449  CB  ASP A1010     9481   8902   7784    190    300    582       C\\nATOM   1450  CG  ASP A1010      27.482  -4.951  41.709  1.00 73.05           C\\nANISOU 1450  CG  ASP A1010     9921   9528   8308    113    358    385       C\\nATOM   1451  OD1 ASP A1010      26.693  -4.307  42.432  1.00 67.48           O\\nANISOU 1451  OD1 ASP A1010     9046   9009   7582    124    341    140       O\\nATOM   1452  OD2 ASP A1010      27.105  -5.691  40.773  1.00 78.54           O\\nANISOU 1452  OD2 ASP A1010    10691  10123   9026     43    418    440       O\\nATOM   1453  N   GLU A1011      31.702  -3.824  42.788  1.00 76.16           N\\nANISOU 1453  N   GLU A1011    10363   9749   8825    334     50    808       N\\nATOM   1454  CA  GLU A1011      33.088  -4.089  43.149  1.00 80.16           C\\nANISOU 1454  CA  GLU A1011    10842  10236   9377    379    -14    997       C\\nATOM   1455  C   GLU A1011      33.663  -2.965  44.003  1.00 86.62           C\\nANISOU 1455  C   GLU A1011    11560  11131  10222    377   -238    897       C\\nATOM   1456  O   GLU A1011      34.212  -3.213  45.081  1.00 98.58           O\\nANISOU 1456  O   GLU A1011    13076  12768  11614    380   -345    952       O\\nATOM   1457  CB  GLU A1011      33.926  -4.284  41.885  1.00 82.54           C\\nANISOU 1457  CB  GLU A1011    11111  10383   9867    418     68   1140       C\\nATOM   1458  CG  GLU A1011      35.344  -4.765  42.134  1.00 89.74           C\\nANISOU 1458  CG  GLU A1011    11913  11291  10894    502     40   1313       C\\nATOM   1459  CD  GLU A1011      35.393  -6.223  42.539  1.00 95.34           C\\nANISOU 1459  CD  GLU A1011    12731  11959  11534    586    111   1445       C\\nATOM   1460  OE1 GLU A1011      35.895  -6.518  43.646  1.00 99.56           O\\nANISOU 1460  OE1 GLU A1011    13255  12559  12013    632    -51   1549       O\\nATOM   1461  OE2 GLU A1011      34.920  -7.072  41.751  1.00 94.59           O\\nANISOU 1461  OE2 GLU A1011    12763  11742  11436    596    295   1450       O\\nATOM   1462  N   GLY A1012      33.549  -1.725  43.534  1.00 83.15           N\\nANISOU 1462  N   GLY A1012    11062  10592   9938    362   -351    758       N\\nATOM   1463  CA  GLY A1012      34.064  -0.590  44.272  1.00 80.42           C\\nANISOU 1463  CA  GLY A1012    10644  10253   9660    339   -589    621       C\\nATOM   1464  C   GLY A1012      35.145   0.176  43.536  1.00 76.41           C\\nANISOU 1464  C   GLY A1012    10041   9573   9418    270   -701    745       C\\nATOM   1465  O   GLY A1012      36.026  -0.422  42.909  1.00 75.35           O\\nANISOU 1465  O   GLY A1012     9829   9430   9369    254   -588    972       O\\nATOM   1466  N   LEU A1013      35.090   1.505  43.610  1.00 72.47           N\\nANISOU 1466  N   LEU A1013     9539   8928   9066    216   -914    581       N\\nATOM   1467  CA  LEU A1013      36.059   2.381  42.960  1.00 75.06           C\\nANISOU 1467  CA  LEU A1013     9799   9069   9653     69  -1037    711       C\\nATOM   1468  C   LEU A1013      37.076   2.842  43.998  1.00 85.43           C\\nANISOU 1468  C   LEU A1013    10980  10447  11031    -12  -1266    645       C\\nATOM   1469  O   LEU A1013      36.730   3.569  44.935  1.00 92.30           O\\nANISOU 1469  O   LEU A1013    11906  11301  11864      3  -1478    364       O\\nATOM   1470  CB  LEU A1013      35.362   3.575  42.309  1.00 76.93           C\\nANISOU 1470  CB  LEU A1013    10164   9014  10053     35  -1188    614       C\\nATOM   1471  CG  LEU A1013      36.264   4.677  41.743  1.00 81.85           C\\nANISOU 1471  CG  LEU A1013    10778   9382  10939   -188  -1361    759       C\\nATOM   1472  CD1 LEU A1013      37.119   4.145  40.607  1.00 83.65           C\\nANISOU 1472  CD1 LEU A1013    10936   9672  11176   -345  -1119   1104       C\\nATOM   1473  CD2 LEU A1013      35.444   5.879  41.290  1.00 79.42           C\\nANISOU 1473  CD2 LEU A1013    10661   8711  10803   -183  -1600    657       C\\nATOM   1474  N   ARG A1014      38.324   2.416  43.830  1.00 82.30           N\\nANISOU 1474  N   ARG A1014    10388  10143  10740    -92  -1229    865       N\\nATOM   1475  CA  ARG A1014      39.431   2.846  44.673  1.00 87.70           C\\nANISOU 1475  CA  ARG A1014    10885  10900  11537   -200  -1487    834       C\\nATOM   1476  C   ARG A1014      40.374   3.720  43.858  1.00 91.11           C\\nANISOU 1476  C   ARG A1014    11154  11170  12293   -454  -1533    970       C\\nATOM   1477  O   ARG A1014      40.854   3.301  42.800  1.00 93.58           O\\nANISOU 1477  O   ARG A1014    11348  11510  12699   -513  -1278   1201       O\\nATOM   1478  CB  ARG A1014      40.189   1.647  45.242  1.00 89.70           C\\nANISOU 1478  CB  ARG A1014    10969  11409  11702    -83  -1465    977       C\\nATOM   1479  CG  ARG A1014      39.445   0.867  46.311  1.00 95.14           C\\nANISOU 1479  CG  ARG A1014    11845  12266  12037     80  -1493    888       C\\nATOM   1480  CD  ARG A1014      40.338   0.658  47.527  1.00103.70           C\\nANISOU 1480  CD  ARG A1014    12817  13547  13039     82  -1799    903       C\\nATOM   1481  NE  ARG A1014      39.801  -0.327  48.462  1.00107.67           N\\nANISOU 1481  NE  ARG A1014    13522  14230  13160    204  -1802    939       N\\nATOM   1482  CZ  ARG A1014      40.399  -0.677  49.597  1.00111.85           C\\nANISOU 1482  CZ  ARG A1014    14048  14948  13504    219  -2094    997       C\\nATOM   1483  NH1 ARG A1014      41.553  -0.119  49.939  1.00113.46           N\\nANISOU 1483  NH1 ARG A1014    14008  15196  13905    140  -2424    984       N\\nATOM   1484  NH2 ARG A1014      39.844  -1.584  50.391  1.00112.62           N\\nANISOU 1484  NH2 ARG A1014    14392  15192  13208    282  -2078   1085       N\\nATOM   1485  N   LEU A1015      40.648   4.926  44.357  1.00 92.65           N\\nANISOU 1485  N   LEU A1015    11353  11202  12646   -633  -1845    811       N\\nATOM   1486  CA  LEU A1015      41.453   5.897  43.627  1.00 98.42           C\\nANISOU 1486  CA  LEU A1015    11974  11728  13694   -955  -1914    952       C\\nATOM   1487  C   LEU A1015      42.928   5.886  44.013  1.00100.85           C\\nANISOU 1487  C   LEU A1015    11893  12218  14209  -1148  -2036   1034       C\\nATOM   1488  O   LEU A1015      43.750   6.434  43.268  1.00 98.40           O\\nANISOU 1488  O   LEU A1015    11399  11829  14161  -1460  -1984   1214       O\\nATOM   1489  CB  LEU A1015      40.885   7.309  43.827  1.00 99.65           C\\nANISOU 1489  CB  LEU A1015    12381  11497  13985  -1071  -2220    736       C\\nATOM   1490  CG  LEU A1015      39.471   7.567  43.292  1.00 99.54           C\\nANISOU 1490  CG  LEU A1015    12694  11242  13885   -893  -2166    655       C\\nATOM   1491  CD1 LEU A1015      39.000   8.964  43.667  1.00 99.18           C\\nANISOU 1491  CD1 LEU A1015    12859  10780  14044   -939  -2532    377       C\\nATOM   1492  CD2 LEU A1015      39.410   7.369  41.782  1.00 97.70           C\\nANISOU 1492  CD2 LEU A1015    12526  10927  13670   -996  -1904   1008       C\\nATOM   1493  N   LYS A1016      43.285   5.285  45.145  1.00105.59           N\\nANISOU 1493  N   LYS A1016    12353  13074  14693   -995  -2209    921       N\\nATOM   1494  CA  LYS A1016      44.673   5.127  45.549  1.00101.07           C\\nANISOU 1494  CA  LYS A1016    11354  12717  14330  -1119  -2373    997       C\\nATOM   1495  C   LYS A1016      45.057   3.654  45.506  1.00 97.42           C\\nANISOU 1495  C   LYS A1016    10673  12549  13792   -837  -2171   1168       C\\nATOM   1496  O   LYS A1016      44.204   2.765  45.581  1.00 93.98           O\\nANISOU 1496  O   LYS A1016    10480  12152  13076   -558  -2006   1179       O\\nATOM   1497  CB  LYS A1016      44.913   5.693  46.953  1.00 96.36           C\\nANISOU 1497  CB  LYS A1016    10775  12159  13680  -1180  -2856    730       C\\nATOM   1498  N   ILE A1017      46.361   3.401  45.382  1.00 93.92           N\\nANISOU 1498  N   ILE A1017     9745  12296  13643   -915  -2196   1291       N\\nATOM   1499  CA  ILE A1017      46.835   2.030  45.257  1.00 95.27           C\\nANISOU 1499  CA  ILE A1017     9663  12692  13845   -609  -2025   1434       C\\nATOM   1500  C   ILE A1017      46.498   1.247  46.517  1.00 93.58           C\\nANISOU 1500  C   ILE A1017     9634  12578  13344   -317  -2322   1390       C\\nATOM   1501  O   ILE A1017      46.630   1.745  47.643  1.00 98.49           O\\nANISOU 1501  O   ILE A1017    10306  13255  13861   -400  -2751   1258       O\\nATOM   1502  CB  ILE A1017      48.346   2.013  44.968  1.00 99.88           C\\nANISOU 1502  CB  ILE A1017     9604  13484  14862   -733  -2035   1517       C\\nATOM   1503  CG1 ILE A1017      48.641   2.776  43.677  1.00 99.15           C\\nANISOU 1503  CG1 ILE A1017     9368  13325  14980  -1097  -1674   1598       C\\nATOM   1504  CG2 ILE A1017      48.859   0.586  44.863  1.00102.32           C\\nANISOU 1504  CG2 ILE A1017     9624  13983  15272   -342  -1894   1617       C\\nATOM   1505  CD1 ILE A1017      50.072   2.657  43.214  1.00100.19           C\\nANISOU 1505  CD1 ILE A1017     8808  13728  15530  -1237  -1535   1668       C\\nATOM   1506  N   TYR A1018      46.040   0.013  46.328  1.00 96.96           N\\nANISOU 1506  N   TYR A1018    10204  13021  13613     -4  -2100   1503       N\\nATOM   1507  CA  TYR A1018      45.693  -0.867  47.432  1.00100.96           C\\nANISOU 1507  CA  TYR A1018    10937  13603  13821    241  -2341   1544       C\\nATOM   1508  C   TYR A1018      45.961  -2.303  47.006  1.00113.96           C\\nANISOU 1508  C   TYR A1018    12472  15250  15576    569  -2149   1734       C\\nATOM   1509  O   TYR A1018      46.224  -2.587  45.835  1.00121.07           O\\nANISOU 1509  O   TYR A1018    13172  16106  16722    616  -1774   1767       O\\nATOM   1510  CB  TYR A1018      44.232  -0.693  47.850  1.00 93.06           C\\nANISOU 1510  CB  TYR A1018    10474  12514  12372    220  -2278   1421       C\\nATOM   1511  CG  TYR A1018      43.253  -1.208  46.822  1.00 94.64           C\\nANISOU 1511  CG  TYR A1018    10901  12566  12493    308  -1824   1465       C\\nATOM   1512  CD1 TYR A1018      43.069  -0.541  45.617  1.00 98.44           C\\nANISOU 1512  CD1 TYR A1018    11346  12911  13146    160  -1544   1428       C\\nATOM   1513  CD2 TYR A1018      42.513  -2.358  47.053  1.00 92.36           C\\nANISOU 1513  CD2 TYR A1018    10884  12266  11944    505  -1704   1563       C\\nATOM   1514  CE1 TYR A1018      42.179  -1.007  44.669  1.00 97.08           C\\nANISOU 1514  CE1 TYR A1018    11389  12624  12873    230  -1183   1460       C\\nATOM   1515  CE2 TYR A1018      41.614  -2.831  46.111  1.00 95.41           C\\nANISOU 1515  CE2 TYR A1018    11463  12519  12271    556  -1325   1577       C\\nATOM   1516  CZ  TYR A1018      41.450  -2.147  44.923  1.00 96.24           C\\nANISOU 1516  CZ  TYR A1018    11515  12518  12534    430  -1079   1511       C\\nATOM   1517  OH  TYR A1018      40.562  -2.611  43.980  1.00 94.30           O\\nANISOU 1517  OH  TYR A1018    11469  12159  12201    471   -755   1517       O\\nATOM   1518  N   LYS A1019      45.882  -3.212  47.972  1.00112.29           N\\nANISOU 1518  N   LYS A1019    12428  15075  15161    787  -2416   1854       N\\nATOM   1519  CA  LYS A1019      46.124  -4.629  47.736  1.00114.49           C\\nANISOU 1519  CA  LYS A1019    12662  15272  15567   1129  -2330   2040       C\\nATOM   1520  C   LYS A1019      44.796  -5.365  47.616  1.00112.47           C\\nANISOU 1520  C   LYS A1019    12933  14846  14954   1191  -2067   2094       C\\nATOM   1521  O   LYS A1019      43.893  -5.162  48.435  1.00114.99           O\\nANISOU 1521  O   LYS A1019    13645  15200  14846   1061  -2176   2073       O\\nATOM   1522  CB  LYS A1019      46.964  -5.233  48.863  1.00116.93           C\\nANISOU 1522  CB  LYS A1019    12829  15675  15923   1330  -2866   2206       C\\nATOM   1523  N   ASP A1020      44.677  -6.212  46.597  1.00112.39           N\\nANISOU 1523  N   ASP A1020    12914  14672  15118   1369  -1707   2129       N\\nATOM   1524  CA  ASP A1020      43.491  -7.038  46.453  1.00108.38           C\\nANISOU 1524  CA  ASP A1020    12868  13981  14329   1415  -1485   2186       C\\nATOM   1525  C   ASP A1020      43.556  -8.206  47.436  1.00111.34           C\\nANISOU 1525  C   ASP A1020    13459  14255  14590   1619  -1796   2432       C\\nATOM   1526  O   ASP A1020      44.475  -8.316  48.253  1.00111.64           O\\nANISOU 1526  O   ASP A1020    13307  14376  14734   1741  -2219   2559       O\\nATOM   1527  CB  ASP A1020      43.344  -7.520  45.010  1.00103.84           C\\nANISOU 1527  CB  ASP A1020    12244  13254  13957   1507  -1026   2105       C\\nATOM   1528  CG  ASP A1020      44.444  -8.477  44.594  1.00108.01           C\\nANISOU 1528  CG  ASP A1020    12440  13694  14903   1844  -1010   2150       C\\nATOM   1529  OD1 ASP A1020      45.525  -8.453  45.217  1.00113.64           O\\nANISOU 1529  OD1 ASP A1020    12802  14515  15861   1981  -1346   2220       O\\nATOM   1530  OD2 ASP A1020      44.228  -9.253  43.639  1.00105.75           O\\nANISOU 1530  OD2 ASP A1020    12227  13235  14718   1987   -677   2082       O\\nATOM   1531  N   THR A1021      42.571  -9.101  47.357  1.00111.86           N\\nANISOU 1531  N   THR A1021    13936  14124  14441   1634  -1618   2524       N\\nATOM   1532  CA  THR A1021      42.498 -10.201  48.311  1.00111.37           C\\nANISOU 1532  CA  THR A1021    14180  13918  14216   1754  -1913   2816       C\\nATOM   1533  C   THR A1021      43.592 -11.242  48.108  1.00113.87           C\\nANISOU 1533  C   THR A1021    14272  14000  14994   2154  -2104   2966       C\\nATOM   1534  O   THR A1021      43.713 -12.150  48.936  1.00122.97           O\\nANISOU 1534  O   THR A1021    15669  14982  16073   2291  -2453   3261       O\\nATOM   1535  CB  THR A1021      41.130 -10.879  48.236  1.00106.11           C\\nANISOU 1535  CB  THR A1021    14000  13085  13230   1600  -1650   2877       C\\nATOM   1536  OG1 THR A1021      40.997 -11.555  46.980  1.00101.52           O\\nANISOU 1536  OG1 THR A1021    13390  12234  12949   1746  -1308   2783       O\\nATOM   1537  CG2 THR A1021      40.020  -9.844  48.372  1.00105.59           C\\nANISOU 1537  CG2 THR A1021    14074  13265  12778   1259  -1443   2671       C\\nATOM   1538  N   GLU A1022      44.388 -11.136  47.045  1.00109.65           N\\nANISOU 1538  N   GLU A1022    13282  13452  14927   2346  -1889   2772       N\\nATOM   1539  CA  GLU A1022      45.477 -12.070  46.790  1.00109.91           C\\nANISOU 1539  CA  GLU A1022    13002  13289  15472   2780  -2033   2824       C\\nATOM   1540  C   GLU A1022      46.850 -11.447  47.014  1.00110.30           C\\nANISOU 1540  C   GLU A1022    12423  13602  15882   2906  -2315   2766       C\\nATOM   1541  O   GLU A1022      47.866 -12.107  46.769  1.00114.91           O\\nANISOU 1541  O   GLU A1022    12609  14084  16969   3299  -2431   2752       O\\nATOM   1542  CB  GLU A1022      45.376 -12.625  45.367  1.00110.94           C\\nANISOU 1542  CB  GLU A1022    13056  13217  15878   2939  -1526   2594       C\\nATOM   1543  N   GLY A1023      46.907 -10.195  47.471  1.00108.89           N\\nANISOU 1543  N   GLY A1023    12123  13753  15498   2586  -2436   2704       N\\nATOM   1544  CA  GLY A1023      48.156  -9.536  47.793  1.00110.44           C\\nANISOU 1544  CA  GLY A1023    11736  14212  16013   2619  -2755   2653       C\\nATOM   1545  C   GLY A1023      48.709  -8.632  46.710  1.00113.05           C\\nANISOU 1545  C   GLY A1023    11548  14751  16654   2465  -2360   2382       C\\nATOM   1546  O   GLY A1023      49.639  -7.862  46.986  1.00112.39           O\\nANISOU 1546  O   GLY A1023    10982  14921  16798   2361  -2597   2323       O\\nATOM   1547  N   TYR A1024      48.174  -8.700  45.495  1.00108.30           N\\nANISOU 1547  N   TYR A1024    11043  14058  16046   2411  -1784   2230       N\\nATOM   1548  CA  TYR A1024      48.663  -7.880  44.398  1.00113.34           C\\nANISOU 1548  CA  TYR A1024    11259  14900  16907   2217  -1372   2019       C\\nATOM   1549  C   TYR A1024      48.186  -6.439  44.545  1.00111.52           C\\nANISOU 1549  C   TYR A1024    11170  14816  16386   1738  -1381   1979       C\\nATOM   1550  O   TYR A1024      47.084  -6.173  45.033  1.00110.91           O\\nANISOU 1550  O   TYR A1024    11615  14645  15882   1574  -1459   2021       O\\nATOM   1551  CB  TYR A1024      48.188  -8.447  43.060  1.00116.94           C\\nANISOU 1551  CB  TYR A1024    11856  15216  17360   2297   -787   1879       C\\nATOM   1552  CG  TYR A1024      48.578  -9.890  42.820  1.00122.30           C\\nANISOU 1552  CG  TYR A1024    12446  15674  18349   2790   -744   1850       C\\nATOM   1553  CD1 TYR A1024      49.830 -10.364  43.189  1.00128.61           C\\nANISOU 1553  CD1 TYR A1024    12689  16530  19645   3150  -1024   1848       C\\nATOM   1554  CD2 TYR A1024      47.689 -10.779  42.227  1.00118.01           C\\nANISOU 1554  CD2 TYR A1024    12364  14836  17638   2906   -460   1804       C\\nATOM   1555  CE1 TYR A1024      50.188 -11.681  42.970  1.00131.77           C\\nANISOU 1555  CE1 TYR A1024    13011  16664  20391   3655  -1019   1793       C\\nATOM   1556  CE2 TYR A1024      48.037 -12.096  42.004  1.00120.38           C\\nANISOU 1556  CE2 TYR A1024    12621  14859  18257   3363   -444   1744       C\\nATOM   1557  CZ  TYR A1024      49.287 -12.542  42.377  1.00129.11           C\\nANISOU 1557  CZ  TYR A1024    13187  15991  19879   3758   -723   1736       C\\nATOM   1558  OH  TYR A1024      49.639 -13.855  42.158  1.00133.04           O\\nANISOU 1558  OH  TYR A1024    13642  16152  20756   4269   -742   1651       O\\nATOM   1559  N   TYR A1025      49.029  -5.504  44.113  1.00117.71           N\\nANISOU 1559  N   TYR A1025    11469  15821  17433   1507  -1294   1881       N\\nATOM   1560  CA  TYR A1025      48.682  -4.087  44.152  1.00110.35           C\\nANISOU 1560  CA  TYR A1025    10659  14955  16314   1049  -1319   1834       C\\nATOM   1561  C   TYR A1025      47.758  -3.760  42.985  1.00104.43           C\\nANISOU 1561  C   TYR A1025    10246  14092  15339    855   -821   1781       C\\nATOM   1562  O   TYR A1025      48.115  -3.979  41.822  1.00101.17           O\\nANISOU 1562  O   TYR A1025     9617  13740  15082    859   -384   1729       O\\nATOM   1563  CB  TYR A1025      49.939  -3.221  44.101  1.00111.84           C\\nANISOU 1563  CB  TYR A1025    10220  15385  16890    814  -1427   1782       C\\nATOM   1564  CG  TYR A1025      50.892  -3.432  45.257  1.00115.51           C\\nANISOU 1564  CG  TYR A1025    10303  15992  17595    978  -1998   1822       C\\nATOM   1565  CD1 TYR A1025      50.776  -2.688  46.423  1.00114.38           C\\nANISOU 1565  CD1 TYR A1025    10332  15875  17252    775  -2517   1825       C\\nATOM   1566  CD2 TYR A1025      51.915  -4.369  45.177  1.00120.42           C\\nANISOU 1566  CD2 TYR A1025    10384  16722  18646   1352  -2046   1830       C\\nATOM   1567  CE1 TYR A1025      51.647  -2.875  47.481  1.00116.89           C\\nANISOU 1567  CE1 TYR A1025    10328  16345  17742    906  -3095   1869       C\\nATOM   1568  CE2 TYR A1025      52.791  -4.563  46.228  1.00124.27           C\\nANISOU 1568  CE2 TYR A1025    10509  17338  19372   1522  -2643   1887       C\\nATOM   1569  CZ  TYR A1025      52.653  -3.813  47.377  1.00124.31           C\\nANISOU 1569  CZ  TYR A1025    10724  17386  19121   1279  -3180   1923       C\\nATOM   1570  OH  TYR A1025      53.523  -4.004  48.428  1.00131.17           O\\nANISOU 1570  OH  TYR A1025    11258  18402  20177   1430  -3829   1986       O\\nATOM   1571  N   THR A1026      46.569  -3.247  43.288  1.00104.70           N\\nANISOU 1571  N   THR A1026    10799  13985  14997    692   -893   1776       N\\nATOM   1572  CA  THR A1026      45.596  -2.892  42.268  1.00105.81           C\\nANISOU 1572  CA  THR A1026    11282  14002  14919    524   -528   1739       C\\nATOM   1573  C   THR A1026      45.108  -1.467  42.499  1.00102.55           C\\nANISOU 1573  C   THR A1026    11058  13525  14382    179   -701   1694       C\\nATOM   1574  O   THR A1026      45.449  -0.819  43.493  1.00 98.86           O\\nANISOU 1574  O   THR A1026    10500  13102  13962     75  -1083   1653       O\\nATOM   1575  CB  THR A1026      44.400  -3.858  42.255  1.00102.47           C\\nANISOU 1575  CB  THR A1026    11323  13413  14198    735   -413   1745       C\\nATOM   1576  OG1 THR A1026      43.497  -3.517  43.312  1.00 98.43           O\\nANISOU 1576  OG1 THR A1026    11152  12846  13400    677   -704   1728       O\\nATOM   1577  CG2 THR A1026      44.861  -5.301  42.437  1.00103.30           C\\nANISOU 1577  CG2 THR A1026    11315  13487  14447   1108   -410   1798       C\\nATOM   1578  N   ILE A1027      44.296  -0.982  41.560  1.00 99.57           N\\nANISOU 1578  N   ILE A1027    10963  13018  13850     15   -450   1686       N\\nATOM   1579  CA  ILE A1027      43.734   0.361  41.638  1.00 94.27           C\\nANISOU 1579  CA  ILE A1027    10513  12198  13107   -265   -621   1637       C\\nATOM   1580  C   ILE A1027      42.483   0.419  40.770  1.00 89.78           C\\nANISOU 1580  C   ILE A1027    10350  11463  12301   -276   -407   1635       C\\nATOM   1581  O   ILE A1027      42.233  -0.483  39.962  1.00 86.52           O\\nANISOU 1581  O   ILE A1027    10008  11080  11787   -145    -97   1677       O\\nATOM   1582  CB  ILE A1027      44.771   1.417  41.213  1.00 89.65           C\\nANISOU 1582  CB  ILE A1027     9615  11643  12803   -620   -639   1700       C\\nATOM   1583  CG1 ILE A1027      44.397   2.796  41.761  1.00 84.69           C\\nANISOU 1583  CG1 ILE A1027     9187  10803  12189   -869   -988   1614       C\\nATOM   1584  CG2 ILE A1027      44.914   1.453  39.698  1.00 80.58           C\\nANISOU 1584  CG2 ILE A1027     8450  10512  11654   -794   -204   1829       C\\nATOM   1585  CD1 ILE A1027      45.403   3.866  41.434  1.00 82.74           C\\nANISOU 1585  CD1 ILE A1027     8667  10528  12241  -1282  -1056   1694       C\\nATOM   1586  N   GLY A1028      41.681   1.469  40.938  1.00 90.15           N\\nANISOU 1586  N   GLY A1028    10659  11318  12274   -414   -605   1560       N\\nATOM   1587  CA  GLY A1028      40.491   1.617  40.118  1.00 84.64           C\\nANISOU 1587  CA  GLY A1028    10306  10458  11396   -412   -482   1559       C\\nATOM   1588  C   GLY A1028      39.429   0.607  40.504  1.00 83.32           C\\nANISOU 1588  C   GLY A1028    10333  10329  10994   -142   -422   1455       C\\nATOM   1589  O   GLY A1028      39.140   0.390  41.685  1.00 81.04           O\\nANISOU 1589  O   GLY A1028    10066  10102  10624    -17   -599   1333       O\\nATOM   1590  N   ILE A1029      38.832  -0.021  39.494  1.00 90.61           N\\nANISOU 1590  N   ILE A1029    11415  11232  11782    -90   -168   1506       N\\nATOM   1591  CA  ILE A1029      37.857  -1.077  39.728  1.00 88.98           C\\nANISOU 1591  CA  ILE A1029    11375  11052  11381    109    -82   1426       C\\nATOM   1592  C   ILE A1029      38.467  -2.405  39.306  1.00 96.86           C\\nANISOU 1592  C   ILE A1029    12278  12138  12386    239    180   1504       C\\nATOM   1593  O   ILE A1029      38.305  -2.841  38.160  1.00 98.47           O\\nANISOU 1593  O   ILE A1029    12577  12322  12515    224    426   1527       O\\nATOM   1594  CB  ILE A1029      36.538  -0.812  38.980  1.00 75.33           C\\nANISOU 1594  CB  ILE A1029     9908   9202   9511     82    -63   1368       C\\nATOM   1595  CG1 ILE A1029      35.978   0.560  39.350  1.00 71.56           C\\nANISOU 1595  CG1 ILE A1029     9501   8581   9108     11   -352   1261       C\\nATOM   1596  CG2 ILE A1029      35.522  -1.900  39.298  1.00 63.88           C\\nANISOU 1596  CG2 ILE A1029     8583   7799   7889    229     23   1272       C\\nATOM   1597  CD1 ILE A1029      34.589   0.806  38.813  1.00 68.30           C\\nANISOU 1597  CD1 ILE A1029     9287   8054   8610     55   -413   1168       C\\nATOM   1598  N   GLY A1030      39.179  -3.050  40.226  1.00 99.15           N\\nANISOU 1598  N   GLY A1030    12396  12511  12765    380    101   1529       N\\nATOM   1599  CA  GLY A1030      39.787  -4.335  39.947  1.00 98.18           C\\nANISOU 1599  CA  GLY A1030    12171  12410  12722    571    291   1577       C\\nATOM   1600  C   GLY A1030      40.760  -4.288  38.789  1.00 94.57           C\\nANISOU 1600  C   GLY A1030    11485  12025  12421    523    562   1598       C\\nATOM   1601  O   GLY A1030      40.506  -4.869  37.728  1.00 95.69           O\\nANISOU 1601  O   GLY A1030    11749  12138  12469    550    849   1553       O\\nATOM   1602  N   HIS A1031      41.878  -3.592  38.977  1.00 87.03           N\\nANISOU 1602  N   HIS A1031    10189  11192  11687    421    486   1644       N\\nATOM   1603  CA  HIS A1031      42.893  -3.436  37.938  1.00 89.86           C\\nANISOU 1603  CA  HIS A1031    10256  11692  12196    312    785   1660       C\\nATOM   1604  C   HIS A1031      44.259  -3.687  38.565  1.00 92.16           C\\nANISOU 1604  C   HIS A1031    10046  12138  12831    439    693   1664       C\\nATOM   1605  O   HIS A1031      44.848  -2.781  39.162  1.00 95.75           O\\nANISOU 1605  O   HIS A1031    10270  12666  13443    260    450   1711       O\\nATOM   1606  CB  HIS A1031      42.821  -2.053  37.308  1.00 89.34           C\\nANISOU 1606  CB  HIS A1031    10256  11621  12066    -69    797   1742       C\\nATOM   1607  CG  HIS A1031      43.762  -1.865  36.161  1.00 92.70           C\\nANISOU 1607  CG  HIS A1031    10434  12232  12556   -271   1167   1789       C\\nATOM   1608  ND1 HIS A1031      43.332  -1.784  34.855  1.00 93.45           N\\nANISOU 1608  ND1 HIS A1031    10789  12339  12379   -440   1471   1824       N\\nATOM   1609  CD2 HIS A1031      45.109  -1.748  36.123  1.00 96.67           C\\nANISOU 1609  CD2 HIS A1031    10434  12956  13341   -356   1297   1798       C\\nATOM   1610  CE1 HIS A1031      44.375  -1.621  34.061  1.00 97.80           C\\nANISOU 1610  CE1 HIS A1031    11037  13125  12996   -641   1814   1858       C\\nATOM   1611  NE2 HIS A1031      45.465  -1.597  34.805  1.00100.11           N\\nANISOU 1611  NE2 HIS A1031    10830  13554  13654   -592   1731   1833       N\\nATOM   1612  N   LEU A1032      44.761  -4.912  38.422  1.00 91.24           N\\nANISOU 1612  N   LEU A1032     9754  12051  12863    756    853   1596       N\\nATOM   1613  CA  LEU A1032      46.058  -5.267  38.982  1.00 95.11           C\\nANISOU 1613  CA  LEU A1032     9720  12682  13737    952    730   1587       C\\nATOM   1614  C   LEU A1032      47.161  -4.499  38.265  1.00 99.71           C\\nANISOU 1614  C   LEU A1032     9815  13531  14540    697    975   1562       C\\nATOM   1615  O   LEU A1032      47.347  -4.649  37.054  1.00 96.96           O\\nANISOU 1615  O   LEU A1032     9403  13297  14140    624   1442   1479       O\\nATOM   1616  CB  LEU A1032      46.290  -6.772  38.868  1.00 93.50           C\\nANISOU 1616  CB  LEU A1032     9457  12381  13686   1392    849   1495       C\\nATOM   1617  N   LEU A1033      47.887  -3.667  39.013  1.00 97.35           N\\nANISOU 1617  N   LEU A1033     9181  13349  14459    521    666   1628       N\\nATOM   1618  CA  LEU A1033      49.025  -2.964  38.434  1.00104.31           C\\nANISOU 1618  CA  LEU A1033     9528  14502  15604    230    883   1619       C\\nATOM   1619  C   LEU A1033      50.158  -3.934  38.121  1.00112.65           C\\nANISOU 1619  C   LEU A1033     9983  15786  17034    550   1131   1473       C\\nATOM   1620  O   LEU A1033      50.737  -3.897  37.029  1.00115.99           O\\nANISOU 1620  O   LEU A1033    10102  16446  17521    410   1635   1381       O\\nATOM   1621  CB  LEU A1033      49.494  -1.861  39.381  1.00103.46           C\\nANISOU 1621  CB  LEU A1033     9213  14430  15668    -55    434   1699       C\\nATOM   1622  N   THR A1034      50.477  -4.818  39.064  1.00114.71           N\\nANISOU 1622  N   THR A1034    10071  15980  17534    990    782   1443       N\\nATOM   1623  CA  THR A1034      51.514  -5.822  38.866  1.00119.05           C\\nANISOU 1623  CA  THR A1034    10043  16677  18514   1403    933   1278       C\\nATOM   1624  C   THR A1034      51.333  -6.919  39.904  1.00116.13           C\\nANISOU 1624  C   THR A1034     9831  16045  18250   1915    470   1326       C\\nATOM   1625  O   THR A1034      50.615  -6.756  40.893  1.00112.94           O\\nANISOU 1625  O   THR A1034     9869  15449  17593   1873     24   1499       O\\nATOM   1626  CB  THR A1034      52.919  -5.218  38.968  1.00123.11           C\\nANISOU 1626  CB  THR A1034     9729  17558  19489   1237    901   1232       C\\nATOM   1627  OG1 THR A1034      53.898  -6.241  38.746  1.00127.31           O\\nANISOU 1627  OG1 THR A1034     9644  18240  20490   1707   1059   1022       O\\nATOM   1628  CG2 THR A1034      53.135  -4.617  40.344  1.00124.58           C\\nANISOU 1628  CG2 THR A1034     9836  17714  19783   1140    210   1384       C\\nATOM   1629  N   LYS A1035      51.998  -8.046  39.660  1.00124.24           N\\nANISOU 1629  N   LYS A1035    10499  17061  19647   2398    588   1165       N\\nATOM   1630  CA  LYS A1035      52.071  -9.132  40.624  1.00115.60           C\\nANISOU 1630  CA  LYS A1035     9471  15694  18757   2910    100   1245       C\\nATOM   1631  C   LYS A1035      53.350  -9.089  41.448  1.00124.45           C\\nANISOU 1631  C   LYS A1035     9878  17011  20395   3112   -361   1270       C\\nATOM   1632  O   LYS A1035      53.591 -10.004  42.241  1.00126.86           O\\nANISOU 1632  O   LYS A1035    10167  17100  20932   3572   -826   1360       O\\nATOM   1633  CB  LYS A1035      51.953 -10.483  39.911  1.00108.04           C\\nANISOU 1633  CB  LYS A1035     8621  14489  17940   3381    417   1046       C\\nATOM   1634  N   SER A1036      54.169  -8.044  41.282  1.00124.75           N\\nANISOU 1634  N   SER A1036     9333  17441  20626   2756   -279   1212       N\\nATOM   1635  CA  SER A1036      55.429  -7.892  41.994  1.00130.16           C\\nANISOU 1635  CA  SER A1036     9248  18374  21834   2880   -717   1205       C\\nATOM   1636  C   SER A1036      55.191  -7.369  43.411  1.00127.51           C\\nANISOU 1636  C   SER A1036     9199  17961  21290   2719  -1470   1465       C\\nATOM   1637  O   SER A1036      54.249  -6.611  43.652  1.00124.62           O\\nANISOU 1637  O   SER A1036     9437  17497  20415   2316  -1507   1585       O\\nATOM   1638  CB  SER A1036      56.351  -6.937  41.243  1.00133.68           C\\nANISOU 1638  CB  SER A1036     8966  19280  22547   2465   -307   1043       C\\nATOM   1639  N   PRO A1037      56.041  -7.758  44.369  1.00132.59           N\\nANISOU 1639  N   PRO A1037     9408  18656  22314   3043  -2094   1531       N\\nATOM   1640  CA  PRO A1037      55.818  -7.332  45.758  1.00131.46           C\\nANISOU 1640  CA  PRO A1037     9590  18465  21895   2895  -2836   1763       C\\nATOM   1641  C   PRO A1037      56.251  -5.907  46.050  1.00131.07           C\\nANISOU 1641  C   PRO A1037     9233  18724  21845   2324  -3004   1723       C\\nATOM   1642  O   PRO A1037      55.767  -5.327  47.031  1.00128.15           O\\nANISOU 1642  O   PRO A1037     9314  18300  21079   2075  -3470   1849       O\\nATOM   1643  CB  PRO A1037      56.658  -8.330  46.564  1.00137.89           C\\nANISOU 1643  CB  PRO A1037    10022  19225  23144   3474  -3467   1855       C\\nATOM   1644  CG  PRO A1037      57.788  -8.659  45.647  1.00141.32           C\\nANISOU 1644  CG  PRO A1037     9525  19887  24282   3748  -3098   1581       C\\nATOM   1645  CD  PRO A1037      57.205  -8.654  44.250  1.00138.32           C\\nANISOU 1645  CD  PRO A1037     9352  19476  23728   3597  -2186   1384       C\\nATOM   1646  N   SER A1038      57.142  -5.329  45.249  1.00134.97           N\\nANISOU 1646  N   SER A1038     8987  19535  22758   2087  -2636   1539       N\\nATOM   1647  CA  SER A1038      57.615  -3.977  45.512  1.00138.82           C\\nANISOU 1647  CA  SER A1038     9165  20272  23307   1497  -2818   1510       C\\nATOM   1648  C   SER A1038      56.508  -2.965  45.234  1.00142.03           C\\nANISOU 1648  C   SER A1038    10304  20506  23157    966  -2548   1556       C\\nATOM   1649  O   SER A1038      55.905  -2.966  44.156  1.00142.81           O\\nANISOU 1649  O   SER A1038    10685  20515  23061    864  -1905   1526       O\\nATOM   1650  CB  SER A1038      58.845  -3.669  44.659  1.00137.97           C\\nANISOU 1650  CB  SER A1038     8060  20560  23801   1331  -2429   1322       C\\nATOM   1651  N   LEU A1039      56.235  -2.105  46.219  1.00148.93           N\\nANISOU 1651  N   LEU A1039    11491  21326  23772    647  -3071   1607       N\\nATOM   1652  CA  LEU A1039      55.237  -1.059  46.027  1.00137.41           C\\nANISOU 1652  CA  LEU A1039    10670  19674  21866    176  -2887   1609       C\\nATOM   1653  C   LEU A1039      55.728  -0.005  45.042  1.00134.86           C\\nANISOU 1653  C   LEU A1039     9968  19484  21790   -372  -2464   1547       C\\nATOM   1654  O   LEU A1039      54.942   0.522  44.246  1.00128.51           O\\nANISOU 1654  O   LEU A1039     9617  18504  20707   -648  -2029   1577       O\\nATOM   1655  CB  LEU A1039      54.882  -0.422  47.371  1.00133.76           C\\nANISOU 1655  CB  LEU A1039    10606  19126  21088      8  -3557   1606       C\\nATOM   1656  CG  LEU A1039      53.969   0.807  47.351  1.00123.44           C\\nANISOU 1656  CG  LEU A1039     9880  17606  19417   -461  -3487   1537       C\\nATOM   1657  CD1 LEU A1039      52.634   0.486  46.697  1.00115.73           C\\nANISOU 1657  CD1 LEU A1039     9575  16373  18024   -334  -3002   1586       C\\nATOM   1658  CD2 LEU A1039      53.766   1.349  48.759  1.00121.51           C\\nANISOU 1658  CD2 LEU A1039     9948  17332  18887   -575  -4163   1451       C\\nATOM   1659  N   ASN A1040      57.027   0.309  45.078  1.00140.78           N\\nANISOU 1659  N   ASN A1040     9881  20545  23065   -557  -2602   1481       N\\nATOM   1660  CA  ASN A1040      57.584   1.273  44.135  1.00137.59           C\\nANISOU 1660  CA  ASN A1040     9069  20297  22910  -1145  -2171   1458       C\\nATOM   1661  C   ASN A1040      57.424   0.803  42.695  1.00142.78           C\\nANISOU 1661  C   ASN A1040     9696  21027  23528  -1086  -1335   1468       C\\nATOM   1662  O   ASN A1040      57.214   1.623  41.793  1.00129.49           O\\nANISOU 1662  O   ASN A1040     8176  19309  21715  -1595   -895   1536       O\\nATOM   1663  CB  ASN A1040      59.058   1.528  44.452  1.00137.97           C\\nANISOU 1663  CB  ASN A1040     8117  20728  23578  -1326  -2453   1368       C\\nATOM   1664  N   ALA A1041      57.513  -0.508  42.459  1.00141.43           N\\nANISOU 1664  N   ALA A1041     9359  20933  23447   -478  -1132   1401       N\\nATOM   1665  CA  ALA A1041      57.326  -1.032  41.111  1.00146.42           C\\nANISOU 1665  CA  ALA A1041    10009  21635  23988   -388   -344   1347       C\\nATOM   1666  C   ALA A1041      55.865  -0.980  40.683  1.00137.93           C\\nANISOU 1666  C   ALA A1041     9919  20195  22294   -425   -117   1454       C\\nATOM   1667  O   ALA A1041      55.576  -0.783  39.497  1.00137.36           O\\nANISOU 1667  O   ALA A1041    10016  20159  22015   -671    490   1467       O\\nATOM   1668  CB  ALA A1041      57.852  -2.465  41.023  1.00155.04           C\\nANISOU 1668  CB  ALA A1041    10644  22857  25406    310   -239   1186       C\\nATOM   1669  N   ALA A1042      54.935  -1.157  41.626  1.00140.82           N\\nANISOU 1669  N   ALA A1042    10925  20238  22341   -200   -595   1527       N\\nATOM   1670  CA  ALA A1042      53.519  -1.060  41.288  1.00132.90           C\\nANISOU 1670  CA  ALA A1042    10790  18913  20795   -244   -420   1604       C\\nATOM   1671  C   ALA A1042      53.142   0.352  40.863  1.00133.14           C\\nANISOU 1671  C   ALA A1042    11109  18838  20640   -869   -326   1693       C\\nATOM   1672  O   ALA A1042      52.205   0.531  40.075  1.00130.01           O\\nANISOU 1672  O   ALA A1042    11253  18260  19885   -986      1   1755       O\\nATOM   1673  CB  ALA A1042      52.662  -1.505  42.472  1.00126.18           C\\nANISOU 1673  CB  ALA A1042    10481  17801  19659     81   -937   1646       C\\nATOM   1674  N   LYS A1043      53.853   1.361  41.370  1.00137.98           N\\nANISOU 1674  N   LYS A1043    11384  19531  21510  -1275   -652   1703       N\\nATOM   1675  CA  LYS A1043      53.613   2.736  40.950  1.00131.35           C\\nANISOU 1675  CA  LYS A1043    10799  18530  20579  -1894   -598   1802       C\\nATOM   1676  C   LYS A1043      54.204   3.022  39.577  1.00133.43           C\\nANISOU 1676  C   LYS A1043    10730  19015  20952  -2291     34   1891       C\\nATOM   1677  O   LYS A1043      53.705   3.899  38.864  1.00133.13           O\\nANISOU 1677  O   LYS A1043    11108  18782  20694  -2733    227   2044       O\\nATOM   1678  CB  LYS A1043      54.192   3.713  41.976  1.00128.92           C\\nANISOU 1678  CB  LYS A1043    10263  18193  20526  -2230  -1186   1758       C\\nATOM   1679  CG  LYS A1043      53.569   3.618  43.359  1.00124.36           C\\nANISOU 1679  CG  LYS A1043    10090  17422  19739  -1936  -1811   1654       C\\nATOM   1680  CD  LYS A1043      54.054   4.744  44.258  1.00124.45           C\\nANISOU 1680  CD  LYS A1043     9973  17371  19941  -2345  -2374   1565       C\\nATOM   1681  CE  LYS A1043      53.301   4.761  45.577  1.00122.13           C\\nANISOU 1681  CE  LYS A1043    10189  16897  19319  -2105  -2935   1426       C\\nATOM   1682  NZ  LYS A1043      53.698   5.919  46.425  1.00124.65           N\\nANISOU 1682  NZ  LYS A1043    10461  17121  19779  -2520  -3485   1275       N\\nATOM   1683  N   SER A1044      55.263   2.305  39.194  1.00130.51           N\\nANISOU 1683  N   SER A1044     9619  19057  20914  -2142    357   1795       N\\nATOM   1684  CA  SER A1044      55.858   2.511  37.879  1.00137.15           C\\nANISOU 1684  CA  SER A1044    10108  20197  21806  -2533   1041   1845       C\\nATOM   1685  C   SER A1044      54.904   2.086  36.770  1.00136.57           C\\nANISOU 1685  C   SER A1044    10643  20016  21232  -2427   1563   1899       C\\nATOM   1686  O   SER A1044      54.789   2.771  35.747  1.00141.22           O\\nANISOU 1686  O   SER A1044    11441  20628  21589  -2937   1967   2067       O\\nATOM   1687  CB  SER A1044      57.179   1.749  37.775  1.00143.25           C\\nANISOU 1687  CB  SER A1044     9888  21468  23072  -2311   1285   1648       C\\nATOM   1688  N   GLU A1045      54.211   0.960  36.954  1.00136.81           N\\nANISOU 1688  N   GLU A1045    10988  19917  21076  -1800   1534   1777       N\\nATOM   1689  CA  GLU A1045      53.243   0.521  35.955  1.00129.18           C\\nANISOU 1689  CA  GLU A1045    10619  18832  19631  -1695   1960   1797       C\\nATOM   1690  C   GLU A1045      52.010   1.415  35.939  1.00128.34           C\\nANISOU 1690  C   GLU A1045    11333  18313  19118  -1974   1718   2002       C\\nATOM   1691  O   GLU A1045      51.383   1.582  34.887  1.00126.75           O\\nANISOU 1691  O   GLU A1045    11575  18053  18531  -2171   2069   2109       O\\nATOM   1692  CB  GLU A1045      52.847  -0.934  36.210  1.00121.20           C\\nANISOU 1692  CB  GLU A1045     9714  17751  18586   -982   1950   1604       C\\nATOM   1693  N   LEU A1046      51.650   1.998  37.088  1.00131.91           N\\nANISOU 1693  N   LEU A1046    11988  18485  19645  -1980   1106   2037       N\\nATOM   1694  CA  LEU A1046      50.490   2.885  37.146  1.00126.43           C\\nANISOU 1694  CA  LEU A1046    12012  17383  18643  -2189    846   2169       C\\nATOM   1695  C   LEU A1046      50.730   4.156  36.342  1.00134.52           C\\nANISOU 1695  C   LEU A1046    13116  18345  19652  -2860    993   2395       C\\nATOM   1696  O   LEU A1046      49.873   4.579  35.558  1.00138.35           O\\nANISOU 1696  O   LEU A1046    14165  18604  19797  -3036   1114   2555       O\\nATOM   1697  CB  LEU A1046      50.156   3.227  38.600  1.00114.87           C\\nANISOU 1697  CB  LEU A1046    10689  15684  17273  -2043    195   2081       C\\nATOM   1698  CG  LEU A1046      49.189   4.395  38.827  1.00103.62           C\\nANISOU 1698  CG  LEU A1046     9857  13838  15674  -2297   -138   2146       C\\nATOM   1699  CD1 LEU A1046      47.828   4.107  38.217  1.00 96.31           C\\nANISOU 1699  CD1 LEU A1046     9556  12698  14341  -2097     22   2183       C\\nATOM   1700  CD2 LEU A1046      49.056   4.722  40.308  1.00 99.47           C\\nANISOU 1700  CD2 LEU A1046     9379  13170  15245  -2171   -734   1980       C\\nATOM   1701  N   ASP A1047      51.893   4.784  36.529  1.00127.49           N\\nANISOU 1701  N   ASP A1047    11667  17635  19137  -3262    951   2433       N\\nATOM   1702  CA  ASP A1047      52.188   6.012  35.801  1.00131.96           C\\nANISOU 1702  CA  ASP A1047    12311  18112  19714  -3978   1078   2692       C\\nATOM   1703  C   ASP A1047      52.444   5.742  34.324  1.00130.92           C\\nANISOU 1703  C   ASP A1047    12130  18291  19323  -4228   1792   2837       C\\nATOM   1704  O   ASP A1047      52.172   6.607  33.483  1.00133.98           O\\nANISOU 1704  O   ASP A1047    12921  18510  19475  -4745   1927   3128       O\\nATOM   1705  CB  ASP A1047      53.382   6.723  36.435  1.00141.47           C\\nANISOU 1705  CB  ASP A1047    12895  19442  21416  -4390    835   2678       C\\nATOM   1706  CG  ASP A1047      53.050   7.320  37.791  1.00139.91           C\\nANISOU 1706  CG  ASP A1047    12900  18874  21385  -4305     95   2555       C\\nATOM   1707  OD1 ASP A1047      51.910   7.125  38.263  1.00133.93           O\\nANISOU 1707  OD1 ASP A1047    12719  17809  20359  -3898   -178   2466       O\\nATOM   1708  OD2 ASP A1047      53.925   7.988  38.382  1.00142.42           O\\nANISOU 1708  OD2 ASP A1047    12791  19231  22093  -4666   -203   2522       O\\nATOM   1709  N   LYS A1048      52.958   4.557  33.986  1.00136.15           N\\nANISOU 1709  N   LYS A1048    12332  19393  20008  -3866   2239   2634       N\\nATOM   1710  CA  LYS A1048      53.156   4.211  32.584  1.00137.23           C\\nANISOU 1710  CA  LYS A1048    12447  19868  19828  -4059   2961   2691       C\\nATOM   1711  C   LYS A1048      51.836   3.990  31.855  1.00136.24           C\\nANISOU 1711  C   LYS A1048    13159  19483  19123  -3907   3045   2785       C\\nATOM   1712  O   LYS A1048      51.813   4.012  30.619  1.00135.03           O\\nANISOU 1712  O   LYS A1048    13198  19529  18579  -4209   3556   2913       O\\nATOM   1713  CB  LYS A1048      54.036   2.964  32.467  1.00137.25           C\\nANISOU 1713  CB  LYS A1048    11720  20374  20055  -3634   3395   2361       C\\nATOM   1714  N   ALA A1049      50.743   3.782  32.587  1.00134.09           N\\nANISOU 1714  N   ALA A1049    13374  18806  18767  -3471   2557   2719       N\\nATOM   1715  CA  ALA A1049      49.423   3.607  31.993  1.00136.97           C\\nANISOU 1715  CA  ALA A1049    14488  18911  18642  -3319   2551   2790       C\\nATOM   1716  C   ALA A1049      48.555   4.853  32.093  1.00139.86           C\\nANISOU 1716  C   ALA A1049    15461  18785  18895  -3629   2088   3059       C\\nATOM   1717  O   ALA A1049      47.775   5.130  31.178  1.00144.34           O\\nANISOU 1717  O   ALA A1049    16587  19202  19054  -3792   2166   3254       O\\nATOM   1718  CB  ALA A1049      48.697   2.429  32.649  1.00134.83           C\\nANISOU 1718  CB  ALA A1049    14339  18543  18349  -2619   2376   2514       C\\nATOM   1719  N   ILE A1050      48.667   5.615  33.186  1.00147.00           N\\nANISOU 1719  N   ILE A1050    16279  19419  20157  -3696   1573   3052       N\\nATOM   1720  CA  ILE A1050      47.884   6.843  33.320  1.00137.76           C\\nANISOU 1720  CA  ILE A1050    15661  17727  18955  -3954   1109   3250       C\\nATOM   1721  C   ILE A1050      48.527   8.029  32.621  1.00135.31           C\\nANISOU 1721  C   ILE A1050    15376  17334  18700  -4696   1193   3602       C\\nATOM   1722  O   ILE A1050      47.861   9.054  32.425  1.00132.09           O\\nANISOU 1722  O   ILE A1050    15513  16449  18227  -4950    855   3834       O\\nATOM   1723  CB  ILE A1050      47.649   7.192  34.802  1.00112.75           C\\nANISOU 1723  CB  ILE A1050    12459  14272  16111  -3710    512   3036       C\\nATOM   1724  N   GLY A1051      49.800   7.923  32.236  1.00128.26           N\\nANISOU 1724  N   GLY A1051    13902  16884  17947  -5058   1630   3652       N\\nATOM   1725  CA  GLY A1051      50.479   8.964  31.501  1.00126.01           C\\nANISOU 1725  CA  GLY A1051    13606  16592  17681  -5844   1802   4017       C\\nATOM   1726  C   GLY A1051      51.114  10.046  32.350  1.00125.68           C\\nANISOU 1726  C   GLY A1051    13328  16279  18144  -6255   1362   4067       C\\nATOM   1727  O   GLY A1051      52.053  10.703  31.888  1.00131.62           O\\nANISOU 1727  O   GLY A1051    13814  17166  19028  -6906   1590   4283       O\\nATOM   1728  N   ARG A1052      50.638  10.250  33.572  1.00125.39           N\\nANISOU 1728  N   ARG A1052    13398  15875  18368  -5892    754   3830       N\\nATOM   1729  CA  ARG A1052      51.137  11.295  34.452  1.00130.48           C\\nANISOU 1729  CA  ARG A1052    13895  16207  19473  -6249    261   3810       C\\nATOM   1730  C   ARG A1052      51.879  10.681  35.633  1.00133.64           C\\nANISOU 1730  C   ARG A1052    13610  16936  20230  -5922     98   3432       C\\nATOM   1731  O   ARG A1052      51.880   9.465  35.836  1.00139.15           O\\nANISOU 1731  O   ARG A1052    14025  18014  20831  -5363    306   3204       O\\nATOM   1732  CB  ARG A1052      49.986  12.174  34.954  1.00127.22           C\\nANISOU 1732  CB  ARG A1052    14202  15072  19066  -6123   -369   3798       C\\nATOM   1733  CG  ARG A1052      49.063  11.466  35.933  1.00118.27           C\\nANISOU 1733  CG  ARG A1052    13210  13879  17849  -5343   -664   3404       C\\nATOM   1734  CD  ARG A1052      47.922  12.363  36.372  1.00115.96           C\\nANISOU 1734  CD  ARG A1052    13565  12916  17579  -5212  -1224   3339       C\\nATOM   1735  NE  ARG A1052      47.116  11.751  37.424  1.00114.03           N\\nANISOU 1735  NE  ARG A1052    13390  12676  17262  -4541  -1477   2931       N\\nATOM   1736  CZ  ARG A1052      47.303  11.960  38.723  1.00115.93           C\\nANISOU 1736  CZ  ARG A1052    13460  12852  17737  -4403  -1881   2594       C\\nATOM   1737  NH1 ARG A1052      48.271  12.768  39.132  1.00119.81           N\\nANISOU 1737  NH1 ARG A1052    13686  13244  18594  -4875  -2117   2592       N\\nATOM   1738  NH2 ARG A1052      46.523  11.364  39.613  1.00113.10           N\\nANISOU 1738  NH2 ARG A1052    13205  12544  17222  -3834  -2048   2259       N\\nATOM   1739  N   ASN A1053      52.517  11.551  36.419  1.00125.16           N\\nANISOU 1739  N   ASN A1053    12297  15678  19580  -6291   -324   3375       N\\nATOM   1740  CA  ASN A1053      53.118  11.156  37.692  1.00123.03           C\\nANISOU 1740  CA  ASN A1053    11481  15629  19636  -6002   -663   3022       C\\nATOM   1741  C   ASN A1053      52.002  11.117  38.731  1.00122.77           C\\nANISOU 1741  C   ASN A1053    11968  15217  19462  -5447  -1194   2750       C\\nATOM   1742  O   ASN A1053      51.786  12.056  39.502  1.00122.02           O\\nANISOU 1742  O   ASN A1053    12131  14690  19541  -5602  -1734   2626       O\\nATOM   1743  CB  ASN A1053      54.234  12.115  38.089  1.00126.67           C\\nANISOU 1743  CB  ASN A1053    11485  16063  20583  -6663   -923   3047       C\\nATOM   1744  N   THR A1054      51.272   9.995  38.739  1.00124.33           N\\nANISOU 1744  N   THR A1054    12319  15587  19333  -4804  -1013   2632       N\\nATOM   1745  CA  THR A1054      50.060   9.901  39.547  1.00119.55           C\\nANISOU 1745  CA  THR A1054    12244  14668  18513  -4306  -1394   2406       C\\nATOM   1746  C   THR A1054      50.366   9.947  41.037  1.00119.71           C\\nANISOU 1746  C   THR A1054    12048  14716  18720  -4133  -1918   2083       C\\nATOM   1747  O   THR A1054      49.504  10.334  41.835  1.00120.96           O\\nANISOU 1747  O   THR A1054    12645  14548  18764  -3922  -2315   1863       O\\nATOM   1748  CB  THR A1054      49.295   8.620  39.212  1.00115.03           C\\nANISOU 1748  CB  THR A1054    11827  14310  17568  -3728  -1059   2370       C\\nATOM   1749  N   ASN A1055      51.577   9.556  41.433  1.00118.97           N\\nANISOU 1749  N   ASN A1055    11271  15030  18901  -4213  -1934   2029       N\\nATOM   1750  CA  ASN A1055      52.004   9.557  42.830  1.00116.22           C\\nANISOU 1750  CA  ASN A1055    10681  14771  18707  -4084  -2473   1748       C\\nATOM   1751  C   ASN A1055      51.115   8.687  43.711  1.00119.38           C\\nANISOU 1751  C   ASN A1055    11395  15214  18750  -3437  -2650   1539       C\\nATOM   1752  O   ASN A1055      51.131   8.822  44.935  1.00121.96           O\\nANISOU 1752  O   ASN A1055    11754  15533  19052  -3324  -3143   1293       O\\nATOM   1753  CB  ASN A1055      52.071  10.984  43.391  1.00109.11           C\\nANISOU 1753  CB  ASN A1055     9992  13444  18023  -4552  -2980   1627       C\\nATOM   1754  N   GLY A1056      50.340   7.783  43.111  1.00115.78           N\\nANISOU 1754  N   GLY A1056    11183  14819  17987  -3045  -2253   1632       N\\nATOM   1755  CA  GLY A1056      49.518   6.838  43.832  1.00115.99           C\\nANISOU 1755  CA  GLY A1056    11480  14915  17677  -2485  -2341   1489       C\\nATOM   1756  C   GLY A1056      48.027   7.076  43.671  1.00112.88           C\\nANISOU 1756  C   GLY A1056    11762  14182  16944  -2317  -2293   1431       C\\nATOM   1757  O   GLY A1056      47.247   6.120  43.742  1.00109.86           O\\nANISOU 1757  O   GLY A1056    11592  13885  16264  -1902  -2132   1408       O\\nATOM   1758  N   VAL A1057      47.618   8.323  43.454  1.00113.85           N\\nANISOU 1758  N   VAL A1057    12208  13906  17145  -2632  -2448   1405       N\\nATOM   1759  CA  VAL A1057      46.211   8.699  43.361  1.00103.36           C\\nANISOU 1759  CA  VAL A1057    11467  12226  15579  -2456  -2483   1304       C\\nATOM   1760  C   VAL A1057      45.881   9.003  41.907  1.00105.21           C\\nANISOU 1760  C   VAL A1057    11904  12256  15814  -2653  -2149   1598       C\\nATOM   1761  O   VAL A1057      46.708   9.560  41.176  1.00111.08           O\\nANISOU 1761  O   VAL A1057    12459  12960  16785  -3103  -2041   1831       O\\nATOM   1762  CB  VAL A1057      45.900   9.912  44.260  1.00 96.42           C\\nANISOU 1762  CB  VAL A1057    10853  10979  14804  -2591  -2980   1005       C\\nATOM   1763  N   ILE A1058      44.667   8.639  41.488  1.00104.59           N\\nANISOU 1763  N   ILE A1058    12209  12071  15459  -2350  -1994   1597       N\\nATOM   1764  CA  ILE A1058      44.203   8.889  40.131  1.00100.91           C\\nANISOU 1764  CA  ILE A1058    12012  11414  14916  -2498  -1744   1872       C\\nATOM   1765  C   ILE A1058      42.794   9.466  40.170  1.00 98.60           C\\nANISOU 1765  C   ILE A1058    12224  10714  14524  -2295  -1978   1737       C\\nATOM   1766  O   ILE A1058      42.091   9.405  41.182  1.00 92.24           O\\nANISOU 1766  O   ILE A1058    11523   9875  13648  -1976  -2199   1403       O\\nATOM   1767  CB  ILE A1058      44.229   7.619  39.253  1.00 94.08           C\\nANISOU 1767  CB  ILE A1058    11024  10914  13808  -2321  -1243   2041       C\\nATOM   1768  CG1 ILE A1058      43.313   6.543  39.831  1.00 82.54           C\\nANISOU 1768  CG1 ILE A1058     9675   9599  12089  -1804  -1208   1830       C\\nATOM   1769  CG2 ILE A1058      45.650   7.101  39.083  1.00 91.55           C\\nANISOU 1769  CG2 ILE A1058    10149  10986  13649  -2498   -980   2147       C\\nATOM   1770  CD1 ILE A1058      43.175   5.325  38.950  1.00 80.94           C\\nANISOU 1770  CD1 ILE A1058     9440   9653  11661  -1618   -764   1951       C\\nATOM   1771  N   THR A1059      42.391  10.038  39.038  1.00100.27           N\\nANISOU 1771  N   THR A1059    12740  10636  14723  -2488  -1928   2000       N\\nATOM   1772  CA  THR A1059      41.046  10.571  38.887  1.00100.12           C\\nANISOU 1772  CA  THR A1059    13164  10218  14658  -2267  -2166   1907       C\\nATOM   1773  C   THR A1059      40.043   9.431  38.714  1.00 93.93           C\\nANISOU 1773  C   THR A1059    12445   9697  13549  -1832  -1928   1816       C\\nATOM   1774  O   THR A1059      40.390   8.322  38.302  1.00 93.12           O\\nANISOU 1774  O   THR A1059    12152   9988  13239  -1781  -1546   1935       O\\nATOM   1775  CB  THR A1059      40.982  11.515  37.681  1.00103.74           C\\nANISOU 1775  CB  THR A1059    13952  10269  15193  -2630  -2248   2286       C\\nATOM   1776  OG1 THR A1059      42.175  12.306  37.630  1.00105.14           O\\nANISOU 1776  OG1 THR A1059    13991  10320  15636  -3159  -2321   2476       O\\nATOM   1777  CG2 THR A1059      39.778  12.440  37.771  1.00108.32           C\\nANISOU 1777  CG2 THR A1059    14955  10292  15912  -2422  -2687   2144       C\\nATOM   1778  N   LYS A1060      38.780   9.709  39.047  1.00 98.18           N\\nANISOU 1778  N   LYS A1060    13229  10001  14072  -1515  -2161   1570       N\\nATOM   1779  CA  LYS A1060      37.721   8.768  38.697  1.00 98.24           C\\nANISOU 1779  CA  LYS A1060    13319  10201  13806  -1182  -1964   1522       C\\nATOM   1780  C   LYS A1060      37.594   8.635  37.188  1.00 99.60           C\\nANISOU 1780  C   LYS A1060    13688  10335  13819  -1346  -1790   1903       C\\nATOM   1781  O   LYS A1060      37.139   7.599  36.688  1.00 95.67           O\\nANISOU 1781  O   LYS A1060    13192  10106  13053  -1183  -1519   1935       O\\nATOM   1782  CB  LYS A1060      36.389   9.207  39.307  1.00 93.38           C\\nANISOU 1782  CB  LYS A1060    12863   9359  13257   -838  -2249   1162       C\\nATOM   1783  N   ASP A1061      37.997   9.671  36.449  1.00103.09           N\\nANISOU 1783  N   ASP A1061    14329  10441  14400  -1703  -1952   2200       N\\nATOM   1784  CA  ASP A1061      38.006   9.603  34.993  1.00101.97           C\\nANISOU 1784  CA  ASP A1061    14414  10301  14028  -1942  -1780   2607       C\\nATOM   1785  C   ASP A1061      39.176   8.768  34.485  1.00100.34           C\\nANISOU 1785  C   ASP A1061    13939  10555  13629  -2196  -1275   2797       C\\nATOM   1786  O   ASP A1061      39.012   7.961  33.563  1.00 99.43           O\\nANISOU 1786  O   ASP A1061    13894  10699  13185  -2180   -958   2926       O\\nATOM   1787  CB  ASP A1061      38.055  11.015  34.413  1.00102.76           C\\nANISOU 1787  CB  ASP A1061    14862   9863  14320  -2281  -2142   2907       C\\nATOM   1788  CG  ASP A1061      37.962  11.029  32.903  1.00102.52           C\\nANISOU 1788  CG  ASP A1061    15156   9822  13974  -2555  -2021   3367       C\\nATOM   1789  OD1 ASP A1061      36.881  10.700  32.371  1.00 98.49           O\\nANISOU 1789  OD1 ASP A1061    14872   9291  13258  -2289  -2114   3362       O\\nATOM   1790  OD2 ASP A1061      38.970  11.374  32.248  1.00105.90           O\\nANISOU 1790  OD2 ASP A1061    15607  10290  14339  -3064  -1832   3728       O\\nATOM   1791  N   GLU A1062      40.362   8.948  35.075  1.00102.50           N\\nANISOU 1791  N   GLU A1062    13880  10945  14119  -2420  -1205   2776       N\\nATOM   1792  CA  GLU A1062      41.504   8.118  34.707  1.00 96.62           C\\nANISOU 1792  CA  GLU A1062    12770  10671  13271  -2592   -725   2880       C\\nATOM   1793  C   GLU A1062      41.237   6.651  35.014  1.00 88.82           C\\nANISOU 1793  C   GLU A1062    11588  10061  12098  -2156   -455   2641       C\\nATOM   1794  O   GLU A1062      41.657   5.764  34.262  1.00 83.40           O\\nANISOU 1794  O   GLU A1062    10776   9705  11208  -2174    -28   2718       O\\nATOM   1795  CB  GLU A1062      42.761   8.595  35.435  1.00 87.02           C\\nANISOU 1795  CB  GLU A1062    11163   9509  12392  -2870   -785   2852       C\\nATOM   1796  CG  GLU A1062      43.240   9.972  35.025  1.00 95.42           C\\nANISOU 1796  CG  GLU A1062    12385  10212  13658  -3416   -988   3136       C\\nATOM   1797  CD  GLU A1062      44.494  10.395  35.768  1.00 99.73           C\\nANISOU 1797  CD  GLU A1062    12491  10838  14563  -3723  -1061   3077       C\\nATOM   1798  OE1 GLU A1062      44.628  10.042  36.959  1.00 95.17           O\\nANISOU 1798  OE1 GLU A1062    11645  10382  14135  -3431  -1231   2743       O\\nATOM   1799  OE2 GLU A1062      45.347  11.075  35.159  1.00104.48           O\\nANISOU 1799  OE2 GLU A1062    13018  11399  15279  -4288   -958   3375       O\\nATOM   1800  N   ALA A1063      40.542   6.377  36.121  1.00 85.45           N\\nANISOU 1800  N   ALA A1063    11151   9581  11735  -1777   -689   2337       N\\nATOM   1801  CA  ALA A1063      40.186   5.003  36.456  1.00 86.64           C\\nANISOU 1801  CA  ALA A1063    11186  10021  11712  -1400   -477   2151       C\\nATOM   1802  C   ALA A1063      39.112   4.459  35.526  1.00 88.99           C\\nANISOU 1802  C   ALA A1063    11790  10309  11715  -1259   -345   2190       C\\nATOM   1803  O   ALA A1063      39.030   3.242  35.325  1.00 88.77           O\\nANISOU 1803  O   ALA A1063    11692  10524  11512  -1068    -60   2120       O\\nATOM   1804  CB  ALA A1063      39.719   4.914  37.909  1.00 84.46           C\\nANISOU 1804  CB  ALA A1063    10850   9716  11524  -1112   -751   1850       C\\nATOM   1805  N   GLU A1064      38.283   5.337  34.957  1.00 91.39           N\\nANISOU 1805  N   GLU A1064    12438  10307  11980  -1346   -590   2294       N\\nATOM   1806  CA  GLU A1064      37.273   4.882  34.009  1.00 91.30           C\\nANISOU 1806  CA  GLU A1064    12709  10296  11686  -1243   -529   2345       C\\nATOM   1807  C   GLU A1064      37.898   4.478  32.678  1.00 95.38           C\\nANISOU 1807  C   GLU A1064    13297  11022  11922  -1504   -156   2596       C\\nATOM   1808  O   GLU A1064      37.402   3.560  32.016  1.00 93.85           O\\nANISOU 1808  O   GLU A1064    13219  10996  11445  -1384     47   2550       O\\nATOM   1809  CB  GLU A1064      36.216   5.969  33.805  1.00 88.36           C\\nANISOU 1809  CB  GLU A1064    12660   9522  11391  -1222   -972   2387       C\\nATOM   1810  CG  GLU A1064      34.995   5.506  33.022  1.00 85.95           C\\nANISOU 1810  CG  GLU A1064    12598   9220  10839  -1054  -1023   2379       C\\nATOM   1811  CD  GLU A1064      33.877   6.532  33.012  1.00 92.64           C\\nANISOU 1811  CD  GLU A1064    13676   9668  11857   -926  -1527   2353       C\\nATOM   1812  OE1 GLU A1064      32.798   6.224  32.460  1.00 92.14           O\\nANISOU 1812  OE1 GLU A1064    13758   9602  11649   -763  -1648   2318       O\\nATOM   1813  OE2 GLU A1064      34.072   7.641  33.555  1.00 96.90           O\\nANISOU 1813  OE2 GLU A1064    14234   9879  12704   -975  -1826   2343       O\\nATOM   1814  N   LYS A1065      38.982   5.144  32.270  1.00 96.04           N\\nANISOU 1814  N   LYS A1065    13309  11119  12064  -1890    -43   2837       N\\nATOM   1815  CA  LYS A1065      39.706   4.695  31.086  1.00 95.76           C\\nANISOU 1815  CA  LYS A1065    13269  11382  11732  -2158    412   3024       C\\nATOM   1816  C   LYS A1065      40.338   3.328  31.321  1.00 92.50           C\\nANISOU 1816  C   LYS A1065    12480  11360  11306  -1927    838   2784       C\\nATOM   1817  O   LYS A1065      40.296   2.460  30.442  1.00 93.15           O\\nANISOU 1817  O   LYS A1065    12640  11673  11077  -1892   1185   2745       O\\nATOM   1818  CB  LYS A1065      40.767   5.724  30.695  1.00 97.00           C\\nANISOU 1818  CB  LYS A1065    13372  11502  11982  -2673    474   3332       C\\nATOM   1819  N   LEU A1066      40.918   3.114  32.505  1.00 86.38           N\\nANISOU 1819  N   LEU A1066    11317  10638  10865  -1755    781   2609       N\\nATOM   1820  CA  LEU A1066      41.504   1.814  32.815  1.00 89.95           C\\nANISOU 1820  CA  LEU A1066    11422  11389  11367  -1482   1095   2400       C\\nATOM   1821  C   LEU A1066      40.439   0.729  32.871  1.00 88.33           C\\nANISOU 1821  C   LEU A1066    11426  11159  10977  -1113   1097   2208       C\\nATOM   1822  O   LEU A1066      40.672  -0.401  32.428  1.00 91.55           O\\nANISOU 1822  O   LEU A1066    11755  11759  11269   -957   1433   2085       O\\nATOM   1823  CB  LEU A1066      42.265   1.875  34.139  1.00 96.43           C\\nANISOU 1823  CB  LEU A1066    11833  12240  12567  -1373    917   2292       C\\nATOM   1824  CG  LEU A1066      43.442   2.845  34.220  1.00110.23           C\\nANISOU 1824  CG  LEU A1066    13274  14038  14572  -1754    899   2439       C\\nATOM   1825  CD1 LEU A1066      44.173   2.679  35.543  1.00109.37           C\\nANISOU 1825  CD1 LEU A1066    12741  14009  14807  -1592    693   2287       C\\nATOM   1826  CD2 LEU A1066      44.392   2.653  33.043  1.00117.21           C\\nANISOU 1826  CD2 LEU A1066    13951  15231  15353  -2035   1407   2560       C\\nATOM   1827  N   PHE A1067      39.266   1.055  33.417  1.00 88.20           N\\nANISOU 1827  N   PHE A1067    11656  10901  10956   -977    731   2152       N\\nATOM   1828  CA  PHE A1067      38.202   0.064  33.527  1.00 86.10           C\\nANISOU 1828  CA  PHE A1067    11554  10620  10539   -687    725   1975       C\\nATOM   1829  C   PHE A1067      37.743  -0.409  32.155  1.00 85.87           C\\nANISOU 1829  C   PHE A1067    11803  10657  10168   -762    941   2008       C\\nATOM   1830  O   PHE A1067      37.513  -1.606  31.949  1.00 84.89           O\\nANISOU 1830  O   PHE A1067    11703  10627   9925   -580   1146   1847       O\\nATOM   1831  CB  PHE A1067      37.028   0.640  34.316  1.00 89.23           C\\nANISOU 1831  CB  PHE A1067    12101  10796  11006   -569    323   1888       C\\nATOM   1832  CG  PHE A1067      35.849  -0.282  34.400  1.00 87.05           C\\nANISOU 1832  CG  PHE A1067    11964  10525  10586   -347    317   1719       C\\nATOM   1833  CD1 PHE A1067      35.865  -1.372  35.252  1.00 83.17           C\\nANISOU 1833  CD1 PHE A1067    11332  10130  10137   -136    418   1574       C\\nATOM   1834  CD2 PHE A1067      34.724  -0.058  33.627  1.00 86.11           C\\nANISOU 1834  CD2 PHE A1067    12115  10304  10299   -373    179   1726       C\\nATOM   1835  CE1 PHE A1067      34.781  -2.221  35.329  1.00 78.20           C\\nANISOU 1835  CE1 PHE A1067    10832   9493   9387     -3    424   1440       C\\nATOM   1836  CE2 PHE A1067      33.638  -0.903  33.702  1.00 81.95           C\\nANISOU 1836  CE2 PHE A1067    11664   9800   9671   -214    168   1558       C\\nATOM   1837  CZ  PHE A1067      33.666  -1.985  34.553  1.00 78.15           C\\nANISOU 1837  CZ  PHE A1067    11043   9414   9235    -52    312   1415       C\\nATOM   1838  N   ASN A1068      37.604   0.516  31.201  1.00 90.24           N\\nANISOU 1838  N   ASN A1068    12604  11140  10543  -1046    869   2222       N\\nATOM   1839  CA  ASN A1068      37.203   0.127  29.853  1.00 83.46           C\\nANISOU 1839  CA  ASN A1068    12053  10378   9278  -1159   1045   2269       C\\nATOM   1840  C   ASN A1068      38.222  -0.816  29.228  1.00 82.78           C\\nANISOU 1840  C   ASN A1068    11803  10602   9046  -1191   1575   2173       C\\nATOM   1841  O   ASN A1068      37.856  -1.728  28.479  1.00 84.94           O\\nANISOU 1841  O   ASN A1068    12255  10985   9033  -1118   1777   2024       O\\nATOM   1842  CB  ASN A1068      37.008   1.367  28.984  1.00 87.76           C\\nANISOU 1842  CB  ASN A1068    12920  10786   9638  -1498    837   2587       C\\nATOM   1843  CG  ASN A1068      35.631   1.982  29.145  1.00 95.27           C\\nANISOU 1843  CG  ASN A1068    14135  11430  10632  -1379    315   2609       C\\nATOM   1844  OD1 ASN A1068      34.845   2.027  28.198  1.00102.99           O\\nANISOU 1844  OD1 ASN A1068    15454  12372  11305  -1446    169   2702       O\\nATOM   1845  ND2 ASN A1068      35.327   2.448  30.350  1.00 94.72           N\\nANISOU 1845  ND2 ASN A1068    13890  11159  10939  -1190     20   2495       N\\nATOM   1846  N   GLN A1069      39.507  -0.618  29.532  1.00 82.90           N\\nANISOU 1846  N   GLN A1069    11450  10766   9281  -1289   1799   2217       N\\nATOM   1847  CA  GLN A1069      40.533  -1.532  29.041  1.00 93.96           C\\nANISOU 1847  CA  GLN A1069    12588  12479  10633  -1250   2317   2059       C\\nATOM   1848  C   GLN A1069      40.355  -2.926  29.631  1.00 96.67           C\\nANISOU 1848  C   GLN A1069    12801  12800  11129   -811   2383   1749       C\\nATOM   1849  O   GLN A1069      40.472  -3.931  28.918  1.00 96.30           O\\nANISOU 1849  O   GLN A1069    12800  12887  10901   -697   2721   1539       O\\nATOM   1850  CB  GLN A1069      41.922  -0.978  29.364  1.00104.31           C\\nANISOU 1850  CB  GLN A1069    13439  13961  12234  -1436   2488   2158       C\\nATOM   1851  CG  GLN A1069      42.191   0.399  28.770  1.00112.15           C\\nANISOU 1851  CG  GLN A1069    14573  14942  13096  -1947   2442   2503       C\\nATOM   1852  CD  GLN A1069      43.505   1.002  29.237  1.00116.78           C\\nANISOU 1852  CD  GLN A1069    14664  15667  14039  -2175   2548   2595       C\\nATOM   1853  OE1 GLN A1069      44.350   0.314  29.812  1.00124.86           O\\nANISOU 1853  OE1 GLN A1069    15191  16882  15370  -1946   2730   2385       O\\nATOM   1854  NE2 GLN A1069      43.681   2.297  28.993  1.00109.98           N\\nANISOU 1854  NE2 GLN A1069    13937  14684  13167  -2636   2395   2919       N\\nATOM   1855  N   ASP A1070      40.068  -3.007  30.934  1.00 93.20           N\\nANISOU 1855  N   ASP A1070    12231  12176  11004   -577   2056   1715       N\\nATOM   1856  CA  ASP A1070      39.831  -4.304  31.560  1.00 92.78           C\\nANISOU 1856  CA  ASP A1070    12121  12049  11083   -206   2064   1494       C\\nATOM   1857  C   ASP A1070      38.580  -4.968  31.000  1.00 84.10           C\\nANISOU 1857  C   ASP A1070    11427  10832   9697   -148   2030   1376       C\\nATOM   1858  O   ASP A1070      38.532  -6.195  30.858  1.00 74.28           O\\nANISOU 1858  O   ASP A1070    10218   9558   8448     64   2204   1167       O\\nATOM   1859  CB  ASP A1070      39.714  -4.145  33.076  1.00 97.16           C\\nANISOU 1859  CB  ASP A1070    12517  12464  11936    -46   1705   1529       C\\nATOM   1860  CG  ASP A1070      40.993  -3.637  33.711  1.00101.50           C\\nANISOU 1860  CG  ASP A1070    12635  13134  12794    -83   1688   1606       C\\nATOM   1861  OD1 ASP A1070      42.082  -3.940  33.181  1.00105.37           O\\nANISOU 1861  OD1 ASP A1070    12832  13826  13379    -89   2015   1558       O\\nATOM   1862  OD2 ASP A1070      40.905  -2.936  34.743  1.00 98.07           O\\nANISOU 1862  OD2 ASP A1070    12136  12614  12514   -110   1349   1680       O\\nATOM   1863  N   VAL A1071      37.557  -4.174  30.679  1.00 85.78           N\\nANISOU 1863  N   VAL A1071    11939  10950   9704   -328   1771   1495       N\\nATOM   1864  CA  VAL A1071      36.322  -4.733  30.136  1.00 82.23           C\\nANISOU 1864  CA  VAL A1071    11829  10413   9002   -301   1681   1379       C\\nATOM   1865  C   VAL A1071      36.565  -5.310  28.749  1.00 86.97           C\\nANISOU 1865  C   VAL A1071    12623  11169   9251   -401   2023   1266       C\\nATOM   1866  O   VAL A1071      36.169  -6.443  28.455  1.00 91.66           O\\nANISOU 1866  O   VAL A1071    13352  11723   9752   -267   2137   1029       O\\nATOM   1867  CB  VAL A1071      35.214  -3.667  30.113  1.00 77.64           C\\nANISOU 1867  CB  VAL A1071    11459   9702   8338   -435   1276   1525       C\\nATOM   1868  CG1 VAL A1071      34.018  -4.169  29.323  1.00 68.20           C\\nANISOU 1868  CG1 VAL A1071    10579   8473   6862   -455   1173   1415       C\\nATOM   1869  CG2 VAL A1071      34.807  -3.308  31.524  1.00 79.71           C\\nANISOU 1869  CG2 VAL A1071    11544   9829   8913   -289    982   1517       C\\nATOM   1870  N   ASP A1072      37.208  -4.533  27.872  1.00 86.89           N\\nANISOU 1870  N   ASP A1072    12656  11340   9019   -672   2197   1425       N\\nATOM   1871  CA  ASP A1072      37.548  -5.045  26.549  1.00 93.69           C\\nANISOU 1871  CA  ASP A1072    13699  12426   9474   -799   2587   1294       C\\nATOM   1872  C   ASP A1072      38.419  -6.289  26.649  1.00 93.29           C\\nANISOU 1872  C   ASP A1072    13380  12470   9598   -530   3002    969       C\\nATOM   1873  O   ASP A1072      38.186  -7.273  25.940  1.00100.45           O\\nANISOU 1873  O   ASP A1072    14485  13404  10277   -445   3208    683       O\\nATOM   1874  CB  ASP A1072      38.246  -3.964  25.724  1.00101.72           C\\nANISOU 1874  CB  ASP A1072    14764  13660  10224  -1186   2755   1563       C\\nATOM   1875  CG  ASP A1072      37.274  -2.951  25.152  1.00105.64           C\\nANISOU 1875  CG  ASP A1072    15691  14039  10407  -1457   2355   1858       C\\nATOM   1876  OD1 ASP A1072      36.104  -3.321  24.911  1.00105.43           O\\nANISOU 1876  OD1 ASP A1072    15959  13888  10212  -1367   2080   1761       O\\nATOM   1877  OD2 ASP A1072      37.677  -1.787  24.942  1.00108.66           O\\nANISOU 1877  OD2 ASP A1072    16112  14434  10740  -1764   2286   2192       O\\nATOM   1878  N   ALA A1073      39.417  -6.269  27.537  1.00 84.98           N\\nANISOU 1878  N   ALA A1073    11874  11440   8973   -376   3089    988       N\\nATOM   1879  CA  ALA A1073      40.250  -7.451  27.738  1.00 87.42           C\\nANISOU 1879  CA  ALA A1073    11887  11783   9546    -46   3401    685       C\\nATOM   1880  C   ALA A1073      39.418  -8.640  28.199  1.00 88.42           C\\nANISOU 1880  C   ALA A1073    12207  11603   9787    254   3220    480       C\\nATOM   1881  O   ALA A1073      39.645  -9.774  27.760  1.00 91.45           O\\nANISOU 1881  O   ALA A1073    12623  11947  10175    465   3482    159       O\\nATOM   1882  CB  ALA A1073      41.357  -7.149  28.747  1.00 88.38           C\\nANISOU 1882  CB  ALA A1073    11477  11958  10146     77   3385    785       C\\nATOM   1883  N   ALA A1074      38.441  -8.397  29.079  1.00 83.01           N\\nANISOU 1883  N   ALA A1074    11651  10689   9199    259   2785    645       N\\nATOM   1884  CA  ALA A1074      37.590  -9.476  29.567  1.00 85.44           C\\nANISOU 1884  CA  ALA A1074    12143  10714   9605    456   2615    500       C\\nATOM   1885  C   ALA A1074      36.749 -10.084  28.454  1.00 93.89           C\\nANISOU 1885  C   ALA A1074    13614  11749  10313    356   2695    279       C\\nATOM   1886  O   ALA A1074      36.388 -11.263  28.528  1.00 97.64           O\\nANISOU 1886  O   ALA A1074    14228  11998  10874    520   2705     57       O\\nATOM   1887  CB  ALA A1074      36.686  -8.968  30.689  1.00 78.28           C\\nANISOU 1887  CB  ALA A1074    11263   9662   8819    417   2191    709       C\\nATOM   1888  N   VAL A1075      36.430  -9.305  27.419  1.00 95.22           N\\nANISOU 1888  N   VAL A1075    13998  12114  10069     70   2718    348       N\\nATOM   1889  CA  VAL A1075      35.614  -9.821  26.325  1.00 92.66           C\\nANISOU 1889  CA  VAL A1075    14075  11790   9341    -54   2737    139       C\\nATOM   1890  C   VAL A1075      36.457 -10.646  25.357  1.00100.97           C\\nANISOU 1890  C   VAL A1075    15170  12983  10213     22   3217   -207       C\\nATOM   1891  O   VAL A1075      35.987 -11.658  24.824  1.00101.40           O\\nANISOU 1891  O   VAL A1075    15489  12912  10125     79   3272   -531       O\\nATOM   1892  CB  VAL A1075      34.888  -8.661  25.617  1.00 82.73           C\\nANISOU 1892  CB  VAL A1075    13071  10672   7689   -380   2491    377       C\\nATOM   1893  CG1 VAL A1075      34.069  -9.171  24.446  1.00 75.94           C\\nANISOU 1893  CG1 VAL A1075    12635   9852   6368   -528   2457    166       C\\nATOM   1894  CG2 VAL A1075      33.993  -7.930  26.604  1.00 76.88           C\\nANISOU 1894  CG2 VAL A1075    12256   9765   7192   -384   2023    620       C\\nATOM   1895  N   ARG A1076      37.712 -10.240  25.115  1.00100.09           N\\nANISOU 1895  N   ARG A1076    14776  13139  10116     17   3583   -182       N\\nATOM   1896  CA  ARG A1076      38.592 -11.049  24.273  1.00106.02           C\\nANISOU 1896  CA  ARG A1076    15475  14062  10744    139   4103   -579       C\\nATOM   1897  C   ARG A1076      38.740 -12.458  24.828  1.00110.21           C\\nANISOU 1897  C   ARG A1076    15911  14258  11706    564   4141   -922       C\\nATOM   1898  O   ARG A1076      38.867 -13.421  24.062  1.00118.72           O\\nANISOU 1898  O   ARG A1076    17153  15310  12647    690   4425  -1359       O\\nATOM   1899  CB  ARG A1076      39.980 -10.411  24.143  1.00109.75           C\\nANISOU 1899  CB  ARG A1076    15519  14893  11289     84   4503   -500       C\\nATOM   1900  CG  ARG A1076      40.027  -8.904  24.227  1.00109.02           C\\nANISOU 1900  CG  ARG A1076    15378  14979  11066   -286   4338    -22       C\\nATOM   1901  CD  ARG A1076      39.706  -8.229  22.910  1.00113.54           C\\nANISOU 1901  CD  ARG A1076    16360  15831  10947   -724   4457     91       C\\nATOM   1902  NE  ARG A1076      39.657  -6.778  23.063  1.00113.48           N\\nANISOU 1902  NE  ARG A1076    16365  15872  10879  -1069   4203    591       N\\nATOM   1903  CZ  ARG A1076      39.507  -5.923  22.058  1.00114.12           C\\nANISOU 1903  CZ  ARG A1076    16787  16166  10409  -1503   4233    842       C\\nATOM   1904  NH1 ARG A1076      39.395  -6.367  20.812  1.00118.70           N\\nANISOU 1904  NH1 ARG A1076    17722  16997  10383  -1663   4528    629       N\\nATOM   1905  NH2 ARG A1076      39.471  -4.619  22.301  1.00110.17           N\\nANISOU 1905  NH2 ARG A1076    16305  15605   9949  -1786   3945   1307       N\\nATOM   1906  N   GLY A1077      38.727 -12.597  26.152  1.00104.33           N\\nANISOU 1906  N   GLY A1077    14938  13235  11468    780   3843   -732       N\\nATOM   1907  CA  GLY A1077      38.862 -13.893  26.781  1.00103.24           C\\nANISOU 1907  CA  GLY A1077    14749  12715  11761   1164   3801   -960       C\\nATOM   1908  C   GLY A1077      37.555 -14.652  26.832  1.00100.52           C\\nANISOU 1908  C   GLY A1077    14844  12012  11338   1106   3509  -1046       C\\nATOM   1909  O   GLY A1077      37.538 -15.875  26.663  1.00104.59           O\\nANISOU 1909  O   GLY A1077    15516  12220  12003   1321   3586  -1382       O\\nATOM   1910  N   ILE A1078      36.453 -13.936  27.070  1.00 99.32           N\\nANISOU 1910  N   ILE A1078    14869  11880  10988    814   3165   -762       N\\nATOM   1911  CA  ILE A1078      35.138 -14.573  27.087  1.00 95.36           C\\nANISOU 1911  CA  ILE A1078    14721  11103  10410    692   2887   -841       C\\nATOM   1912  C   ILE A1078      34.872 -15.266  25.758  1.00 94.23           C\\nANISOU 1912  C   ILE A1078    14931  10962   9909    611   3076  -1259       C\\nATOM   1913  O   ILE A1078      34.461 -16.432  25.713  1.00 91.07           O\\nANISOU 1913  O   ILE A1078    14757  10213   9633    693   3032  -1537       O\\nATOM   1914  CB  ILE A1078      34.042 -13.542  27.412  1.00 93.90           C\\nANISOU 1914  CB  ILE A1078    14585  11030  10063    404   2522   -518       C\\nATOM   1915  CG1 ILE A1078      33.993 -13.263  28.917  1.00 93.60           C\\nANISOU 1915  CG1 ILE A1078    14291  10873  10400    497   2289   -213       C\\nATOM   1916  CG2 ILE A1078      32.692 -14.024  26.911  1.00 91.88           C\\nANISOU 1916  CG2 ILE A1078    14674  10646   9590    192   2300   -673       C\\nATOM   1917  CD1 ILE A1078      33.002 -12.183  29.313  1.00 86.14           C\\nANISOU 1917  CD1 ILE A1078    13326  10053   9351    273   1966     41       C\\nATOM   1918  N   LEU A1079      35.121 -14.560  24.654  1.00 96.21           N\\nANISOU 1918  N   LEU A1079    15266  11598   9690    421   3283  -1311       N\\nATOM   1919  CA  LEU A1079      34.910 -15.148  23.339  1.00 99.06           C\\nANISOU 1919  CA  LEU A1079    15997  12035   9608    315   3475  -1730       C\\nATOM   1920  C   LEU A1079      35.911 -16.261  23.058  1.00104.43           C\\nANISOU 1920  C   LEU A1079    16609  12586  10483    653   3898  -2204       C\\nATOM   1921  O   LEU A1079      35.576 -17.237  22.375  1.00107.18           O\\nANISOU 1921  O   LEU A1079    17287  12752  10686    675   3966  -2650       O\\nATOM   1922  CB  LEU A1079      34.990 -14.061  22.271  1.00 97.08           C\\nANISOU 1922  CB  LEU A1079    15879  12261   8747     -2   3592  -1606       C\\nATOM   1923  CG  LEU A1079      34.022 -12.896  22.494  1.00 92.62           C\\nANISOU 1923  CG  LEU A1079    15381  11775   8035   -286   3126  -1146       C\\nATOM   1924  CD1 LEU A1079      34.208 -11.832  21.427  1.00 87.85           C\\nANISOU 1924  CD1 LEU A1079    14956  11583   6838   -599   3216   -967       C\\nATOM   1925  CD2 LEU A1079      32.586 -13.395  22.521  1.00 89.61           C\\nANISOU 1925  CD2 LEU A1079    15271  11148   7628   -399   2691  -1233       C\\nATOM   1926  N   ARG A1080      37.134 -16.141  23.574  1.00102.78           N\\nANISOU 1926  N   ARG A1080    15961  12455  10635    932   4161  -2150       N\\nATOM   1927  CA  ARG A1080      38.113 -17.215  23.463  1.00106.42           C\\nANISOU 1927  CA  ARG A1080    16265  12749  11422   1346   4516  -2607       C\\nATOM   1928  C   ARG A1080      37.864 -18.345  24.454  1.00114.00           C\\nANISOU 1928  C   ARG A1080    17260  13084  12971   1658   4225  -2653       C\\nATOM   1929  O   ARG A1080      38.585 -19.348  24.417  1.00121.35           O\\nANISOU 1929  O   ARG A1080    18104  13749  14255   2055   4430  -3041       O\\nATOM   1930  CB  ARG A1080      39.528 -16.662  23.652  1.00 95.46           C\\nANISOU 1930  CB  ARG A1080    14320  11699  10249   1534   4874  -2535       C\\nATOM   1931  N   ASN A1081      36.877 -18.203  25.339  1.00113.30           N\\nANISOU 1931  N   ASN A1081    17292  12754  13003   1487   3760  -2268       N\\nATOM   1932  CA  ASN A1081      36.488 -19.263  26.264  1.00110.82           C\\nANISOU 1932  CA  ASN A1081    17098  11850  13160   1666   3466  -2242       C\\nATOM   1933  C   ASN A1081      35.348 -20.052  25.630  1.00107.85           C\\nANISOU 1933  C   ASN A1081    17225  11189  12565   1437   3324  -2533       C\\nATOM   1934  O   ASN A1081      34.255 -19.516  25.418  1.00 96.74           O\\nANISOU 1934  O   ASN A1081    16004   9943  10809   1044   3098  -2372       O\\nATOM   1935  CB  ASN A1081      36.075 -18.682  27.614  1.00104.89           C\\nANISOU 1935  CB  ASN A1081    16179  11052  12621   1564   3094  -1681       C\\nATOM   1936  CG  ASN A1081      35.935 -19.745  28.696  1.00100.82           C\\nANISOU 1936  CG  ASN A1081    15751   9964  12593   1757   2830  -1573       C\\nATOM   1937  OD1 ASN A1081      35.536 -20.881  28.430  1.00 96.54           O\\nANISOU 1937  OD1 ASN A1081    15540   8975  12166   1793   2783  -1851       O\\nATOM   1938  ND2 ASN A1081      36.265 -19.375  29.927  1.00 99.41           N\\nANISOU 1938  ND2 ASN A1081    15308   9782  12683   1855   2634  -1158       N\\nATOM   1939  N   ALA A1082      35.603 -21.330  25.335  1.00104.72           N\\nANISOU 1939  N   ALA A1082    17030  10346  12412   1693   3425  -2982       N\\nATOM   1940  CA  ALA A1082      34.620 -22.148  24.633  1.00104.56           C\\nANISOU 1940  CA  ALA A1082    17500  10033  12195   1466   3305  -3342       C\\nATOM   1941  C   ALA A1082      33.348 -22.360  25.442  1.00101.54           C\\nANISOU 1941  C   ALA A1082    17302   9334  11945   1142   2845  -3001       C\\nATOM   1942  O   ALA A1082      32.300 -22.654  24.856  1.00101.98           O\\nANISOU 1942  O   ALA A1082    17693   9314  11739    801   2679  -3190       O\\nATOM   1943  CB  ALA A1082      35.231 -23.499  24.264  1.00107.82           C\\nANISOU 1943  CB  ALA A1082    18086   9944  12935   1850   3489  -3914       C\\nATOM   1944  N   LYS A1083      33.409 -22.219  26.764  1.00105.02           N\\nANISOU 1944  N   LYS A1083    17519   9623  12760   1215   2642  -2520       N\\nATOM   1945  CA  LYS A1083      32.243 -22.435  27.607  1.00 99.72           C\\nANISOU 1945  CA  LYS A1083    16986   8701  12202    885   2273  -2194       C\\nATOM   1946  C   LYS A1083      31.446 -21.163  27.871  1.00 97.98           C\\nANISOU 1946  C   LYS A1083    16574   8985  11668    541   2119  -1821       C\\nATOM   1947  O   LYS A1083      30.317 -21.253  28.366  1.00 96.09           O\\nANISOU 1947  O   LYS A1083    16414   8652  11442    209   1857  -1636       O\\nATOM   1948  CB  LYS A1083      32.666 -23.061  28.941  1.00 98.15           C\\nANISOU 1948  CB  LYS A1083    16717   8046  12528   1114   2120  -1873       C\\nATOM   1949  N   LEU A1084      31.992 -19.986  27.551  1.00 99.46           N\\nANISOU 1949  N   LEU A1084    16502   9689  11600    605   2275  -1719       N\\nATOM   1950  CA  LEU A1084      31.288 -18.729  27.771  1.00 97.55           C\\nANISOU 1950  CA  LEU A1084    16090   9867  11109    333   2100  -1390       C\\nATOM   1951  C   LEU A1084      30.919 -17.993  26.491  1.00101.44           C\\nANISOU 1951  C   LEU A1084    16699  10753  11090    121   2131  -1554       C\\nATOM   1952  O   LEU A1084      30.009 -17.161  26.521  1.00102.09           O\\nANISOU 1952  O   LEU A1084    16730  11072  10987   -136   1884  -1351       O\\nATOM   1953  CB  LEU A1084      32.124 -17.790  28.654  1.00 93.67           C\\nANISOU 1953  CB  LEU A1084    15216   9609  10766    522   2147  -1024       C\\nATOM   1954  CG  LEU A1084      32.376 -18.250  30.092  1.00 99.39           C\\nANISOU 1954  CG  LEU A1084    15814  10040  11911    678   2020   -744       C\\nATOM   1955  CD1 LEU A1084      33.068 -17.160  30.896  1.00100.96           C\\nANISOU 1955  CD1 LEU A1084    15645  10540  12174    797   2010   -411       C\\nATOM   1956  CD2 LEU A1084      31.075 -18.668  30.757  1.00 98.30           C\\nANISOU 1956  CD2 LEU A1084    15830   9700  11820    371   1756   -602       C\\nATOM   1957  N   LYS A1085      31.598 -18.269  25.378  1.00102.45           N\\nANISOU 1957  N   LYS A1085    16983  10965  10978    227   2417  -1917       N\\nATOM   1958  CA  LYS A1085      31.262 -17.597  24.126  1.00 99.55           C\\nANISOU 1958  CA  LYS A1085    16799  10990  10037    -13   2431  -2041       C\\nATOM   1959  C   LYS A1085      29.850 -17.899  23.627  1.00 99.81           C\\nANISOU 1959  C   LYS A1085    17128  10950   9847   -354   2083  -2182       C\\nATOM   1960  O   LYS A1085      29.193 -16.966  23.138  1.00 92.79           O\\nANISOU 1960  O   LYS A1085    16268  10388   8598   -594   1861  -2023       O\\nATOM   1961  CB  LYS A1085      32.301 -17.947  23.053  1.00 96.22           C\\nANISOU 1961  CB  LYS A1085    16501  10703   9355    149   2870  -2453       C\\nATOM   1962  N   PRO A1086      29.335 -19.137  23.693  1.00105.32           N\\nANISOU 1962  N   PRO A1086    18044  11220  10751   -402   1987  -2468       N\\nATOM   1963  CA  PRO A1086      27.961 -19.366  23.201  1.00106.72           C\\nANISOU 1963  CA  PRO A1086    18449  11373  10729   -778   1625  -2606       C\\nATOM   1964  C   PRO A1086      26.904 -18.527  23.902  1.00101.72           C\\nANISOU 1964  C   PRO A1086    17551  10915  10184  -1000   1260  -2201       C\\nATOM   1965  O   PRO A1086      26.130 -17.830  23.232  1.00 97.88           O\\nANISOU 1965  O   PRO A1086    17104  10733   9353  -1226    992  -2175       O\\nATOM   1966  CB  PRO A1086      27.759 -20.868  23.445  1.00108.18           C\\nANISOU 1966  CB  PRO A1086    18857  10979  11267   -780   1611  -2917       C\\nATOM   1967  CG  PRO A1086      29.125 -21.438  23.364  1.00108.60           C\\nANISOU 1967  CG  PRO A1086    18951  10834  11479   -369   2012  -3150       C\\nATOM   1968  CD  PRO A1086      30.018 -20.411  23.991  1.00103.81           C\\nANISOU 1968  CD  PRO A1086    17951  10542  10950   -127   2192  -2744       C\\nATOM   1969  N   VAL A1087      26.844 -18.575  25.235  1.00 98.45           N\\nANISOU 1969  N   VAL A1087    16867  10324  10214   -932   1231  -1899       N\\nATOM   1970  CA  VAL A1087      25.825 -17.817  25.956  1.00 96.16           C\\nANISOU 1970  CA  VAL A1087    16290  10223  10024  -1125    937  -1588       C\\nATOM   1971  C   VAL A1087      26.024 -16.321  25.749  1.00 94.05           C\\nANISOU 1971  C   VAL A1087    15830  10386   9517  -1049    881  -1337       C\\nATOM   1972  O   VAL A1087      25.055 -15.564  25.617  1.00 93.16           O\\nANISOU 1972  O   VAL A1087    15592  10501   9302  -1221    565  -1236       O\\nATOM   1973  CB  VAL A1087      25.834 -18.196  27.449  1.00 97.74           C\\nANISOU 1973  CB  VAL A1087    16281  10182  10673  -1078    978  -1328       C\\nATOM   1974  CG1 VAL A1087      27.238 -18.088  28.024  1.00102.40           C\\nANISOU 1974  CG1 VAL A1087    16780  10706  11420   -706   1259  -1166       C\\nATOM   1975  CG2 VAL A1087      24.863 -17.323  28.230  1.00 89.97           C\\nANISOU 1975  CG2 VAL A1087    14954   9465   9765  -1245    754  -1058       C\\nATOM   1976  N   TYR A1088      27.284 -15.876  25.692  1.00 89.69           N\\nANISOU 1976  N   TYR A1088    15242   9934   8902   -793   1168  -1242       N\\nATOM   1977  CA  TYR A1088      27.580 -14.457  25.515  1.00 90.57           C\\nANISOU 1977  CA  TYR A1088    15204  10393   8813   -755   1125   -975       C\\nATOM   1978  C   TYR A1088      26.959 -13.916  24.234  1.00 95.61           C\\nANISOU 1978  C   TYR A1088    16073  11277   8976   -968    892  -1053       C\\nATOM   1979  O   TYR A1088      26.470 -12.781  24.202  1.00 93.98           O\\nANISOU 1979  O   TYR A1088    15753  11275   8682  -1035    611   -805       O\\nATOM   1980  CB  TYR A1088      29.095 -14.250  25.512  1.00 93.94           C\\nANISOU 1980  CB  TYR A1088    15566  10885   9242   -509   1510   -919       C\\nATOM   1981  CG  TYR A1088      29.544 -12.810  25.574  1.00 98.44           C\\nANISOU 1981  CG  TYR A1088    15953  11742   9710   -493   1488   -591       C\\nATOM   1982  CD1 TYR A1088      29.740 -12.178  26.794  1.00 98.86           C\\nANISOU 1982  CD1 TYR A1088    15682  11781  10099   -378   1424   -304       C\\nATOM   1983  CD2 TYR A1088      29.792 -12.088  24.415  1.00103.73           C\\nANISOU 1983  CD2 TYR A1088    16808  12681   9923   -622   1523   -565       C\\nATOM   1984  CE1 TYR A1088      30.162 -10.863  26.860  1.00 99.84           C\\nANISOU 1984  CE1 TYR A1088    15661  12107  10167   -380   1378    -29       C\\nATOM   1985  CE2 TYR A1088      30.213 -10.771  24.470  1.00106.12           C\\nANISOU 1985  CE2 TYR A1088    16981  13181  10158   -650   1482   -232       C\\nATOM   1986  CZ  TYR A1088      30.395 -10.164  25.696  1.00103.83           C\\nANISOU 1986  CZ  TYR A1088    16357  12826  10268   -522   1402     20       C\\nATOM   1987  OH  TYR A1088      30.810  -8.854  25.759  1.00103.35           O\\nANISOU 1987  OH  TYR A1088    16189  12904  10176   -568   1333    326       O\\nATOM   1988  N   ASP A1089      26.969 -14.714  23.164  1.00102.12           N\\nANISOU 1988  N   ASP A1089    17248  12069   9485  -1067    973  -1406       N\\nATOM   1989  CA  ASP A1089      26.320 -14.293  21.927  1.00102.51           C\\nANISOU 1989  CA  ASP A1089    17573  12361   9018  -1301    696  -1486       C\\nATOM   1990  C   ASP A1089      24.810 -14.185  22.110  1.00 97.68           C\\nANISOU 1990  C   ASP A1089    16847  11734   8531  -1503    175  -1453       C\\nATOM   1991  O   ASP A1089      24.193 -13.208  21.669  1.00 94.27           O\\nANISOU 1991  O   ASP A1089    16405  11528   7886  -1603   -198  -1266       O\\nATOM   1992  CB  ASP A1089      26.658 -15.270  20.798  1.00107.75           C\\nANISOU 1992  CB  ASP A1089    18652  12996   9292  -1371    911  -1943       C\\nATOM   1993  CG  ASP A1089      28.153 -15.360  20.522  1.00109.36           C\\nANISOU 1993  CG  ASP A1089    18906  13282   9365  -1158   1468  -2039       C\\nATOM   1994  OD1 ASP A1089      28.859 -14.349  20.724  1.00107.83           O\\nANISOU 1994  OD1 ASP A1089    18522  13306   9142  -1077   1610  -1702       O\\nATOM   1995  OD2 ASP A1089      28.623 -16.442  20.104  1.00108.54           O\\nANISOU 1995  OD2 ASP A1089    19006  13016   9217  -1074   1762  -2478       O\\nATOM   1996  N   SER A1090      24.200 -15.124  22.768  1.00 95.52           N\\nANISOU 1996  N   SER A1090    16469  11190   8635  -1571    131  -1622       N\\nATOM   1997  CA  SER A1090      22.775 -15.087  22.914  1.00100.79           C\\nANISOU 1997  CA  SER A1090    16964  11869   9463  -1805   -311  -1652       C\\nATOM   1998  C   SER A1090      22.220 -13.982  23.739  1.00102.57           C\\nANISOU 1998  C   SER A1090    16755  12269   9949  -1733   -541  -1311       C\\nATOM   1999  O   SER A1090      21.034 -13.763  23.747  1.00106.04           O\\nANISOU 1999  O   SER A1090    16983  12810  10497  -1894   -938  -1340       O\\nATOM   2000  CB  SER A1090      22.377 -16.406  23.588  1.00 99.01           C\\nANISOU 2000  CB  SER A1090    16709  11296   9615  -1937   -227  -1860       C\\nATOM   2001  OG  SER A1090      21.208 -16.357  24.395  1.00 95.53           O\\nANISOU 2001  OG  SER A1090    15874  10901   9522  -2092   -478  -1730       O\\nATOM   2002  N   LEU A1091      23.062 -13.325  24.481  1.00 99.87           N\\nANISOU 2002  N   LEU A1091    16250  11965   9730  -1492   -315  -1031       N\\nATOM   2003  CA  LEU A1091      22.607 -12.416  25.517  1.00 95.87           C\\nANISOU 2003  CA  LEU A1091    15324  11551   9550  -1398   -463   -783       C\\nATOM   2004  C   LEU A1091      22.327 -11.026  24.968  1.00 97.76           C\\nANISOU 2004  C   LEU A1091    15525  12007   9612  -1342   -816   -587       C\\nATOM   2005  O   LEU A1091      23.032 -10.535  24.083  1.00 95.64           O\\nANISOU 2005  O   LEU A1091    15549  11818   8971  -1317   -786   -485       O\\nATOM   2006  CB  LEU A1091      23.641 -12.333  26.638  1.00 87.84           C\\nANISOU 2006  CB  LEU A1091    14159  10436   8780  -1181    -92   -597       C\\nATOM   2007  CG  LEU A1091      23.680 -13.560  27.542  1.00 82.06           C\\nANISOU 2007  CG  LEU A1091    13386   9458   8336  -1224    143   -690       C\\nATOM   2008  CD1 LEU A1091      24.786 -13.425  28.573  1.00 80.82           C\\nANISOU 2008  CD1 LEU A1091    13114   9224   8371   -989    440   -482       C\\nATOM   2009  CD2 LEU A1091      22.327 -13.769  28.206  1.00 80.36           C\\nANISOU 2009  CD2 LEU A1091    12890   9277   8367  -1435    -70   -736       C\\nATOM   2010  N   ASP A1092      21.376 -10.343  25.562  1.00 96.05           N\\nANISOU 2010  N   ASP A1092    14944  11880   9672  -1329  -1151   -538       N\\nATOM   2011  CA  ASP A1092      21.052  -8.988  25.248  1.00 94.58           C\\nANISOU 2011  CA  ASP A1092    14656  11809   9469  -1194  -1512   -321       C\\nATOM   2012  C   ASP A1092      22.222  -8.197  25.771  1.00 90.97           C\\nANISOU 2012  C   ASP A1092    14182  11304   9080   -989  -1249    -61       C\\nATOM   2013  O   ASP A1092      22.961  -8.670  26.567  1.00 94.84           O\\nANISOU 2013  O   ASP A1092    14566  11715   9754   -916   -857    -59       O\\nATOM   2014  CB  ASP A1092      19.780  -8.669  26.007  1.00101.30           C\\nANISOU 2014  CB  ASP A1092    15029  12751  10711  -1166  -1868   -406       C\\nATOM   2015  CG  ASP A1092      19.607  -7.210  26.318  1.00111.33           C\\nANISOU 2015  CG  ASP A1092    16080  14045  12176   -914  -2131   -205       C\\nATOM   2016  OD1 ASP A1092      20.277  -6.361  25.708  1.00117.45           O\\nANISOU 2016  OD1 ASP A1092    17125  14798  12702   -861  -2417     -1       O\\nATOM   2017  OD2 ASP A1092      18.756  -6.904  27.171  1.00112.11           O\\nANISOU 2017  OD2 ASP A1092    15757  14174  12666   -784  -2057   -258       O\\nATOM   2018  N   ALA A1093      22.381  -6.966  25.331  1.00 96.88           N\\nANISOU 2018  N   ALA A1093    15054  12081   9674   -916  -1505    178       N\\nATOM   2019  CA  ALA A1093      23.488  -6.122  25.778  1.00 91.46           C\\nANISOU 2019  CA  ALA A1093    14374  11336   9042   -782  -1292    431       C\\nATOM   2020  C   ALA A1093      23.421  -5.832  27.272  1.00 93.10           C\\nANISOU 2020  C   ALA A1093    14165  11492   9718   -603  -1188    414       C\\nATOM   2021  O   ALA A1093      24.464  -5.712  27.927  1.00 87.73           O\\nANISOU 2021  O   ALA A1093    13451  10765   9118   -524   -866    519       O\\nATOM   2022  CB  ALA A1093      23.503  -4.814  24.988  1.00 88.70           C\\nANISOU 2022  CB  ALA A1093    14227  10970   8505   -779  -1676    717       C\\nATOM   2023  N   VAL A1094      22.214  -5.720  27.829  1.00 97.94           N\\nANISOU 2023  N   VAL A1094    14439  12147  10627   -546  -1450    262       N\\nATOM   2024  CA  VAL A1094      22.076  -5.445  29.257  1.00 93.00           C\\nANISOU 2024  CA  VAL A1094    13427  11531  10378   -399  -1324    200       C\\nATOM   2025  C   VAL A1094      22.441  -6.680  30.072  1.00 88.59           C\\nANISOU 2025  C   VAL A1094    12819  10982   9860   -491   -879     98       C\\nATOM   2026  O   VAL A1094      23.204  -6.601  31.041  1.00 83.02           O\\nANISOU 2026  O   VAL A1094    12036  10247   9261   -400   -616    175       O\\nATOM   2027  CB  VAL A1094      20.652  -4.956  29.576  1.00 91.34           C\\nANISOU 2027  CB  VAL A1094    12822  11413  10469   -310  -1694     21       C\\nATOM   2028  CG1 VAL A1094      20.546  -4.549  31.038  1.00 87.18           C\\nANISOU 2028  CG1 VAL A1094    11914  10940  10271   -155  -1529    -81       C\\nATOM   2029  CG2 VAL A1094      20.261  -3.802  28.656  1.00 92.19           C\\nANISOU 2029  CG2 VAL A1094    13027  11445  10557   -192  -2230    148       C\\nATOM   2030  N   ARG A1095      21.898  -7.840  29.694  1.00 90.63           N\\nANISOU 2030  N   ARG A1095    13144  11253  10038   -685   -833    -66       N\\nATOM   2031  CA  ARG A1095      22.284  -9.087  30.344  1.00 90.96           C\\nANISOU 2031  CA  ARG A1095    13231  11214  10116   -790   -456   -122       C\\nATOM   2032  C   ARG A1095      23.746  -9.427  30.091  1.00 87.34           C\\nANISOU 2032  C   ARG A1095    13078  10619   9487   -715   -154      0       C\\nATOM   2033  O   ARG A1095      24.354 -10.144  30.893  1.00 79.42           O\\nANISOU 2033  O   ARG A1095    12074   9515   8587   -689    132     31       O\\nATOM   2034  CB  ARG A1095      21.389 -10.229  29.864  1.00 87.99           C\\nANISOU 2034  CB  ARG A1095    12907  10817   9709  -1046   -517   -333       C\\nATOM   2035  CG  ARG A1095      19.913  -9.890  29.887  1.00 88.08           C\\nANISOU 2035  CG  ARG A1095    12562  11010   9896  -1139   -853   -486       C\\nATOM   2036  CD  ARG A1095      19.099 -10.979  29.236  1.00 93.06           C\\nANISOU 2036  CD  ARG A1095    13265  11616  10479  -1439   -963   -697       C\\nATOM   2037  NE  ARG A1095      17.793 -10.502  28.791  1.00103.22           N\\nANISOU 2037  NE  ARG A1095    14244  13099  11877  -1501  -1404   -846       N\\nATOM   2038  CZ  ARG A1095      16.679 -10.583  29.511  1.00102.98           C\\nANISOU 2038  CZ  ARG A1095    13724  13246  12157  -1620  -1455   -997       C\\nATOM   2039  NH1 ARG A1095      16.705 -11.126  30.720  1.00101.20           N\\nANISOU 2039  NH1 ARG A1095    13324  13034  12095  -1735  -1072   -988       N\\nATOM   2040  NH2 ARG A1095      15.535 -10.122  29.020  1.00102.93           N\\nANISOU 2040  NH2 ARG A1095    13394  13427  12289  -1634  -1897  -1154       N\\nATOM   2041  N   ARG A1096      24.321  -8.920  29.001  1.00 90.45           N\\nANISOU 2041  N   ARG A1096    13718  11024   9623   -685   -218     78       N\\nATOM   2042  CA  ARG A1096      25.730  -9.168  28.728  1.00 86.04           C\\nANISOU 2042  CA  ARG A1096    13368  10402   8921   -614    110    159       C\\nATOM   2043  C   ARG A1096      26.623  -8.481  29.750  1.00 81.52           C\\nANISOU 2043  C   ARG A1096    12598   9829   8548   -445    250    350       C\\nATOM   2044  O   ARG A1096      27.697  -8.997  30.076  1.00 76.37           O\\nANISOU 2044  O   ARG A1096    11967   9110   7940   -359    548    380       O\\nATOM   2045  CB  ARG A1096      26.072  -8.706  27.313  1.00 85.80           C\\nANISOU 2045  CB  ARG A1096    13637  10453   8510   -686     38    205       C\\nATOM   2046  CG  ARG A1096      26.974  -9.657  26.568  1.00 82.89           C\\nANISOU 2046  CG  ARG A1096    13541  10054   7898   -716    389     63       C\\nATOM   2047  CD  ARG A1096      27.247  -9.180  25.159  1.00 85.44           C\\nANISOU 2047  CD  ARG A1096    14183  10531   7750   -844    350    102       C\\nATOM   2048  NE  ARG A1096      26.098  -9.355  24.282  1.00 94.36           N\\nANISOU 2048  NE  ARG A1096    15514  11710   8629  -1018     -6    -32       N\\nATOM   2049  CZ  ARG A1096      26.167  -9.297  22.957  1.00 97.59           C\\nANISOU 2049  CZ  ARG A1096    16291  12257   8531  -1179    -60    -72       C\\nATOM   2050  NH1 ARG A1096      27.333  -9.075  22.369  1.00 93.17           N\\nANISOU 2050  NH1 ARG A1096    15919  11820   7663  -1201    286      6       N\\nATOM   2051  NH2 ARG A1096      25.078  -9.465  22.222  1.00102.27           N\\nANISOU 2051  NH2 ARG A1096    17053  12899   8906  -1338   -456   -197       N\\nATOM   2052  N   ALA A1097      26.196  -7.325  30.270  1.00 83.15           N\\nANISOU 2052  N   ALA A1097    12599  10095   8899   -381     10    450       N\\nATOM   2053  CA  ALA A1097      26.963  -6.656  31.316  1.00 74.83           C\\nANISOU 2053  CA  ALA A1097    11361   9035   8036   -245    100    585       C\\nATOM   2054  C   ALA A1097      26.946  -7.446  32.617  1.00 73.67           C\\nANISOU 2054  C   ALA A1097    11047   8874   8072   -207    277    525       C\\nATOM   2055  O   ALA A1097      27.942  -7.452  33.348  1.00 74.45           O\\nANISOU 2055  O   ALA A1097    11087   8949   8253   -111    442    628       O\\nATOM   2056  CB  ALA A1097      26.423  -5.246  31.550  1.00 63.51           C\\nANISOU 2056  CB  ALA A1097     9778   7621   6732   -175   -226    643       C\\nATOM   2057  N   ALA A1098      25.832  -8.117  32.923  1.00 71.99           N\\nANISOU 2057  N   ALA A1098    10755   8685   7912   -311    230    379       N\\nATOM   2058  CA  ALA A1098      25.774  -8.940  34.125  1.00 74.69           C\\nANISOU 2058  CA  ALA A1098    11001   9011   8365   -346    407    373       C\\nATOM   2059  C   ALA A1098      26.760 -10.098  34.047  1.00 83.58           C\\nANISOU 2059  C   ALA A1098    12344   9949   9462   -326    646    434       C\\nATOM   2060  O   ALA A1098      27.358 -10.485  35.059  1.00 82.43           O\\nANISOU 2060  O   ALA A1098    12168   9750   9403   -262    768    547       O\\nATOM   2061  CB  ALA A1098      24.351  -9.450  34.338  1.00 76.99           C\\nANISOU 2061  CB  ALA A1098    11160   9381   8710   -537    335    213       C\\nATOM   2062  N   LEU A1099      26.946 -10.665  32.852  1.00 86.05           N\\nANISOU 2062  N   LEU A1099    12886  10156   9651   -363    693    343       N\\nATOM   2063  CA  LEU A1099      27.950 -11.710  32.691  1.00 84.37           C\\nANISOU 2063  CA  LEU A1099    12858   9742   9457   -276    922    336       C\\nATOM   2064  C   LEU A1099      29.360 -11.153  32.838  1.00 75.62           C\\nANISOU 2064  C   LEU A1099    11669   8675   8388    -65   1050    473       C\\nATOM   2065  O   LEU A1099      30.242 -11.829  33.380  1.00 59.72           O\\nANISOU 2065  O   LEU A1099     9651   6525   6517     79   1192    528       O\\nATOM   2066  CB  LEU A1099      27.785 -12.397  31.335  1.00 88.81           C\\nANISOU 2066  CB  LEU A1099    13687  10211   9847   -362    961    126       C\\nATOM   2067  CG  LEU A1099      28.635 -13.647  31.091  1.00 89.13           C\\nANISOU 2067  CG  LEU A1099    13929   9988   9947   -253   1195     11       C\\nATOM   2068  CD1 LEU A1099      28.246 -14.750  32.060  1.00 88.78           C\\nANISOU 2068  CD1 LEU A1099    13929   9678  10126   -318   1188     43       C\\nATOM   2069  CD2 LEU A1099      28.496 -14.118  29.655  1.00 91.08           C\\nANISOU 2069  CD2 LEU A1099    14451  10201   9955   -337   1240   -262       C\\nATOM   2070  N   ILE A1100      29.591  -9.928  32.363  1.00 70.27           N\\nANISOU 2070  N   ILE A1100    10921   8168   7612    -56    974    541       N\\nATOM   2071  CA  ILE A1100      30.888  -9.294  32.557  1.00 70.30           C\\nANISOU 2071  CA  ILE A1100    10796   8234   7680     77   1083    680       C\\nATOM   2072  C   ILE A1100      31.120  -9.006  34.034  1.00 76.98           C\\nANISOU 2072  C   ILE A1100    11428   9092   8729    165   1006    808       C\\nATOM   2073  O   ILE A1100      32.244  -9.120  34.537  1.00 80.54           O\\nANISOU 2073  O   ILE A1100    11764   9529   9310    301   1104    897       O\\nATOM   2074  CB  ILE A1100      30.983  -8.022  31.697  1.00 68.88           C\\nANISOU 2074  CB  ILE A1100    10638   8193   7340    -10    989    761       C\\nATOM   2075  CG1 ILE A1100      30.869  -8.386  30.212  1.00 75.73           C\\nANISOU 2075  CG1 ILE A1100    11771   9090   7912   -120   1082    646       C\\nATOM   2076  CG2 ILE A1100      32.279  -7.281  31.978  1.00 63.94           C\\nANISOU 2076  CG2 ILE A1100     9841   7638   6817     56   1090    917       C\\nATOM   2077  CD1 ILE A1100      30.869  -7.196  29.275  1.00 65.67           C\\nANISOU 2077  CD1 ILE A1100    10607   7938   6405   -260    954    784       C\\nATOM   2078  N   ASN A1101      30.057  -8.645  34.757  1.00 76.26           N\\nANISOU 2078  N   ASN A1101    11262   9055   8656     88    828    795       N\\nATOM   2079  CA  ASN A1101      30.161  -8.449  36.200  1.00 71.74           C\\nANISOU 2079  CA  ASN A1101    10532   8535   8191    138    773    876       C\\nATOM   2080  C   ASN A1101      30.619  -9.725  36.896  1.00 69.64           C\\nANISOU 2080  C   ASN A1101    10339   8134   7987    190    891    949       C\\nATOM   2081  O   ASN A1101      31.439  -9.679  37.821  1.00 64.42           O\\nANISOU 2081  O   ASN A1101     9588   7486   7403    297    869   1078       O\\nATOM   2082  CB  ASN A1101      28.811  -7.981  36.750  1.00 72.99           C\\nANISOU 2082  CB  ASN A1101    10589   8814   8330     34    629    774       C\\nATOM   2083  CG  ASN A1101      28.882  -7.542  38.204  1.00 79.76           C\\nANISOU 2083  CG  ASN A1101    11293   9793   9219     68    586    807       C\\nATOM   2084  OD1 ASN A1101      29.385  -8.264  39.065  1.00 88.11           O\\nANISOU 2084  OD1 ASN A1101    12391  10824  10262     80    664    919       O\\nATOM   2085  ND2 ASN A1101      28.363  -6.353  38.484  1.00 77.04           N\\nANISOU 2085  ND2 ASN A1101    10794   9569   8909     92    434    696       N\\nATOM   2086  N   MET A1102      30.111 -10.877  36.452  1.00 67.47           N\\nANISOU 2086  N   MET A1102    10246   7696   7691    110    973    875       N\\nATOM   2087  CA  MET A1102      30.457 -12.137  37.100  1.00 68.00           C\\nANISOU 2087  CA  MET A1102    10442   7546   7851    150   1035    971       C\\nATOM   2088  C   MET A1102      31.900 -12.539  36.815  1.00 75.21           C\\nANISOU 2088  C   MET A1102    11354   8314   8910    407   1126   1011       C\\nATOM   2089  O   MET A1102      32.611 -12.984  37.723  1.00 77.63           O\\nANISOU 2089  O   MET A1102    11635   8519   9341    543   1075   1172       O\\nATOM   2090  CB  MET A1102      29.492 -13.233  36.655  1.00 70.40           C\\nANISOU 2090  CB  MET A1102    10958   7659   8132    -38   1075    861       C\\nATOM   2091  CG  MET A1102      28.072 -13.024  37.150  1.00 76.57           C\\nANISOU 2091  CG  MET A1102    11663   8605   8824   -310   1005    826       C\\nATOM   2092  SD  MET A1102      27.010 -14.445  36.822  1.00 81.97           S\\nANISOU 2092  SD  MET A1102    12572   9042   9532   -608   1039    733       S\\nATOM   2093  CE  MET A1102      27.916 -15.743  37.652  1.00 80.68           C\\nANISOU 2093  CE  MET A1102    12664   8490   9502   -523   1086    972       C\\nATOM   2094  N   VAL A1103      32.352 -12.395  35.565  1.00 79.58           N\\nANISOU 2094  N   VAL A1103    11918   8879   9439    475   1257    861       N\\nATOM   2095  CA  VAL A1103      33.743 -12.721  35.251  1.00 82.54           C\\nANISOU 2095  CA  VAL A1103    12205   9184   9974    728   1400    840       C\\nATOM   2096  C   VAL A1103      34.689 -11.726  35.912  1.00 80.24           C\\nANISOU 2096  C   VAL A1103    11618   9095   9774    826   1331   1000       C\\nATOM   2097  O   VAL A1103      35.848 -12.053  36.198  1.00 82.23           O\\nANISOU 2097  O   VAL A1103    11705   9299  10238   1051   1366   1045       O\\nATOM   2098  CB  VAL A1103      33.969 -12.782  33.727  1.00 84.75           C\\nANISOU 2098  CB  VAL A1103    12570   9500  10133    729   1619    609       C\\nATOM   2099  CG1 VAL A1103      32.942 -13.689  33.066  1.00 85.19           C\\nANISOU 2099  CG1 VAL A1103    12933   9364  10070    590   1631    415       C\\nATOM   2100  CG2 VAL A1103      33.931 -11.394  33.115  1.00 83.71           C\\nANISOU 2100  CG2 VAL A1103    12339   9665   9801    582   1615    646       C\\nATOM   2101  N   PHE A1104      34.222 -10.502  36.163  1.00 72.46           N\\nANISOU 2101  N   PHE A1104    10543   8321   8669    670   1206   1064       N\\nATOM   2102  CA  PHE A1104      35.025  -9.556  36.927  1.00 74.27           C\\nANISOU 2102  CA  PHE A1104    10521   8703   8994    721   1090   1196       C\\nATOM   2103  C   PHE A1104      35.203 -10.013  38.369  1.00 79.15           C\\nANISOU 2103  C   PHE A1104    11108   9268   9696    808    920   1340       C\\nATOM   2104  O   PHE A1104      36.258  -9.779  38.969  1.00 81.90           O\\nANISOU 2104  O   PHE A1104    11250   9676  10191    937    827   1439       O\\nATOM   2105  CB  PHE A1104      34.382  -8.171  36.883  1.00 67.54           C\\nANISOU 2105  CB  PHE A1104     9633   8010   8019    545    959   1195       C\\nATOM   2106  CG  PHE A1104      35.032  -7.234  35.911  1.00 71.68           C\\nANISOU 2106  CG  PHE A1104    10068   8632   8534    483   1036   1205       C\\nATOM   2107  CD1 PHE A1104      34.785  -7.340  34.554  1.00 74.18           C\\nANISOU 2107  CD1 PHE A1104    10546   8950   8690    396   1191   1126       C\\nATOM   2108  CD2 PHE A1104      35.892  -6.243  36.356  1.00 80.86           C\\nANISOU 2108  CD2 PHE A1104    11011   9893   9821    465    944   1303       C\\nATOM   2109  CE1 PHE A1104      35.384  -6.477  33.659  1.00 78.16           C\\nANISOU 2109  CE1 PHE A1104    11011   9565   9121    278   1280   1183       C\\nATOM   2110  CE2 PHE A1104      36.492  -5.376  35.467  1.00 85.63           C\\nANISOU 2110  CE2 PHE A1104    11550  10576  10412    335   1028   1354       C\\nATOM   2111  CZ  PHE A1104      36.238  -5.493  34.115  1.00 81.25           C\\nANISOU 2111  CZ  PHE A1104    11176  10035   9661    234   1209   1314       C\\nATOM   2112  N   GLN A1105      34.192 -10.669  38.935  1.00 80.45           N\\nANISOU 2112  N   GLN A1105    11475   9341   9754    708    866   1365       N\\nATOM   2113  CA  GLN A1105      34.237 -11.118  40.319  1.00 76.17           C\\nANISOU 2113  CA  GLN A1105    10978   8769   9193    723    706   1544       C\\nATOM   2114  C   GLN A1105      34.839 -12.508  40.465  1.00 79.87           C\\nANISOU 2114  C   GLN A1105    11579   8938   9829    899    695   1660       C\\nATOM   2115  O   GLN A1105      35.670 -12.731  41.352  1.00 77.78           O\\nANISOU 2115  O   GLN A1105    11252   8640   9660   1051    517   1841       O\\nATOM   2116  CB  GLN A1105      32.830 -11.107  40.918  1.00 71.88           C\\nANISOU 2116  CB  GLN A1105    10574   8313   8426    472    687   1531       C\\nATOM   2117  CG  GLN A1105      32.752 -11.692  42.313  1.00 71.95           C\\nANISOU 2117  CG  GLN A1105    10707   8315   8315    408    569   1741       C\\nATOM   2118  CD  GLN A1105      31.379 -11.534  42.928  1.00 72.70           C\\nANISOU 2118  CD  GLN A1105    10864   8598   8159    121    622   1689       C\\nATOM   2119  OE1 GLN A1105      30.414 -11.193  42.241  1.00 76.06           O\\nANISOU 2119  OE1 GLN A1105    11232   9099   8567     -1    727   1488       O\\nATOM   2120  NE2 GLN A1105      31.282 -11.777  44.230  1.00 68.30           N\\nANISOU 2120  NE2 GLN A1105    10410   8146   7396      7    545   1865       N\\nATOM   2121  N   MET A1106      34.433 -13.446  39.607  1.00 80.28           N\\nANISOU 2121  N   MET A1106    11826   8743   9934    892    842   1548       N\\nATOM   2122  CA  MET A1106      34.803 -14.847  39.734  1.00 82.95           C\\nANISOU 2122  CA  MET A1106    12358   8697  10463   1051    807   1630       C\\nATOM   2123  C   MET A1106      35.843 -15.311  38.725  1.00 89.43           C\\nANISOU 2123  C   MET A1106    13075   9350  11554   1362    949   1444       C\\nATOM   2124  O   MET A1106      36.305 -16.452  38.830  1.00 92.75           O\\nANISOU 2124  O   MET A1106    13623   9404  12215   1580    890   1476       O\\nATOM   2125  CB  MET A1106      33.551 -15.727  39.604  1.00 79.57           C\\nANISOU 2125  CB  MET A1106    12259   8043   9930    793    855   1607       C\\nATOM   2126  CG  MET A1106      32.706 -15.755  40.856  1.00 84.73           C\\nANISOU 2126  CG  MET A1106    13038   8785  10370    512    733   1843       C\\nATOM   2127  SD  MET A1106      30.984 -16.135  40.503  1.00 86.03           S\\nANISOU 2127  SD  MET A1106    13388   8937  10364     82    862   1721       S\\nATOM   2128  CE  MET A1106      30.421 -14.540  39.929  1.00 88.27           C\\nANISOU 2128  CE  MET A1106    13356   9694  10490     13    937   1471       C\\nATOM   2129  N   GLY A1107      36.219 -14.477  37.763  1.00 83.47           N\\nANISOU 2129  N   GLY A1107    12104   8844  10768   1383   1136   1249       N\\nATOM   2130  CA  GLY A1107      37.045 -14.923  36.668  1.00 86.98           C\\nANISOU 2130  CA  GLY A1107    12460   9202  11389   1617   1365   1006       C\\nATOM   2131  C   GLY A1107      36.292 -15.824  35.707  1.00 88.79           C\\nANISOU 2131  C   GLY A1107    13014   9179  11544   1543   1521    764       C\\nATOM   2132  O   GLY A1107      35.264 -16.426  36.027  1.00 86.13           O\\nANISOU 2132  O   GLY A1107    12973   8625  11128   1354   1409    824       O\\nATOM   2133  N   GLU A1108      36.843 -15.917  34.497  1.00 89.49           N\\nANISOU 2133  N   GLU A1108    13038   9319  11644   1667   1796    468       N\\nATOM   2134  CA  GLU A1108      36.262 -16.761  33.464  1.00 87.52           C\\nANISOU 2134  CA  GLU A1108    13103   8850  11300   1613   1951    163       C\\nATOM   2135  C   GLU A1108      36.230 -18.231  33.861  1.00 85.64           C\\nANISOU 2135  C   GLU A1108    13113   8070  11356   1798   1837    124       C\\nATOM   2136  O   GLU A1108      35.365 -18.973  33.377  1.00 84.49           O\\nANISOU 2136  O   GLU A1108    13313   7661  11130   1634   1842    -46       O\\nATOM   2137  CB  GLU A1108      37.029 -16.590  32.160  1.00 95.88           C\\nANISOU 2137  CB  GLU A1108    14037  10114  12279   1733   2303   -169       C\\nATOM   2138  CG  GLU A1108      36.931 -15.181  31.598  1.00102.62           C\\nANISOU 2138  CG  GLU A1108    14756  11443  12792   1470   2402   -100       C\\nATOM   2139  CD  GLU A1108      37.375 -15.104  30.157  1.00109.37           C\\nANISOU 2139  CD  GLU A1108    15629  12514  13413   1456   2771   -421       C\\nATOM   2140  OE1 GLU A1108      37.716 -16.168  29.591  1.00113.53           O\\nANISOU 2140  OE1 GLU A1108    16260  12832  14044   1672   2970   -764       O\\nATOM   2141  OE2 GLU A1108      37.380 -13.985  29.593  1.00105.41           O\\nANISOU 2141  OE2 GLU A1108    15063  12377  12612   1221   2859   -335       O\\nATOM   2142  N   THR A1109      37.155 -18.669  34.719  1.00 90.70           N\\nANISOU 2142  N   THR A1109    13597   8510  12353   2124   1695    286       N\\nATOM   2143  CA  THR A1109      37.120 -20.042  35.207  1.00 95.84           C\\nANISOU 2143  CA  THR A1109    14532   8571  13311   2298   1506    331       C\\nATOM   2144  C   THR A1109      35.855 -20.297  36.012  1.00 92.70           C\\nANISOU 2144  C   THR A1109    14477   8003  12741   1906   1273    629       C\\nATOM   2145  O   THR A1109      35.133 -21.269  35.766  1.00 95.09           O\\nANISOU 2145  O   THR A1109    15151   7895  13084   1765   1241    533       O\\nATOM   2146  CB  THR A1109      38.349 -20.335  36.066  1.00 97.86           C\\nANISOU 2146  CB  THR A1109    14535   8674  13974   2728   1309    517       C\\nATOM   2147  OG1 THR A1109      39.538 -19.920  35.381  1.00102.45           O\\nANISOU 2147  OG1 THR A1109    14672   9535  14718   3048   1561    242       O\\nATOM   2148  CG2 THR A1109      38.427 -21.828  36.376  1.00 97.85           C\\nANISOU 2148  CG2 THR A1109    14861   7969  14349   2976   1099    531       C\\nATOM   2149  N   GLY A1110      35.567 -19.420  36.975  1.00 95.75           N\\nANISOU 2149  N   GLY A1110    14731   8720  12931   1701   1128    965       N\\nATOM   2150  CA  GLY A1110      34.456 -19.660  37.880  1.00 94.88           C\\nANISOU 2150  CA  GLY A1110    14887   8513  12649   1331    949   1253       C\\nATOM   2151  C   GLY A1110      33.103 -19.552  37.204  1.00 88.67           C\\nANISOU 2151  C   GLY A1110    14261   7826  11602    922   1075   1072       C\\nATOM   2152  O   GLY A1110      32.191 -20.329  37.497  1.00 82.42           O\\nANISOU 2152  O   GLY A1110    13765   6760  10793    635    997   1160       O\\nATOM   2153  N   VAL A1111      32.952 -18.588  36.296  1.00 85.36           N\\nANISOU 2153  N   VAL A1111    13649   7799  10986    866   1244    836       N\\nATOM   2154  CA  VAL A1111      31.676 -18.422  35.606  1.00 83.59           C\\nANISOU 2154  CA  VAL A1111    13541   7694  10525    508   1297    660       C\\nATOM   2155  C   VAL A1111      31.371 -19.646  34.751  1.00 86.94           C\\nANISOU 2155  C   VAL A1111    14292   7686  11055    469   1346    385       C\\nATOM   2156  O   VAL A1111      30.217 -20.080  34.649  1.00 84.62           O\\nANISOU 2156  O   VAL A1111    14188   7281  10681    116   1284    338       O\\nATOM   2157  CB  VAL A1111      31.689 -17.125  34.776  1.00 78.72           C\\nANISOU 2157  CB  VAL A1111    12692   7539   9679    492   1403    508       C\\nATOM   2158  CG1 VAL A1111      30.403 -16.979  33.994  1.00 82.94           C\\nANISOU 2158  CG1 VAL A1111    13340   8183   9992    166   1385    324       C\\nATOM   2159  CG2 VAL A1111      31.894 -15.925  35.684  1.00 68.67           C\\nANISOU 2159  CG2 VAL A1111    11133   6621   8339    498   1317    755       C\\nATOM   2160  N   ALA A1112      32.402 -20.242  34.147  1.00 83.83           N\\nANISOU 2160  N   ALA A1112    13946   7039  10867    828   1457    166       N\\nATOM   2161  CA  ALA A1112      32.208 -21.434  33.331  1.00 86.95           C\\nANISOU 2161  CA  ALA A1112    14676   6976  11386    838   1502   -166       C\\nATOM   2162  C   ALA A1112      31.727 -22.636  34.137  1.00 97.68           C\\nANISOU 2162  C   ALA A1112    16361   7762  12989    696   1293     31       C\\nATOM   2163  O   ALA A1112      31.408 -23.672  33.541  1.00107.07           O\\nANISOU 2163  O   ALA A1112    17878   8495  14308    634   1283   -236       O\\nATOM   2164  CB  ALA A1112      33.504 -21.784  32.597  1.00 82.87           C\\nANISOU 2164  CB  ALA A1112    14088   6331  11068   1312   1699   -487       C\\nATOM   2165  N   GLY A1113      31.670 -22.528  35.467  1.00 94.08           N\\nANISOU 2165  N   GLY A1113    15859   7311  12576    613   1121    490       N\\nATOM   2166  CA  GLY A1113      31.127 -23.580  36.301  1.00 91.96           C\\nANISOU 2166  CA  GLY A1113    15934   6547  12461    374    924    767       C\\nATOM   2167  C   GLY A1113      29.632 -23.536  36.499  1.00 88.01           C\\nANISOU 2167  C   GLY A1113    15526   6189  11726   -228    907    854       C\\nATOM   2168  O   GLY A1113      29.067 -24.463  37.088  1.00 90.55           O\\nANISOU 2168  O   GLY A1113    16155   6098  12153   -532    780   1074       O\\nATOM   2169  N   PHE A1114      28.975 -22.477  36.030  1.00 89.32           N\\nANISOU 2169  N   PHE A1114    15419   6923  11597   -417   1020    697       N\\nATOM   2170  CA  PHE A1114      27.518 -22.347  36.101  1.00 93.06           C\\nANISOU 2170  CA  PHE A1114    15868   7604  11887   -955   1007    701       C\\nATOM   2171  C   PHE A1114      26.844 -22.935  34.867  1.00 97.68           C\\nANISOU 2171  C   PHE A1114    16640   7982  12490  -1154   1008    293       C\\nATOM   2172  O   PHE A1114      25.996 -22.294  34.250  1.00100.46           O\\nANISOU 2172  O   PHE A1114    16812   8720  12638  -1379   1016     94       O\\nATOM   2173  CB  PHE A1114      27.127 -20.883  36.266  1.00 94.49           C\\nANISOU 2173  CB  PHE A1114    15638   8468  11794  -1010   1062    728       C\\nATOM   2174  CG  PHE A1114      27.602 -20.258  37.542  1.00 95.33           C\\nANISOU 2174  CG  PHE A1114    15570   8818  11834   -900   1044   1086       C\\nATOM   2175  CD1 PHE A1114      26.863 -20.382  38.706  1.00 96.26           C\\nANISOU 2175  CD1 PHE A1114    15694   9032  11847  -1255   1023   1375       C\\nATOM   2176  CD2 PHE A1114      28.773 -19.521  37.572  1.00 93.76           C\\nANISOU 2176  CD2 PHE A1114    15190   8788  11647   -478   1057   1113       C\\nATOM   2177  CE1 PHE A1114      27.293 -19.799  39.881  1.00 93.49           C\\nANISOU 2177  CE1 PHE A1114    15219   8937  11366  -1170    999   1669       C\\nATOM   2178  CE2 PHE A1114      29.209 -18.933  38.743  1.00 90.99           C\\nANISOU 2178  CE2 PHE A1114    14688   8664  11219   -396    999   1410       C\\nATOM   2179  CZ  PHE A1114      28.468 -19.072  39.900  1.00 89.90           C\\nANISOU 2179  CZ  PHE A1114    14603   8619  10937   -731    961   1678       C\\nATOM   2180  N   THR A1115      27.213 -24.163  34.496  1.00 93.63           N\\nANISOU 2180  N   THR A1115    16502   6840  12234  -1062    963    146       N\\nATOM   2181  CA  THR A1115      26.755 -24.715  33.225  1.00 97.80           C\\nANISOU 2181  CA  THR A1115    17241   7160  12760  -1192    960   -325       C\\nATOM   2182  C   THR A1115      25.237 -24.821  33.175  1.00101.53           C\\nANISOU 2182  C   THR A1115    17699   7752  13126  -1809    862   -353       C\\nATOM   2183  O   THR A1115      24.618 -24.467  32.164  1.00100.69           O\\nANISOU 2183  O   THR A1115    17515   7914  12829  -1958    838   -694       O\\nATOM   2184  CB  THR A1115      27.395 -26.081  32.984  1.00104.56           C\\nANISOU 2184  CB  THR A1115    18523   7240  13966   -980    909   -494       C\\nATOM   2185  OG1 THR A1115      26.936 -27.010  33.974  1.00111.74           O\\nANISOU 2185  OG1 THR A1115    19700   7650  15106  -1304    745   -134       O\\nATOM   2186  CG2 THR A1115      28.912 -25.975  33.059  1.00103.25           C\\nANISOU 2186  CG2 THR A1115    18273   6991  13964   -334   1002   -493       C\\nATOM   2187  N   ASN A1116      24.617 -25.292  34.259  1.00109.01           N\\nANISOU 2187  N   ASN A1116    18703   8536  14180  -2193    797     12       N\\nATOM   2188  CA  ASN A1116      23.168 -25.450  34.256  1.00114.25           C\\nANISOU 2188  CA  ASN A1116    19286   9335  14790  -2821    734    -24       C\\nATOM   2189  C   ASN A1116      22.464 -24.103  34.180  1.00108.33           C\\nANISOU 2189  C   ASN A1116    18027   9368  13766  -2910    776    -69       C\\nATOM   2190  O   ASN A1116      21.401 -23.993  33.560  1.00112.39           O\\nANISOU 2190  O   ASN A1116    18389  10096  14219  -3257    688   -317       O\\nATOM   2191  CB  ASN A1116      22.716 -26.227  35.496  1.00119.12           C\\nANISOU 2191  CB  ASN A1116    20066   9646  15546  -3254    712    417       C\\nATOM   2192  N   SER A1117      23.040 -23.071  34.794  1.00107.10           N\\nANISOU 2192  N   SER A1117    17599   9621  13474  -2592    871    149       N\\nATOM   2193  CA  SER A1117      22.434 -21.748  34.719  1.00102.31           C\\nANISOU 2193  CA  SER A1117    16531   9686  12658  -2613    880     85       C\\nATOM   2194  C   SER A1117      22.674 -21.101  33.361  1.00102.29           C\\nANISOU 2194  C   SER A1117    16484   9870  12513  -2343    814   -265       C\\nATOM   2195  O   SER A1117      21.756 -20.507  32.785  1.00100.23           O\\nANISOU 2195  O   SER A1117    15984   9960  12139  -2521    696   -453       O\\nATOM   2196  CB  SER A1117      22.981 -20.857  35.835  1.00 98.47           C\\nANISOU 2196  CB  SER A1117    15811   9527  12076  -2381    982    404       C\\nATOM   2197  OG  SER A1117      22.892 -21.504  37.092  1.00 97.73           O\\nANISOU 2197  OG  SER A1117    15842   9258  12035  -2624   1039    761       O\\nATOM   2198  N   LEU A1118      23.897 -21.215  32.836  1.00104.26           N\\nANISOU 2198  N   LEU A1118    16951   9904  12761  -1923    883   -351       N\\nATOM   2199  CA  LEU A1118      24.243 -20.548  31.585  1.00100.23           C\\nANISOU 2199  CA  LEU A1118    16425   9622  12038  -1690    875   -637       C\\nATOM   2200  C   LEU A1118      23.389 -21.046  30.427  1.00107.73           C\\nANISOU 2200  C   LEU A1118    17547  10492  12892  -1976    724  -1011       C\\nATOM   2201  O   LEU A1118      23.041 -20.274  29.525  1.00110.02           O\\nANISOU 2201  O   LEU A1118    17736  11135  12931  -1982    613  -1185       O\\nATOM   2202  CB  LEU A1118      25.722 -20.757  31.279  1.00 92.05           C\\nANISOU 2202  CB  LEU A1118    15569   8366  11040  -1233   1041   -692       C\\nATOM   2203  CG  LEU A1118      26.695 -19.998  32.171  1.00 86.98           C\\nANISOU 2203  CG  LEU A1118    14695   7910  10443   -907   1144   -375       C\\nATOM   2204  CD1 LEU A1118      28.100 -20.549  32.003  1.00 86.56           C\\nANISOU 2204  CD1 LEU A1118    14792   7548  10551   -488   1291   -444       C\\nATOM   2205  CD2 LEU A1118      26.654 -18.516  31.846  1.00 86.67           C\\nANISOU 2205  CD2 LEU A1118    14359   8413  10159   -835   1133   -349       C\\nATOM   2206  N   ARG A1119      23.046 -22.333  30.429  1.00104.44           N\\nANISOU 2206  N   ARG A1119    17422   9590  12668  -2232    680  -1129       N\\nATOM   2207  CA  ARG A1119      22.191 -22.858  29.372  1.00103.70           C\\nANISOU 2207  CA  ARG A1119    17500   9406  12496  -2554    498  -1514       C\\nATOM   2208  C   ARG A1119      20.795 -22.250  29.433  1.00102.63           C\\nANISOU 2208  C   ARG A1119    16991   9707  12297  -2952    292  -1490       C\\nATOM   2209  O   ARG A1119      20.133 -22.113  28.398  1.00102.11           O\\nANISOU 2209  O   ARG A1119    16930   9811  12055  -3119     75  -1792       O\\nATOM   2210  CB  ARG A1119      22.123 -24.383  29.466  1.00105.66           C\\nANISOU 2210  CB  ARG A1119    18150   8971  13026  -2774    474  -1635       C\\nATOM   2211  CG  ARG A1119      21.461 -25.066  28.282  1.00110.68           C\\nANISOU 2211  CG  ARG A1119    19053   9414  13586  -3068    283  -2116       C\\nATOM   2212  CD  ARG A1119      21.400 -26.576  28.478  1.00119.37           C\\nANISOU 2212  CD  ARG A1119    20574   9750  15030  -3303    239  -2220       C\\nATOM   2213  NE  ARG A1119      20.881 -26.936  29.795  1.00121.59           N\\nANISOU 2213  NE  ARG A1119    20741   9865  15590  -3652    240  -1772       N\\nATOM   2214  CZ  ARG A1119      21.609 -27.484  30.763  1.00120.23           C\\nANISOU 2214  CZ  ARG A1119    20757   9256  15669  -3483    350  -1432       C\\nATOM   2215  NH1 ARG A1119      22.893 -27.748  30.561  1.00119.50           N\\nANISOU 2215  NH1 ARG A1119    20917   8831  15658  -2927    455  -1524       N\\nATOM   2216  NH2 ARG A1119      21.053 -27.772  31.933  1.00120.62           N\\nANISOU 2216  NH2 ARG A1119    20732   9219  15878  -3878    351  -1000       N\\nATOM   2217  N   MET A1120      20.338 -21.863  30.627  1.00100.48           N\\nANISOU 2217  N   MET A1120    16375   9649  12155  -3093    347  -1158       N\\nATOM   2218  CA  MET A1120      19.012 -21.263  30.756  1.00103.10           C\\nANISOU 2218  CA  MET A1120    16260  10430  12486  -3427    184  -1176       C\\nATOM   2219  C   MET A1120      19.000 -19.818  30.272  1.00100.31           C\\nANISOU 2219  C   MET A1120    15604  10594  11915  -3129     66  -1209       C\\nATOM   2220  O   MET A1120      18.009 -19.365  29.686  1.00100.24           O\\nANISOU 2220  O   MET A1120    15342  10888  11857  -3303   -198  -1388       O\\nATOM   2221  CB  MET A1120      18.535 -21.349  32.203  1.00106.18           C\\nANISOU 2221  CB  MET A1120    16380  10910  13054  -3686    341   -856       C\\nATOM   2222  CG  MET A1120      18.420 -22.776  32.714  1.00117.71           C\\nANISOU 2222  CG  MET A1120    18166  11832  14725  -4073    415   -750       C\\nATOM   2223  SD  MET A1120      17.789 -22.885  34.401  1.00123.98           S\\nANISOU 2223  SD  MET A1120    18683  12804  15620  -4485    629   -335       S\\nATOM   2224  CE  MET A1120      17.761 -24.663  34.625  1.00131.09           C\\nANISOU 2224  CE  MET A1120    20134  12916  16760  -4951    624   -214       C\\nATOM   2225  N   LEU A1121      20.082 -19.075  30.519  1.00100.35           N\\nANISOU 2225  N   LEU A1121    15626  10687  11815  -2692    222  -1026       N\\nATOM   2226  CA  LEU A1121      20.236 -17.769  29.884  1.00100.41           C\\nANISOU 2226  CA  LEU A1121    15473  11071  11608  -2415     91  -1049       C\\nATOM   2227  C   LEU A1121      20.299 -17.911  28.369  1.00105.95           C\\nANISOU 2227  C   LEU A1121    16480  11732  12045  -2411    -85  -1340       C\\nATOM   2228  O   LEU A1121      19.794 -17.057  27.629  1.00108.90           O\\nANISOU 2228  O   LEU A1121    16728  12416  12235  -2399   -355  -1411       O\\nATOM   2229  CB  LEU A1121      21.498 -17.077  30.396  1.00 89.96           C\\nANISOU 2229  CB  LEU A1121    14156   9787  10238  -2005    306   -807       C\\nATOM   2230  CG  LEU A1121      21.578 -16.711  31.874  1.00 82.79           C\\nANISOU 2230  CG  LEU A1121    12972   8988   9494  -1956    454   -522       C\\nATOM   2231  CD1 LEU A1121      22.975 -16.220  32.204  1.00 72.92           C\\nANISOU 2231  CD1 LEU A1121    11799   7708   8200  -1566    625   -331       C\\nATOM   2232  CD2 LEU A1121      20.549 -15.649  32.207  1.00 85.66           C\\nANISOU 2232  CD2 LEU A1121    12882   9776   9890  -2027    296   -524       C\\nATOM   2233  N   GLN A1122      20.920 -18.991  27.892  1.00 98.13           N\\nANISOU 2233  N   GLN A1122    15913  10351  11023  -2411     46  -1520       N\\nATOM   2234  CA  GLN A1122      21.020 -19.232  26.459  1.00 98.26           C\\nANISOU 2234  CA  GLN A1122    16271  10336  10727  -2427    -75  -1857       C\\nATOM   2235  C   GLN A1122      19.667 -19.584  25.852  1.00 96.39           C\\nANISOU 2235  C   GLN A1122    15998  10161  10466  -2846   -440  -2111       C\\nATOM   2236  O   GLN A1122      19.425 -19.301  24.674  1.00 98.68           O\\nANISOU 2236  O   GLN A1122    16445  10634  10417  -2889   -682  -2330       O\\nATOM   2237  CB  GLN A1122      22.036 -20.346  26.201  1.00103.05           C\\nANISOU 2237  CB  GLN A1122    17309  10483  11362  -2283    189  -2053       C\\nATOM   2238  CG  GLN A1122      22.347 -20.616  24.747  1.00107.55           C\\nANISOU 2238  CG  GLN A1122    18269  11042  11552  -2252    165  -2458       C\\nATOM   2239  CD  GLN A1122      23.447 -21.645  24.581  1.00111.75           C\\nANISOU 2239  CD  GLN A1122    19160  11128  12172  -2017    475  -2696       C\\nATOM   2240  OE1 GLN A1122      24.039 -22.100  25.559  1.00115.12           O\\nANISOU 2240  OE1 GLN A1122    19540  11237  12962  -1840    666  -2506       O\\nATOM   2241  NE2 GLN A1122      23.726 -22.017  23.338  1.00113.25           N\\nANISOU 2241  NE2 GLN A1122    19714  11294  12023  -1998    511  -3131       N\\nATOM   2242  N   GLN A1123      18.773 -20.184  26.639  1.00102.08           N\\nANISOU 2242  N   GLN A1123    16506  10761  11521  -3189   -495  -2073       N\\nATOM   2243  CA  GLN A1123      17.459 -20.603  26.168  1.00103.74           C\\nANISOU 2243  CA  GLN A1123    16604  11025  11786  -3643   -839  -2321       C\\nATOM   2244  C   GLN A1123      16.362 -19.590  26.496  1.00108.72           C\\nANISOU 2244  C   GLN A1123    16638  12153  12517  -3742  -1093  -2203       C\\nATOM   2245  O   GLN A1123      15.179 -19.947  26.486  1.00110.87           O\\nANISOU 2245  O   GLN A1123    16643  12510  12973  -4152  -1332  -2352       O\\nATOM   2246  CB  GLN A1123      17.101 -21.971  26.754  1.00101.84           C\\nANISOU 2246  CB  GLN A1123    16492  10326  11878  -4039   -744  -2378       C\\nATOM   2247  CG  GLN A1123      17.964 -23.119  26.251  1.00 99.00           C\\nANISOU 2247  CG  GLN A1123    16739   9389  11487  -3971   -604  -2613       C\\nATOM   2248  CD  GLN A1123      17.609 -24.442  26.905  1.00109.60           C\\nANISOU 2248  CD  GLN A1123    18244  10191  13208  -4372   -553  -2607       C\\nATOM   2249  OE1 GLN A1123      17.694 -24.589  28.124  1.00109.83           O\\nANISOU 2249  OE1 GLN A1123    18131  10108  13491  -4423   -352  -2243       O\\nATOM   2250  NE2 GLN A1123      17.200 -25.410  26.095  1.00111.61           N\\nANISOU 2250  NE2 GLN A1123    18833  10095  13478  -4692   -754  -3005       N\\nATOM   2251  N   LYS A1124      16.728 -18.344  26.794  1.00101.10           N\\nANISOU 2251  N   LYS A1124    15436  11503  11475  -3376  -1053  -1965       N\\nATOM   2252  CA  LYS A1124      15.801 -17.264  27.128  1.00102.00           C\\nANISOU 2252  CA  LYS A1124    14979  12055  11722  -3354  -1290  -1880       C\\nATOM   2253  C   LYS A1124      14.956 -17.560  28.362  1.00106.14           C\\nANISOU 2253  C   LYS A1124    15026  12671  12629  -3642  -1145  -1813       C\\nATOM   2254  O   LYS A1124      13.969 -16.858  28.613  1.00108.27           O\\nANISOU 2254  O   LYS A1124    14746  13316  13075  -3688  -1344  -1851       O\\nATOM   2255  CB  LYS A1124      14.875 -16.927  25.950  1.00104.85           C\\nANISOU 2255  CB  LYS A1124    15253  12649  11937  -3482  -1823  -2115       C\\nATOM   2256  CG  LYS A1124      15.585 -16.569  24.655  1.00106.34           C\\nANISOU 2256  CG  LYS A1124    15931  12827  11648  -3267  -1994  -2170       C\\nATOM   2257  CD  LYS A1124      16.318 -15.246  24.762  1.00102.53           C\\nANISOU 2257  CD  LYS A1124    15411  12521  11026  -2834  -1939  -1876       C\\nATOM   2258  CE  LYS A1124      16.710 -14.725  23.392  1.00104.63           C\\nANISOU 2258  CE  LYS A1124    16088  12882  10786  -2721  -2205  -1897       C\\nATOM   2259  NZ  LYS A1124      15.510 -14.429  22.560  1.00109.17           N\\nANISOU 2259  NZ  LYS A1124    16517  13684  11279  -2897  -2828  -2043       N\\nATOM   2260  N   ARG A1125      15.311 -18.583  29.142  1.00109.81           N\\nANISOU 2260  N   ARG A1125    15685  12809  13228  -3839   -806  -1713       N\\nATOM   2261  CA  ARG A1125      14.563 -18.937  30.349  1.00105.46           C\\nANISOU 2261  CA  ARG A1125    14749  12354  12966  -4188   -611  -1603       C\\nATOM   2262  C   ARG A1125      15.011 -18.038  31.502  1.00105.15           C\\nANISOU 2262  C   ARG A1125    14454  12555  12943  -3878   -338  -1327       C\\nATOM   2263  O   ARG A1125      15.645 -18.469  32.467  1.00102.11           O\\nANISOU 2263  O   ARG A1125    14245  11977  12576  -3884    -12  -1083       O\\nATOM   2264  CB  ARG A1125      14.757 -20.408  30.687  1.00100.56           C\\nANISOU 2264  CB  ARG A1125    14519  11232  12456  -4562   -413  -1558       C\\nATOM   2265  CG  ARG A1125      14.118 -21.370  29.702  1.00104.76           C\\nANISOU 2265  CG  ARG A1125    15255  11516  13034  -4972   -689  -1879       C\\nATOM   2266  CD  ARG A1125      14.117 -22.790  30.251  1.00109.68           C\\nANISOU 2266  CD  ARG A1125    16197  11614  13861  -5418   -505  -1800       C\\nATOM   2267  NE  ARG A1125      15.435 -23.419  30.187  1.00111.71           N\\nANISOU 2267  NE  ARG A1125    17086  11317  14042  -5114   -333  -1714       N\\nATOM   2268  CZ  ARG A1125      15.756 -24.551  30.807  1.00114.79           C\\nANISOU 2268  CZ  ARG A1125    17840  11156  14619  -5338   -166  -1549       C\\nATOM   2269  NH1 ARG A1125      14.859 -25.182  31.553  1.00117.33           N\\nANISOU 2269  NH1 ARG A1125    17995  11419  15168  -5934   -115  -1411       N\\nATOM   2270  NH2 ARG A1125      16.978 -25.051  30.689  1.00114.27           N\\nANISOU 2270  NH2 ARG A1125    18294  10594  14529  -4971    -54  -1512       N\\nATOM   2271  N   TRP A1126      14.657 -16.753  31.387  1.00102.43           N\\nANISOU 2271  N   TRP A1126    13702  12620  12595  -3599   -520  -1377       N\\nATOM   2272  CA  TRP A1126      15.103 -15.775  32.375  1.00 99.11           C\\nANISOU 2272  CA  TRP A1126    13061  12418  12179  -3267   -310  -1183       C\\nATOM   2273  C   TRP A1126      14.567 -16.088  33.763  1.00100.00           C\\nANISOU 2273  C   TRP A1126    12842  12708  12447  -3564     17  -1092       C\\nATOM   2274  O   TRP A1126      15.235 -15.807  34.763  1.00 95.88           O\\nANISOU 2274  O   TRP A1126    12367  12211  11852  -3395    296   -877       O\\nATOM   2275  CB  TRP A1126      14.683 -14.363  31.959  1.00 98.18           C\\nANISOU 2275  CB  TRP A1126    12566  12644  12092  -2934   -622  -1293       C\\nATOM   2276  CG  TRP A1126      15.001 -14.027  30.537  1.00 99.97           C\\nANISOU 2276  CG  TRP A1126    13108  12760  12116  -2737   -990  -1360       C\\nATOM   2277  CD1 TRP A1126      14.127 -13.586  29.588  1.00102.49           C\\nANISOU 2277  CD1 TRP A1126    13224  13259  12460  -2750  -1458  -1549       C\\nATOM   2278  CD2 TRP A1126      16.280 -14.113  29.895  1.00100.88           C\\nANISOU 2278  CD2 TRP A1126    13796  12592  11940  -2519   -920  -1236       C\\nATOM   2279  NE1 TRP A1126      14.782 -13.387  28.397  1.00102.69           N\\nANISOU 2279  NE1 TRP A1126    13720  13132  12164  -2582  -1684  -1520       N\\nATOM   2280  CE2 TRP A1126      16.105 -13.705  28.559  1.00102.48           C\\nANISOU 2280  CE2 TRP A1126    14155  12841  11942  -2447  -1322  -1348       C\\nATOM   2281  CE3 TRP A1126      17.558 -14.494  30.321  1.00101.84           C\\nANISOU 2281  CE3 TRP A1126    14288  12451  11954  -2377   -563  -1048       C\\nATOM   2282  CZ2 TRP A1126      17.157 -13.666  27.646  1.00107.44           C\\nANISOU 2282  CZ2 TRP A1126    15302  13297  12222  -2277  -1308  -1288       C\\nATOM   2283  CZ3 TRP A1126      18.601 -14.457  29.411  1.00101.67           C\\nANISOU 2283  CZ3 TRP A1126    14713  12253  11664  -2171   -560  -1020       C\\nATOM   2284  CH2 TRP A1126      18.393 -14.051  28.088  1.00104.96           C\\nANISOU 2284  CH2 TRP A1126    15284  12756  11842  -2142   -895  -1146       C\\nATOM   2285  N   ASP A1127      13.370 -16.667  33.848  1.00105.05           N\\nANISOU 2285  N   ASP A1127    13142  13500  13273  -4040    -10  -1251       N\\nATOM   2286  CA  ASP A1127      12.801 -16.985  35.152  1.00105.65           C\\nANISOU 2286  CA  ASP A1127    12891  13805  13446  -4403    350  -1159       C\\nATOM   2287  C   ASP A1127      13.638 -18.034  35.873  1.00102.58           C\\nANISOU 2287  C   ASP A1127    13044  13002  12929  -4604    661   -828       C\\nATOM   2288  O   ASP A1127      14.085 -17.819  37.005  1.00 97.10           O\\nANISOU 2288  O   ASP A1127    12362  12413  12117  -4531    958   -598       O\\nATOM   2289  CB  ASP A1127      11.355 -17.458  34.988  1.00113.14           C\\nANISOU 2289  CB  ASP A1127    13346  15002  14642  -4937    260  -1403       C\\nATOM   2290  N   GLU A1128      13.877 -19.175  35.221  1.00105.05           N\\nANISOU 2290  N   GLU A1128    13834  12818  13263  -4840    560   -812       N\\nATOM   2291  CA  GLU A1128      14.589 -20.266  35.881  1.00101.37           C\\nANISOU 2291  CA  GLU A1128    13890  11878  12749  -5036    788   -497       C\\nATOM   2292  C   GLU A1128      16.064 -19.940  36.072  1.00 98.59           C\\nANISOU 2292  C   GLU A1128    13939  11292  12227  -4482    856   -278       C\\nATOM   2293  O   GLU A1128      16.652 -20.294  37.101  1.00 98.75           O\\nANISOU 2293  O   GLU A1128    14183  11164  12175  -4507   1075     48       O\\nATOM   2294  CB  GLU A1128      14.433 -21.557  35.083  1.00102.72           C\\nANISOU 2294  CB  GLU A1128    14465  11516  13047  -5400    625   -601       C\\nATOM   2295  CG  GLU A1128      13.004 -22.014  34.909  1.00109.16           C\\nANISOU 2295  CG  GLU A1128    14894  12518  14063  -6031    538   -807       C\\nATOM   2296  CD  GLU A1128      12.920 -23.465  34.496  1.00117.05           C\\nANISOU 2296  CD  GLU A1128    16374  12895  15205  -6501    444   -827       C\\nATOM   2297  OE1 GLU A1128      13.445 -24.324  35.236  1.00119.18           O\\nANISOU 2297  OE1 GLU A1128    17078  12716  15487  -6681    639   -499       O\\nATOM   2298  OE2 GLU A1128      12.343 -23.744  33.426  1.00122.20           O\\nANISOU 2298  OE2 GLU A1128    16997  13477  15956  -6685    137  -1171       O\\nATOM   2299  N   ALA A1129      16.686 -19.280  35.090  1.00106.39           N\\nANISOU 2299  N   ALA A1129    15026  12259  13140  -4007    658   -438       N\\nATOM   2300  CA  ALA A1129      18.089 -18.904  35.232  1.00 98.44           C\\nANISOU 2300  CA  ALA A1129    14315  11087  12002  -3503    734   -256       C\\nATOM   2301  C   ALA A1129      18.313 -18.065  36.481  1.00 99.96           C\\nANISOU 2301  C   ALA A1129    14247  11624  12110  -3345    925    -40       C\\nATOM   2302  O   ALA A1129      19.394 -18.111  37.080  1.00 91.71           O\\nANISOU 2302  O   ALA A1129    13458  10403  10986  -3100   1037    208       O\\nATOM   2303  CB  ALA A1129      18.562 -18.146  33.991  1.00 90.27           C\\nANISOU 2303  CB  ALA A1129    13335  10100  10864  -3097    524   -462       C\\nATOM   2304  N   ALA A1130      17.300 -17.301  36.894  1.00101.90           N\\nANISOU 2304  N   ALA A1130    13969  12366  12382  -3472    950   -165       N\\nATOM   2305  CA  ALA A1130      17.396 -16.557  38.143  1.00100.47           C\\nANISOU 2305  CA  ALA A1130    13541  12535  12097  -3370   1159    -30       C\\nATOM   2306  C   ALA A1130      17.236 -17.478  39.344  1.00 96.24           C\\nANISOU 2306  C   ALA A1130    13135  11951  11481  -3804   1437    243       C\\nATOM   2307  O   ALA A1130      17.958 -17.340  40.339  1.00 91.99           O\\nANISOU 2307  O   ALA A1130    12752  11434  10767  -3682   1586    498       O\\nATOM   2308  CB  ALA A1130      16.348 -15.446  38.172  1.00102.74           C\\nANISOU 2308  CB  ALA A1130    13205  13359  12471  -3324   1106   -319       C\\nATOM   2309  N   VAL A1131      16.303 -18.428  39.267  1.00 92.07           N\\nANISOU 2309  N   VAL A1131    12568  11350  11062  -4347   1484    213       N\\nATOM   2310  CA  VAL A1131      16.030 -19.294  40.409  1.00 92.71           C\\nANISOU 2310  CA  VAL A1131    12779  11404  11044  -4858   1755    513       C\\nATOM   2311  C   VAL A1131      17.210 -20.220  40.681  1.00 93.11           C\\nANISOU 2311  C   VAL A1131    13506  10845  11028  -4781   1726    899       C\\nATOM   2312  O   VAL A1131      17.533 -20.509  41.839  1.00 94.49           O\\nANISOU 2312  O   VAL A1131    13879  11018  11005  -4935   1900   1255       O\\nATOM   2313  CB  VAL A1131      14.728 -20.083  40.179  1.00 91.93           C\\nANISOU 2313  CB  VAL A1131    12455  11353  11120  -5514   1797    386       C\\nATOM   2314  N   ASN A1132      17.877 -20.696  39.626  1.00 98.73           N\\nANISOU 2314  N   ASN A1132    14580  11039  11893  -4528   1494    823       N\\nATOM   2315  CA  ASN A1132      19.028 -21.572  39.827  1.00 99.57           C\\nANISOU 2315  CA  ASN A1132    15279  10537  12016  -4371   1439   1132       C\\nATOM   2316  C   ASN A1132      20.208 -20.804  40.407  1.00 98.88           C\\nANISOU 2316  C   ASN A1132    15239  10564  11768  -3840   1452   1311       C\\nATOM   2317  O   ASN A1132      20.866 -21.282  41.338  1.00106.13           O\\nANISOU 2317  O   ASN A1132    16469  11262  12593  -3844   1482   1689       O\\nATOM   2318  CB  ASN A1132      19.417 -22.244  38.508  1.00100.70           C\\nANISOU 2318  CB  ASN A1132    15748  10141  12372  -4206   1226    906       C\\nATOM   2319  CG  ASN A1132      20.355 -23.432  38.702  1.00102.63           C\\nANISOU 2319  CG  ASN A1132    16592   9660  12743  -4136   1159   1173       C\\nATOM   2320  OD1 ASN A1132      21.259 -23.402  39.538  1.00 99.29           O\\nANISOU 2320  OD1 ASN A1132    16345   9141  12242  -3883   1185   1501       O\\nATOM   2321  ND2 ASN A1132      20.136 -24.489  37.929  1.00107.31           N\\nANISOU 2321  ND2 ASN A1132    17502   9719  13554  -4348   1034   1014       N\\nATOM   2322  N   LEU A1133      20.483 -19.606  39.881  1.00 85.10           N\\nANISOU 2322  N   LEU A1133    13195   9149   9988  -3405   1394   1062       N\\nATOM   2323  CA  LEU A1133      21.652 -18.849  40.317  1.00 79.83           C\\nANISOU 2323  CA  LEU A1133    12558   8566   9209  -2920   1377   1196       C\\nATOM   2324  C   LEU A1133      21.591 -18.470  41.792  1.00 85.06           C\\nANISOU 2324  C   LEU A1133    13112   9576   9629  -3048   1529   1445       C\\nATOM   2325  O   LEU A1133      22.638 -18.221  42.399  1.00 82.43           O\\nANISOU 2325  O   LEU A1133    12927   9198   9193  -2748   1484   1656       O\\nATOM   2326  CB  LEU A1133      21.813 -17.596  39.454  1.00 84.72           C\\nANISOU 2326  CB  LEU A1133    12879   9469   9842  -2527   1283    893       C\\nATOM   2327  CG  LEU A1133      22.459 -17.798  38.079  1.00 88.21           C\\nANISOU 2327  CG  LEU A1133    13529   9583  10405  -2245   1143    716       C\\nATOM   2328  CD1 LEU A1133      22.334 -16.537  37.242  1.00 90.94           C\\nANISOU 2328  CD1 LEU A1133    13587  10258  10710  -1997   1039    463       C\\nATOM   2329  CD2 LEU A1133      23.920 -18.203  38.219  1.00 83.43           C\\nANISOU 2329  CD2 LEU A1133    13242   8615   9844  -1895   1135    911       C\\nATOM   2330  N   ALA A1134      20.399 -18.433  42.386  1.00 84.49           N\\nANISOU 2330  N   ALA A1134    12774   9880   9449  -3501   1713   1404       N\\nATOM   2331  CA  ALA A1134      20.263 -18.129  43.804  1.00 83.30           C\\nANISOU 2331  CA  ALA A1134    12544  10115   8992  -3684   1912   1604       C\\nATOM   2332  C   ALA A1134      20.570 -19.322  44.697  1.00 95.28           C\\nANISOU 2332  C   ALA A1134    14547  11297  10359  -4027   1952   2087       C\\nATOM   2333  O   ALA A1134      20.536 -19.181  45.925  1.00100.46           O\\nANISOU 2333  O   ALA A1134    15234  12260  10675  -4222   2106   2315       O\\nATOM   2334  CB  ALA A1134      18.855 -17.614  44.103  1.00 88.70           C\\nANISOU 2334  CB  ALA A1134    12701  11389   9612  -4038   2147   1331       C\\nATOM   2335  N   LYS A1135      20.860 -20.486  44.116  1.00 88.10           N\\nANISOU 2335  N   LYS A1135    14044   9751   9678  -4109   1800   2243       N\\nATOM   2336  CA  LYS A1135      21.205 -21.680  44.871  1.00 87.20           C\\nANISOU 2336  CA  LYS A1135    14461   9179   9491  -4398   1755   2737       C\\nATOM   2337  C   LYS A1135      22.701 -21.967  44.852  1.00 86.32           C\\nANISOU 2337  C   LYS A1135    14744   8566   9488  -3866   1479   2966       C\\nATOM   2338  O   LYS A1135      23.109 -23.103  45.109  1.00102.38           O\\nANISOU 2338  O   LYS A1135    17270  10011  11619  -3979   1327   3328       O\\nATOM   2339  CB  LYS A1135      20.432 -22.884  44.332  1.00 91.82           C\\nANISOU 2339  CB  LYS A1135    15253   9320  10313  -4902   1752   2756       C\\nATOM   2340  N   SER A1136      23.523 -20.968  44.553  1.00 82.36           N\\nANISOU 2340  N   SER A1136    14022   8267   9005  -3296   1395   2765       N\\nATOM   2341  CA  SER A1136      24.959 -21.160  44.431  1.00 83.52           C\\nANISOU 2341  CA  SER A1136    14419   8004   9312  -2765   1149   2911       C\\nATOM   2342  C   SER A1136      25.684 -20.619  45.656  1.00 88.67           C\\nANISOU 2342  C   SER A1136    15092   8930   9667  -2607   1075   3205       C\\nATOM   2343  O   SER A1136      25.148 -19.816  46.424  1.00 92.03           O\\nANISOU 2343  O   SER A1136    15281   9935   9752  -2806   1240   3175       O\\nATOM   2344  CB  SER A1136      25.494 -20.477  43.171  1.00 79.24           C\\nANISOU 2344  CB  SER A1136    13626   7476   9007  -2270   1101   2495       C\\nATOM   2345  OG  SER A1136      25.423 -19.068  43.285  1.00 73.97           O\\nANISOU 2345  OG  SER A1136    12540   7401   8165  -2108   1183   2288       O\\nATOM   2346  N   ARG A1137      26.926 -21.078  45.832  1.00 91.39           N\\nANISOU 2346  N   ARG A1137    15712   8855  10158  -2229    806   3459       N\\nATOM   2347  CA  ARG A1137      27.767 -20.540  46.894  1.00 91.41           C\\nANISOU 2347  CA  ARG A1137    15721   9100   9909  -2019    652   3712       C\\nATOM   2348  C   ARG A1137      28.177 -19.101  46.613  1.00 85.85           C\\nANISOU 2348  C   ARG A1137    14558   8882   9179  -1656    695   3357       C\\nATOM   2349  O   ARG A1137      28.655 -18.413  47.521  1.00 85.58           O\\nANISOU 2349  O   ARG A1137    14453   9182   8883  -1561    604   3470       O\\nATOM   2350  CB  ARG A1137      29.009 -21.414  47.089  1.00 94.63           C\\nANISOU 2350  CB  ARG A1137    16484   8915  10557  -1666    293   4057       C\\nATOM   2351  N   TRP A1138      28.013 -18.639  45.372  1.00 85.61           N\\nANISOU 2351  N   TRP A1138    14253   8876   9400  -1476    803   2943       N\\nATOM   2352  CA  TRP A1138      28.240 -17.235  45.053  1.00 83.05           C\\nANISOU 2352  CA  TRP A1138    13523   8984   9049  -1214    846   2628       C\\nATOM   2353  C   TRP A1138      27.118 -16.360  45.596  1.00 83.65           C\\nANISOU 2353  C   TRP A1138    13343   9618   8821  -1522   1044   2460       C\\nATOM   2354  O   TRP A1138      27.378 -15.303  46.181  1.00 74.31           O\\nANISOU 2354  O   TRP A1138    11960   8813   7461  -1395   1022   2377       O\\nATOM   2355  CB  TRP A1138      28.387 -17.069  43.541  1.00 81.72           C\\nANISOU 2355  CB  TRP A1138    13205   8653   9191   -970    885   2291       C\\nATOM   2356  CG  TRP A1138      28.200 -15.675  43.038  1.00 80.37           C\\nANISOU 2356  CG  TRP A1138    12659   8893   8984   -845    952   1971       C\\nATOM   2357  CD1 TRP A1138      29.008 -14.601  43.270  1.00 79.75           C\\nANISOU 2357  CD1 TRP A1138    12375   9046   8880   -571    866   1931       C\\nATOM   2358  CD2 TRP A1138      27.151 -15.209  42.179  1.00 79.40           C\\nANISOU 2358  CD2 TRP A1138    12339   8950   8882   -990   1065   1659       C\\nATOM   2359  NE1 TRP A1138      28.520 -13.492  42.620  1.00 74.10           N\\nANISOU 2359  NE1 TRP A1138    11385   8600   8171   -543    925   1634       N\\nATOM   2360  CE2 TRP A1138      27.381 -13.840  41.944  1.00 77.74           C\\nANISOU 2360  CE2 TRP A1138    11841   9040   8657   -775   1031   1470       C\\nATOM   2361  CE3 TRP A1138      26.036 -15.814  41.592  1.00 70.14           C\\nANISOU 2361  CE3 TRP A1138    11201   7697   7754  -1292   1152   1527       C\\nATOM   2362  CZ2 TRP A1138      26.539 -13.069  41.149  1.00 75.61           C\\nANISOU 2362  CZ2 TRP A1138    11345   8968   8416   -815   1054   1185       C\\nATOM   2363  CZ3 TRP A1138      25.201 -15.044  40.801  1.00 72.99           C\\nANISOU 2363  CZ3 TRP A1138    11290   8307   8136  -1332   1174   1217       C\\nATOM   2364  CH2 TRP A1138      25.457 -13.689  40.588  1.00 72.54           C\\nANISOU 2364  CH2 TRP A1138    10974   8524   8064  -1078   1113   1063       C\\nATOM   2365  N   TYR A1139      25.867 -16.790  45.424  1.00 82.65           N\\nANISOU 2365  N   TYR A1139    13198   9549   8658  -1927   1233   2375       N\\nATOM   2366  CA  TYR A1139      24.743 -16.053  45.987  1.00 86.12           C\\nANISOU 2366  CA  TYR A1139    13337  10541   8845  -2219   1452   2182       C\\nATOM   2367  C   TYR A1139      24.771 -16.040  47.509  1.00 83.42           C\\nANISOU 2367  C   TYR A1139    13129  10492   8073  -2444   1516   2445       C\\nATOM   2368  O   TYR A1139      24.214 -15.122  48.120  1.00 85.20           O\\nANISOU 2368  O   TYR A1139    13075  11244   8055  -2528   1680   2223       O\\nATOM   2369  CB  TYR A1139      23.424 -16.647  45.483  1.00 93.06           C\\nANISOU 2369  CB  TYR A1139    14126  11418   9815  -2639   1632   2048       C\\nATOM   2370  CG  TYR A1139      22.187 -15.947  45.998  1.00 97.27           C\\nANISOU 2370  CG  TYR A1139    14256  12545  10156  -2931   1887   1793       C\\nATOM   2371  CD1 TYR A1139      21.714 -14.791  45.393  1.00 97.09           C\\nANISOU 2371  CD1 TYR A1139    13784  12829  10275  -2703   1891   1360       C\\nATOM   2372  CD2 TYR A1139      21.487 -16.449  47.086  1.00101.31           C\\nANISOU 2372  CD2 TYR A1139    14831  13310  10352  -3435   2125   1984       C\\nATOM   2373  CE1 TYR A1139      20.582 -14.152  45.862  1.00 98.45           C\\nANISOU 2373  CE1 TYR A1139    13534  13534  10340  -2906   2113   1072       C\\nATOM   2374  CE2 TYR A1139      20.357 -15.817  47.560  1.00102.23           C\\nANISOU 2374  CE2 TYR A1139    14515  14020  10307  -3689   2412   1691       C\\nATOM   2375  CZ  TYR A1139      19.909 -14.671  46.946  1.00 98.03           C\\nANISOU 2375  CZ  TYR A1139    13492  13774   9981  -3392   2400   1210       C\\nATOM   2376  OH  TYR A1139      18.781 -14.044  47.424  1.00 96.25           O\\nANISOU 2376  OH  TYR A1139    12784  14130   9656  -3586   2677    868       O\\nATOM   2377  N   ASN A1140      25.410 -17.028  48.134  1.00 84.98           N\\nANISOU 2377  N   ASN A1140    13766  10358   8165  -2531   1372   2902       N\\nATOM   2378  CA  ASN A1140      25.511 -17.069  49.585  1.00 81.09           C\\nANISOU 2378  CA  ASN A1140    13485  10139   7189  -2767   1384   3212       C\\nATOM   2379  C   ASN A1140      26.720 -16.316  50.123  1.00 81.14           C\\nANISOU 2379  C   ASN A1140    13495  10255   7081  -2354   1121   3259       C\\nATOM   2380  O   ASN A1140      26.732 -15.963  51.308  1.00 91.34           O\\nANISOU 2380  O   ASN A1140    14868  11933   7905  -2514   1139   3371       O\\nATOM   2381  CB  ASN A1140      25.564 -18.521  50.073  1.00 83.93           C\\nANISOU 2381  CB  ASN A1140    14351  10066   7474  -3090   1289   3738       C\\nATOM   2382  CG  ASN A1140      24.263 -19.268  49.834  1.00 88.69           C\\nANISOU 2382  CG  ASN A1140    14898  10646   8154  -3583   1553   3682       C\\nATOM   2383  OD1 ASN A1140      23.328 -19.182  50.631  1.00 94.13           O\\nANISOU 2383  OD1 ASN A1140    15427  11795   8542  -3964   1814   3633       O\\nATOM   2384  ND2 ASN A1140      24.203 -20.015  48.739  1.00 88.26           N\\nANISOU 2384  ND2 ASN A1140    14971  10056   8508  -3583   1485   3663       N\\nATOM   2385  N   GLN A1141      27.731 -16.058  49.292  1.00 79.05           N\\nANISOU 2385  N   GLN A1141    13135   9692   7209  -1861    889   3159       N\\nATOM   2386  CA  GLN A1141      28.944 -15.389  49.751  1.00 83.34           C\\nANISOU 2386  CA  GLN A1141    13640  10316   7710  -1493    612   3207       C\\nATOM   2387  C   GLN A1141      28.857 -13.872  49.622  1.00 86.83           C\\nANISOU 2387  C   GLN A1141    13669  11193   8130  -1321    691   2761       C\\nATOM   2388  O   GLN A1141      29.270 -13.148  50.534  1.00 90.33           O\\nANISOU 2388  O   GLN A1141    14085  11948   8290  -1274    578   2742       O\\nATOM   2389  CB  GLN A1141      30.158 -15.908  48.974  1.00 81.76           C\\nANISOU 2389  CB  GLN A1141    13505   9595   7966  -1066    339   3330       C\\nATOM   2390  N   THR A1142      28.341 -13.378  48.497  1.00 81.15           N\\nANISOU 2390  N   THR A1142    12660  10468   7708  -1228    841   2404       N\\nATOM   2391  CA  THR A1142      28.099 -11.952  48.276  1.00 75.62           C\\nANISOU 2391  CA  THR A1142    11594  10099   7040  -1081    896   1987       C\\nATOM   2392  C   THR A1142      26.654 -11.815  47.825  1.00 80.15           C\\nANISOU 2392  C   THR A1142    11953  10861   7638  -1313   1170   1698       C\\nATOM   2393  O   THR A1142      26.373 -11.645  46.629  1.00 76.21           O\\nANISOU 2393  O   THR A1142    11292  10208   7456  -1195   1180   1504       O\\nATOM   2394  CB  THR A1142      29.064 -11.368  47.245  1.00 71.01           C\\nANISOU 2394  CB  THR A1142    10854   9291   6836   -689    721   1873       C\\nATOM   2395  OG1 THR A1142      28.852 -12.004  45.979  1.00 61.90           O\\nANISOU 2395  OG1 THR A1142     9720   7819   5981   -656    792   1847       O\\nATOM   2396  CG2 THR A1142      30.507 -11.581  47.678  1.00 64.20           C\\nANISOU 2396  CG2 THR A1142    10120   8261   6011   -463    447   2144       C\\nATOM   2397  N   PRO A1143      25.702 -11.890  48.760  1.00 78.66           N\\nANISOU 2397  N   PRO A1143    11743  11039   7106  -1659   1396   1658       N\\nATOM   2398  CA  PRO A1143      24.288 -11.947  48.355  1.00 77.44           C\\nANISOU 2398  CA  PRO A1143    11332  11073   7019  -1917   1663   1400       C\\nATOM   2399  C   PRO A1143      23.754 -10.645  47.786  1.00 81.38           C\\nANISOU 2399  C   PRO A1143    11396  11793   7731  -1681   1672    913       C\\nATOM   2400  O   PRO A1143      22.964 -10.679  46.836  1.00 67.23           O\\nANISOU 2400  O   PRO A1143     9390   9947   6208  -1709   1715    723       O\\nATOM   2401  CB  PRO A1143      23.575 -12.337  49.655  1.00 74.02           C\\nANISOU 2401  CB  PRO A1143    10976  11033   6115  -2363   1931   1502       C\\nATOM   2402  CG  PRO A1143      24.484 -11.856  50.733  1.00 74.95           C\\nANISOU 2402  CG  PRO A1143    11275  11318   5883  -2235   1792   1614       C\\nATOM   2403  CD  PRO A1143      25.873 -12.037  50.213  1.00 80.85           C\\nANISOU 2403  CD  PRO A1143    12236  11590   6893  -1870   1423   1866       C\\nATOM   2404  N   ASN A1144      24.148  -9.498  48.346  1.00 79.84           N\\nANISOU 2404  N   ASN A1144    11080  11820   7435  -1453   1593    702       N\\nATOM   2405  CA  ASN A1144      23.656  -8.219  47.839  1.00 82.18           C\\nANISOU 2405  CA  ASN A1144    11000  12248   7977  -1203   1550    249       C\\nATOM   2406  C   ASN A1144      24.024  -8.031  46.372  1.00 83.32           C\\nANISOU 2406  C   ASN A1144    11122  12002   8536   -947   1323    262       C\\nATOM   2407  O   ASN A1144      23.168  -7.712  45.538  1.00 77.89           O\\nANISOU 2407  O   ASN A1144    10184  11322   8089   -907   1317     25       O\\nATOM   2408  CB  ASN A1144      24.209  -7.072  48.683  1.00 86.17           C\\nANISOU 2408  CB  ASN A1144    11466  12947   8328   -999   1448     44       C\\nATOM   2409  CG  ASN A1144      23.399  -6.831  49.942  1.00 91.58           C\\nANISOU 2409  CG  ASN A1144    12020  14149   8626  -1210   1730   -220       C\\nATOM   2410  OD1 ASN A1144      22.445  -6.054  49.938  1.00 89.43           O\\nANISOU 2410  OD1 ASN A1144    11378  14135   8467  -1137   1861   -680       O\\nATOM   2411  ND2 ASN A1144      23.778  -7.496  51.028  1.00 95.06           N\\nANISOU 2411  ND2 ASN A1144    12763  14756   8600  -1466   1818     62       N\\nATOM   2412  N   ARG A1145      25.302  -8.228  46.040  1.00 83.54           N\\nANISOU 2412  N   ARG A1145    11397  11711   8633   -780   1132    536       N\\nATOM   2413  CA  ARG A1145      25.740  -8.103  44.655  1.00 77.75           C\\nANISOU 2413  CA  ARG A1145    10673  10652   8215   -579    973    561       C\\nATOM   2414  C   ARG A1145      25.101  -9.167  43.774  1.00 76.82           C\\nANISOU 2414  C   ARG A1145    10624  10365   8200   -753   1062    630       C\\nATOM   2415  O   ARG A1145      24.721  -8.887  42.631  1.00 82.58           O\\nANISOU 2415  O   ARG A1145    11252  10993   9130   -675    981    488       O\\nATOM   2416  CB  ARG A1145      27.264  -8.189  44.587  1.00 73.67           C\\nANISOU 2416  CB  ARG A1145    10353   9896   7744   -393    814    816       C\\nATOM   2417  CG  ARG A1145      27.829  -8.227  43.179  1.00 69.75           C\\nANISOU 2417  CG  ARG A1145     9893   9104   7505   -234    729    865       C\\nATOM   2418  CD  ARG A1145      29.352  -8.232  43.189  1.00 73.59           C\\nANISOU 2418  CD  ARG A1145    10468   9428   8064    -50    612   1067       C\\nATOM   2419  NE  ARG A1145      29.897  -8.135  41.837  1.00 80.75           N\\nANISOU 2419  NE  ARG A1145    11375  10131   9175     79    594   1070       N\\nATOM   2420  CZ  ARG A1145      31.175  -7.901  41.556  1.00 82.83           C\\nANISOU 2420  CZ  ARG A1145    11612  10298   9561    237    528   1175       C\\nATOM   2421  NH1 ARG A1145      32.054  -7.734  42.535  1.00 82.57           N\\nANISOU 2421  NH1 ARG A1145    11535  10328   9508    307    415   1287       N\\nATOM   2422  NH2 ARG A1145      31.574  -7.829  40.293  1.00 85.74           N\\nANISOU 2422  NH2 ARG A1145    11982  10541  10053    302    578   1158       N\\nATOM   2423  N   ALA A1146      24.974 -10.393  44.287  1.00 78.38           N\\nANISOU 2423  N   ALA A1146    11025  10507   8249  -1011   1196    857       N\\nATOM   2424  CA  ALA A1146      24.412 -11.480  43.491  1.00 77.28           C\\nANISOU 2424  CA  ALA A1146    10992  10148   8224  -1212   1259    913       C\\nATOM   2425  C   ALA A1146      22.965 -11.191  43.114  1.00 83.69           C\\nANISOU 2425  C   ALA A1146    11482  11202   9113  -1389   1341    610       C\\nATOM   2426  O   ALA A1146      22.575 -11.340  41.951  1.00 81.20           O\\nANISOU 2426  O   ALA A1146    11127  10738   8988  -1380   1252    495       O\\nATOM   2427  CB  ALA A1146      24.519 -12.800  44.253  1.00 75.31           C\\nANISOU 2427  CB  ALA A1146    11049   9751   7813  -1491   1359   1239       C\\nATOM   2428  N   LYS A1147      22.154 -10.771  44.090  1.00 81.29           N\\nANISOU 2428  N   LYS A1147    10927  11303   8657  -1547   1506    451       N\\nATOM   2429  CA  LYS A1147      20.760 -10.442  43.804  1.00 80.52           C\\nANISOU 2429  CA  LYS A1147    10420  11486   8686  -1680   1585    116       C\\nATOM   2430  C   LYS A1147      20.649  -9.302  42.799  1.00 83.83           C\\nANISOU 2430  C   LYS A1147    10611  11866   9377  -1325   1329   -152       C\\nATOM   2431  O   LYS A1147      19.710  -9.273  41.995  1.00 68.30           O\\nANISOU 2431  O   LYS A1147     8403   9940   7609  -1375   1246   -350       O\\nATOM   2432  CB  LYS A1147      20.023 -10.088  45.098  1.00 67.35           C\\nANISOU 2432  CB  LYS A1147     8483  10311   6797  -1863   1853    -63       C\\nATOM   2433  N   ARG A1148      21.599  -8.365  42.815  1.00 85.54           N\\nANISOU 2433  N   ARG A1148    10910  11984   9606   -988   1167   -140       N\\nATOM   2434  CA  ARG A1148      21.574  -7.277  41.842  1.00 79.68           C\\nANISOU 2434  CA  ARG A1148    10031  11139   9107   -685    892   -317       C\\nATOM   2435  C   ARG A1148      21.891  -7.783  40.437  1.00 82.33           C\\nANISOU 2435  C   ARG A1148    10589  11152   9539   -673    733   -165       C\\nATOM   2436  O   ARG A1148      21.289  -7.330  39.457  1.00 90.33           O\\nANISOU 2436  O   ARG A1148    11469  12136  10717   -591    526   -312       O\\nATOM   2437  CB  ARG A1148      22.555  -6.182  42.261  1.00 70.66           C\\nANISOU 2437  CB  ARG A1148     8952   9944   7952   -403    768   -316       C\\nATOM   2438  CG  ARG A1148      21.892  -4.860  42.620  1.00 71.12           C\\nANISOU 2438  CG  ARG A1148     8676  10192   8155   -198    669   -688       C\\nATOM   2439  CD  ARG A1148      22.475  -4.260  43.892  1.00 73.19           C\\nANISOU 2439  CD  ARG A1148     8962  10601   8247   -122    743   -769       C\\nATOM   2440  NE  ARG A1148      23.934  -4.303  43.899  1.00 73.07           N\\nANISOU 2440  NE  ARG A1148     9271  10346   8145    -63    641   -461       N\\nATOM   2441  CZ  ARG A1148      24.686  -4.003  44.953  1.00 72.04           C\\nANISOU 2441  CZ  ARG A1148     9236  10306   7829    -40    656   -444       C\\nATOM   2442  NH1 ARG A1148      24.121  -3.632  46.093  1.00 77.77           N\\nANISOU 2442  NH1 ARG A1148     9809  11363   8378    -79    795   -729       N\\nATOM   2443  NH2 ARG A1148      26.005  -4.075  44.867  1.00 70.75           N\\nANISOU 2443  NH2 ARG A1148     9301   9933   7647     15    532   -167       N\\nATOM   2444  N   VAL A1149      22.824  -8.727  40.321  1.00 86.59           N\\nANISOU 2444  N   VAL A1149    11473  11454   9974   -742    812    112       N\\nATOM   2445  CA  VAL A1149      23.201  -9.252  39.011  1.00 82.53           C\\nANISOU 2445  CA  VAL A1149    11189  10655   9513   -723    713    200       C\\nATOM   2446  C   VAL A1149      22.160 -10.240  38.500  1.00 89.46           C\\nANISOU 2446  C   VAL A1149    12052  11515  10424  -1007    747    112       C\\nATOM   2447  O   VAL A1149      21.841 -10.260  37.304  1.00 88.71           O\\nANISOU 2447  O   VAL A1149    11995  11326  10387  -1003    583     17       O\\nATOM   2448  CB  VAL A1149      24.603  -9.881  39.089  1.00 69.15           C\\nANISOU 2448  CB  VAL A1149     9812   8710   7751   -638    790    459       C\\nATOM   2449  CG1 VAL A1149      24.961 -10.583  37.793  1.00 62.41           C\\nANISOU 2449  CG1 VAL A1149     9197   7590   6927   -632    765    483       C\\nATOM   2450  CG2 VAL A1149      25.636  -8.812  39.423  1.00 65.57           C\\nANISOU 2450  CG2 VAL A1149     9323   8286   7303   -385    710    522       C\\nATOM   2451  N   ILE A1150      21.606 -11.063  39.394  1.00 84.73           N\\nANISOU 2451  N   ILE A1150    11413  11014   9767  -1295    945    151       N\\nATOM   2452  CA  ILE A1150      20.566 -12.008  38.997  1.00 83.24           C\\nANISOU 2452  CA  ILE A1150    11179  10809   9639  -1639    980     64       C\\nATOM   2453  C   ILE A1150      19.315 -11.263  38.545  1.00 84.16           C\\nANISOU 2453  C   ILE A1150    10861  11211   9905  -1651    831   -246       C\\nATOM   2454  O   ILE A1150      18.622 -11.692  37.612  1.00 93.69           O\\nANISOU 2454  O   ILE A1150    12028  12360  11209  -1807    688   -369       O\\nATOM   2455  CB  ILE A1150      20.272 -12.986  40.152  1.00 84.83           C\\nANISOU 2455  CB  ILE A1150    11442  11060   9730  -2003   1240    225       C\\nATOM   2456  CG1 ILE A1150      21.486 -13.878  40.414  1.00 82.12           C\\nANISOU 2456  CG1 ILE A1150    11568  10333   9299  -1964   1285    553       C\\nATOM   2457  CG2 ILE A1150      19.059 -13.839  39.844  1.00 86.81           C\\nANISOU 2457  CG2 ILE A1150    11564  11344  10076  -2432   1287    113       C\\nATOM   2458  CD1 ILE A1150      21.367 -14.717  41.663  1.00 70.60           C\\nANISOU 2458  CD1 ILE A1150    10253   8891   7682  -2294   1484    806       C\\nATOM   2459  N   THR A1151      19.009 -10.131  39.188  1.00 79.62           N\\nANISOU 2459  N   THR A1151     9946  10934   9371  -1467    829   -404       N\\nATOM   2460  CA  THR A1151      17.920  -9.283  38.713  1.00 85.27           C\\nANISOU 2460  CA  THR A1151    10223  11875  10301  -1363    618   -716       C\\nATOM   2461  C   THR A1151      18.194  -8.785  37.302  1.00 88.73           C\\nANISOU 2461  C   THR A1151    10820  12078  10815  -1128    245   -709       C\\nATOM   2462  O   THR A1151      17.290  -8.744  36.460  1.00 89.80           O\\nANISOU 2462  O   THR A1151    10761  12268  11090  -1177     -2   -876       O\\nATOM   2463  CB  THR A1151      17.713  -8.098  39.655  1.00 85.11           C\\nANISOU 2463  CB  THR A1151     9861  12141  10338  -1127    668   -919       C\\nATOM   2464  OG1 THR A1151      17.364  -8.577  40.957  1.00 90.34           O\\nANISOU 2464  OG1 THR A1151    10377  13098  10849  -1398   1046   -947       O\\nATOM   2465  CG2 THR A1151      16.602  -7.194  39.144  1.00 80.06           C\\nANISOU 2465  CG2 THR A1151     8743  11680   9998   -942    398  -1262       C\\nATOM   2466  N   THR A1152      19.440  -8.402  37.023  1.00 89.05           N\\nANISOU 2466  N   THR A1152    11208  11880  10745   -898    191   -508       N\\nATOM   2467  CA  THR A1152      19.772  -7.948  35.679  1.00 88.03           C\\nANISOU 2467  CA  THR A1152    11283  11556  10607   -736   -114   -459       C\\nATOM   2468  C   THR A1152      19.666  -9.080  34.665  1.00 84.57           C\\nANISOU 2468  C   THR A1152    11105  10963  10066   -967   -143   -432       C\\nATOM   2469  O   THR A1152      19.276  -8.846  33.516  1.00 88.93           O\\nANISOU 2469  O   THR A1152    11704  11483  10603   -948   -442   -501       O\\nATOM   2470  CB  THR A1152      21.170  -7.335  35.670  1.00 84.93           C\\nANISOU 2470  CB  THR A1152    11169  10986  10115   -508    -96   -248       C\\nATOM   2471  OG1 THR A1152      21.238  -6.314  36.674  1.00 87.26           O\\nANISOU 2471  OG1 THR A1152    11240  11404  10511   -322    -88   -315       O\\nATOM   2472  CG2 THR A1152      21.473  -6.721  34.321  1.00 75.79           C\\nANISOU 2472  CG2 THR A1152    10215   9677   8903   -385   -386   -175       C\\nATOM   2473  N   PHE A1153      19.988 -10.311  35.069  1.00 80.31           N\\nANISOU 2473  N   PHE A1153    10763  10305   9447  -1189    130   -341       N\\nATOM   2474  CA  PHE A1153      19.838 -11.445  34.163  1.00 86.85           C\\nANISOU 2474  CA  PHE A1153    11850  10938  10209  -1417    102   -378       C\\nATOM   2475  C   PHE A1153      18.375 -11.753  33.876  1.00 94.28           C\\nANISOU 2475  C   PHE A1153    12493  12048  11280  -1692    -61   -605       C\\nATOM   2476  O   PHE A1153      18.051 -12.271  32.802  1.00 97.03           O\\nANISOU 2476  O   PHE A1153    13001  12289  11578  -1834   -250   -712       O\\nATOM   2477  CB  PHE A1153      20.524 -12.681  34.744  1.00 85.98           C\\nANISOU 2477  CB  PHE A1153    12033  10584  10052  -1564    394   -224       C\\nATOM   2478  CG  PHE A1153      21.973 -12.790  34.388  1.00 82.81           C\\nANISOU 2478  CG  PHE A1153    11993   9932   9541  -1323    479    -73       C\\nATOM   2479  CD1 PHE A1153      22.400 -12.549  33.096  1.00 87.89           C\\nANISOU 2479  CD1 PHE A1153    12840  10494  10062  -1196    348   -140       C\\nATOM   2480  CD2 PHE A1153      22.908 -13.132  35.345  1.00 77.41           C\\nANISOU 2480  CD2 PHE A1153    11425   9126   8862  -1234    685    132       C\\nATOM   2481  CE1 PHE A1153      23.735 -12.650  32.764  1.00 85.44           C\\nANISOU 2481  CE1 PHE A1153    12792  10012   9660   -991    485    -39       C\\nATOM   2482  CE2 PHE A1153      24.244 -13.233  35.021  1.00 77.07           C\\nANISOU 2482  CE2 PHE A1153    11625   8883   8776   -993    759    238       C\\nATOM   2483  CZ  PHE A1153      24.658 -12.992  33.729  1.00 80.39           C\\nANISOU 2483  CZ  PHE A1153    12194   9251   9099   -874    690    135       C\\nATOM   2484  N   ARG A1154      17.484 -11.446  34.817  1.00 88.53           N\\nANISOU 2484  N   ARG A1154    11311  11612  10713  -1783     15   -710       N\\nATOM   2485  CA  ARG A1154      16.070 -11.771  34.679  1.00 90.56           C\\nANISOU 2485  CA  ARG A1154    11175  12087  11146  -2076    -96   -944       C\\nATOM   2486  C   ARG A1154      15.287 -10.657  33.990  1.00 94.08           C\\nANISOU 2486  C   ARG A1154    11255  12736  11753  -1845   -507  -1151       C\\nATOM   2487  O   ARG A1154      14.589 -10.908  33.004  1.00 98.43           O\\nANISOU 2487  O   ARG A1154    11752  13292  12353  -1977   -823  -1290       O\\nATOM   2488  CB  ARG A1154      15.471 -12.072  36.056  1.00 91.66           C\\nANISOU 2488  CB  ARG A1154    10967  12492  11368  -2333    250   -973       C\\nATOM   2489  CG  ARG A1154      13.953 -12.110  36.087  1.00 98.75           C\\nANISOU 2489  CG  ARG A1154    11273  13741  12505  -2600    179  -1261       C\\nATOM   2490  CD  ARG A1154      13.450 -12.527  37.460  1.00 98.15           C\\nANISOU 2490  CD  ARG A1154    10903  13957  12432  -2937    616  -1264       C\\nATOM   2491  NE  ARG A1154      14.141 -11.809  38.526  1.00 96.23           N\\nANISOU 2491  NE  ARG A1154    10691  13830  12042  -2666    855  -1169       N\\nATOM   2492  CZ  ARG A1154      13.729 -10.656  39.043  1.00 99.35           C\\nANISOU 2492  CZ  ARG A1154    10627  14571  12550  -2384    862  -1413       C\\nATOM   2493  NH1 ARG A1154      12.618 -10.085  38.594  1.00102.81           N\\nANISOU 2493  NH1 ARG A1154    10503  15271  13290  -2299    634  -1752       N\\nATOM   2494  NH2 ARG A1154      14.426 -10.074  40.011  1.00 97.58           N\\nANISOU 2494  NH2 ARG A1154    10500  14418  12157  -2171   1067  -1343       N\\nATOM   2495  N   THR A1155      15.394  -9.425  34.492  1.00 91.70           N\\nANISOU 2495  N   THR A1155    10720  12575  11545  -1493   -553  -1180       N\\nATOM   2496  CA  THR A1155      14.626  -8.327  33.913  1.00 95.66           C\\nANISOU 2496  CA  THR A1155    10869  13211  12265  -1227   -991  -1368       C\\nATOM   2497  C   THR A1155      15.189  -7.887  32.570  1.00 97.84           C\\nANISOU 2497  C   THR A1155    11567  13229  12380  -1038  -1391  -1215       C\\nATOM   2498  O   THR A1155      14.426  -7.500  31.678  1.00103.63           O\\nANISOU 2498  O   THR A1155    12148  14011  13216   -975  -1852  -1325       O\\nATOM   2499  CB  THR A1155      14.590  -7.135  34.871  1.00 96.53           C\\nANISOU 2499  CB  THR A1155    10639  13482  12554   -890   -932  -1480       C\\nATOM   2500  OG1 THR A1155      15.865  -6.481  34.875  1.00 89.26           O\\nANISOU 2500  OG1 THR A1155    10139  12306  11469   -624   -926  -1243       O\\nATOM   2501  CG2 THR A1155      14.254  -7.597  36.282  1.00102.13           C\\nANISOU 2501  CG2 THR A1155    11038  14480  13285  -1108   -443  -1599       C\\nATOM   2502  N   GLY A1156      16.506  -7.938  32.402  1.00 98.59           N\\nANISOU 2502  N   GLY A1156    12176  13074  12209   -961  -1232   -958       N\\nATOM   2503  CA  GLY A1156      17.109  -7.426  31.192  1.00 97.17           C\\nANISOU 2503  CA  GLY A1156    12393  12702  11824   -813  -1538   -796       C\\nATOM   2504  C   GLY A1156      17.208  -5.922  31.139  1.00 94.99           C\\nANISOU 2504  C   GLY A1156    12028  12391  11674   -459  -1843   -727       C\\nATOM   2505  O   GLY A1156      17.414  -5.364  30.057  1.00 94.83           O\\nANISOU 2505  O   GLY A1156    12287  12241  11502   -370  -2199   -582       O\\nATOM   2506  N   THR A1157      17.055  -5.243  32.275  1.00 98.59           N\\nANISOU 2506  N   THR A1157    12130  12944  12386   -269  -1724   -831       N\\nATOM   2507  CA  THR A1157      17.188  -3.793  32.334  1.00 99.99           C\\nANISOU 2507  CA  THR A1157    12241  13012  12740     83  -2014   -798       C\\nATOM   2508  C   THR A1157      18.117  -3.396  33.475  1.00 95.58           C\\nANISOU 2508  C   THR A1157    11722  12408  12187    197  -1666   -741       C\\nATOM   2509  O   THR A1157      18.739  -4.258  34.103  1.00 99.83           O\\nANISOU 2509  O   THR A1157    12385  12993  12552     13  -1238   -673       O\\nATOM   2510  CB  THR A1157      15.819  -3.130  32.503  1.00100.53           C\\nANISOU 2510  CB  THR A1157    11744  13243  13210    283  -2359  -1106       C\\nATOM   2511  N   TRP A1158      18.225  -2.094  33.747  1.00 93.22           N\\nANISOU 2511  N   TRP A1158    11337  11987  12095    500  -1890   -770       N\\nATOM   2512  CA  TRP A1158      19.077  -1.577  34.810  1.00 93.29           C\\nANISOU 2512  CA  TRP A1158    11380  11944  12121    611  -1638   -757       C\\nATOM   2513  C   TRP A1158      18.284  -1.180  36.050  1.00100.83           C\\nANISOU 2513  C   TRP A1158    11839  13130  13343    767  -1520  -1143       C\\nATOM   2514  O   TRP A1158      18.687  -0.262  36.773  1.00104.41           O\\nANISOU 2514  O   TRP A1158    12262  13494  13913    976  -1523  -1234       O\\nATOM   2515  CB  TRP A1158      19.888  -0.380  34.315  1.00 93.24           C\\nANISOU 2515  CB  TRP A1158    11675  11603  12148    796  -1939   -534       C\\nATOM   2516  CG  TRP A1158      20.831  -0.689  33.202  1.00 90.86           C\\nANISOU 2516  CG  TRP A1158    11861  11134  11527    615  -1955   -159       C\\nATOM   2517  CD1 TRP A1158      20.661  -0.401  31.878  1.00 92.31           C\\nANISOU 2517  CD1 TRP A1158    12294  11175  11605    591  -2335     30       C\\nATOM   2518  CD2 TRP A1158      22.100  -1.341  33.312  1.00 84.64           C\\nANISOU 2518  CD2 TRP A1158    11359  10335  10467    435  -1569     52       C\\nATOM   2519  NE1 TRP A1158      21.746  -0.835  31.158  1.00 87.61           N\\nANISOU 2519  NE1 TRP A1158    12125  10516  10649    382  -2146    322       N\\nATOM   2520  CE2 TRP A1158      22.643  -1.417  32.015  1.00 81.33           C\\nANISOU 2520  CE2 TRP A1158    11324   9793   9787    307  -1675    322       C\\nATOM   2521  CE3 TRP A1158      22.829  -1.871  34.381  1.00 79.01           C\\nANISOU 2521  CE3 TRP A1158    10605   9715   9699    377  -1161     35       C\\nATOM   2522  CZ2 TRP A1158      23.881  -2.001  31.759  1.00 77.25           C\\nANISOU 2522  CZ2 TRP A1158    11088   9260   9004    149  -1343    521       C\\nATOM   2523  CZ3 TRP A1158      24.059  -2.452  34.124  1.00 69.87           C\\nANISOU 2523  CZ3 TRP A1158     9733   8502   8314    244   -903    268       C\\nATOM   2524  CH2 TRP A1158      24.572  -2.511  32.824  1.00 69.73           C\\nANISOU 2524  CH2 TRP A1158    10033   8375   8085    144   -972    482       C\\nATOM   2525  N   ASP A1159      17.156  -1.850  36.306  1.00 98.45           N\\nANISOU 2525  N   ASP A1159    11135  13138  13133    646  -1402  -1399       N\\nATOM   2526  CA  ASP A1159      16.331  -1.497  37.457  1.00 97.23           C\\nANISOU 2526  CA  ASP A1159    10456  13283  13205    769  -1227  -1814       C\\nATOM   2527  C   ASP A1159      17.098  -1.638  38.765  1.00 90.66           C\\nANISOU 2527  C   ASP A1159     9725  12569  12151    685   -774  -1819       C\\nATOM   2528  O   ASP A1159      16.820  -0.916  39.727  1.00 92.33           O\\nANISOU 2528  O   ASP A1159     9651  12933  12497    879   -679  -2146       O\\nATOM   2529  CB  ASP A1159      15.076  -2.368  37.498  1.00105.69           C\\nANISOU 2529  CB  ASP A1159    11073  14718  14366    540  -1095  -2046       C\\nATOM   2530  CG  ASP A1159      14.329  -2.379  36.182  1.00109.35           C\\nANISOU 2530  CG  ASP A1159    11447  15092  15007    573  -1581  -2031       C\\nATOM   2531  OD1 ASP A1159      14.839  -2.991  35.220  1.00106.95           O\\nANISOU 2531  OD1 ASP A1159    11588  14593  14457    378  -1693  -1714       O\\nATOM   2532  OD2 ASP A1159      13.231  -1.786  36.115  1.00113.68           O\\nANISOU 2532  OD2 ASP A1159    11472  15783  15940    804  -1860  -2361       O\\nATOM   2533  N   ALA A1160      18.061  -2.558  38.822  1.00 90.75           N\\nANISOU 2533  N   ALA A1160    10142  12514  11824    416   -516  -1483       N\\nATOM   2534  CA  ALA A1160      18.793  -2.777  40.062  1.00 83.07           C\\nANISOU 2534  CA  ALA A1160     9285  11661  10616    322   -147  -1445       C\\nATOM   2535  C   ALA A1160      19.805  -1.671  40.330  1.00 83.07           C\\nANISOU 2535  C   ALA A1160     9492  11427  10644    577   -301  -1398       C\\nATOM   2536  O   ALA A1160      20.159  -1.427  41.488  1.00 80.26           O\\nANISOU 2536  O   ALA A1160     9111  11213  10170    595    -98  -1520       O\\nATOM   2537  CB  ALA A1160      19.490  -4.133  40.023  1.00 69.19           C\\nANISOU 2537  CB  ALA A1160     7878   9858   8554     -5    110  -1098       C\\nATOM   2538  N   TYR A1161      20.270  -0.989  39.289  1.00 85.89           N\\nANISOU 2538  N   TYR A1161    10067  11436  11131    737   -663  -1221       N\\nATOM   2539  CA  TYR A1161      21.312   0.021  39.439  1.00 81.29           C\\nANISOU 2539  CA  TYR A1161     9712  10587  10590    902   -820  -1122       C\\nATOM   2540  C   TYR A1161      20.830   1.413  39.031  1.00 86.56           C\\nANISOU 2540  C   TYR A1161    10259  11009  11620   1221  -1257  -1309       C\\nATOM   2541  O   TYR A1161      19.780   1.882  39.473  1.00 90.75           O\\nANISOU 2541  O   TYR A1161    10405  11678  12398   1423  -1325  -1710       O\\nATOM   2542  CB  TYR A1161      22.541  -0.357  38.608  1.00 78.82           C\\nANISOU 2542  CB  TYR A1161     9822  10037  10089    757   -833   -681       C\\nATOM   2543  CG  TYR A1161      23.144  -1.708  38.932  1.00 79.07           C\\nANISOU 2543  CG  TYR A1161    10004  10209   9831    508   -467   -486       C\\nATOM   2544  CD1 TYR A1161      22.612  -2.876  38.400  1.00 78.87           C\\nANISOU 2544  CD1 TYR A1161     9993  10274   9701    320   -342   -427       C\\nATOM   2545  CD2 TYR A1161      24.263  -1.813  39.748  1.00 75.01           C\\nANISOU 2545  CD2 TYR A1161     9629   9697   9174    468   -297   -359       C\\nATOM   2546  CE1 TYR A1161      23.166  -4.110  38.683  1.00 74.50           C\\nANISOU 2546  CE1 TYR A1161     9613   9760   8934    118    -53   -248       C\\nATOM   2547  CE2 TYR A1161      24.824  -3.042  40.039  1.00 67.83           C\\nANISOU 2547  CE2 TYR A1161     8865   8860   8048    288    -30   -162       C\\nATOM   2548  CZ  TYR A1161      24.272  -4.189  39.504  1.00 71.43           C\\nANISOU 2548  CZ  TYR A1161     9359   9354   8428    123     94   -104       C\\nATOM   2549  OH  TYR A1161      24.829  -5.416  39.787  1.00 69.66           O\\nANISOU 2549  OH  TYR A1161     9313   9118   8037    -32    319     91       O\\nATOM   2550  N   SER A 364      17.508   3.047  36.367  1.00104.00           N\\nATOM   2551  CA  SER A 364      18.568   3.670  35.585  1.00104.92           C\\nATOM   2552  C   SER A 364      18.623   3.097  34.167  1.00111.72           C\\nATOM   2553  O   SER A 364      19.675   3.111  33.526  1.00111.66           O\\nATOM   2554  CB  SER A 364      19.919   3.488  36.282  1.00 97.65           C\\nATOM   2555  N   GLN A 365      17.486   2.600  33.682  1.00122.15           N\\nATOM   2556  CA  GLN A 365      17.397   1.937  32.386  1.00115.38           C\\nATOM   2557  C   GLN A 365      16.553   2.767  31.428  1.00110.61           C\\nATOM   2558  O   GLN A 365      15.419   3.137  31.753  1.00 98.43           O\\nATOM   2559  CB  GLN A 365      16.796   0.536  32.527  1.00106.22           C\\nATOM   2560  N   GLN A 366      17.101   3.039  30.246  1.00120.06           N\\nATOM   2561  CA  GLN A 366      16.385   3.791  29.223  1.00115.06           C\\nATOM   2562  C   GLN A 366      15.363   2.887  28.544  1.00110.82           C\\nATOM   2563  O   GLN A 366      15.719   1.836  27.999  1.00106.83           O\\nATOM   2564  CB  GLN A 366      17.364   4.363  28.199  1.00114.61           C\\nATOM   2565  N   LYS A 367      14.097   3.295  28.574  1.00106.95           N\\nATOM   2566  CA  LYS A 367      13.014   2.529  27.974  1.00112.85           C\\nATOM   2567  C   LYS A 367      12.771   2.895  26.516  1.00109.20           C\\nATOM   2568  O   LYS A 367      11.803   2.410  25.921  1.00103.35           O\\nATOM   2569  CB  LYS A 367      11.727   2.721  28.781  1.00115.42           C\\nATOM   2570  N   GLU A 368      13.626   3.733  25.930  1.00114.20           N\\nATOM   2571  CA  GLU A 368      13.436   4.206  24.566  1.00 99.97           C\\nATOM   2572  C   GLU A 368      14.152   3.361  23.525  1.00100.67           C\\nATOM   2573  O   GLU A 368      13.805   3.444  22.342  1.00 97.34           O\\nATOM   2574  CB  GLU A 368      13.920   5.655  24.437  1.00 81.44           C\\nATOM   2575  CG  GLU A 368      13.087   6.681  25.188  1.00 79.48           C\\nATOM   2576  CD  GLU A 368      11.923   7.216  24.368  1.00 87.69           C\\nATOM   2577  OE1 GLU A 368      11.484   6.529  23.419  1.00 87.57           O\\nATOM   2578  OE2 GLU A 368      11.451   8.332  24.674  1.00 90.78           O\\nATOM   2579  N   LYS A 369      15.139   2.557  23.932  1.00101.97           N\\nATOM   2580  CA  LYS A 369      15.965   1.842  22.963  1.00 93.96           C\\nATOM   2581  C   LYS A 369      15.123   0.959  22.051  1.00 87.89           C\\nATOM   2582  O   LYS A 369      15.377   0.886  20.844  1.00 84.82           O\\nATOM   2583  CB  LYS A 369      17.025   1.012  23.689  1.00 94.15           C\\nATOM   2584  N   LYS A 370      14.107   0.291  22.605  1.00 95.07           N\\nATOM   2585  CA  LYS A 370      13.254  -0.567  21.787  1.00 92.51           C\\nATOM   2586  C   LYS A 370      12.587   0.220  20.665  1.00 85.60           C\\nATOM   2587  O   LYS A 370      12.454  -0.280  19.541  1.00 77.93           O\\nATOM   2588  CB  LYS A 370      12.203  -1.254  22.662  1.00 85.65           C\\nATOM   2589  N   ALA A 371      12.167   1.454  20.944  1.00 85.70           N\\nATOM   2590  CA  ALA A 371      11.556   2.271  19.901  1.00 78.85           C\\nATOM   2591  C   ALA A 371      12.589   2.776  18.902  1.00 73.40           C\\nATOM   2592  O   ALA A 371      12.274   2.940  17.718  1.00 67.94           O\\nATOM   2593  CB  ALA A 371      10.805   3.440  20.520  1.00 20.00           C\\nATOM   2594  N   THR A 372      13.820   3.030  19.357  1.00 75.36           N\\nATOM   2595  CA  THR A 372      14.875   3.470  18.451  1.00 64.07           C\\nATOM   2596  C   THR A 372      15.326   2.343  17.535  1.00 71.79           C\\nATOM   2597  O   THR A 372      15.714   2.593  16.389  1.00 80.74           O\\nATOM   2598  CB  THR A 372      16.066   4.010  19.246  1.00 69.33           C\\nATOM   2599  OG1 THR A 372      15.634   5.071  20.104  1.00 74.68           O\\nATOM   2600  CG2 THR A 372      17.138   4.544  18.316  1.00 68.04           C\\nATOM   2601  N   GLN A 373      15.283   1.100  18.019  1.00 68.72           N\\nATOM   2602  CA  GLN A 373      15.663  -0.031  17.180  1.00 79.96           C\\nATOM   2603  C   GLN A 373      14.624  -0.283  16.095  1.00 79.40           C\\nATOM   2604  O   GLN A 373      14.972  -0.633  14.961  1.00 75.09           O\\nATOM   2605  CB  GLN A 373      15.857  -1.276  18.043  1.00 95.27           C\\nATOM   2606  CG  GLN A 373      17.006  -1.162  19.028  1.00107.01           C\\nATOM   2607  CD  GLN A 373      16.835  -2.074  20.228  1.00113.19           C\\nATOM   2608  OE1 GLN A 373      15.768  -2.652  20.438  1.00109.22           O\\nATOM   2609  NE2 GLN A 373      17.889  -2.204  21.025  1.00117.08           N\\nATOM   2610  N   MET A 374      13.345  -0.105  16.421  1.00 79.17           N\\nATOM   2611  CA  MET A 374      12.307  -0.277  15.413  1.00 76.40           C\\nATOM   2612  C   MET A 374      12.384   0.814  14.350  1.00 70.69           C\\nATOM   2613  O   MET A 374      12.182   0.543  13.160  1.00 68.25           O\\nATOM   2614  CB  MET A 374      10.934  -0.292  16.079  1.00 77.49           C\\nATOM   2615  CG  MET A 374       9.801  -0.689  15.153  1.00 81.14           C\\nATOM   2616  SD  MET A 374       8.219  -0.741  16.009  1.00 84.97           S\\nATOM   2617  CE  MET A 374       8.086   0.958  16.565  1.00103.28           C\\nATOM   2618  N   ALA A 375      12.684   2.052  14.756  1.00 72.85           N\\nATOM   2619  CA  ALA A 375      12.789   3.144  13.793  1.00 69.01           C\\nATOM   2620  C   ALA A 375      13.899   2.887  12.783  1.00 71.99           C\\nATOM   2621  O   ALA A 375      13.756   3.203  11.596  1.00 68.65           O\\nATOM   2622  CB  ALA A 375      13.021   4.464  14.513  1.00 20.00           C\\nATOM   2623  N   ALA A 376      15.014   2.312  13.234  1.00 72.30           N\\nATOM   2624  CA  ALA A 376      16.110   2.018  12.320  1.00 74.21           C\\nATOM   2625  C   ALA A 376      15.790   0.830  11.427  1.00 77.19           C\\nATOM   2626  O   ALA A 376      16.261   0.771  10.285  1.00 87.02           O\\nATOM   2627  CB  ALA A 376      17.398   1.765  13.104  1.00 74.32           C\\nATOM   2628  N   ILE A 377      15.001  -0.125  11.921  1.00 87.67           N\\nATOM   2629  CA  ILE A 377      14.633  -1.265  11.089  1.00 95.90           C\\nATOM   2630  C   ILE A 377      13.706  -0.839   9.957  1.00101.03           C\\nATOM   2631  O   ILE A 377      13.826  -1.331   8.830  1.00 92.85           O\\nATOM   2632  CB  ILE A 377      13.963  -2.361  11.939  1.00 20.00           C\\nATOM   2633  CG1 ILE A 377      14.964  -2.954  12.932  1.00 20.00           C\\nATOM   2634  CG2 ILE A 377      13.385  -3.448  11.046  1.00 20.00           C\\nATOM   2635  CD1 ILE A 377      14.332  -3.844  13.978  1.00 20.00           C\\nATOM   2636  N   VAL A 378      12.786   0.088  10.234  1.00 89.06           N\\nATOM   2637  CA  VAL A 378      11.896   0.596   9.192  1.00 75.68           C\\nATOM   2638  C   VAL A 378      12.683   1.387   8.156  1.00 75.18           C\\nATOM   2639  O   VAL A 378      12.445   1.268   6.948  1.00 76.19           O\\nATOM   2640  CB  VAL A 378      10.775   1.445   9.820  1.00 64.00           C\\nATOM   2641  CG1 VAL A 378       9.960   2.132   8.740  1.00 62.64           C\\nATOM   2642  CG2 VAL A 378       9.887   0.580  10.701  1.00 69.48           C\\nATOM   2643  N   ALA A 379      13.629   2.210   8.612  1.00 84.87           N\\nATOM   2644  CA  ALA A 379      14.470   2.963   7.688  1.00 87.10           C\\nATOM   2645  C   ALA A 379      15.330   2.035   6.842  1.00 88.96           C\\nATOM   2646  O   ALA A 379      15.578   2.310   5.662  1.00 81.40           O\\nATOM   2647  CB  ALA A 379      15.348   3.945   8.463  1.00 44.79           C\\nATOM   2648  N   GLY A 380      15.802   0.935   7.428  1.00 77.23           N\\nATOM   2649  CA  GLY A 380      16.620   0.001   6.670  1.00 80.45           C\\nATOM   2650  C   GLY A 380      15.818  -0.749   5.624  1.00 77.59           C\\nATOM   2651  O   GLY A 380      16.246  -0.884   4.475  1.00 69.34           O\\nATOM   2652  N   VAL A 381      14.642  -1.252   6.012  1.00 81.99           N\\nATOM   2653  CA  VAL A 381      13.758  -1.918   5.057  1.00 83.38           C\\nATOM   2654  C   VAL A 381      13.412  -0.978   3.910  1.00 77.79           C\\nATOM   2655  O   VAL A 381      13.311  -1.397   2.751  1.00 66.26           O\\nATOM   2656  CB  VAL A 381      12.494  -2.434   5.772  1.00 76.89           C\\nATOM   2657  CG1 VAL A 381      11.472  -2.937   4.769  1.00 69.18           C\\nATOM   2658  CG2 VAL A 381      12.858  -3.534   6.752  1.00 75.31           C\\nATOM   2659  N   PHE A 382      13.231   0.308   4.214  1.00 79.75           N\\nATOM   2660  CA  PHE A 382      13.014   1.298   3.166  1.00 68.40           C\\nATOM   2661  C   PHE A 382      14.165   1.294   2.171  1.00 73.80           C\\nATOM   2662  O   PHE A 382      13.953   1.186   0.958  1.00 78.38           O\\nATOM   2663  CB  PHE A 382      12.844   2.679   3.796  1.00 62.89           C\\nATOM   2664  CG  PHE A 382      12.514   3.767   2.815  1.00 69.81           C\\nATOM   2665  CD1 PHE A 382      11.203   4.013   2.452  1.00 78.17           C\\nATOM   2666  CD2 PHE A 382      13.513   4.560   2.276  1.00 67.00           C\\nATOM   2667  CE1 PHE A 382      10.895   5.021   1.557  1.00 75.89           C\\nATOM   2668  CE2 PHE A 382      13.211   5.566   1.380  1.00 62.38           C\\nATOM   2669  CZ  PHE A 382      11.900   5.797   1.021  1.00 65.04           C\\nATOM   2670  N   ILE A 383      15.399   1.395   2.672  1.00 79.94           N\\nATOM   2671  CA  ILE A 383      16.564   1.405   1.792  1.00 76.66           C\\nATOM   2672  C   ILE A 383      16.668   0.093   1.027  1.00 74.25           C\\nATOM   2673  O   ILE A 383      17.053   0.072  -0.148  1.00 81.52           O\\nATOM   2674  CB  ILE A 383      17.840   1.702   2.601  1.00 71.78           C\\nATOM   2675  CG1 ILE A 383      17.851   3.163   3.035  1.00 63.66           C\\nATOM   2676  CG2 ILE A 383      19.084   1.400   1.789  1.00 79.30           C\\nATOM   2677  CD1 ILE A 383      17.701   4.126   1.880  1.00 64.10           C\\nATOM   2678  N   ILE A 384      16.309  -1.019   1.668  1.00 77.47           N\\nANISOU 2678  N   ILE A 384    10269   8636  10532   1676   -785   -446       N\\nATOM   2679  CA  ILE A 384      16.346  -2.312   0.990  1.00 77.09           C\\nANISOU 2679  CA  ILE A 384    10626   8415  10249   1786   -743   -487       C\\nATOM   2680  C   ILE A 384      15.395  -2.323  -0.203  1.00 79.25           C\\nANISOU 2680  C   ILE A 384    11068   8660  10381   1476   -652   -397       C\\nATOM   2681  O   ILE A 384      15.699  -2.905  -1.252  1.00 79.85           O\\nANISOU 2681  O   ILE A 384    11325   8712  10302   1540   -544   -477       O\\nATOM   2682  CB  ILE A 384      16.026  -3.439   1.989  1.00 74.75           C\\nANISOU 2682  CB  ILE A 384    10740   7870   9793   1895   -906   -471       C\\nATOM   2683  CG1 ILE A 384      17.200  -3.648   2.941  1.00 77.41           C\\nANISOU 2683  CG1 ILE A 384    10961   8240  10210   2294  -1026   -570       C\\nATOM   2684  CG2 ILE A 384      15.704  -4.737   1.267  1.00 71.60           C\\nANISOU 2684  CG2 ILE A 384    10844   7191   9169   1898   -891   -497       C\\nATOM   2685  CD1 ILE A 384      18.443  -4.186   2.256  1.00 79.90           C\\nANISOU 2685  CD1 ILE A 384    11224   8571  10564   2673   -951   -738       C\\nATOM   2686  N   CYS A 385      14.245  -1.657  -0.076  1.00 75.66           N\\nANISOU 2686  N   CYS A 385    10540   8236   9971   1156   -704   -252       N\\nATOM   2687  CA  CYS A 385      13.214  -1.744  -1.106  1.00 79.40           C\\nANISOU 2687  CA  CYS A 385    11178   8693  10298    856   -690   -152       C\\nATOM   2688  C   CYS A 385      13.483  -0.807  -2.281  1.00 77.99           C\\nANISOU 2688  C   CYS A 385    10754   8710  10168    769   -575    -84       C\\nATOM   2689  O   CYS A 385      13.199  -1.160  -3.432  1.00 80.47           O\\nANISOU 2689  O   CYS A 385    11270   9043  10261    646   -531    -66       O\\nATOM   2690  CB  CYS A 385      11.842  -1.449  -0.500  1.00 80.67           C\\nANISOU 2690  CB  CYS A 385    11312   8841  10500    576   -801    -23       C\\nATOM   2691  SG  CYS A 385      11.235  -2.722   0.645  1.00 83.19           S\\nANISOU 2691  SG  CYS A 385    12017   8939  10653    532   -901    -25       S\\nATOM   2692  N   TRP A 386      14.018   0.384  -2.024  1.00 68.60           N\\nANISOU 2692  N   TRP A 386     9160   7658   9246    804   -535    -37       N\\nATOM   2693  CA  TRP A 386      14.213   1.350  -3.095  1.00 71.32           C\\nANISOU 2693  CA  TRP A 386     9293   8158   9646    667   -432     98       C\\nATOM   2694  C   TRP A 386      15.618   1.346  -3.677  1.00 73.91           C\\nANISOU 2694  C   TRP A 386     9483   8642   9959    842   -227     12       C\\nATOM   2695  O   TRP A 386      15.812   1.874  -4.776  1.00 77.41           O\\nANISOU 2695  O   TRP A 386     9849   9237  10328    705    -92    139       O\\nATOM   2696  CB  TRP A 386      13.885   2.767  -2.612  1.00 68.85           C\\nANISOU 2696  CB  TRP A 386     8631   7857   9670    543   -510    230       C\\nATOM   2697  CG  TRP A 386      12.415   3.071  -2.565  1.00 72.68           C\\nANISOU 2697  CG  TRP A 386     9161   8279  10174    338   -661    365       C\\nATOM   2698  CD1 TRP A 386      11.648   3.236  -1.448  1.00 67.00           C\\nANISOU 2698  CD1 TRP A 386     8370   7494   9594    332   -777    320       C\\nATOM   2699  CD2 TRP A 386      11.534   3.244  -3.684  1.00 78.89           C\\nANISOU 2699  CD2 TRP A 386    10042   9108  10823    121   -715    558       C\\nATOM   2700  NE1 TRP A 386      10.348   3.502  -1.801  1.00 70.95           N\\nANISOU 2700  NE1 TRP A 386     8865   8000  10093    139   -882    461       N\\nATOM   2701  CE2 TRP A 386      10.251   3.512  -3.168  1.00 76.55           C\\nANISOU 2701  CE2 TRP A 386     9677   8767  10641      9   -876    617       C\\nATOM   2702  CE3 TRP A 386      11.706   3.200  -5.072  1.00 78.88           C\\nANISOU 2702  CE3 TRP A 386    10168   9215  10586     17   -646    682       C\\nATOM   2703  CZ2 TRP A 386       9.146   3.736  -3.988  1.00 75.36           C\\nANISOU 2703  CZ2 TRP A 386     9547   8666  10419   -188  -1008    800       C\\nATOM   2704  CZ3 TRP A 386      10.606   3.421  -5.885  1.00 78.84           C\\nANISOU 2704  CZ3 TRP A 386    10240   9252  10462   -196   -791    875       C\\nATOM   2705  CH2 TRP A 386       9.343   3.684  -5.340  1.00 78.30           C\\nANISOU 2705  CH2 TRP A 386    10069   9128  10555   -289   -989    935       C\\nATOM   2706  N   LEU A 387      16.599   0.779  -2.986  1.00 71.16           N\\nANISOU 2706  N   LEU A 387     9082   8289   9666   1138   -199   -185       N\\nATOM   2707  CA  LEU A 387      17.963   0.908  -3.486  1.00 77.39           C\\nANISOU 2707  CA  LEU A 387     9613   9290  10501   1307     10   -275       C\\nATOM   2708  C   LEU A 387      18.178   0.130  -4.783  1.00 81.59           C\\nANISOU 2708  C   LEU A 387    10394   9919  10687   1358    212   -346       C\\nATOM   2709  O   LEU A 387      18.816   0.661  -5.701  1.00 86.35           O\\nANISOU 2709  O   LEU A 387    10786  10774  11250   1288    442   -288       O\\nATOM   2710  CB  LEU A 387      18.985   0.473  -2.436  1.00 76.08           C\\nANISOU 2710  CB  LEU A 387     9284   9129  10492   1656    -47   -481       C\\nATOM   2711  CG  LEU A 387      20.393   0.933  -2.792  1.00 73.95           C\\nANISOU 2711  CG  LEU A 387     8566   9145  10385   1779    152   -557       C\\nATOM   2712  CD1 LEU A 387      20.380   2.425  -3.067  1.00 70.62           C\\nANISOU 2712  CD1 LEU A 387     7792   8838  10202   1432    210   -352       C\\nATOM   2713  CD2 LEU A 387      21.363   0.599  -1.677  1.00 74.27           C\\nANISOU 2713  CD2 LEU A 387     8384   9220  10617   2125     25   -752       C\\nATOM   2714  N   PRO A 388      17.692  -1.112  -4.913  1.00 79.42           N\\nANISOU 2714  N   PRO A 388    10576   9454  10144   1463    148   -479       N\\nATOM   2715  CA  PRO A 388      17.785  -1.780  -6.223  1.00 83.37           C\\nANISOU 2715  CA  PRO A 388    11355  10040  10283   1481    328   -585       C\\nATOM   2716  C   PRO A 388      17.190  -0.967  -7.356  1.00 88.60           C\\nANISOU 2716  C   PRO A 388    12005  10889  10771   1117    400   -357       C\\nATOM   2717  O   PRO A 388      17.670  -1.054  -8.493  1.00 89.35           O\\nANISOU 2717  O   PRO A 388    12143  11216  10591   1123    637   -407       O\\nATOM   2718  CB  PRO A 388      17.015  -3.085  -5.998  1.00 78.09           C\\nANISOU 2718  CB  PRO A 388    11219   9031   9418   1534    148   -722       C\\nATOM   2719  CG  PRO A 388      17.214  -3.371  -4.563  1.00 73.10           C\\nANISOU 2719  CG  PRO A 388    10537   8200   9037   1742    -22   -758       C\\nATOM   2720  CD  PRO A 388      17.196  -2.039  -3.878  1.00 74.29           C\\nANISOU 2720  CD  PRO A 388    10229   8503   9495   1588    -73   -564       C\\nATOM   2721  N   PHE A 389      16.157  -0.168  -7.077  1.00 87.86           N\\nANISOU 2721  N   PHE A 389    11851  10717  10815    821    202   -105       N\\nATOM   2722  CA  PHE A 389      15.588   0.699  -8.103  1.00 88.83           C\\nANISOU 2722  CA  PHE A 389    11946  10997  10808    504    215    164       C\\nATOM   2723  C   PHE A 389      16.581   1.776  -8.524  1.00 87.11           C\\nANISOU 2723  C   PHE A 389    11342  11030  10726    460    445    317       C\\nATOM   2724  O   PHE A 389      16.791   2.009  -9.719  1.00 91.58           O\\nANISOU 2724  O   PHE A 389    11960  11831  11005    327    627    435       O\\nATOM   2725  CB  PHE A 389      14.287   1.323  -7.592  1.00 81.78           C\\nANISOU 2725  CB  PHE A 389    11019   9946  10106    271    -69    378       C\\nATOM   2726  CG  PHE A 389      13.670   2.319  -8.536  1.00 78.75           C\\nANISOU 2726  CG  PHE A 389    10580   9686   9656    -11   -125    698       C\\nATOM   2727  CD1 PHE A 389      12.947   1.897  -9.638  1.00 72.20           C\\nANISOU 2727  CD1 PHE A 389    10065   8946   8421   -182   -197    758       C\\nATOM   2728  CD2 PHE A 389      13.795   3.677  -8.309  1.00 74.32           C\\nANISOU 2728  CD2 PHE A 389     9675   9124   9438   -104   -142    940       C\\nATOM   2729  CE1 PHE A 389      12.374   2.812 -10.501  1.00 66.21           C\\nANISOU 2729  CE1 PHE A 389     9270   8308   7580   -418   -296   1089       C\\nATOM   2730  CE2 PHE A 389      13.221   4.593  -9.169  1.00 73.66           C\\nANISOU 2730  CE2 PHE A 389     9576   9102   9309   -336   -229   1275       C\\nATOM   2731  CZ  PHE A 389      12.508   4.160 -10.263  1.00 67.96           C\\nANISOU 2731  CZ  PHE A 389     9160   8501   8161   -483   -313   1367       C\\nATOM   2732  N   PHE A 390      17.211   2.438  -7.553  1.00 78.28           N\\nANISOU 2732  N   PHE A 390     9842   9876  10022    542    440    319       N\\nATOM   2733  CA  PHE A 390      18.154   3.503  -7.865  1.00 77.80           C\\nANISOU 2733  CA  PHE A 390     9387  10020  10154    435    640    473       C\\nATOM   2734  C   PHE A 390      19.520   2.977  -8.285  1.00 85.50           C\\nANISOU 2734  C   PHE A 390    10201  11281  11003    650    968    266       C\\nATOM   2735  O   PHE A 390      20.266   3.699  -8.955  1.00 80.65           O\\nANISOU 2735  O   PHE A 390     9313  10928  10401    495   1220    418       O\\nATOM   2736  CB  PHE A 390      18.290   4.441  -6.666  1.00 72.78           C\\nANISOU 2736  CB  PHE A 390     8403   9227  10023    409    479    515       C\\nATOM   2737  CG  PHE A 390      17.046   5.229  -6.384  1.00 71.97           C\\nANISOU 2737  CG  PHE A 390     8367   8891  10086    201    217    731       C\\nATOM   2738  CD1 PHE A 390      16.770   6.384  -7.095  1.00 73.92           C\\nANISOU 2738  CD1 PHE A 390     8531   9132  10422    -77    215   1066       C\\nATOM   2739  CD2 PHE A 390      16.146   4.810  -5.423  1.00 69.40           C\\nANISOU 2739  CD2 PHE A 390     8185   8358   9824    295    -21    611       C\\nATOM   2740  CE1 PHE A 390      15.624   7.110  -6.848  1.00 69.85           C\\nANISOU 2740  CE1 PHE A 390     8056   8392  10093   -202    -42   1247       C\\nATOM   2741  CE2 PHE A 390      14.995   5.533  -5.171  1.00 69.17           C\\nANISOU 2741  CE2 PHE A 390     8161   8162   9960    142   -234    777       C\\nATOM   2742  CZ  PHE A 390      14.735   6.685  -5.884  1.00 63.89           C\\nANISOU 2742  CZ  PHE A 390     7389   7471   9415    -78   -256   1080       C\\nATOM   2743  N   ILE A 391      19.865   1.744  -7.905  1.00 83.05           N\\nANISOU 2743  N   ILE A 391    10043  10926  10586   1005    976    -67       N\\nATOM   2744  CA  ILE A 391      21.044   1.100  -8.477  1.00 88.93           C\\nANISOU 2744  CA  ILE A 391    10677  11954  11158   1273   1299   -305       C\\nATOM   2745  C   ILE A 391      20.854   0.907  -9.975  1.00 91.28           C\\nANISOU 2745  C   ILE A 391    11243  12480  10960   1127   1541   -254       C\\nATOM   2746  O   ILE A 391      21.789   1.084 -10.766  1.00 94.74           O\\nANISOU 2746  O   ILE A 391    11451  13294  11253   1139   1904   -276       O\\nATOM   2747  CB  ILE A 391      21.321  -0.238  -7.761  1.00 85.00           C\\nANISOU 2747  CB  ILE A 391    10370  11271  10655   1728   1197   -664       C\\nATOM   2748  CG1 ILE A 391      21.803   0.004  -6.329  1.00 81.99           C\\nANISOU 2748  CG1 ILE A 391     9657  10782  10715   1901    995   -715       C\\nATOM   2749  CG2 ILE A 391      22.336  -1.068  -8.534  1.00 85.18           C\\nANISOU 2749  CG2 ILE A 391    10376  11551  10438   2063   1525   -960       C\\nATOM   2750  CD1 ILE A 391      22.006  -1.268  -5.531  1.00 79.71           C\\nANISOU 2750  CD1 ILE A 391     9598  10266  10423   2344    833   -991       C\\nATOM   2751  N   THR A 392      19.633   0.564 -10.388  1.00 91.03           N\\nANISOU 2751  N   THR A 392    11682  12262  10642    965   1345   -183       N\\nATOM   2752  CA  THR A 392      19.347   0.341 -11.801  1.00 92.03           C\\nANISOU 2752  CA  THR A 392    12124  12607  10236    813   1511   -151       C\\nATOM   2753  C   THR A 392      19.510   1.622 -12.611  1.00 96.64           C\\nANISOU 2753  C   THR A 392    12473  13487  10758    456   1684    247       C\\nATOM   2754  O   THR A 392      19.972   1.585 -13.759  1.00 99.51           O\\nANISOU 2754  O   THR A 392    12896  14212  10701    394   2002    256       O\\nATOM   2755  CB  THR A 392      17.934  -0.222 -11.949  1.00 85.65           C\\nANISOU 2755  CB  THR A 392    11821  11527   9195    670   1183   -144       C\\nATOM   2756  OG1 THR A 392      17.843  -1.462 -11.238  1.00 86.36           O\\nANISOU 2756  OG1 THR A 392    12169  11313   9330    965   1047   -489       O\\nATOM   2757  CG2 THR A 392      17.589  -0.458 -13.404  1.00 82.50           C\\nANISOU 2757  CG2 THR A 392    11776  11367   8203    498   1292   -131       C\\nATOM   2758  N   HIS A 393      19.187   2.742 -12.031  1.00 88.71           N\\nANISOU 2758  N   HIS A 393    11226  12324  10155    219   1485    579       N\\nATOM   2759  CA  HIS A 393      19.363   3.957 -12.738  1.00 88.98           C\\nANISOU 2759  CA  HIS A 393    11056  12550  10202   -130   1618   1001       C\\nATOM   2760  C   HIS A 393      20.809   4.181 -13.033  1.00 88.31           C\\nANISOU 2760  C   HIS A 393    10554  12829  10172   -105   2051    965       C\\nATOM   2761  O   HIS A 393      21.145   4.651 -14.071  1.00 90.40           O\\nANISOU 2761  O   HIS A 393    10759  13392  10197   -381   2313   1255       O\\nATOM   2762  CB  HIS A 393      18.863   5.074 -11.893  1.00 92.81           C\\nANISOU 2762  CB  HIS A 393    11357  12712  11192   -324   1304   1294       C\\nATOM   2763  CG  HIS A 393      17.412   5.334 -12.064  1.00 96.38           C\\nANISOU 2763  CG  HIS A 393    12141  12922  11557   -443    932   1454       C\\nATOM   2764  ND1 HIS A 393      16.815   5.355 -13.296  1.00101.35           N\\nANISOU 2764  ND1 HIS A 393    12985  13642  11882   -712    860   1815       N\\nATOM   2765  CD2 HIS A 393      16.440   5.591 -11.168  1.00 93.09           C\\nANISOU 2765  CD2 HIS A 393    11851  12212  11307   -333    611   1312       C\\nATOM   2766  CE1 HIS A 393      15.536   5.622 -13.155  1.00 98.51           C\\nANISOU 2766  CE1 HIS A 393    12830  13059  11540   -744    489   1868       C\\nATOM   2767  NE2 HIS A 393      15.282   5.762 -11.872  1.00 93.35           N\\nANISOU 2767  NE2 HIS A 393    12117  12180  11171   -533    357   1563       N\\nATOM   2768  N   ILE A 394      21.675   3.869 -12.094  1.00 95.53           N\\nANISOU 2768  N   ILE A 394    11157  13746  11395    209   2124    635       N\\nATOM   2769  CA  ILE A 394      23.103   4.065 -12.304  1.00100.46           C\\nANISOU 2769  CA  ILE A 394    11300  14765  12104    258   2532    556       C\\nATOM   2770  C   ILE A 394      23.590   3.234 -13.480  1.00110.00           C\\nANISOU 2770  C   ILE A 394    12669  16389  12736    410   2939    349       C\\nATOM   2771  O   ILE A 394      24.530   3.628 -14.181  1.00116.65           O\\nANISOU 2771  O   ILE A 394    13187  17679  13455    283   3367    434       O\\nATOM   2772  CB  ILE A 394      23.876   3.735 -11.014  1.00 95.87           C\\nANISOU 2772  CB  ILE A 394    10335  14092  12001    599   2436    239       C\\nATOM   2773  N   LEU A 395      22.959   2.084 -13.726  1.00109.05           N\\nANISOU 2773  N   LEU A 395    13051  16136  12246    661   2828     65       N\\nATOM   2774  CA  LEU A 395      23.384   1.213 -14.816  1.00115.80           C\\nANISOU 2774  CA  LEU A 395    14119  17349  12533    853   3195   -221       C\\nATOM   2775  C   LEU A 395      22.911   1.731 -16.169  1.00123.98           C\\nANISOU 2775  C   LEU A 395    15434  18666  13007    451   3352    106       C\\nATOM   2776  O   LEU A 395      23.622   1.591 -17.170  1.00132.70           O\\nANISOU 2776  O   LEU A 395    16488  20259  13673    459   3812     22       O\\nATOM   2777  CB  LEU A 395      22.873  -0.208 -14.578  1.00113.04           C\\nANISOU 2777  CB  LEU A 395    14254  16684  12011   1243   2983   -662       C\\nATOM   2778  CG  LEU A 395      23.285  -0.827 -13.242  1.00107.58           C\\nANISOU 2778  CG  LEU A 395    13379  15684  11813   1666   2788   -952       C\\nATOM   2779  CD1 LEU A 395      22.874  -2.287 -13.174  1.00109.94           C\\nANISOU 2779  CD1 LEU A 395    14213  15663  11896   2035   2631  -1369       C\\nATOM   2780  CD2 LEU A 395      24.782  -0.681 -13.009  1.00102.89           C\\nANISOU 2780  CD2 LEU A 395    12151  15454  11490   1927   3132  -1110       C\\nATOM   2781  N   ASN A 396      21.713   2.324 -16.219  1.00120.69           N\\nANISOU 2781  N   ASN A 396    15306  17974  12576    116   2975    478       N\\nATOM   2782  CA  ASN A 396      21.242   2.943 -17.454  1.00120.58           C\\nANISOU 2782  CA  ASN A 396    15547  18214  12053   -278   3052    871       C\\nATOM   2783  C   ASN A 396      22.194   4.031 -17.930  1.00122.42           C\\nANISOU 2783  C   ASN A 396    15355  18837  12322   -573   3455   1241       C\\nATOM   2784  O   ASN A 396      22.387   4.205 -19.139  1.00125.81           O\\nANISOU 2784  O   ASN A 396    15933  19697  12171   -784   3770   1420       O\\nATOM   2785  CB  ASN A 396      19.841   3.523 -17.251  1.00116.75           C\\nANISOU 2785  CB  ASN A 396    15328  17340  11693   -546   2527   1239       C\\nATOM   2786  CG  ASN A 396      18.760   2.676 -17.888  1.00117.94           C\\nANISOU 2786  CG  ASN A 396    16062  17433  11316   -534   2274   1087       C\\nATOM   2787  OD1 ASN A 396      18.987   1.516 -18.228  1.00121.59           O\\nANISOU 2787  OD1 ASN A 396    16780  18007  11413   -276   2424    626       O\\nATOM   2788  ND2 ASN A 396      17.576   3.253 -18.057  1.00116.24           N\\nANISOU 2788  ND2 ASN A 396    16052  17032  11079   -807   1870   1457       N\\nATOM   2789  N   ILE A 397      22.806   4.760 -16.997  1.00128.30           N\\nANISOU 2789  N   ILE A 397    15581  19448  13721   -619   3450   1356       N\\nATOM   2790  CA  ILE A 397      23.706   5.849 -17.357  1.00131.63           C\\nANISOU 2790  CA  ILE A 397    15568  20182  14265   -972   3805   1730       C\\nATOM   2791  C   ILE A 397      25.103   5.322 -17.667  1.00137.13           C\\nANISOU 2791  C   ILE A 397    15858  21427  14818   -764   4380   1392       C\\nATOM   2792  O   ILE A 397      25.789   5.839 -18.556  1.00140.52           O\\nANISOU 2792  O   ILE A 397    16093  22338  14959  -1056   4838   1642       O\\nATOM   2793  CB  ILE A 397      23.731   6.896 -16.228  1.00123.72           C\\nANISOU 2793  CB  ILE A 397    14191  18774  14042  -1149   3517   1971       C\\nATOM   2794  CG1 ILE A 397      22.331   7.473 -16.007  1.00113.56           C\\nANISOU 2794  CG1 ILE A 397    13280  16985  12883  -1327   2987   2301       C\\nATOM   2795  CG2 ILE A 397      24.735   8.002 -16.530  1.00125.40           C\\nANISOU 2795  CG2 ILE A 397    13930  19262  14453  -1557   3873   2337       C\\nATOM   2796  CD1 ILE A 397      22.251   8.459 -14.860  1.00102.21           C\\nANISOU 2796  CD1 ILE A 397    11537  15104  12195  -1449   2680   2462       C\\nATOM   2797  N   HIS A 398      25.537   4.278 -16.959  1.00136.75           N\\nANISOU 2797  N   HIS A 398    15674  21329  14958   -248   4372    832       N\\nATOM   2798  CA  HIS A 398      26.930   3.846 -17.033  1.00140.25           C\\nANISOU 2798  CA  HIS A 398    15599  22260  15431     23   4867    485       C\\nATOM   2799  C   HIS A 398      27.250   3.199 -18.376  1.00154.68           C\\nANISOU 2799  C   HIS A 398    17644  24638  16490    117   5371    293       C\\nATOM   2800  O   HIS A 398      28.121   3.674 -19.114  1.00162.37           O\\nANISOU 2800  O   HIS A 398    18256  26184  17254   -111   5901    448       O\\nATOM   2801  CB  HIS A 398      27.240   2.881 -15.886  1.00132.50           C\\nANISOU 2801  CB  HIS A 398    14462  21019  14861    602   4649    -39       C\\nATOM   2802  N   CYS A 399      26.570   2.103 -18.707  1.00157.99           N\\nANISOU 2802  N   CYS A 399    18652  24908  16468    436   5229    -65       N\\nATOM   2803  CA  CYS A 399      26.929   1.309 -19.875  1.00171.19           C\\nANISOU 2803  CA  CYS A 399    20554  27077  17414    635   5693   -403       C\\nATOM   2804  C   CYS A 399      25.915   1.388 -21.006  1.00172.38           C\\nANISOU 2804  C   CYS A 399    21379  27292  16826    306   5614   -163       C\\nATOM   2805  O   CYS A 399      26.152   0.799 -22.069  1.00171.94           O\\nANISOU 2805  O   CYS A 399    21574  27683  16070    417   5999   -433       O\\nATOM   2806  CB  CYS A 399      27.145  -0.157 -19.472  1.00177.68           C\\nANISOU 2806  CB  CYS A 399    21527  27720  18264   1324   5648  -1118       C\\nATOM   2807  SG  CYS A 399      25.689  -1.129 -18.956  1.00177.65           S\\nANISOU 2807  SG  CYS A 399    22318  26935  18245   1520   4957  -1341       S\\nATOM   2808  N   ASP A 400      24.802   2.093 -20.815  1.00169.42           N\\nANISOU 2808  N   ASP A 400    21292  26506  16572    -73   5118    313       N\\nATOM   2809  CA  ASP A 400      23.708   2.176 -21.779  1.00172.19           C\\nANISOU 2809  CA  ASP A 400    22278  26866  16282   -369   4909    565       C\\nATOM   2810  C   ASP A 400      23.130   0.810 -22.126  1.00178.49           C\\nANISOU 2810  C   ASP A 400    23661  27552  16606    -24   4760      1       C\\nATOM   2811  O   ASP A 400      22.354   0.694 -23.084  1.00180.90           O\\nANISOU 2811  O   ASP A 400    24500  27979  16254   -230   4642     91       O\\nATOM   2812  CB  ASP A 400      24.139   2.903 -23.061  1.00174.58           C\\nANISOU 2812  CB  ASP A 400    22570  27804  15958   -772   5382    965       C\\nATOM   2813  N   CYS A 401      23.494  -0.229 -21.377  1.00180.63           N\\nANISOU 2813  N   CYS A 401    23862  27575  17194    489   4738   -576       N\\nATOM   2814  CA  CYS A 401      22.923  -1.551 -21.583  1.00179.00           C\\nANISOU 2814  CA  CYS A 401    24242  27130  16641    806   4543  -1120       C\\nATOM   2815  C   CYS A 401      21.440  -1.519 -21.252  1.00170.63           C\\nANISOU 2815  C   CYS A 401    23622  25538  15671    556   3881   -897       C\\nATOM   2816  O   CYS A 401      21.063  -1.243 -20.109  1.00166.40           O\\nANISOU 2816  O   CYS A 401    22893  24541  15789    548   3513   -729       O\\nATOM   2817  CB  CYS A 401      23.624  -2.583 -20.701  1.00179.14           C\\nANISOU 2817  CB  CYS A 401    24079  26891  17096   1410   4598  -1700       C\\nATOM   2818  SG  CYS A 401      25.421  -2.457 -20.478  1.00183.37           S\\nANISOU 2818  SG  CYS A 401    23801  27930  17940   1774   5237  -1908       S\\nATOM   2819  N   ASN A 402      20.597  -1.793 -22.244  1.00163.09           N\\nANISOU 2819  N   ASN A 402    23235  24683  14049    348   3727   -908       N\\nATOM   2820  CA  ASN A 402      19.171  -1.877 -21.964  1.00152.09           C\\nANISOU 2820  CA  ASN A 402    22222  22828  12736    126   3092   -755       C\\nATOM   2821  C   ASN A 402      18.914  -3.031 -21.004  1.00144.87           C\\nANISOU 2821  C   ASN A 402    21476  21352  12215    479   2819  -1242       C\\nATOM   2822  O   ASN A 402      19.334  -4.167 -21.242  1.00148.09           O\\nANISOU 2822  O   ASN A 402    22151  21737  12380    836   2997  -1823       O\\nATOM   2823  CB  ASN A 402      18.364  -2.039 -23.255  1.00153.00           C\\nANISOU 2823  CB  ASN A 402    22907  23202  12025   -153   2955   -727       C\\nATOM   2824  CG  ASN A 402      18.644  -3.344 -23.970  1.00154.48           C\\nANISOU 2824  CG  ASN A 402    23550  23525  11619    142   3169  -1424       C\\nATOM   2825  OD1 ASN A 402      18.048  -4.376 -23.657  1.00152.23           O\\nANISOU 2825  OD1 ASN A 402    23645  22801  11394    294   2842  -1846       O\\nATOM   2826  ND2 ASN A 402      19.540  -3.303 -24.949  1.00156.47           N\\nANISOU 2826  ND2 ASN A 402    23784  24383  11285    209   3730  -1554       N\\nATOM   2827  N   ILE A 403      18.259  -2.719 -19.893  1.00137.95           N\\nANISOU 2827  N   ILE A 403    20445  20015  11956    389   2403   -999       N\\nATOM   2828  CA  ILE A 403      18.056  -3.664 -18.801  1.00126.08           C\\nANISOU 2828  CA  ILE A 403    19041  17968  10897    679   2150  -1342       C\\nATOM   2829  C   ILE A 403      16.725  -4.370 -19.025  1.00123.67           C\\nANISOU 2829  C   ILE A 403    19300  17348  10341    476   1691  -1463       C\\nATOM   2830  O   ILE A 403      15.774  -3.737 -19.506  1.00123.23           O\\nANISOU 2830  O   ILE A 403    19345  17396  10082     73   1419  -1099       O\\nATOM   2831  CB  ILE A 403      18.121  -2.936 -17.448  1.00116.57           C\\nANISOU 2831  CB  ILE A 403    17344  16498  10450    680   1990  -1029       C\\nATOM   2832  CG1 ILE A 403      19.571  -2.545 -17.154  1.00117.76           C\\nANISOU 2832  CG1 ILE A 403    16950  16923  10871    944   2430  -1064       C\\nATOM   2833  CG2 ILE A 403      17.524  -3.771 -16.324  1.00111.83           C\\nANISOU 2833  CG2 ILE A 403    16927  15326  10238    834   1619  -1235       C\\nATOM   2834  CD1 ILE A 403      19.744  -1.682 -15.938  1.00115.05           C\\nANISOU 2834  CD1 ILE A 403    16103  16396  11214    903   2293   -760       C\\nATOM   2835  N   PRO A 404      16.628  -5.671 -18.745  1.00118.90           N\\nANISOU 2835  N   PRO A 404    19074  16363   9738    731   1581  -1960       N\\nATOM   2836  CA  PRO A 404      15.360  -6.387 -18.918  1.00118.90           C\\nANISOU 2836  CA  PRO A 404    19598  16036   9542    479   1130  -2089       C\\nATOM   2837  C   PRO A 404      14.199  -5.600 -18.342  1.00114.46           C\\nANISOU 2837  C   PRO A 404    18849  15327   9312     80    700  -1589       C\\nATOM   2838  O   PRO A 404      14.149  -5.345 -17.130  1.00111.06           O\\nANISOU 2838  O   PRO A 404    18106  14611   9479    144    589  -1414       O\\nATOM   2839  CB  PRO A 404      15.590  -7.690 -18.142  1.00118.42           C\\nANISOU 2839  CB  PRO A 404    19799  15435   9759    841   1069  -2563       C\\nATOM   2840  CG  PRO A 404      17.050  -7.938 -18.305  1.00121.83           C\\nANISOU 2840  CG  PRO A 404    20054  16085  10152   1347   1569  -2883       C\\nATOM   2841  CD  PRO A 404      17.718  -6.580 -18.344  1.00119.79           C\\nANISOU 2841  CD  PRO A 404    19169  16331  10014   1271   1867  -2444       C\\nATOM   2842  N   PRO A 405      13.257  -5.175 -19.187  1.00111.48           N\\nANISOU 2842  N   PRO A 405    18639  15168   8549   -316    448  -1354       N\\nATOM   2843  CA  PRO A 405      12.126  -4.381 -18.686  1.00109.02           C\\nANISOU 2843  CA  PRO A 405    18100  14751   8571   -653     36   -886       C\\nATOM   2844  C   PRO A 405      11.320  -5.093 -17.621  1.00107.40           C\\nANISOU 2844  C   PRO A 405    17974  14039   8792   -700   -301  -1012       C\\nATOM   2845  O   PRO A 405      10.656  -4.425 -16.820  1.00106.74           O\\nANISOU 2845  O   PRO A 405    17562  13840   9155   -851   -528   -666       O\\nATOM   2846  CB  PRO A 405      11.292  -4.119 -19.948  1.00110.35           C\\nANISOU 2846  CB  PRO A 405    18539  15248   8141  -1009   -207   -731       C\\nATOM   2847  CG  PRO A 405      11.691  -5.197 -20.899  1.00113.76           C\\nANISOU 2847  CG  PRO A 405    19491  15789   7942   -900    -38  -1264       C\\nATOM   2848  CD  PRO A 405      13.141  -5.456 -20.627  1.00117.16           C\\nANISOU 2848  CD  PRO A 405    19780  16246   8490   -452    496  -1536       C\\nATOM   2849  N   VAL A 406      11.356  -6.428 -17.580  1.00111.87           N\\nANISOU 2849  N   VAL A 406    18978  14290   9236   -579   -329  -1496       N\\nATOM   2850  CA  VAL A 406      10.738  -7.139 -16.469  1.00102.56           C\\nANISOU 2850  CA  VAL A 406    17881  12600   8486   -624   -592  -1581       C\\nATOM   2851  C   VAL A 406      11.508  -6.882 -15.181  1.00104.10           C\\nANISOU 2851  C   VAL A 406    17697  12610   9246   -300   -398  -1479       C\\nATOM   2852  O   VAL A 406      10.926  -6.894 -14.090  1.00102.17           O\\nANISOU 2852  O   VAL A 406    17313  12081   9424   -395   -602  -1324       O\\nATOM   2853  CB  VAL A 406      10.640  -8.644 -16.776  1.00 94.49           C\\nANISOU 2853  CB  VAL A 406    17480  11217   7203   -584   -680  -2114       C\\nATOM   2854  N   LEU A 407      12.818  -6.639 -15.277  1.00103.82           N\\nANISOU 2854  N   LEU A 407    17468  12769   9209     74     -3  -1567       N\\nATOM   2855  CA  LEU A 407      13.592  -6.296 -14.089  1.00100.38           C\\nANISOU 2855  CA  LEU A 407    16623  12220   9296    369    146  -1462       C\\nATOM   2856  C   LEU A 407      13.390  -4.838 -13.698  1.00 94.26           C\\nANISOU 2856  C   LEU A 407    15315  11675   8824    182    114   -975       C\\nATOM   2857  O   LEU A 407      13.200  -4.533 -12.516  1.00 88.29           O\\nANISOU 2857  O   LEU A 407    14299  10718   8529    200     -8   -812       O\\nATOM   2858  CB  LEU A 407      15.077  -6.584 -14.317  1.00101.90           C\\nANISOU 2858  CB  LEU A 407    16737  12562   9418    837    561  -1755       C\\nATOM   2859  N   TYR A 408      13.370  -3.956 -14.650  1.00 94.06           N\\nANISOU 2859  N   TYR A 408    15152  12055   8531      5    218   -738       N\\nATOM   2860  CA  TYR A 408      13.143  -2.599 -14.299  1.00 92.67           C\\nANISOU 2860  CA  TYR A 408    14536  12021   8655   -189    141   -264       C\\nATOM   2861  C   TYR A 408      11.764  -2.493 -13.713  1.00 95.64           C\\nANISOU 2861  C   TYR A 408    14901  12179   9258   -462   -278    -65       C\\nATOM   2862  O   TYR A 408      11.578  -1.795 -12.766  1.00 92.85           O\\nANISOU 2862  O   TYR A 408    14175  11751   9352   -489   -366    194       O\\nATOM   2863  CB  TYR A 408      13.263  -1.746 -15.521  1.00 92.66           C\\nANISOU 2863  CB  TYR A 408    14496  12449   8263   -369    283     -7       C\\nATOM   2864  CG  TYR A 408      13.909  -0.444 -15.274  1.00 92.93           C\\nANISOU 2864  CG  TYR A 408    14043  12651   8617   -377    472    359       C\\nATOM   2865  CD1 TYR A 408      13.694   0.227 -14.129  1.00 88.51           C\\nANISOU 2865  CD1 TYR A 408    13122  11858   8651   -379    316    564       C\\nATOM   2866  CD2 TYR A 408      14.725   0.122 -16.199  1.00 98.66           C\\nANISOU 2866  CD2 TYR A 408    14681  13767   9040   -406    819    487       C\\nATOM   2867  CE1 TYR A 408      14.287   1.434 -13.904  1.00 87.26           C\\nANISOU 2867  CE1 TYR A 408    12549  11797   8809   -413    462    866       C\\nATOM   2868  CE2 TYR A 408      15.323   1.331 -15.973  1.00 98.99           C\\nANISOU 2868  CE2 TYR A 408    14288  13921   9401   -474    985    837       C\\nATOM   2869  CZ  TYR A 408      15.086   1.974 -14.814  1.00 95.40           C\\nANISOU 2869  CZ  TYR A 408    13502  13174   9570   -479    786   1014       C\\nATOM   2870  OH  TYR A 408      15.640   3.178 -14.533  1.00 98.94           O\\nANISOU 2870  OH  TYR A 408    13550  13681  10361   -572    923   1329       O\\nATOM   2871  N   SER A 409      10.781  -3.173 -14.278  1.00105.38           N\\nANISOU 2871  N   SER A 409    16521  13320  10198   -667   -536   -211       N\\nATOM   2872  CA  SER A 409       9.431  -3.119 -13.727  1.00100.18           C\\nANISOU 2872  CA  SER A 409    15802  12496   9765   -940   -916    -53       C\\nATOM   2873  C   SER A 409       9.363  -3.750 -12.341  1.00 91.59           C\\nANISOU 2873  C   SER A 409    14684  11035   9081   -825   -948   -193       C\\nATOM   2874  O   SER A 409       8.543  -3.336 -11.513  1.00 85.61           O\\nANISOU 2874  O   SER A 409    13671  10195   8661   -967  -1137      4       O\\nATOM   2875  CB  SER A 409       8.447  -3.811 -14.672  1.00102.06           C\\nANISOU 2875  CB  SER A 409    16434  12778   9567  -1245  -1202   -175       C\\nATOM   2876  OG  SER A 409       8.493  -3.239 -15.967  1.00105.65           O\\nANISOU 2876  OG  SER A 409    16956  13611   9576  -1354  -1197    -26       O\\nATOM   2877  N   ALA A 410      10.216  -4.740 -12.069  1.00 90.76           N\\nANISOU 2877  N   ALA A 410    14837  10715   8935   -552   -765   -524       N\\nATOM   2878  CA  ALA A 410      10.196  -5.405 -10.769  1.00 84.55           C\\nANISOU 2878  CA  ALA A 410    14089   9558   8478   -436   -813   -622       C\\nATOM   2879  C   ALA A 410      10.716  -4.488  -9.669  1.00 85.46           C\\nANISOU 2879  C   ALA A 410    13726   9716   9028   -244   -702   -420       C\\nATOM   2880  O   ALA A 410      10.097  -4.365  -8.607  1.00 76.26           O\\nANISOU 2880  O   ALA A 410    12411   8410   8155   -337   -841   -294       O\\nATOM   2881  CB  ALA A 410      11.018  -6.693 -10.829  1.00 79.54           C\\nANISOU 2881  CB  ALA A 410    13883   8649   7690   -141   -680  -1016       C\\nATOM   2882  N   PHE A 411      11.858  -3.837  -9.904  1.00 82.88           N\\nANISOU 2882  N   PHE A 411    13149   9606   8736      5   -442   -403       N\\nATOM   2883  CA  PHE A 411      12.446  -2.977  -8.883  1.00 81.51           C\\nANISOU 2883  CA  PHE A 411    12529   9464   8975    175   -355   -259       C\\nATOM   2884  C   PHE A 411      11.593  -1.745  -8.614  1.00 76.95           C\\nANISOU 2884  C   PHE A 411    11608   8991   8637    -75   -511     73       C\\nATOM   2885  O   PHE A 411      11.658  -1.179  -7.516  1.00 76.38           O\\nANISOU 2885  O   PHE A 411    11240   8854   8929      0   -536    155       O\\nATOM   2886  CB  PHE A 411      13.859  -2.567  -9.293  1.00 88.89           C\\nANISOU 2886  CB  PHE A 411    13244  10633   9898    438    -44   -321       C\\nATOM   2887  CG  PHE A 411      14.856  -3.688  -9.233  1.00 94.35           C\\nANISOU 2887  CG  PHE A 411    14147  11212  10488    811    121   -674       C\\nATOM   2888  CD1 PHE A 411      14.562  -4.860  -8.555  1.00 93.62           C\\nANISOU 2888  CD1 PHE A 411    14407  10746  10418    926    -36   -865       C\\nATOM   2889  CD2 PHE A 411      16.092  -3.568  -9.846  1.00 94.90           C\\nANISOU 2889  CD2 PHE A 411    14052  11548  10457   1055    438   -805       C\\nATOM   2890  CE1 PHE A 411      15.480  -5.891  -8.497  1.00 91.66           C\\nANISOU 2890  CE1 PHE A 411    14375  10339  10112   1324     82  -1184       C\\nATOM   2891  CE2 PHE A 411      17.013  -4.595  -9.790  1.00 91.21           C\\nANISOU 2891  CE2 PHE A 411    13738  10988   9931   1464    585  -1156       C\\nATOM   2892  CZ  PHE A 411      16.707  -5.757  -9.115  1.00 90.35           C\\nANISOU 2892  CZ  PHE A 411    14011  10453   9865   1623    389  -1349       C\\nATOM   2893  N   THR A 412      10.799  -1.310  -9.596  1.00 86.37           N\\nANISOU 2893  N   THR A 412    12841  10347   9628   -346   -634    251       N\\nATOM   2894  CA  THR A 412       9.854  -0.225  -9.353  1.00 83.78           C\\nANISOU 2894  CA  THR A 412    12208  10075   9551   -541   -831    553       C\\nATOM   2895  C   THR A 412       8.712  -0.693  -8.459  1.00 78.58           C\\nANISOU 2895  C   THR A 412    11565   9242   9050   -678  -1053    522       C\\nATOM   2896  O   THR A 412       8.335  -0.005  -7.503  1.00 75.36           O\\nANISOU 2896  O   THR A 412    10841   8797   8997   -662  -1111    634       O\\nATOM   2897  CB  THR A 412       9.310   0.315 -10.677  1.00 83.99           C\\nANISOU 2897  CB  THR A 412    12287  10328   9297   -765   -948    775       C\\nATOM   2898  OG1 THR A 412      10.397   0.624 -11.557  1.00 88.79           O\\nANISOU 2898  OG1 THR A 412    12926  11134   9675   -676   -690    805       O\\nATOM   2899  CG2 THR A 412       8.491   1.578 -10.436  1.00 76.49           C\\nANISOU 2899  CG2 THR A 412    10981   9411   8671   -879  -1149   1106       C\\nATOM   2900  N   TRP A 413       8.148  -1.866  -8.758  1.00 79.97           N\\nANISOU 2900  N   TRP A 413    12110   9314   8961   -831  -1168    357       N\\nATOM   2901  CA  TRP A 413       7.078  -2.406  -7.927  1.00 79.43           C\\nANISOU 2901  CA  TRP A 413    12060   9094   9024  -1024  -1347    342       C\\nATOM   2902  C   TRP A 413       7.576  -2.703  -6.520  1.00 73.46           C\\nANISOU 2902  C   TRP A 413    11258   8138   8517   -819  -1224    254       C\\nATOM   2903  O   TRP A 413       6.853  -2.491  -5.539  1.00 70.81           O\\nANISOU 2903  O   TRP A 413    10714   7782   8407   -915  -1295    340       O\\nATOM   2904  CB  TRP A 413       6.498  -3.667  -8.569  1.00 85.80           C\\nANISOU 2904  CB  TRP A 413    13317   9783   9501  -1268  -1494    166       C\\nATOM   2905  CG  TRP A 413       5.728  -3.398  -9.828  1.00 91.51           C\\nANISOU 2905  CG  TRP A 413    14070  10739   9962  -1534  -1703    261       C\\nATOM   2906  CD1 TRP A 413       5.242  -2.195 -10.250  1.00 85.59           C\\nANISOU 2906  CD1 TRP A 413    12966  10256   9299  -1598  -1823    542       C\\nATOM   2907  CD2 TRP A 413       5.358  -4.354 -10.833  1.00 96.72           C\\nANISOU 2907  CD2 TRP A 413    15160  11373  10216  -1760  -1855     72       C\\nATOM   2908  NE1 TRP A 413       4.589  -2.343 -11.449  1.00 88.41           N\\nANISOU 2908  NE1 TRP A 413    13492  10790   9309  -1846  -2056    571       N\\nATOM   2909  CE2 TRP A 413       4.646  -3.658 -11.829  1.00 95.02           C\\nANISOU 2909  CE2 TRP A 413    14808  11468   9826  -1963  -2077    265       C\\nATOM   2910  CE3 TRP A 413       5.558  -5.731 -10.985  1.00100.43           C\\nANISOU 2910  CE3 TRP A 413    16143  11559  10456  -1802  -1850   -252       C\\nATOM   2911  CZ2 TRP A 413       4.135  -4.290 -12.963  1.00 98.69           C\\nANISOU 2911  CZ2 TRP A 413    15618  12022   9858  -2226  -2299    130       C\\nATOM   2912  CZ3 TRP A 413       5.049  -6.356 -12.111  1.00103.40           C\\nANISOU 2912  CZ3 TRP A 413    16876  11980  10432  -2067  -2053   -417       C\\nATOM   2913  CH2 TRP A 413       4.347  -5.636 -13.085  1.00102.66           C\\nANISOU 2913  CH2 TRP A 413    16621  12251  10133  -2286  -2277   -233       C\\nATOM   2914  N   LEU A 414       8.817  -3.184  -6.402  1.00 75.32           N\\nANISOU 2914  N   LEU A 414    11667   8256   8695   -521  -1041     79       N\\nATOM   2915  CA  LEU A 414       9.384  -3.467  -5.087  1.00 69.21           C\\nANISOU 2915  CA  LEU A 414    10863   7310   8123   -291   -967     10       C\\nATOM   2916  C   LEU A 414       9.434  -2.210  -4.226  1.00 77.59           C\\nANISOU 2916  C   LEU A 414    11447   8517   9516   -215   -939    159       C\\nATOM   2917  O   LEU A 414       9.179  -2.265  -3.016  1.00 79.71           O\\nANISOU 2917  O   LEU A 414    11637   8710   9938   -194   -969    169       O\\nATOM   2918  CB  LEU A 414      10.778  -4.078  -5.238  1.00 67.92           C\\nANISOU 2918  CB  LEU A 414    10893   7049   7867     71   -800   -201       C\\nATOM   2919  CG  LEU A 414      11.552  -4.368  -3.947  1.00 71.97           C\\nANISOU 2919  CG  LEU A 414    11370   7408   8567    375   -760   -268       C\\nATOM   2920  CD1 LEU A 414      10.756  -5.279  -3.035  1.00 56.68           C\\nANISOU 2920  CD1 LEU A 414     9726   5197   6611    226   -906   -242       C\\nATOM   2921  CD2 LEU A 414      12.904  -4.980  -4.260  1.00 76.87           C\\nANISOU 2921  CD2 LEU A 414    12133   7966   9108    768   -617   -490       C\\nATOM   2922  N   GLY A 415       9.747  -1.065  -4.832  1.00 76.07           N\\nANISOU 2922  N   GLY A 415    10960   8524   9421   -187   -885    275       N\\nATOM   2923  CA  GLY A 415       9.745   0.179  -4.081  1.00 72.96           C\\nANISOU 2923  CA  GLY A 415    10144   8207   9369   -132   -886    390       C\\nATOM   2924  C   GLY A 415       8.357   0.581  -3.618  1.00 74.19           C\\nANISOU 2924  C   GLY A 415    10131   8394   9665   -339  -1044    507       C\\nATOM   2925  O   GLY A 415       8.180   1.043  -2.488  1.00 75.00           O\\nANISOU 2925  O   GLY A 415    10010   8487   9999   -269  -1044    489       O\\nATOM   2926  N   TYR A 416       7.355   0.423  -4.485  1.00 71.29           N\\nANISOU 2926  N   TYR A 416     9841   8097   9148   -588  -1184    609       N\\nATOM   2927  CA  TYR A 416       5.978   0.695  -4.089  1.00 65.72           C\\nANISOU 2927  CA  TYR A 416     8925   7466   8580   -782  -1337    704       C\\nATOM   2928  C   TYR A 416       5.494  -0.288  -3.030  1.00 74.23           C\\nANISOU 2928  C   TYR A 416    10136   8452   9617   -880  -1320    595       C\\nATOM   2929  O   TYR A 416       4.629   0.058  -2.215  1.00 72.94           O\\nANISOU 2929  O   TYR A 416     9706   8378   9627   -957  -1345    631       O\\nATOM   2930  CB  TYR A 416       5.065   0.646  -5.312  1.00 62.97           C\\nANISOU 2930  CB  TYR A 416     8626   7243   8059  -1034  -1533    831       C\\nATOM   2931  CG  TYR A 416       5.257   1.800  -6.266  1.00 72.57           C\\nANISOU 2931  CG  TYR A 416     9671   8573   9328   -975  -1592   1030       C\\nATOM   2932  CD1 TYR A 416       5.334   3.107  -5.802  1.00 77.77           C\\nANISOU 2932  CD1 TYR A 416     9966   9229  10353   -816  -1582   1149       C\\nATOM   2933  CD2 TYR A 416       5.362   1.584  -7.633  1.00 70.98           C\\nANISOU 2933  CD2 TYR A 416     9709   8467   8795  -1089  -1663   1103       C\\nATOM   2934  CE1 TYR A 416       5.505   4.166  -6.675  1.00 81.18           C\\nANISOU 2934  CE1 TYR A 416    10288   9707  10852   -788  -1652   1381       C\\nATOM   2935  CE2 TYR A 416       5.537   2.637  -8.513  1.00 78.84           C\\nANISOU 2935  CE2 TYR A 416    10587   9572   9796  -1063  -1716   1345       C\\nATOM   2936  CZ  TYR A 416       5.608   3.925  -8.030  1.00 78.01           C\\nANISOU 2936  CZ  TYR A 416    10131   9419  10091   -919  -1715   1507       C\\nATOM   2937  OH  TYR A 416       5.781   4.974  -8.906  1.00 66.59           O\\nANISOU 2937  OH  TYR A 416     8612   8022   8665   -917  -1783   1795       O\\nATOM   2938  N   VAL A 417       6.036  -1.510  -3.031  1.00 75.00           N\\nANISOU 2938  N   VAL A 417    10650   8367   9481   -873  -1268    468       N\\nATOM   2939  CA  VAL A 417       5.682  -2.503  -2.019  1.00 75.22           C\\nANISOU 2939  CA  VAL A 417    10882   8250   9450   -979  -1253    416       C\\nATOM   2940  C   VAL A 417       6.049  -2.017  -0.621  1.00 75.65           C\\nANISOU 2940  C   VAL A 417    10726   8332   9686   -769  -1144    400       C\\nATOM   2941  O   VAL A 417       5.383  -2.367   0.363  1.00 73.28           O\\nANISOU 2941  O   VAL A 417    10419   8044   9381   -909  -1125    429       O\\nATOM   2942  CB  VAL A 417       6.357  -3.847  -2.359  1.00 69.42           C\\nANISOU 2942  CB  VAL A 417    10679   7234   8461   -938  -1241    282       C\\nATOM   2943  CG1 VAL A 417       6.474  -4.740  -1.133  1.00 66.88           C\\nANISOU 2943  CG1 VAL A 417    10605   6693   8112   -911  -1204    262       C\\nATOM   2944  CG2 VAL A 417       5.575  -4.550  -3.446  1.00 68.97           C\\nANISOU 2944  CG2 VAL A 417    10878   7133   8193  -1268  -1387    262       C\\nATOM   2945  N   ASN A 418       7.086  -1.184  -0.510  1.00 69.14           N\\nANISOU 2945  N   ASN A 418     9719   7544   9007   -464  -1071    354       N\\nATOM   2946  CA  ASN A 418       7.506  -0.674   0.790  1.00 59.69           C\\nANISOU 2946  CA  ASN A 418     8331   6385   7962   -263  -1004    296       C\\nATOM   2947  C   ASN A 418       6.365   0.000   1.544  1.00 72.46           C\\nANISOU 2947  C   ASN A 418     9629   8176   9728   -397  -1007    338       C\\nATOM   2948  O   ASN A 418       6.372   0.033   2.780  1.00 78.40           O\\nANISOU 2948  O   ASN A 418    10330   8974  10483   -321   -946    277       O\\nATOM   2949  CB  ASN A 418       8.666   0.302   0.607  1.00 65.48           C\\nANISOU 2949  CB  ASN A 418     8842   7154   8882      6   -958    240       C\\nATOM   2950  CG  ASN A 418       9.105   0.938   1.907  1.00 70.06           C\\nANISOU 2950  CG  ASN A 418     9208   7784   9627    195   -932    141       C\\nATOM   2951  OD1 ASN A 418       9.915   0.373   2.644  1.00 72.31           O\\nANISOU 2951  OD1 ASN A 418     9648   8008   9820    376   -923     50       O\\nATOM   2952  ND2 ASN A 418       8.575   2.123   2.197  1.00 73.88           N\\nANISOU 2952  ND2 ASN A 418     9344   8372  10354    175   -946    143       N\\nATOM   2953  N   SER A 419       5.371   0.528   0.828  1.00 73.71           N\\nANISOU 2953  N   SER A 419     9563   8456   9988   -577  -1081    433       N\\nATOM   2954  CA  SER A 419       4.257   1.208   1.479  1.00 74.87           C\\nANISOU 2954  CA  SER A 419     9342   8795  10311   -653  -1075    444       C\\nATOM   2955  C   SER A 419       3.387   0.269   2.304  1.00 71.13           C\\nANISOU 2955  C   SER A 419     8963   8398   9665   -899  -1010    455       C\\nATOM   2956  O   SER A 419       2.578   0.748   3.105  1.00 79.35           O\\nANISOU 2956  O   SER A 419     9691   9646  10814   -930   -935    423       O\\nATOM   2957  CB  SER A 419       3.402   1.927   0.433  1.00 76.98           C\\nANISOU 2957  CB  SER A 419     9339   9174  10737   -757  -1215    564       C\\nATOM   2958  OG  SER A 419       4.102   3.028  -0.124  1.00 76.00           O\\nANISOU 2958  OG  SER A 419     9078   8985  10813   -542  -1256    597       O\\nATOM   2959  N   ALA A 420       3.532  -1.043   2.146  1.00 64.52           N\\nANISOU 2959  N   ALA A 420     8553   7392   8567  -1076  -1023    494       N\\nATOM   2960  CA  ALA A 420       2.711  -1.998   2.873  1.00 70.62           C\\nANISOU 2960  CA  ALA A 420     9465   8194   9173  -1382   -964    556       C\\nATOM   2961  C   ALA A 420       3.486  -2.802   3.908  1.00 76.87           C\\nANISOU 2961  C   ALA A 420    10638   8808   9762  -1279   -878    546       C\\nATOM   2962  O   ALA A 420       2.886  -3.634   4.598  1.00 79.00           O\\nANISOU 2962  O   ALA A 420    11085   9071   9862  -1550   -815    643       O\\nATOM   2963  CB  ALA A 420       2.026  -2.954   1.892  1.00 69.09           C\\nANISOU 2963  CB  ALA A 420     9496   7901   8853  -1760  -1092    637       C\\nATOM   2964  N   VAL A 421       4.793  -2.590   4.035  1.00 77.91           N\\nANISOU 2964  N   VAL A 421    10893   8806   9904   -910   -888    455       N\\nATOM   2965  CA  VAL A 421       5.579  -3.412   4.946  1.00 79.27           C\\nANISOU 2965  CA  VAL A 421    11443   8799   9879   -770   -869    464       C\\nATOM   2966  C   VAL A 421       5.680  -2.792   6.335  1.00 78.59           C\\nANISOU 2966  C   VAL A 421    11159   8929   9775   -616   -776    415       C\\nATOM   2967  O   VAL A 421       5.844  -3.521   7.319  1.00 80.37           O\\nANISOU 2967  O   VAL A 421    11677   9096   9766   -626   -753    490       O\\nATOM   2968  CB  VAL A 421       6.980  -3.686   4.367  1.00 73.59           C\\nANISOU 2968  CB  VAL A 421    10961   7841   9160   -437   -947    375       C\\nATOM   2969  CG1 VAL A 421       6.871  -4.312   2.991  1.00 71.39           C\\nANISOU 2969  CG1 VAL A 421    10910   7375   8838   -578  -1015    377       C\\nATOM   2970  CG2 VAL A 421       7.810  -2.409   4.324  1.00 65.73           C\\nANISOU 2970  CG2 VAL A 421     9584   7002   8387   -121   -934    246       C\\nATOM   2971  N   ASN A 422       5.581  -1.466   6.440  1.00 74.03           N\\nANISOU 2971  N   ASN A 422    10123   8582   9422   -475   -738    288       N\\nATOM   2972  CA  ASN A 422       5.742  -0.820   7.742  1.00 73.83           C\\nANISOU 2972  CA  ASN A 422     9929   8759   9366   -304   -662    170       C\\nATOM   2973  C   ASN A 422       4.697  -1.265   8.756  1.00 74.68           C\\nANISOU 2973  C   ASN A 422    10063   9076   9236   -564   -510    254       C\\nATOM   2974  O   ASN A 422       5.081  -1.611   9.887  1.00 76.59           O\\nANISOU 2974  O   ASN A 422    10516   9367   9218   -484   -475    261       O\\nATOM   2975  CB  ASN A 422       5.757   0.700   7.560  1.00 72.41           C\\nANISOU 2975  CB  ASN A 422     9279   8717   9517   -120   -663     -7       C\\nATOM   2976  CG  ASN A 422       7.075   1.199   7.026  1.00 70.46           C\\nANISOU 2976  CG  ASN A 422     9018   8305   9448    152   -777    -94       C\\nATOM   2977  OD1 ASN A 422       8.006   0.419   6.829  1.00 69.93           O\\nANISOU 2977  OD1 ASN A 422     9248   8068   9254    251   -842    -54       O\\nATOM   2978  ND2 ASN A 422       7.166   2.500   6.780  1.00 74.23           N\\nANISOU 2978  ND2 ASN A 422     9142   8823  10239    275   -798   -213       N\\nATOM   2979  N   PRO A 423       3.396  -1.299   8.444  1.00 74.98           N\\nANISOU 2979  N   PRO A 423     9889   9275   9326   -884   -418    332       N\\nATOM   2980  CA  PRO A 423       2.439  -1.829   9.431  1.00 79.39           C\\nANISOU 2980  CA  PRO A 423    10466  10068   9629  -1180   -229    435       C\\nATOM   2981  C   PRO A 423       2.722  -3.267   9.832  1.00 83.90           C\\nANISOU 2981  C   PRO A 423    11615  10404   9861  -1378   -249    663       C\\nATOM   2982  O   PRO A 423       2.406  -3.662  10.961  1.00 90.16           O\\nANISOU 2982  O   PRO A 423    12538  11363  10356  -1521    -99    763       O\\nATOM   2983  CB  PRO A 423       1.089  -1.697   8.713  1.00 72.48           C\\nANISOU 2983  CB  PRO A 423     9227   9375   8937  -1503   -180    488       C\\nATOM   2984  CG  PRO A 423       1.299  -0.620   7.719  1.00 68.97           C\\nANISOU 2984  CG  PRO A 423     8463   8890   8854  -1250   -321    353       C\\nATOM   2985  CD  PRO A 423       2.703  -0.792   7.246  1.00 69.67           C\\nANISOU 2985  CD  PRO A 423     8902   8634   8934   -993   -481    335       C\\nATOM   2986  N   ILE A 424       3.313  -4.062   8.939  1.00 83.26           N\\nANISOU 2986  N   ILE A 424    11907   9927   9801  -1380   -427    747       N\\nATOM   2987  CA  ILE A 424       3.682  -5.430   9.285  1.00 83.10           C\\nANISOU 2987  CA  ILE A 424    12489   9580   9504  -1500   -487    952       C\\nATOM   2988  C   ILE A 424       4.819  -5.441  10.300  1.00 81.27           C\\nANISOU 2988  C   ILE A 424    12492   9304   9083  -1119   -542    931       C\\nATOM   2989  O   ILE A 424       4.919  -6.359  11.125  1.00 80.08           O\\nANISOU 2989  O   ILE A 424    12773   9025   8629  -1213   -546   1138       O\\nATOM   2990  CB  ILE A 424       4.040  -6.206   8.002  1.00 78.55           C\\nANISOU 2990  CB  ILE A 424    12237   8582   9027  -1536   -666    971       C\\nATOM   2991  CG1 ILE A 424       2.825  -6.276   7.073  1.00 73.56           C\\nANISOU 2991  CG1 ILE A 424    11398   8028   8524  -1971   -654   1003       C\\nATOM   2992  CG2 ILE A 424       4.560  -7.600   8.325  1.00 80.22           C\\nANISOU 2992  CG2 ILE A 424    13116   8357   9008  -1567   -766   1149       C\\nATOM   2993  CD1 ILE A 424       3.095  -6.975   5.758  1.00 71.89           C\\nANISOU 2993  CD1 ILE A 424    11502   7446   8367  -2028   -834    970       C\\nATOM   2994  N   ILE A 425       5.680  -4.422  10.275  1.00 72.91           N\\nANISOU 2994  N   ILE A 425    11155   8352   8197   -705   -607    699       N\\nATOM   2995  CA  ILE A 425       6.795  -4.363  11.215  1.00 77.19           C\\nANISOU 2995  CA  ILE A 425    11857   8894   8577   -341   -708    646       C\\nATOM   2996  C   ILE A 425       6.320  -3.961  12.608  1.00 86.64           C\\nANISOU 2996  C   ILE A 425    12947  10469   9504   -403   -561    636       C\\nATOM   2997  O   ILE A 425       6.863  -4.432  13.615  1.00 84.58           O\\nANISOU 2997  O   ILE A 425    13008  10207   8921   -280   -633    733       O\\nATOM   2998  CB  ILE A 425       7.877  -3.406  10.689  1.00 71.65           C\\nANISOU 2998  CB  ILE A 425    10863   8188   8172     58   -830    392       C\\nATOM   2999  CG1 ILE A 425       8.343  -3.850   9.303  1.00 71.05           C\\nANISOU 2999  CG1 ILE A 425    10906   7796   8294    111   -926    402       C\\nATOM   3000  CG2 ILE A 425       9.062  -3.360  11.634  1.00 68.37           C\\nANISOU 3000  CG2 ILE A 425    10565   7798   7613    422   -980    318       C\\nATOM   3001  CD1 ILE A 425       9.377  -2.939   8.685  1.00 69.86           C\\nANISOU 3001  CD1 ILE A 425    10448   7667   8427    435  -1000    194       C\\nATOM   3002  N   TYR A 426       5.302  -3.102  12.695  1.00 80.85           N\\nANISOU 3002  N   TYR A 426    11769  10077   8874   -571   -359    514       N\\nATOM   3003  CA  TYR A 426       4.811  -2.668  13.999  1.00 87.40           C\\nANISOU 3003  CA  TYR A 426    12467  11316   9424   -609   -172    444       C\\nATOM   3004  C   TYR A 426       4.159  -3.813  14.767  1.00 95.75           C\\nANISOU 3004  C   TYR A 426    13906  12427  10045   -980    -30    771       C\\nATOM   3005  O   TYR A 426       4.175  -3.815  16.004  1.00 99.16           O\\nANISOU 3005  O   TYR A 426    14463  13130  10085   -961     67    794       O\\nATOM   3006  CB  TYR A 426       3.826  -1.511  13.828  1.00 86.99           C\\nANISOU 3006  CB  TYR A 426    11825  11596   9630   -664     22    214       C\\nATOM   3007  CG  TYR A 426       4.370  -0.345  13.027  1.00 85.70           C\\nANISOU 3007  CG  TYR A 426    11311  11332   9920   -350   -120    -55       C\\nATOM   3008  CD1 TYR A 426       5.706   0.027  13.118  1.00 83.30           C\\nANISOU 3008  CD1 TYR A 426    11097  10869   9684      2   -327   -201       C\\nATOM   3009  CD2 TYR A 426       3.547   0.381  12.176  1.00 83.93           C\\nANISOU 3009  CD2 TYR A 426    10656  11172  10061   -422    -61   -137       C\\nATOM   3010  CE1 TYR A 426       6.206   1.093  12.385  1.00 79.72           C\\nANISOU 3010  CE1 TYR A 426    10330  10311   9648    224   -438   -408       C\\nATOM   3011  CE2 TYR A 426       4.037   1.447  11.441  1.00 82.37           C\\nANISOU 3011  CE2 TYR A 426    10186  10845  10265   -163   -196   -323       C\\nATOM   3012  CZ  TYR A 426       5.368   1.799  11.548  1.00 77.29           C\\nANISOU 3012  CZ  TYR A 426     9656  10030   9679    135   -368   -452       C\\nATOM   3013  OH  TYR A 426       5.859   2.858  10.815  1.00 65.48           O\\nANISOU 3013  OH  TYR A 426     7898   8395   8588    330   -485   -601       O\\nATOM   3014  N   THR A 427       3.583  -4.790  14.059  1.00 94.12           N\\nANISOU 3014  N   THR A 427    13912  11967   9880  -1346    -21   1029       N\\nATOM   3015  CA  THR A 427       2.981  -5.936  14.735  1.00 94.73           C\\nANISOU 3015  CA  THR A 427    14395  12024   9574  -1766    104   1385       C\\nATOM   3016  C   THR A 427       4.036  -6.873  15.301  1.00 93.77           C\\nANISOU 3016  C   THR A 427    14923  11553   9151  -1581   -115   1608       C\\nATOM   3017  O   THR A 427       3.779  -7.565  16.293  1.00107.23           O\\nANISOU 3017  O   THR A 427    16989  13325  10429  -1808    -22   1896       O\\nATOM   3018  CB  THR A 427       2.076  -6.711  13.777  1.00 92.02           C\\nANISOU 3018  CB  THR A 427    14101  11462   9402  -2246    135   1572       C\\nATOM   3019  OG1 THR A 427       2.869  -7.267  12.722  1.00 87.69           O\\nANISOU 3019  OG1 THR A 427    13873  10378   9067  -2083   -148   1577       O\\nATOM   3020  CG2 THR A 427       1.028  -5.801  13.182  1.00 92.49           C\\nANISOU 3020  CG2 THR A 427    13488  11881   9771  -2397    298   1371       C\\nATOM   3021  N   THR A 428       5.216  -6.918  14.687  1.00 86.78           N\\nANISOU 3021  N   THR A 428    14188  10309   8477  -1167   -404   1497       N\\nATOM   3022  CA  THR A 428       6.250  -7.850  15.112  1.00 80.90           C\\nANISOU 3022  CA  THR A 428    14030   9197   7512   -924   -656   1699       C\\nATOM   3023  C   THR A 428       7.087  -7.298  16.260  1.00 88.26           C\\nANISOU 3023  C   THR A 428    14945  10410   8178   -536   -758   1595       C\\nATOM   3024  O   THR A 428       7.228  -7.954  17.297  1.00 98.04           O\\nANISOU 3024  O   THR A 428    16618  11653   8981   -567   -810   1867       O\\nATOM   3025  CB  THR A 428       7.162  -8.200  13.934  1.00 75.14           C\\nANISOU 3025  CB  THR A 428    13433   7992   7124   -626   -905   1599       C\\nATOM   3026  OG1 THR A 428       6.369  -8.438  12.764  1.00 66.95           O\\nANISOU 3026  OG1 THR A 428    12310   6784   6344   -965   -819   1592       O\\nATOM   3027  CG2 THR A 428       7.977  -9.450  14.258  1.00 74.10           C\\nANISOU 3027  CG2 THR A 428    13971   7385   6798   -439  -1156   1861       C\\nATOM   3028  N   PHE A 429       7.642  -6.097  16.092  1.00 82.80           N\\nANISOU 3028  N   PHE A 429    13778   9948   7733   -194   -807   1216       N\\nATOM   3029  CA  PHE A 429       8.628  -5.569  17.024  1.00 85.65           C\\nANISOU 3029  CA  PHE A 429    14115  10520   7909    205   -988   1057       C\\nATOM   3030  C   PHE A 429       8.031  -4.731  18.145  1.00 88.27           C\\nANISOU 3030  C   PHE A 429    14208  11398   7933    109   -780    904       C\\nATOM   3031  O   PHE A 429       8.759  -4.373  19.077  1.00 94.52           O\\nANISOU 3031  O   PHE A 429    15046  12401   8467    386   -940    780       O\\nATOM   3032  CB  PHE A 429       9.666  -4.731  16.274  1.00 81.51           C\\nANISOU 3032  CB  PHE A 429    13220   9923   7826    606  -1176    717       C\\nATOM   3033  CG  PHE A 429      10.610  -5.545  15.451  1.00 86.84           C\\nANISOU 3033  CG  PHE A 429    14151  10141   8702    848  -1415    814       C\\nATOM   3034  CD1 PHE A 429      11.723  -6.132  16.031  1.00 95.71           C\\nANISOU 3034  CD1 PHE A 429    15590  11131   9647   1208  -1714    909       C\\nATOM   3035  CD2 PHE A 429      10.383  -5.736  14.099  1.00 90.50           C\\nANISOU 3035  CD2 PHE A 429    14539  10330   9515    740  -1348    797       C\\nATOM   3036  CE1 PHE A 429      12.597  -6.891  15.275  1.00100.77           C\\nANISOU 3036  CE1 PHE A 429    16434  11359  10493   1488  -1918    962       C\\nATOM   3037  CE2 PHE A 429      11.253  -6.492  13.334  1.00 94.15           C\\nANISOU 3037  CE2 PHE A 429    15239  10395  10137    990  -1533    835       C\\nATOM   3038  CZ  PHE A 429      12.362  -7.070  13.923  1.00 99.97           C\\nANISOU 3038  CZ  PHE A 429    16261  10992  10733   1381  -1805    907       C\\nATOM   3039  N   ASN A 430       6.743  -4.409  18.090  1.00 83.72           N\\nANISOU 3039  N   ASN A 430    13363  11080   7368   -257   -438    882       N\\nATOM   3040  CA  ASN A 430       6.116  -3.571  19.103  1.00 88.98           C\\nANISOU 3040  CA  ASN A 430    13756  12293   7759   -315   -190    673       C\\nATOM   3041  C   ASN A 430       4.910  -4.295  19.678  1.00 94.26           C\\nANISOU 3041  C   ASN A 430    14603  13185   8026   -804    139    994       C\\nATOM   3042  O   ASN A 430       3.949  -4.578  18.954  1.00 90.37           O\\nANISOU 3042  O   ASN A 430    13952  12628   7755  -1162    332   1116       O\\nATOM   3043  CB  ASN A 430       5.708  -2.218  18.523  1.00 82.34           C\\nANISOU 3043  CB  ASN A 430    12274  11632   7378   -219    -60    251       C\\nATOM   3044  CG  ASN A 430       5.177  -1.278  19.577  1.00 86.94           C\\nANISOU 3044  CG  ASN A 430    12575  12746   7711   -183    175    -57       C\\nATOM   3045  OD1 ASN A 430       3.978  -1.247  19.844  1.00 86.57           O\\nANISOU 3045  OD1 ASN A 430    12339  13023   7531   -474    525    -28       O\\nATOM   3046  ND2 ASN A 430       6.069  -0.510  20.193  1.00 93.49           N\\nANISOU 3046  ND2 ASN A 430    13362  13689   8473    174    -14   -380       N\\nATOM   3047  N   ILE A 431       4.963  -4.590  20.979  1.00 96.66           N\\nANISOU 3047  N   ILE A 431    15226  13779   7721   -842    197   1137       N\\nATOM   3048  CA  ILE A 431       3.848  -5.262  21.638  1.00 92.58           C\\nANISOU 3048  CA  ILE A 431    14883  13536   6757  -1346    552   1472       C\\nATOM   3049  C   ILE A 431       2.630  -4.348  21.695  1.00 98.55           C\\nANISOU 3049  C   ILE A 431    15013  14819   7614  -1537    984   1175       C\\nATOM   3050  O   ILE A 431       1.488  -4.806  21.569  1.00 98.81           O\\nANISOU 3050  O   ILE A 431    14936  14997   7611  -2018   1303   1397       O\\nATOM   3051  CB  ILE A 431       4.263  -5.738  23.042  1.00 91.00           C\\nANISOU 3051  CB  ILE A 431    15200  13558   5818  -1318    503   1710       C\\nATOM   3052  N   GLU A 432       2.851  -3.043  21.881  1.00 96.20           N\\nANISOU 3052  N   GLU A 432    14279  14803   7470  -1163    992    657       N\\nATOM   3053  CA  GLU A 432       1.733  -2.109  21.979  1.00 93.30           C\\nANISOU 3053  CA  GLU A 432    13305  14920   7225  -1248   1385    325       C\\nATOM   3054  C   GLU A 432       1.005  -1.971  20.646  1.00 90.82           C\\nANISOU 3054  C   GLU A 432    12560  14400   7549  -1408   1437    316       C\\nATOM   3055  O   GLU A 432      -0.230  -1.927  20.610  1.00 84.30           O\\nANISOU 3055  O   GLU A 432    11363  13912   6757  -1725   1791    333       O\\nATOM   3056  CB  GLU A 432       2.229  -0.750  22.471  1.00 88.42           C\\nANISOU 3056  CB  GLU A 432    12394  14544   6659   -774   1324   -250       C\\nATOM   3057  N   PHE A 433       1.747  -1.901  19.538  1.00 90.26           N\\nANISOU 3057  N   PHE A 433    12509  13817   7970  -1197   1087    288       N\\nATOM   3058  CA  PHE A 433       1.098  -1.850  18.232  1.00 93.03           C\\nANISOU 3058  CA  PHE A 433    12520  13969   8860  -1363   1090    317       C\\nATOM   3059  C   PHE A 433       0.366  -3.155  17.929  1.00 92.59           C\\nANISOU 3059  C   PHE A 433    12717  13789   8674  -1909   1194    776       C\\nATOM   3060  O   PHE A 433      -0.768  -3.136  17.438  1.00 86.48           O\\nANISOU 3060  O   PHE A 433    11554  13195   8111  -2229   1396    805       O\\nATOM   3061  CB  PHE A 433       2.125  -1.540  17.137  1.00 94.23           C\\nANISOU 3061  CB  PHE A 433    12696  13628   9479  -1036    712    208       C\\nATOM   3062  CG  PHE A 433       2.253  -0.070  16.807  1.00 90.02           C\\nANISOU 3062  CG  PHE A 433    11657  13176   9371   -672    669   -233       C\\nATOM   3063  CD1 PHE A 433       1.220   0.604  16.178  1.00 82.18           C\\nANISOU 3063  CD1 PHE A 433    10137  12335   8753   -746    821   -367       C\\nATOM   3064  CD2 PHE A 433       3.413   0.630  17.106  1.00 88.82           C\\nANISOU 3064  CD2 PHE A 433    11559  12920   9269   -265    446   -498       C\\nATOM   3065  CE1 PHE A 433       1.331   1.949  15.867  1.00 78.56           C\\nANISOU 3065  CE1 PHE A 433     9265  11877   8709   -401    756   -738       C\\nATOM   3066  CE2 PHE A 433       3.531   1.976  16.796  1.00 82.75           C\\nANISOU 3066  CE2 PHE A 433    10368  12155   8919     24    394   -882       C\\nATOM   3067  CZ  PHE A 433       2.487   2.635  16.177  1.00 81.74           C\\nANISOU 3067  CZ  PHE A 433     9768  12128   9161    -34    550   -991       C\\nATOM   3068  N   ARG A 434       0.991  -4.296  18.232  1.00 96.08           N\\nANISOU 3068  N   ARG A 434    13805  13913   8786  -2025   1037   1134       N\\nATOM   3069  CA  ARG A 434       0.385  -5.588  17.918  1.00 91.88           C\\nANISOU 3069  CA  ARG A 434    13600  13146   8164  -2562   1089   1576       C\\nATOM   3070  C   ARG A 434      -0.930  -5.778  18.663  1.00 88.38           C\\nANISOU 3070  C   ARG A 434    12942  13229   7411  -3068   1532   1730       C\\nATOM   3071  O   ARG A 434      -1.944  -6.162  18.068  1.00 89.59           O\\nANISOU 3071  O   ARG A 434    12864  13413   7764  -3530   1674   1870       O\\nATOM   3072  CB  ARG A 434       1.360  -6.718  18.249  1.00 91.99           C\\nANISOU 3072  CB  ARG A 434    14390  12689   7871  -2520    823   1923       C\\nATOM   3073  N   LYS A 435      -0.934  -5.515  19.973  1.00 92.30           N\\nANISOU 3073  N   LYS A 435    13491  14183   7397  -3005   1759   1697       N\\nATOM   3074  CA  LYS A 435      -2.157  -5.679  20.753  1.00 95.80           C\\nANISOU 3074  CA  LYS A 435    13709  15207   7485  -3485   2243   1837       C\\nATOM   3075  C   LYS A 435      -3.199  -4.633  20.385  1.00 95.39           C\\nANISOU 3075  C   LYS A 435    12798  15636   7810  -3466   2525   1447       C\\nATOM   3076  O   LYS A 435      -4.399  -4.865  20.566  1.00100.11           O\\nANISOU 3076  O   LYS A 435    13054  16654   8329  -3942   2904   1572       O\\nATOM   3077  CB  LYS A 435      -1.843  -5.617  22.249  1.00100.45           C\\nANISOU 3077  CB  LYS A 435    14594  16206   7366  -3383   2418   1871       C\\nATOM   3078  N   ALA A 436      -2.763  -3.482  19.869  1.00 97.48           N\\nANISOU 3078  N   ALA A 436    12695  15840   8503  -2926   2339    989       N\\nATOM   3079  CA  ALA A 436      -3.711  -2.457  19.446  1.00 99.12           C\\nANISOU 3079  CA  ALA A 436    12109  16422   9131  -2835   2542    627       C\\nATOM   3080  C   ALA A 436      -4.463  -2.884  18.193  1.00 98.71           C\\nANISOU 3080  C   ALA A 436    11791  16164   9549  -3194   2456    809       C\\nATOM   3081  O   ALA A 436      -5.682  -2.702  18.103  1.00 98.79           O\\nANISOU 3081  O   ALA A 436    11222  16613   9701  -3464   2744    764       O\\nATOM   3082  CB  ALA A 436      -2.984  -1.133  19.210  1.00 94.08           C\\nANISOU 3082  CB  ALA A 436    11230  15675   8839  -2179   2321    134       C\\nATOM   3083  N   PHE A 437      -3.753  -3.456  17.217  1.00 90.64           N\\nANISOU 3083  N   PHE A 437    11168  14510   8763  -3193   2056    991       N\\nATOM   3084  CA  PHE A 437      -4.405  -3.888  15.985  1.00 89.75           C\\nANISOU 3084  CA  PHE A 437    10864  14185   9052  -3536   1925   1136       C\\nATOM   3085  C   PHE A 437      -5.403  -5.004  16.256  1.00 98.61           C\\nANISOU 3085  C   PHE A 437    12055  15479   9935  -4263   2173   1518       C\\nATOM   3086  O   PHE A 437      -6.491  -5.031  15.669  1.00 97.68           O\\nANISOU 3086  O   PHE A 437    11436  15585  10092  -4617   2265   1534       O\\nATOM   3087  CB  PHE A 437      -3.365  -4.353  14.965  1.00 85.17           C\\nANISOU 3087  CB  PHE A 437    10775  12904   8681  -3381   1477   1231       C\\nATOM   3088  CG  PHE A 437      -2.480  -3.255  14.437  1.00 86.40           C\\nANISOU 3088  CG  PHE A 437    10779  12886   9165  -2763   1230    890       C\\nATOM   3089  CD1 PHE A 437      -2.661  -1.937  14.822  1.00 90.40           C\\nANISOU 3089  CD1 PHE A 437    10767  13767   9814  -2388   1365    522       C\\nATOM   3090  CD2 PHE A 437      -1.469  -3.548  13.540  1.00 80.59           C\\nANISOU 3090  CD2 PHE A 437    10422  11598   8603  -2569    873    931       C\\nATOM   3091  CE1 PHE A 437      -1.838  -0.938  14.328  1.00 85.90           C\\nANISOU 3091  CE1 PHE A 437    10090  12981   9568  -1879   1127    241       C\\nATOM   3092  CE2 PHE A 437      -0.645  -2.555  13.044  1.00 80.08           C\\nANISOU 3092  CE2 PHE A 437    10206  11388   8833  -2065    672    655       C\\nATOM   3093  CZ  PHE A 437      -0.831  -1.248  13.438  1.00 81.28           C\\nANISOU 3093  CZ  PHE A 437     9867  11875   9140  -1744    789    329       C\\nATOM   3094  N   LEU A 438      -5.047  -5.938  17.144  1.00 97.43           N\\nANISOU 3094  N   LEU A 438    12520  15222   9276  -4511   2262   1848       N\\nATOM   3095  CA  LEU A 438      -5.930  -7.059  17.446  1.00 99.16           C\\nANISOU 3095  CA  LEU A 438    12887  15540   9250  -5265   2497   2270       C\\nATOM   3096  C   LEU A 438      -7.187  -6.605  18.176  1.00104.88           C\\nANISOU 3096  C   LEU A 438    12926  17091   9832  -5548   3020   2189       C\\nATOM   3097  O   LEU A 438      -8.233  -7.257  18.066  1.00112.28           O\\nANISOU 3097  O   LEU A 438    13646  18228  10786  -6211   3228   2440       O\\nATOM   3098  CB  LEU A 438      -5.179  -8.106  18.269  1.00101.79           C\\nANISOU 3098  CB  LEU A 438    14093  15526   9057  -5410   2445   2676       C\\nATOM   3099  N   LYS A 439      -7.108  -5.501  18.923  1.00104.77           N\\nANISOU 3099  N   LYS A 439    12553  17573   9684  -5064   3242   1817       N\\nATOM   3100  CA  LYS A 439      -8.295  -4.960  19.574  1.00111.86           C\\nANISOU 3100  CA  LYS A 439    12728  19296  10480  -5232   3763   1648       C\\nATOM   3101  C   LYS A 439      -9.200  -4.234  18.588  1.00113.57           C\\nANISOU 3101  C   LYS A 439    12089  19730  11334  -5165   3740   1359       C\\nATOM   3102  O   LYS A 439     -10.419  -4.192  18.788  1.00116.22           O\\nANISOU 3102  O   LYS A 439    11788  20658  11710  -5514   4113   1349       O\\nATOM   3103  CB  LYS A 439      -7.894  -4.019  20.711  1.00111.35           C\\nANISOU 3103  CB  LYS A 439    12602  19665  10042  -4703   3997   1288       C\\nATOM   3104  N   ILE A 440      -8.629  -3.664  17.526  1.00111.11           N\\nANISOU 3104  N   ILE A 440    11741  18958  11519  -4713   3295   1139       N\\nATOM   3105  CA  ILE A 440      -9.451  -3.036  16.502  1.00110.51           C\\nANISOU 3105  CA  ILE A 440    10923  19028  12037  -4650   3192    931       C\\nATOM   3106  C   ILE A 440     -10.182  -4.088  15.675  1.00112.85           C\\nANISOU 3106  C   ILE A 440    11191  19185  12503  -5352   3077   1285       C\\nATOM   3107  O   ILE A 440     -11.326  -3.874  15.259  1.00112.91           O\\nANISOU 3107  O   ILE A 440    10465  19613  12823  -5584   3184   1219       O\\nATOM   3108  CB  ILE A 440      -8.581  -2.115  15.629  1.00104.69           C\\nANISOU 3108  CB  ILE A 440    10219  17834  11725  -3988   2753    640       C\\nATOM   3109  CG1 ILE A 440      -7.927  -1.040  16.500  1.00107.61           C\\nANISOU 3109  CG1 ILE A 440    10580  18352  11953  -3351   2868    257       C\\nATOM   3110  CG2 ILE A 440      -9.411  -1.469  14.537  1.00101.39           C\\nANISOU 3110  CG2 ILE A 440     9088  17539  11896  -3905   2594    477       C\\nATOM   3111  CD1 ILE A 440      -7.131  -0.015  15.728  1.00100.57           C\\nANISOU 3111  CD1 ILE A 440     9658  17052  11502  -2734   2483    -35       C\\nATOM   3112  N   LEU A 441      -9.554  -5.245  15.440  1.00112.02           N\\nANISOU 3112  N   LEU A 441    11866  18490  12207  -5698   2844   1648       N\\nATOM   3113  CA  LEU A 441     -10.167  -6.342  14.697  1.00113.38           C\\nANISOU 3113  CA  LEU A 441    12136  18432  12510  -6402   2704   1969       C\\nATOM   3114  C   LEU A 441     -10.959  -7.287  15.593  1.00125.26           C\\nANISOU 3114  C   LEU A 441    13779  20090  13724  -6864   2989   2236       C\\nATOM   3115  O   LEU A 441     -11.000  -8.499  15.335  1.00130.59           O\\nANISOU 3115  O   LEU A 441    14979  20276  14364  -7284   2800   2536       O\\nATOM   3116  CB  LEU A 441      -9.096  -7.115  13.924  1.00105.56           C\\nANISOU 3116  CB  LEU A 441    11981  16582  11546  -6372   2234   2137       C\\nATOM   3117  CG  LEU A 441      -8.272  -6.304  12.915  1.00100.01           C\\nANISOU 3117  CG  LEU A 441    11276  15521  11203  -5710   1825   1833       C\\nATOM   3118  CD1 LEU A 441      -7.049  -7.083  12.435  1.00 92.92           C\\nANISOU 3118  CD1 LEU A 441    11249  13839  10218  -5600   1460   1975       C\\nATOM   3119  CD2 LEU A 441      -9.133  -5.880  11.735  1.00101.27           C\\nANISOU 3119  CD2 LEU A 441    10791  15843  11843  -5803   1635   1687       C\\nATOM   3120  N   HIS A 442     -11.587  -6.766  16.640  1.00118.20           N\\nANISOU 3120  N   HIS A 442    12431  19851  12628  -6779   3439   2114       N\\nATOM   3121  CA  HIS A 442     -12.365  -7.591  17.554  1.00126.48           C\\nANISOU 3121  CA  HIS A 442    13562  21110  13385  -7224   3754   2376       C\\nATOM   3122  C   HIS A 442     -13.375  -6.752  18.337  1.00131.96           C\\nANISOU 3122  C   HIS A 442    13462  22622  14057  -7071   4227   2114       C\\nATOM   3123  O   HIS A 442     -14.028  -5.864  17.785  1.00131.46           O\\nANISOU 3123  O   HIS A 442    12638  22887  14424  -6809   4221   1787       O\\nATOM   3124  CB  HIS A 442     -11.436  -8.335  18.515  1.00127.27           C\\nANISOU 3124  CB  HIS A 442    14545  20900  12913  -7295   3807   2692       C\\nCONECT    1    2\\nCONECT    2    1    5    3\\nCONECT    3    2    4    6\\nCONECT    4    3\\nCONECT    5    2\\nCONECT    6    7    3\\nCONECT    7    6   10    8\\nCONECT    8    7    9   11\\nCONECT    9    8\\nCONECT   10    7\\nCONECT   58   59   53\\nCONECT   59   58   62   60\\nCONECT   60   59   61   63\\nCONECT   61   60\\nCONECT   62   59\\nCONECT  194  195  185\\nCONECT  195  194  198  196\\nCONECT  196  195  197  199\\nCONECT  197  196\\nCONECT  198  195\\nCONECT  199  200  196\\nCONECT  200  199  203  201\\nCONECT  201  200  202  204\\nCONECT  202  201\\nCONECT  203  200\\nCONECT  451  452  444\\nCONECT  452  451  455  453\\nCONECT  453  452  454  456\\nCONECT  454  453\\nCONECT  455  452\\nCONECT  467  468  465\\nCONECT  468  467  471  469\\nCONECT  469  468  470  472\\nCONECT  470  469\\nCONECT  471  468\\nCONECT  486  487  474\\nCONECT  487  486  490  488\\nCONECT  488  487  489  491\\nCONECT  489  488\\nCONECT  490  487\\nCONECT  542 1057  541\\nCONECT  772  778  773  766\\nCONECT  773  772  776  774\\nCONECT  774  773  775\\nCONECT  775  774\\nCONECT  776  773  777\\nCONECT  777  776  778\\nCONECT  778  772  777\\nCONECT  779  780\\nCONECT  780  779  783  781\\nCONECT  781  780  782  784\\nCONECT  782  781\\nCONECT  783  780\\nCONECT  784  785  781\\nCONECT  785  784  788  786\\nCONECT  786  785  787  789\\nCONECT  787  786\\nCONECT  788  785\\nCONECT  801  802  791\\nCONECT  802  801  805  803\\nCONECT  803  802  804  806\\nCONECT  804  803\\nCONECT  805  802\\nCONECT  812  813  808\\nCONECT  813  812  816  814\\nCONECT  814  813  815  817\\nCONECT  815  814\\nCONECT  816  813\\nCONECT  817  818  814\\nCONECT  818  817  821  819\\nCONECT  819  818  820  822\\nCONECT  820  819\\nCONECT  821  818\\nCONECT 1018 1019 1012\\nCONECT 1019 1018 1022 1020\\nCONECT 1020 1019 1021 1023\\nCONECT 1021 1020\\nCONECT 1022 1019\\nCONECT 1028 1029 1025\\nCONECT 1029 1028 1032 1030\\nCONECT 1030 1029 1031 1033\\nCONECT 1031 1030\\nCONECT 1032 1029\\nCONECT 1033 1034 1030\\nCONECT 1034 1033 1037 1035\\nCONECT 1035 1034 1036 1038\\nCONECT 1036 1035\\nCONECT 1037 1034\\nCONECT 1038 1039 1035\\nCONECT 1039 1038 1042 1040\\nCONECT 1040 1039 1041 1043\\nCONECT 1041 1040\\nCONECT 1042 1039\\nCONECT 1057  542 1056\\nCONECT 1282 1283 1276\\nCONECT 1283 1282 1286 1284\\nCONECT 1284 1283 1285 1289\\nCONECT 1285 1284\\nCONECT 1286 1283 1287\\nCONECT 1287 1286 1288\\nCONECT 1288 1287\\nCONECT 1332 1333 1326\\nCONECT 1333 1332 1336 1334\\nCONECT 1334 1333 1335 1337\\nCONECT 1335 1334\\nCONECT 1336 1333\\nCONECT 1337 1338 1334\\nCONECT 1338 1337 1341 1339\\nCONECT 1339 1338 1340 1342\\nCONECT 1340 1339\\nCONECT 1341 1338\\nCONECT 1364 1365 1355\\nCONECT 1365 1364 1368 1366\\nCONECT 1366 1365 1367 1369\\nCONECT 1367 1366\\nCONECT 1368 1365\\nCONECT 1369 1370 1366\\nCONECT 1370 1369 1373 1371\\nCONECT 1371 1370 1372 1374\\nCONECT 1372 1371\\nCONECT 1373 1370\\nCONECT 1493 1494 1487\\nCONECT 1494 1493 1497 1495\\nCONECT 1495 1494 1496 1498\\nCONECT 1496 1495\\nCONECT 1497 1494\\nCONECT 1518 1519 1508\\nCONECT 1519 1518 1522 1520\\nCONECT 1520 1519 1521 1523\\nCONECT 1521 1520\\nCONECT 1522 1519\\nCONECT 1538 1539 1533\\nCONECT 1539 1538 1542 1540\\nCONECT 1540 1539 1541 1543\\nCONECT 1541 1540\\nCONECT 1542 1539\\nCONECT 1612 1613 1604\\nCONECT 1613 1612 1616 1614\\nCONECT 1614 1613 1615 1617\\nCONECT 1615 1614\\nCONECT 1616 1613\\nCONECT 1617 1618 1614\\nCONECT 1618 1617 1621 1619\\nCONECT 1619 1618 1620 1622\\nCONECT 1620 1619\\nCONECT 1621 1618\\nCONECT 1629 1630 1624\\nCONECT 1630 1629 1633 1631\\nCONECT 1631 1630 1632 1634\\nCONECT 1632 1631\\nCONECT 1633 1630\\nCONECT 1634 1635 1631\\nCONECT 1635 1634 1638 1636\\nCONECT 1636 1635 1637 1639\\nCONECT 1637 1636\\nCONECT 1638 1635\\nCONECT 1646 1647 1641\\nCONECT 1647 1646 1650 1648\\nCONECT 1648 1647 1649 1651\\nCONECT 1649 1648\\nCONECT 1650 1647\\nCONECT 1659 1660 1653\\nCONECT 1660 1659 1663 1661\\nCONECT 1661 1660 1662 1664\\nCONECT 1662 1661\\nCONECT 1663 1660\\nCONECT 1683 1684 1676\\nCONECT 1684 1683 1687 1685\\nCONECT 1685 1684 1686 1688\\nCONECT 1686 1685\\nCONECT 1687 1684\\nCONECT 1688 1689 1685\\nCONECT 1689 1688 1692 1690\\nCONECT 1690 1689 1691 1693\\nCONECT 1691 1690\\nCONECT 1692 1689\\nCONECT 1709 1710 1703\\nCONECT 1710 1709 1713 1711\\nCONECT 1711 1710 1712 1714\\nCONECT 1712 1711\\nCONECT 1713 1710\\nCONECT 1719 1720 1716\\nCONECT 1720 1719 1723 1721\\nCONECT 1721 1720 1722 1724\\nCONECT 1722 1721\\nCONECT 1723 1720\\nCONECT 1739 1740 1730\\nCONECT 1740 1739 1743 1741\\nCONECT 1741 1740 1742 1744\\nCONECT 1742 1741\\nCONECT 1743 1740\\nCONECT 1744 1745 1741\\nCONECT 1745 1744 1748 1746\\nCONECT 1746 1745 1747 1749\\nCONECT 1747 1746\\nCONECT 1748 1745\\nCONECT 1749 1750 1746\\nCONECT 1750 1749 1753 1751\\nCONECT 1751 1750 1752 1754\\nCONECT 1752 1751\\nCONECT 1753 1750\\nCONECT 1758 1759 1756\\nCONECT 1759 1758 1762 1760\\nCONECT 1760 1759 1761 1763\\nCONECT 1761 1760\\nCONECT 1762 1759\\nCONECT 1778 1779 1773\\nCONECT 1779 1778 1782 1780\\nCONECT 1780 1779 1781 1783\\nCONECT 1781 1780\\nCONECT 1782 1779\\nCONECT 1814 1815 1807\\nCONECT 1815 1814 1818 1816\\nCONECT 1816 1815 1817 1819\\nCONECT 1817 1816\\nCONECT 1818 1815\\nCONECT 1926 1927 1920\\nCONECT 1927 1926 1930 1928\\nCONECT 1928 1927 1929 1931\\nCONECT 1929 1928\\nCONECT 1930 1927\\nCONECT 1944 1945 1941\\nCONECT 1945 1944 1948 1946\\nCONECT 1946 1945 1947 1949\\nCONECT 1947 1946\\nCONECT 1948 1945\\nCONECT 1957 1958 1951\\nCONECT 1958 1957 1961 1959\\nCONECT 1959 1958 1960 1962\\nCONECT 1960 1959\\nCONECT 1961 1958\\nCONECT 2187 2188 2182\\nCONECT 2188 2187 2191 2189\\nCONECT 2189 2188 2190 2192\\nCONECT 2190 2189\\nCONECT 2191 2188\\nCONECT 2285 2286 2273\\nCONECT 2286 2285 2289 2287\\nCONECT 2287 2286 2288 2290\\nCONECT 2288 2287\\nCONECT 2289 2286\\nCONECT 2309 2310 2306\\nCONECT 2310 2309 2313 2311\\nCONECT 2311 2310 2312 2314\\nCONECT 2312 2311\\nCONECT 2313 2310\\nCONECT 2335 2336 2332\\nCONECT 2336 2335 2339 2337\\nCONECT 2337 2336 2338 2340\\nCONECT 2338 2337\\nCONECT 2339 2336\\nCONECT 2346 2347 2342\\nCONECT 2347 2346 2350 2348\\nCONECT 2348 2347 2349 2351\\nCONECT 2349 2348\\nCONECT 2350 2347\\nCONECT 2385 2386 2379\\nCONECT 2386 2385 2389 2387\\nCONECT 2387 2386 2388 2390\\nCONECT 2388 2387\\nCONECT 2389 2386\\nCONECT 2428 2429 2425\\nCONECT 2429 2428 2432 2430\\nCONECT 2430 2429 2431 2433\\nCONECT 2431 2430\\nCONECT 2432 2429\\nCONECT 2506 2507 2504\\nCONECT 2507 2506 2510 2508\\nCONECT 2508 2507 2509 2511\\nCONECT 2509 2508\\nCONECT 2510 2507\\nCONECT 2538 2539 2535\\nCONECT 2539 2538 2542 2540\\nCONECT 2540 2539 2541\\nCONECT 2541 2540\\nCONECT 2542 2539 2543\\nCONECT 2543 2542 2544 2545\\nCONECT 2544 2543 2546\\nCONECT 2545 2543 2547\\nCONECT 2546 2544 2548\\nCONECT 2547 2545 2548\\nCONECT 2548 2546 2547 2549\\nCONECT 2549 2548\\nCONECT 2550 2551\\nCONECT 2551 2550 2554 2552\\nCONECT 2552 2551 2553 2555\\nCONECT 2553 2552\\nCONECT 2554 2551\\nCONECT 2555 2556 2552\\nCONECT 2556 2555 2559 2557\\nCONECT 2557 2556 2558 2560\\nCONECT 2558 2557\\nCONECT 2559 2556\\nCONECT 2560 2561 2557\\nCONECT 2561 2560 2564 2562\\nCONECT 2562 2561 2563 2565\\nCONECT 2563 2562\\nCONECT 2564 2561\\nCONECT 2565 2566 2562\\nCONECT 2566 2565 2569 2567\\nCONECT 2567 2566 2568 2570\\nCONECT 2568 2567\\nCONECT 2569 2566\\nCONECT 2579 2580 2572\\nCONECT 2580 2579 2583 2581\\nCONECT 2581 2580 2582 2584\\nCONECT 2582 2581\\nCONECT 2583 2580\\nCONECT 2584 2585 2581\\nCONECT 2585 2584 2588 2586\\nCONECT 2586 2585 2587 2589\\nCONECT 2587 2586\\nCONECT 2588 2585\\nCONECT 2768 2769 2760\\nCONECT 2769 2768 2772 2770\\nCONECT 2770 2769 2771 2773\\nCONECT 2771 2770\\nCONECT 2772 2769\\nCONECT 2797 2798 2791\\nCONECT 2798 2797 2801 2799\\nCONECT 2799 2798 2800 2802\\nCONECT 2800 2799\\nCONECT 2801 2798\\nCONECT 2807 2818 2806\\nCONECT 2808 2809 2804\\nCONECT 2809 2808 2812 2810\\nCONECT 2810 2809 2811 2813\\nCONECT 2811 2810\\nCONECT 2812 2809\\nCONECT 2818 2807 2817\\nCONECT 2849 2850 2844\\nCONECT 2850 2849 2853 2851\\nCONECT 2851 2850 2852 2854\\nCONECT 2852 2851\\nCONECT 2853 2850\\nCONECT 2854 2855 2851\\nCONECT 2855 2854 2858 2856\\nCONECT 2856 2855 2857 2859\\nCONECT 2857 2856\\nCONECT 2858 2855\\nCONECT 3047 3048 3041\\nCONECT 3048 3047 3051 3049\\nCONECT 3049 3048 3050 3052\\nCONECT 3050 3049\\nCONECT 3051 3048\\nCONECT 3052 3053 3049\\nCONECT 3053 3052 3056 3054\\nCONECT 3054 3053 3055 3057\\nCONECT 3055 3054\\nCONECT 3056 3053\\nCONECT 3068 3069 3059\\nCONECT 3069 3068 3072 3070\\nCONECT 3070 3069 3071 3073\\nCONECT 3071 3070\\nCONECT 3072 3069\\nCONECT 3073 3074 3070\\nCONECT 3074 3073 3077 3075\\nCONECT 3075 3074 3076 3078\\nCONECT 3076 3075\\nCONECT 3077 3074\\nCONECT 3094 3095 3085\\nCONECT 3095 3094 3098 3096\\nCONECT 3096 3095 3097 3099\\nCONECT 3097 3096\\nCONECT 3098 3095\\nCONECT 3099 3100 3096\\nCONECT 3100 3099 3103 3101\\nCONECT 3101 3100 3102 3104\\nCONECT 3102 3101\\nCONECT 3103 3100\\nCONECT 3120 3121 3114\\nCONECT 3121 3120 3124 3122\\nCONECT 3122 3121 3123\\nCONECT 3123 3122\\nCONECT 3124 3121\\nEND\\n\",\"pdb\");\n\tviewer_1716802976377794.setStyle({\"model\": 0},{\"cartoon\": {}});\n\tviewer_1716802976377794.addSurface(null,{\"opacity\": 1, \"color\": \"lightgray\"});\n\tviewer_1716802976377794.addModels(\"HETATM    1 C18  UNL   1        7.832   6.691 -12.018  1.00  0.00           C  \\nHETATM    2 C19  UNL   1        9.368   6.654 -12.071  1.00  0.00           C  \\nHETATM    3 C20  UNL   1        9.972   5.608 -13.005  1.00  0.00           C  \\nHETATM    4 C21  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-4.383  1.00  0.00           N1+\\nHETATM   29 C43  UNL   1       11.722   9.234  -3.773  1.00  0.00           C  \\nHETATM   30 C44  UNL   1       11.299   7.895  -4.372  1.00  0.00           C  \\nHETATM   31 O4   UNL   1       12.016   8.010 -10.855  1.00  0.00           O  \\nCONECT    1    2\\nCONECT    2    1    3   19\\nCONECT    3    2    4    4    8\\nCONECT   19    2   20\\nCONECT    4    3    3    5\\nCONECT    8    3    7    7\\nCONECT    5    4    6    6\\nCONECT    6    5    5    7   11\\nCONECT    7    6    8    8    9\\nCONECT   11    6   10   10\\nCONECT    9    7   10   12\\nCONECT   10    9   11   11\\nCONECT   12    9   13\\nCONECT   13   12   14   18\\nCONECT   14   13   15\\nCONECT   18   13   17\\nCONECT   15   14   16\\nCONECT   16   15   17\\nCONECT   17   16   18\\nCONECT   20   19   21   31\\nCONECT   21   20   22   22   26\\nCONECT   31   20\\nCONECT   22   21   21   23\\nCONECT   26   21   25   25\\nCONECT   23   22   24   24\\nCONECT   24   23   23   25   30\\nCONECT   25   24   26   26   27\\nCONECT   30   24   29\\nCONECT   27   25   28\\nCONECT   28   27   29\\nCONECT   29   28   30\\nEND\",\"pdb\");\n\tviewer_1716802976377794.setStyle({\"model\": 1},{\"stick\": {\"color\": \"cyan\"}});\n\tviewer_1716802976377794.zoomTo();\nviewer_1716802976377794.render();\n});\n</script>",
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       "        <p id=\"3dmolwarning_1716802976377794\" style=\"background-color:#ffcccc;color:black\">You appear to be running in JupyterLab (or JavaScript failed to load for some other reason).  You need to install the 3dmol extension: <br>\n",
       "        <tt>jupyter labextension install jupyterlab_3dmol</tt></p>\n",
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       "viewer_1716802976377794 = $3Dmol.createViewer(document.getElementById(\"3dmolviewer_1716802976377794\"),{backgroundColor:\"white\"});\n",
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       "\tviewer_1716802976377794.addModels(\"HEADER    MEMBRANE PROTEIN                        02-MAR-18   6CM4              \\nTITLE     STRUCTURE OF THE D2 DOPAMINE RECEPTOR BOUND TO THE ATYPICAL           \\nTITLE    2 ANTIPSYCHOTIC DRUG RISPERIDONE                                       \\nCOMPND    MOL_ID: 1;                                                            \\nCOMPND   2 MOLECULE: D(2) DOPAMINE RECEPTOR, ENDOLYSIN CHIMERA;                 \\nCOMPND   3 CHAIN: A;                                                            \\nCOMPND   4 SYNONYM: DOPAMINE D2 RECEPTOR, LYSIS PROTEIN, LYSOZYME, MURAMIDASE,  \\nCOMPND   5 DOPAMINE D2 RECEPTOR;                                                \\nCOMPND   6 EC: 3.2.1.17;                                                        \\nCOMPND   7 ENGINEERED: YES                                                      \\nSOURCE    MOL_ID: 1;                                                            \\nSOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, ENTEROBACTERIA PHAGE T4;          \\nSOURCE   3 ORGANISM_COMMON: HUMAN, BACTERIOPHAGE T4;                            \\nSOURCE   4 ORGANISM_TAXID: 9606, 10665;                                         \\nSOURCE   5 GENE: DRD2, E, T4TP126;                                              \\nSOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            \\nSOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             \\nSOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;                                       \\nSOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          \\nSOURCE  10 EXPRESSION_SYSTEM_PLASMID: PFASTBAC1-HM                              \\nKEYWDS    GPCR, D2, DOPAMINE RECEPTOR, ANTIPSYCHOTIC, RISPERIDONE, MEMBRANE     \\nKEYWDS   2 PROTEIN                                                              \\nEXPDTA    X-RAY DIFFRACTION                                                     \\nAUTHOR    S.WANG,T.CHE,A.LEVIT,B.K.SHOICHET,D.WACKER,B.L.ROTH                   \\nREVDAT   6   04-OCT-23 6CM4    1       REMARK                                   \\nREVDAT   5   27-NOV-19 6CM4    1       REMARK                                   \\nREVDAT   4   20-FEB-19 6CM4    1       REMARK                                   \\nREVDAT   3   11-APR-18 6CM4    1       DBREF                                    \\nREVDAT   2   21-MAR-18 6CM4    1       JRNL                                     \\nREVDAT   1   14-MAR-18 6CM4    0                                                \\nSPRSDE     14-MAR-18 6CM4      6C38                                             \\nJRNL        AUTH   S.WANG,T.CHE,A.LEVIT,B.K.SHOICHET,D.WACKER,B.L.ROTH          \\nJRNL        TITL   STRUCTURE OF THE D2 DOPAMINE RECEPTOR BOUND TO THE ATYPICAL  \\nJRNL        TITL 2 ANTIPSYCHOTIC DRUG RISPERIDONE.                              \\nJRNL        REF    NATURE                        V. 555   269 2018              \\nJRNL        REFN                   ESSN 1476-4687                               \\nJRNL        PMID   29466326                                                     \\nJRNL        DOI    10.1038/NATURE25758                                          \\nREMARK   2                                                                      \\nREMARK   2 RESOLUTION.    2.87 ANGSTROMS.                                       \\nREMARK   3                                                                      \\nREMARK   3 REFINEMENT.                                                          \\nREMARK   3   PROGRAM     : PHENIX (1.12_2829: ???)                              \\nREMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            \\nREMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           \\nREMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            \\nREMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              \\nREMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               \\nREMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           \\nREMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  \\nREMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  \\nREMARK   3                                                                      \\nREMARK   3    REFINEMENT TARGET : ML                                            \\nREMARK   3                                                                      \\nREMARK   3  DATA USED IN REFINEMENT.                                            \\nREMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.87                           \\nREMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.55                          \\nREMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.360                          \\nREMARK   3   COMPLETENESS FOR RANGE        (%) : 95.2                           \\nREMARK   3   NUMBER OF REFLECTIONS             : 12814                          \\nREMARK   3                                                                      \\nREMARK   3  FIT TO DATA USED IN REFINEMENT.                                     \\nREMARK   3   R VALUE     (WORKING + TEST SET) : 0.227                           \\nREMARK   3   R VALUE            (WORKING SET) : 0.226                           \\nREMARK   3   FREE R VALUE                     : 0.249                           \\nREMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.850                           \\nREMARK   3   FREE R VALUE TEST SET COUNT      : 622                             \\nREMARK   3                                                                      \\nREMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           \\nREMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        \\nREMARK   3     1 29.5504 -  4.5475    0.98     3287   157  0.2103 0.2188        \\nREMARK   3     2  4.5475 -  3.6116    0.99     3151   170  0.2090 0.2511        \\nREMARK   3     3  3.6116 -  3.1556    0.99     3111   162  0.2730 0.3034        \\nREMARK   3     4  3.1556 -  2.8674    0.84     2643   133  0.3166 0.3214        \\nREMARK   3                                                                      \\nREMARK   3  BULK SOLVENT MODELLING.                                             \\nREMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       \\nREMARK   3   SOLVENT RADIUS     : 1.11                                          \\nREMARK   3   SHRINKAGE RADIUS   : 0.90                                          \\nREMARK   3   K_SOL              : NULL                                          \\nREMARK   3   B_SOL              : NULL                                          \\nREMARK   3                                                                      \\nREMARK   3  ERROR ESTIMATES.                                                    \\nREMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.390            \\nREMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.640           \\nREMARK   3                                                                      \\nREMARK   3  B VALUES.                                                           \\nREMARK   3   FROM WILSON PLOT           (A**2) : NULL                           \\nREMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           \\nREMARK   3   OVERALL ANISOTROPIC B VALUE.                                       \\nREMARK   3    B11 (A**2) : NULL                                                 \\nREMARK   3    B22 (A**2) : NULL                                                 \\nREMARK   3    B33 (A**2) : NULL                                                 \\nREMARK   3    B12 (A**2) : NULL                                                 \\nREMARK   3    B13 (A**2) : NULL                                                 \\nREMARK   3    B23 (A**2) : NULL                                                 \\nREMARK   3                                                                      \\nREMARK   3  TWINNING INFORMATION.                                               \\nREMARK   3   FRACTION: NULL                                                     \\nREMARK   3   OPERATOR: NULL                                                     \\nREMARK   3                                                                      \\nREMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       \\nREMARK   3                 RMSD          COUNT                                  \\nREMARK   3   BOND      :  0.003           3283                                  \\nREMARK   3   ANGLE     :  0.516           4483                                  \\nREMARK   3   CHIRALITY :  0.037            544                                  \\nREMARK   3   PLANARITY :  0.003            549                                  \\nREMARK   3   DIHEDRAL  : 10.862           1928                                  \\nREMARK   3                                                                      \\nREMARK   3  TLS DETAILS                                                         \\nREMARK   3   NUMBER OF TLS GROUPS  : 3                                          \\nREMARK   3   TLS GROUP : 1                                                      \\nREMARK   3    SELECTION: CHAIN 'A' AND (RESID 36 THROUGH 222 )                  \\nREMARK   3    ORIGIN FOR THE GROUP (A):   7.6595   9.9883   1.8227              \\nREMARK   3    T TENSOR                                                          \\nREMARK   3      T11:   0.3906 T22:   0.3948                                     \\nREMARK   3      T33:   0.4097 T12:  -0.0409                                     \\nREMARK   3      T13:   0.0298 T23:   0.0323                                     \\nREMARK   3    L TENSOR                                                          \\nREMARK   3      L11:   4.8704 L22:   2.9655                                     \\nREMARK   3      L33:   4.7317 L12:   0.7811                                     \\nREMARK   3      L13:   2.8181 L23:   1.4507                                     \\nREMARK   3    S TENSOR                                                          \\nREMARK   3      S11:   0.0593 S12:  -0.1051 S13:   0.0093                       \\nREMARK   3      S21:   0.1418 S22:  -0.1464 S23:   0.1356                       \\nREMARK   3      S31:   0.4299 S32:  -0.3974 S33:  -0.0137                       \\nREMARK   3   TLS GROUP : 2                                                      \\nREMARK   3    SELECTION: CHAIN 'A' AND (RESID 1002 THROUGH 1161 )               \\nREMARK   3    ORIGIN FOR THE GROUP (A):  32.7700  -7.7446  36.3658              \\nREMARK   3    T TENSOR                                                          \\nREMARK   3      T11:   0.6968 T22:   0.5198                                     \\nREMARK   3      T33:   0.5000 T12:   0.0363                                     \\nREMARK   3      T13:   0.0872 T23:   0.1084                                     \\nREMARK   3    L TENSOR                                                          \\nREMARK   3      L11:   6.6697 L22:   6.8821                                     \\nREMARK   3      L33:   6.4568 L12:   1.6541                                     \\nREMARK   3      L13:   1.9941 L23:   1.4205                                     \\nREMARK   3    S TENSOR                                                          \\nREMARK   3      S11:  -0.2551 S12:   0.1211 S13:  -0.2547                       \\nREMARK   3      S21:  -0.3908 S22:  -0.0566 S23:  -0.4642                       \\nREMARK   3      S31:   0.4711 S32:   0.2364 S33:   0.3147                       \\nREMARK   3   TLS GROUP : 3                                                      \\nREMARK   3    SELECTION: CHAIN 'A' AND (RESID 384 THROUGH 460 )                 \\nREMARK   3    ORIGIN FOR THE GROUP (A):   9.8885  -1.6530  -1.3224              \\nREMARK   3    T TENSOR                                                          \\nREMARK   3      T11:   0.6392 T22:   0.3770                                     \\nREMARK   3      T33:   0.5276 T12:   0.0087                                     \\nREMARK   3      T13:  -0.0908 T23:   0.0140                                     \\nREMARK   3    L TENSOR                                                          \\nREMARK   3      L11:   6.0244 L22:   5.3813                                     \\nREMARK   3      L33:   6.7255 L12:   0.3578                                     \\nREMARK   3      L13:   1.1698 L23:   0.5209                                     \\nREMARK   3    S TENSOR                                                          \\nREMARK   3      S11:  -0.0948 S12:   0.3307 S13:   0.0832                       \\nREMARK   3      S21:  -0.4022 S22:   0.2772 S23:  -0.0581                       \\nREMARK   3      S31:   1.2902 S32:  -0.0417 S33:  -0.2847                       \\nREMARK   3                                                                      \\nREMARK   3  NCS DETAILS                                                         \\nREMARK   3   NUMBER OF NCS GROUPS : NULL                                        \\nREMARK   3                                                                      \\nREMARK   3  OTHER REFINEMENT REMARKS: NULL                                      \\nREMARK   4                                                                      \\nREMARK   4 6CM4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         \\nREMARK 100                                                                      \\nREMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-MAR-18.                  \\nREMARK 100 THE DEPOSITION ID IS D_1000232947.                                   \\nREMARK 200                                                                      \\nREMARK 200 EXPERIMENTAL DETAILS                                                 \\nREMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  \\nREMARK 200  DATE OF DATA COLLECTION        : 13-AUG-17                          \\nREMARK 200  TEMPERATURE           (KELVIN) : 100                                \\nREMARK 200  PH                             : NULL                               \\nREMARK 200  NUMBER OF CRYSTALS USED        : 1                                  \\nREMARK 200                                                                      \\nREMARK 200  SYNCHROTRON              (Y/N) : Y                                  \\nREMARK 200  RADIATION SOURCE               : APS                                \\nREMARK 200  BEAMLINE                       : 23-ID-B                            \\nREMARK 200  X-RAY GENERATOR MODEL          : NULL                               \\nREMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  \\nREMARK 200  WAVELENGTH OR RANGE        (A) : 1.033                              \\nREMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL CRYO-COOLED         \\nREMARK 200                                   SI(111)                            \\nREMARK 200  OPTICS                         : NULL                               \\nREMARK 200                                                                      \\nREMARK 200  DETECTOR TYPE                  : PIXEL                              \\nREMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER X 16M                \\nREMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000                           \\nREMARK 200  DATA SCALING SOFTWARE          : HKL-3000                           \\nREMARK 200                                                                      \\nREMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 12826                              \\nREMARK 200  RESOLUTION RANGE HIGH      (A) : 2.867                              \\nREMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             \\nREMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               \\nREMARK 200                                                                      \\nREMARK 200 OVERALL.                                                             \\nREMARK 200  COMPLETENESS FOR RANGE     (%) : 97.3                               \\nREMARK 200  DATA REDUNDANCY                : 5.500                              \\nREMARK 200  R MERGE                    (I) : 0.13400                            \\nREMARK 200  R SYM                      (I) : NULL                               \\nREMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.2000                            \\nREMARK 200                                                                      \\nREMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     \\nREMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90                     \\nREMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.99                     \\nREMARK 200  COMPLETENESS FOR SHELL     (%) : 86.9                               \\nREMARK 200  DATA REDUNDANCY IN SHELL       : 2.50                               \\nREMARK 200  R MERGE FOR SHELL          (I) : 0.73800                            \\nREMARK 200  R SYM FOR SHELL            (I) : NULL                               \\nREMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.000                              \\nREMARK 200                                                                      \\nREMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              \\nREMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        \\nREMARK 200 SOFTWARE USED: PHASER                                                \\nREMARK 200 STARTING MODEL: PDB ENTRIES 5WIU & 2RH1                              \\nREMARK 200                                                                      \\nREMARK 200 REMARK: NULL                                                         \\nREMARK 280                                                                      \\nREMARK 280 CRYSTAL                                                              \\nREMARK 280 SOLVENT CONTENT, VS   (%): 57.13                                     \\nREMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.87                     \\nREMARK 280                                                                      \\nREMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM TRIS-HCL, PH 7.8, 230 MM          \\nREMARK 280  LITHIUM NITRATE, 25% PEG400, 4% 1,3-BUTANEDIOL, LIPIDIC CUBIC       \\nREMARK 280  PHASE, TEMPERATURE 293K                                             \\nREMARK 290                                                                      \\nREMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            \\nREMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       \\nREMARK 290                                                                      \\nREMARK 290      SYMOP   SYMMETRY                                                \\nREMARK 290     NNNMMM   OPERATOR                                                \\nREMARK 290       1555   X,Y,Z                                                   \\nREMARK 290       2555   -X+1/2,-Y,Z+1/2                                         \\nREMARK 290       3555   -X,Y+1/2,-Z+1/2                                         \\nREMARK 290       4555   X+1/2,-Y+1/2,-Z                                         \\nREMARK 290                                                                      \\nREMARK 290     WHERE NNN -> OPERATOR NUMBER                                     \\nREMARK 290           MMM -> TRANSLATION VECTOR                                  \\nREMARK 290                                                                      \\nREMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            \\nREMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             \\nREMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                \\nREMARK 290 RELATED MOLECULES.                                                   \\nREMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            \\nREMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            \\nREMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            \\nREMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       25.48950            \\nREMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            \\nREMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       75.65350            \\nREMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            \\nREMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       36.26150            \\nREMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       75.65350            \\nREMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       25.48950            \\nREMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       36.26150            \\nREMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            \\nREMARK 290                                                                      \\nREMARK 290 REMARK: NULL                                                         \\nREMARK 300                                                                      \\nREMARK 300 BIOMOLECULE: 1                                                       \\nREMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                \\nREMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  \\nREMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               \\nREMARK 300 BURIED SURFACE AREA.                                                 \\nREMARK 350                                                                      \\nREMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           \\nREMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                \\nREMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          \\nREMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          \\nREMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               \\nREMARK 350                                                                      \\nREMARK 350 BIOMOLECULE: 1                                                       \\nREMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         \\nREMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  \\nREMARK 350 SOFTWARE USED: PISA                                                  \\nREMARK 350 TOTAL BURIED SURFACE AREA: 1850 ANGSTROM**2                          \\nREMARK 350 SURFACE AREA OF THE COMPLEX: 20460 ANGSTROM**2                       \\nREMARK 350 CHANGE IN SOLVENT FREE ENERGY: 12.0 KCAL/MOL                         \\nREMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     \\nREMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            \\nREMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            \\nREMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            \\nREMARK 465                                                                      \\nREMARK 465 MISSING RESIDUES                                                     \\nREMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       \\nREMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               \\nREMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                \\nREMARK 465                                                                      \\nREMARK 465   M RES C SSSEQI                                                     \\nREMARK 465     MET A   140                                                      \\nREMARK 465     LEU A   141                                                      \\nREMARK 465     TYR A   142                                                      \\nREMARK 465     ASN A   143                                                      \\nREMARK 465     LYS A   362                                                      \\nREMARK 465     LEU A   363                                                      \\nREMARK 465     CYS A   443                                                      \\nREMARK 470                                                                      \\nREMARK 470 MISSING ATOM                                                         \\nREMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           \\nREMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          \\nREMARK 470 I=INSERTION CODE):                                                   \\nREMARK 470   M RES CSSEQI  ATOMS                                                \\nREMARK 470     ASN A  35    CG   OD1  ND2                                       \\nREMARK 470     TYR A  36    CG   CD1  CD2  CE1  CE2  CZ   OH                    \\nREMARK 470     LEU A  43    CG   CD1  CD2                                       \\nREMARK 470     GLU A  62    CG   CD   OE1  OE2                                  \\nREMARK 470     LYS A  63    CG   CD   CE   NZ                                   \\nREMARK 470     VAL A  96    CG1  CG2                                            \\nREMARK 470     GLU A  99    CG   CD   OE1  OE2                                  \\nREMARK 470     LYS A 101    CG   CD   CE   NZ                                   \\nREMARK 470     THR A 144    OG1  CG2                                            \\nREMARK 470     ARG A 145    CG   CD   NE   CZ   NH1  NH2                        \\nREMARK 470     SER A 147    OG                                                  \\nREMARK 470     LYS A 149    CG   CD   CE   NZ                                   \\nREMARK 470     ARG A 150    CG   CD   NE   CZ   NH1  NH2                        \\nREMARK 470     ASN A 176    CG   OD1  ND2                                       \\nREMARK 470     ASP A 178    CG   OD1  OD2                                       \\nREMARK 470     GLN A 179    CG   CD   OE1  NE2                                  \\nREMARK 470     ASN A 180    CG   OD1  ND2                                       \\nREMARK 470     LYS A 211    CE   NZ                                             \\nREMARK 470     ARG A 217    CG   CD   NE   CZ   NH1  NH2                        \\nREMARK 470     ARG A 218    CG   CD   NE   CZ   NH1  NH2                        \\nREMARK 470     LYS A 221    CG   CD   CE   NZ                                   \\nREMARK 470     ARG A 222    CG   CD   NE   CZ   NH1  NH2                        \\nREMARK 470     LYS A1016    CG   CD   CE   NZ                                   \\nREMARK 470     LYS A1019    CG   CD   CE   NZ                                   \\nREMARK 470     GLU A1022    CG   CD   OE1  OE2                                  \\nREMARK 470     LEU A1032    CG   CD1  CD2                                       \\nREMARK 470     LEU A1033    CG   CD1  CD2                                       \\nREMARK 470     LYS A1035    CG   CD   CE   NZ                                   \\nREMARK 470     SER A1036    OG                                                  \\nREMARK 470     SER A1038    OG                                                  \\nREMARK 470     ASN A1040    CG   OD1  ND2                                       \\nREMARK 470     SER A1044    OG                                                  \\nREMARK 470     GLU A1045    CG   CD   OE1  OE2                                  \\nREMARK 470     LYS A1048    CG   CD   CE   NZ                                   \\nREMARK 470     ILE A1050    CG1  CG2  CD1                                       \\nREMARK 470     ASN A1053    CG   OD1  ND2                                       \\nREMARK 470     THR A1054    OG1  CG2                                            \\nREMARK 470     ASN A1055    CG   OD1  ND2                                       \\nREMARK 470     VAL A1057    CG1  CG2                                            \\nREMARK 470     LYS A1060    CG   CD   CE   NZ                                   \\nREMARK 470     LYS A1065    CG   CD   CE   NZ                                   \\nREMARK 470     ARG A1080    CG   CD   NE   CZ   NH1  NH2                        \\nREMARK 470     LYS A1083    CG   CD   CE   NZ                                   \\nREMARK 470     LYS A1085    CG   CD   CE   NZ                                   \\nREMARK 470     ASN A1116    CG   OD1  ND2                                       \\nREMARK 470     ASP A1127    CG   OD1  OD2                                       \\nREMARK 470     VAL A1131    CG1  CG2                                            \\nREMARK 470     LYS A1135    CG   CD   CE   NZ                                   \\nREMARK 470     ARG A1137    CG   CD   NE   CZ   NH1  NH2                        \\nREMARK 470     GLN A1141    CG   CD   OE1  NE2                                  \\nREMARK 470     LYS A1147    CG   CD   CE   NZ                                   \\nREMARK 470     THR A1157    OG1  CG2                                            \\nREMARK 470     SER A 364    OG                                                  \\nREMARK 470     GLN A 365    CG   CD   OE1  NE2                                  \\nREMARK 470     GLN A 366    CG   CD   OE1  NE2                                  \\nREMARK 470     LYS A 367    CG   CD   CE   NZ                                   \\nREMARK 470     LYS A 369    CG   CD   CE   NZ                                   \\nREMARK 470     LYS A 370    CG   CD   CE   NZ                                   \\nREMARK 470     ILE A 394    CG1  CG2  CD1                                       \\nREMARK 470     HIS A 398    CG   ND1  CD2  CE1  NE2                             \\nREMARK 470     ASP A 400    CG   OD1  OD2                                       \\nREMARK 470     VAL A 406    CG1  CG2                                            \\nREMARK 470     LEU A 407    CG   CD1  CD2                                       \\nREMARK 470     ILE A 431    CG1  CG2  CD1                                       \\nREMARK 470     GLU A 432    CG   CD   OE1  OE2                                  \\nREMARK 470     ARG A 434    CG   CD   NE   CZ   NH1  NH2                        \\nREMARK 470     LYS A 435    CG   CD   CE   NZ                                   \\nREMARK 470     LEU A 438    CG   CD1  CD2                                       \\nREMARK 470     LYS A 439    CG   CD   CE   NZ                                   \\nREMARK 470     HIS A 442    CG   ND1  CD2  CE1  NE2                             \\nREMARK 500                                                                      \\nREMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         \\nREMARK 500 SUBTOPIC: TORSION ANGLES                                             \\nREMARK 500                                                                      \\nREMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            \\nREMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               \\nREMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             \\nREMARK 500                                                                      \\nREMARK 500 STANDARD TABLE:                                                      \\nREMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    \\nREMARK 500                                                                      \\nREMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           \\nREMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            \\nREMARK 500                                                                      \\nREMARK 500  M RES CSSEQI        PSI       PHI                                   \\nREMARK 500    GLN A  66       70.23   -104.22                                   \\nREMARK 500    VAL A  87      -52.46   -121.67                                   \\nREMARK 500    PHE A 198      -60.72   -124.56                                   \\nREMARK 500    ASN A1055       17.81     58.75                                   \\nREMARK 500    PHE A1114       49.44    -89.78                                   \\nREMARK 500    ASP A 400       11.47     57.92                                   \\nREMARK 500    LEU A 441       33.98    -88.55                                   \\nREMARK 500                                                                      \\nREMARK 500 REMARK: NULL                                                         \\nREMARK 610                                                                      \\nREMARK 610 MISSING HETEROATOM                                                   \\nREMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           \\nREMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          \\nREMARK 610 I=INSERTION CODE):                                                   \\nREMARK 610   M RES C SSEQI                                                      \\nREMARK 610     OLA A 2005                                                       \\nREMARK 610     OLA A 2006                                                       \\nDBREF  6CM4 A   35   222  UNP    P14416   DRD2_HUMAN      35    222             \\nDBREF  6CM4 A 1002  1161  UNP    D9IEF7   D9IEF7_BPT4      2    161             \\nDBREF  6CM4 A  362   443  UNP    P14416   DRD2_HUMAN     362    443             \\nSEQADV 6CM4 ALA A  122  UNP  P14416    ILE   122 CONFLICT                       \\nSEQADV 6CM4 THR A 1054  UNP  D9IEF7    CYS    54 CONFLICT                       \\nSEQADV 6CM4 ALA A 1097  UNP  D9IEF7    CYS    97 CONFLICT                       \\nSEQADV 6CM4 ALA A  375  UNP  P14416    LEU   375 CONFLICT                       \\nSEQADV 6CM4 ALA A  379  UNP  P14416    LEU   379 CONFLICT                       \\nSEQRES   1 A  430  ASN TYR TYR ALA THR LEU LEU THR LEU LEU ILE ALA VAL\\nSEQRES   2 A  430  ILE VAL PHE GLY ASN VAL LEU VAL CYS MET ALA VAL SER\\nSEQRES   3 A  430  ARG GLU LYS ALA LEU GLN THR THR THR ASN TYR LEU ILE\\nSEQRES   4 A  430  VAL SER LEU ALA VAL ALA ASP LEU LEU VAL ALA THR LEU\\nSEQRES   5 A  430  VAL MET PRO TRP VAL VAL TYR LEU GLU VAL VAL GLY GLU\\nSEQRES   6 A  430  TRP LYS PHE SER ARG ILE HIS CYS ASP ILE PHE VAL THR\\nSEQRES   7 A  430  LEU ASP VAL MET MET CYS THR ALA SER ALA LEU ASN LEU\\nSEQRES   8 A  430  CYS ALA ILE SER ILE ASP ARG TYR THR ALA VAL ALA MET\\nSEQRES   9 A  430  PRO MET LEU TYR ASN THR ARG TYR SER SER LYS ARG ARG\\nSEQRES  10 A  430  VAL THR VAL MET ILE SER ILE VAL TRP VAL LEU SER PHE\\nSEQRES  11 A  430  THR ILE SER CYS PRO LEU LEU PHE GLY LEU ASN ASN ALA\\nSEQRES  12 A  430  ASP GLN ASN GLU CYS ILE ILE ALA ASN PRO ALA PHE VAL\\nSEQRES  13 A  430  VAL TYR SER SER ILE VAL SER PHE TYR VAL PRO PHE ILE\\nSEQRES  14 A  430  VAL THR LEU LEU VAL TYR ILE LYS ILE TYR ILE VAL LEU\\nSEQRES  15 A  430  ARG ARG ARG ARG LYS ARG ASN ILE PHE GLU MET LEU ARG\\nSEQRES  16 A  430  ILE ASP GLU GLY LEU ARG LEU LYS ILE TYR LYS ASP THR\\nSEQRES  17 A  430  GLU GLY TYR TYR THR ILE GLY ILE GLY HIS LEU LEU THR\\nSEQRES  18 A  430  LYS SER PRO SER LEU ASN ALA ALA LYS SER GLU LEU ASP\\nSEQRES  19 A  430  LYS ALA ILE GLY ARG ASN THR ASN GLY VAL ILE THR LYS\\nSEQRES  20 A  430  ASP GLU ALA GLU LYS LEU PHE ASN GLN ASP VAL ASP ALA\\nSEQRES  21 A  430  ALA VAL ARG GLY ILE LEU ARG ASN ALA LYS LEU LYS PRO\\nSEQRES  22 A  430  VAL TYR ASP SER LEU ASP ALA VAL ARG ARG ALA ALA LEU\\nSEQRES  23 A  430  ILE ASN MET VAL PHE GLN MET GLY GLU THR GLY VAL ALA\\nSEQRES  24 A  430  GLY PHE THR ASN SER LEU ARG MET LEU GLN GLN LYS ARG\\nSEQRES  25 A  430  TRP ASP GLU ALA ALA VAL ASN LEU ALA LYS SER ARG TRP\\nSEQRES  26 A  430  TYR ASN GLN THR PRO ASN ARG ALA LYS ARG VAL ILE THR\\nSEQRES  27 A  430  THR PHE ARG THR GLY THR TRP ASP ALA TYR LYS LEU SER\\nSEQRES  28 A  430  GLN GLN LYS GLU LYS LYS ALA THR GLN MET ALA ALA ILE\\nSEQRES  29 A  430  VAL ALA GLY VAL PHE ILE ILE CYS TRP LEU PRO PHE PHE\\nSEQRES  30 A  430  ILE THR HIS ILE LEU ASN ILE HIS CYS ASP CYS ASN ILE\\nSEQRES  31 A  430  PRO PRO VAL LEU TYR SER ALA PHE THR TRP LEU GLY TYR\\nSEQRES  32 A  430  VAL ASN SER ALA VAL ASN PRO ILE ILE TYR THR THR PHE\\nSEQRES  33 A  430  ASN ILE GLU PHE ARG LYS ALA PHE LEU LYS ILE LEU HIS\\nSEQRES  34 A  430  CYS\\nHET    8NU  A2001      30                                                       \\nHET    PEG  A2002       7                                                       \\nHET    PEG  A2003       7                                                       \\nHET    PEG  A2004       7                                                       \\nHET    OLA  A2005      13                                                       \\nHET    OLA  A2006      12                                                       \\nHET    OLA  A2007      20                                                       \\nHETNAM     8NU 3-[2-[4-(6-FLUORANYL-1,2-BENZOXAZOL-3-YL)PIPERIDIN-1-            \\nHETNAM   2 8NU  YL]ETHYL]-2-METHYL-6,7,8,9-TETRAHYDROPYRIDO[1,2-                \\nHETNAM   3 8NU  A]PYRIMIDIN-4-ONE                                               \\nHETNAM     PEG DI(HYDROXYETHYL)ETHER                                            \\nHETNAM     OLA OLEIC ACID                                                       \\nFORMUL   2  8NU    C23 H27 F N4 O2                                              \\nFORMUL   3  PEG    3(C4 H10 O3)                                                 \\nFORMUL   6  OLA    3(C18 H34 O2)                                                \\nFORMUL   9  HOH   *16(H2 O)                                                     \\nHELIX    1   1 ASN A   35  GLU A   62  1                                  28\\nHELIX    2   2 LYS A   63  GLN A   66  1                                   4\\nHELIX    3   3 THR A   67  LEU A   86  1                                  20\\nHELIX    4   4 VAL A   87  GLY A   98  1                                  12\\nHELIX    5   5 SER A  103  MET A  138  1                                  36\\nHELIX    6   6 TYR A  146  CYS A  168  1                                  23\\nHELIX    7   7 PRO A  169  ASN A  176  1                                   8\\nHELIX    8   8 CYS A  182  ASN A  186  1                                   5\\nHELIX    9   9 ALA A  188  VAL A  196  1                                   9\\nHELIX   10  10 PHE A  198  GLU A 1011  1                                  35\\nHELIX   11  11 SER A 1038  GLY A 1051  1                                  14\\nHELIX   12  12 THR A 1059  ASN A 1081  1                                  23\\nHELIX   13  13 LEU A 1084  LEU A 1091  1                                   8\\nHELIX   14  14 ASP A 1092  ALA A 1112  1                                  21\\nHELIX   15  15 PHE A 1114  GLN A 1123  1                                  10\\nHELIX   16  16 ARG A 1125  ALA A 1134  1                                  10\\nHELIX   17  17 SER A 1136  GLN A 1141  1                                   6\\nHELIX   18  18 THR A 1142  GLY A 1156  1                                  15\\nHELIX   19  19 GLU A  368  CYS A  399  1                                  32\\nHELIX   20  20 PRO A  404  ASN A  418  1                                  15\\nHELIX   21  21 VAL A  421  PHE A  429  1                                   9\\nHELIX   22  22 ASN A  430  LEU A  441  1                                  12\\nSHEET    1   1 1 ARG A1014  LYS A1019  0\\nSHEET    2   2 1 TYR A1025  GLY A1028  0\\nSHEET    3   3 1 HIS A1031  THR A1034  0\\nSSBOND   1 CYS A  107    CYS A  182                          1555   1555  2.03\\nSSBOND   2 CYS A  399    CYS A  401                          1555   1555  2.04\\nCRYST1   50.979   72.523  151.307  90.00  90.00  90.00 P 21 21 21    4          \\nORIGX1      1.000000  0.000000  0.000000        0.00000                         \\nORIGX2      0.000000  1.000000  0.000000        0.00000                         \\nORIGX3      0.000000  0.000000  1.000000        0.00000                         \\nSCALE1      0.019616  0.000000  0.000000        0.00000                         \\nSCALE2      0.000000  0.013789  0.000000        0.00000                         \\nSCALE3      0.000000  0.000000  0.006609        0.00000                         \\nATOM      1  N   ASN A  35      -5.317  -8.666 -16.658  1.00108.95           N\\nATOM      2  CA  ASN A  35      -3.999  -9.279 -16.550  1.00112.41           C\\nATOM      3  C   ASN A  35      -3.770  -9.829 -15.148  1.00103.98           C\\nATOM      4  O   ASN A  35      -4.596  -9.642 -14.253  1.00111.14           O\\nATOM      5  CB  ASN A  35      -2.903  -8.271 -16.904  1.00115.88           C\\nATOM      6  N   TYR A  36      -2.640 -10.512 -14.962  1.00122.79           N\\nANISOU    6  N   TYR A  36    17290  13079  16284  -1997  -3163  -3043       N\\nATOM      7  CA  TYR A  36      -2.284 -11.046 -13.653  1.00105.49           C\\nANISOU    7  CA  TYR A  36    15314  10451  14315  -2168  -3210  -2776       C\\nATOM      8  C   TYR A  36      -1.522 -10.036 -12.804  1.00100.38           C\\nANISOU    8  C   TYR A  36    14564  10022  13555  -2013  -2870  -2480       C\\nATOM      9  O   TYR A  36      -1.767  -9.933 -11.597  1.00 95.60           O\\nANISOU    9  O   TYR A  36    13979   9308  13038  -2297  -2774  -2120       O\\nATOM     10  CB  TYR A  36      -1.455 -12.323 -13.811  1.00 98.01           C\\nANISOU   10  CB  TYR A  36    14721   8957  13564  -1967  -3571  -3071       C\\nATOM     11  N   TYR A  37      -0.606  -9.280 -13.416  1.00105.86           N\\nANISOU   11  N   TYR A  37    15140  11047  14036  -1589  -2687  -2627       N\\nATOM     12  CA  TYR A  37       0.202  -8.334 -12.652  1.00101.50           C\\nANISOU   12  CA  TYR A  37    14496  10678  13392  -1434  -2394  -2372       C\\nATOM     13  C   TYR A  37      -0.596  -7.105 -12.233  1.00 97.18           C\\nANISOU   13  C   TYR A  37    13669  10521  12732  -1638  -2109  -2055       C\\nATOM     14  O   TYR A  37      -0.269  -6.474 -11.221  1.00 92.55           O\\nANISOU   14  O   TYR A  37    13035   9983  12145  -1663  -1908  -1774       O\\nATOM     15  CB  TYR A  37       1.435  -7.931 -13.459  1.00105.43           C\\nANISOU   15  CB  TYR A  37    14938  11423  13698   -962  -2294  -2627       C\\nATOM     16  CG  TYR A  37       2.442  -9.052 -13.603  1.00112.39           C\\nANISOU   16  CG  TYR A  37    16060  11928  14715   -688  -2547  -2949       C\\nATOM     17  CD1 TYR A  37       2.745  -9.880 -12.528  1.00116.25           C\\nANISOU   17  CD1 TYR A  37    16804  11893  15472   -778  -2740  -2820       C\\nATOM     18  CD2 TYR A  37       3.084  -9.291 -14.814  1.00112.70           C\\nANISOU   18  CD2 TYR A  37    16070  12145  14606   -332  -2615  -3395       C\\nATOM     19  CE1 TYR A  37       3.662 -10.907 -12.650  1.00117.63           C\\nANISOU   19  CE1 TYR A  37    17203  11682  15808   -489  -3027  -3136       C\\nATOM     20  CE2 TYR A  37       4.002 -10.320 -14.944  1.00114.52           C\\nANISOU   20  CE2 TYR A  37    16488  12042  14980    -35  -2866  -3754       C\\nATOM     21  CZ  TYR A  37       4.287 -11.123 -13.860  1.00116.82           C\\nANISOU   21  CZ  TYR A  37    17037  11766  15584    -99  -3089  -3627       C\\nATOM     22  OH  TYR A  37       5.200 -12.147 -13.987  1.00116.76           O\\nANISOU   22  OH  TYR A  37    17222  11387  15756    236  -3393  -4004       O\\nATOM     23  N   ALA A  38      -1.639  -6.750 -12.985  1.00 96.22           N\\nANISOU   23  N   ALA A  38    13359  10676  12525  -1764  -2113  -2120       N\\nATOM     24  CA  ALA A  38      -2.506  -5.655 -12.566  1.00 90.24           C\\nANISOU   24  CA  ALA A  38    12324  10255  11709  -1946  -1899  -1864       C\\nATOM     25  C   ALA A  38      -3.348  -6.039 -11.356  1.00 93.14           C\\nANISOU   25  C   ALA A  38    12686  10447  12255  -2375  -1898  -1620       C\\nATOM     26  O   ALA A  38      -3.625  -5.191 -10.500  1.00 89.27           O\\nANISOU   26  O   ALA A  38    12015  10164  11737  -2476  -1673  -1375       O\\nATOM     27  CB  ALA A  38      -3.409  -5.222 -13.721  1.00 92.04           C\\nANISOU   27  CB  ALA A  38    12349  10812  11811  -1948  -1956  -2018       C\\nATOM     28  N   THR A  39      -3.759  -7.307 -11.265  1.00101.53           N\\nANISOU   28  N   THR A  39    13946  11141  13491  -2646  -2152  -1687       N\\nATOM     29  CA  THR A  39      -4.521  -7.761 -10.105  1.00 98.62           C\\nANISOU   29  CA  THR A  39    13594  10616  13261  -3121  -2155  -1423       C\\nATOM     30  C   THR A  39      -3.673  -7.706  -8.839  1.00 94.46           C\\nANISOU   30  C   THR A  39    13228   9915  12749  -3111  -2033  -1154       C\\nATOM     31  O   THR A  39      -4.127  -7.220  -7.795  1.00 90.19           O\\nANISOU   31  O   THR A  39    12545   9551  12174  -3363  -1831   -884       O\\nATOM     32  CB  THR A  39      -5.041  -9.178 -10.345  1.00 96.91           C\\nANISOU   32  CB  THR A  39    13602   9983  13235  -3430  -2502  -1538       C\\nATOM     33  OG1 THR A  39      -5.673  -9.242 -11.631  1.00 99.65           O\\nANISOU   33  OG1 THR A  39    13821  10489  13554  -3372  -2644  -1841       O\\nATOM     34  CG2 THR A  39      -6.044  -9.566  -9.272  1.00 85.14           C\\nANISOU   34  CG2 THR A  39    12068   8436  11847  -4016  -2487  -1245       C\\nATOM     35  N   LEU A  40      -2.434  -8.202  -8.915  1.00 91.92           N\\nANISOU   35  N   LEU A  40    13187   9271  12469  -2807  -2162  -1251       N\\nATOM     36  CA  LEU A  40      -1.537  -8.138  -7.766  1.00 89.55           C\\nANISOU   36  CA  LEU A  40    13043   8803  12179  -2751  -2081  -1015       C\\nATOM     37  C   LEU A  40      -1.335  -6.702  -7.304  1.00 83.76           C\\nANISOU   37  C   LEU A  40    12038   8512  11276  -2605  -1722   -856       C\\nATOM     38  O   LEU A  40      -1.301  -6.429  -6.098  1.00 87.36           O\\nANISOU   38  O   LEU A  40    12497   8987  11709  -2775  -1584   -580       O\\nATOM     39  CB  LEU A  40      -0.191  -8.777  -8.104  1.00 87.94           C\\nANISOU   39  CB  LEU A  40    13114   8249  12051  -2357  -2285  -1222       C\\nATOM     40  CG  LEU A  40      -0.166 -10.273  -8.417  1.00 86.57           C\\nANISOU   40  CG  LEU A  40    13274   7524  12094  -2433  -2707  -1405       C\\nATOM     41  CD1 LEU A  40       1.260 -10.798  -8.334  1.00 81.27           C\\nANISOU   41  CD1 LEU A  40    12855   6507  11518  -2029  -2890  -1557       C\\nATOM     42  CD2 LEU A  40      -1.085 -11.041  -7.480  1.00 87.43           C\\nANISOU   42  CD2 LEU A  40    13549   7331  12340  -3007  -2857  -1101       C\\nATOM     43  N   LEU A  41      -1.202  -5.770  -8.248  1.00 77.53           N\\nANISOU   43  N   LEU A  41    11027   8075  10356  -2302  -1588  -1023       N\\nATOM     44  CA  LEU A  41      -1.025  -4.372  -7.871  1.00 83.20           C\\nANISOU   44  CA  LEU A  41    11504   9166  10941  -2162  -1296   -879       C\\nATOM     45  C   LEU A  41      -2.242  -3.847  -7.120  1.00 91.88           C\\nANISOU   45  C   LEU A  41    12365  10511  12032  -2501  -1145   -694       C\\nATOM     46  O   LEU A  41      -2.101  -3.145  -6.111  1.00 94.79           O\\nANISOU   46  O   LEU A  41    12646  11017  12354  -2528   -951   -503       O\\nATOM     47  CB  LEU A  41      -0.739  -3.520  -9.108  1.00 84.35           C\\nANISOU   47  CB  LEU A  41    11487   9616  10946  -1830  -1231  -1064       C\\nATOM     48  CG  LEU A  41       0.684  -3.615  -9.668  1.00 84.82           C\\nANISOU   48  CG  LEU A  41    11682   9604  10941  -1449  -1257  -1222       C\\nATOM     49  CD1 LEU A  41       0.863  -2.686 -10.856  1.00 82.66           C\\nANISOU   49  CD1 LEU A  41    11233   9703  10473  -1206  -1167  -1345       C\\nATOM     50  CD2 LEU A  41       1.708  -3.304  -8.588  1.00 84.95           C\\nANISOU   50  CD2 LEU A  41    11768   9527  10981  -1340  -1134  -1042       C\\nATOM     51  N   THR A  42      -3.447  -4.187  -7.587  1.00 91.95           N\\nANISOU   51  N   THR A  42    12247  10603  12085  -2760  -1237   -778       N\\nATOM     52  CA  THR A  42      -4.651  -3.758  -6.883  1.00 87.42           C\\nANISOU   52  CA  THR A  42    11395  10312  11509  -3092  -1095   -650       C\\nATOM     53  C   THR A  42      -4.741  -4.405  -5.507  1.00 89.21           C\\nANISOU   53  C   THR A  42    11759  10370  11767  -3467  -1059   -402       C\\nATOM     54  O   THR A  42      -5.141  -3.757  -4.533  1.00 90.48           O\\nANISOU   54  O   THR A  42    11720  10805  11853  -3617   -841   -252       O\\nATOM     55  CB  THR A  42      -5.894  -4.085  -7.708  1.00 81.63           C\\nANISOU   55  CB  THR A  42    10483   9703  10829  -3302  -1229   -812       C\\nATOM     56  OG1 THR A  42      -5.719  -3.600  -9.045  1.00 80.89           O\\nANISOU   56  OG1 THR A  42    10326   9737  10673  -2956  -1306  -1030       O\\nATOM     57  CG2 THR A  42      -7.122  -3.427  -7.095  1.00 73.78           C\\nANISOU   57  CG2 THR A  42     9102   9107   9822  -3566  -1057   -743       C\\nATOM     58  N   LEU A  43      -4.372  -5.685  -5.408  1.00 89.32           N\\nANISOU   58  N   LEU A  43    12123   9933  11882  -3624  -1291   -363       N\\nATOM     59  CA  LEU A  43      -4.291  -6.324  -4.100  1.00 89.41           C\\nANISOU   59  CA  LEU A  43    12339   9733  11900  -3975  -1300    -78       C\\nATOM     60  C   LEU A  43      -3.297  -5.599  -3.203  1.00 85.76           C\\nANISOU   60  C   LEU A  43    11923   9332  11330  -3737  -1117     75       C\\nATOM     61  O   LEU A  43      -3.540  -5.429  -2.003  1.00 86.73           O\\nANISOU   61  O   LEU A  43    12007   9591  11355  -4009   -965    311       O\\nATOM     62  CB  LEU A  43      -3.907  -7.795  -4.254  1.00 92.73           C\\nANISOU   62  CB  LEU A  43    13182   9571  12480  -4106  -1657    -74       C\\nATOM     63  N   LEU A  44      -2.173  -5.155  -3.773  1.00 83.60           N\\nANISOU   63  N   LEU A  44    11715   8995  11055  -3246  -1124    -66       N\\nATOM     64  CA  LEU A  44      -1.214  -4.375  -3.000  1.00 85.11           C\\nANISOU   64  CA  LEU A  44    11914   9267  11155  -3006   -957     53       C\\nATOM     65  C   LEU A  44      -1.839  -3.078  -2.502  1.00 85.13           C\\nANISOU   65  C   LEU A  44    11557   9754  11035  -3039   -660    109       C\\nATOM     66  O   LEU A  44      -1.633  -2.688  -1.347  1.00 86.93           O\\nANISOU   66  O   LEU A  44    11776  10082  11172  -3118   -515    286       O\\nATOM     67  CB  LEU A  44       0.031  -4.082  -3.838  1.00 87.56           C\\nANISOU   67  CB  LEU A  44    12295   9491  11483  -2502  -1005   -135       C\\nATOM     68  CG  LEU A  44       1.048  -3.125  -3.207  1.00 86.61           C\\nANISOU   68  CG  LEU A  44    12129   9496  11281  -2230   -831    -46       C\\nATOM     69  CD1 LEU A  44       1.618  -3.719  -1.930  1.00 87.91           C\\nANISOU   69  CD1 LEU A  44    12554   9391  11458  -2363   -905    175       C\\nATOM     70  CD2 LEU A  44       2.164  -2.764  -4.177  1.00 83.34           C\\nANISOU   70  CD2 LEU A  44    11712   9091  10864  -1783   -849   -246       C\\nATOM     71  N   ILE A  45      -2.611  -2.400  -3.356  1.00 82.86           N\\nANISOU   71  N   ILE A  45    10974   9766  10745  -2965   -594    -59       N\\nATOM     72  CA  ILE A  45      -3.287  -1.172  -2.940  1.00 83.78           C\\nANISOU   72  CA  ILE A  45    10732  10317  10784  -2961   -364    -56       C\\nATOM     73  C   ILE A  45      -4.154  -1.429  -1.715  1.00 85.75           C\\nANISOU   73  C   ILE A  45    10876  10734  10969  -3402   -243     98       C\\nATOM     74  O   ILE A  45      -4.169  -0.633  -0.767  1.00 85.46           O\\nANISOU   74  O   ILE A  45    10685  10954  10832  -3395    -44    165       O\\nATOM     75  CB  ILE A  45      -4.118  -0.594  -4.101  1.00 80.09           C\\nANISOU   75  CB  ILE A  45     9986  10096  10350  -2847   -391   -260       C\\nATOM     76  CG1 ILE A  45      -3.232  -0.296  -5.309  1.00 82.72           C\\nANISOU   76  CG1 ILE A  45    10426  10322  10681  -2446   -492   -386       C\\nATOM     77  CG2 ILE A  45      -4.845   0.666  -3.657  1.00 71.03           C\\nANISOU   77  CG2 ILE A  45     8464   9363   9163  -2807   -205   -292       C\\nATOM     78  CD1 ILE A  45      -3.998   0.221  -6.511  1.00 85.25           C\\nANISOU   78  CD1 ILE A  45    10525  10865  11002  -2340   -563   -559       C\\nATOM     79  N   ALA A  46      -4.887  -2.544  -1.711  1.00 89.24           N\\nANISOU   79  N   ALA A  46    11398  11053  11455  -3812   -363    150       N\\nATOM     80  CA  ALA A  46      -5.719  -2.875  -0.560  1.00 84.99           C\\nANISOU   80  CA  ALA A  46    10762  10712  10819  -4309   -240    325       C\\nATOM     81  C   ALA A  46      -4.868  -3.120   0.678  1.00 86.02           C\\nANISOU   81  C   ALA A  46    11172  10680  10833  -4395   -199    583       C\\nATOM     82  O   ALA A  46      -5.201  -2.653   1.773  1.00 82.61           O\\nANISOU   82  O   ALA A  46    10575  10580  10232  -4584     19    688       O\\nATOM     83  CB  ALA A  46      -6.581  -4.096  -0.869  1.00 77.37           C\\nANISOU   83  CB  ALA A  46     9868   9590   9938  -4771   -418    360       C\\nATOM     84  N   VAL A  47      -3.758  -3.841   0.522  1.00 84.11           N\\nANISOU   84  N   VAL A  47    11343   9946  10669  -4238   -419    662       N\\nATOM     85  CA  VAL A  47      -2.894  -4.117   1.664  1.00 83.65           C\\nANISOU   85  CA  VAL A  47    11575   9696  10512  -4292   -436    908       C\\nATOM     86  C   VAL A  47      -2.272  -2.829   2.191  1.00 82.63           C\\nANISOU   86  C   VAL A  47    11279   9847  10269  -3948   -212    871       C\\nATOM     87  O   VAL A  47      -2.139  -2.644   3.406  1.00 89.41           O\\nANISOU   87  O   VAL A  47    12171  10845  10957  -4107    -91   1051       O\\nATOM     88  CB  VAL A  47      -1.826  -5.156   1.281  1.00 85.45           C\\nANISOU   88  CB  VAL A  47    12252   9322  10892  -4129   -768    941       C\\nATOM     89  CG1 VAL A  47      -0.873  -5.397   2.438  1.00 84.04           C\\nANISOU   89  CG1 VAL A  47    12375   8931  10627  -4135   -829   1190       C\\nATOM     90  CG2 VAL A  47      -2.490  -6.457   0.863  1.00 89.97           C\\nANISOU   90  CG2 VAL A  47    13015   9574  11594  -4506  -1029    979       C\\nATOM     91  N   ILE A  48      -1.893  -1.915   1.294  1.00 78.76           N\\nANISOU   91  N   ILE A  48    10618   9450   9859  -3495   -165    645       N\\nATOM     92  CA  ILE A  48      -1.320  -0.643   1.730  1.00 77.79           C\\nANISOU   92  CA  ILE A  48    10338   9559   9659  -3180     16    603       C\\nATOM     93  C   ILE A  48      -2.344   0.158   2.522  1.00 82.81           C\\nANISOU   93  C   ILE A  48    10623  10681  10158  -3375    261    582       C\\nATOM     94  O   ILE A  48      -2.025   0.749   3.560  1.00 85.46           O\\nANISOU   94  O   ILE A  48    10924  11187  10359  -3347    400    647       O\\nATOM     95  CB  ILE A  48      -0.797   0.158   0.525  1.00 76.69           C\\nANISOU   95  CB  ILE A  48    10090   9420   9628  -2722     -7    395       C\\nATOM     96  CG1 ILE A  48       0.350  -0.582  -0.162  1.00 81.09           C\\nANISOU   96  CG1 ILE A  48    10957   9571  10283  -2498   -216    373       C\\nATOM     97  CG2 ILE A  48      -0.339   1.535   0.969  1.00 73.83           C\\nANISOU   97  CG2 ILE A  48     9552   9290   9212  -2449    157    360       C\\nATOM     98  CD1 ILE A  48       0.859   0.105  -1.411  1.00 83.26           C\\nANISOU   98  CD1 ILE A  48    11128   9896  10613  -2110   -227    183       C\\nATOM     99  N   VAL A  49      -3.590   0.189   2.047  1.00 85.62           N\\nANISOU   99  N   VAL A  49    10696  11290  10545  -3560    309    458       N\\nATOM    100  CA  VAL A  49      -4.628   0.950   2.736  1.00 86.41           C\\nANISOU  100  CA  VAL A  49    10399  11901  10530  -3713    539    369       C\\nATOM    101  C   VAL A  49      -5.028   0.256   4.033  1.00 86.76           C\\nANISOU  101  C   VAL A  49    10505  12094  10367  -4215    646    582       C\\nATOM    102  O   VAL A  49      -5.154   0.896   5.083  1.00 84.97           O\\nANISOU  102  O   VAL A  49    10110  12216   9958  -4262    848    578       O\\nATOM    103  CB  VAL A  49      -5.837   1.166   1.811  1.00 85.12           C\\nANISOU  103  CB  VAL A  49     9887  11980  10477  -3747    531    151       C\\nATOM    104  CG1 VAL A  49      -7.004   1.745   2.592  1.00 88.42           C\\nANISOU  104  CG1 VAL A  49     9863  12953  10781  -3956    756     30       C\\nATOM    105  CG2 VAL A  49      -5.456   2.084   0.662  1.00 80.88           C\\nANISOU  105  CG2 VAL A  49     9274  11370  10087  -3251    439    -34       C\\nATOM    106  N   PHE A  50      -5.229  -1.063   3.980  1.00 87.95           N\\nANISOU  106  N   PHE A  50    10908  11980  10529  -4611    497    773       N\\nATOM    107  CA  PHE A  50      -5.635  -1.794   5.177  1.00 89.88           C\\nANISOU  107  CA  PHE A  50    11255  12333  10561  -5041    554   1009       C\\nATOM    108  C   PHE A  50      -4.604  -1.654   6.289  1.00 92.06           C\\nANISOU  108  C   PHE A  50    11792  12524  10663  -4962    580   1197       C\\nATOM    109  O   PHE A  50      -4.957  -1.394   7.445  1.00 93.62           O\\nANISOU  109  O   PHE A  50    11871  13085  10613  -5087    752   1242       O\\nATOM    110  CB  PHE A  50      -5.857  -3.269   4.846  1.00 88.37           C\\nANISOU  110  CB  PHE A  50    11370  11743  10463  -5313    300   1176       C\\nATOM    111  CG  PHE A  50      -6.166  -4.119   6.048  1.00 91.54           C\\nANISOU  111  CG  PHE A  50    11945  12184  10651  -5658    293   1438       C\\nATOM    112  CD1 PHE A  50      -7.465  -4.232   6.518  1.00 92.88           C\\nANISOU  112  CD1 PHE A  50    11823  12793  10672  -5976    452   1419       C\\nATOM    113  CD2 PHE A  50      -5.157  -4.805   6.708  1.00 90.81           C\\nANISOU  113  CD2 PHE A  50    12302  11702  10500  -5665    108   1698       C\\nATOM    114  CE1 PHE A  50      -7.752  -5.011   7.623  1.00 96.10           C\\nANISOU  114  CE1 PHE A  50    12394  13265  10853  -6335    441   1672       C\\nATOM    115  CE2 PHE A  50      -5.439  -5.583   7.816  1.00 94.85           C\\nANISOU  115  CE2 PHE A  50    12982  12260  10797  -6003     73   1952       C\\nATOM    116  CZ  PHE A  50      -6.737  -5.688   8.272  1.00 98.38           C\\nANISOU  116  CZ  PHE A  50    13146  13159  11074  -6358    245   1949       C\\nATOM    117  N   GLY A  51      -3.324  -1.822   5.959  1.00 89.17           N\\nANISOU  117  N   GLY A  51    11775  11692  10415  -4731    395   1283       N\\nATOM    118  CA  GLY A  51      -2.301  -1.796   6.988  1.00 84.51           C\\nANISOU  118  CA  GLY A  51    11458  10976   9676  -4664    370   1475       C\\nATOM    119  C   GLY A  51      -2.075  -0.415   7.573  1.00 79.23           C\\nANISOU  119  C   GLY A  51    10517  10705   8881  -4366    607   1313       C\\nATOM    120  O   GLY A  51      -1.800  -0.278   8.767  1.00 79.21           O\\nANISOU  120  O   GLY A  51    10593  10866   8639  -4497    694   1454       O\\nATOM    121  N   ASN A  52      -2.183   0.626   6.746  1.00 74.87           N\\nANISOU  121  N   ASN A  52     9661  10300   8487  -3969    686   1017       N\\nATOM    122  CA  ASN A  52      -1.869   1.971   7.213  1.00 72.04           C\\nANISOU  122  CA  ASN A  52     9081  10223   8066  -3641    847    847       C\\nATOM    123  C   ASN A  52      -3.057   2.680   7.841  1.00 76.56           C\\nANISOU  123  C   ASN A  52     9223  11393   8475  -3813   1107    674       C\\nATOM    124  O   ASN A  52      -2.860   3.566   8.681  1.00 76.05           O\\nANISOU  124  O   ASN A  52     9026  11599   8272  -3672   1243    574       O\\nATOM    125  CB  ASN A  52      -1.305   2.809   6.069  1.00 68.61           C\\nANISOU  125  CB  ASN A  52     8565   9624   7879  -3132    768    642       C\\nATOM    126  CG  ASN A  52       0.113   2.416   5.715  1.00 79.96           C\\nANISOU  126  CG  ASN A  52    10362  10592   9427  -2882    569    754       C\\nATOM    127  OD1 ASN A  52       1.065   2.835   6.370  1.00 77.35           O\\nANISOU  127  OD1 ASN A  52    10144  10206   9041  -2704    566    802       O\\nATOM    128  ND2 ASN A  52       0.261   1.600   4.681  1.00 80.13           N\\nANISOU  128  ND2 ASN A  52    10547  10294   9604  -2861    393    767       N\\nATOM    129  N   VAL A  53      -4.286   2.318   7.468  1.00 82.38           N\\nANISOU  129  N   VAL A  53     9715  12360   9224  -4106   1170    606       N\\nATOM    130  CA  VAL A  53      -5.441   2.817   8.209  1.00 86.81           C\\nANISOU  130  CA  VAL A  53     9853  13535   9597  -4309   1419    435       C\\nATOM    131  C   VAL A  53      -5.398   2.300   9.643  1.00 91.28           C\\nANISOU  131  C   VAL A  53    10607  14230   9845  -4566   1474    633       C\\nATOM    132  O   VAL A  53      -5.768   3.009  10.588  1.00 98.44           O\\nANISOU  132  O   VAL A  53    11273  15582  10548  -4528   1653    471       O\\nATOM    133  CB  VAL A  53      -6.751   2.433   7.494  1.00 83.17           C\\nANISOU  133  CB  VAL A  53     9126  13231   9243  -4473   1406    307       C\\nATOM    134  CG1 VAL A  53      -7.949   2.691   8.387  1.00 78.74           C\\nANISOU  134  CG1 VAL A  53     8217  13227   8475  -4616   1596    143       C\\nATOM    135  CG2 VAL A  53      -6.893   3.217   6.198  1.00 79.84           C\\nANISOU  135  CG2 VAL A  53     8453  12777   9107  -4129   1341     45       C\\nATOM    136  N   LEU A  54      -4.923   1.065   9.827  1.00 86.53           N\\nANISOU  136  N   LEU A  54    10442  13233   9201  -4813   1292    968       N\\nATOM    137  CA  LEU A  54      -4.726   0.529  11.172  1.00 88.26           C\\nANISOU  137  CA  LEU A  54    10891  13520   9123  -5054   1288   1196       C\\nATOM    138  C   LEU A  54      -3.747   1.383  11.968  1.00 86.94           C\\nANISOU  138  C   LEU A  54    10787  13428   8817  -4810   1356   1171       C\\nATOM    139  O   LEU A  54      -4.002   1.722  13.130  1.00 94.33           O\\nANISOU  139  O   LEU A  54    11611  14759   9469  -4901   1496   1127       O\\nATOM    140  CB  LEU A  54      -4.224  -0.914  11.097  1.00 90.28           C\\nANISOU  140  CB  LEU A  54    11637  13240   9427  -5281   1006   1548       C\\nATOM    141  CG  LEU A  54      -5.198  -2.030  10.729  1.00 92.89           C\\nANISOU  141  CG  LEU A  54    11990  13500   9806  -5638    909   1650       C\\nATOM    142  CD1 LEU A  54      -4.459  -3.354  10.614  1.00 97.20           C\\nANISOU  142  CD1 LEU A  54    13055  13428  10449  -5757    575   1961       C\\nATOM    143  CD2 LEU A  54      -6.301  -2.128  11.763  1.00 96.43           C\\nANISOU  143  CD2 LEU A  54    12213  14478   9948  -5990   1090   1654       C\\nATOM    144  N   VAL A  55      -2.613   1.737  11.356  1.00 84.36           N\\nANISOU  144  N   VAL A  55    10638  12737   8678  -4508   1252   1188       N\\nATOM    145  CA  VAL A  55      -1.593   2.518  12.053  1.00 89.47           C\\nANISOU  145  CA  VAL A  55    11371  13417   9208  -4276   1291   1178       C\\nATOM    146  C   VAL A  55      -2.164   3.838  12.551  1.00 92.31           C\\nANISOU  146  C   VAL A  55    11279  14347   9446  -4112   1550    831       C\\nATOM    147  O   VAL A  55      -1.801   4.314  13.634  1.00 95.44           O\\nANISOU  147  O   VAL A  55    11689  14966   9606  -4066   1624    802       O\\nATOM    148  CB  VAL A  55      -0.374   2.741  11.133  1.00 85.96           C\\nANISOU  148  CB  VAL A  55    11134  12447   9082  -3803   1074   1151       C\\nATOM    149  CG1 VAL A  55       0.679   3.587  11.829  1.00 76.85           C\\nANISOU  149  CG1 VAL A  55    10045  11292   7864  -3476   1063   1092       C\\nATOM    150  CG2 VAL A  55       0.217   1.408  10.697  1.00 86.37           C\\nANISOU  150  CG2 VAL A  55    11619  11948   9251  -3934    799   1439       C\\nATOM    151  N   CYS A  56      -3.075   4.442  11.786  1.00 85.56           N\\nANISOU  151  N   CYS A  56    10018  13731   8759  -3998   1660    538       N\\nATOM    152  CA  CYS A  56      -3.627   5.737  12.175  1.00 80.56           C\\nANISOU  152  CA  CYS A  56     8941  13592   8075  -3762   1850    148       C\\nATOM    153  C   CYS A  56      -4.603   5.598  13.334  1.00 86.48           C\\nANISOU  153  C   CYS A  56     9514  14821   8522  -4005   1984     66       C\\nATOM    154  O   CYS A  56      -4.495   6.313  14.337  1.00 84.77           O\\nANISOU  154  O   CYS A  56     9186  14923   8102  -3899   2089   -102       O\\nATOM    155  CB  CYS A  56      -4.301   6.398  10.975  1.00 67.26           C\\nANISOU  155  CB  CYS A  56     6920  11917   6720  -3468   1818   -150       C\\nATOM    156  SG  CYS A  56      -3.139   6.859   9.688  1.00 71.11           S\\nANISOU  156  SG  CYS A  56     7652  11761   7605  -2939   1540   -134       S\\nATOM    157  N   MET A  57      -5.565   4.680  13.217  1.00 89.30           N\\nANISOU  157  N   MET A  57     9839  15250   8838  -4343   1978    170       N\\nATOM    158  CA  MET A  57      -6.547   4.508  14.283  1.00 99.11           C\\nANISOU  158  CA  MET A  57    10893  16987   9777  -4621   2115     99       C\\nATOM    159  C   MET A  57      -5.891   4.028  15.570  1.00100.31           C\\nANISOU  159  C   MET A  57    11370  17145   9601  -4843   2094    365       C\\nATOM    160  O   MET A  57      -6.282   4.448  16.665  1.00109.98           O\\nANISOU  160  O   MET A  57    12410  18838  10541  -4909   2235    210       O\\nATOM    161  CB  MET A  57      -7.633   3.529  13.845  1.00106.16           C\\nANISOU  161  CB  MET A  57    11719  17920  10695  -4975   2095    198       C\\nATOM    162  CG  MET A  57      -8.458   4.012  12.672  1.00104.93           C\\nANISOU  162  CG  MET A  57    11195  17843  10830  -4777   2113    -94       C\\nATOM    163  SD  MET A  57      -9.729   2.811  12.239  1.00106.23           S\\nANISOU  163  SD  MET A  57    11291  18073  11000  -5226   2085     28       S\\nATOM    164  CE  MET A  57      -8.718   1.360  11.965  1.00104.77           C\\nANISOU  164  CE  MET A  57    11736  17203  10870  -5491   1838    545       C\\nATOM    165  N   ALA A  58      -4.891   3.151  15.458  1.00 91.70           N\\nANISOU  165  N   ALA A  58    10761  15535   8547  -4945   1896    749       N\\nATOM    166  CA  ALA A  58      -4.253   2.590  16.647  1.00 94.86           C\\nANISOU  166  CA  ALA A  58    11502  15887   8653  -5159   1819   1033       C\\nATOM    167  C   ALA A  58      -3.578   3.673  17.478  1.00 93.98           C\\nANISOU  167  C   ALA A  58    11323  16005   8380  -4887   1912    851       C\\nATOM    168  O   ALA A  58      -3.795   3.769  18.691  1.00 97.13           O\\nANISOU  168  O   ALA A  58    11671  16787   8447  -5049   2002    828       O\\nATOM    169  CB  ALA A  58      -3.240   1.521  16.244  1.00 92.30           C\\nANISOU  169  CB  ALA A  58    11700  14899   8471  -5223   1532   1429       C\\nATOM    170  N   VAL A  59      -2.740   4.492  16.841  1.00 96.30           N\\nANISOU  170  N   VAL A  59    11619  16077   8895  -4483   1883    717       N\\nATOM    171  CA  VAL A  59      -2.102   5.595  17.551  1.00 91.92           C\\nANISOU  171  CA  VAL A  59    10983  15733   8211  -4197   1959    504       C\\nATOM    172  C   VAL A  59      -3.144   6.585  18.045  1.00 91.74           C\\nANISOU  172  C   VAL A  59    10460  16322   8077  -4097   2177     56       C\\nATOM    173  O   VAL A  59      -2.990   7.184  19.117  1.00 99.07           O\\nANISOU  173  O   VAL A  59    11313  17573   8756  -4030   2251   -105       O\\nATOM    174  CB  VAL A  59      -1.062   6.271  16.638  1.00 84.96           C\\nANISOU  174  CB  VAL A  59    10179  14491   7608  -3805   1881    441       C\\nATOM    175  CG1 VAL A  59      -0.446   7.484  17.318  1.00 88.37           C\\nANISOU  175  CG1 VAL A  59    10505  15150   7923  -3491   1949    173       C\\nATOM    176  CG2 VAL A  59       0.009   5.267  16.235  1.00 77.23           C\\nANISOU  176  CG2 VAL A  59     9704  12913   6729  -3889   1637    864       C\\nATOM    177  N   SER A  60      -4.229   6.759  17.291  1.00 95.26           N\\nANISOU  177  N   SER A  60    10557  16933   8706  -4072   2257   -169       N\\nATOM    178  CA  SER A  60      -5.247   7.733  17.658  1.00 98.05           C\\nANISOU  178  CA  SER A  60    10416  17831   9007  -3917   2417   -638       C\\nATOM    179  C   SER A  60      -6.057   7.307  18.875  1.00104.36           C\\nANISOU  179  C   SER A  60    11113  19121   9420  -4286   2535   -633       C\\nATOM    180  O   SER A  60      -6.732   8.148  19.479  1.00107.43           O\\nANISOU  180  O   SER A  60    11125  20003   9691  -4157   2661  -1033       O\\nATOM    181  CB  SER A  60      -6.183   7.974  16.473  1.00 97.14           C\\nANISOU  181  CB  SER A  60     9973  17730   9205  -3784   2427   -864       C\\nATOM    182  OG  SER A  60      -7.148   8.967  16.770  1.00 99.99           O\\nANISOU  182  OG  SER A  60     9859  18573   9559  -3574   2531  -1349       O\\nATOM    183  N   ARG A  61      -6.003   6.030  19.255  1.00 98.78           N\\nANISOU  183  N   ARG A  61    10729  18286   8518  -4738   2478   -202       N\\nATOM    184  CA  ARG A  61      -6.880   5.512  20.291  1.00103.46           C\\nANISOU  184  CA  ARG A  61    11212  19353   8745  -5156   2589   -162       C\\nATOM    185  C   ARG A  61      -6.159   4.772  21.410  1.00107.55           C\\nANISOU  185  C   ARG A  61    12131  19803   8928  -5464   2513    219       C\\nATOM    186  O   ARG A  61      -6.808   4.395  22.392  1.00117.52           O\\nANISOU  186  O   ARG A  61    13311  21498   9842  -5828   2609    262       O\\nATOM    187  CB  ARG A  61      -7.937   4.590  19.664  1.00104.53           C\\nANISOU  187  CB  ARG A  61    11265  19502   8951  -5497   2593    -37       C\\nATOM    188  CG  ARG A  61      -8.730   5.267  18.557  1.00 96.67           C\\nANISOU  188  CG  ARG A  61     9865  18588   8277  -5209   2647   -407       C\\nATOM    189  CD  ARG A  61     -10.016   4.534  18.248  1.00108.57           C\\nANISOU  189  CD  ARG A  61    11174  20320   9758  -5564   2702   -387       C\\nATOM    190  NE  ARG A  61      -9.801   3.362  17.409  1.00109.71           N\\nANISOU  190  NE  ARG A  61    11662  19943  10079  -5797   2536     11       N\\nATOM    191  CZ  ARG A  61     -10.778   2.566  16.987  1.00115.93           C\\nANISOU  191  CZ  ARG A  61    12357  20800  10890  -6123   2537     93       C\\nATOM    192  NH1 ARG A  61     -12.034   2.820  17.330  1.00116.46           N\\nANISOU  192  NH1 ARG A  61    11988  21459  10801  -6264   2710   -185       N\\nATOM    193  NH2 ARG A  61     -10.501   1.519  16.223  1.00119.11           N\\nANISOU  193  NH2 ARG A  61    13096  20686  11475  -6303   2354    434       N\\nATOM    194  N   GLU A  62      -4.853   4.558  21.301  1.00 96.97           N\\nANISOU  194  N   GLU A  62    11215  17953   7675  -5333   2333    491       N\\nATOM    195  CA  GLU A  62      -4.083   3.859  22.320  1.00101.43           C\\nANISOU  195  CA  GLU A  62    12192  18393   7956  -5580   2207    858       C\\nATOM    196  C   GLU A  62      -3.184   4.851  23.046  1.00102.22           C\\nANISOU  196  C   GLU A  62    12307  18603   7928  -5257   2227    678       C\\nATOM    197  O   GLU A  62      -2.426   5.591  22.409  1.00 92.57           O\\nANISOU  197  O   GLU A  62    11100  17116   6955  -4842   2178    531       O\\nATOM    198  CB  GLU A  62      -3.246   2.737  21.703  1.00100.84           C\\nANISOU  198  CB  GLU A  62    12621  17618   8074  -5678   1928   1315       C\\nATOM    199  N   LYS A  63      -3.269   4.854  24.378  1.00108.00           N\\nANISOU  199  N   LYS A  63    13040  19738   8259  -5463   2293    691       N\\nATOM    200  CA  LYS A  63      -2.467   5.770  25.183  1.00106.16           C\\nANISOU  200  CA  LYS A  63    12820  19652   7864  -5180   2305    504       C\\nATOM    201  C   LYS A  63      -0.976   5.535  24.970  1.00 98.83           C\\nANISOU  201  C   LYS A  63    12367  18125   7059  -4996   2054    800       C\\nATOM    202  O   LYS A  63      -0.243   6.439  24.552  1.00 90.24           O\\nANISOU  202  O   LYS A  63    11250  16879   6157  -4571   2024    584       O\\nATOM    203  CB  LYS A  63      -2.833   5.616  26.660  1.00114.28           C\\nANISOU  203  CB  LYS A  63    13807  21206   8408  -5502   2401    526       C\\nATOM    204  N   ALA A  64      -0.510   4.312  25.239  1.00108.15           N\\nANISOU  204  N   ALA A  64    13988  18956   8148  -5308   1844   1286       N\\nATOM    205  CA  ALA A  64       0.917   4.011  25.200  1.00103.75           C\\nANISOU  205  CA  ALA A  64    13892  17853   7678  -5142   1563   1569       C\\nATOM    206  C   ALA A  64       1.513   4.169  23.805  1.00 99.33           C\\nANISOU  206  C   ALA A  64    13405  16779   7558  -4812   1452   1552       C\\nATOM    207  O   ALA A  64       2.735   4.041  23.649  1.00 84.58           O\\nANISOU  207  O   ALA A  64    11875  14464   5799  -4615   1215   1732       O\\nATOM    208  CB  ALA A  64       1.164   2.590  25.719  1.00103.60           C\\nANISOU  208  CB  ALA A  64    14310  17538   7516  -5540   1320   2073       C\\nATOM    209  N   LEU A  65       0.685   4.450  22.798  1.00 91.85           N\\nANISOU  209  N   LEU A  65    12140  15902   6858  -4745   1606   1334       N\\nATOM    210  CA  LEU A  65       1.126   4.676  21.429  1.00 92.45           C\\nANISOU  210  CA  LEU A  65    12233  15560   7334  -4450   1535   1288       C\\nATOM    211  C   LEU A  65       1.071   6.143  21.021  1.00 91.55           C\\nANISOU  211  C   LEU A  65    11741  15700   7344  -4047   1715    824       C\\nATOM    212  O   LEU A  65       1.216   6.447  19.835  1.00 98.95           O\\nANISOU  212  O   LEU A  65    12606  16387   8603  -3825   1705    736       O\\nATOM    213  CB  LEU A  65       0.282   3.842  20.465  1.00 91.67           C\\nANISOU  213  CB  LEU A  65    12087  15284   7459  -4662   1529   1402       C\\nATOM    214  CG  LEU A  65       0.533   2.337  20.472  1.00 96.52           C\\nANISOU  214  CG  LEU A  65    13133  15448   8091  -4973   1266   1854       C\\nATOM    215  CD1 LEU A  65      -0.389   1.627  19.490  1.00101.66           C\\nANISOU  215  CD1 LEU A  65    13694  15972   8962  -5162   1269   1895       C\\nATOM    216  CD2 LEU A  65       1.987   2.059  20.143  1.00 88.49           C\\nANISOU  216  CD2 LEU A  65    12531  13837   7256  -4733    974   2071       C\\nATOM    217  N   GLN A  66       0.870   7.056  21.966  1.00 97.64           N\\nANISOU  217  N   GLN A  66    12271  16951   7878  -3940   1858    509       N\\nATOM    218  CA  GLN A  66       0.729   8.476  21.643  1.00 91.59           C\\nANISOU  218  CA  GLN A  66    11125  16421   7256  -3531   1991      9       C\\nATOM    219  C   GLN A  66       2.014   9.220  22.003  1.00 88.27           C\\nANISOU  219  C   GLN A  66    10883  15873   6783  -3219   1872    -76       C\\nATOM    220  O   GLN A  66       2.081  10.015  22.940  1.00 95.43           O\\nANISOU  220  O   GLN A  66    11654  17116   7488  -3077   1921   -364       O\\nATOM    221  CB  GLN A  66      -0.488   9.060  22.354  1.00 94.21           C\\nANISOU  221  CB  GLN A  66    11011  17366   7418  -3569   2200   -377       C\\nATOM    222  CG  GLN A  66      -1.806   8.615  21.747  1.00 90.38           C\\nANISOU  222  CG  GLN A  66    10255  17032   7053  -3778   2313   -412       C\\nATOM    223  CD  GLN A  66      -3.010   9.067  22.544  1.00 98.45           C\\nANISOU  223  CD  GLN A  66    10853  18690   7865  -3861   2497   -767       C\\nATOM    224  OE1 GLN A  66      -2.887   9.506  23.689  1.00102.35           O\\nANISOU  224  OE1 GLN A  66    11295  19524   8070  -3847   2548   -921       O\\nATOM    225  NE2 GLN A  66      -4.187   8.960  21.941  1.00101.41           N\\nANISOU  225  NE2 GLN A  66    10914  19243   8376  -3945   2588   -913       N\\nATOM    226  N   THR A  67       3.049   8.942  21.221  1.00 81.40           N\\nANISOU  226  N   THR A  67    10313  14420   6193  -3058   1648    159       N\\nATOM    227  CA  THR A  67       4.366   9.523  21.416  1.00 80.16           C\\nANISOU  227  CA  THR A  67    10341  13928   6189  -2690   1412    112       C\\nATOM    228  C   THR A  67       4.724  10.396  20.219  1.00 81.81           C\\nANISOU  228  C   THR A  67    10385  13739   6959  -2223   1303   -122       C\\nATOM    229  O   THR A  67       4.047  10.388  19.187  1.00 83.11           O\\nANISOU  229  O   THR A  67    10366  13821   7392  -2189   1372   -182       O\\nATOM    230  CB  THR A  67       5.424   8.430  21.618  1.00 74.28           C\\nANISOU  230  CB  THR A  67    10089  12752   5384  -2838   1150    588       C\\nATOM    231  OG1 THR A  67       5.732   7.823  20.359  1.00 77.15           O\\nANISOU  231  OG1 THR A  67    10579  12565   6169  -2749   1000    784       O\\nATOM    232  CG2 THR A  67       4.909   7.358  22.566  1.00 76.90           C\\nANISOU  232  CG2 THR A  67    10631  13398   5190  -3391   1228    928       C\\nATOM    233  N   THR A  68       5.803  11.165  20.370  1.00 86.60           N\\nANISOU  233  N   THR A  68    11062  14111   7731  -1884   1119   -244       N\\nATOM    234  CA  THR A  68       6.274  11.984  19.259  1.00 81.90           C\\nANISOU  234  CA  THR A  68    10353  13120   7646  -1492    990   -405       C\\nATOM    235  C   THR A  68       6.614  11.116  18.055  1.00 76.38           C\\nANISOU  235  C   THR A  68     9828  11956   7236  -1519    883    -94       C\\nATOM    236  O   THR A  68       6.157  11.379  16.939  1.00 74.99           O\\nANISOU  236  O   THR A  68     9479  11652   7360  -1401    915   -182       O\\nATOM    237  CB  THR A  68       7.490  12.816  19.681  1.00 80.77           C\\nANISOU  237  CB  THR A  68    10291  12786   7611  -1198    788   -526       C\\nATOM    238  OG1 THR A  68       8.582  11.948  20.014  1.00 75.97           O\\nANISOU  238  OG1 THR A  68    10037  11917   6911  -1290    604   -182       O\\nATOM    239  CG2 THR A  68       7.155  13.692  20.878  1.00 83.25           C\\nANISOU  239  CG2 THR A  68    10436  13561   7636  -1147    872   -884       C\\nATOM    240  N   THR A  69       7.412  10.066  18.270  1.00 78.37           N\\nANISOU  240  N   THR A  69    10426  11955   7395  -1662    733    255       N\\nATOM    241  CA  THR A  69       7.811   9.195  17.168  1.00 78.88           C\\nANISOU  241  CA  THR A  69    10662  11578   7732  -1656    605    503       C\\nATOM    242  C   THR A  69       6.596   8.584  16.482  1.00 78.27           C\\nANISOU  242  C   THR A  69    10482  11594   7664  -1890    759    558       C\\nATOM    243  O   THR A  69       6.522   8.550  15.247  1.00 73.15           O\\nANISOU  243  O   THR A  69     9763  10702   7330  -1761    732    539       O\\nATOM    244  CB  THR A  69       8.748   8.097  17.676  1.00 76.37           C\\nANISOU  244  CB  THR A  69    10733  11000   7285  -1777    388    839       C\\nATOM    245  OG1 THR A  69       9.982   8.680  18.112  1.00 72.19           O\\nANISOU  245  OG1 THR A  69    10268  10338   6821  -1513    212    771       O\\nATOM    246  CG2 THR A  69       9.035   7.083  16.582  1.00 74.02           C\\nANISOU  246  CG2 THR A  69    10604  10273   7247  -1776    252   1050       C\\nATOM    247  N   ASN A  70       5.625   8.114  17.269  1.00 82.86           N\\nANISOU  247  N   ASN A  70    11039  12561   7884  -2256    925    618       N\\nATOM    248  CA  ASN A  70       4.436   7.496  16.698  1.00 81.91           C\\nANISOU  248  CA  ASN A  70    10800  12565   7757  -2530   1069    672       C\\nATOM    249  C   ASN A  70       3.562   8.494  15.947  1.00 81.00           C\\nANISOU  249  C   ASN A  70    10269  12649   7860  -2327   1221    314       C\\nATOM    250  O   ASN A  70       2.805   8.084  15.063  1.00 74.10           O\\nANISOU  250  O   ASN A  70     9290  11736   7128  -2431   1271    335       O\\nATOM    251  CB  ASN A  70       3.629   6.801  17.798  1.00 79.20           C\\nANISOU  251  CB  ASN A  70    10505  12647   6942  -3020   1221    832       C\\nATOM    252  CG  ASN A  70       4.333   5.581  18.348  1.00 78.28           C\\nANISOU  252  CG  ASN A  70    10856  12250   6638  -3286   1014   1268       C\\nATOM    253  OD1 ASN A  70       5.224   5.030  17.706  1.00 74.09           O\\nANISOU  253  OD1 ASN A  70    10588  11183   6379  -3127    762   1443       O\\nATOM    254  ND2 ASN A  70       3.941   5.152  19.542  1.00 73.15           N\\nANISOU  254  ND2 ASN A  70    10308  11972   5512  -3692   1103   1439       N\\nATOM    255  N   TYR A  71       3.640   9.786  16.274  1.00 84.07           N\\nANISOU  255  N   TYR A  71    10427  13227   8291  -2033   1261    -20       N\\nATOM    256  CA  TYR A  71       2.933  10.782  15.475  1.00 77.80           C\\nANISOU  256  CA  TYR A  71     9275  12516   7768  -1780   1321   -352       C\\nATOM    257  C   TYR A  71       3.632  11.001  14.143  1.00 70.85           C\\nANISOU  257  C   TYR A  71     8477  11134   7310  -1497   1135   -290       C\\nATOM    258  O   TYR A  71       2.978  11.216  13.117  1.00 65.56           O\\nANISOU  258  O   TYR A  71     7626  10422   6864  -1416   1148   -386       O\\nATOM    259  CB  TYR A  71       2.809  12.094  16.246  1.00 74.68           C\\nANISOU  259  CB  TYR A  71     8632  12431   7314  -1540   1370   -746       C\\nATOM    260  CG  TYR A  71       1.783  12.035  17.350  1.00 80.29           C\\nANISOU  260  CG  TYR A  71     9123  13772   7611  -1796   1612   -924       C\\nATOM    261  CD1 TYR A  71       0.690  11.189  17.253  1.00 82.22           C\\nANISOU  261  CD1 TYR A  71     9248  14311   7681  -2164   1796   -825       C\\nATOM    262  CD2 TYR A  71       1.912  12.814  18.492  1.00 84.10           C\\nANISOU  262  CD2 TYR A  71     9504  14589   7861  -1688   1658  -1202       C\\nATOM    263  CE1 TYR A  71      -0.250  11.123  18.258  1.00 91.89           C\\nANISOU  263  CE1 TYR A  71    10236  16183   8495  -2441   2045   -986       C\\nATOM    264  CE2 TYR A  71       0.976  12.756  19.503  1.00 85.39           C\\nANISOU  264  CE2 TYR A  71     9439  15406   7599  -1932   1905  -1392       C\\nATOM    265  CZ  TYR A  71      -0.103  11.907  19.381  1.00 94.33           C\\nANISOU  265  CZ  TYR A  71    10434  16859   8548  -2320   2110  -1275       C\\nATOM    266  OH  TYR A  71      -1.045  11.839  20.381  1.00 99.85           O\\nANISOU  266  OH  TYR A  71    10911  18103   8926  -2541   2275  -1429       O\\nATOM    267  N   LEU A  72       4.963  10.950  14.139  1.00 66.28           N\\nANISOU  267  N   LEU A  72     8155  10205   6825  -1355    960   -134       N\\nATOM    268  CA  LEU A  72       5.688  10.938  12.880  1.00 65.47           C\\nANISOU  268  CA  LEU A  72     8142   9678   7057  -1158    810    -34       C\\nATOM    269  C   LEU A  72       5.520   9.612  12.156  1.00 66.26           C\\nANISOU  269  C   LEU A  72     8411   9590   7173  -1363    790    218       C\\nATOM    270  O   LEU A  72       5.755   9.545  10.947  1.00 70.26           O\\nANISOU  270  O   LEU A  72     8925   9843   7928  -1232    713    248       O\\nATOM    271  CB  LEU A  72       7.166  11.237  13.129  1.00 68.98           C\\nANISOU  271  CB  LEU A  72     8763   9860   7585   -964    640     32       C\\nATOM    272  CG  LEU A  72       7.464  12.668  13.586  1.00 71.02           C\\nANISOU  272  CG  LEU A  72     8861  10200   7924   -721    600   -231       C\\nATOM    273  CD1 LEU A  72       8.795  12.745  14.308  1.00 68.45           C\\nANISOU  273  CD1 LEU A  72     8719   9732   7557   -638    454   -157       C\\nATOM    274  CD2 LEU A  72       7.449  13.618  12.399  1.00 69.98           C\\nANISOU  274  CD2 LEU A  72     8565   9884   8138   -488    531   -351       C\\nATOM    275  N   ILE A  73       5.112   8.562  12.866  1.00 69.01           N\\nANISOU  275  N   ILE A  73     8906  10062   7254  -1697    844    397       N\\nATOM    276  CA  ILE A  73       4.844   7.288  12.214  1.00 67.68           C\\nANISOU  276  CA  ILE A  73     8907   9691   7118  -1917    795    618       C\\nATOM    277  C   ILE A  73       3.522   7.340  11.460  1.00 71.94           C\\nANISOU  277  C   ILE A  73     9183  10422   7728  -2023    929    489       C\\nATOM    278  O   ILE A  73       3.411   6.809  10.350  1.00 75.02           O\\nANISOU  278  O   ILE A  73     9617  10582   8307  -2015    856    546       O\\nATOM    279  CB  ILE A  73       4.880   6.148  13.249  1.00 69.17           C\\nANISOU  279  CB  ILE A  73     9379   9898   7006  -2275    759    894       C\\nATOM    280  CG1 ILE A  73       6.327   5.743  13.542  1.00 66.13           C\\nANISOU  280  CG1 ILE A  73     9319   9150   6659  -2128    522   1069       C\\nATOM    281  CG2 ILE A  73       4.072   4.944  12.777  1.00 68.47           C\\nANISOU  281  CG2 ILE A  73     9386   9730   6900  -2615    755   1076       C\\nATOM    282  CD1 ILE A  73       6.453   4.548  14.461  1.00 67.07           C\\nANISOU  282  CD1 ILE A  73     9782   9188   6514  -2462    402   1387       C\\nATOM    283  N   VAL A  74       2.507   7.996  12.029  1.00 70.79           N\\nANISOU  283  N   VAL A  74     8739  10720   7436  -2102   1115    280       N\\nATOM    284  CA  VAL A  74       1.244   8.128  11.308  1.00 74.58           C\\nANISOU  284  CA  VAL A  74     8921  11407   8009  -2166   1221    118       C\\nATOM    285  C   VAL A  74       1.392   9.116  10.161  1.00 73.54           C\\nANISOU  285  C   VAL A  74     8633  11099   8211  -1776   1127    -73       C\\nATOM    286  O   VAL A  74       0.708   8.995   9.137  1.00 75.63           O\\nANISOU  286  O   VAL A  74     8769  11334   8631  -1776   1112   -121       O\\nATOM    287  CB  VAL A  74       0.095   8.527  12.256  1.00 73.62           C\\nANISOU  287  CB  VAL A  74     8477  11862   7633  -2350   1446    -95       C\\nATOM    288  CG1 VAL A  74       0.133   7.692  13.523  1.00 69.23           C\\nANISOU  288  CG1 VAL A  74     8110  11512   6684  -2747   1535    127       C\\nATOM    289  CG2 VAL A  74       0.126  10.011  12.581  1.00 69.08           C\\nANISOU  289  CG2 VAL A  74     7641  11478   7130  -1988   1471   -451       C\\nATOM    290  N   SER A  75       2.276  10.106  10.306  1.00 69.43           N\\nANISOU  290  N   SER A  75     8129  10455   7797  -1464   1043   -169       N\\nATOM    291  CA  SER A  75       2.644  10.933   9.164  1.00 66.75           C\\nANISOU  291  CA  SER A  75     7729   9871   7764  -1146    912   -253       C\\nATOM    292  C   SER A  75       3.278  10.082   8.075  1.00 68.29           C\\nANISOU  292  C   SER A  75     8151   9714   8082  -1158    801    -30       C\\nATOM    293  O   SER A  75       3.025  10.291   6.882  1.00 67.91           O\\nANISOU  293  O   SER A  75     8025   9564   8214  -1048    739    -65       O\\nATOM    294  CB  SER A  75       3.595  12.044   9.605  1.00 65.59           C\\nANISOU  294  CB  SER A  75     7599   9627   7697   -876    823   -350       C\\nATOM    295  OG  SER A  75       4.148  12.722   8.492  1.00 65.64           O\\nANISOU  295  OG  SER A  75     7609   9355   7975   -636    678   -344       O\\nATOM    296  N   LEU A  76       4.099   9.107   8.470  1.00 69.61           N\\nANISOU  296  N   LEU A  76     8600   9702   8145  -1281    755    185       N\\nATOM    297  CA  LEU A  76       4.653   8.169   7.503  1.00 70.39           C\\nANISOU  297  CA  LEU A  76     8904   9490   8352  -1284    641    344       C\\nATOM    298  C   LEU A  76       3.555   7.304   6.898  1.00 71.56           C\\nANISOU  298  C   LEU A  76     9015   9685   8488  -1514    675    369       C\\nATOM    299  O   LEU A  76       3.587   6.994   5.700  1.00 67.72           O\\nANISOU  299  O   LEU A  76     8556   9030   8146  -1442    597    372       O\\nATOM    300  CB  LEU A  76       5.725   7.307   8.170  1.00 71.65           C\\nANISOU  300  CB  LEU A  76     9365   9437   8421  -1339    541    534       C\\nATOM    301  CG  LEU A  76       6.488   6.311   7.296  1.00 73.93           C\\nANISOU  301  CG  LEU A  76     9872   9386   8833  -1283    387    648       C\\nATOM    302  CD1 LEU A  76       7.050   6.993   6.057  1.00 66.82           C\\nANISOU  302  CD1 LEU A  76     8859   8395   8135  -1003    352    542       C\\nATOM    303  CD2 LEU A  76       7.598   5.643   8.104  1.00 66.32           C\\nANISOU  303  CD2 LEU A  76     9178   8218   7804  -1274    247    796       C\\nATOM    304  N   ALA A  77       2.567   6.918   7.708  1.00 76.17           N\\nANISOU  304  N   ALA A  77     9525  10531   8886  -1810    794    379       N\\nATOM    305  CA  ALA A  77       1.468   6.103   7.203  1.00 75.85           C\\nANISOU  305  CA  ALA A  77     9422  10562   8836  -2078    825    401       C\\nATOM    306  C   ALA A  77       0.603   6.875   6.217  1.00 76.40           C\\nANISOU  306  C   ALA A  77     9182  10781   9066  -1929    853    183       C\\nATOM    307  O   ALA A  77       0.034   6.277   5.295  1.00 74.94           O\\nANISOU  307  O   ALA A  77     8980  10529   8965  -2027    802    189       O\\nATOM    308  CB  ALA A  77       0.618   5.589   8.364  1.00 77.54           C\\nANISOU  308  CB  ALA A  77     9590  11086   8784  -2476    967    470       C\\nATOM    309  N   VAL A  78       0.484   8.192   6.395  1.00 72.57           N\\nANISOU  309  N   VAL A  78     8462  10479   8634  -1687    898    -17       N\\nATOM    310  CA  VAL A  78      -0.263   9.001   5.438  1.00 73.72           C\\nANISOU  310  CA  VAL A  78     8340  10714   8956  -1502    861   -213       C\\nATOM    311  C   VAL A  78       0.492   9.092   4.118  1.00 73.77           C\\nANISOU  311  C   VAL A  78     8495  10392   9143  -1286    699   -137       C\\nATOM    312  O   VAL A  78      -0.108   9.025   3.037  1.00 75.36           O\\nANISOU  312  O   VAL A  78     8606  10583   9444  -1265    631   -185       O\\nATOM    313  CB  VAL A  78      -0.556  10.391   6.030  1.00 69.67           C\\nANISOU  313  CB  VAL A  78     7563  10433   8477  -1281    899   -460       C\\nATOM    314  CG1 VAL A  78      -1.042  11.346   4.951  1.00 67.83           C\\nANISOU  314  CG1 VAL A  78     7129  10169   8475  -1016    769   -625       C\\nATOM    315  CG2 VAL A  78      -1.591  10.281   7.138  1.00 54.88           C\\nANISOU  315  CG2 VAL A  78     5447   9002   6402  -1505   1086   -609       C\\nATOM    316  N   ALA A  79       1.819   9.239   4.180  1.00 71.40           N\\nANISOU  316  N   ALA A  79     8408   9854   8865  -1136    637    -25       N\\nATOM    317  CA  ALA A  79       2.617   9.243   2.959  1.00 72.25           C\\nANISOU  317  CA  ALA A  79     8642   9715   9095   -969    515     48       C\\nATOM    318  C   ALA A  79       2.382   7.976   2.148  1.00 78.12           C\\nANISOU  318  C   ALA A  79     9512  10348   9824  -1122    472    118       C\\nATOM    319  O   ALA A  79       2.254   8.030   0.919  1.00 82.23           O\\nANISOU  319  O   ALA A  79    10005  10818  10420  -1035    394     87       O\\nATOM    320  CB  ALA A  79       4.097   9.398   3.301  1.00 67.24           C\\nANISOU  320  CB  ALA A  79     8191   8894   8464   -836    476    149       C\\nATOM    321  N   ASP A  80       2.306   6.826   2.820  1.00 70.96           N\\nANISOU  321  N   ASP A  80     8756   9392   8812  -1362    499    214       N\\nATOM    322  CA  ASP A  80       2.041   5.580   2.113  1.00 74.85           C\\nANISOU  322  CA  ASP A  80     9387   9736   9318  -1522    420    263       C\\nATOM    323  C   ASP A  80       0.578   5.468   1.707  1.00 70.40           C\\nANISOU  323  C   ASP A  80     8610   9377   8763  -1703    452    165       C\\nATOM    324  O   ASP A  80       0.275   4.919   0.641  1.00 75.04           O\\nANISOU  324  O   ASP A  80     9225   9874   9413  -1725    358    129       O\\nATOM    325  CB  ASP A  80       2.453   4.386   2.975  1.00 85.13           C\\nANISOU  325  CB  ASP A  80    10957  10859  10529  -1735    379    424       C\\nATOM    326  CG  ASP A  80       3.955   4.316   3.193  1.00 91.73           C\\nANISOU  326  CG  ASP A  80    12008  11459  11389  -1526    293    497       C\\nATOM    327  OD1 ASP A  80       4.707   4.814   2.326  1.00 90.12           O\\nANISOU  327  OD1 ASP A  80    11774  11187  11279  -1257    253    424       O\\nATOM    328  OD2 ASP A  80       4.383   3.762   4.231  1.00 93.76           O\\nANISOU  328  OD2 ASP A  80    12452  11616  11555  -1644    259    631       O\\nATOM    329  N   LEU A  81      -0.340   5.974   2.535  1.00 74.65           N\\nANISOU  329  N   LEU A  81     8912  10218   9233  -1827    580     91       N\\nATOM    330  CA  LEU A  81      -1.751   5.961   2.159  1.00 71.55           C\\nANISOU  330  CA  LEU A  81     8249  10074   8865  -1978    612    -40       C\\nATOM    331  C   LEU A  81      -2.001   6.765   0.893  1.00 74.65           C\\nANISOU  331  C   LEU A  81     8488  10471   9406  -1709    505   -178       C\\nATOM    332  O   LEU A  81      -2.886   6.418   0.105  1.00 69.21           O\\nANISOU  332  O   LEU A  81     7680   9851   8766  -1803    444   -254       O\\nATOM    333  CB  LEU A  81      -2.611   6.504   3.297  1.00 69.87           C\\nANISOU  333  CB  LEU A  81     7752  10250   8545  -2106    782   -153       C\\nATOM    334  CG  LEU A  81      -3.075   5.485   4.331  1.00 74.99           C\\nANISOU  334  CG  LEU A  81     8452  11043   8999  -2544    901    -27       C\\nATOM    335  CD1 LEU A  81      -3.852   6.179   5.437  1.00 74.69           C\\nANISOU  335  CD1 LEU A  81     8087  11477   8814  -2632   1099   -186       C\\nATOM    336  CD2 LEU A  81      -3.924   4.409   3.669  1.00 73.03           C\\nANISOU  336  CD2 LEU A  81     8197  10767   8785  -2854    842     14       C\\nATOM    337  N   LEU A  82      -1.237   7.838   0.678  1.00 69.87           N\\nANISOU  337  N   LEU A  82     7892   9789   8867  -1397    460   -196       N\\nATOM    338  CA  LEU A  82      -1.409   8.637  -0.529  1.00 65.99           C\\nANISOU  338  CA  LEU A  82     7299   9280   8492  -1167    327   -272       C\\nATOM    339  C   LEU A  82      -0.757   7.982  -1.740  1.00 70.21           C\\nANISOU  339  C   LEU A  82     8057   9596   9025  -1131    218   -180       C\\nATOM    340  O   LEU A  82      -1.178   8.231  -2.875  1.00 71.57           O\\nANISOU  340  O   LEU A  82     8160   9794   9239  -1047    101   -233       O\\nATOM    341  CB  LEU A  82      -0.848  10.040  -0.313  1.00 59.37           C\\nANISOU  341  CB  LEU A  82     6407   8421   7728   -892    291   -300       C\\nATOM    342  CG  LEU A  82      -1.644  10.851   0.706  1.00 62.33           C\\nANISOU  342  CG  LEU A  82     6510   9044   8130   -856    360   -482       C\\nATOM    343  CD1 LEU A  82      -1.091  12.261   0.855  1.00 55.10           C\\nANISOU  343  CD1 LEU A  82     5564   8044   7327   -570    267   -530       C\\nATOM    344  CD2 LEU A  82      -3.114  10.883   0.314  1.00 64.42           C\\nANISOU  344  CD2 LEU A  82     6475   9550   8451   -907    325   -667       C\\nATOM    345  N   VAL A  83       0.261   7.147  -1.524  1.00 71.76           N\\nANISOU  345  N   VAL A  83     8510   9592   9162  -1179    238    -64       N\\nATOM    346  CA  VAL A  83       0.813   6.355  -2.620  1.00 69.53           C\\nANISOU  346  CA  VAL A  83     8414   9139   8867  -1147    140    -43       C\\nATOM    347  C   VAL A  83      -0.238   5.394  -3.158  1.00 73.89           C\\nANISOU  347  C   VAL A  83     8937   9715   9422  -1353     76   -116       C\\nATOM    348  O   VAL A  83      -0.404   5.247  -4.375  1.00 79.13           O\\nANISOU  348  O   VAL A  83     9606  10373  10087  -1289    -32   -185       O\\nATOM    349  CB  VAL A  83       2.078   5.608  -2.159  1.00 61.51           C\\nANISOU  349  CB  VAL A  83     7653   7900   7818  -1130    147     49       C\\nATOM    350  CG1 VAL A  83       2.537   4.623  -3.222  1.00 56.33           C\\nANISOU  350  CG1 VAL A  83     7164   7084   7153  -1094     37      1       C\\nATOM    351  CG2 VAL A  83       3.187   6.592  -1.827  1.00 55.01           C\\nANISOU  351  CG2 VAL A  83     6836   7065   7001   -921    189    106       C\\nATOM    352  N   ALA A  84      -0.973   4.732  -2.264  1.00 63.07           N\\nANISOU  352  N   ALA A  84     7532   8393   8036  -1628    136   -100       N\\nATOM    353  CA  ALA A  84      -1.979   3.777  -2.713  1.00 68.51           C\\nANISOU  353  CA  ALA A  84     8190   9097   8744  -1877     65   -159       C\\nATOM    354  C   ALA A  84      -3.109   4.458  -3.475  1.00 67.78           C\\nANISOU  354  C   ALA A  84     7803   9251   8701  -1831     21   -306       C\\nATOM    355  O   ALA A  84      -3.668   3.871  -4.408  1.00 63.21           O\\nANISOU  355  O   ALA A  84     7217   8653   8146  -1911   -101   -386       O\\nATOM    356  CB  ALA A  84      -2.540   3.003  -1.520  1.00 70.03           C\\nANISOU  356  CB  ALA A  84     8393   9327   8888  -2241    149    -72       C\\nATOM    357  N   THR A  85      -3.449   5.692  -3.108  1.00 59.88           N\\nANISOU  357  N   THR A  85     6561   8463   7726  -1685     85   -362       N\\nATOM    358  CA  THR A  85      -4.630   6.368  -3.632  1.00 70.05           C\\nANISOU  358  CA  THR A  85     7536   9994   9087  -1632     16   -521       C\\nATOM    359  C   THR A  85      -4.329   7.352  -4.758  1.00 73.23           C\\nANISOU  359  C   THR A  85     7938  10354   9531  -1316   -140   -540       C\\nATOM    360  O   THR A  85      -5.144   7.493  -5.674  1.00 73.60           O\\nANISOU  360  O   THR A  85     7844  10501   9619  -1283   -285   -640       O\\nATOM    361  CB  THR A  85      -5.355   7.103  -2.501  1.00 66.86           C\\nANISOU  361  CB  THR A  85     6829   9873   8704  -1660    148   -625       C\\nATOM    362  OG1 THR A  85      -4.432   7.958  -1.812  1.00 68.22           O\\nANISOU  362  OG1 THR A  85     7080   9977   8864  -1454    215   -567       O\\nATOM    363  CG2 THR A  85      -5.948   6.109  -1.519  1.00 61.69           C\\nANISOU  363  CG2 THR A  85     6117   9358   7964  -2054    299   -604       C\\nATOM    364  N   LEU A  86      -3.186   8.043  -4.718  1.00 62.95           N\\nANISOU  364  N   LEU A  86     6792   8914   8211  -1106   -129   -431       N\\nATOM    365  CA  LEU A  86      -2.875   9.074  -5.699  1.00 69.96           C\\nANISOU  365  CA  LEU A  86     7691   9770   9119   -857   -279   -398       C\\nATOM    366  C   LEU A  86      -1.823   8.663  -6.718  1.00 73.74           C\\nANISOU  366  C   LEU A  86     8430  10102   9484   -805   -327   -290       C\\nATOM    367  O   LEU A  86      -1.627   9.386  -7.700  1.00 78.44           O\\nANISOU  367  O   LEU A  86     9050  10709  10044   -662   -458   -237       O\\nATOM    368  CB  LEU A  86      -2.400  10.356  -5.000  1.00 71.90           C\\nANISOU  368  CB  LEU A  86     7888   9995   9438   -669   -260   -361       C\\nATOM    369  CG  LEU A  86      -3.358  11.015  -4.012  1.00 70.39           C\\nANISOU  369  CG  LEU A  86     7407   9983   9357   -640   -226   -527       C\\nATOM    370  CD1 LEU A  86      -2.805  12.358  -3.572  1.00 66.08           C\\nANISOU  370  CD1 LEU A  86     6851   9355   8902   -408   -280   -511       C\\nATOM    371  CD2 LEU A  86      -4.735  11.169  -4.633  1.00 73.10           C\\nANISOU  371  CD2 LEU A  86     7488  10505   9781   -625   -371   -694       C\\nATOM    372  N   VAL A  87      -1.137   7.538  -6.512  1.00 71.08           N\\nANISOU  372  N   VAL A  87     8285   9640   9081   -916   -240   -262       N\\nATOM    373  CA  VAL A  87      -0.068   7.087  -7.395  1.00 73.29           C\\nANISOU  373  CA  VAL A  87     8777   9820   9251   -840   -268   -222       C\\nATOM    374  C   VAL A  87      -0.364   5.702  -7.963  1.00 77.64           C\\nANISOU  374  C   VAL A  87     9430  10309   9760   -973   -330   -334       C\\nATOM    375  O   VAL A  87      -0.313   5.497  -9.179  1.00 73.98           O\\nANISOU  375  O   VAL A  87     9018   9892   9199   -916   -433   -399       O\\nATOM    376  CB  VAL A  87       1.295   7.094  -6.673  1.00 71.74           C\\nANISOU  376  CB  VAL A  87     8723   9494   9039   -769   -152   -126       C\\nATOM    377  CG1 VAL A  87       2.408   6.688  -7.635  1.00 74.66           C\\nANISOU  377  CG1 VAL A  87     9249   9829   9290   -667   -171   -133       C\\nATOM    378  CG2 VAL A  87       1.561   8.458  -6.054  1.00 66.12           C\\nANISOU  378  CG2 VAL A  87     7914   8818   8388   -656   -114    -33       C\\nATOM    379  N   MET A  88      -0.666   4.743  -7.091  1.00 80.11           N\\nANISOU  379  N   MET A  88     9788  10515  10136  -1166   -284   -354       N\\nATOM    380  CA  MET A  88      -0.910   3.374  -7.543  1.00 77.27           C\\nANISOU  380  CA  MET A  88     9560  10025   9773  -1313   -382   -456       C\\nATOM    381  C   MET A  88      -2.014   3.257  -8.587  1.00 74.77           C\\nANISOU  381  C   MET A  88     9120   9842   9447  -1377   -521   -585       C\\nATOM    382  O   MET A  88      -1.856   2.434  -9.508  1.00 75.54           O\\nANISOU  382  O   MET A  88     9351   9858   9492  -1370   -641   -704       O\\nATOM    383  CB  MET A  88      -1.213   2.478  -6.335  1.00 80.86           C\\nANISOU  383  CB  MET A  88    10082  10339  10303  -1575   -337   -400       C\\nATOM    384  CG  MET A  88      -0.060   2.322  -5.349  1.00 81.25           C\\nANISOU  384  CG  MET A  88    10311  10211  10350  -1521   -256   -278       C\\nATOM    385  SD  MET A  88       1.427   1.569  -6.040  1.00 83.45           S\\nANISOU  385  SD  MET A  88    10860  10245  10603  -1297   -355   -350       S\\nATOM    386  CE  MET A  88       0.780   0.002  -6.622  1.00 86.55           C\\nANISOU  386  CE  MET A  88    11408  10421  11056  -1493   -560   -493       C\\nATOM    387  N   PRO A  89      -3.134   3.998  -8.521  1.00 73.85           N\\nANISOU  387  N   PRO A  89     8745   9932   9382  -1424   -534   -603       N\\nATOM    388  CA  PRO A  89      -4.103   3.930  -9.629  1.00 74.48           C\\nANISOU  388  CA  PRO A  89     8707  10146   9448  -1448   -704   -735       C\\nATOM    389  C   PRO A  89      -3.480   4.213 -10.985  1.00 73.67           C\\nANISOU  389  C   PRO A  89     8725  10074   9192  -1237   -816   -758       C\\nATOM    390  O   PRO A  89      -3.834   3.559 -11.972  1.00 74.04           O\\nANISOU  390  O   PRO A  89     8817  10141   9174  -1277   -962   -893       O\\nATOM    391  CB  PRO A  89      -5.142   4.990  -9.248  1.00 73.14           C\\nANISOU  391  CB  PRO A  89     8221  10200   9368  -1431   -703   -747       C\\nATOM    392  CG  PRO A  89      -5.085   5.041  -7.779  1.00 71.74           C\\nANISOU  392  CG  PRO A  89     7982  10016   9258  -1543   -514   -680       C\\nATOM    393  CD  PRO A  89      -3.645   4.834  -7.418  1.00 67.98           C\\nANISOU  393  CD  PRO A  89     7787   9325   8719  -1455   -417   -550       C\\nATOM    394  N   TRP A  90      -2.552   5.170 -11.056  1.00 69.93           N\\nANISOU  394  N   TRP A  90     8302   9624   8643  -1037   -753   -630       N\\nATOM    395  CA  TRP A  90      -1.831   5.402 -12.301  1.00 70.06           C\\nANISOU  395  CA  TRP A  90     8440   9716   8463   -885   -824   -623       C\\nATOM    396  C   TRP A  90      -0.927   4.229 -12.652  1.00 73.43           C\\nANISOU  396  C   TRP A  90     9074  10033   8794   -879   -795   -740       C\\nATOM    397  O   TRP A  90      -0.713   3.948 -13.836  1.00 80.52           O\\nANISOU  397  O   TRP A  90    10046  11036   9511   -815   -885   -849       O\\nATOM    398  CB  TRP A  90      -0.996   6.677 -12.206  1.00 72.68           C\\nANISOU  398  CB  TRP A  90     8778  10094   8744   -730   -758   -431       C\\nATOM    399  CG  TRP A  90      -1.743   7.924 -11.827  1.00 78.23           C\\nANISOU  399  CG  TRP A  90     9301  10853   9571   -681   -825   -337       C\\nATOM    400  CD1 TRP A  90      -2.061   8.338 -10.567  1.00 78.70           C\\nANISOU  400  CD1 TRP A  90     9229  10858   9814   -696   -738   -319       C\\nATOM    401  CD2 TRP A  90      -2.229   8.939 -12.716  1.00 88.37           C\\nANISOU  401  CD2 TRP A  90    10523  12253  10801   -588  -1022   -264       C\\nATOM    402  NE1 TRP A  90      -2.729   9.539 -10.616  1.00 79.87           N\\nANISOU  402  NE1 TRP A  90     9218  11075  10052   -589   -872   -284       N\\nATOM    403  CE2 TRP A  90      -2.844   9.929 -11.925  1.00 85.91           C\\nANISOU  403  CE2 TRP A  90    10036  11918  10690   -521  -1067   -232       C\\nATOM    404  CE3 TRP A  90      -2.213   9.101 -14.106  1.00 93.09           C\\nANISOU  404  CE3 TRP A  90    11205  12978  11187   -553  -1185   -228       C\\nATOM    405  CZ2 TRP A  90      -3.436  11.064 -12.476  1.00 91.05           C\\nANISOU  405  CZ2 TRP A  90    10603  12614  11379   -398  -1303   -166       C\\nATOM    406  CZ3 TRP A  90      -2.801  10.229 -14.651  1.00 88.71           C\\nANISOU  406  CZ3 TRP A  90    10584  12483  10637   -467  -1412   -117       C\\nATOM    407  CH2 TRP A  90      -3.404  11.195 -13.838  1.00 91.05           C\\nANISOU  407  CH2 TRP A  90    10716  12700  11179   -380  -1486    -87       C\\nATOM    408  N   VAL A  91      -0.382   3.540 -11.646  1.00 69.25           N\\nANISOU  408  N   VAL A  91     8640   9297   8374   -930   -690   -736       N\\nATOM    409  CA  VAL A  91       0.555   2.453 -11.912  1.00 71.26           C\\nANISOU  409  CA  VAL A  91     9090   9406   8578   -872   -701   -873       C\\nATOM    410  C   VAL A  91      -0.181   1.188 -12.341  1.00 81.86           C\\nANISOU  410  C   VAL A  91    10506  10626   9969  -1010   -867  -1076       C\\nATOM    411  O   VAL A  91       0.272   0.468 -13.239  1.00 84.97           O\\nANISOU  411  O   VAL A  91    11020  11005  10261   -913   -961  -1279       O\\nATOM    412  CB  VAL A  91       1.447   2.203 -10.683  1.00 66.23           C\\nANISOU  412  CB  VAL A  91     8549   8562   8051   -856   -583   -782       C\\nATOM    413  CG1 VAL A  91       2.331   0.984 -10.905  1.00 66.75           C\\nANISOU  413  CG1 VAL A  91     8812   8434   8116   -769   -652   -961       C\\nATOM    414  CG2 VAL A  91       2.295   3.427 -10.395  1.00 71.66           C\\nANISOU  414  CG2 VAL A  91     9171   9373   8685   -712   -442   -614       C\\nATOM    415  N   VAL A  92      -1.320   0.890 -11.713  1.00 76.99           N\\nANISOU  415  N   VAL A  92     9808   9938   9507  -1247   -911  -1047       N\\nATOM    416  CA  VAL A  92      -2.100  -0.267 -12.139  1.00 83.11           C\\nANISOU  416  CA  VAL A  92    10641  10591  10346  -1426  -1092  -1225       C\\nATOM    417  C   VAL A  92      -2.714  -0.014 -13.513  1.00 85.39           C\\nANISOU  417  C   VAL A  92    10837  11112  10496  -1365  -1232  -1373       C\\nATOM    418  O   VAL A  92      -2.760  -0.914 -14.362  1.00 87.20           O\\nANISOU  418  O   VAL A  92    11179  11274  10677  -1366  -1396  -1596       O\\nATOM    419  CB  VAL A  92      -3.160  -0.626 -11.077  1.00 86.97           C\\nANISOU  419  CB  VAL A  92    11035  10994  11015  -1752  -1083  -1133       C\\nATOM    420  CG1 VAL A  92      -4.059   0.557 -10.774  1.00 88.40           C\\nANISOU  420  CG1 VAL A  92    10916  11464  11208  -1788   -990  -1030       C\\nATOM    421  CG2 VAL A  92      -3.984  -1.823 -11.526  1.00 90.14           C\\nANISOU  421  CG2 VAL A  92    11495  11253  11500  -1988  -1291  -1301       C\\nATOM    422  N   TYR A  93      -3.173   1.217 -13.762  1.00 86.77           N\\nANISOU  422  N   TYR A  93    10817  11548  10602  -1298  -1201  -1261       N\\nATOM    423  CA  TYR A  93      -3.600   1.598 -15.106  1.00 83.84           C\\nANISOU  423  CA  TYR A  93    10389  11409  10056  -1209  -1354  -1357       C\\nATOM    424  C   TYR A  93      -2.477   1.379 -16.111  1.00 80.40           C\\nANISOU  424  C   TYR A  93    10133  11042   9375  -1017  -1359  -1466       C\\nATOM    425  O   TYR A  93      -2.706   0.878 -17.219  1.00 74.40           O\\nANISOU  425  O   TYR A  93     9423  10381   8465   -997  -1517  -1669       O\\nATOM    426  CB  TYR A  93      -4.062   3.059 -15.102  1.00 86.78           C\\nANISOU  426  CB  TYR A  93    10567  11993  10412  -1130  -1345  -1178       C\\nATOM    427  CG  TYR A  93      -4.289   3.683 -16.465  1.00 96.56           C\\nANISOU  427  CG  TYR A  93    11788  13469  11430  -1012  -1516  -1193       C\\nATOM    428  CD1 TYR A  93      -5.528   3.603 -17.096  1.00 94.66           C\\nANISOU  428  CD1 TYR A  93    11412  13349  11207  -1088  -1737  -1310       C\\nATOM    429  CD2 TYR A  93      -3.274   4.383 -17.106  1.00 98.40           C\\nANISOU  429  CD2 TYR A  93    12135  13829  11423   -849  -1468  -1073       C\\nATOM    430  CE1 TYR A  93      -5.739   4.185 -18.334  1.00 95.59           C\\nANISOU  430  CE1 TYR A  93    11537  13682  11100   -983  -1926  -1302       C\\nATOM    431  CE2 TYR A  93      -3.475   4.965 -18.343  1.00 97.04           C\\nANISOU  431  CE2 TYR A  93    11974  13889  11007   -780  -1636  -1042       C\\nATOM    432  CZ  TYR A  93      -4.707   4.864 -18.952  1.00 96.39           C\\nANISOU  432  CZ  TYR A  93    11785  13900  10937   -837  -1876  -1153       C\\nATOM    433  OH  TYR A  93      -4.903   5.446 -20.182  1.00 95.53           O\\nANISOU  433  OH  TYR A  93    11712  14022  10562   -771  -2074  -1102       O\\nATOM    434  N   LEU A  94      -1.250   1.724 -15.722  1.00 88.56           N\\nANISOU  434  N   LEU A  94    11244  12051  10355   -879  -1185  -1358       N\\nATOM    435  CA  LEU A  94      -0.090   1.590 -16.592  1.00 90.25           C\\nANISOU  435  CA  LEU A  94    11571  12398  10320   -698  -1144  -1470       C\\nATOM    436  C   LEU A  94       0.187   0.143 -16.984  1.00 86.74           C\\nANISOU  436  C   LEU A  94    11276  11802   9879   -668  -1251  -1798       C\\nATOM    437  O   LEU A  94       0.806  -0.096 -18.027  1.00 79.60           O\\nANISOU  437  O   LEU A  94    10426  11091   8726   -524  -1274  -1999       O\\nATOM    438  CB  LEU A  94       1.131   2.192 -15.893  1.00 91.19           C\\nANISOU  438  CB  LEU A  94    11704  12504  10440   -587   -935  -1297       C\\nATOM    439  CG  LEU A  94       2.362   2.481 -16.745  1.00 96.59           C\\nANISOU  439  CG  LEU A  94    12420  13445  10836   -422   -839  -1342       C\\nATOM    440  CD1 LEU A  94       1.952   3.241 -17.987  1.00 95.48           C\\nANISOU  440  CD1 LEU A  94    12233  13639  10407   -435   -921  -1281       C\\nATOM    441  CD2 LEU A  94       3.366   3.277 -15.931  1.00 94.01           C\\nANISOU  441  CD2 LEU A  94    12057  13105  10556   -364   -648  -1120       C\\nATOM    442  N   GLU A  95      -0.244  -0.827 -16.175  1.00 91.64           N\\nANISOU  442  N   GLU A  95    11967  12086  10767   -809  -1328  -1863       N\\nATOM    443  CA  GLU A  95      -0.007  -2.228 -16.505  1.00 89.73           C\\nANISOU  443  CA  GLU A  95    11897  11617  10578   -779  -1491  -2179       C\\nATOM    444  C   GLU A  95      -1.104  -2.803 -17.392  1.00 87.68           C\\nANISOU  444  C   GLU A  95    11631  11388  10293   -904  -1724  -2391       C\\nATOM    445  O   GLU A  95      -0.812  -3.568 -18.317  1.00 89.77           O\\nANISOU  445  O   GLU A  95    12002  11667  10441   -784  -1865  -2717       O\\nATOM    446  CB  GLU A  95       0.121  -3.065 -15.229  1.00 87.59           C\\nANISOU  446  CB  GLU A  95    11758  10917  10607   -899  -1515  -2120       C\\nATOM    447  CG  GLU A  95       0.439  -4.539 -15.480  1.00 93.67           C\\nANISOU  447  CG  GLU A  95    12747  11357  11487   -851  -1741  -2438       C\\nATOM    448  CD  GLU A  95       1.851  -4.758 -16.002  1.00102.62           C\\nANISOU  448  CD  GLU A  95    13952  12557  12482   -504  -1707  -2681       C\\nATOM    449  OE1 GLU A  95       2.722  -3.902 -15.740  1.00104.20           O\\nANISOU  449  OE1 GLU A  95    14062  12957  12571   -357  -1484  -2527       O\\nATOM    450  OE2 GLU A  95       2.093  -5.788 -16.670  1.00107.64           O\\nANISOU  450  OE2 GLU A  95    14717  13056  13125   -376  -1910  -3051       O\\nATOM    451  N   VAL A  96      -2.362  -2.449 -17.129  1.00 78.94           N\\nANISOU  451  N   VAL A  96    10382  10316   9297  -1131  -1774  -2245       N\\nATOM    452  CA  VAL A  96      -3.462  -2.952 -17.947  1.00 80.52           C\\nANISOU  452  CA  VAL A  96    10543  10563   9488  -1267  -2011  -2444       C\\nATOM    453  C   VAL A  96      -3.331  -2.439 -19.375  1.00 85.05           C\\nANISOU  453  C   VAL A  96    11087  11511   9717  -1081  -2072  -2578       C\\nATOM    454  O   VAL A  96      -3.404  -3.209 -20.340  1.00 82.90           O\\nANISOU  454  O   VAL A  96    10906  11266   9327  -1037  -2258  -2893       O\\nATOM    455  CB  VAL A  96      -4.816  -2.561 -17.328  1.00 77.18           C\\nANISOU  455  CB  VAL A  96     9907  10166   9251  -1538  -2032  -2265       C\\nATOM    456  N   VAL A  97      -3.117  -1.130 -19.528  1.00 87.40           N\\nANISOU  456  N   VAL A  97    11271  12099   9836   -979  -1932  -2336       N\\nATOM    457  CA  VAL A  97      -2.995  -0.529 -20.854  1.00 88.86           C\\nANISOU  457  CA  VAL A  97    11446  12664   9653   -847  -1994  -2384       C\\nATOM    458  C   VAL A  97      -1.719  -0.983 -21.554  1.00 90.16           C\\nANISOU  458  C   VAL A  97    11752  12956   9548   -647  -1919  -2608       C\\nATOM    459  O   VAL A  97      -1.694  -1.122 -22.783  1.00 92.93           O\\nANISOU  459  O   VAL A  97    12140  13588   9583   -572  -2028  -2817       O\\nATOM    460  CB  VAL A  97      -3.061   1.005 -20.740  1.00 86.80           C\\nANISOU  460  CB  VAL A  97    11060  12617   9305   -817  -1897  -2025       C\\nATOM    461  CG1 VAL A  97      -2.893   1.659 -22.106  1.00 88.76           C\\nANISOU  461  CG1 VAL A  97    11335  13252   9139   -721  -1981  -2009       C\\nATOM    462  CG2 VAL A  97      -4.372   1.434 -20.086  1.00 86.16           C\\nANISOU  462  CG2 VAL A  97    10792  12448   9495   -970  -1990  -1884       C\\nATOM    463  N   GLY A  98      -0.650  -1.230 -20.800  1.00 88.15           N\\nANISOU  463  N   GLY A  98    11562  12531   9400   -550  -1740  -2596       N\\nATOM    464  CA  GLY A  98       0.613  -1.604 -21.402  1.00 89.34           C\\nANISOU  464  CA  GLY A  98    11789  12846   9310   -334  -1652  -2837       C\\nATOM    465  C   GLY A  98       1.360  -0.469 -22.059  1.00 91.48           C\\nANISOU  465  C   GLY A  98    11987  13570   9202   -247  -1473  -2660       C\\nATOM    466  O   GLY A  98       2.307  -0.717 -22.810  1.00 93.59           O\\nANISOU  466  O   GLY A  98    12270  14114   9177    -92  -1395  -2892       O\\nATOM    467  N   GLU A  99       0.962   0.772 -21.797  1.00 93.52           N\\nANISOU  467  N   GLU A  99    12159  13918   9455   -352  -1418  -2264       N\\nATOM    468  CA  GLU A  99       1.609   1.938 -22.378  1.00 95.54           C\\nANISOU  468  CA  GLU A  99    12373  14557   9372   -328  -1286  -2022       C\\nATOM    469  C   GLU A  99       1.259   3.151 -21.529  1.00 92.97           C\\nANISOU  469  C   GLU A  99    11976  14105   9244   -422  -1241  -1593       C\\nATOM    470  O   GLU A  99       0.253   3.163 -20.815  1.00 85.82           O\\nANISOU  470  O   GLU A  99    11021  12937   8648   -506  -1345  -1519       O\\nATOM    471  CB  GLU A  99       1.181   2.153 -23.835  1.00 94.86           C\\nANISOU  471  CB  GLU A  99    12308  14866   8868   -355  -1437  -2092       C\\nATOM    472  N   TRP A 100       2.110   4.174 -21.614  1.00 89.68           N\\nANISOU  472  N   TRP A 100    11539  13894   8642   -414  -1089  -1330       N\\nATOM    473  CA  TRP A 100       1.871   5.446 -20.932  1.00 88.27           C\\nANISOU  473  CA  TRP A 100    11308  13606   8625   -483  -1080   -935       C\\nATOM    474  C   TRP A 100       0.892   6.302 -21.742  1.00 91.37           C\\nANISOU  474  C   TRP A 100    11702  14149   8867   -556  -1315   -744       C\\nATOM    475  O   TRP A 100       1.217   7.382 -22.236  1.00 95.09           O\\nANISOU  475  O   TRP A 100    12204  14809   9115   -605  -1334   -453       O\\nATOM    476  CB  TRP A 100       3.188   6.177 -20.702  1.00 86.77           C\\nANISOU  476  CB  TRP A 100    11107  13540   8322   -471   -861   -729       C\\nATOM    477  CG  TRP A 100       4.148   5.471 -19.784  1.00 92.86           C\\nANISOU  477  CG  TRP A 100    11859  14140   9283   -376   -663   -888       C\\nATOM    478  CD1 TRP A 100       4.731   4.252 -19.983  1.00 99.53           C\\nANISOU  478  CD1 TRP A 100    12726  15011  10078   -261   -605  -1253       C\\nATOM    479  CD2 TRP A 100       4.655   5.958 -18.534  1.00 93.04           C\\nANISOU  479  CD2 TRP A 100    11841  13932   9577   -369   -533   -700       C\\nATOM    480  NE1 TRP A 100       5.558   3.944 -18.928  1.00 99.78           N\\nANISOU  480  NE1 TRP A 100    12740  14828  10345   -179   -465  -1286       N\\nATOM    481  CE2 TRP A 100       5.530   4.975 -18.027  1.00 94.10           C\\nANISOU  481  CE2 TRP A 100    11981  13965   9809   -254   -408   -944       C\\nATOM    482  CE3 TRP A 100       4.449   7.125 -17.792  1.00 92.42           C\\nANISOU  482  CE3 TRP A 100    11726  13714   9675   -431   -538   -373       C\\nATOM    483  CZ2 TRP A 100       6.198   5.125 -16.811  1.00 92.35           C\\nANISOU  483  CZ2 TRP A 100    11733  13525   9830   -217   -285   -845       C\\nATOM    484  CZ3 TRP A 100       5.114   7.273 -16.583  1.00 87.83           C\\nANISOU  484  CZ3 TRP A 100    11114  12928   9330   -397   -398   -300       C\\nATOM    485  CH2 TRP A 100       5.977   6.279 -16.107  1.00 90.94           C\\nANISOU  485  CH2 TRP A 100    11517  13244   9792   -299   -271   -522       C\\nATOM    486  N   LYS A 101      -0.329   5.791 -21.877  1.00 95.15           N\\nANISOU  486  N   LYS A 101    12148  14527   9477   -577  -1521   -906       N\\nATOM    487  CA  LYS A 101      -1.365   6.446 -22.678  1.00 96.45           C\\nANISOU  487  CA  LYS A 101    12300  14824   9522   -619  -1798   -787       C\\nATOM    488  C   LYS A 101      -2.121   7.498 -21.869  1.00 98.53           C\\nANISOU  488  C   LYS A 101    12457  14876  10104   -621  -1907   -529       C\\nATOM    489  O   LYS A 101      -3.351   7.502 -21.813  1.00100.15           O\\nANISOU  489  O   LYS A 101    12553  15004  10495   -628  -2120   -595       O\\nATOM    490  CB  LYS A 101      -2.319   5.405 -23.251  1.00 91.01           C\\nANISOU  490  CB  LYS A 101    11597  14158   8826   -638  -1991  -1116       C\\nATOM    491  N   PHE A 102      -1.377   8.397 -21.223  1.00 92.76           N\\nANISOU  491  N   PHE A 102    11736  14060   9449   -605  -1768   -264       N\\nATOM    492  CA  PHE A 102      -1.943   9.593 -20.620  1.00 93.22           C\\nANISOU  492  CA  PHE A 102    11716  13947   9756   -575  -1904    -18       C\\nATOM    493  C   PHE A 102      -1.857  10.735 -21.628  1.00 91.71           C\\nANISOU  493  C   PHE A 102    11641  13918   9287   -599  -2119    289       C\\nATOM    494  O   PHE A 102      -1.422  10.558 -22.768  1.00103.07           O\\nANISOU  494  O   PHE A 102    13204  15642  10313   -665  -2138    313       O\\nATOM    495  CB  PHE A 102      -1.202   9.983 -19.340  1.00 94.22           C\\nANISOU  495  CB  PHE A 102    11808  13862  10129   -551  -1677     95       C\\nATOM    496  CG  PHE A 102      -0.815   8.827 -18.469  1.00 91.97           C\\nANISOU  496  CG  PHE A 102    11490  13455  10000   -556  -1432   -141       C\\nATOM    497  CD1 PHE A 102      -1.737   8.243 -17.618  1.00 88.34           C\\nANISOU  497  CD1 PHE A 102    10903  12822   9841   -574  -1444   -314       C\\nATOM    498  CD2 PHE A 102       0.483   8.344 -18.477  1.00 88.17           C\\nANISOU  498  CD2 PHE A 102    11097  13037   9364   -553  -1204   -181       C\\nATOM    499  CE1 PHE A 102      -1.375   7.184 -16.805  1.00 84.23           C\\nANISOU  499  CE1 PHE A 102    10394  12156   9452   -611  -1257   -481       C\\nATOM    500  CE2 PHE A 102       0.849   7.286 -17.667  1.00 83.36           C\\nANISOU  500  CE2 PHE A 102    10485  12270   8917   -538  -1037   -386       C\\nATOM    501  CZ  PHE A 102      -0.082   6.706 -16.830  1.00 81.83           C\\nANISOU  501  CZ  PHE A 102    10213  11865   9014   -578  -1075   -513       C\\nATOM    502  N   SER A 103      -2.265  11.924 -21.210  1.00 88.70           N\\nANISOU  502  N   SER A 103    11226  13356   9120   -550  -2299    526       N\\nATOM    503  CA  SER A 103      -1.855  13.135 -21.896  1.00 82.43           C\\nANISOU  503  CA  SER A 103    10589  12620   8110   -603  -2476    904       C\\nATOM    504  C   SER A 103      -0.586  13.661 -21.237  1.00 83.13           C\\nANISOU  504  C   SER A 103    10732  12623   8230   -660  -2230   1106       C\\nATOM    505  O   SER A 103      -0.135  13.148 -20.210  1.00 83.31           O\\nANISOU  505  O   SER A 103    10661  12526   8466   -622  -1957    945       O\\nATOM    506  CB  SER A 103      -2.969  14.182 -21.869  1.00 79.20           C\\nANISOU  506  CB  SER A 103    10137  12018   7939   -498  -2879   1043       C\\nATOM    507  OG  SER A 103      -3.335  14.521 -20.542  1.00 76.16           O\\nANISOU  507  OG  SER A 103     9579  11344   8016   -372  -2840    955       O\\nATOM    508  N   ARG A 104       0.009  14.689 -21.845  1.00 84.27           N\\nANISOU  508  N   ARG A 104    11037  12833   8148   -776  -2344   1478       N\\nATOM    509  CA  ARG A 104       1.252  15.212 -21.290  1.00 80.60           C\\nANISOU  509  CA  ARG A 104    10612  12312   7701   -868  -2123   1679       C\\nATOM    510  C   ARG A 104       1.025  15.830 -19.921  1.00 77.44           C\\nANISOU  510  C   ARG A 104    10113  11518   7794   -740  -2150   1682       C\\nATOM    511  O   ARG A 104       1.913  15.783 -19.064  1.00 78.86           O\\nANISOU  511  O   ARG A 104    10250  11620   8096   -755  -1890   1666       O\\nATOM    512  CB  ARG A 104       1.881  16.231 -22.235  1.00 80.66           C\\nANISOU  512  CB  ARG A 104    10815  12469   7362  -1078  -2266   2114       C\\nATOM    513  CG  ARG A 104       3.382  16.383 -22.031  1.00 90.20           C\\nANISOU  513  CG  ARG A 104    12038  13815   8417  -1248  -1948   2260       C\\nATOM    514  CD  ARG A 104       3.766  17.736 -21.446  1.00101.17           C\\nANISOU  514  CD  ARG A 104    13504  14894  10041  -1329  -2089   2624       C\\nATOM    515  NE  ARG A 104       3.451  18.831 -22.359  1.00106.68           N\\nANISOU  515  NE  ARG A 104    14414  15562  10556  -1484  -2476   3046       N\\nATOM    516  CZ  ARG A 104       2.650  19.849 -22.059  1.00108.76           C\\nANISOU  516  CZ  ARG A 104    14758  15416  11150  -1381  -2885   3220       C\\nATOM    517  NH1 ARG A 104       2.092  19.927 -20.857  1.00104.63           N\\nANISOU  517  NH1 ARG A 104    14088  14533  11136  -1126  -2918   2984       N\\nATOM    518  NH2 ARG A 104       2.417  20.795 -22.961  1.00112.28           N\\nANISOU  518  NH2 ARG A 104    15433  15822  11408  -1532  -3275   3626       N\\nATOM    519  N   ILE A 105      -0.160  16.392 -19.688  1.00 79.98           N\\nANISOU  519  N   ILE A 105    10379  11613   8397   -597  -2469   1666       N\\nATOM    520  CA  ILE A 105      -0.435  17.000 -18.394  1.00 78.38           C\\nANISOU  520  CA  ILE A 105    10057  11079   8646   -452  -2502   1613       C\\nATOM    521  C   ILE A 105      -0.797  15.939 -17.359  1.00 74.85           C\\nANISOU  521  C   ILE A 105     9401  10617   8423   -355  -2239   1232       C\\nATOM    522  O   ILE A 105      -0.422  16.063 -16.189  1.00 73.96           O\\nANISOU  522  O   ILE A 105     9211  10343   8549   -307  -2066   1171       O\\nATOM    523  CB  ILE A 105      -1.528  18.076 -18.534  1.00 77.26           C\\nANISOU  523  CB  ILE A 105     9910  10715   8730   -308  -2966   1710       C\\nATOM    524  CG1 ILE A 105      -1.691  18.858 -17.227  1.00 76.93           C\\nANISOU  524  CG1 ILE A 105     9750  10345   9133   -142  -3017   1643       C\\nATOM    525  CG2 ILE A 105      -2.847  17.465 -18.989  1.00 71.80           C\\nANISOU  525  CG2 ILE A 105     9083  10142   8055   -199  -3143   1458       C\\nATOM    526  CD1 ILE A 105      -0.522  19.761 -16.903  1.00 63.79           C\\nANISOU  526  CD1 ILE A 105     8244   8504   7489   -248  -2982   1938       C\\nATOM    527  N   HIS A 106      -1.425  14.862 -17.789  1.00 78.10           N\\nANISOU  527  N   HIS A 106     9732  11194   8747   -350  -2214    984       N\\nATOM    528  CA  HIS A 106      -1.751  13.780 -16.889  1.00 72.04           C\\nANISOU  528  CA  HIS A 106     8805  10412   8157   -326  -1967    668       C\\nATOM    529  C   HIS A 106      -0.480  13.081 -16.470  1.00 75.28           C\\nANISOU  529  C   HIS A 106     9289  10863   8451   -409  -1617    644       C\\nATOM    530  O   HIS A 106      -0.345  12.663 -15.351  1.00 70.37           O\\nANISOU  530  O   HIS A 106     8580  10125   8032   -389  -1418    503       O\\nATOM    531  CB  HIS A 106      -2.690  12.806 -17.558  1.00 69.03           C\\nANISOU  531  CB  HIS A 106     8344  10182   7701   -344  -2050    426       C\\nATOM    532  CG  HIS A 106      -4.109  13.257 -17.558  1.00 86.66           C\\nANISOU  532  CG  HIS A 106    10420  12382  10122   -239  -2375    359       C\\nATOM    533  ND1 HIS A 106      -4.497  14.469 -17.043  1.00 93.53           N\\nANISOU  533  ND1 HIS A 106    11265  13098  11175   -109  -2634    518       N\\nATOM    534  CD2 HIS A 106      -5.234  12.662 -18.003  1.00 92.54           C\\nANISOU  534  CD2 HIS A 106    11011  13228  10921   -235  -2507    125       C\\nATOM    535  CE1 HIS A 106      -5.801  14.602 -17.170  1.00 95.16           C\\nANISOU  535  CE1 HIS A 106    11292  13325  11539     -1  -2912    369       C\\nATOM    536  NE2 HIS A 106      -6.273  13.520 -17.751  1.00 94.46           N\\nANISOU  536  NE2 HIS A 106    11111  13409  11371    -89  -2829    134       N\\nATOM    537  N   CYS A 107       0.459  12.953 -17.384  1.00 74.40           N\\nANISOU  537  N   CYS A 107     9326  10942   8001   -501  -1547    768       N\\nATOM    538  CA  CYS A 107       1.750  12.355 -17.073  1.00 74.41           C\\nANISOU  538  CA  CYS A 107     9366  11008   7898   -548  -1239    725       C\\nATOM    539  C   CYS A 107       2.520  13.220 -16.082  1.00 69.26           C\\nANISOU  539  C   CYS A 107     8705  10174   7436   -541  -1146    902       C\\nATOM    540  O   CYS A 107       3.036  12.718 -15.076  1.00 62.15           O\\nANISOU  540  O   CYS A 107     7754   9173   6688   -508   -936    780       O\\nATOM    541  CB  CYS A 107       2.542  12.149 -18.368  1.00 77.98           C\\nANISOU  541  CB  CYS A 107     9930  11782   7918   -646  -1190    790       C\\nATOM    542  SG  CYS A 107       4.200  11.445 -18.193  1.00 79.49           S\\nANISOU  542  SG  CYS A 107    10119  12137   7945   -673   -832    689       S\\nATOM    543  N   ASP A 108       2.590  14.530 -16.341  1.00 68.64           N\\nANISOU  543  N   ASP A 108     8692  10029   7359   -576  -1335   1195       N\\nATOM    544  CA  ASP A 108       3.289  15.433 -15.430  1.00 67.61           C\\nANISOU  544  CA  ASP A 108     8561   9699   7427   -578  -1293   1358       C\\nATOM    545  C   ASP A 108       2.673  15.405 -14.037  1.00 65.65           C\\nANISOU  545  C   ASP A 108     8180   9208   7557   -435  -1270   1167       C\\nATOM    546  O   ASP A 108       3.393  15.362 -13.033  1.00 66.27           O\\nANISOU  546  O   ASP A 108     8226   9190   7765   -423  -1086   1133       O\\nATOM    547  CB  ASP A 108       3.280  16.856 -15.990  1.00 70.02           C\\nANISOU  547  CB  ASP A 108     8985   9912   7707   -648  -1582   1705       C\\nATOM    548  CG  ASP A 108       4.274  17.047 -17.124  1.00 81.41           C\\nANISOU  548  CG  ASP A 108    10562  11623   8747   -867  -1532   1967       C\\nATOM    549  OD1 ASP A 108       5.293  16.329 -17.150  1.00 84.41           O\\nANISOU  549  OD1 ASP A 108    10904  12225   8943   -940  -1226   1879       O\\nATOM    550  OD2 ASP A 108       4.043  17.922 -17.986  1.00 86.93           O\\nANISOU  550  OD2 ASP A 108    11397  12326   9305   -971  -1808   2260       O\\nATOM    551  N   ILE A 109       1.341  15.424 -13.956  1.00 63.48           N\\nANISOU  551  N   ILE A 109     7808   8870   7442   -332  -1455   1030       N\\nATOM    552  CA  ILE A 109       0.665  15.365 -12.662  1.00 61.96           C\\nANISOU  552  CA  ILE A 109     7449   8532   7562   -218  -1412    821       C\\nATOM    553  C   ILE A 109       1.015  14.072 -11.937  1.00 63.72           C\\nANISOU  553  C   ILE A 109     7629   8811   7771   -268  -1106    623       C\\nATOM    554  O   ILE A 109       1.341  14.076 -10.743  1.00 59.23           O\\nANISOU  554  O   ILE A 109     7010   8137   7359   -241   -960    564       O\\nATOM    555  CB  ILE A 109      -0.856  15.511 -12.845  1.00 58.03           C\\nANISOU  555  CB  ILE A 109     6805   8039   7204   -115  -1656    674       C\\nATOM    556  CG1 ILE A 109      -1.212  16.937 -13.262  1.00 58.42           C\\nANISOU  556  CG1 ILE A 109     6896   7940   7362    -12  -2018    855       C\\nATOM    557  CG2 ILE A 109      -1.588  15.133 -11.573  1.00 56.04           C\\nANISOU  557  CG2 ILE A 109     6336   7761   7197    -50  -1535    405       C\\nATOM    558  CD1 ILE A 109      -2.681  17.131 -13.524  1.00 59.89           C\\nANISOU  558  CD1 ILE A 109     6917   8142   7695    126  -2302    693       C\\nATOM    559  N   PHE A 110       0.949  12.945 -12.648  1.00 61.78           N\\nANISOU  559  N   PHE A 110     7422   8717   7335   -338  -1034    516       N\\nATOM    560  CA  PHE A 110       1.250  11.658 -12.031  1.00 58.79           C\\nANISOU  560  CA  PHE A 110     7039   8336   6961   -385   -808    335       C\\nATOM    561  C   PHE A 110       2.679  11.622 -11.510  1.00 63.91           C\\nANISOU  561  C   PHE A 110     7771   8939   7574   -390   -613    414       C\\nATOM    562  O   PHE A 110       2.921  11.236 -10.361  1.00 59.44           O\\nANISOU  562  O   PHE A 110     7180   8260   7146   -384   -476    340       O\\nATOM    563  CB  PHE A 110       0.997  10.530 -13.034  1.00 61.38           C\\nANISOU  563  CB  PHE A 110     7419   8803   7098   -442   -823    194       C\\nATOM    564  CG  PHE A 110       1.692   9.234 -12.700  1.00 68.94           C\\nANISOU  564  CG  PHE A 110     8447   9728   8016   -477   -636     42       C\\nATOM    565  CD1 PHE A 110       1.579   8.662 -11.444  1.00 75.18           C\\nANISOU  565  CD1 PHE A 110     9204  10361   8999   -508   -525    -42       C\\nATOM    566  CD2 PHE A 110       2.437   8.573 -13.660  1.00 71.59           C\\nANISOU  566  CD2 PHE A 110     8887  10201   8115   -474   -595    -28       C\\nATOM    567  CE1 PHE A 110       2.216   7.472 -11.150  1.00 77.40           C\\nANISOU  567  CE1 PHE A 110     9585  10560   9264   -531   -416   -161       C\\nATOM    568  CE2 PHE A 110       3.070   7.383 -13.372  1.00 74.90           C\\nANISOU  568  CE2 PHE A 110     9372  10553   8534   -462   -477   -203       C\\nATOM    569  CZ  PHE A 110       2.960   6.833 -12.116  1.00 77.70           C\\nANISOU  569  CZ  PHE A 110     9724  10690   9110   -489   -407   -255       C\\nATOM    570  N   VAL A 111       3.641  12.034 -12.340  1.00 65.60           N\\nANISOU  570  N   VAL A 111     8072   9264   7587   -416   -603    568       N\\nATOM    571  CA  VAL A 111       5.043  11.987 -11.930  1.00 66.54           C\\nANISOU  571  CA  VAL A 111     8228   9388   7667   -424   -420    620       C\\nATOM    572  C   VAL A 111       5.288  12.924 -10.757  1.00 60.65           C\\nANISOU  572  C   VAL A 111     7442   8452   7150   -393   -417    727       C\\nATOM    573  O   VAL A 111       6.026  12.590  -9.822  1.00 56.21           O\\nANISOU  573  O   VAL A 111     6872   7814   6670   -370   -270    674       O\\nATOM    574  CB  VAL A 111       5.960  12.317 -13.119  1.00 69.81           C\\nANISOU  574  CB  VAL A 111     8700  10035   7791   -499   -401    765       C\\nATOM    575  CG1 VAL A 111       7.405  12.336 -12.671  1.00 60.98           C\\nANISOU  575  CG1 VAL A 111     7563   8955   6651   -512   -214    801       C\\nATOM    576  CG2 VAL A 111       5.758  11.308 -14.235  1.00 72.95           C\\nANISOU  576  CG2 VAL A 111     9130  10652   7937   -508   -394    597       C\\nATOM    577  N   THR A 112       4.669  14.106 -10.784  1.00 59.23           N\\nANISOU  577  N   THR A 112     7242   8180   7083   -374   -610    861       N\\nATOM    578  CA  THR A 112       4.789  15.036  -9.664  1.00 65.31           C\\nANISOU  578  CA  THR A 112     7970   8754   8090   -319   -646    910       C\\nATOM    579  C   THR A 112       4.286  14.407  -8.371  1.00 66.52           C\\nANISOU  579  C   THR A 112     8031   8833   8410   -256   -532    693       C\\nATOM    580  O   THR A 112       4.970  14.440  -7.343  1.00 76.31           O\\nANISOU  580  O   THR A 112     9268   9991   9734   -241   -417    676       O\\nATOM    581  CB  THR A 112       4.019  16.321  -9.963  1.00 64.71           C\\nANISOU  581  CB  THR A 112     7889   8561   8139   -269   -933   1031       C\\nATOM    582  OG1 THR A 112       4.645  17.010 -11.052  1.00 63.73           O\\nANISOU  582  OG1 THR A 112     7888   8484   7843   -379  -1048   1304       O\\nATOM    583  CG2 THR A 112       3.995  17.223  -8.744  1.00 62.38           C\\nANISOU  583  CG2 THR A 112     7534   8052   8116   -171   -994    998       C\\nATOM    584  N   LEU A 113       3.086  13.825  -8.407  1.00 61.29           N\\nANISOU  584  N   LEU A 113     7289   8219   7778   -245   -569    534       N\\nATOM    585  CA  LEU A 113       2.533  13.195  -7.214  1.00 68.29           C\\nANISOU  585  CA  LEU A 113     8081   9085   8780   -248   -453    353       C\\nATOM    586  C   LEU A 113       3.348  11.975  -6.799  1.00 67.53           C\\nANISOU  586  C   LEU A 113     8081   8983   8595   -321   -257    312       C\\nATOM    587  O   LEU A 113       3.573  11.752  -5.604  1.00 68.67           O\\nANISOU  587  O   LEU A 113     8216   9064   8811   -332   -149    267       O\\nATOM    588  CB  LEU A 113       1.075  12.808  -7.454  1.00 70.65           C\\nANISOU  588  CB  LEU A 113     8249   9477   9119   -266   -536    201       C\\nATOM    589  CG  LEU A 113       0.073  13.960  -7.517  1.00 65.91           C\\nANISOU  589  CG  LEU A 113     7497   8872   8673   -146   -751    162       C\\nATOM    590  CD1 LEU A 113      -1.287  13.451  -7.958  1.00 61.41           C\\nANISOU  590  CD1 LEU A 113     6776   8439   8118   -174   -840      2       C\\nATOM    591  CD2 LEU A 113      -0.016  14.648  -6.165  1.00 61.76           C\\nANISOU  591  CD2 LEU A 113     6853   8287   8324    -59   -710     69       C\\nATOM    592  N   ASP A 114       3.794  11.174  -7.768  1.00 63.91           N\\nANISOU  592  N   ASP A 114     7718   8590   7975   -359   -233    311       N\\nATOM    593  CA  ASP A 114       4.598   9.999  -7.445  1.00 66.05           C\\nANISOU  593  CA  ASP A 114     8086   8820   8191   -384   -102    240       C\\nATOM    594  C   ASP A 114       5.885  10.392  -6.734  1.00 66.08           C\\nANISOU  594  C   ASP A 114     8124   8760   8225   -333    -12    324       C\\nATOM    595  O   ASP A 114       6.262   9.778  -5.730  1.00 69.96           O\\nANISOU  595  O   ASP A 114     8658   9151   8773   -337     64    278       O\\nATOM    596  CB  ASP A 114       4.901   9.208  -8.720  1.00 75.01           C\\nANISOU  596  CB  ASP A 114     9296  10059   9148   -388   -118    174       C\\nATOM    597  CG  ASP A 114       5.951   8.133  -8.509  1.00 75.49           C\\nANISOU  597  CG  ASP A 114     9451  10063   9168   -352    -25     76       C\\nATOM    598  OD1 ASP A 114       5.746   7.255  -7.648  1.00 74.37           O\\nANISOU  598  OD1 ASP A 114     9364   9766   9125   -388     -9     -2       O\\nATOM    599  OD2 ASP A 114       6.981   8.161  -9.214  1.00 76.15           O\\nANISOU  599  OD2 ASP A 114     9549  10268   9116   -291     20     74       O\\nATOM    600  N   VAL A 115       6.568  11.421  -7.235  1.00 71.45           N\\nANISOU  600  N   VAL A 115     8790   9494   8864   -306    -41    464       N\\nATOM    601  CA  VAL A 115       7.809  11.865  -6.610  1.00 70.24           C\\nANISOU  601  CA  VAL A 115     8641   9297   8749   -279     30    542       C\\nATOM    602  C   VAL A 115       7.535  12.461  -5.234  1.00 69.24           C\\nANISOU  602  C   VAL A 115     8477   9030   8802   -253     19    542       C\\nATOM    603  O   VAL A 115       8.282  12.220  -4.279  1.00 70.91           O\\nANISOU  603  O   VAL A 115     8710   9175   9059   -230     93    521       O\\nATOM    604  CB  VAL A 115       8.536  12.862  -7.531  1.00 65.07           C\\nANISOU  604  CB  VAL A 115     7975   8750   7999   -319     -9    719       C\\nATOM    605  CG1 VAL A 115       9.683  13.529  -6.804  1.00 60.52           C\\nANISOU  605  CG1 VAL A 115     7374   8118   7505   -321     36    809       C\\nATOM    606  CG2 VAL A 115       9.043  12.156  -8.778  1.00 62.56           C\\nANISOU  606  CG2 VAL A 115     7676   8649   7446   -346     53    680       C\\nATOM    607  N   MET A 116       6.454  13.232  -5.103  1.00 72.12           N\\nANISOU  607  N   MET A 116     8773   9364   9266   -239    -88    539       N\\nATOM    608  CA  MET A 116       6.164  13.889  -3.832  1.00 68.31           C\\nANISOU  608  CA  MET A 116     8226   8792   8936   -191   -103    487       C\\nATOM    609  C   MET A 116       5.814  12.877  -2.746  1.00 67.37           C\\nANISOU  609  C   MET A 116     8106   8685   8808   -232     19    357       C\\nATOM    610  O   MET A 116       6.435  12.860  -1.677  1.00 67.14           O\\nANISOU  610  O   MET A 116     8105   8604   8802   -221     83    349       O\\nATOM    611  CB  MET A 116       5.031  14.896  -4.005  1.00 66.63           C\\nANISOU  611  CB  MET A 116     7912   8564   8843   -129   -269    455       C\\nATOM    612  CG  MET A 116       4.669  15.602  -2.718  1.00 65.54           C\\nANISOU  612  CG  MET A 116     7676   8370   8856    -46   -291    332       C\\nATOM    613  SD  MET A 116       3.209  16.636  -2.880  1.00 73.08           S\\nANISOU  613  SD  MET A 116     8464   9323   9980     85   -509    199       S\\nATOM    614  CE  MET A 116       3.000  17.178  -1.184  1.00 75.15           C\\nANISOU  614  CE  MET A 116     8597   9592  10365    186   -462    -23       C\\nATOM    615  N   MET A 117       4.820  12.023  -3.000  1.00 57.68           N\\nANISOU  615  N   MET A 117     6854   7527   7535   -303     36    271       N\\nATOM    616  CA  MET A 117       4.373  11.084  -1.977  1.00 63.01           C\\nANISOU  616  CA  MET A 117     7536   8218   8187   -406    135    188       C\\nATOM    617  C   MET A 117       5.457  10.093  -1.578  1.00 71.53           C\\nANISOU  617  C   MET A 117     8783   9196   9201   -439    202    236       C\\nATOM    618  O   MET A 117       5.388   9.526  -0.482  1.00 77.20           O\\nANISOU  618  O   MET A 117     9549   9888   9894   -524    260    225       O\\nATOM    619  CB  MET A 117       3.132  10.337  -2.457  1.00 61.50           C\\nANISOU  619  CB  MET A 117     7283   8115   7968   -518    120    103       C\\nATOM    620  CG  MET A 117       1.975  11.258  -2.770  1.00 64.85           C\\nANISOU  620  CG  MET A 117     7509   8654   8476   -463     28     19       C\\nATOM    621  SD  MET A 117       1.790  12.509  -1.489  1.00 62.59           S\\nANISOU  621  SD  MET A 117     7071   8409   8301   -354     37    -66       S\\nATOM    622  CE  MET A 117       0.518  13.548  -2.206  1.00 56.74           C\\nANISOU  622  CE  MET A 117     6109   7754   7697   -221   -153   -189       C\\nATOM    623  N   CYS A 118       6.449   9.867  -2.434  1.00 70.60           N\\nANISOU  623  N   CYS A 118     8747   9036   9042   -373    183    282       N\\nATOM    624  CA  CYS A 118       7.576   9.023  -2.062  1.00 70.67           C\\nANISOU  624  CA  CYS A 118     8885   8946   9021   -346    211    289       C\\nATOM    625  C   CYS A 118       8.689   9.813  -1.387  1.00 68.27           C\\nANISOU  625  C   CYS A 118     8564   8615   8761   -260    228    351       C\\nATOM    626  O   CYS A 118       9.435   9.249  -0.578  1.00 62.32           O\\nANISOU  626  O   CYS A 118     7898   7774   8009   -239    233    351       O\\nATOM    627  CB  CYS A 118       8.121   8.295  -3.295  1.00 71.86           C\\nANISOU  627  CB  CYS A 118     9091   9112   9101   -295    188    239       C\\nATOM    628  SG  CYS A 118       6.974   7.093  -4.021  1.00 68.74           S\\nANISOU  628  SG  CYS A 118     8755   8698   8664   -398    132    131       S\\nATOM    629  N   THR A 119       8.819  11.105  -1.703  1.00 71.90           N\\nANISOU  629  N   THR A 119     8925   9128   9267   -218    203    409       N\\nATOM    630  CA  THR A 119       9.769  11.947  -0.985  1.00 68.93           C\\nANISOU  630  CA  THR A 119     8523   8711   8956   -165    196    461       C\\nATOM    631  C   THR A 119       9.300  12.212   0.440  1.00 62.52           C\\nANISOU  631  C   THR A 119     7704   7861   8191   -175    201    411       C\\nATOM    632  O   THR A 119      10.125  12.295   1.357  1.00 61.89           O\\nANISOU  632  O   THR A 119     7656   7732   8127   -144    202    417       O\\nATOM    633  CB  THR A 119       9.981  13.271  -1.728  1.00 67.89           C\\nANISOU  633  CB  THR A 119     8314   8606   8874   -156    129    558       C\\nATOM    634  OG1 THR A 119      10.268  13.009  -3.105  1.00 63.88           O\\nANISOU  634  OG1 THR A 119     7808   8202   8260   -182    139    610       O\\nATOM    635  CG2 THR A 119      11.148  14.045  -1.129  1.00 64.40           C\\nANISOU  635  CG2 THR A 119     7848   8113   8507   -132    108    616       C\\nATOM    636  N   ALA A 120       7.987  12.343   0.642  1.00 61.79           N\\nANISOU  636  N   ALA A 120     7547   7824   8105   -218    203    341       N\\nATOM    637  CA  ALA A 120       7.457  12.486   1.992  1.00 59.49           C\\nANISOU  637  CA  ALA A 120     7220   7579   7805   -246    240    258       C\\nATOM    638  C   ALA A 120       7.815  11.283   2.852  1.00 61.28           C\\nANISOU  638  C   ALA A 120     7585   7779   7919   -337    300    286       C\\nATOM    639  O   ALA A 120       8.114  11.433   4.041  1.00 62.06           O\\nANISOU  639  O   ALA A 120     7711   7891   7976   -343    316    271       O\\nATOM    640  CB  ALA A 120       5.943  12.676   1.947  1.00 60.06           C\\nANISOU  640  CB  ALA A 120     7153   7780   7886   -287    251    145       C\\nATOM    641  N   SER A 121       7.784  10.080   2.268  1.00 59.91           N\\nANISOU  641  N   SER A 121     7518   7552   7694   -409    305    325       N\\nATOM    642  CA  SER A 121       8.208   8.889   2.998  1.00 65.17           C\\nANISOU  642  CA  SER A 121     8361   8120   8282   -489    296    378       C\\nATOM    643  C   SER A 121       9.662   9.003   3.431  1.00 68.85           C\\nANISOU  643  C   SER A 121     8900   8486   8775   -361    241    416       C\\nATOM    644  O   SER A 121      10.014   8.643   4.561  1.00 69.48           O\\nANISOU  644  O   SER A 121     9088   8521   8792   -399    214    457       O\\nATOM    645  CB  SER A 121       8.013   7.640   2.137  1.00 61.09           C\\nANISOU  645  CB  SER A 121     7954   7505   7753   -550    254    383       C\\nATOM    646  OG  SER A 121       6.661   7.485   1.747  1.00 71.73           O\\nANISOU  646  OG  SER A 121     9221   8952   9081   -688    290    343       O\\nATOM    647  N   ALA A 122      10.522   9.500   2.544  1.00 66.20           N\\nANISOU  647  N   ALA A 122     8498   8140   8516   -228    219    409       N\\nATOM    648  CA  ALA A 122      11.932   9.632   2.882  1.00 64.09           C\\nANISOU  648  CA  ALA A 122     8247   7817   8288   -115    169    424       C\\nATOM    649  C   ALA A 122      12.144  10.731   3.911  1.00 67.35           C\\nANISOU  649  C   ALA A 122     8599   8264   8729    -99    162    428       C\\nATOM    650  O   ALA A 122      12.870  10.544   4.893  1.00 67.60           O\\nANISOU  650  O   ALA A 122     8699   8245   8739    -68    109    438       O\\nATOM    651  CB  ALA A 122      12.746   9.905   1.621  1.00 62.95           C\\nANISOU  651  CB  ALA A 122     8005   7723   8189    -24    175    411       C\\nATOM    652  N   LEU A 123      11.511  11.886   3.707  1.00 62.65           N\\nANISOU  652  N   LEU A 123     7879   7737   8186   -107    182    403       N\\nATOM    653  CA  LEU A 123      11.661  12.982   4.654  1.00 64.73           C\\nANISOU  653  CA  LEU A 123     8084   8013   8499    -71    145    360       C\\nATOM    654  C   LEU A 123      11.002  12.677   5.993  1.00 68.58           C\\nANISOU  654  C   LEU A 123     8623   8569   8865   -134    179    297       C\\nATOM    655  O   LEU A 123      11.397  13.259   7.008  1.00 65.26           O\\nANISOU  655  O   LEU A 123     8197   8165   8435    -96    140    244       O\\nATOM    656  CB  LEU A 123      11.095  14.271   4.056  1.00 60.03           C\\nANISOU  656  CB  LEU A 123     7361   7429   8020    -42    106    331       C\\nATOM    657  CG  LEU A 123      12.060  15.137   3.236  1.00 62.40           C\\nANISOU  657  CG  LEU A 123     7610   7663   8437    -13     31    421       C\\nATOM    658  CD1 LEU A 123      12.857  14.325   2.223  1.00 59.85           C\\nANISOU  658  CD1 LEU A 123     7308   7374   8057    -33     81    508       C\\nATOM    659  CD2 LEU A 123      11.293  16.248   2.540  1.00 58.42           C\\nANISOU  659  CD2 LEU A 123     7032   7125   8039     -7    -54    431       C\\nATOM    660  N   ASN A 124      10.015  11.778   6.022  1.00 64.20           N\\nANISOU  660  N   ASN A 124     8115   8078   8200   -253    250    303       N\\nATOM    661  CA  ASN A 124       9.452  11.343   7.295  1.00 68.55           C\\nANISOU  661  CA  ASN A 124     8724   8742   8580   -376    301    282       C\\nATOM    662  C   ASN A 124      10.430  10.450   8.047  1.00 72.49           C\\nANISOU  662  C   ASN A 124     9424   9133   8985   -402    229    393       C\\nATOM    663  O   ASN A 124      10.617  10.600   9.260  1.00 78.80           O\\nANISOU  663  O   ASN A 124    10273  10006   9661   -433    215    382       O\\nATOM    664  CB  ASN A 124       8.129  10.616   7.067  1.00 63.03           C\\nANISOU  664  CB  ASN A 124     8004   8152   7791   -549    391    281       C\\nATOM    665  CG  ASN A 124       6.940  11.540   7.141  1.00 59.12           C\\nANISOU  665  CG  ASN A 124     7283   7866   7312   -543    463    113       C\\nATOM    666  OD1 ASN A 124       6.864  12.399   8.016  1.00 58.74           O\\nANISOU  666  OD1 ASN A 124     7141   7941   7236   -481    474    -16       O\\nATOM    667  ND2 ASN A 124       6.000  11.373   6.218  1.00 59.97           N\\nANISOU  667  ND2 ASN A 124     7292   8020   7473   -588    490     83       N\\nATOM    668  N   LEU A 125      11.062   9.508   7.343  1.00 66.29           N\\nANISOU  668  N   LEU A 125     8756   8179   8253   -373    162    480       N\\nATOM    669  CA  LEU A 125      12.084   8.682   7.972  1.00 65.46           C\\nANISOU  669  CA  LEU A 125     8836   7929   8106   -343     35    565       C\\nATOM    670  C   LEU A 125      13.243   9.524   8.477  1.00 65.97           C\\nANISOU  670  C   LEU A 125     8840   7991   8234   -191    -37    522       C\\nATOM    671  O   LEU A 125      13.922   9.139   9.436  1.00 61.15           O\\nANISOU  671  O   LEU A 125     8360   7325   7547   -177   -149    572       O\\nATOM    672  CB  LEU A 125      12.583   7.629   6.988  1.00 62.70           C\\nANISOU  672  CB  LEU A 125     8578   7397   7847   -276    -48    593       C\\nATOM    673  CG  LEU A 125      11.555   6.553   6.663  1.00 64.43           C\\nANISOU  673  CG  LEU A 125     8919   7557   8006   -451    -38    646       C\\nATOM    674  CD1 LEU A 125      12.089   5.633   5.597  1.00 62.96           C\\nANISOU  674  CD1 LEU A 125     8802   7188   7932   -337   -140    608       C\\nATOM    675  CD2 LEU A 125      11.214   5.779   7.920  1.00 61.82           C\\nANISOU  675  CD2 LEU A 125     8799   7183   7505   -650   -100    783       C\\nATOM    676  N   CYS A 126      13.482  10.673   7.849  1.00 67.22           N\\nANISOU  676  N   CYS A 126     8812   8199   8530    -94      0    444       N\\nATOM    677  CA  CYS A 126      14.522  11.568   8.333  1.00 68.85           C\\nANISOU  677  CA  CYS A 126     8945   8402   8814     11    -78    401       C\\nATOM    678  C   CYS A 126      14.084  12.257   9.617  1.00 71.84           C\\nANISOU  678  C   CYS A 126     9323   8885   9086    -30    -78    330       C\\nATOM    679  O   CYS A 126      14.848  12.331  10.588  1.00 74.42           O\\nANISOU  679  O   CYS A 126     9709   9205   9362      8   -177    320       O\\nATOM    680  CB  CYS A 126      14.866  12.592   7.257  1.00 64.79           C\\nANISOU  680  CB  CYS A 126     8252   7891   8474     72    -60    375       C\\nATOM    681  SG  CYS A 126      16.409  13.441   7.561  1.00 69.06           S\\nANISOU  681  SG  CYS A 126     8693   8402   9146    160   -175    353       S\\nATOM    682  N   ALA A 127      12.849  12.762   9.642  1.00 60.58           N\\nANISOU  682  N   ALA A 127     7817   7582   7618    -95     24    250       N\\nATOM    683  CA  ALA A 127      12.322  13.375  10.854  1.00 61.10           C\\nANISOU  683  CA  ALA A 127     7852   7809   7555   -121     44    122       C\\nATOM    684  C   ALA A 127      12.220  12.369  11.990  1.00 65.12           C\\nANISOU  684  C   ALA A 127     8538   8411   7794   -256     52    201       C\\nATOM    685  O   ALA A 127      12.407  12.729  13.158  1.00 65.71           O\\nANISOU  685  O   ALA A 127     8640   8603   7724   -258     16    127       O\\nATOM    686  CB  ALA A 127      10.957  13.996  10.570  1.00 60.25           C\\nANISOU  686  CB  ALA A 127     7585   7843   7462   -141    147    -17       C\\nATOM    687  N   ILE A 128      11.925  11.108  11.673  1.00 64.09           N\\nANISOU  687  N   ILE A 128     8546   8221   7582   -384     77    357       N\\nATOM    688  CA  ILE A 128      11.829  10.083  12.705  1.00 61.38           C\\nANISOU  688  CA  ILE A 128     8417   7924   6982   -558     46    492       C\\nATOM    689  C   ILE A 128      13.184   9.868  13.370  1.00 64.99           C\\nANISOU  689  C   ILE A 128     9025   8241   7426   -455   -148    563       C\\nATOM    690  O   ILE A 128      13.286   9.807  14.600  1.00 69.74           O\\nANISOU  690  O   ILE A 128     9740   8959   7800   -534   -198    591       O\\nATOM    691  CB  ILE A 128      11.271   8.779  12.108  1.00 62.32           C\\nANISOU  691  CB  ILE A 128     8673   7934   7072   -722     61    653       C\\nATOM    692  CG1 ILE A 128       9.772   8.923  11.836  1.00 63.83           C\\nANISOU  692  CG1 ILE A 128     8711   8345   7195   -888    252    582       C\\nATOM    693  CG2 ILE A 128      11.548   7.604  13.028  1.00 64.88           C\\nANISOU  693  CG2 ILE A 128     9290   8172   7190   -886    -69    860       C\\nATOM    694  CD1 ILE A 128       9.120   7.668  11.294  1.00 68.59           C\\nANISOU  694  CD1 ILE A 128     9440   8852   7770  -1092    259    730       C\\nATOM    695  N   SER A 129      14.244   9.756  12.565  1.00 66.20           N\\nANISOU  695  N   SER A 129     9164   8178   7810   -278   -262    578       N\\nATOM    696  CA  SER A 129      15.586   9.611  13.121  1.00 63.02           C\\nANISOU  696  CA  SER A 129     8848   7658   7438   -147   -463    607       C\\nATOM    697  C   SER A 129      15.949  10.799  13.998  1.00 65.47           C\\nANISOU  697  C   SER A 129     9055   8109   7713    -86   -487    474       C\\nATOM    698  O   SER A 129      16.527  10.629  15.078  1.00 65.88           O\\nANISOU  698  O   SER A 129     9234   8177   7619    -82   -631    506       O\\nATOM    699  CB  SER A 129      16.603   9.467  11.995  1.00 65.36           C\\nANISOU  699  CB  SER A 129     9050   7784   7998     39   -538    582       C\\nATOM    700  OG  SER A 129      16.749  10.693  11.302  1.00 65.87           O\\nANISOU  700  OG  SER A 129     8871   7922   8235    114   -445    460       O\\nATOM    701  N   ILE A 130      15.624  12.011  13.546  1.00 64.82           N\\nANISOU  701  N   ILE A 130     8755   8106   7766    -35   -383    319       N\\nATOM    702  CA  ILE A 130      15.959  13.208  14.313  1.00 68.76           C\\nANISOU  702  CA  ILE A 130     9156   8695   8276     36   -439    156       C\\nATOM    703  C   ILE A 130      15.205  13.216  15.636  1.00 70.22           C\\nANISOU  703  C   ILE A 130     9425   9110   8144    -76   -395     92       C\\nATOM    704  O   ILE A 130      15.775  13.502  16.695  1.00 76.17           O\\nANISOU  704  O   ILE A 130    10235   9933   8773    -45   -514     30       O\\nATOM    705  CB  ILE A 130      15.668  14.473  13.488  1.00 69.26           C\\nANISOU  705  CB  ILE A 130     9002   8739   8574    105   -379     19       C\\nATOM    706  CG1 ILE A 130      16.553  14.504  12.241  1.00 65.51           C\\nANISOU  706  CG1 ILE A 130     8440   8094   8355    174   -420    103       C\\nATOM    707  CG2 ILE A 130      15.878  15.716  14.329  1.00 65.28           C\\nANISOU  707  CG2 ILE A 130     8415   8293   8097    175   -469   -180       C\\nATOM    708  CD1 ILE A 130      16.380  15.745  11.402  1.00 62.56           C\\nANISOU  708  CD1 ILE A 130     7895   7673   8203    202   -405     32       C\\nATOM    709  N   ASP A 131      13.909  12.904  15.595  1.00 70.28           N\\nANISOU  709  N   ASP A 131     9426   9280   7998   -221   -219     94       N\\nATOM    710  CA  ASP A 131      13.155  12.749  16.833  1.00 71.28           C\\nANISOU  710  CA  ASP A 131     9617   9702   7763   -378   -141     50       C\\nATOM    711  C   ASP A 131      13.708  11.611  17.677  1.00 75.20           C\\nANISOU  711  C   ASP A 131    10397  10170   8008   -506   -269    283       C\\nATOM    712  O   ASP A 131      13.639  11.660  18.910  1.00 73.14           O\\nANISOU  712  O   ASP A 131    10222  10134   7432   -599   -289    255       O\\nATOM    713  CB  ASP A 131      11.678  12.515  16.525  1.00 70.71           C\\nANISOU  713  CB  ASP A 131     9449   9834   7586   -540     79     22       C\\nATOM    714  CG  ASP A 131      10.820  12.477  17.775  1.00 76.68           C\\nANISOU  714  CG  ASP A 131    10201  10991   7942   -727    206    -66       C\\nATOM    715  OD1 ASP A 131      10.819  13.472  18.528  1.00 78.05           O\\nANISOU  715  OD1 ASP A 131    10254  11363   8039   -619    204   -327       O\\nATOM    716  OD2 ASP A 131      10.140  11.455  18.001  1.00 79.31           O\\nANISOU  716  OD2 ASP A 131    10647  11456   8030   -996    304    118       O\\nATOM    717  N   ARG A 132      14.264  10.581  17.036  1.00 72.55           N\\nANISOU  717  N   ARG A 132    10215   9556   7796   -504   -380    502       N\\nATOM    718  CA  ARG A 132      14.921   9.521  17.791  1.00 74.39           C\\nANISOU  718  CA  ARG A 132    10739   9679   7847   -579   -584    726       C\\nATOM    719  C   ARG A 132      16.221  10.003  18.417  1.00 74.84           C\\nANISOU  719  C   ARG A 132    10811   9673   7954   -388   -804    656       C\\nATOM    720  O   ARG A 132      16.614   9.507  19.479  1.00 74.70           O\\nANISOU  720  O   ARG A 132    11012   9686   7686   -458   -973    778       O\\nATOM    721  CB  ARG A 132      15.175   8.307  16.894  1.00 71.71           C\\nANISOU  721  CB  ARG A 132    10547   9024   7674   -578   -687    923       C\\nATOM    722  CG  ARG A 132      13.976   7.378  16.715  1.00 69.10           C\\nANISOU  722  CG  ARG A 132    10338   8727   7188   -858   -567   1086       C\\nATOM    723  CD  ARG A 132      13.493   6.832  18.055  1.00 75.91           C\\nANISOU  723  CD  ARG A 132    11433   9782   7627  -1155   -591   1269       C\\nATOM    724  NE  ARG A 132      12.518   7.717  18.686  1.00 77.94           N\\nANISOU  724  NE  ARG A 132    11497  10480   7636  -1291   -337   1099       N\\nATOM    725  CZ  ARG A 132      12.271   7.756  19.990  1.00 77.58           C\\nANISOU  725  CZ  ARG A 132    11552  10740   7186  -1484   -317   1141       C\\nATOM    726  NH1 ARG A 132      12.931   6.960  20.822  1.00 76.41           N\\nANISOU  726  NH1 ARG A 132    11728  10477   6827  -1585   -559   1394       N\\nATOM    727  NH2 ARG A 132      11.366   8.602  20.464  1.00 79.78           N\\nANISOU  727  NH2 ARG A 132    11599  11452   7261  -1565    -71    912       N\\nATOM    728  N   TYR A 133      16.902  10.960  17.786  1.00 73.32           N\\nANISOU  728  N   TYR A 133    10393   9395   8070   -171   -822    476       N\\nATOM    729  CA  TYR A 133      18.124  11.492  18.379  1.00 72.55           C\\nANISOU  729  CA  TYR A 133    10271   9257   8037    -13  -1032    389       C\\nATOM    730  C   TYR A 133      17.813  12.311  19.624  1.00 76.41           C\\nANISOU  730  C   TYR A 133    10753  10016   8263    -65  -1020    228       C\\nATOM    731  O   TYR A 133      18.475  12.161  20.658  1.00 82.66           O\\nANISOU  731  O   TYR A 133    11685  10852   8869    -54  -1214    255       O\\nATOM    732  CB  TYR A 133      18.894  12.340  17.365  1.00 65.57           C\\nANISOU  732  CB  TYR A 133     9133   8238   7542    169  -1045    254       C\\nATOM    733  CG  TYR A 133      20.160  12.957  17.931  1.00 69.03           C\\nANISOU  733  CG  TYR A 133     9504   8648   8079    305  -1262    149       C\\nATOM    734  CD1 TYR A 133      21.367  12.268  17.901  1.00 73.59           C\\nANISOU  734  CD1 TYR A 133    10124   9075   8760    424  -1482    232       C\\nATOM    735  CD2 TYR A 133      20.148  14.224  18.502  1.00 67.30           C\\nANISOU  735  CD2 TYR A 133     9162   8546   7862    326  -1271    -61       C\\nATOM    736  CE1 TYR A 133      22.526  12.825  18.419  1.00 73.44           C\\nANISOU  736  CE1 TYR A 133    10011   9052   8839    539  -1690    123       C\\nATOM    737  CE2 TYR A 133      21.303  14.789  19.022  1.00 69.25           C\\nANISOU  737  CE2 TYR A 133     9341   8760   8209    429  -1488   -164       C\\nATOM    738  CZ  TYR A 133      22.488  14.084  18.977  1.00 74.54           C\\nANISOU  738  CZ  TYR A 133    10039   9309   8975    524  -1689    -64       C\\nATOM    739  OH  TYR A 133      23.637  14.640  19.490  1.00 78.51           O\\nANISOU  739  OH  TYR A 133    10443   9800   9586    618  -1914   -178       O\\nATOM    740  N   THR A 134      16.813  13.190  19.544  1.00 70.79           N\\nANISOU  740  N   THR A 134     9871   9496   7530   -102   -814     34       N\\nATOM    741  CA  THR A 134      16.526  14.064  20.674  1.00 74.84           C\\nANISOU  741  CA  THR A 134    10337  10284   7814   -106   -805   -201       C\\nATOM    742  C   THR A 134      16.021  13.276  21.876  1.00 73.81           C\\nANISOU  742  C   THR A 134    10425  10433   7188   -319   -780    -82       C\\nATOM    743  O   THR A 134      16.266  13.672  23.021  1.00 83.45           O\\nANISOU  743  O   THR A 134    11696  11863   8150   -318   -870   -208       O\\nATOM    744  CB  THR A 134      15.517  15.137  20.270  1.00 81.04           C\\nANISOU  744  CB  THR A 134    10877  11199   8715    -61   -617   -471       C\\nATOM    745  OG1 THR A 134      14.231  14.541  20.084  1.00 85.24           O\\nANISOU  745  OG1 THR A 134    11407  11920   9060   -236   -387   -405       O\\nATOM    746  CG2 THR A 134      15.945  15.803  18.969  1.00 80.96           C\\nANISOU  746  CG2 THR A 134    10697  10893   9169     91   -653   -505       C\\nATOM    747  N   ALA A 135      15.341  12.151  21.642  1.00 74.49           N\\nANISOU  747  N   ALA A 135    10655  10530   7120   -527   -674    172       N\\nATOM    748  CA  ALA A 135      14.858  11.340  22.756  1.00 76.81           C\\nANISOU  748  CA  ALA A 135    11182  11087   6918   -800   -658    350       C\\nATOM    749  C   ALA A 135      16.008  10.654  23.480  1.00 76.81           C\\nANISOU  749  C   ALA A 135    11471  10921   6791   -787   -978    571       C\\nATOM    750  O   ALA A 135      15.979  10.505  24.707  1.00 82.26           O\\nANISOU  750  O   ALA A 135    12330  11871   7053   -935  -1044    623       O\\nATOM    751  CB  ALA A 135      13.849  10.307  22.259  1.00 69.76           C\\nANISOU  751  CB  ALA A 135    10373  10203   5930  -1063   -492    588       C\\nATOM    752  N   VAL A 136      17.029  10.233  22.739  1.00 76.95           N\\nANISOU  752  N   VAL A 136    11539  10534   7164   -603  -1189    688       N\\nATOM    753  CA  VAL A 136      18.154   9.535  23.350  1.00 82.31           C\\nANISOU  753  CA  VAL A 136    12472  11024   7777   -545  -1537    878       C\\nATOM    754  C   VAL A 136      19.136  10.524  23.967  1.00 82.04           C\\nANISOU  754  C   VAL A 136    12325  11053   7795   -336  -1708    644       C\\nATOM    755  O   VAL A 136      19.554  10.367  25.120  1.00 81.48           O\\nANISOU  755  O   VAL A 136    12446  11103   7411   -382  -1911    704       O\\nATOM    756  CB  VAL A 136      18.839   8.630  22.309  1.00 77.31           C\\nANISOU  756  CB  VAL A 136    11904   9961   7508   -406  -1706   1045       C\\nATOM    757  CG1 VAL A 136      20.246   8.278  22.755  1.00 77.43           C\\nANISOU  757  CG1 VAL A 136    12049   9764   7606   -210  -2095   1106       C\\nATOM    758  CG2 VAL A 136      18.017   7.366  22.083  1.00 72.64           C\\nANISOU  758  CG2 VAL A 136    11557   9266   6777   -655  -1667   1340       C\\nATOM    759  N   ALA A 137      19.501  11.568  23.224  1.00 77.79           N\\nANISOU  759  N   ALA A 137    11484  10437   7637   -128  -1644    384       N\\nATOM    760  CA  ALA A 137      20.609  12.434  23.603  1.00 80.22           C\\nANISOU  760  CA  ALA A 137    11669  10715   8097     69  -1852    182       C\\nATOM    761  C   ALA A 137      20.209  13.605  24.491  1.00 87.12           C\\nANISOU  761  C   ALA A 137    12440  11898   8765     54  -1780   -115       C\\nATOM    762  O   ALA A 137      21.094  14.243  25.073  1.00 87.55           O\\nANISOU  762  O   ALA A 137    12447  11955   8861    179  -1994   -277       O\\nATOM    763  CB  ALA A 137      21.304  12.975  22.349  1.00 74.40           C\\nANISOU  763  CB  ALA A 137    10663   9730   7877    260  -1849     74       C\\nATOM    764  N   MET A 138      18.922  13.910  24.616  1.00 85.65           N\\nANISOU  764  N   MET A 138    12198  11978   8368    -81  -1504   -224       N\\nATOM    765  CA  MET A 138      18.517  15.099  25.348  1.00 91.36           C\\nANISOU  765  CA  MET A 138    12776  12989   8948    -40  -1439   -587       C\\nATOM    766  C   MET A 138      17.450  14.760  26.377  1.00 93.65           C\\nANISOU  766  C   MET A 138    13184  13730   8670   -264  -1268   -595       C\\nATOM    767  O   MET A 138      16.648  13.844  26.169  1.00 90.32           O\\nANISOU  767  O   MET A 138    12865  13389   8064   -478  -1095   -353       O\\nATOM    768  CB  MET A 138      18.001  16.181  24.387  1.00 94.18           C\\nANISOU  768  CB  MET A 138    12839  13259   9687     83  -1276   -847       C\\nATOM    769  CG  MET A 138      19.095  16.769  23.500  1.00 98.65           C\\nANISOU  769  CG  MET A 138    13264  13452  10767    263  -1446   -874       C\\nATOM    770  SD  MET A 138      18.521  18.077  22.402  1.00105.80           S\\nANISOU  770  SD  MET A 138    13881  14215  12101    371  -1319  -1121       S\\nATOM    771  CE  MET A 138      20.031  18.481  21.533  1.00105.56           C\\nANISOU  771  CE  MET A 138    13744  13805  12559    477  -1542  -1039       C\\nATOM    772  N   PRO A 139      17.425  15.482  27.515  1.00104.46           N\\nANISOU  772  N   PRO A 139    14532  15425   9735   -241  -1315   -880       N\\nATOM    773  CA  PRO A 139      16.509  15.224  28.635  1.00105.59           C\\nANISOU  773  CA  PRO A 139    14765  16095   9259   -469  -1152   -923       C\\nATOM    774  C   PRO A 139      15.042  15.103  28.221  1.00104.65           C\\nANISOU  774  C   PRO A 139    14492  16238   9033   -630   -782   -969       C\\nATOM    775  O   PRO A 139      14.317  16.097  28.261  1.00106.02           O\\nANISOU  775  O   PRO A 139    14394  16653   9234   -519   -617  -1385       O\\nATOM    776  CB  PRO A 139      16.714  16.446  29.535  1.00103.32           C\\nANISOU  776  CB  PRO A 139    14347  16058   8852   -301  -1242  -1390       C\\nATOM    777  CG  PRO A 139      18.112  16.868  29.263  1.00100.62           C\\nANISOU  777  CG  PRO A 139    14009  15289   8934    -72  -1575  -1406       C\\nATOM    778  CD  PRO A 139      18.340  16.603  27.805  1.00 97.12           C\\nANISOU  778  CD  PRO A 139    13483  14389   9030     -4  -1545  -1193       C\\nATOM    779  N   THR A 144       8.716  17.350  27.929  1.00103.31           N\\nANISOU  779  N   THR A 144    12885  17966   8400   -718    631  -2535       N\\nATOM    780  CA  THR A 144       7.590  18.233  28.208  1.00111.55           C\\nANISOU  780  CA  THR A 144    13533  19499   9351   -578    832  -3111       C\\nATOM    781  C   THR A 144       6.396  17.895  27.318  1.00111.78           C\\nANISOU  781  C   THR A 144    13322  19627   9521   -685   1084  -3075       C\\nATOM    782  O   THR A 144       6.556  17.666  26.122  1.00115.16           O\\nANISOU  782  O   THR A 144    13802  19541  10411   -631   1006  -2812       O\\nATOM    783  CB  THR A 144       7.971  19.712  28.006  1.00112.47           C\\nANISOU  783  CB  THR A 144    13477  19327   9931   -104    597  -3618       C\\nATOM    784  N   ARG A 145       5.198  17.868  27.907  1.00112.87           N\\nANISOU  784  N   ARG A 145    13181  20279   9425   -824   1334  -3251       N\\nATOM    785  CA  ARG A 145       4.002  17.509  27.151  1.00114.09           C\\nANISOU  785  CA  ARG A 145    13078  20551   9719   -950   1551  -3212       C\\nATOM    786  C   ARG A 145       3.581  18.596  26.170  1.00118.73           C\\nANISOU  786  C   ARG A 145    13352  20930  10830   -531   1477  -3651       C\\nATOM    787  O   ARG A 145       2.846  18.305  25.221  1.00119.01           O\\nANISOU  787  O   ARG A 145    13234  20913  11072   -582   1585  -3578       O\\nATOM    788  CB  ARG A 145       2.846  17.198  28.104  1.00118.50           C\\nANISOU  788  CB  ARG A 145    13396  21689   9937  -1221   1786  -3270       C\\nATOM    789  N   TYR A 146       4.024  19.834  26.375  1.00121.59           N\\nANISOU  789  N   TYR A 146    13630  21133  11434   -123   1259  -4089       N\\nATOM    790  CA  TYR A 146       3.700  20.948  25.491  1.00117.64           C\\nANISOU  790  CA  TYR A 146    12880  20335  11482    295   1102  -4485       C\\nATOM    791  C   TYR A 146       4.829  21.280  24.526  1.00108.31           C\\nANISOU  791  C   TYR A 146    11951  18428  10772    498    805  -4303       C\\nATOM    792  O   TYR A 146       4.573  21.530  23.344  1.00100.71           O\\nANISOU  792  O   TYR A 146    10911  17078  10275    638    718  -4241       O\\nATOM    793  CB  TYR A 146       3.345  22.185  26.325  1.00124.08           C\\nANISOU  793  CB  TYR A 146    13429  21323  12394    606    974  -5030       C\\nATOM    794  CG  TYR A 146       3.156  23.462  25.533  1.00125.41           C\\nANISOU  794  CG  TYR A 146    13400  21084  13165   1062    702  -5422       C\\nATOM    795  CD1 TYR A 146       1.920  23.794  24.993  1.00128.22           C\\nANISOU  795  CD1 TYR A 146    13405  21556  13758   1181    740  -5641       C\\nATOM    796  CD2 TYR A 146       4.211  24.347  25.345  1.00125.84           C\\nANISOU  796  CD2 TYR A 146    13634  20614  13563   1355    362  -5554       C\\nATOM    797  CE1 TYR A 146       1.746  24.966  24.276  1.00131.82           C\\nANISOU  797  CE1 TYR A 146    13721  21595  14769   1588    432  -5955       C\\nATOM    798  CE2 TYR A 146       4.047  25.515  24.631  1.00128.03           C\\nANISOU  798  CE2 TYR A 146    13776  20456  14413   1732     64  -5846       C\\nATOM    799  CZ  TYR A 146       2.815  25.821  24.099  1.00132.64           C\\nANISOU  799  CZ  TYR A 146    14037  21147  15214   1852     92  -6034       C\\nATOM    800  OH  TYR A 146       2.656  26.988  23.388  1.00136.93           O\\nANISOU  800  OH  TYR A 146    14484  21222  16320   2213   -261  -6277       O\\nATOM    801  N   SER A 147       6.076  21.287  25.005  1.00108.97           N\\nANISOU  801  N   SER A 147    12336  18257  10810    490    611  -4125       N\\nATOM    802  CA  SER A 147       7.206  21.602  24.138  1.00104.01           C\\nANISOU  802  CA  SER A 147    11926  16901  10691    633    308  -3860       C\\nATOM    803  C   SER A 147       7.407  20.541  23.065  1.00103.85           C\\nANISOU  803  C   SER A 147    12083  16559  10818    407    370  -3277       C\\nATOM    804  O   SER A 147       7.842  20.861  21.953  1.00 99.45           O\\nANISOU  804  O   SER A 147    11570  15480  10738    539    199  -3123       O\\nATOM    805  CB  SER A 147       8.481  21.758  24.972  1.00101.67           C\\nANISOU  805  CB  SER A 147    11877  16479  10273    647     99  -3814       C\\nATOM    806  N   SER A 148       7.103  19.279  23.375  1.00100.58           N\\nANISOU  806  N   SER A 148    11778  16447   9991     56    598  -2950       N\\nATOM    807  CA  SER A 148       7.325  18.214  22.404  1.00 97.98           C\\nANISOU  807  CA  SER A 148    11636  15794   9798   -147    625  -2427       C\\nATOM    808  C   SER A 148       6.273  18.239  21.303  1.00 88.88           C\\nANISOU  808  C   SER A 148    10254  14611   8905   -117    745  -2472       C\\nATOM    809  O   SER A 148       6.602  18.071  20.125  1.00 80.56           O\\nANISOU  809  O   SER A 148     9283  13109   8218    -74    646  -2217       O\\nATOM    810  CB  SER A 148       7.339  16.858  23.106  1.00103.00           C\\nANISOU  810  CB  SER A 148    12497  16702   9935   -541    771  -2055       C\\nATOM    811  OG  SER A 148       6.089  16.599  23.719  1.00106.17           O\\nANISOU  811  OG  SER A 148    12692  17721   9926   -754   1057  -2228       O\\nATOM    812  N   LYS A 149       5.003  18.446  21.667  1.00 92.05           N\\nANISOU  812  N   LYS A 149    10349  15519   9108   -139    955  -2812       N\\nATOM    813  CA  LYS A 149       3.946  18.506  20.661  1.00 84.26           C\\nANISOU  813  CA  LYS A 149     9110  14536   8369    -93   1046  -2895       C\\nATOM    814  C   LYS A 149       4.192  19.638  19.673  1.00 88.93           C\\nANISOU  814  C   LYS A 149     9627  14634   9529    289    781  -3067       C\\nATOM    815  O   LYS A 149       3.943  19.488  18.470  1.00 93.01           O\\nANISOU  815  O   LYS A 149    10125  14862  10350    308    742  -2887       O\\nATOM    816  CB  LYS A 149       2.585  18.670  21.333  1.00 79.97           C\\nANISOU  816  CB  LYS A 149     8188  14678   7518   -142   1299  -3315       C\\nATOM    817  N   ARG A 150       4.688  20.778  20.160  1.00 87.49           N\\nANISOU  817  N   ARG A 150     9416  14340   9487    578    575  -3405       N\\nATOM    818  CA  ARG A 150       5.060  21.865  19.261  1.00 81.69           C\\nANISOU  818  CA  ARG A 150     8671  13071   9295    893    273  -3505       C\\nATOM    819  C   ARG A 150       6.223  21.474  18.359  1.00 80.21           C\\nANISOU  819  C   ARG A 150     8786  12341   9349    799    130  -2998       C\\nATOM    820  O   ARG A 150       6.317  21.964  17.230  1.00 82.46           O\\nANISOU  820  O   ARG A 150     9071  12222  10039    928    -38  -2909       O\\nATOM    821  CB  ARG A 150       5.411  23.117  20.063  1.00 80.33           C\\nANISOU  821  CB  ARG A 150     8437  12868   9215   1187     52  -3965       C\\nATOM    822  N   ARG A 151       7.111  20.595  18.831  1.00 78.36           N\\nANISOU  822  N   ARG A 151     8802  12110   8862    578    185  -2672       N\\nATOM    823  CA  ARG A 151       8.234  20.166  18.003  1.00 72.71           C\\nANISOU  823  CA  ARG A 151     8328  10937   8361    507     62  -2239       C\\nATOM    824  C   ARG A 151       7.780  19.202  16.916  1.00 79.91           C\\nANISOU  824  C   ARG A 151     9266  11777   9319    342    198  -1915       C\\nATOM    825  O   ARG A 151       8.310  19.226  15.799  1.00 80.42           O\\nANISOU  825  O   ARG A 151     9410  11464   9683    376     87  -1687       O\\nATOM    826  CB  ARG A 151       9.319  19.528  18.870  1.00 74.01           C\\nANISOU  826  CB  ARG A 151     8732  11123   8264    367     34  -2034       C\\nATOM    827  CG  ARG A 151      10.576  19.134  18.110  1.00 82.30           C\\nANISOU  827  CG  ARG A 151     9986  11745   9540    333   -108  -1658       C\\nATOM    828  CD  ARG A 151      11.637  18.577  19.045  1.00 87.06           C\\nANISOU  828  CD  ARG A 151    10798  12374   9905    242   -184  -1509       C\\nATOM    829  NE  ARG A 151      11.097  17.537  19.917  1.00 91.56           N\\nANISOU  829  NE  ARG A 151    11463  13317  10010     18     -7  -1413       N\\nATOM    830  CZ  ARG A 151      11.047  16.249  19.600  1.00 88.57           C\\nANISOU  830  CZ  ARG A 151    11241  12910   9500   -194     83  -1059       C\\nATOM    831  NH1 ARG A 151      10.538  15.370  20.453  1.00 83.32           N\\nANISOU  831  NH1 ARG A 151    10680  12574   8402   -440    216   -953       N\\nATOM    832  NH2 ARG A 151      11.506  15.837  18.428  1.00 87.56           N\\nANISOU  832  NH2 ARG A 151    11174  12429   9667   -175     27   -816       N\\nATOM    833  N   VAL A 152       6.797  18.350  17.218  1.00 81.56           N\\nANISOU  833  N   VAL A 152     9402  12365   9221    140    437  -1897       N\\nATOM    834  CA  VAL A 152       6.288  17.429  16.204  1.00 81.36           C\\nANISOU  834  CA  VAL A 152     9394  12272   9245    -25    549  -1623       C\\nATOM    835  C   VAL A 152       5.564  18.196  15.104  1.00 80.65           C\\nANISOU  835  C   VAL A 152     9093  12045   9504    168    481  -1785       C\\nATOM    836  O   VAL A 152       5.709  17.888  13.915  1.00 78.73           O\\nANISOU  836  O   VAL A 152     8921  11517   9474    149    431  -1543       O\\nATOM    837  CB  VAL A 152       5.377  16.364  16.843  1.00 80.98           C\\nANISOU  837  CB  VAL A 152     9312  12669   8787   -333    803  -1562       C\\nATOM    838  CG1 VAL A 152       5.106  15.241  15.863  1.00 82.24           C\\nANISOU  838  CG1 VAL A 152     9570  12682   8997   -541    871  -1224       C\\nATOM    839  CG2 VAL A 152       6.004  15.810  18.104  1.00 83.35           C\\nANISOU  839  CG2 VAL A 152     9819  13145   8703   -511    831  -1443       C\\nATOM    840  N   THR A 153       4.781  19.211  15.482  1.00 84.22           N\\nANISOU  840  N   THR A 153     9285  12700  10015    371    455  -2213       N\\nATOM    841  CA  THR A 153       4.057  20.004  14.492  1.00 78.54           C\\nANISOU  841  CA  THR A 153     8369  11830   9642    587    332  -2387       C\\nATOM    842  C   THR A 153       5.011  20.696  13.525  1.00 75.61           C\\nANISOU  842  C   THR A 153     8160  10910   9657    737     57  -2208       C\\nATOM    843  O   THR A 153       4.738  20.779  12.322  1.00 76.21           O\\nANISOU  843  O   THR A 153     8221  10766   9967    773    -25  -2073       O\\nATOM    844  CB  THR A 153       3.168  21.031  15.195  1.00 80.46           C\\nANISOU  844  CB  THR A 153     8306  12365   9901    832    300  -2933       C\\nATOM    845  OG1 THR A 153       2.144  20.354  15.937  1.00 82.11           O\\nANISOU  845  OG1 THR A 153     8305  13162   9733    652    595  -3096       O\\nATOM    846  CG2 THR A 153       2.527  21.976  14.186  1.00 77.79           C\\nANISOU  846  CG2 THR A 153     7796  11785   9977   1109     80  -3121       C\\nATOM    847  N   VAL A 154       6.141  21.193  14.030  1.00 73.65           N\\nANISOU  847  N   VAL A 154     8065  10459   9460    799    -90  -2194       N\\nATOM    848  CA  VAL A 154       7.112  21.843  13.156  1.00 71.40           C\\nANISOU  848  CA  VAL A 154     7922   9692   9516    880   -337  -2000       C\\nATOM    849  C   VAL A 154       7.787  20.821  12.246  1.00 67.73           C\\nANISOU  849  C   VAL A 154     7638   9069   9028    675   -255  -1548       C\\nATOM    850  O   VAL A 154       8.007  21.079  11.057  1.00 61.81           O\\nANISOU  850  O   VAL A 154     6927   8041   8515    690   -370  -1361       O\\nATOM    851  CB  VAL A 154       8.137  22.627  13.993  1.00 65.37           C\\nANISOU  851  CB  VAL A 154     7244   8781   8811    974   -518  -2127       C\\nATOM    852  CG1 VAL A 154       9.256  23.154  13.108  1.00 56.93           C\\nANISOU  852  CG1 VAL A 154     6321   7254   8055    968   -742  -1864       C\\nATOM    853  CG2 VAL A 154       7.453  23.767  14.722  1.00 60.75           C\\nANISOU  853  CG2 VAL A 154     6475   8294   8312   1228   -654  -2627       C\\nATOM    854  N   MET A 155       8.122  19.645  12.784  1.00 69.04           N\\nANISOU  854  N   MET A 155     7921   9413   8899    483    -75  -1374       N\\nATOM    855  CA  MET A 155       8.784  18.630  11.972  1.00 68.64           C\\nANISOU  855  CA  MET A 155     8035   9207   8837    329    -24  -1003       C\\nATOM    856  C   MET A 155       7.875  18.134  10.856  1.00 64.55           C\\nANISOU  856  C   MET A 155     7452   8706   8368    269     63   -905       C\\nATOM    857  O   MET A 155       8.316  17.979   9.712  1.00 59.62           O\\nANISOU  857  O   MET A 155     6898   7863   7894    252      8   -690       O\\nATOM    858  CB  MET A 155       9.241  17.467  12.851  1.00 72.37           C\\nANISOU  858  CB  MET A 155     8663   9833   9001    158     94   -859       C\\nATOM    859  CG  MET A 155      10.407  17.803  13.768  1.00 80.64           C\\nANISOU  859  CG  MET A 155     9815  10814  10011    208    -29   -884       C\\nATOM    860  SD  MET A 155      11.031  16.373  14.674  1.00 89.65           S\\nANISOU  860  SD  MET A 155    11184  12069  10810     19     37   -657       S\\nATOM    861  CE  MET A 155      12.405  17.110  15.553  1.00 99.07           C\\nANISOU  861  CE  MET A 155    12443  13153  12047    140   -171   -742       C\\nATOM    862  N   ILE A 156       6.602  17.886  11.166  1.00 67.34           N\\nANISOU  862  N   ILE A 156     7652   9352   8582    227    200  -1075       N\\nATOM    863  CA  ILE A 156       5.685  17.372  10.156  1.00 68.91           C\\nANISOU  863  CA  ILE A 156     7773   9590   8821    157    271  -1001       C\\nATOM    864  C   ILE A 156       5.469  18.403   9.059  1.00 69.08           C\\nANISOU  864  C   ILE A 156     7705   9384   9158    345     81  -1053       C\\nATOM    865  O   ILE A 156       5.484  18.072   7.867  1.00 70.31           O\\nANISOU  865  O   ILE A 156     7916   9392   9407    300     52   -852       O\\nATOM    866  CB  ILE A 156       4.357  16.945  10.806  1.00 70.36           C\\nANISOU  866  CB  ILE A 156     7765  10184   8786     48    458  -1197       C\\nATOM    867  CG1 ILE A 156       4.590  15.773  11.761  1.00 67.02           C\\nANISOU  867  CG1 ILE A 156     7488   9956   8020   -215    628  -1044       C\\nATOM    868  CG2 ILE A 156       3.332  16.571   9.742  1.00 64.85           C\\nANISOU  868  CG2 ILE A 156     6940   9528   8171     -3    496  -1169       C\\nATOM    869  CD1 ILE A 156       3.333  15.249  12.401  1.00 60.59           C\\nANISOU  869  CD1 ILE A 156     6493   9587   6942   -411    838  -1180       C\\nATOM    870  N   SER A 157       5.271  19.668   9.439  1.00 67.59           N\\nANISOU  870  N   SER A 157     7393   9155   9133    558    -76  -1325       N\\nATOM    871  CA  SER A 157       5.081  20.719   8.446  1.00 66.91           C\\nANISOU  871  CA  SER A 157     7261   8799   9364    734   -321  -1352       C\\nATOM    872  C   SER A 157       6.261  20.789   7.488  1.00 65.20           C\\nANISOU  872  C   SER A 157     7252   8247   9275    664   -437  -1006       C\\nATOM    873  O   SER A 157       6.079  20.905   6.271  1.00 70.97           O\\nANISOU  873  O   SER A 157     8005   8831  10130    658   -531   -845       O\\nATOM    874  CB  SER A 157       4.876  22.064   9.138  1.00 53.19           C\\nANISOU  874  CB  SER A 157     5403   7001   7805    983   -525  -1706       C\\nATOM    875  OG  SER A 157       3.770  22.013  10.019  1.00 59.25           O\\nANISOU  875  OG  SER A 157     5930   8154   8428   1059   -395  -2076       O\\nATOM    876  N   ILE A 158       7.481  20.701   8.019  1.00 63.38           N\\nANISOU  876  N   ILE A 158     7159   7930   8993    600   -428   -895       N\\nATOM    877  CA  ILE A 158       8.662  20.757   7.168  1.00 62.29           C\\nANISOU  877  CA  ILE A 158     7167   7544   8955    516   -512   -595       C\\nATOM    878  C   ILE A 158       8.684  19.577   6.207  1.00 66.42           C\\nANISOU  878  C   ILE A 158     7754   8134   9350    369   -356   -352       C\\nATOM    879  O   ILE A 158       9.069  19.717   5.042  1.00 76.92           O\\nANISOU  879  O   ILE A 158     9134   9324  10767    323   -426   -148       O\\nATOM    880  CB  ILE A 158       9.935  20.815   8.030  1.00 62.52           C\\nANISOU  880  CB  ILE A 158     7286   7519   8948    483   -529   -568       C\\nATOM    881  CG1 ILE A 158       9.969  22.114   8.833  1.00 61.54           C\\nANISOU  881  CG1 ILE A 158     7112   7280   8990    635   -734   -823       C\\nATOM    882  CG2 ILE A 158      11.177  20.683   7.165  1.00 56.51           C\\nANISOU  882  CG2 ILE A 158     6625   6594   8253    369   -564   -273       C\\nATOM    883  CD1 ILE A 158      11.102  22.178   9.819  1.00 68.44           C\\nANISOU  883  CD1 ILE A 158     8055   8136   9811    610   -764   -846       C\\nATOM    884  N   VAL A 159       8.260  18.399   6.670  1.00 61.58           N\\nANISOU  884  N   VAL A 159     7145   7737   8515    280   -157   -371       N\\nATOM    885  CA  VAL A 159       8.270  17.217   5.808  1.00 61.95           C\\nANISOU  885  CA  VAL A 159     7267   7816   8456    152    -40   -177       C\\nATOM    886  C   VAL A 159       7.403  17.448   4.578  1.00 58.47           C\\nANISOU  886  C   VAL A 159     6754   7353   8111    173    -97   -152       C\\nATOM    887  O   VAL A 159       7.847  17.270   3.437  1.00 64.62           O\\nANISOU  887  O   VAL A 159     7599   8038   8915    129   -128     32       O\\nATOM    888  CB  VAL A 159       7.811  15.973   6.589  1.00 61.71           C\\nANISOU  888  CB  VAL A 159     7270   7984   8194     28    136   -202       C\\nATOM    889  CG1 VAL A 159       7.571  14.812   5.641  1.00 58.85           C\\nANISOU  889  CG1 VAL A 159     6974   7622   7763    -90    212    -53       C\\nATOM    890  CG2 VAL A 159       8.840  15.593   7.634  1.00 64.69           C\\nANISOU  890  CG2 VAL A 159     7772   8351   8457     -6    154   -157       C\\nATOM    891  N   TRP A 160       6.156  17.865   4.792  1.00 55.67           N\\nANISOU  891  N   TRP A 160     6244   7112   7797    249   -122   -357       N\\nATOM    892  CA  TRP A 160       5.209  17.964   3.688  1.00 61.87           C\\nANISOU  892  CA  TRP A 160     6946   7902   8658    275   -191   -352       C\\nATOM    893  C   TRP A 160       5.414  19.222   2.854  1.00 68.14           C\\nANISOU  893  C   TRP A 160     7758   8458   9675    394   -447   -287       C\\nATOM    894  O   TRP A 160       5.155  19.201   1.645  1.00 72.46           O\\nANISOU  894  O   TRP A 160     8331   8951  10250    369   -527   -148       O\\nATOM    895  CB  TRP A 160       3.778  17.893   4.226  1.00 54.20           C\\nANISOU  895  CB  TRP A 160     5762   7176   7654    313   -130   -618       C\\nATOM    896  CG  TRP A 160       3.447  16.528   4.729  1.00 59.47           C\\nANISOU  896  CG  TRP A 160     6436   8074   8087    111    106   -599       C\\nATOM    897  CD1 TRP A 160       3.428  16.111   6.027  1.00 64.43           C\\nANISOU  897  CD1 TRP A 160     7047   8894   8538     21    258   -694       C\\nATOM    898  CD2 TRP A 160       3.129  15.380   3.933  1.00 65.48           C\\nANISOU  898  CD2 TRP A 160     7253   8873   8755    -53    190   -456       C\\nATOM    899  NE1 TRP A 160       3.105  14.776   6.089  1.00 64.83           N\\nANISOU  899  NE1 TRP A 160     7153   9080   8400   -211    420   -586       N\\nATOM    900  CE2 TRP A 160       2.917  14.305   4.817  1.00 67.13           C\\nANISOU  900  CE2 TRP A 160     7487   9263   8758   -251    374   -455       C\\nATOM    901  CE3 TRP A 160       2.997  15.161   2.558  1.00 66.76           C\\nANISOU  901  CE3 TRP A 160     7455   8935   8975    -62    110   -331       C\\nATOM    902  CZ2 TRP A 160       2.575  13.030   4.371  1.00 70.04           C\\nANISOU  902  CZ2 TRP A 160     7926   9666   9019   -454    457   -337       C\\nATOM    903  CZ3 TRP A 160       2.659  13.895   2.117  1.00 69.12           C\\nANISOU  903  CZ3 TRP A 160     7807   9302   9154   -239    209   -252       C\\nATOM    904  CH2 TRP A 160       2.451  12.846   3.021  1.00 68.25           C\\nANISOU  904  CH2 TRP A 160     7727   9325   8880   -431    370   -257       C\\nATOM    905  N   VAL A 161       5.874  20.317   3.463  1.00 67.95           N\\nANISOU  905  N   VAL A 161     7737   8280   9802    507   -599   -373       N\\nATOM    906  CA  VAL A 161       6.140  21.520   2.680  1.00 69.19           C\\nANISOU  906  CA  VAL A 161     7952   8155  10182    576   -883   -262       C\\nATOM    907  C   VAL A 161       7.379  21.323   1.823  1.00 65.64           C\\nANISOU  907  C   VAL A 161     7665   7597   9678    402   -867     76       C\\nATOM    908  O   VAL A 161       7.447  21.799   0.684  1.00 71.00           O\\nANISOU  908  O   VAL A 161     8411   8144  10420    354  -1023    278       O\\nATOM    909  CB  VAL A 161       6.273  22.747   3.599  1.00 68.92           C\\nANISOU  909  CB  VAL A 161     7883   7953  10351    740  -1087   -473       C\\nATOM    910  CG1 VAL A 161       6.754  23.958   2.810  1.00 55.10           C\\nANISOU  910  CG1 VAL A 161     6251   5845   8841    751  -1414   -291       C\\nATOM    911  CG2 VAL A 161       4.941  23.041   4.271  1.00 68.37           C\\nANISOU  911  CG2 VAL A 161     7604   8033  10340    947  -1123   -858       C\\nATOM    912  N   LEU A 162       8.370  20.607   2.346  1.00 57.34           N\\nANISOU  912  N   LEU A 162     6669   6627   8492    302   -683    137       N\\nATOM    913  CA  LEU A 162       9.567  20.343   1.562  1.00 62.34           C\\nANISOU  913  CA  LEU A 162     7399   7226   9060    152   -640    403       C\\nATOM    914  C   LEU A 162       9.274  19.375   0.424  1.00 64.44           C\\nANISOU  914  C   LEU A 162     7686   7633   9165     68   -521    527       C\\nATOM    915  O   LEU A 162       9.756  19.565  -0.698  1.00 73.70           O\\nANISOU  915  O   LEU A 162     8910   8787  10307    -32   -568    735       O\\nATOM    916  CB  LEU A 162      10.668  19.803   2.467  1.00 66.33           C\\nANISOU  916  CB  LEU A 162     7929   7786   9485    111   -507    389       C\\nATOM    917  CG  LEU A 162      12.083  19.741   1.909  1.00 71.44           C\\nANISOU  917  CG  LEU A 162     8616   8419  10108    -16   -484    596       C\\nATOM    918  CD1 LEU A 162      12.409  21.020   1.165  1.00 63.78           C\\nANISOU  918  CD1 LEU A 162     7665   7275   9293    -96   -691    765       C\\nATOM    919  CD2 LEU A 162      13.044  19.530   3.061  1.00 75.47           C\\nANISOU  919  CD2 LEU A 162     9125   8941  10610      0   -439    519       C\\nATOM    920  N   SER A 163       8.481  18.334   0.691  1.00 62.39           N\\nANISOU  920  N   SER A 163     7390   7531   8786     86   -371    399       N\\nATOM    921  CA  SER A 163       8.099  17.410  -0.371  1.00 64.81           C\\nANISOU  921  CA  SER A 163     7718   7951   8957     15   -289    475       C\\nATOM    922  C   SER A 163       7.384  18.143  -1.499  1.00 65.90           C\\nANISOU  922  C   SER A 163     7840   8039   9160     33   -467    552       C\\nATOM    923  O   SER A 163       7.634  17.874  -2.680  1.00 71.94           O\\nANISOU  923  O   SER A 163     8662   8855   9817    -51   -466    710       O\\nATOM    924  CB  SER A 163       7.213  16.302   0.193  1.00 64.78           C\\nANISOU  924  CB  SER A 163     7674   8087   8852      4   -146    321       C\\nATOM    925  OG  SER A 163       7.785  15.740   1.357  1.00 61.15           O\\nANISOU  925  OG  SER A 163     7254   7650   8329    -18    -31    269       O\\nATOM    926  N   PHE A 164       6.497  19.078  -1.153  1.00 60.59           N\\nANISOU  926  N   PHE A 164     7089   7277   8655    156   -639    427       N\\nATOM    927  CA  PHE A 164       5.825  19.887  -2.164  1.00 61.72           C\\nANISOU  927  CA  PHE A 164     7234   7322   8893    201   -880    505       C\\nATOM    928  C   PHE A 164       6.833  20.691  -2.972  1.00 65.16           C\\nANISOU  928  C   PHE A 164     7806   7601   9350     94  -1027    793       C\\nATOM    929  O   PHE A 164       6.879  20.597  -4.203  1.00 65.92           O\\nANISOU  929  O   PHE A 164     7974   7746   9327    -10  -1074    992       O\\nATOM    930  CB  PHE A 164       4.803  20.813  -1.496  1.00 57.42           C\\nANISOU  930  CB  PHE A 164     6564   6683   8568    400  -1076    267       C\\nATOM    931  CG  PHE A 164       4.135  21.779  -2.443  1.00 61.42           C\\nANISOU  931  CG  PHE A 164     7089   7023   9226    488  -1405    340       C\\nATOM    932  CD1 PHE A 164       3.067  21.374  -3.232  1.00 63.79           C\\nANISOU  932  CD1 PHE A 164     7317   7446   9476    519  -1453    302       C\\nATOM    933  CD2 PHE A 164       4.563  23.097  -2.528  1.00 60.79           C\\nANISOU  933  CD2 PHE A 164     7109   6640   9350    534  -1703    451       C\\nATOM    934  CE1 PHE A 164       2.450  22.259  -4.099  1.00 64.22           C\\nANISOU  934  CE1 PHE A 164     7400   7336   9667    615  -1799    378       C\\nATOM    935  CE2 PHE A 164       3.946  23.988  -3.393  1.00 65.28           C\\nANISOU  935  CE2 PHE A 164     7729   7008  10065    614  -2062    545       C\\nATOM    936  CZ  PHE A 164       2.889  23.566  -4.178  1.00 64.54           C\\nANISOU  936  CZ  PHE A 164     7564   7051   9906    666  -2113    510       C\\nATOM    937  N   THR A 165       7.667  21.477  -2.285  1.00 60.91           N\\nANISOU  937  N   THR A 165     7302   6899   8944     90  -1100    820       N\\nATOM    938  CA  THR A 165       8.590  22.366  -2.984  1.00 68.08           C\\nANISOU  938  CA  THR A 165     8326   7648   9893    -59  -1264   1109       C\\nATOM    939  C   THR A 165       9.585  21.592  -3.836  1.00 67.06           C\\nANISOU  939  C   THR A 165     8237   7731   9511   -266  -1055   1321       C\\nATOM    940  O   THR A 165      10.068  22.114  -4.846  1.00 74.56           O\\nANISOU  940  O   THR A 165     9269   8666  10395   -439  -1158   1596       O\\nATOM    941  CB  THR A 165       9.335  23.256  -1.988  1.00 72.21           C\\nANISOU  941  CB  THR A 165     8862   7963  10613    -43  -1373   1067       C\\nATOM    942  OG1 THR A 165      10.064  22.439  -1.068  1.00 84.36           O\\nANISOU  942  OG1 THR A 165    10343   9656  12055    -52  -1111    946       O\\nATOM    943  CG2 THR A 165       8.362  24.133  -1.215  1.00 69.54           C\\nANISOU  943  CG2 THR A 165     8475   7415  10531    191  -1616    813       C\\nATOM    944  N   ILE A 166       9.898  20.352  -3.455  1.00 69.64           N\\nANISOU  944  N   ILE A 166     8506   8267   9687   -255   -775   1193       N\\nATOM    945  CA  ILE A 166      10.825  19.548  -4.247  1.00 72.15           C\\nANISOU  945  CA  ILE A 166     8831   8805   9778   -397   -585   1317       C\\nATOM    946  C   ILE A 166      10.150  19.043  -5.520  1.00 72.60           C\\nANISOU  946  C   ILE A 166     8918   9016   9653   -435   -578   1379       C\\nATOM    947  O   ILE A 166      10.751  19.045  -6.601  1.00 74.34           O\\nANISOU  947  O   ILE A 166     9167   9388   9690   -588   -548   1564       O\\nATOM    948  CB  ILE A 166      11.383  18.389  -3.402  1.00 64.44           C\\nANISOU  948  CB  ILE A 166     7804   7945   8737   -337   -355   1141       C\\nATOM    949  CG1 ILE A 166      12.401  18.911  -2.386  1.00 65.09           C\\nANISOU  949  CG1 ILE A 166     7859   7927   8946   -345   -368   1133       C\\nATOM    950  CG2 ILE A 166      12.008  17.326  -4.294  1.00 61.90           C\\nANISOU  950  CG2 ILE A 166     7469   7861   8189   -405   -177   1168       C\\nATOM    951  CD1 ILE A 166      12.979  17.825  -1.505  1.00 55.41           C\\nANISOU  951  CD1 ILE A 166     6604   6788   7663   -276   -195    979       C\\nATOM    952  N   SER A 167       8.896  18.605  -5.414  1.00 66.08           N\\nANISOU  952  N   SER A 167     8070   8185   8852   -311   -603   1216       N\\nATOM    953  CA  SER A 167       8.168  18.066  -6.554  1.00 69.77           C\\nANISOU  953  CA  SER A 167     8557   8794   9156   -335   -616   1237       C\\nATOM    954  C   SER A 167       7.500  19.138  -7.404  1.00 70.97           C\\nANISOU  954  C   SER A 167     8769   8841   9355   -354   -900   1407       C\\nATOM    955  O   SER A 167       7.132  18.860  -8.553  1.00 69.63           O\\nANISOU  955  O   SER A 167     8642   8809   9005   -415   -942   1493       O\\nATOM    956  CB  SER A 167       7.104  17.078  -6.070  1.00 67.68           C\\nANISOU  956  CB  SER A 167     8226   8582   8907   -228   -531    989       C\\nATOM    957  OG  SER A 167       6.153  17.737  -5.251  1.00 68.82           O\\nANISOU  957  OG  SER A 167     8295   8591   9261   -104   -663    859       O\\nATOM    958  N   CYS A 168       7.324  20.345  -6.871  1.00 72.75           N\\nANISOU  958  N   CYS A 168     9009   8812   9819   -293  -1126   1446       N\\nATOM    959  CA  CYS A 168       6.648  21.393  -7.631  1.00 73.51           C\\nANISOU  959  CA  CYS A 168     9186   8743  10001   -284  -1466   1607       C\\nATOM    960  C   CYS A 168       7.347  21.747  -8.942  1.00 77.62           C\\nANISOU  960  C   CYS A 168     9848   9341  10301   -524  -1540   1966       C\\nATOM    961  O   CYS A 168       6.638  22.045  -9.918  1.00 81.68           O\\nANISOU  961  O   CYS A 168    10442   9849  10744   -540  -1760   2098       O\\nATOM    962  CB  CYS A 168       6.478  22.640  -6.754  1.00 74.94           C\\nANISOU  962  CB  CYS A 168     9371   8593  10510   -158  -1727   1556       C\\nATOM    963  SG  CYS A 168       5.411  23.906  -7.472  1.00 83.98           S\\nANISOU  963  SG  CYS A 168    10608   9450  11852    -51  -2231   1669       S\\nATOM    964  N   PRO A 169       8.683  21.755  -9.044  1.00 78.38           N\\nANISOU  964  N   PRO A 169     9970   9541  10269   -727  -1380   2136       N\\nATOM    965  CA  PRO A 169       9.296  22.005 -10.360  1.00 83.73           C\\nANISOU  965  CA  PRO A 169    10752  10394  10669   -996  -1410   2471       C\\nATOM    966  C   PRO A 169       8.894  21.001 -11.428  1.00 84.95           C\\nANISOU  966  C   PRO A 169    10900  10878  10501  -1015  -1280   2429       C\\nATOM    967  O   PRO A 169       8.857  21.362 -12.611  1.00 84.19           O\\nANISOU  967  O   PRO A 169    10915  10894  10178  -1189  -1413   2692       O\\nATOM    968  CB  PRO A 169      10.799  21.935 -10.063  1.00 82.55           C\\nANISOU  968  CB  PRO A 169    10540  10383  10443  -1178  -1179   2547       C\\nATOM    969  CG  PRO A 169      10.912  22.332  -8.645  1.00 76.42           C\\nANISOU  969  CG  PRO A 169     9712   9325   9998  -1032  -1220   2380       C\\nATOM    970  CD  PRO A 169       9.698  21.762  -7.973  1.00 74.69           C\\nANISOU  970  CD  PRO A 169     9435   9030   9916   -740  -1219   2057       C\\nATOM    971  N   LEU A 170       8.584  19.755 -11.051  1.00 79.08           N\\nANISOU  971  N   LEU A 170    10044  10281   9723   -856  -1047   2113       N\\nATOM    972  CA  LEU A 170       8.270  18.731 -12.044  1.00 73.43           C\\nANISOU  972  CA  LEU A 170     9322   9863   8714   -871   -932   2033       C\\nATOM    973  C   LEU A 170       7.035  19.090 -12.860  1.00 76.56           C\\nANISOU  973  C   LEU A 170     9801  10208   9081   -835  -1215   2109       C\\nATOM    974  O   LEU A 170       6.917  18.677 -14.020  1.00 77.86           O\\nANISOU  974  O   LEU A 170    10015  10626   8942   -927  -1211   2171       O\\nATOM    975  CB  LEU A 170       8.080  17.380 -11.356  1.00 67.28           C\\nANISOU  975  CB  LEU A 170     8435   9155   7972   -710   -697   1684       C\\nATOM    976  CG  LEU A 170       9.176  16.975 -10.366  1.00 66.79           C\\nANISOU  976  CG  LEU A 170     8297   9091   7988   -692   -470   1577       C\\nATOM    977  CD1 LEU A 170       8.737  15.773  -9.563  1.00 66.74           C\\nANISOU  977  CD1 LEU A 170     8235   9057   8068   -536   -332   1276       C\\nATOM    978  CD2 LEU A 170      10.488  16.689 -11.074  1.00 61.58           C\\nANISOU  978  CD2 LEU A 170     7607   8724   7065   -840   -287   1659       C\\nATOM    979  N   LEU A 171       6.108  19.856 -12.280  1.00 72.91           N\\nANISOU  979  N   LEU A 171     9340   9439   8925   -685  -1477   2076       N\\nATOM    980  CA  LEU A 171       4.945  20.322 -13.024  1.00 75.80           C\\nANISOU  980  CA  LEU A 171     9768   9727   9306   -622  -1806   2146       C\\nATOM    981  C   LEU A 171       5.311  21.339 -14.094  1.00 79.71           C\\nANISOU  981  C   LEU A 171    10460  10190   9637   -830  -2066   2561       C\\nATOM    982  O   LEU A 171       4.541  21.531 -15.041  1.00 84.88           O\\nANISOU  982  O   LEU A 171    11203  10874  10173   -833  -2320   2673       O\\nATOM    983  CB  LEU A 171       3.917  20.942 -12.075  1.00 74.05           C\\nANISOU  983  CB  LEU A 171     9460   9199   9478   -376  -2034   1961       C\\nATOM    984  CG  LEU A 171       2.918  20.015 -11.385  1.00 69.74           C\\nANISOU  984  CG  LEU A 171     8717   8733   9050   -185  -1900   1574       C\\nATOM    985  CD1 LEU A 171       2.056  20.807 -10.416  1.00 68.86           C\\nANISOU  985  CD1 LEU A 171     8486   8373   9305     44  -2112   1385       C\\nATOM    986  CD2 LEU A 171       2.059  19.311 -12.420  1.00 65.45           C\\nANISOU  986  CD2 LEU A 171     8160   8395   8313   -188  -1959   1520       C\\nATOM    987  N   PHE A 172       6.460  21.995 -13.967  1.00 68.04           N\\nANISOU  987  N   PHE A 172     9054   8656   8140  -1028  -2027   2807       N\\nATOM    988  CA  PHE A 172       6.795  23.074 -14.882  1.00 78.77           C\\nANISOU  988  CA  PHE A 172    10620   9942   9366  -1280  -2310   3252       C\\nATOM    989  C   PHE A 172       8.096  22.777 -15.619  1.00 85.91           C\\nANISOU  989  C   PHE A 172    11542  11237   9862  -1615  -2028   3473       C\\nATOM    990  O   PHE A 172       9.011  23.607 -15.641  1.00 88.20           O\\nANISOU  990  O   PHE A 172    11911  11460  10141  -1873  -2078   3779       O\\nATOM    991  CB  PHE A 172       6.876  24.399 -14.118  1.00 84.73           C\\nANISOU  991  CB  PHE A 172    11461  10224  10509  -1254  -2621   3391       C\\nATOM    992  CG  PHE A 172       5.617  24.738 -13.360  1.00 85.93           C\\nANISOU  992  CG  PHE A 172    11551  10035  11063   -893  -2895   3113       C\\nATOM    993  CD1 PHE A 172       4.602  25.461 -13.964  1.00 86.94           C\\nANISOU  993  CD1 PHE A 172    11803   9937  11293   -793  -3356   3232       C\\nATOM    994  CD2 PHE A 172       5.447  24.323 -12.046  1.00 83.56           C\\nANISOU  994  CD2 PHE A 172    11054   9673  11022   -654  -2699   2721       C\\nATOM    995  CE1 PHE A 172       3.443  25.769 -13.275  1.00 83.30           C\\nANISOU  995  CE1 PHE A 172    11232   9212  11208   -436  -3605   2923       C\\nATOM    996  CE2 PHE A 172       4.288  24.629 -11.350  1.00 82.96           C\\nANISOU  996  CE2 PHE A 172    10876   9366  11280   -334  -2919   2431       C\\nATOM    997  CZ  PHE A 172       3.286  25.353 -11.967  1.00 83.10           C\\nANISOU  997  CZ  PHE A 172    10978   9179  11417   -212  -3367   2511       C\\nATOM    998  N   GLY A 173       8.179  21.592 -16.224  1.00 92.00           N\\nANISOU  998  N   GLY A 173    12224  12431  10302  -1618  -1741   3296       N\\nATOM    999  CA  GLY A 173       9.333  21.223 -17.023  1.00 99.29           C\\nANISOU  999  CA  GLY A 173    13120  13810  10797  -1900  -1463   3431       C\\nATOM   1000  C   GLY A 173      10.629  21.114 -16.255  1.00105.40           C\\nANISOU 1000  C   GLY A 173    13746  14661  11642  -1983  -1167   3370       C\\nATOM   1001  O   GLY A 173      11.703  21.225 -16.853  1.00109.34           O\\nANISOU 1001  O   GLY A 173    14209  15498  11836  -2275   -998   3563       O\\nATOM   1002  N   LEU A 174      10.558  20.899 -14.940  1.00100.46           N\\nANISOU 1002  N   LEU A 174    13015  13761  11393  -1742  -1102   3100       N\\nATOM   1003  CA  LEU A 174      11.734  20.873 -14.068  1.00103.35           C\\nANISOU 1003  CA  LEU A 174    13246  14141  11880  -1788   -879   3034       C\\nATOM   1004  C   LEU A 174      12.539  22.163 -14.183  1.00110.64           C\\nANISOU 1004  C   LEU A 174    14250  14960  12828  -2107  -1028   3434       C\\nATOM   1005  O   LEU A 174      13.746  22.179 -13.930  1.00113.38           O\\nANISOU 1005  O   LEU A 174    14470  15481  13128  -2273   -823   3467       O\\nATOM   1006  CB  LEU A 174      12.615  19.654 -14.361  1.00 97.67           C\\nANISOU 1006  CB  LEU A 174    12350  13885  10875  -1796   -492   2806       C\\nATOM   1007  CG  LEU A 174      13.534  19.118 -13.264  1.00 92.37           C\\nANISOU 1007  CG  LEU A 174    11502  13215  10381  -1682   -254   2560       C\\nATOM   1008  CD1 LEU A 174      12.928  19.339 -11.890  1.00 88.80           C\\nANISOU 1008  CD1 LEU A 174    11078  12307  10354  -1450   -387   2419       C\\nATOM   1009  CD2 LEU A 174      13.792  17.638 -13.505  1.00 90.06           C\\nANISOU 1009  CD2 LEU A 174    11076  13252   9891  -1525     22   2210       C\\nATOM   1010  N   ASN A 175      11.863  23.254 -14.556  1.00127.08           N\\nANISOU 1010  N   ASN A 175    16542  16739  15004  -2196  -1417   3738       N\\nATOM   1011  CA  ASN A 175      12.511  24.539 -14.814  1.00131.09           C\\nANISOU 1011  CA  ASN A 175    17185  17092  15530  -2547  -1637   4178       C\\nATOM   1012  C   ASN A 175      13.737  24.358 -15.706  1.00135.52           C\\nANISOU 1012  C   ASN A 175    17627  18169  15696  -2875  -1339   4267       C\\nATOM   1013  O   ASN A 175      14.777  24.991 -15.516  1.00141.49           O\\nANISOU 1013  O   ASN A 175    18317  18930  16514  -3096  -1295   4368       O\\nATOM   1014  CB  ASN A 175      12.876  25.244 -13.504  1.00127.19           C\\nANISOU 1014  CB  ASN A 175    16665  16177  15484  -2475  -1748   4122       C\\nATOM   1015  CG  ASN A 175      11.656  25.790 -12.774  1.00121.37           C\\nANISOU 1015  CG  ASN A 175    16035  14913  15169  -2144  -2109   3974       C\\nATOM   1016  OD1 ASN A 175      10.689  26.228 -13.400  1.00120.30           O\\nANISOU 1016  OD1 ASN A 175    16064  14605  15041  -2092  -2430   4105       O\\nATOM   1017  ND2 ASN A 175      11.697  25.764 -11.445  1.00115.08           N\\nANISOU 1017  ND2 ASN A 175    15127  13886  14713  -1906  -2061   3672       N\\nATOM   1018  N   ASN A 176      13.611  23.469 -16.686  1.00138.51           N\\nANISOU 1018  N   ASN A 176    17960  19005  15662  -2893  -1141   4194       N\\nATOM   1019  CA  ASN A 176      14.702  23.139 -17.593  1.00128.90           C\\nANISOU 1019  CA  ASN A 176    16590  18346  14041  -3148   -837   4194       C\\nATOM   1020  C   ASN A 176      14.143  23.135 -19.012  1.00130.29           C\\nANISOU 1020  C   ASN A 176    16893  18756  13854  -3256   -934   4312       C\\nATOM   1021  O   ASN A 176      13.054  23.656 -19.280  1.00128.25           O\\nANISOU 1021  O   ASN A 176    16856  18174  13701  -3186  -1280   4456       O\\nATOM   1022  CB  ASN A 176      15.347  21.804 -17.188  1.00114.40           C\\nANISOU 1022  CB  ASN A 176    14490  16909  12066  -3004   -416   3849       C\\nATOM   1023  N   ALA A 177      14.888  22.541 -19.940  1.00131.35           N\\nANISOU 1023  N   ALA A 177    16876  19466  13564  -3410   -639   4223       N\\nATOM   1024  CA  ALA A 177      14.518  22.512 -21.354  1.00133.06           C\\nANISOU 1024  CA  ALA A 177    17193  19978  13388  -3547   -695   4324       C\\nATOM   1025  C   ALA A 177      13.850  21.175 -21.665  1.00139.43           C\\nANISOU 1025  C   ALA A 177    17953  21060  13966  -3279   -543   3999       C\\nATOM   1026  O   ALA A 177      14.499  20.218 -22.087  1.00134.42           O\\nANISOU 1026  O   ALA A 177    17113  20932  13028  -3260   -210   3722       O\\nATOM   1027  CB  ALA A 177      15.744  22.740 -22.230  1.00132.82           C\\nANISOU 1027  CB  ALA A 177    17018  20431  13018  -3895   -487   4415       C\\nATOM   1028  N   ASP A 178      12.535  21.113 -21.456  1.00139.56           N\\nANISOU 1028  N   ASP A 178    18147  20737  14141  -3057   -814   4002       N\\nATOM   1029  CA  ASP A 178      11.738  19.985 -21.927  1.00140.00           C\\nANISOU 1029  CA  ASP A 178    18203  21034  13957  -2843   -761   3735       C\\nATOM   1030  C   ASP A 178      10.328  20.465 -22.235  1.00139.46           C\\nANISOU 1030  C   ASP A 178    18375  20618  13994  -2746  -1185   3897       C\\nATOM   1031  O   ASP A 178       9.372  20.082 -21.554  1.00142.64           O\\nANISOU 1031  O   ASP A 178    18808  20766  14622  -2479  -1336   3761       O\\nATOM   1032  CB  ASP A 178      11.711  18.857 -20.894  1.00137.06           C\\nANISOU 1032  CB  ASP A 178    17675  20675  13728  -2556   -547   3368       C\\nATOM   1033  N   GLN A 179      10.191  21.295 -23.270  1.00143.02           N\\nANISOU 1033  N   GLN A 179    18983  21074  14284  -2960  -1392   4178       N\\nATOM   1034  CA  GLN A 179       8.987  22.105 -23.424  1.00133.33           C\\nANISOU 1034  CA  GLN A 179    17987  19403  13269  -2879  -1859   4383       C\\nATOM   1035  C   GLN A 179       7.753  21.243 -23.675  1.00128.51           C\\nANISOU 1035  C   GLN A 179    17406  18844  12578  -2605  -1987   4153       C\\nATOM   1036  O   GLN A 179       6.787  21.279 -22.902  1.00124.40           O\\nANISOU 1036  O   GLN A 179    16911  17946  12410  -2345  -2237   4071       O\\nATOM   1037  CB  GLN A 179       9.188  23.117 -24.553  1.00132.56           C\\nANISOU 1037  CB  GLN A 179    18056  19342  12970  -3191  -2041   4737       C\\nATOM   1038  N   ASN A 180       7.766  20.455 -24.749  1.00126.77           N\\nANISOU 1038  N   ASN A 180    17160  19104  11903  -2656  -1831   4014       N\\nATOM   1039  CA  ASN A 180       6.565  19.780 -25.230  1.00115.92           C\\nANISOU 1039  CA  ASN A 180    15839  17790  10414  -2448  -2017   3825       C\\nATOM   1040  C   ASN A 180       6.535  18.292 -24.886  1.00111.57           C\\nANISOU 1040  C   ASN A 180    15109  17542   9741  -2253  -1745   3379       C\\nATOM   1041  O   ASN A 180       5.949  17.498 -25.625  1.00103.18           O\\nANISOU 1041  O   ASN A 180    14050  16740   8415  -2166  -1771   3154       O\\nATOM   1042  CB  ASN A 180       6.419  19.972 -26.739  1.00115.56           C\\nANISOU 1042  CB  ASN A 180    15926  18028   9952  -2620  -2110   3964       C\\nATOM   1043  N   GLU A 181       7.135  17.896 -23.764  1.00104.62           N\\nANISOU 1043  N   GLU A 181    14065  16578   9107  -2156  -1490   3195       N\\nATOM   1044  CA  GLU A 181       7.136  16.494 -23.369  1.00106.80           C\\nANISOU 1044  CA  GLU A 181    14149  16965   9465  -1902  -1204   2656       C\\nATOM   1045  C   GLU A 181       6.948  16.366 -21.867  1.00100.72           C\\nANISOU 1045  C   GLU A 181    13266  15721   9281  -1661  -1157   2456       C\\nATOM   1046  O   GLU A 181       7.211  17.295 -21.099  1.00102.83           O\\nANISOU 1046  O   GLU A 181    13557  15677   9838  -1708  -1233   2688       O\\nATOM   1047  CB  GLU A 181       8.426  15.780 -23.782  1.00111.20           C\\nANISOU 1047  CB  GLU A 181    14562  18052   9639  -2014   -799   2478       C\\nATOM   1048  CG  GLU A 181       8.455  15.363 -25.237  1.00118.18           C\\nANISOU 1048  CG  GLU A 181    15491  19499   9912  -2150   -768   2439       C\\nATOM   1049  CD  GLU A 181       9.558  14.373 -25.529  1.00125.80           C\\nANISOU 1049  CD  GLU A 181    16244  20936  10620  -2119   -359   2054       C\\nATOM   1050  OE1 GLU A 181       9.649  13.356 -24.809  1.00127.00           O\\nANISOU 1050  OE1 GLU A 181    16258  20997  10999  -1858   -200   1630       O\\nATOM   1051  OE2 GLU A 181      10.339  14.618 -26.473  1.00132.18           O\\nANISOU 1051  OE2 GLU A 181    16999  22090  11133  -2311   -210   2123       O\\nATOM   1052  N   CYS A 182       6.490  15.185 -21.461  1.00 85.77           N\\nANISOU 1052  N   CYS A 182    11262  13784   7544  -1421  -1042   2020       N\\nATOM   1053  CA  CYS A 182       6.326  14.886 -20.051  1.00 85.01           C\\nANISOU 1053  CA  CYS A 182    11057  13309   7934  -1219   -963   1809       C\\nATOM   1054  C   CYS A 182       7.659  15.034 -19.325  1.00 85.25           C\\nANISOU 1054  C   CYS A 182    10998  13354   8038  -1280   -699   1848       C\\nATOM   1055  O   CYS A 182       8.737  14.991 -19.927  1.00 87.66           O\\nANISOU 1055  O   CYS A 182    11266  14030   8011  -1441   -506   1910       O\\nATOM   1056  CB  CYS A 182       5.770  13.473 -19.864  1.00 85.07           C\\nANISOU 1056  CB  CYS A 182    10980  13320   8021  -1022   -869   1364       C\\nATOM   1057  SG  CYS A 182       5.430  13.056 -18.147  1.00 88.55           S\\nANISOU 1057  SG  CYS A 182    11313  13325   9006   -826   -793   1143       S\\nATOM   1058  N   ILE A 183       7.575  15.222 -18.009  1.00 86.69           N\\nANISOU 1058  N   ILE A 183    11127  13162   8650  -1153   -694   1796       N\\nATOM   1059  CA  ILE A 183       8.782  15.505 -17.243  1.00 88.06           C\\nANISOU 1059  CA  ILE A 183    11221  13307   8931  -1209   -498   1856       C\\nATOM   1060  C   ILE A 183       9.631  14.253 -17.070  1.00 90.76           C\\nANISOU 1060  C   ILE A 183    11430  13873   9183  -1113   -193   1518       C\\nATOM   1061  O   ILE A 183      10.856  14.349 -16.944  1.00 89.70           O\\nANISOU 1061  O   ILE A 183    11199  13916   8966  -1199     -1   1550       O\\nATOM   1062  CB  ILE A 183       8.428  16.141 -15.888  1.00 82.65           C\\nANISOU 1062  CB  ILE A 183    10529  12169   8706  -1098   -610   1893       C\\nATOM   1063  CG1 ILE A 183       9.689  16.703 -15.236  1.00 81.90           C\\nANISOU 1063  CG1 ILE A 183    10377  12044   8696  -1203   -475   2026       C\\nATOM   1064  CG2 ILE A 183       7.755  15.134 -14.972  1.00 80.02           C\\nANISOU 1064  CG2 ILE A 183    10121  11657   8626   -869   -543   1542       C\\nATOM   1065  CD1 ILE A 183      10.562  17.486 -16.201  1.00 77.13           C\\nANISOU 1065  CD1 ILE A 183     9815  11711   7778  -1501   -472   2363       C\\nATOM   1066  N   ILE A 184       9.020  13.066 -17.078  1.00 86.05           N\\nANISOU 1066  N   ILE A 184    10817  13266   8612   -938   -167   1182       N\\nATOM   1067  CA  ILE A 184       9.808  11.848 -16.945  1.00 81.50           C\\nANISOU 1067  CA  ILE A 184    10141  12849   7978   -818     61    843       C\\nATOM   1068  C   ILE A 184      10.649  11.603 -18.187  1.00 77.44           C\\nANISOU 1068  C   ILE A 184     9566  12848   7010   -918    205    786       C\\nATOM   1069  O   ILE A 184      11.589  10.802 -18.148  1.00 77.18           O\\nANISOU 1069  O   ILE A 184     9408  13014   6904   -822    403    514       O\\nATOM   1070  CB  ILE A 184       8.907  10.636 -16.645  1.00 80.64           C\\nANISOU 1070  CB  ILE A 184    10060  12549   8030   -635      7    515       C\\nATOM   1071  CG1 ILE A 184       9.694   9.574 -15.876  1.00 78.25           C\\nANISOU 1071  CG1 ILE A 184     9688  12171   7873   -478    168    222       C\\nATOM   1072  CG2 ILE A 184       8.346  10.052 -17.932  1.00 83.92           C\\nANISOU 1072  CG2 ILE A 184    10523  13226   8137   -643    -67    367       C\\nATOM   1073  CD1 ILE A 184       8.861   8.383 -15.456  1.00 80.33           C\\nANISOU 1073  CD1 ILE A 184    10011  12185   8326   -346     90    -54       C\\nATOM   1074  N   ALA A 185      10.335  12.279 -19.291  1.00 80.23           N\\nANISOU 1074  N   ALA A 185     9999  13442   7044  -1105     98   1028       N\\nATOM   1075  CA  ALA A 185      11.162  12.234 -20.487  1.00 83.51           C\\nANISOU 1075  CA  ALA A 185    10349  14420   6960  -1262    251   1031       C\\nATOM   1076  C   ALA A 185      12.352  13.177 -20.411  1.00 83.75           C\\nANISOU 1076  C   ALA A 185    10288  14647   6887  -1499    393   1327       C\\nATOM   1077  O   ALA A 185      13.207  13.143 -21.301  1.00 89.61           O\\nANISOU 1077  O   ALA A 185    10921  15924   7202  -1661    576   1320       O\\nATOM   1078  CB  ALA A 185      10.320  12.565 -21.723  1.00 73.89           C\\nANISOU 1078  CB  ALA A 185     9279  13403   5395  -1401     57   1201       C\\nATOM   1079  N   ASN A 186      12.425  14.011 -19.384  1.00 87.95           N\\nANISOU 1079  N   ASN A 186    10846  14788   7782  -1536    315   1567       N\\nATOM   1080  CA  ASN A 186      13.545  14.931 -19.235  1.00 90.37           C\\nANISOU 1080  CA  ASN A 186    11066  15232   8039  -1784    421   1852       C\\nATOM   1081  C   ASN A 186      14.781  14.156 -18.795  1.00 93.04           C\\nANISOU 1081  C   ASN A 186    11153  15806   8392  -1671    718   1526       C\\nATOM   1082  O   ASN A 186      14.734  13.472 -17.765  1.00 90.82           O\\nANISOU 1082  O   ASN A 186    10830  15214   8462  -1399    737   1252       O\\nATOM   1083  CB  ASN A 186      13.200  16.017 -18.220  1.00 86.22           C\\nANISOU 1083  CB  ASN A 186    10651  14175   7934  -1820    209   2150       C\\nATOM   1084  CG  ASN A 186      14.162  17.185 -18.259  1.00 89.29           C\\nANISOU 1084  CG  ASN A 186    11013  14659   8255  -2152    225   2537       C\\nATOM   1085  OD1 ASN A 186      15.380  17.008 -18.241  1.00 95.97           O\\nANISOU 1085  OD1 ASN A 186    11655  15837   8971  -2255    479   2464       O\\nATOM   1086  ND2 ASN A 186      13.616  18.393 -18.314  1.00 87.60           N\\nANISOU 1086  ND2 ASN A 186    10997  14142   8145  -2325    -71   2943       N\\nATOM   1087  N   PRO A 187      15.895  14.232 -19.527  1.00 95.07           N\\nANISOU 1087  N   PRO A 187    11229  16621   8273  -1873    941   1541       N\\nATOM   1088  CA  PRO A 187      17.095  13.486 -19.110  1.00 94.27           C\\nANISOU 1088  CA  PRO A 187    10845  16765   8209  -1726   1203   1183       C\\nATOM   1089  C   PRO A 187      17.587  13.857 -17.721  1.00 93.98           C\\nANISOU 1089  C   PRO A 187    10749  16330   8627  -1662   1185   1242       C\\nATOM   1090  O   PRO A 187      18.317  13.067 -17.109  1.00 94.56           O\\nANISOU 1090  O   PRO A 187    10638  16436   8855  -1433   1319    896       O\\nATOM   1091  CB  PRO A 187      18.127  13.845 -20.190  1.00 87.30           C\\nANISOU 1091  CB  PRO A 187     9769  16534   6867  -2026   1406   1271       C\\nATOM   1092  CG  PRO A 187      17.630  15.128 -20.784  1.00 81.91           C\\nANISOU 1092  CG  PRO A 187     9311  15710   6102  -2368   1189   1793       C\\nATOM   1093  CD  PRO A 187      16.135  15.035 -20.737  1.00 89.48           C\\nANISOU 1093  CD  PRO A 187    10552  16349   7098  -2256    952   1890       C\\nATOM   1094  N   ALA A 188      17.198  15.020 -17.198  1.00 89.90           N\\nANISOU 1094  N   ALA A 188    10393  15427   8337  -1837    994   1648       N\\nATOM   1095  CA  ALA A 188      17.621  15.462 -15.877  1.00 87.20           C\\nANISOU 1095  CA  ALA A 188    10012  14708   8411  -1788    952   1704       C\\nATOM   1096  C   ALA A 188      16.681  15.017 -14.764  1.00 83.84           C\\nANISOU 1096  C   ALA A 188     9732  13727   8396  -1473    795   1536       C\\nATOM   1097  O   ALA A 188      16.983  15.253 -13.591  1.00 75.80           O\\nANISOU 1097  O   ALA A 188     8687  12406   7707  -1395    761   1530       O\\nATOM   1098  CB  ALA A 188      17.750  16.987 -15.848  1.00 80.85           C\\nANISOU 1098  CB  ALA A 188     9302  13764   7654  -2142    804   2201       C\\nATOM   1099  N   PHE A 189      15.554  14.386 -15.094  1.00 80.92           N\\nANISOU 1099  N   PHE A 189     9504  13244   7997  -1314    698   1400       N\\nATOM   1100  CA  PHE A 189      14.640  13.936 -14.051  1.00 78.27           C\\nANISOU 1100  CA  PHE A 189     9281  12440   8018  -1065    570   1248       C\\nATOM   1101  C   PHE A 189      15.276  12.851 -13.193  1.00 80.35           C\\nANISOU 1101  C   PHE A 189     9430  12648   8450   -824    697    901       C\\nATOM   1102  O   PHE A 189      15.128  12.856 -11.964  1.00 75.11           O\\nANISOU 1102  O   PHE A 189     8806  11626   8105   -710    633    876       O\\nATOM   1103  CB  PHE A 189      13.335  13.437 -14.671  1.00 80.58           C\\nANISOU 1103  CB  PHE A 189     9715  12675   8225   -983    445   1165       C\\nATOM   1104  CG  PHE A 189      12.426  12.754 -13.693  1.00 85.91           C\\nANISOU 1104  CG  PHE A 189    10465  12965   9214   -760    358    965       C\\nATOM   1105  CD1 PHE A 189      11.690  13.490 -12.780  1.00 86.83           C\\nANISOU 1105  CD1 PHE A 189    10658  12708   9625   -749    203   1115       C\\nATOM   1106  CD2 PHE A 189      12.306  11.375 -13.683  1.00 84.50           C\\nANISOU 1106  CD2 PHE A 189    10274  12804   9028   -575    421    619       C\\nATOM   1107  CE1 PHE A 189      10.853  12.861 -11.873  1.00 82.22           C\\nANISOU 1107  CE1 PHE A 189    10115  11841   9283   -588    152    936       C\\nATOM   1108  CE2 PHE A 189      11.471  10.742 -12.779  1.00 79.97           C\\nANISOU 1108  CE2 PHE A 189     9777  11887   8720   -435    339    479       C\\nATOM   1109  CZ  PHE A 189      10.745  11.486 -11.874  1.00 75.49           C\\nANISOU 1109  CZ  PHE A 189     9262  11015   8404   -457    224    645       C\\nATOM   1110  N   VAL A 190      15.990  11.913 -13.820  1.00 82.64           N\\nANISOU 1110  N   VAL A 190     9581  13296   8524   -736    857    620       N\\nATOM   1111  CA  VAL A 190      16.608  10.825 -13.066  1.00 79.80           C\\nANISOU 1111  CA  VAL A 190     9129  12855   8338   -476    921    274       C\\nATOM   1112  C   VAL A 190      17.619  11.375 -12.070  1.00 73.96           C\\nANISOU 1112  C   VAL A 190     8263  12038   7801   -501    965    362       C\\nATOM   1113  O   VAL A 190      17.647  10.963 -10.905  1.00 69.81           O\\nANISOU 1113  O   VAL A 190     7780  11184   7561   -328    899    257       O\\nATOM   1114  CB  VAL A 190      17.246   9.799 -14.024  1.00 76.29           C\\nANISOU 1114  CB  VAL A 190     8531  12834   7621   -350   1058    -85       C\\nATOM   1115  CG1 VAL A 190      18.329   8.997 -13.321  1.00 73.98           C\\nANISOU 1115  CG1 VAL A 190     8071  12543   7496   -111   1121   -401       C\\nATOM   1116  CG2 VAL A 190      16.181   8.863 -14.570  1.00 70.22           C\\nANISOU 1116  CG2 VAL A 190     7922  11973   6787   -219    957   -292       C\\nATOM   1117  N   VAL A 191      18.449  12.327 -12.502  1.00 74.89           N\\nANISOU 1117  N   VAL A 191     8232  12459   7764   -745   1062    574       N\\nATOM   1118  CA  VAL A 191      19.440  12.910 -11.603  1.00 69.99           C\\nANISOU 1118  CA  VAL A 191     7472  11783   7337   -800   1089    659       C\\nATOM   1119  C   VAL A 191      18.756  13.666 -10.472  1.00 71.73           C\\nANISOU 1119  C   VAL A 191     7882  11494   7879   -818    904    880       C\\nATOM   1120  O   VAL A 191      19.167  13.580  -9.308  1.00 74.22           O\\nANISOU 1120  O   VAL A 191     8168  11584   8449   -696    866    802       O\\nATOM   1121  CB  VAL A 191      20.401  13.820 -12.387  1.00 69.86           C\\nANISOU 1121  CB  VAL A 191     7256  12216   7071  -1128   1224    873       C\\nATOM   1122  CG1 VAL A 191      21.588  14.210 -11.518  1.00 61.69           C\\nANISOU 1122  CG1 VAL A 191     6014  11194   6229  -1167   1269    875       C\\nATOM   1123  CG2 VAL A 191      20.860  13.135 -13.669  1.00 71.25           C\\nANISOU 1123  CG2 VAL A 191     7250  12975   6848  -1136   1419    651       C\\nATOM   1124  N   TYR A 192      17.698  14.409 -10.792  1.00 73.30           N\\nANISOU 1124  N   TYR A 192     8269  11519   8064   -952    769   1133       N\\nATOM   1125  CA  TYR A 192      17.008  15.209  -9.786  1.00 69.49           C\\nANISOU 1125  CA  TYR A 192     7937  10591   7877   -952    585   1300       C\\nATOM   1126  C   TYR A 192      16.386  14.323  -8.714  1.00 69.05           C\\nANISOU 1126  C   TYR A 192     7966  10230   8040   -683    540   1063       C\\nATOM   1127  O   TYR A 192      16.743  14.407  -7.534  1.00 70.50           O\\nANISOU 1127  O   TYR A 192     8135  10210   8443   -602    510   1018       O\\nATOM   1128  CB  TYR A 192      15.946  16.079 -10.460  1.00 70.53           C\\nANISOU 1128  CB  TYR A 192     8235  10616   7948  -1102    419   1566       C\\nATOM   1129  CG  TYR A 192      15.223  17.022  -9.524  1.00 71.79           C\\nANISOU 1129  CG  TYR A 192     8522  10343   8412  -1083    204   1704       C\\nATOM   1130  CD1 TYR A 192      15.814  18.212  -9.114  1.00 72.52           C\\nANISOU 1130  CD1 TYR A 192     8604  10305   8647  -1251    105   1926       C\\nATOM   1131  CD2 TYR A 192      13.943  16.733  -9.066  1.00 75.40           C\\nANISOU 1131  CD2 TYR A 192     9093  10543   9014   -904     92   1589       C\\nATOM   1132  CE1 TYR A 192      15.157  19.082  -8.265  1.00 72.60           C\\nANISOU 1132  CE1 TYR A 192     8724   9917   8942  -1200   -114   1996       C\\nATOM   1133  CE2 TYR A 192      13.275  17.600  -8.217  1.00 78.40           C\\nANISOU 1133  CE2 TYR A 192     9549  10580   9658   -860    -96   1656       C\\nATOM   1134  CZ  TYR A 192      13.887  18.772  -7.820  1.00 72.16           C\\nANISOU 1134  CZ  TYR A 192     8758   9648   9013   -988   -206   1843       C\\nATOM   1135  OH  TYR A 192      13.226  19.632  -6.973  1.00 63.34           O\\nANISOU 1135  OH  TYR A 192     7711   8188   8168   -909   -415   1853       O\\nATOM   1136  N   SER A 193      15.457  13.449  -9.114  1.00 72.61           N\\nANISOU 1136  N   SER A 193     8511  10659   8417   -566    526    916       N\\nATOM   1137  CA  SER A 193      14.715  12.654  -8.139  1.00 77.34           C\\nANISOU 1137  CA  SER A 193     9213  10968   9205   -382    469    746       C\\nATOM   1138  C   SER A 193      15.615  11.681  -7.386  1.00 75.22           C\\nANISOU 1138  C   SER A 193     8884  10678   9019   -217    535    524       C\\nATOM   1139  O   SER A 193      15.294  11.286  -6.260  1.00 76.80           O\\nANISOU 1139  O   SER A 193     9170  10614   9397   -116    473    460       O\\nATOM   1140  CB  SER A 193      13.580  11.897  -8.830  1.00 79.11           C\\nANISOU 1140  CB  SER A 193     9536  11195   9327   -336    430    640       C\\nATOM   1141  OG  SER A 193      14.075  10.934  -9.741  1.00 69.99           O\\nANISOU 1141  OG  SER A 193     8324  10300   7968   -274    524    442       O\\nATOM   1142  N   SER A 194      16.739  11.283  -7.980  1.00 71.25           N\\nANISOU 1142  N   SER A 194     8226  10467   8381   -186    646    398       N\\nATOM   1143  CA  SER A 194      17.664  10.407  -7.271  1.00 72.26           C\\nANISOU 1143  CA  SER A 194     8279  10561   8614      6    663    171       C\\nATOM   1144  C   SER A 194      18.401  11.166  -6.177  1.00 76.18           C\\nANISOU 1144  C   SER A 194     8709  10947   9290    -29    635    286       C\\nATOM   1145  O   SER A 194      18.423  10.741  -5.014  1.00 72.02           O\\nANISOU 1145  O   SER A 194     8263  10164   8939     99    550    218       O\\nATOM   1146  CB  SER A 194      18.661   9.784  -8.246  1.00 72.31           C\\nANISOU 1146  CB  SER A 194     8087  10955   8432     84    784    -57       C\\nATOM   1147  OG  SER A 194      17.998   9.092  -9.286  1.00 80.43           O\\nANISOU 1147  OG  SER A 194     9180  12101   9277    122    797   -194       O\\nATOM   1148  N   ILE A 195      19.005  12.300  -6.530  1.00 77.08           N\\nANISOU 1148  N   ILE A 195     8687  11249   9349   -226    688    474       N\\nATOM   1149  CA  ILE A 195      19.847  13.021  -5.580  1.00 70.51           C\\nANISOU 1149  CA  ILE A 195     7763  10342   8685   -272    652    555       C\\nATOM   1150  C   ILE A 195      18.988  13.748  -4.552  1.00 66.52           C\\nANISOU 1150  C   ILE A 195     7438   9466   8370   -304    511    708       C\\nATOM   1151  O   ILE A 195      19.129  13.541  -3.341  1.00 74.63           O\\nANISOU 1151  O   ILE A 195     8511  10286   9557   -186    438    633       O\\nATOM   1152  CB  ILE A 195      20.787  13.987  -6.321  1.00 68.49           C\\nANISOU 1152  CB  ILE A 195     7299  10412   8313   -520    744    715       C\\nATOM   1153  CG1 ILE A 195      21.784  13.200  -7.177  1.00 66.22           C\\nANISOU 1153  CG1 ILE A 195     6764  10568   7828   -459    911    488       C\\nATOM   1154  CG2 ILE A 195      21.510  14.892  -5.337  1.00 63.89           C\\nANISOU 1154  CG2 ILE A 195     6643   9700   7932   -613    668    829       C\\nATOM   1155  CD1 ILE A 195      22.738  14.064  -7.971  1.00 56.97           C\\nANISOU 1155  CD1 ILE A 195     5348   9813   6484   -752   1041    642       C\\nATOM   1156  N   VAL A 196      18.073  14.597  -5.019  1.00 62.66           N\\nANISOU 1156  N   VAL A 196     7052   8902   7854   -450    454    905       N\\nATOM   1157  CA  VAL A 196      17.332  15.463  -4.105  1.00 67.97           C\\nANISOU 1157  CA  VAL A 196     7847   9264   8715   -469    309   1012       C\\nATOM   1158  C   VAL A 196      16.343  14.656  -3.269  1.00 67.07           C\\nANISOU 1158  C   VAL A 196     7868   8944   8670   -296    275    861       C\\nATOM   1159  O   VAL A 196      16.268  14.814  -2.046  1.00 61.49           O\\nANISOU 1159  O   VAL A 196     7206   8054   8102   -231    210    818       O\\nATOM   1160  CB  VAL A 196      16.626  16.582  -4.888  1.00 64.23           C\\nANISOU 1160  CB  VAL A 196     7440   8750   8216   -643    212   1244       C\\nATOM   1161  CG1 VAL A 196      15.849  17.474  -3.945  1.00 52.97           C\\nANISOU 1161  CG1 VAL A 196     6116   7001   7009   -610     37   1287       C\\nATOM   1162  CG2 VAL A 196      17.638  17.392  -5.674  1.00 71.96           C\\nANISOU 1162  CG2 VAL A 196     8304   9935   9102   -883    238   1445       C\\nATOM   1163  N   SER A 197      15.571  13.778  -3.911  1.00 68.31           N\\nANISOU 1163  N   SER A 197     8091   9151   8712   -244    315    780       N\\nATOM   1164  CA  SER A 197      14.505  13.073  -3.211  1.00 64.29           C\\nANISOU 1164  CA  SER A 197     7706   8466   8256   -150    280    676       C\\nATOM   1165  C   SER A 197      14.986  11.839  -2.460  1.00 64.86           C\\nANISOU 1165  C   SER A 197     7819   8478   8346    -22    301    516       C\\nATOM   1166  O   SER A 197      14.304  11.401  -1.528  1.00 71.84           O\\nANISOU 1166  O   SER A 197     8812   9202   9284      7    262    476       O\\nATOM   1167  CB  SER A 197      13.401  12.668  -4.191  1.00 64.34           C\\nANISOU 1167  CB  SER A 197     7768   8525   8155   -175    281    661       C\\nATOM   1168  OG  SER A 197      12.416  13.677  -4.297  1.00 65.40           O\\nANISOU 1168  OG  SER A 197     7921   8583   8345   -241    188    775       O\\nATOM   1169  N   PHE A 198      16.134  11.265  -2.824  1.00 56.65           N\\nANISOU 1169  N   PHE A 198     6693   7571   7259     50    348    422       N\\nATOM   1170  CA  PHE A 198      16.563  10.006  -2.225  1.00 61.84           C\\nANISOU 1170  CA  PHE A 198     7413   8131   7953    205    308    258       C\\nATOM   1171  C   PHE A 198      17.951  10.080  -1.597  1.00 66.94           C\\nANISOU 1171  C   PHE A 198     7945   8814   8677    293    283    207       C\\nATOM   1172  O   PHE A 198      18.076   9.853  -0.391  1.00 63.30           O\\nANISOU 1172  O   PHE A 198     7574   8170   8306    352    191    202       O\\nATOM   1173  CB  PHE A 198      16.518   8.887  -3.269  1.00 62.27           C\\nANISOU 1173  CB  PHE A 198     7477   8279   7904    290    331     91       C\\nATOM   1174  CG  PHE A 198      16.836   7.525  -2.714  1.00 71.87           C\\nANISOU 1174  CG  PHE A 198     8800   9318   9188    461    226    -82       C\\nATOM   1175  CD1 PHE A 198      15.889   6.822  -1.986  1.00 73.26           C\\nANISOU 1175  CD1 PHE A 198     9194   9229   9414    432    130    -54       C\\nATOM   1176  CD2 PHE A 198      18.074   6.944  -2.927  1.00 66.14           C\\nANISOU 1176  CD2 PHE A 198     7955   8695   8481    641    204   -273       C\\nATOM   1177  CE1 PHE A 198      16.173   5.566  -1.481  1.00 70.07           C\\nANISOU 1177  CE1 PHE A 198     8932   8611   9079    560    -15   -171       C\\nATOM   1178  CE2 PHE A 198      18.365   5.687  -2.423  1.00 70.55           C\\nANISOU 1178  CE2 PHE A 198     8637   9036   9134    826     45   -436       C\\nATOM   1179  CZ  PHE A 198      17.412   4.997  -1.700  1.00 69.64           C\\nANISOU 1179  CZ  PHE A 198     8787   8602   9070    775    -79   -363       C\\nATOM   1180  N   TYR A 199      18.996  10.380  -2.373  1.00 67.17           N\\nANISOU 1180  N   TYR A 199     7766   9103   8654    290    360    166       N\\nATOM   1181  CA  TYR A 199      20.356  10.230  -1.861  1.00 67.05           C\\nANISOU 1181  CA  TYR A 199     7598   9159   8719    402    329     58       C\\nATOM   1182  C   TYR A 199      20.656  11.224  -0.746  1.00 67.17           C\\nANISOU 1182  C   TYR A 199     7604   9058   8859    323    261    193       C\\nATOM   1183  O   TYR A 199      21.379  10.897   0.202  1.00 60.26           O\\nANISOU 1183  O   TYR A 199     6716   8098   8082    445    161    112       O\\nATOM   1184  CB  TYR A 199      21.367  10.375  -2.997  1.00 71.88           C\\nANISOU 1184  CB  TYR A 199     7935  10155   9221    380    457    -32       C\\nATOM   1185  CG  TYR A 199      21.372   9.197  -3.942  1.00 81.30           C\\nANISOU 1185  CG  TYR A 199     9102  11489  10299    540    498   -275       C\\nATOM   1186  CD1 TYR A 199      21.185   7.907  -3.469  1.00 86.13           C\\nANISOU 1186  CD1 TYR A 199     9871  11856  10998    769    359   -463       C\\nATOM   1187  CD2 TYR A 199      21.545   9.374  -5.307  1.00 83.10           C\\nANISOU 1187  CD2 TYR A 199     9165  12088  10320    449    652   -315       C\\nATOM   1188  CE1 TYR A 199      21.177   6.825  -4.325  1.00 85.63           C\\nANISOU 1188  CE1 TYR A 199     9799  11878  10859    933    355   -719       C\\nATOM   1189  CE2 TYR A 199      21.538   8.297  -6.171  1.00 80.51           C\\nANISOU 1189  CE2 TYR A 199     8809  11905   9875    615    680   -585       C\\nATOM   1190  CZ  TYR A 199      21.352   7.026  -5.674  1.00 76.43           C\\nANISOU 1190  CZ  TYR A 199     8448  11104   9487    871    522   -803       C\\nATOM   1191  OH  TYR A 199      21.344   5.950  -6.531  1.00 69.70           O\\nANISOU 1191  OH  TYR A 199     7579  10355   8547   1053    510  -1106       O\\nATOM   1192  N   VAL A 200      20.116  12.435  -0.831  1.00 65.74           N\\nANISOU 1192  N   VAL A 200     7439   8856   8685    133    281    383       N\\nATOM   1193  CA  VAL A 200      20.375  13.434   0.206  1.00 71.58           C\\nANISOU 1193  CA  VAL A 200     8173   9468   9555     66    193    476       C\\nATOM   1194  C   VAL A 200      19.616  13.076   1.483  1.00 70.25           C\\nANISOU 1194  C   VAL A 200     8210   9046   9435    156     95    445       C\\nATOM   1195  O   VAL A 200      20.203  13.156   2.571  1.00 66.48           O\\nANISOU 1195  O   VAL A 200     7736   8490   9035    213      0    407       O\\nATOM   1196  CB  VAL A 200      20.038  14.854  -0.281  1.00 71.46           C\\nANISOU 1196  CB  VAL A 200     8129   9461   9562   -148    192    671       C\\nATOM   1197  CG1 VAL A 200      20.109  15.848   0.873  1.00 70.31           C\\nANISOU 1197  CG1 VAL A 200     8017   9123   9575   -187     60    720       C\\nATOM   1198  CG2 VAL A 200      20.992  15.264  -1.393  1.00 67.72           C\\nANISOU 1198  CG2 VAL A 200     7444   9277   9011   -300    285    742       C\\nATOM   1199  N   PRO A 201      18.333  12.691   1.432  1.00 68.63           N\\nANISOU 1199  N   PRO A 201     8167   8739   9171    150    111    459       N\\nATOM   1200  CA  PRO A 201      17.717  12.147   2.655  1.00 67.01           C\\nANISOU 1200  CA  PRO A 201     8135   8363   8962    204     43    424       C\\nATOM   1201  C   PRO A 201      18.416  10.898   3.166  1.00 63.12           C\\nANISOU 1201  C   PRO A 201     7712   7811   8461    342    -32    331       C\\nATOM   1202  O   PRO A 201      18.541  10.711   4.383  1.00 64.72           O\\nANISOU 1202  O   PRO A 201     8019   7903   8669    376   -131    332       O\\nATOM   1203  CB  PRO A 201      16.275  11.860   2.217  1.00 66.92           C\\nANISOU 1203  CB  PRO A 201     8227   8319   8879    142     97    446       C\\nATOM   1204  CG  PRO A 201      16.022  12.833   1.137  1.00 66.63           C\\nANISOU 1204  CG  PRO A 201     8086   8379   8852     55    144    523       C\\nATOM   1205  CD  PRO A 201      17.319  12.916   0.383  1.00 66.70           C\\nANISOU 1205  CD  PRO A 201     7946   8542   8857     61    178    525       C\\nATOM   1206  N   PHE A 202      18.884  10.041   2.258  1.00 56.10           N\\nANISOU 1206  N   PHE A 202     6771   6992   7551    435    -11    238       N\\nATOM   1207  CA  PHE A 202      19.593   8.829   2.655  1.00 63.87           C\\nANISOU 1207  CA  PHE A 202     7821   7882   8566    610   -137    119       C\\nATOM   1208  C   PHE A 202      20.816   9.156   3.509  1.00 70.36           C\\nANISOU 1208  C   PHE A 202     8539   8718   9475    697   -242     86       C\\nATOM   1209  O   PHE A 202      20.977   8.621   4.613  1.00 72.54           O\\nANISOU 1209  O   PHE A 202     8969   8826   9768    771   -400     91       O\\nATOM   1210  CB  PHE A 202      19.992   8.047   1.402  1.00 62.85           C\\nANISOU 1210  CB  PHE A 202     7591   7872   8416    726    -97    -41       C\\nATOM   1211  CG  PHE A 202      20.499   6.659   1.671  1.00 70.17           C\\nANISOU 1211  CG  PHE A 202     8620   8639   9403    941   -273   -200       C\\nATOM   1212  CD1 PHE A 202      20.468   6.114   2.942  1.00 73.47           C\\nANISOU 1212  CD1 PHE A 202     9254   8795   9864    982   -462   -139       C\\nATOM   1213  CD2 PHE A 202      21.014   5.899   0.638  1.00 76.10           C\\nANISOU 1213  CD2 PHE A 202     9257   9501  10156   1108   -271   -423       C\\nATOM   1214  CE1 PHE A 202      20.939   4.847   3.177  1.00 78.88           C\\nANISOU 1214  CE1 PHE A 202    10067   9279  10625   1182   -682   -264       C\\nATOM   1215  CE2 PHE A 202      21.485   4.628   0.866  1.00 75.62           C\\nANISOU 1215  CE2 PHE A 202     9296   9248  10187   1343   -483   -603       C\\nATOM   1216  CZ  PHE A 202      21.447   4.100   2.137  1.00 79.28           C\\nANISOU 1216  CZ  PHE A 202    10003   9395  10724   1380   -707   -507       C\\nATOM   1217  N   ILE A 203      21.692  10.031   3.011  1.00 69.89           N\\nANISOU 1217  N   ILE A 203     8223   8871   9462    667   -169     66       N\\nATOM   1218  CA  ILE A 203      22.931  10.333   3.726  1.00 70.07           C\\nANISOU 1218  CA  ILE A 203     8101   8940   9583    743   -275      9       C\\nATOM   1219  C   ILE A 203      22.628  10.977   5.074  1.00 68.51           C\\nANISOU 1219  C   ILE A 203     8043   8585   9403    671   -375    114       C\\nATOM   1220  O   ILE A 203      23.185  10.584   6.106  1.00 61.96           O\\nANISOU 1220  O   ILE A 203     7279   7659   8605    783   -545     72       O\\nATOM   1221  CB  ILE A 203      23.843  11.227   2.870  1.00 67.00           C\\nANISOU 1221  CB  ILE A 203     7390   8840   9226    648   -158     -7       C\\nATOM   1222  CG1 ILE A 203      24.189  10.534   1.555  1.00 68.52           C\\nANISOU 1222  CG1 ILE A 203     7420   9264   9349    728    -43   -152       C\\nATOM   1223  CG2 ILE A 203      25.111  11.566   3.623  1.00 62.39           C\\nANISOU 1223  CG2 ILE A 203     6625   8319   8761    704   -276    -75       C\\nATOM   1224  CD1 ILE A 203      24.882  11.438   0.566  1.00 75.16           C\\nANISOU 1224  CD1 ILE A 203     7956  10453  10148    555    118   -121       C\\nATOM   1225  N   VAL A 204      21.738  11.974   5.082  1.00 68.09           N\\nANISOU 1225  N   VAL A 204     8035   8512   9324    499   -292    232       N\\nATOM   1226  CA  VAL A 204      21.439  12.706   6.313  1.00 64.98           C\\nANISOU 1226  CA  VAL A 204     7739   8013   8938    443   -378    276       C\\nATOM   1227  C   VAL A 204      20.881  11.767   7.375  1.00 65.55           C\\nANISOU 1227  C   VAL A 204     8061   7945   8902    504   -469    277       C\\nATOM   1228  O   VAL A 204      21.332  11.764   8.527  1.00 66.60           O\\nANISOU 1228  O   VAL A 204     8259   8027   9017    550   -610    260       O\\nATOM   1229  CB  VAL A 204      20.471  13.865   6.027  1.00 56.49           C\\nANISOU 1229  CB  VAL A 204     6664   6928   7872    291   -296    354       C\\nATOM   1230  CG1 VAL A 204      19.900  14.399   7.325  1.00 59.98           C\\nANISOU 1230  CG1 VAL A 204     7227   7276   8289    274   -375    333       C\\nATOM   1231  CG2 VAL A 204      21.185  14.972   5.267  1.00 55.27           C\\nANISOU 1231  CG2 VAL A 204     6299   6869   7831    182   -275    403       C\\nATOM   1232  N   THR A 205      19.886  10.960   7.005  1.00 66.29           N\\nANISOU 1232  N   THR A 205     8302   7982   8903    478   -403    312       N\\nATOM   1233  CA  THR A 205      19.340   9.991   7.947  1.00 66.07           C\\nANISOU 1233  CA  THR A 205     8524   7824   8753    475   -492    356       C\\nATOM   1234  C   THR A 205      20.407   9.003   8.395  1.00 73.22           C\\nANISOU 1234  C   THR A 205     9501   8627   9694    637   -693    319       C\\nATOM   1235  O   THR A 205      20.450   8.611   9.567  1.00 73.97           O\\nANISOU 1235  O   THR A 205     9780   8626   9698    635   -843    376       O\\nATOM   1236  CB  THR A 205      18.162   9.258   7.313  1.00 64.13           C\\nANISOU 1236  CB  THR A 205     8398   7536   8434    391   -397    399       C\\nATOM   1237  OG1 THR A 205      17.159  10.210   6.937  1.00 70.05           O\\nANISOU 1237  OG1 THR A 205     9065   8385   9167    268   -244    415       O\\nATOM   1238  CG2 THR A 205      17.567   8.265   8.291  1.00 59.18           C\\nANISOU 1238  CG2 THR A 205     8038   6780   7668    317   -492    485       C\\nATOM   1239  N   LEU A 206      21.282   8.594   7.476  1.00 71.22           N\\nANISOU 1239  N   LEU A 206     9095   8407   9557    784   -714    211       N\\nATOM   1240  CA  LEU A 206      22.343   7.663   7.839  1.00 69.37           C\\nANISOU 1240  CA  LEU A 206     8891   8070   9395    992   -940    126       C\\nATOM   1241  C   LEU A 206      23.325   8.302   8.810  1.00 67.69           C\\nANISOU 1241  C   LEU A 206     8584   7907   9228   1046  -1074    104       C\\nATOM   1242  O   LEU A 206      23.847   7.629   9.705  1.00 63.83           O\\nANISOU 1242  O   LEU A 206     8237   7281   8736   1166  -1318    106       O\\nATOM   1243  CB  LEU A 206      23.069   7.177   6.586  1.00 68.74           C\\nANISOU 1243  CB  LEU A 206     8603   8086   9429   1162   -911    -54       C\\nATOM   1244  CG  LEU A 206      24.254   6.253   6.864  1.00 66.60           C\\nANISOU 1244  CG  LEU A 206     8300   7728   9276   1438  -1170   -212       C\\nATOM   1245  CD1 LEU A 206      23.779   4.999   7.577  1.00 68.61           C\\nANISOU 1245  CD1 LEU A 206     8929   7645   9495   1492  -1416   -131       C\\nATOM   1246  CD2 LEU A 206      24.981   5.908   5.578  1.00 65.91           C\\nANISOU 1246  CD2 LEU A 206     7933   7826   9284   1614  -1102   -453       C\\nATOM   1247  N   LEU A 207      23.592   9.597   8.647  1.00 71.05           N\\nANISOU 1247  N   LEU A 207     8784   8507   9703    951   -950     91       N\\nATOM   1248  CA  LEU A 207      24.489  10.279   9.572  1.00 68.27           C\\nANISOU 1248  CA  LEU A 207     8336   8199   9405    979  -1088     58       C\\nATOM   1249  C   LEU A 207      23.856  10.418  10.949  1.00 68.21           C\\nANISOU 1249  C   LEU A 207     8586   8088   9244    897  -1186    154       C\\nATOM   1250  O   LEU A 207      24.552  10.352  11.967  1.00 66.32           O\\nANISOU 1250  O   LEU A 207     8392   7815   8989    976  -1395    132       O\\nATOM   1251  CB  LEU A 207      24.875  11.645   9.012  1.00 63.44           C\\nANISOU 1251  CB  LEU A 207     7441   7765   8897    855   -953     35       C\\nATOM   1252  CG  LEU A 207      25.757  11.605   7.765  1.00 58.28           C\\nANISOU 1252  CG  LEU A 207     6481   7306   8356    900   -859    -62       C\\nATOM   1253  CD1 LEU A 207      25.869  12.987   7.135  1.00 58.28           C\\nANISOU 1253  CD1 LEU A 207     6266   7458   8418    685   -713     -2       C\\nATOM   1254  CD2 LEU A 207      27.133  11.057   8.115  1.00 60.06           C\\nANISOU 1254  CD2 LEU A 207     6537   7593   8688   1106  -1049   -219       C\\nATOM   1255  N   VAL A 208      22.536  10.604  11.000  1.00 65.76           N\\nANISOU 1255  N   VAL A 208     8427   7760   8800    740  -1039    244       N\\nATOM   1256  CA  VAL A 208      21.850  10.728  12.283  1.00 70.01           C\\nANISOU 1256  CA  VAL A 208     9179   8279   9143    643  -1090    309       C\\nATOM   1257  C   VAL A 208      21.897   9.408  13.042  1.00 72.90           C\\nANISOU 1257  C   VAL A 208     9821   8505   9370    686  -1284    405       C\\nATOM   1258  O   VAL A 208      22.211   9.371  14.237  1.00 72.29           O\\nANISOU 1258  O   VAL A 208     9878   8422   9167    690  -1459    437       O\\nATOM   1259  CB  VAL A 208      20.403  11.205  12.072  1.00 62.31           C\\nANISOU 1259  CB  VAL A 208     8243   7366   8066    475   -875    344       C\\nATOM   1260  CG1 VAL A 208      19.616  11.100  13.361  1.00 57.35           C\\nANISOU 1260  CG1 VAL A 208     7821   6784   7185    363   -898    391       C\\nATOM   1261  CG2 VAL A 208      20.388  12.634  11.560  1.00 55.34           C\\nANISOU 1261  CG2 VAL A 208     7134   6567   7324    438   -769    263       C\\nATOM   1262  N   TYR A 209      21.584   8.304  12.360  1.00 67.17           N\\nANISOU 1262  N   TYR A 209     9206   7651   8663    711  -1285    458       N\\nATOM   1263  CA  TYR A 209      21.578   7.010  13.032  1.00 62.85           C\\nANISOU 1263  CA  TYR A 209     8966   6907   8008    728  -1515    581       C\\nATOM   1264  C   TYR A 209      22.975   6.598  13.468  1.00 67.38           C\\nANISOU 1264  C   TYR A 209     9528   7379   8695    962  -1822    518       C\\nATOM   1265  O   TYR A 209      23.130   5.942  14.504  1.00 76.08           O\\nANISOU 1265  O   TYR A 209    10894   8346   9666    963  -2077    640       O\\nATOM   1266  CB  TYR A 209      20.960   5.946  12.126  1.00 60.49           C\\nANISOU 1266  CB  TYR A 209     8784   6452   7749    710  -1483    623       C\\nATOM   1267  CG  TYR A 209      19.452   5.927  12.179  1.00 66.56           C\\nANISOU 1267  CG  TYR A 209     9685   7270   8334    437  -1286    750       C\\nATOM   1268  CD1 TYR A 209      18.788   5.544  13.335  1.00 66.30           C\\nANISOU 1268  CD1 TYR A 209     9921   7223   8047    229  -1351    931       C\\nATOM   1269  CD2 TYR A 209      18.693   6.292  11.078  1.00 67.85           C\\nANISOU 1269  CD2 TYR A 209     9692   7530   8559    372  -1040    687       C\\nATOM   1270  CE1 TYR A 209      17.408   5.526  13.397  1.00 71.51           C\\nANISOU 1270  CE1 TYR A 209    10651   7990   8531    -39  -1153   1024       C\\nATOM   1271  CE2 TYR A 209      17.312   6.271  11.129  1.00 67.87           C\\nANISOU 1271  CE2 TYR A 209     9776   7601   8410    135   -874    776       C\\nATOM   1272  CZ  TYR A 209      16.675   5.892  12.292  1.00 73.98           C\\nANISOU 1272  CZ  TYR A 209    10778   8387   8944    -71   -920    933       C\\nATOM   1273  OH  TYR A 209      15.301   5.875  12.350  1.00 78.65           O\\nANISOU 1273  OH  TYR A 209    11400   9107   9378   -325   -736    998       O\\nATOM   1274  N   ILE A 210      24.002   6.972  12.702  1.00 65.59           N\\nANISOU 1274  N   ILE A 210     8989   7235   8698   1151  -1815    332       N\\nATOM   1275  CA  ILE A 210      25.373   6.731  13.144  1.00 66.53           C\\nANISOU 1275  CA  ILE A 210     9020   7316   8943   1384  -2102    228       C\\nATOM   1276  C   ILE A 210      25.669   7.536  14.402  1.00 68.90           C\\nANISOU 1276  C   ILE A 210     9347   7706   9128   1318  -2205    265       C\\nATOM   1277  O   ILE A 210      26.296   7.036  15.343  1.00 66.82           O\\nANISOU 1277  O   ILE A 210     9234   7337   8820   1429  -2518    299       O\\nATOM   1278  CB  ILE A 210      26.368   7.053  12.015  1.00 68.77           C\\nANISOU 1278  CB  ILE A 210     8898   7760   9473   1556  -2020      2       C\\nATOM   1279  CG1 ILE A 210      26.237   6.043  10.879  1.00 66.91           C\\nANISOU 1279  CG1 ILE A 210     8656   7435   9331   1685  -1991    -87       C\\nATOM   1280  CG2 ILE A 210      27.792   7.062  12.545  1.00 69.56           C\\nANISOU 1280  CG2 ILE A 210     8822   7898   9711   1774  -2291   -139       C\\nATOM   1281  CD1 ILE A 210      27.237   6.254   9.771  1.00 66.26           C\\nANISOU 1281  CD1 ILE A 210     8158   7579   9440   1852  -1900   -335       C\\nATOM   1282  N   LYS A 211      25.221   8.797  14.439  1.00 68.09           N\\nANISOU 1282  N   LYS A 211     9108   7786   8977   1147  -1974    247       N\\nATOM   1283  CA  LYS A 211      25.368   9.607  15.645  1.00 72.77           C\\nANISOU 1283  CA  LYS A 211     9739   8468   9442   1077  -2066    245       C\\nATOM   1284  C   LYS A 211      24.551   9.044  16.798  1.00 75.75           C\\nANISOU 1284  C   LYS A 211    10492   8790   9501    949  -2158    418       C\\nATOM   1285  O   LYS A 211      24.918   9.225  17.965  1.00 75.16           O\\nANISOU 1285  O   LYS A 211    10526   8758   9275    949  -2353    430       O\\nATOM   1286  CB  LYS A 211      24.956  11.053  15.367  1.00 72.52           C\\nANISOU 1286  CB  LYS A 211     9503   8598   9455    934  -1825    165       C\\nATOM   1287  CG  LYS A 211      26.059  11.921  14.784  1.00 76.74           C\\nANISOU 1287  CG  LYS A 211     9682   9223  10251    997  -1830     21       C\\nATOM   1288  CD  LYS A 211      27.081  12.304  15.845  1.00 80.50           C\\nANISOU 1288  CD  LYS A 211    10106   9734  10746   1072  -2092    -66       C\\nATOM   1289  N   ILE A 212      23.444   8.363  16.492  1.00 76.82           N\\nANISOU 1289  N   ILE A 212    10821   8858   9510    813  -2022    555       N\\nATOM   1290  CA  ILE A 212      22.634   7.738  17.534  1.00 75.49           C\\nANISOU 1290  CA  ILE A 212    11004   8670   9009    629  -2092    753       C\\nATOM   1291  C   ILE A 212      23.351   6.523  18.110  1.00 78.85           C\\nANISOU 1291  C   ILE A 212    11697   8862   9401    741  -2475    889       C\\nATOM   1292  O   ILE A 212      23.426   6.348  19.332  1.00 81.23           O\\nANISOU 1292  O   ILE A 212    12234   9186   9445    664  -2673   1015       O\\nATOM   1293  CB  ILE A 212      21.244   7.368  16.983  1.00 72.94           C\\nANISOU 1293  CB  ILE A 212    10775   8353   8584    420  -1838    858       C\\nATOM   1294  CG1 ILE A 212      20.367   8.618  16.858  1.00 72.24           C\\nANISOU 1294  CG1 ILE A 212    10488   8519   8442    291  -1522    738       C\\nATOM   1295  CG2 ILE A 212      20.575   6.319  17.861  1.00 71.22           C\\nANISOU 1295  CG2 ILE A 212    10941   8062   8058    211  -1961   1112       C\\nATOM   1296  CD1 ILE A 212      18.962   8.339  16.351  1.00 65.08           C\\nANISOU 1296  CD1 ILE A 212     9627   7664   7437     90  -1276    811       C\\nATOM   1297  N   TYR A 213      23.890   5.666  17.237  1.00 80.40           N\\nANISOU 1297  N   TYR A 213    11866   8833   9849    936  -2607    855       N\\nATOM   1298  CA  TYR A 213      24.609   4.484  17.706  1.00 74.91           C\\nANISOU 1298  CA  TYR A 213    11423   7857   9182   1095  -3032    956       C\\nATOM   1299  C   TYR A 213      25.796   4.871  18.580  1.00 76.60           C\\nANISOU 1299  C   TYR A 213    11566   8127   9414   1272  -3314    873       C\\nATOM   1300  O   TYR A 213      26.091   4.197  19.574  1.00 75.58           O\\nANISOU 1300  O   TYR A 213    11741   7846   9129   1288  -3670   1037       O\\nATOM   1301  CB  TYR A 213      25.070   3.642  16.515  1.00 69.47           C\\nANISOU 1301  CB  TYR A 213    10637   6949   8811   1339  -3122    828       C\\nATOM   1302  CG  TYR A 213      25.850   2.401  16.899  1.00 82.87           C\\nANISOU 1302  CG  TYR A 213    12578   8305  10605   1567  -3612    881       C\\nATOM   1303  CD1 TYR A 213      25.198   1.248  17.317  1.00 88.00           C\\nANISOU 1303  CD1 TYR A 213    13681   8643  11110   1422  -3838   1153       C\\nATOM   1304  CD2 TYR A 213      27.237   2.376  16.828  1.00 83.04           C\\nANISOU 1304  CD2 TYR A 213    12370   8305  10877   1924  -3876    656       C\\nATOM   1305  CE1 TYR A 213      25.906   0.107  17.664  1.00 88.45           C\\nANISOU 1305  CE1 TYR A 213    13945   8382  11281   1597  -4262   1171       C\\nATOM   1306  CE2 TYR A 213      27.955   1.241  17.174  1.00 84.14           C\\nANISOU 1306  CE2 TYR A 213    12701   8139  11130   2144  -4318    655       C\\nATOM   1307  CZ  TYR A 213      27.286   0.109  17.589  1.00 88.74           C\\nANISOU 1307  CZ  TYR A 213    13713   8432  11572   1950  -4461    892       C\\nATOM   1308  OH  TYR A 213      27.998  -1.023  17.933  1.00 93.97           O\\nANISOU 1308  OH  TYR A 213    14524   8828  12351   2091  -4813    843       O\\nATOM   1309  N   ILE A 214      26.491   5.955  18.226  1.00 79.22           N\\nANISOU 1309  N   ILE A 214    11503   8668   9929   1388  -3184    634       N\\nATOM   1310  CA  ILE A 214      27.667   6.368  18.988  1.00 79.71           C\\nANISOU 1310  CA  ILE A 214    11448   8796  10043   1553  -3456    525       C\\nATOM   1311  C   ILE A 214      27.278   6.769  20.407  1.00 82.99           C\\nANISOU 1311  C   ILE A 214    12112   9325  10094   1359  -3536    663       C\\nATOM   1312  O   ILE A 214      27.993   6.468  21.373  1.00 77.18           O\\nANISOU 1312  O   ILE A 214    11526   8534   9267   1459  -3903    709       O\\nATOM   1313  CB  ILE A 214      28.405   7.505  18.256  1.00 74.49           C\\nANISOU 1313  CB  ILE A 214    10301   8350   9651   1642  -3272    259       C\\nATOM   1314  CG1 ILE A 214      28.993   6.995  16.944  1.00 73.37           C\\nANISOU 1314  CG1 ILE A 214     9897   8156   9825   1855  -3239    102       C\\nATOM   1315  CG2 ILE A 214      29.508   8.085  19.125  1.00 79.54           C\\nANISOU 1315  CG2 ILE A 214    10802   9091  10328   1753  -3532    141       C\\nATOM   1316  CD1 ILE A 214      29.840   8.022  16.221  1.00 79.87           C\\nANISOU 1316  CD1 ILE A 214    10233   9224  10891   1906  -3079   -130       C\\nATOM   1317  N   VAL A 215      26.138   7.447  20.558  1.00 80.48           N\\nANISOU 1317  N   VAL A 215    11834   9193   9553   1092  -3207    710       N\\nATOM   1318  CA  VAL A 215      25.693   7.866  21.883  1.00 80.01           C\\nANISOU 1318  CA  VAL A 215    11978   9313   9108    905  -3241    790       C\\nATOM   1319  C   VAL A 215      25.303   6.658  22.722  1.00 86.31           C\\nANISOU 1319  C   VAL A 215    13235   9978   9582    774  -3480   1098       C\\nATOM   1320  O   VAL A 215      25.668   6.557  23.900  1.00 89.76           O\\nANISOU 1320  O   VAL A 215    13882  10466   9758    750  -3755   1189       O\\nATOM   1321  CB  VAL A 215      24.532   8.868  21.764  1.00 69.82           C\\nANISOU 1321  CB  VAL A 215    10575   8272   7681    685  -2829    710       C\\nATOM   1322  CG1 VAL A 215      23.873   9.073  23.115  1.00 70.46           C\\nANISOU 1322  CG1 VAL A 215    10891   8582   7299    474  -2833    787       C\\nATOM   1323  CG2 VAL A 215      25.035  10.188  21.201  1.00 70.96           C\\nANISOU 1323  CG2 VAL A 215    10323   8520   8117    791  -2692    435       C\\nATOM   1324  N   LEU A 216      24.556   5.722  22.131  1.00 88.27           N\\nANISOU 1324  N   LEU A 216    13660  10047   9830    664  -3400   1278       N\\nATOM   1325  CA  LEU A 216      24.129   4.539  22.870  1.00 81.42           C\\nANISOU 1325  CA  LEU A 216    13257   9014   8666    480  -3641   1616       C\\nATOM   1326  C   LEU A 216      25.314   3.682  23.294  1.00 84.21           C\\nANISOU 1326  C   LEU A 216    13802   9063   9129    728  -4180   1700       C\\nATOM   1327  O   LEU A 216      25.268   3.046  24.353  1.00 81.69           O\\nANISOU 1327  O   LEU A 216    13836   8687   8514    577  -4427   1947       O\\nATOM   1328  CB  LEU A 216      23.148   3.725  22.025  1.00 83.40           C\\nANISOU 1328  CB  LEU A 216    13629   9094   8967    318  -3470   1765       C\\nATOM   1329  CG  LEU A 216      21.846   4.440  21.657  1.00 89.34           C\\nANISOU 1329  CG  LEU A 216    14218  10142   9584     56  -2973   1707       C\\nATOM   1330  CD1 LEU A 216      21.017   3.625  20.676  1.00 88.79           C\\nANISOU 1330  CD1 LEU A 216    14221   9881   9633    -62  -2839   1814       C\\nATOM   1331  CD2 LEU A 216      21.046   4.736  22.911  1.00 97.88           C\\nANISOU 1331  CD2 LEU A 216    15482  11550  10159   -274  -2870   1850       C\\nATOM   1332  N   ARG A 217      26.382   3.651  22.492  1.00 81.94           N\\nANISOU 1332  N   ARG A 217    13237   8618   9279   1094  -4322   1464       N\\nATOM   1333  CA  ARG A 217      27.561   2.877  22.871  1.00 83.41           C\\nANISOU 1333  CA  ARG A 217    13486   8566   9641   1348  -4750   1435       C\\nATOM   1334  C   ARG A 217      28.345   3.556  23.985  1.00 85.61           C\\nANISOU 1334  C   ARG A 217    13711   9042   9775   1403  -4934   1364       C\\nATOM   1335  O   ARG A 217      28.952   2.873  24.816  1.00 80.30           O\\nANISOU 1335  O   ARG A 217    13221   8234   9057   1442  -5229   1443       O\\nATOM   1336  CB  ARG A 217      28.460   2.641  21.658  1.00 74.00           C\\nANISOU 1336  CB  ARG A 217    11946   7228   8942   1710  -4789   1141       C\\nATOM   1337  N   ARG A 218      28.347   4.891  24.021  1.00 77.47           N\\nANISOU 1337  N   ARG A 218    12427   8320   8687   1399  -4771   1198       N\\nATOM   1338  CA  ARG A 218      28.948   5.589  25.152  1.00 79.95           C\\nANISOU 1338  CA  ARG A 218    12725   8839   8812   1411  -4955   1127       C\\nATOM   1339  C   ARG A 218      28.170   5.328  26.435  1.00 82.04           C\\nANISOU 1339  C   ARG A 218    13403   9226   8543   1087  -4970   1402       C\\nATOM   1340  O   ARG A 218      28.765   5.243  27.517  1.00 84.60           O\\nANISOU 1340  O   ARG A 218    13838   9600   8707   1097  -5207   1432       O\\nATOM   1341  CB  ARG A 218      29.022   7.089  24.868  1.00 75.14           C\\nANISOU 1341  CB  ARG A 218    11692   8536   8320   1397  -4623    823       C\\nATOM   1342  N   ARG A 219      26.847   5.179  26.326  1.00 85.99           N\\nANISOU 1342  N   ARG A 219    14111   9803   8758    785  -4704   1599       N\\nATOM   1343  CA  ARG A 219      26.016   4.885  27.490  1.00 84.46           C\\nANISOU 1343  CA  ARG A 219    14260   9795   8035    425  -4645   1858       C\\nATOM   1344  C   ARG A 219      26.340   3.511  28.066  1.00 86.08           C\\nANISOU 1344  C   ARG A 219    14765   9710   8230    380  -4920   2118       C\\nATOM   1345  O   ARG A 219      26.501   3.361  29.283  1.00 90.06           O\\nANISOU 1345  O   ARG A 219    15467  10337   8414    256  -5076   2247       O\\nATOM   1346  CB  ARG A 219      24.539   4.978  27.102  1.00 85.75           C\\nANISOU 1346  CB  ARG A 219    14494  10127   7961    100  -4243   1970       C\\nATOM   1347  CG  ARG A 219      23.566   4.985  28.270  1.00 97.90           C\\nANISOU 1347  CG  ARG A 219    16277  12019   8900   -302  -4086   2160       C\\nATOM   1348  CD  ARG A 219      22.137   5.191  27.780  1.00103.51           C\\nANISOU 1348  CD  ARG A 219    16923  12951   9455   -597  -3619   2177       C\\nATOM   1349  NE  ARG A 219      22.015   6.380  26.940  1.00103.98           N\\nANISOU 1349  NE  ARG A 219    16513  13152   9842   -422  -3259   1780       N\\nATOM   1350  CZ  ARG A 219      21.746   7.599  27.400  1.00102.81           C\\nANISOU 1350  CZ  ARG A 219    16138  13388   9536   -439  -3032   1497       C\\nATOM   1351  NH1 ARG A 219      21.567   7.793  28.700  1.00112.25           N\\nANISOU 1351  NH1 ARG A 219    17509  14920  10223   -616  -3093   1534       N\\nATOM   1352  NH2 ARG A 219      21.656   8.624  26.563  1.00 90.07           N\\nANISOU 1352  NH2 ARG A 219    14137  11821   8266   -282  -2765   1173       N\\nATOM   1353  N   ARG A 220      26.443   2.493  27.205  1.00 85.93           N\\nANISOU 1353  N   ARG A 220    14788   9305   8558    483  -5002   2177       N\\nATOM   1354  CA  ARG A 220      26.753   1.145  27.680  1.00 92.53           C\\nANISOU 1354  CA  ARG A 220    15922   9808   9426    451  -5313   2391       C\\nATOM   1355  C   ARG A 220      28.118   1.092  28.355  1.00 98.18           C\\nANISOU 1355  C   ARG A 220    16600  10438  10265    730  -5700   2278       C\\nATOM   1356  O   ARG A 220      28.296   0.384  29.353  1.00 99.06           O\\nANISOU 1356  O   ARG A 220    17008  10452  10178    616  -5960   2492       O\\nATOM   1357  CB  ARG A 220      26.686   0.149  26.522  1.00 94.83           C\\nANISOU 1357  CB  ARG A 220    16221   9701  10109    561  -5350   2378       C\\nATOM   1358  CG  ARG A 220      25.281  -0.055  25.969  1.00100.75           C\\nANISOU 1358  CG  ARG A 220    17071  10487  10720    234  -5015   2543       C\\nATOM   1359  CD  ARG A 220      25.299  -0.715  24.596  1.00102.73           C\\nANISOU 1359  CD  ARG A 220    17220  10409  11403    417  -5011   2417       C\\nATOM   1360  NE  ARG A 220      23.971  -0.712  23.986  1.00105.76           N\\nANISOU 1360  NE  ARG A 220    17640  10872  11673    124  -4663   2533       N\\nATOM   1361  CZ  ARG A 220      23.743  -0.876  22.687  1.00111.13           C\\nANISOU 1361  CZ  ARG A 220    18166  11401  12658    249  -4533   2393       C\\nATOM   1362  NH1 ARG A 220      24.756  -1.052  21.850  1.00115.91           N\\nANISOU 1362  NH1 ARG A 220    18552  11801  13687    664  -4699   2115       N\\nATOM   1363  NH2 ARG A 220      22.500  -0.857  22.220  1.00109.07           N\\nANISOU 1363  NH2 ARG A 220    17943  11230  12267    -44  -4223   2509       N\\nATOM   1364  N   LYS A 221      29.096   1.832  27.826  1.00 87.90           N\\nANISOU 1364  N   LYS A 221    14922   9183   9293   1081  -5746   1943       N\\nATOM   1365  CA  LYS A 221      30.396   1.903  28.485  1.00 91.01           C\\nANISOU 1365  CA  LYS A 221    15227   9552   9800   1332  -6088   1803       C\\nATOM   1366  C   LYS A 221      30.311   2.643  29.815  1.00 92.81           C\\nANISOU 1366  C   LYS A 221    15563  10123   9576   1152  -6111   1881       C\\nATOM   1367  O   LYS A 221      31.080   2.348  30.738  1.00 97.14           O\\nANISOU 1367  O   LYS A 221    16229  10626  10054   1227  -6434   1922       O\\nATOM   1368  CB  LYS A 221      31.420   2.575  27.569  1.00 88.24           C\\nANISOU 1368  CB  LYS A 221    14391   9229   9907   1702  -6082   1409       C\\nATOM   1369  N   ARG A 222      29.386   3.599  29.935  1.00 89.90           N\\nANISOU 1369  N   ARG A 222    15156  10111   8890    923  -5782   1877       N\\nATOM   1370  CA  ARG A 222      29.220   4.328  31.190  1.00 91.86           C\\nANISOU 1370  CA  ARG A 222    15494  10740   8669    746  -5774   1897       C\\nATOM   1371  C   ARG A 222      28.375   3.544  32.190  1.00 96.10           C\\nANISOU 1371  C   ARG A 222    16450  11352   8712    379  -5763   2271       C\\nATOM   1372  O   ARG A 222      28.677   3.536  33.390  1.00100.34           O\\nANISOU 1372  O   ARG A 222    17145  12050   8928    306  -5948   2359       O\\nATOM   1373  CB  ARG A 222      28.596   5.698  30.923  1.00 87.62           C\\nANISOU 1373  CB  ARG A 222    14726  10572   7995    668  -5443   1670       C\\nATOM   1374  N   ASN A1002      27.322   2.874  31.712  1.00 85.72           N\\nANISOU 1374  N   ASN A1002    12716   9421  10431    154  -1889   1403       N\\nATOM   1375  CA  ASN A1002      26.456   2.104  32.601  1.00 78.54           C\\nANISOU 1375  CA  ASN A1002    11488   8720   9636    336  -1772   1042       C\\nATOM   1376  C   ASN A1002      27.206   0.951  33.259  1.00 74.17           C\\nANISOU 1376  C   ASN A1002    10829   8409   8943    253  -1283    980       C\\nATOM   1377  O   ASN A1002      26.974   0.646  34.435  1.00 77.99           O\\nANISOU 1377  O   ASN A1002    11066   9013   9552    361  -1151    748       O\\nATOM   1378  CB  ASN A1002      25.242   1.584  31.828  1.00 72.27           C\\nANISOU 1378  CB  ASN A1002    10694   8018   8747    370  -1959    956       C\\nATOM   1379  CG  ASN A1002      24.296   2.693  31.414  1.00 85.39           C\\nANISOU 1379  CG  ASN A1002    12363   9440  10641    548  -2522    954       C\\nATOM   1380  OD1 ASN A1002      24.569   3.871  31.643  1.00 91.93           O\\nANISOU 1380  OD1 ASN A1002    13249   9977  11701    641  -2774   1033       O\\nATOM   1381  ND2 ASN A1002      23.179   2.324  30.796  1.00 95.12           N\\nANISOU 1381  ND2 ASN A1002    13533  10764  11844    599  -2763    857       N\\nATOM   1382  N   ILE A1003      28.104   0.295  32.520  1.00 69.88           N\\nANISOU 1382  N   ILE A1003    10476   7942   8134     67  -1017   1180       N\\nATOM   1383  CA  ILE A1003      28.844  -0.824  33.094  1.00 75.25           C\\nANISOU 1383  CA  ILE A1003    11058   8796   8739     40   -607   1126       C\\nATOM   1384  C   ILE A1003      29.846  -0.336  34.137  1.00 79.70           C\\nANISOU 1384  C   ILE A1003    11473   9334   9474     69   -527   1154       C\\nATOM   1385  O   ILE A1003      30.117  -1.035  35.121  1.00 81.90           O\\nANISOU 1385  O   ILE A1003    11597   9734   9788    131   -334   1048       O\\nATOM   1386  CB  ILE A1003      29.526  -1.644  31.981  1.00 76.66           C\\nANISOU 1386  CB  ILE A1003    11445   9056   8624   -116   -342   1259       C\\nATOM   1387  CG1 ILE A1003      30.131  -2.927  32.553  1.00 83.23           C\\nANISOU 1387  CG1 ILE A1003    12171  10007   9446    -76     25   1164       C\\nATOM   1388  CG2 ILE A1003      30.599  -0.830  31.276  1.00 75.86           C\\nANISOU 1388  CG2 ILE A1003    11492   8897   8434   -279   -312   1524       C\\nATOM   1389  CD1 ILE A1003      30.765  -3.812  31.509  1.00 89.05           C\\nANISOU 1389  CD1 ILE A1003    13083  10813   9939   -170    311   1194       C\\nATOM   1390  N   PHE A1004      30.403   0.862  33.954  1.00 72.73           N\\nANISOU 1390  N   PHE A1004    10657   8281   8697      0   -708   1309       N\\nATOM   1391  CA  PHE A1004      31.300   1.419  34.961  1.00 72.86           C\\nANISOU 1391  CA  PHE A1004    10523   8260   8901      1   -698   1302       C\\nATOM   1392  C   PHE A1004      30.561   1.658  36.271  1.00 75.78           C\\nANISOU 1392  C   PHE A1004    10709   8641   9442    194   -837   1009       C\\nATOM   1393  O   PHE A1004      31.045   1.293  37.349  1.00 75.51           O\\nANISOU 1393  O   PHE A1004    10525   8740   9424    231   -703    911       O\\nATOM   1394  CB  PHE A1004      31.920   2.718  34.446  1.00 74.85           C\\nANISOU 1394  CB  PHE A1004    10908   8273   9256   -164   -904   1525       C\\nATOM   1395  CG  PHE A1004      32.831   3.387  35.431  1.00 80.49           C\\nANISOU 1395  CG  PHE A1004    11471   8921  10192   -205   -951   1497       C\\nATOM   1396  CD1 PHE A1004      34.093   2.876  35.685  1.00 79.31           C\\nANISOU 1396  CD1 PHE A1004    11166   8951  10018   -317   -675   1584       C\\nATOM   1397  CD2 PHE A1004      32.429   4.533  36.100  1.00 83.97           C\\nANISOU 1397  CD2 PHE A1004    11907   9110  10888   -118  -1297   1351       C\\nATOM   1398  CE1 PHE A1004      34.938   3.492  36.589  1.00 82.95           C\\nANISOU 1398  CE1 PHE A1004    11465   9368  10684   -377   -769   1550       C\\nATOM   1399  CE2 PHE A1004      33.269   5.154  37.007  1.00 85.07           C\\nANISOU 1399  CE2 PHE A1004    11928   9181  11215   -183  -1370   1289       C\\nATOM   1400  CZ  PHE A1004      34.525   4.633  37.251  1.00 84.25           C\\nANISOU 1400  CZ  PHE A1004    11666   9282  11062   -331  -1119   1402       C\\nATOM   1401  N   GLU A1005      29.376   2.270  36.194  1.00 75.34           N\\nANISOU 1401  N   GLU A1005    10654   8467   9503    325  -1114    852       N\\nATOM   1402  CA  GLU A1005      28.576   2.488  37.395  1.00 80.23           C\\nANISOU 1402  CA  GLU A1005    11062   9155  10266    516  -1188    504       C\\nATOM   1403  C   GLU A1005      28.115   1.169  38.000  1.00 86.02           C\\nANISOU 1403  C   GLU A1005    11656  10202  10825    527   -889    366       C\\nATOM   1404  O   GLU A1005      28.046   1.030  39.227  1.00 90.45           O\\nANISOU 1404  O   GLU A1005    12070  10923  11372    580   -788    167       O\\nATOM   1405  CB  GLU A1005      27.375   3.375  37.076  1.00 77.92           C\\nANISOU 1405  CB  GLU A1005    10741   8676  10189    694  -1544    334       C\\nATOM   1406  CG  GLU A1005      27.742   4.831  36.890  1.00 84.80           C\\nANISOU 1406  CG  GLU A1005    11751   9159  11311    720  -1903    409       C\\nATOM   1407  CD  GLU A1005      28.491   5.393  38.081  1.00 89.89           C\\nANISOU 1407  CD  GLU A1005    12315   9761  12076    724  -1883    248       C\\nATOM   1408  OE1 GLU A1005      27.991   5.262  39.219  1.00 89.61           O\\nANISOU 1408  OE1 GLU A1005    12069   9916  12064    880  -1796   -120       O\\nATOM   1409  OE2 GLU A1005      29.591   5.949  37.880  1.00 88.50           O\\nANISOU 1409  OE2 GLU A1005    12285   9394  11947    539  -1944    483       O\\nATOM   1410  N   MET A1006      27.798   0.187  37.153  1.00 78.13           N\\nANISOU 1410  N   MET A1006    10736   9284   9667    448   -755    474       N\\nATOM   1411  CA  MET A1006      27.337  -1.104  37.657  1.00 72.09           C\\nANISOU 1411  CA  MET A1006     9881   8748   8762    410   -494    376       C\\nATOM   1412  C   MET A1006      28.381  -1.755  38.553  1.00 75.65           C\\nANISOU 1412  C   MET A1006    10336   9295   9114    362   -262    468       C\\nATOM   1413  O   MET A1006      28.038  -2.402  39.549  1.00 76.42           O\\nANISOU 1413  O   MET A1006    10345   9565   9126    348   -119    363       O\\nATOM   1414  CB  MET A1006      26.994  -2.033  36.497  1.00 63.48           C\\nANISOU 1414  CB  MET A1006     8926   7661   7531    307   -419    476       C\\nATOM   1415  CG  MET A1006      26.279  -3.292  36.913  1.00 70.23           C\\nANISOU 1415  CG  MET A1006     9703   8684   8298    231   -215    360       C\\nATOM   1416  SD  MET A1006      26.609  -4.663  35.798  1.00 70.93           S\\nANISOU 1416  SD  MET A1006    10037   8714   8198     86    -29    502       S\\nATOM   1417  CE  MET A1006      25.235  -5.747  36.183  1.00 79.60           C\\nANISOU 1417  CE  MET A1006    11010   9948   9288    -46     55    311       C\\nATOM   1418  N   LEU A1007      29.660  -1.591  38.223  1.00 74.32           N\\nANISOU 1418  N   LEU A1007    10257   9030   8951    321   -234    678       N\\nATOM   1419  CA  LEU A1007      30.716  -2.231  38.992  1.00 72.19           C\\nANISOU 1419  CA  LEU A1007     9955   8841   8633    310    -74    777       C\\nATOM   1420  C   LEU A1007      31.310  -1.346  40.078  1.00 77.91           C\\nANISOU 1420  C   LEU A1007    10574   9585   9442    343   -217    715       C\\nATOM   1421  O   LEU A1007      31.846  -1.881  41.054  1.00 81.18           O\\nANISOU 1421  O   LEU A1007    10944  10120   9781    352   -154    740       O\\nATOM   1422  CB  LEU A1007      31.835  -2.718  38.066  1.00 71.02           C\\nANISOU 1422  CB  LEU A1007     9882   8633   8470    261     76    992       C\\nATOM   1423  CG  LEU A1007      31.556  -4.102  37.475  1.00 67.80           C\\nANISOU 1423  CG  LEU A1007     9585   8237   7941    251    288   1010       C\\nATOM   1424  CD1 LEU A1007      30.727  -4.015  36.198  1.00 65.13           C\\nANISOU 1424  CD1 LEU A1007     9386   7844   7514    183    249    974       C\\nATOM   1425  CD2 LEU A1007      32.848  -4.848  37.236  1.00 68.79           C\\nANISOU 1425  CD2 LEU A1007     9698   8348   8090    287    481   1140       C\\nATOM   1426  N   ARG A1008      31.232  -0.018  39.954  1.00 81.15           N\\nANISOU 1426  N   ARG A1008    10972   9855  10007    355   -447    635       N\\nATOM   1427  CA  ARG A1008      31.610   0.793  41.106  1.00 79.83           C\\nANISOU 1427  CA  ARG A1008    10721   9701   9912    383   -602    485       C\\nATOM   1428  C   ARG A1008      30.583   0.693  42.224  1.00 79.95           C\\nANISOU 1428  C   ARG A1008    10660   9903   9815    473   -581    181       C\\nATOM   1429  O   ARG A1008      30.878   1.089  43.357  1.00 82.62           O\\nANISOU 1429  O   ARG A1008    10953  10337  10104    486   -655     22       O\\nATOM   1430  CB  ARG A1008      31.814   2.257  40.711  1.00 75.25           C\\nANISOU 1430  CB  ARG A1008    10178   8848   9565    361   -878    461       C\\nATOM   1431  CG  ARG A1008      30.548   3.009  40.384  1.00 84.73           C\\nANISOU 1431  CG  ARG A1008    11405   9893  10893    488  -1070    258       C\\nATOM   1432  CD  ARG A1008      30.759   4.502  40.562  1.00 91.79           C\\nANISOU 1432  CD  ARG A1008    12342  10481  12053    509  -1399    147       C\\nATOM   1433  NE  ARG A1008      30.802   4.870  41.973  1.00 97.78           N\\nANISOU 1433  NE  ARG A1008    12996  11338  12815    587  -1451   -187       N\\nATOM   1434  CZ  ARG A1008      29.731   5.209  42.684  1.00100.58           C\\nANISOU 1434  CZ  ARG A1008    13254  11756  13206    785  -1504   -595       C\\nATOM   1435  NH1 ARG A1008      28.534   5.231  42.111  1.00 94.43           N\\nANISOU 1435  NH1 ARG A1008    12420  10935  12522    941  -1541   -707       N\\nATOM   1436  NH2 ARG A1008      29.857   5.526  43.966  1.00105.64           N\\nANISOU 1436  NH2 ARG A1008    13834  12529  13777    825  -1520   -917       N\\nATOM   1437  N   ILE A1009      29.394   0.171  41.926  1.00 74.25           N\\nANISOU 1437  N   ILE A1009     9910   9267   9034    507   -473     81       N\\nATOM   1438  CA  ILE A1009      28.416  -0.151  42.956  1.00 75.30           C\\nANISOU 1438  CA  ILE A1009     9929   9661   9019    531   -350   -186       C\\nATOM   1439  C   ILE A1009      28.680  -1.535  43.536  1.00 78.79           C\\nANISOU 1439  C   ILE A1009    10438  10305   9194    403   -107     -8       C\\nATOM   1440  O   ILE A1009      28.534  -1.752  44.743  1.00 85.17           O\\nANISOU 1440  O   ILE A1009    11227  11348   9787    355    -20   -120       O\\nATOM   1441  CB  ILE A1009      26.996  -0.039  42.373  1.00 72.07           C\\nANISOU 1441  CB  ILE A1009     9394   9267   8722    603   -364   -387       C\\nATOM   1442  CG1 ILE A1009      26.670   1.415  42.030  1.00 73.75           C\\nANISOU 1442  CG1 ILE A1009     9547   9243   9230    783   -675   -591       C\\nATOM   1443  CG2 ILE A1009      25.968  -0.620  43.332  1.00 70.49           C\\nANISOU 1443  CG2 ILE A1009     9027   9408   8349    556   -136   -634       C\\nATOM   1444  CD1 ILE A1009      25.423   1.572  41.190  1.00 76.17           C\\nANISOU 1444  CD1 ILE A1009     9730   9499   9713    890   -796   -718       C\\nATOM   1445  N   ASP A1010      29.079  -2.490  42.694  1.00 72.06           N\\nANISOU 1445  N   ASP A1010     9694   9350   8336    343     -7    269       N\\nATOM   1446  CA  ASP A1010      29.286  -3.870  43.127  1.00 72.56           C\\nANISOU 1446  CA  ASP A1010     9858   9501   8210    243    179    457       C\\nATOM   1447  C   ASP A1010      30.708  -4.106  43.629  1.00 75.95           C\\nANISOU 1447  C   ASP A1010    10352   9894   8612    272    117    675       C\\nATOM   1448  O   ASP A1010      30.908  -4.550  44.763  1.00 79.91           O\\nANISOU 1448  O   ASP A1010    10905  10541   8916    226    124    730       O\\nATOM   1449  CB  ASP A1010      28.966  -4.834  41.979  1.00 68.87           C\\nANISOU 1449  CB  ASP A1010     9481   8902   7784    190    300    582       C\\nATOM   1450  CG  ASP A1010      27.482  -4.951  41.709  1.00 73.05           C\\nANISOU 1450  CG  ASP A1010     9921   9528   8308    113    358    385       C\\nATOM   1451  OD1 ASP A1010      26.693  -4.307  42.432  1.00 67.48           O\\nANISOU 1451  OD1 ASP A1010     9046   9009   7582    124    341    140       O\\nATOM   1452  OD2 ASP A1010      27.105  -5.691  40.773  1.00 78.54           O\\nANISOU 1452  OD2 ASP A1010    10691  10123   9026     43    418    440       O\\nATOM   1453  N   GLU A1011      31.702  -3.824  42.788  1.00 76.16           N\\nANISOU 1453  N   GLU A1011    10363   9749   8825    334     50    808       N\\nATOM   1454  CA  GLU A1011      33.088  -4.089  43.149  1.00 80.16           C\\nANISOU 1454  CA  GLU A1011    10842  10236   9377    379    -14    997       C\\nATOM   1455  C   GLU A1011      33.663  -2.965  44.003  1.00 86.62           C\\nANISOU 1455  C   GLU A1011    11560  11131  10222    377   -238    897       C\\nATOM   1456  O   GLU A1011      34.212  -3.213  45.081  1.00 98.58           O\\nANISOU 1456  O   GLU A1011    13076  12768  11614    380   -345    952       O\\nATOM   1457  CB  GLU A1011      33.926  -4.284  41.885  1.00 82.54           C\\nANISOU 1457  CB  GLU A1011    11111  10383   9867    418     68   1140       C\\nATOM   1458  CG  GLU A1011      35.344  -4.765  42.134  1.00 89.74           C\\nANISOU 1458  CG  GLU A1011    11913  11291  10894    502     40   1313       C\\nATOM   1459  CD  GLU A1011      35.393  -6.223  42.539  1.00 95.34           C\\nANISOU 1459  CD  GLU A1011    12731  11959  11534    586    111   1445       C\\nATOM   1460  OE1 GLU A1011      35.895  -6.518  43.646  1.00 99.56           O\\nANISOU 1460  OE1 GLU A1011    13255  12559  12013    632    -51   1549       O\\nATOM   1461  OE2 GLU A1011      34.920  -7.072  41.751  1.00 94.59           O\\nANISOU 1461  OE2 GLU A1011    12763  11742  11436    596    295   1450       O\\nATOM   1462  N   GLY A1012      33.549  -1.725  43.534  1.00 83.15           N\\nANISOU 1462  N   GLY A1012    11062  10592   9938    362   -351    758       N\\nATOM   1463  CA  GLY A1012      34.064  -0.590  44.272  1.00 80.42           C\\nANISOU 1463  CA  GLY A1012    10644  10253   9660    339   -589    621       C\\nATOM   1464  C   GLY A1012      35.145   0.176  43.536  1.00 76.41           C\\nANISOU 1464  C   GLY A1012    10041   9573   9418    270   -701    745       C\\nATOM   1465  O   GLY A1012      36.026  -0.422  42.909  1.00 75.35           O\\nANISOU 1465  O   GLY A1012     9829   9430   9369    254   -588    972       O\\nATOM   1466  N   LEU A1013      35.090   1.505  43.610  1.00 72.47           N\\nANISOU 1466  N   LEU A1013     9539   8928   9066    216   -914    581       N\\nATOM   1467  CA  LEU A1013      36.059   2.381  42.960  1.00 75.06           C\\nANISOU 1467  CA  LEU A1013     9799   9069   9653     69  -1037    711       C\\nATOM   1468  C   LEU A1013      37.076   2.842  43.998  1.00 85.43           C\\nANISOU 1468  C   LEU A1013    10980  10447  11031    -12  -1266    645       C\\nATOM   1469  O   LEU A1013      36.730   3.569  44.935  1.00 92.30           O\\nANISOU 1469  O   LEU A1013    11906  11301  11864      3  -1478    364       O\\nATOM   1470  CB  LEU A1013      35.362   3.575  42.309  1.00 76.93           C\\nANISOU 1470  CB  LEU A1013    10164   9014  10053     35  -1188    614       C\\nATOM   1471  CG  LEU A1013      36.264   4.677  41.743  1.00 81.85           C\\nANISOU 1471  CG  LEU A1013    10778   9382  10939   -188  -1361    759       C\\nATOM   1472  CD1 LEU A1013      37.119   4.145  40.607  1.00 83.65           C\\nANISOU 1472  CD1 LEU A1013    10936   9672  11176   -345  -1119   1104       C\\nATOM   1473  CD2 LEU A1013      35.444   5.879  41.290  1.00 79.42           C\\nANISOU 1473  CD2 LEU A1013    10661   8711  10803   -183  -1600    657       C\\nATOM   1474  N   ARG A1014      38.324   2.416  43.830  1.00 82.30           N\\nANISOU 1474  N   ARG A1014    10388  10143  10740    -92  -1229    865       N\\nATOM   1475  CA  ARG A1014      39.431   2.846  44.673  1.00 87.70           C\\nANISOU 1475  CA  ARG A1014    10885  10900  11537   -200  -1487    834       C\\nATOM   1476  C   ARG A1014      40.374   3.720  43.858  1.00 91.11           C\\nANISOU 1476  C   ARG A1014    11154  11170  12293   -454  -1533    970       C\\nATOM   1477  O   ARG A1014      40.854   3.301  42.800  1.00 93.58           O\\nANISOU 1477  O   ARG A1014    11348  11510  12699   -513  -1278   1201       O\\nATOM   1478  CB  ARG A1014      40.189   1.647  45.242  1.00 89.70           C\\nANISOU 1478  CB  ARG A1014    10969  11409  11702    -83  -1465    977       C\\nATOM   1479  CG  ARG A1014      39.445   0.867  46.311  1.00 95.14           C\\nANISOU 1479  CG  ARG A1014    11845  12266  12037     80  -1493    888       C\\nATOM   1480  CD  ARG A1014      40.338   0.658  47.527  1.00103.70           C\\nANISOU 1480  CD  ARG A1014    12817  13547  13039     82  -1799    903       C\\nATOM   1481  NE  ARG A1014      39.801  -0.327  48.462  1.00107.67           N\\nANISOU 1481  NE  ARG A1014    13522  14230  13160    204  -1802    939       N\\nATOM   1482  CZ  ARG A1014      40.399  -0.677  49.597  1.00111.85           C\\nANISOU 1482  CZ  ARG A1014    14048  14948  13504    219  -2094    997       C\\nATOM   1483  NH1 ARG A1014      41.553  -0.119  49.939  1.00113.46           N\\nANISOU 1483  NH1 ARG A1014    14008  15196  13905    140  -2424    984       N\\nATOM   1484  NH2 ARG A1014      39.844  -1.584  50.391  1.00112.62           N\\nANISOU 1484  NH2 ARG A1014    14392  15192  13208    282  -2078   1085       N\\nATOM   1485  N   LEU A1015      40.648   4.926  44.357  1.00 92.65           N\\nANISOU 1485  N   LEU A1015    11353  11202  12646   -633  -1845    811       N\\nATOM   1486  CA  LEU A1015      41.453   5.897  43.627  1.00 98.42           C\\nANISOU 1486  CA  LEU A1015    11974  11728  13694   -955  -1914    952       C\\nATOM   1487  C   LEU A1015      42.928   5.886  44.013  1.00100.85           C\\nANISOU 1487  C   LEU A1015    11893  12218  14209  -1148  -2036   1034       C\\nATOM   1488  O   LEU A1015      43.750   6.434  43.268  1.00 98.40           O\\nANISOU 1488  O   LEU A1015    11399  11829  14161  -1460  -1984   1214       O\\nATOM   1489  CB  LEU A1015      40.885   7.309  43.827  1.00 99.65           C\\nANISOU 1489  CB  LEU A1015    12381  11497  13985  -1071  -2220    736       C\\nATOM   1490  CG  LEU A1015      39.471   7.567  43.292  1.00 99.54           C\\nANISOU 1490  CG  LEU A1015    12694  11242  13885   -893  -2166    655       C\\nATOM   1491  CD1 LEU A1015      39.000   8.964  43.667  1.00 99.18           C\\nANISOU 1491  CD1 LEU A1015    12859  10780  14044   -939  -2532    377       C\\nATOM   1492  CD2 LEU A1015      39.410   7.369  41.782  1.00 97.70           C\\nANISOU 1492  CD2 LEU A1015    12526  10927  13670   -996  -1904   1008       C\\nATOM   1493  N   LYS A1016      43.285   5.285  45.145  1.00105.59           N\\nANISOU 1493  N   LYS A1016    12353  13074  14693   -995  -2209    921       N\\nATOM   1494  CA  LYS A1016      44.673   5.127  45.549  1.00101.07           C\\nANISOU 1494  CA  LYS A1016    11354  12717  14330  -1119  -2373    997       C\\nATOM   1495  C   LYS A1016      45.057   3.654  45.506  1.00 97.42           C\\nANISOU 1495  C   LYS A1016    10673  12549  13792   -837  -2171   1168       C\\nATOM   1496  O   LYS A1016      44.204   2.765  45.581  1.00 93.98           O\\nANISOU 1496  O   LYS A1016    10480  12152  13076   -558  -2006   1179       O\\nATOM   1497  CB  LYS A1016      44.913   5.693  46.953  1.00 96.36           C\\nANISOU 1497  CB  LYS A1016    10775  12159  13680  -1180  -2856    730       C\\nATOM   1498  N   ILE A1017      46.361   3.401  45.382  1.00 93.92           N\\nANISOU 1498  N   ILE A1017     9745  12296  13643   -915  -2196   1291       N\\nATOM   1499  CA  ILE A1017      46.835   2.030  45.257  1.00 95.27           C\\nANISOU 1499  CA  ILE A1017     9663  12692  13845   -609  -2025   1434       C\\nATOM   1500  C   ILE A1017      46.498   1.247  46.517  1.00 93.58           C\\nANISOU 1500  C   ILE A1017     9634  12578  13344   -317  -2322   1390       C\\nATOM   1501  O   ILE A1017      46.630   1.745  47.643  1.00 98.49           O\\nANISOU 1501  O   ILE A1017    10306  13255  13861   -400  -2751   1258       O\\nATOM   1502  CB  ILE A1017      48.346   2.013  44.968  1.00 99.88           C\\nANISOU 1502  CB  ILE A1017     9604  13484  14862   -733  -2035   1517       C\\nATOM   1503  CG1 ILE A1017      48.641   2.776  43.677  1.00 99.15           C\\nANISOU 1503  CG1 ILE A1017     9368  13325  14980  -1097  -1674   1598       C\\nATOM   1504  CG2 ILE A1017      48.859   0.586  44.863  1.00102.32           C\\nANISOU 1504  CG2 ILE A1017     9624  13983  15272   -342  -1894   1617       C\\nATOM   1505  CD1 ILE A1017      50.072   2.657  43.214  1.00100.19           C\\nANISOU 1505  CD1 ILE A1017     8808  13728  15530  -1237  -1535   1668       C\\nATOM   1506  N   TYR A1018      46.040   0.013  46.328  1.00 96.96           N\\nANISOU 1506  N   TYR A1018    10204  13021  13613     -4  -2100   1503       N\\nATOM   1507  CA  TYR A1018      45.693  -0.867  47.432  1.00100.96           C\\nANISOU 1507  CA  TYR A1018    10937  13603  13821    241  -2341   1544       C\\nATOM   1508  C   TYR A1018      45.961  -2.303  47.006  1.00113.96           C\\nANISOU 1508  C   TYR A1018    12472  15250  15576    569  -2149   1734       C\\nATOM   1509  O   TYR A1018      46.224  -2.587  45.835  1.00121.07           O\\nANISOU 1509  O   TYR A1018    13172  16106  16722    616  -1774   1767       O\\nATOM   1510  CB  TYR A1018      44.232  -0.693  47.850  1.00 93.06           C\\nANISOU 1510  CB  TYR A1018    10474  12514  12372    220  -2278   1421       C\\nATOM   1511  CG  TYR A1018      43.253  -1.208  46.822  1.00 94.64           C\\nANISOU 1511  CG  TYR A1018    10901  12566  12493    308  -1824   1465       C\\nATOM   1512  CD1 TYR A1018      43.069  -0.541  45.617  1.00 98.44           C\\nANISOU 1512  CD1 TYR A1018    11346  12911  13146    160  -1544   1428       C\\nATOM   1513  CD2 TYR A1018      42.513  -2.358  47.053  1.00 92.36           C\\nANISOU 1513  CD2 TYR A1018    10884  12266  11944    505  -1704   1563       C\\nATOM   1514  CE1 TYR A1018      42.179  -1.007  44.669  1.00 97.08           C\\nANISOU 1514  CE1 TYR A1018    11389  12624  12873    230  -1183   1460       C\\nATOM   1515  CE2 TYR A1018      41.614  -2.831  46.111  1.00 95.41           C\\nANISOU 1515  CE2 TYR A1018    11463  12519  12271    556  -1325   1577       C\\nATOM   1516  CZ  TYR A1018      41.450  -2.147  44.923  1.00 96.24           C\\nANISOU 1516  CZ  TYR A1018    11515  12518  12534    430  -1079   1511       C\\nATOM   1517  OH  TYR A1018      40.562  -2.611  43.980  1.00 94.30           O\\nANISOU 1517  OH  TYR A1018    11469  12159  12201    471   -755   1517       O\\nATOM   1518  N   LYS A1019      45.882  -3.212  47.972  1.00112.29           N\\nANISOU 1518  N   LYS A1019    12428  15075  15161    787  -2416   1854       N\\nATOM   1519  CA  LYS A1019      46.124  -4.629  47.736  1.00114.49           C\\nANISOU 1519  CA  LYS A1019    12662  15272  15567   1129  -2330   2040       C\\nATOM   1520  C   LYS A1019      44.796  -5.365  47.616  1.00112.47           C\\nANISOU 1520  C   LYS A1019    12933  14846  14954   1191  -2067   2094       C\\nATOM   1521  O   LYS A1019      43.893  -5.162  48.435  1.00114.99           O\\nANISOU 1521  O   LYS A1019    13645  15200  14846   1061  -2176   2073       O\\nATOM   1522  CB  LYS A1019      46.964  -5.233  48.863  1.00116.93           C\\nANISOU 1522  CB  LYS A1019    12829  15675  15923   1330  -2866   2206       C\\nATOM   1523  N   ASP A1020      44.677  -6.212  46.597  1.00112.39           N\\nANISOU 1523  N   ASP A1020    12914  14672  15118   1369  -1707   2129       N\\nATOM   1524  CA  ASP A1020      43.491  -7.038  46.453  1.00108.38           C\\nANISOU 1524  CA  ASP A1020    12868  13981  14329   1415  -1485   2186       C\\nATOM   1525  C   ASP A1020      43.556  -8.206  47.436  1.00111.34           C\\nANISOU 1525  C   ASP A1020    13459  14255  14590   1619  -1796   2432       C\\nATOM   1526  O   ASP A1020      44.475  -8.316  48.253  1.00111.64           O\\nANISOU 1526  O   ASP A1020    13307  14376  14734   1741  -2219   2559       O\\nATOM   1527  CB  ASP A1020      43.344  -7.520  45.010  1.00103.84           C\\nANISOU 1527  CB  ASP A1020    12244  13254  13957   1507  -1026   2105       C\\nATOM   1528  CG  ASP A1020      44.444  -8.477  44.594  1.00108.01           C\\nANISOU 1528  CG  ASP A1020    12440  13694  14903   1844  -1010   2150       C\\nATOM   1529  OD1 ASP A1020      45.525  -8.453  45.217  1.00113.64           O\\nANISOU 1529  OD1 ASP A1020    12802  14515  15861   1981  -1346   2220       O\\nATOM   1530  OD2 ASP A1020      44.228  -9.253  43.639  1.00105.75           O\\nANISOU 1530  OD2 ASP A1020    12227  13235  14718   1987   -677   2082       O\\nATOM   1531  N   THR A1021      42.571  -9.101  47.357  1.00111.86           N\\nANISOU 1531  N   THR A1021    13936  14124  14441   1634  -1618   2524       N\\nATOM   1532  CA  THR A1021      42.498 -10.201  48.311  1.00111.37           C\\nANISOU 1532  CA  THR A1021    14180  13918  14216   1754  -1913   2816       C\\nATOM   1533  C   THR A1021      43.592 -11.242  48.108  1.00113.87           C\\nANISOU 1533  C   THR A1021    14272  14000  14994   2154  -2104   2966       C\\nATOM   1534  O   THR A1021      43.713 -12.150  48.936  1.00122.97           O\\nANISOU 1534  O   THR A1021    15669  14982  16073   2291  -2453   3261       O\\nATOM   1535  CB  THR A1021      41.130 -10.879  48.236  1.00106.11           C\\nANISOU 1535  CB  THR A1021    14000  13085  13230   1600  -1650   2877       C\\nATOM   1536  OG1 THR A1021      40.997 -11.555  46.980  1.00101.52           O\\nANISOU 1536  OG1 THR A1021    13390  12234  12949   1746  -1308   2783       O\\nATOM   1537  CG2 THR A1021      40.020  -9.844  48.372  1.00105.59           C\\nANISOU 1537  CG2 THR A1021    14074  13265  12778   1259  -1443   2671       C\\nATOM   1538  N   GLU A1022      44.388 -11.136  47.045  1.00109.65           N\\nANISOU 1538  N   GLU A1022    13282  13452  14927   2346  -1889   2772       N\\nATOM   1539  CA  GLU A1022      45.477 -12.070  46.790  1.00109.91           C\\nANISOU 1539  CA  GLU A1022    13002  13289  15472   2780  -2033   2824       C\\nATOM   1540  C   GLU A1022      46.850 -11.447  47.014  1.00110.30           C\\nANISOU 1540  C   GLU A1022    12423  13602  15882   2906  -2315   2766       C\\nATOM   1541  O   GLU A1022      47.866 -12.107  46.769  1.00114.91           O\\nANISOU 1541  O   GLU A1022    12609  14084  16969   3299  -2431   2752       O\\nATOM   1542  CB  GLU A1022      45.376 -12.625  45.367  1.00110.94           C\\nANISOU 1542  CB  GLU A1022    13056  13217  15878   2939  -1526   2594       C\\nATOM   1543  N   GLY A1023      46.907 -10.195  47.471  1.00108.89           N\\nANISOU 1543  N   GLY A1023    12123  13753  15498   2586  -2436   2704       N\\nATOM   1544  CA  GLY A1023      48.156  -9.536  47.793  1.00110.44           C\\nANISOU 1544  CA  GLY A1023    11736  14212  16013   2619  -2755   2653       C\\nATOM   1545  C   GLY A1023      48.709  -8.632  46.710  1.00113.05           C\\nANISOU 1545  C   GLY A1023    11548  14751  16654   2465  -2360   2382       C\\nATOM   1546  O   GLY A1023      49.639  -7.862  46.986  1.00112.39           O\\nANISOU 1546  O   GLY A1023    10982  14921  16798   2361  -2597   2323       O\\nATOM   1547  N   TYR A1024      48.174  -8.700  45.495  1.00108.30           N\\nANISOU 1547  N   TYR A1024    11043  14058  16046   2411  -1784   2230       N\\nATOM   1548  CA  TYR A1024      48.663  -7.880  44.398  1.00113.34           C\\nANISOU 1548  CA  TYR A1024    11259  14900  16907   2217  -1372   2019       C\\nATOM   1549  C   TYR A1024      48.186  -6.439  44.545  1.00111.52           C\\nANISOU 1549  C   TYR A1024    11170  14816  16386   1738  -1381   1979       C\\nATOM   1550  O   TYR A1024      47.084  -6.173  45.033  1.00110.91           O\\nANISOU 1550  O   TYR A1024    11615  14645  15882   1574  -1459   2021       O\\nATOM   1551  CB  TYR A1024      48.188  -8.447  43.060  1.00116.94           C\\nANISOU 1551  CB  TYR A1024    11856  15216  17360   2297   -787   1879       C\\nATOM   1552  CG  TYR A1024      48.578  -9.890  42.820  1.00122.30           C\\nANISOU 1552  CG  TYR A1024    12446  15674  18349   2790   -744   1850       C\\nATOM   1553  CD1 TYR A1024      49.830 -10.364  43.189  1.00128.61           C\\nANISOU 1553  CD1 TYR A1024    12689  16530  19645   3150  -1024   1848       C\\nATOM   1554  CD2 TYR A1024      47.689 -10.779  42.227  1.00118.01           C\\nANISOU 1554  CD2 TYR A1024    12364  14836  17638   2906   -460   1804       C\\nATOM   1555  CE1 TYR A1024      50.188 -11.681  42.970  1.00131.77           C\\nANISOU 1555  CE1 TYR A1024    13011  16664  20391   3655  -1019   1793       C\\nATOM   1556  CE2 TYR A1024      48.037 -12.096  42.004  1.00120.38           C\\nANISOU 1556  CE2 TYR A1024    12621  14859  18257   3363   -444   1744       C\\nATOM   1557  CZ  TYR A1024      49.287 -12.542  42.377  1.00129.11           C\\nANISOU 1557  CZ  TYR A1024    13187  15991  19879   3758   -723   1736       C\\nATOM   1558  OH  TYR A1024      49.639 -13.855  42.158  1.00133.04           O\\nANISOU 1558  OH  TYR A1024    13642  16152  20756   4269   -742   1651       O\\nATOM   1559  N   TYR A1025      49.029  -5.504  44.113  1.00117.71           N\\nANISOU 1559  N   TYR A1025    11469  15821  17433   1507  -1294   1881       N\\nATOM   1560  CA  TYR A1025      48.682  -4.087  44.152  1.00110.35           C\\nANISOU 1560  CA  TYR A1025    10659  14955  16314   1049  -1319   1834       C\\nATOM   1561  C   TYR A1025      47.758  -3.760  42.985  1.00104.43           C\\nANISOU 1561  C   TYR A1025    10246  14092  15339    855   -821   1781       C\\nATOM   1562  O   TYR A1025      48.115  -3.979  41.822  1.00101.17           O\\nANISOU 1562  O   TYR A1025     9617  13740  15082    859   -384   1729       O\\nATOM   1563  CB  TYR A1025      49.939  -3.221  44.101  1.00111.84           C\\nANISOU 1563  CB  TYR A1025    10220  15385  16890    814  -1427   1782       C\\nATOM   1564  CG  TYR A1025      50.892  -3.432  45.257  1.00115.51           C\\nANISOU 1564  CG  TYR A1025    10303  15992  17595    978  -1998   1822       C\\nATOM   1565  CD1 TYR A1025      50.776  -2.688  46.423  1.00114.38           C\\nANISOU 1565  CD1 TYR A1025    10332  15875  17252    775  -2517   1825       C\\nATOM   1566  CD2 TYR A1025      51.915  -4.369  45.177  1.00120.42           C\\nANISOU 1566  CD2 TYR A1025    10384  16722  18646   1352  -2046   1830       C\\nATOM   1567  CE1 TYR A1025      51.647  -2.875  47.481  1.00116.89           C\\nANISOU 1567  CE1 TYR A1025    10328  16345  17742    906  -3095   1869       C\\nATOM   1568  CE2 TYR A1025      52.791  -4.563  46.228  1.00124.27           C\\nANISOU 1568  CE2 TYR A1025    10509  17338  19372   1522  -2643   1887       C\\nATOM   1569  CZ  TYR A1025      52.653  -3.813  47.377  1.00124.31           C\\nANISOU 1569  CZ  TYR A1025    10724  17386  19121   1279  -3180   1923       C\\nATOM   1570  OH  TYR A1025      53.523  -4.004  48.428  1.00131.17           O\\nANISOU 1570  OH  TYR A1025    11258  18402  20177   1430  -3829   1986       O\\nATOM   1571  N   THR A1026      46.569  -3.247  43.288  1.00104.70           N\\nANISOU 1571  N   THR A1026    10799  13985  14997    692   -893   1776       N\\nATOM   1572  CA  THR A1026      45.596  -2.892  42.268  1.00105.81           C\\nANISOU 1572  CA  THR A1026    11282  14002  14919    524   -528   1739       C\\nATOM   1573  C   THR A1026      45.108  -1.467  42.499  1.00102.55           C\\nANISOU 1573  C   THR A1026    11058  13525  14382    179   -701   1694       C\\nATOM   1574  O   THR A1026      45.449  -0.819  43.493  1.00 98.86           O\\nANISOU 1574  O   THR A1026    10500  13102  13962     75  -1083   1653       O\\nATOM   1575  CB  THR A1026      44.400  -3.858  42.255  1.00102.47           C\\nANISOU 1575  CB  THR A1026    11323  13413  14198    735   -413   1745       C\\nATOM   1576  OG1 THR A1026      43.497  -3.517  43.312  1.00 98.43           O\\nANISOU 1576  OG1 THR A1026    11152  12846  13400    677   -704   1728       O\\nATOM   1577  CG2 THR A1026      44.861  -5.301  42.437  1.00103.30           C\\nANISOU 1577  CG2 THR A1026    11315  13487  14447   1108   -410   1798       C\\nATOM   1578  N   ILE A1027      44.296  -0.982  41.560  1.00 99.57           N\\nANISOU 1578  N   ILE A1027    10963  13018  13850     15   -450   1686       N\\nATOM   1579  CA  ILE A1027      43.734   0.361  41.638  1.00 94.27           C\\nANISOU 1579  CA  ILE A1027    10513  12198  13107   -265   -621   1637       C\\nATOM   1580  C   ILE A1027      42.483   0.419  40.770  1.00 89.78           C\\nANISOU 1580  C   ILE A1027    10350  11463  12301   -276   -407   1635       C\\nATOM   1581  O   ILE A1027      42.233  -0.483  39.962  1.00 86.52           O\\nANISOU 1581  O   ILE A1027    10008  11080  11787   -145    -97   1677       O\\nATOM   1582  CB  ILE A1027      44.771   1.417  41.213  1.00 89.65           C\\nANISOU 1582  CB  ILE A1027     9615  11643  12803   -620   -639   1700       C\\nATOM   1583  CG1 ILE A1027      44.397   2.796  41.761  1.00 84.69           C\\nANISOU 1583  CG1 ILE A1027     9187  10803  12189   -869   -988   1614       C\\nATOM   1584  CG2 ILE A1027      44.914   1.453  39.698  1.00 80.58           C\\nANISOU 1584  CG2 ILE A1027     8450  10512  11654   -794   -204   1829       C\\nATOM   1585  CD1 ILE A1027      45.403   3.866  41.434  1.00 82.74           C\\nANISOU 1585  CD1 ILE A1027     8667  10528  12241  -1282  -1056   1694       C\\nATOM   1586  N   GLY A1028      41.681   1.469  40.938  1.00 90.15           N\\nANISOU 1586  N   GLY A1028    10659  11318  12274   -414   -605   1560       N\\nATOM   1587  CA  GLY A1028      40.491   1.617  40.118  1.00 84.64           C\\nANISOU 1587  CA  GLY A1028    10306  10458  11396   -412   -482   1559       C\\nATOM   1588  C   GLY A1028      39.429   0.607  40.504  1.00 83.32           C\\nANISOU 1588  C   GLY A1028    10333  10329  10994   -142   -422   1455       C\\nATOM   1589  O   GLY A1028      39.140   0.390  41.685  1.00 81.04           O\\nANISOU 1589  O   GLY A1028    10066  10102  10624    -17   -599   1333       O\\nATOM   1590  N   ILE A1029      38.832  -0.021  39.494  1.00 90.61           N\\nANISOU 1590  N   ILE A1029    11415  11232  11782    -90   -168   1506       N\\nATOM   1591  CA  ILE A1029      37.857  -1.077  39.728  1.00 88.98           C\\nANISOU 1591  CA  ILE A1029    11375  11052  11381    109    -82   1426       C\\nATOM   1592  C   ILE A1029      38.467  -2.405  39.306  1.00 96.86           C\\nANISOU 1592  C   ILE A1029    12278  12138  12386    239    180   1504       C\\nATOM   1593  O   ILE A1029      38.305  -2.841  38.160  1.00 98.47           O\\nANISOU 1593  O   ILE A1029    12577  12322  12515    224    426   1527       O\\nATOM   1594  CB  ILE A1029      36.538  -0.812  38.980  1.00 75.33           C\\nANISOU 1594  CB  ILE A1029     9908   9202   9511     82    -63   1368       C\\nATOM   1595  CG1 ILE A1029      35.978   0.560  39.350  1.00 71.56           C\\nANISOU 1595  CG1 ILE A1029     9501   8581   9108     11   -352   1261       C\\nATOM   1596  CG2 ILE A1029      35.522  -1.900  39.298  1.00 63.88           C\\nANISOU 1596  CG2 ILE A1029     8583   7799   7889    229     23   1272       C\\nATOM   1597  CD1 ILE A1029      34.589   0.806  38.813  1.00 68.30           C\\nANISOU 1597  CD1 ILE A1029     9287   8054   8610     55   -413   1168       C\\nATOM   1598  N   GLY A1030      39.179  -3.050  40.226  1.00 99.15           N\\nANISOU 1598  N   GLY A1030    12396  12511  12765    380    101   1529       N\\nATOM   1599  CA  GLY A1030      39.787  -4.335  39.947  1.00 98.18           C\\nANISOU 1599  CA  GLY A1030    12171  12410  12722    571    291   1577       C\\nATOM   1600  C   GLY A1030      40.760  -4.288  38.789  1.00 94.57           C\\nANISOU 1600  C   GLY A1030    11485  12025  12421    523    562   1598       C\\nATOM   1601  O   GLY A1030      40.506  -4.869  37.728  1.00 95.69           O\\nANISOU 1601  O   GLY A1030    11749  12138  12469    550    849   1553       O\\nATOM   1602  N   HIS A1031      41.878  -3.592  38.977  1.00 87.03           N\\nANISOU 1602  N   HIS A1031    10189  11192  11687    421    486   1644       N\\nATOM   1603  CA  HIS A1031      42.893  -3.436  37.938  1.00 89.86           C\\nANISOU 1603  CA  HIS A1031    10256  11692  12196    312    785   1660       C\\nATOM   1604  C   HIS A1031      44.259  -3.687  38.565  1.00 92.16           C\\nANISOU 1604  C   HIS A1031    10046  12138  12831    439    693   1664       C\\nATOM   1605  O   HIS A1031      44.848  -2.781  39.162  1.00 95.75           O\\nANISOU 1605  O   HIS A1031    10270  12666  13443    260    450   1711       O\\nATOM   1606  CB  HIS A1031      42.821  -2.053  37.308  1.00 89.34           C\\nANISOU 1606  CB  HIS A1031    10256  11621  12066    -69    797   1742       C\\nATOM   1607  CG  HIS A1031      43.762  -1.865  36.161  1.00 92.70           C\\nANISOU 1607  CG  HIS A1031    10434  12232  12556   -271   1167   1789       C\\nATOM   1608  ND1 HIS A1031      43.332  -1.784  34.855  1.00 93.45           N\\nANISOU 1608  ND1 HIS A1031    10789  12339  12379   -440   1471   1824       N\\nATOM   1609  CD2 HIS A1031      45.109  -1.748  36.123  1.00 96.67           C\\nANISOU 1609  CD2 HIS A1031    10434  12956  13341   -356   1297   1798       C\\nATOM   1610  CE1 HIS A1031      44.375  -1.621  34.061  1.00 97.80           C\\nANISOU 1610  CE1 HIS A1031    11037  13125  12996   -641   1814   1858       C\\nATOM   1611  NE2 HIS A1031      45.465  -1.597  34.805  1.00100.11           N\\nANISOU 1611  NE2 HIS A1031    10830  13554  13654   -592   1731   1833       N\\nATOM   1612  N   LEU A1032      44.761  -4.912  38.422  1.00 91.24           N\\nANISOU 1612  N   LEU A1032     9754  12051  12863    756    853   1596       N\\nATOM   1613  CA  LEU A1032      46.058  -5.267  38.982  1.00 95.11           C\\nANISOU 1613  CA  LEU A1032     9720  12682  13737    952    730   1587       C\\nATOM   1614  C   LEU A1032      47.161  -4.499  38.265  1.00 99.71           C\\nANISOU 1614  C   LEU A1032     9815  13531  14540    697    975   1562       C\\nATOM   1615  O   LEU A1032      47.347  -4.649  37.054  1.00 96.96           O\\nANISOU 1615  O   LEU A1032     9403  13297  14140    624   1442   1479       O\\nATOM   1616  CB  LEU A1032      46.290  -6.772  38.868  1.00 93.50           C\\nANISOU 1616  CB  LEU A1032     9457  12381  13686   1392    849   1495       C\\nATOM   1617  N   LEU A1033      47.887  -3.667  39.013  1.00 97.35           N\\nANISOU 1617  N   LEU A1033     9181  13349  14459    521    666   1628       N\\nATOM   1618  CA  LEU A1033      49.025  -2.964  38.434  1.00104.31           C\\nANISOU 1618  CA  LEU A1033     9528  14502  15604    230    883   1619       C\\nATOM   1619  C   LEU A1033      50.158  -3.934  38.121  1.00112.65           C\\nANISOU 1619  C   LEU A1033     9983  15786  17034    550   1131   1473       C\\nATOM   1620  O   LEU A1033      50.737  -3.897  37.029  1.00115.99           O\\nANISOU 1620  O   LEU A1033    10102  16446  17521    410   1635   1381       O\\nATOM   1621  CB  LEU A1033      49.494  -1.861  39.381  1.00103.46           C\\nANISOU 1621  CB  LEU A1033     9213  14430  15668    -55    434   1699       C\\nATOM   1622  N   THR A1034      50.477  -4.818  39.064  1.00114.71           N\\nANISOU 1622  N   THR A1034    10071  15980  17534    990    782   1443       N\\nATOM   1623  CA  THR A1034      51.514  -5.822  38.866  1.00119.05           C\\nANISOU 1623  CA  THR A1034    10043  16677  18514   1403    933   1278       C\\nATOM   1624  C   THR A1034      51.333  -6.919  39.904  1.00116.13           C\\nANISOU 1624  C   THR A1034     9831  16045  18250   1915    470   1326       C\\nATOM   1625  O   THR A1034      50.615  -6.756  40.893  1.00112.94           O\\nANISOU 1625  O   THR A1034     9869  15449  17593   1873     24   1499       O\\nATOM   1626  CB  THR A1034      52.919  -5.218  38.968  1.00123.11           C\\nANISOU 1626  CB  THR A1034     9729  17558  19489   1237    901   1232       C\\nATOM   1627  OG1 THR A1034      53.898  -6.241  38.746  1.00127.31           O\\nANISOU 1627  OG1 THR A1034     9644  18240  20490   1707   1059   1022       O\\nATOM   1628  CG2 THR A1034      53.135  -4.617  40.344  1.00124.58           C\\nANISOU 1628  CG2 THR A1034     9836  17714  19783   1140    210   1384       C\\nATOM   1629  N   LYS A1035      51.998  -8.046  39.660  1.00124.24           N\\nANISOU 1629  N   LYS A1035    10499  17061  19647   2398    588   1165       N\\nATOM   1630  CA  LYS A1035      52.071  -9.132  40.624  1.00115.60           C\\nANISOU 1630  CA  LYS A1035     9471  15694  18757   2910    100   1245       C\\nATOM   1631  C   LYS A1035      53.350  -9.089  41.448  1.00124.45           C\\nANISOU 1631  C   LYS A1035     9878  17011  20395   3112   -361   1270       C\\nATOM   1632  O   LYS A1035      53.591 -10.004  42.241  1.00126.86           O\\nANISOU 1632  O   LYS A1035    10167  17100  20932   3572   -826   1360       O\\nATOM   1633  CB  LYS A1035      51.953 -10.483  39.911  1.00108.04           C\\nANISOU 1633  CB  LYS A1035     8621  14489  17940   3381    417   1046       C\\nATOM   1634  N   SER A1036      54.169  -8.044  41.282  1.00124.75           N\\nANISOU 1634  N   SER A1036     9333  17441  20626   2756   -279   1212       N\\nATOM   1635  CA  SER A1036      55.429  -7.892  41.994  1.00130.16           C\\nANISOU 1635  CA  SER A1036     9248  18374  21834   2880   -717   1205       C\\nATOM   1636  C   SER A1036      55.191  -7.369  43.411  1.00127.51           C\\nANISOU 1636  C   SER A1036     9199  17961  21290   2719  -1470   1465       C\\nATOM   1637  O   SER A1036      54.249  -6.611  43.652  1.00124.62           O\\nANISOU 1637  O   SER A1036     9437  17497  20415   2316  -1507   1585       O\\nATOM   1638  CB  SER A1036      56.351  -6.937  41.243  1.00133.68           C\\nANISOU 1638  CB  SER A1036     8966  19280  22547   2465   -307   1043       C\\nATOM   1639  N   PRO A1037      56.041  -7.758  44.369  1.00132.59           N\\nANISOU 1639  N   PRO A1037     9408  18656  22314   3043  -2094   1531       N\\nATOM   1640  CA  PRO A1037      55.818  -7.332  45.758  1.00131.46           C\\nANISOU 1640  CA  PRO A1037     9590  18465  21895   2895  -2836   1763       C\\nATOM   1641  C   PRO A1037      56.251  -5.907  46.050  1.00131.07           C\\nANISOU 1641  C   PRO A1037     9233  18724  21845   2324  -3004   1723       C\\nATOM   1642  O   PRO A1037      55.767  -5.327  47.031  1.00128.15           O\\nANISOU 1642  O   PRO A1037     9314  18300  21079   2075  -3470   1849       O\\nATOM   1643  CB  PRO A1037      56.658  -8.330  46.564  1.00137.89           C\\nANISOU 1643  CB  PRO A1037    10022  19225  23144   3474  -3467   1855       C\\nATOM   1644  CG  PRO A1037      57.788  -8.659  45.647  1.00141.32           C\\nANISOU 1644  CG  PRO A1037     9525  19887  24282   3748  -3098   1581       C\\nATOM   1645  CD  PRO A1037      57.205  -8.654  44.250  1.00138.32           C\\nANISOU 1645  CD  PRO A1037     9352  19476  23728   3597  -2186   1384       C\\nATOM   1646  N   SER A1038      57.142  -5.329  45.249  1.00134.97           N\\nANISOU 1646  N   SER A1038     8987  19535  22758   2087  -2636   1539       N\\nATOM   1647  CA  SER A1038      57.615  -3.977  45.512  1.00138.82           C\\nANISOU 1647  CA  SER A1038     9165  20272  23307   1497  -2818   1510       C\\nATOM   1648  C   SER A1038      56.508  -2.965  45.234  1.00142.03           C\\nANISOU 1648  C   SER A1038    10304  20506  23157    966  -2548   1556       C\\nATOM   1649  O   SER A1038      55.905  -2.966  44.156  1.00142.81           O\\nANISOU 1649  O   SER A1038    10685  20515  23061    864  -1905   1526       O\\nATOM   1650  CB  SER A1038      58.845  -3.669  44.659  1.00137.97           C\\nANISOU 1650  CB  SER A1038     8060  20560  23801   1331  -2429   1322       C\\nATOM   1651  N   LEU A1039      56.235  -2.105  46.219  1.00148.93           N\\nANISOU 1651  N   LEU A1039    11491  21326  23772    647  -3071   1607       N\\nATOM   1652  CA  LEU A1039      55.237  -1.059  46.027  1.00137.41           C\\nANISOU 1652  CA  LEU A1039    10670  19674  21866    176  -2887   1609       C\\nATOM   1653  C   LEU A1039      55.728  -0.005  45.042  1.00134.86           C\\nANISOU 1653  C   LEU A1039     9968  19484  21790   -372  -2464   1547       C\\nATOM   1654  O   LEU A1039      54.942   0.522  44.246  1.00128.51           O\\nANISOU 1654  O   LEU A1039     9617  18504  20707   -648  -2029   1577       O\\nATOM   1655  CB  LEU A1039      54.882  -0.422  47.371  1.00133.76           C\\nANISOU 1655  CB  LEU A1039    10606  19126  21088      8  -3557   1606       C\\nATOM   1656  CG  LEU A1039      53.969   0.807  47.351  1.00123.44           C\\nANISOU 1656  CG  LEU A1039     9880  17606  19417   -461  -3487   1537       C\\nATOM   1657  CD1 LEU A1039      52.634   0.486  46.697  1.00115.73           C\\nANISOU 1657  CD1 LEU A1039     9575  16373  18024   -334  -3002   1586       C\\nATOM   1658  CD2 LEU A1039      53.766   1.349  48.759  1.00121.51           C\\nANISOU 1658  CD2 LEU A1039     9948  17332  18887   -575  -4163   1451       C\\nATOM   1659  N   ASN A1040      57.027   0.309  45.078  1.00140.78           N\\nANISOU 1659  N   ASN A1040     9881  20545  23065   -557  -2602   1481       N\\nATOM   1660  CA  ASN A1040      57.584   1.273  44.135  1.00137.59           C\\nANISOU 1660  CA  ASN A1040     9069  20297  22910  -1145  -2171   1458       C\\nATOM   1661  C   ASN A1040      57.424   0.803  42.695  1.00142.78           C\\nANISOU 1661  C   ASN A1040     9696  21027  23528  -1086  -1335   1468       C\\nATOM   1662  O   ASN A1040      57.214   1.623  41.793  1.00129.49           O\\nANISOU 1662  O   ASN A1040     8176  19309  21715  -1595   -895   1536       O\\nATOM   1663  CB  ASN A1040      59.058   1.528  44.452  1.00137.97           C\\nANISOU 1663  CB  ASN A1040     8117  20728  23578  -1326  -2453   1368       C\\nATOM   1664  N   ALA A1041      57.513  -0.508  42.459  1.00141.43           N\\nANISOU 1664  N   ALA A1041     9359  20933  23447   -478  -1132   1401       N\\nATOM   1665  CA  ALA A1041      57.326  -1.032  41.111  1.00146.42           C\\nANISOU 1665  CA  ALA A1041    10009  21635  23988   -388   -344   1347       C\\nATOM   1666  C   ALA A1041      55.865  -0.980  40.683  1.00137.93           C\\nANISOU 1666  C   ALA A1041     9919  20195  22294   -425   -117   1454       C\\nATOM   1667  O   ALA A1041      55.576  -0.783  39.497  1.00137.36           O\\nANISOU 1667  O   ALA A1041    10016  20159  22015   -671    490   1467       O\\nATOM   1668  CB  ALA A1041      57.852  -2.465  41.023  1.00155.04           C\\nANISOU 1668  CB  ALA A1041    10644  22857  25406    310   -239   1186       C\\nATOM   1669  N   ALA A1042      54.935  -1.157  41.626  1.00140.82           N\\nANISOU 1669  N   ALA A1042    10925  20238  22341   -200   -595   1527       N\\nATOM   1670  CA  ALA A1042      53.519  -1.060  41.288  1.00132.90           C\\nANISOU 1670  CA  ALA A1042    10790  18913  20795   -244   -420   1604       C\\nATOM   1671  C   ALA A1042      53.142   0.352  40.863  1.00133.14           C\\nANISOU 1671  C   ALA A1042    11109  18838  20640   -869   -326   1693       C\\nATOM   1672  O   ALA A1042      52.205   0.531  40.075  1.00130.01           O\\nANISOU 1672  O   ALA A1042    11253  18260  19885   -986      1   1755       O\\nATOM   1673  CB  ALA A1042      52.662  -1.505  42.472  1.00126.18           C\\nANISOU 1673  CB  ALA A1042    10481  17801  19659     81   -937   1646       C\\nATOM   1674  N   LYS A1043      53.853   1.361  41.370  1.00137.98           N\\nANISOU 1674  N   LYS A1043    11384  19531  21510  -1275   -652   1703       N\\nATOM   1675  CA  LYS A1043      53.613   2.736  40.950  1.00131.35           C\\nANISOU 1675  CA  LYS A1043    10799  18530  20579  -1894   -598   1802       C\\nATOM   1676  C   LYS A1043      54.204   3.022  39.577  1.00133.43           C\\nANISOU 1676  C   LYS A1043    10730  19015  20952  -2291     34   1891       C\\nATOM   1677  O   LYS A1043      53.705   3.899  38.864  1.00133.13           O\\nANISOU 1677  O   LYS A1043    11108  18782  20694  -2733    227   2044       O\\nATOM   1678  CB  LYS A1043      54.192   3.713  41.976  1.00128.92           C\\nANISOU 1678  CB  LYS A1043    10263  18193  20526  -2230  -1186   1758       C\\nATOM   1679  CG  LYS A1043      53.569   3.618  43.359  1.00124.36           C\\nANISOU 1679  CG  LYS A1043    10090  17422  19739  -1936  -1811   1654       C\\nATOM   1680  CD  LYS A1043      54.054   4.744  44.258  1.00124.45           C\\nANISOU 1680  CD  LYS A1043     9973  17371  19941  -2345  -2374   1565       C\\nATOM   1681  CE  LYS A1043      53.301   4.761  45.577  1.00122.13           C\\nANISOU 1681  CE  LYS A1043    10189  16897  19319  -2105  -2935   1426       C\\nATOM   1682  NZ  LYS A1043      53.698   5.919  46.425  1.00124.65           N\\nANISOU 1682  NZ  LYS A1043    10461  17121  19779  -2520  -3485   1275       N\\nATOM   1683  N   SER A1044      55.263   2.305  39.194  1.00130.51           N\\nANISOU 1683  N   SER A1044     9619  19057  20914  -2142    357   1795       N\\nATOM   1684  CA  SER A1044      55.858   2.511  37.879  1.00137.15           C\\nANISOU 1684  CA  SER A1044    10108  20197  21806  -2533   1041   1845       C\\nATOM   1685  C   SER A1044      54.904   2.086  36.770  1.00136.57           C\\nANISOU 1685  C   SER A1044    10643  20016  21232  -2427   1563   1899       C\\nATOM   1686  O   SER A1044      54.789   2.771  35.747  1.00141.22           O\\nANISOU 1686  O   SER A1044    11441  20628  21589  -2937   1967   2067       O\\nATOM   1687  CB  SER A1044      57.179   1.749  37.775  1.00143.25           C\\nANISOU 1687  CB  SER A1044     9888  21468  23072  -2311   1285   1648       C\\nATOM   1688  N   GLU A1045      54.211   0.960  36.954  1.00136.81           N\\nANISOU 1688  N   GLU A1045    10988  19917  21076  -1800   1534   1777       N\\nATOM   1689  CA  GLU A1045      53.243   0.521  35.955  1.00129.18           C\\nANISOU 1689  CA  GLU A1045    10619  18832  19631  -1695   1960   1797       C\\nATOM   1690  C   GLU A1045      52.010   1.415  35.939  1.00128.34           C\\nANISOU 1690  C   GLU A1045    11333  18313  19118  -1974   1718   2002       C\\nATOM   1691  O   GLU A1045      51.383   1.582  34.887  1.00126.75           O\\nANISOU 1691  O   GLU A1045    11575  18053  18531  -2171   2069   2109       O\\nATOM   1692  CB  GLU A1045      52.847  -0.934  36.210  1.00121.20           C\\nANISOU 1692  CB  GLU A1045     9714  17751  18586   -982   1950   1604       C\\nATOM   1693  N   LEU A1046      51.650   1.998  37.088  1.00131.91           N\\nANISOU 1693  N   LEU A1046    11988  18485  19645  -1980   1106   2037       N\\nATOM   1694  CA  LEU A1046      50.490   2.885  37.146  1.00126.43           C\\nANISOU 1694  CA  LEU A1046    12012  17383  18643  -2189    846   2169       C\\nATOM   1695  C   LEU A1046      50.730   4.156  36.342  1.00134.52           C\\nANISOU 1695  C   LEU A1046    13116  18345  19652  -2860    993   2395       C\\nATOM   1696  O   LEU A1046      49.873   4.579  35.558  1.00138.35           O\\nANISOU 1696  O   LEU A1046    14165  18604  19797  -3036   1114   2555       O\\nATOM   1697  CB  LEU A1046      50.156   3.227  38.600  1.00114.87           C\\nANISOU 1697  CB  LEU A1046    10689  15684  17273  -2043    195   2081       C\\nATOM   1698  CG  LEU A1046      49.189   4.395  38.827  1.00103.62           C\\nANISOU 1698  CG  LEU A1046     9857  13838  15674  -2297   -138   2146       C\\nATOM   1699  CD1 LEU A1046      47.828   4.107  38.217  1.00 96.31           C\\nANISOU 1699  CD1 LEU A1046     9556  12698  14341  -2097     22   2183       C\\nATOM   1700  CD2 LEU A1046      49.056   4.722  40.308  1.00 99.47           C\\nANISOU 1700  CD2 LEU A1046     9379  13170  15245  -2171   -734   1980       C\\nATOM   1701  N   ASP A1047      51.893   4.784  36.529  1.00127.49           N\\nANISOU 1701  N   ASP A1047    11667  17635  19137  -3262    951   2433       N\\nATOM   1702  CA  ASP A1047      52.188   6.012  35.801  1.00131.96           C\\nANISOU 1702  CA  ASP A1047    12311  18112  19714  -3978   1078   2692       C\\nATOM   1703  C   ASP A1047      52.444   5.742  34.324  1.00130.92           C\\nANISOU 1703  C   ASP A1047    12130  18291  19323  -4228   1792   2837       C\\nATOM   1704  O   ASP A1047      52.172   6.607  33.483  1.00133.98           O\\nANISOU 1704  O   ASP A1047    12921  18510  19475  -4745   1927   3128       O\\nATOM   1705  CB  ASP A1047      53.382   6.723  36.435  1.00141.47           C\\nANISOU 1705  CB  ASP A1047    12895  19442  21416  -4390    835   2678       C\\nATOM   1706  CG  ASP A1047      53.050   7.320  37.791  1.00139.91           C\\nANISOU 1706  CG  ASP A1047    12900  18874  21385  -4305     95   2555       C\\nATOM   1707  OD1 ASP A1047      51.910   7.125  38.263  1.00133.93           O\\nANISOU 1707  OD1 ASP A1047    12719  17809  20359  -3898   -178   2466       O\\nATOM   1708  OD2 ASP A1047      53.925   7.988  38.382  1.00142.42           O\\nANISOU 1708  OD2 ASP A1047    12791  19231  22093  -4666   -203   2522       O\\nATOM   1709  N   LYS A1048      52.958   4.557  33.986  1.00136.15           N\\nANISOU 1709  N   LYS A1048    12332  19393  20008  -3866   2239   2634       N\\nATOM   1710  CA  LYS A1048      53.156   4.211  32.584  1.00137.23           C\\nANISOU 1710  CA  LYS A1048    12447  19868  19828  -4059   2961   2691       C\\nATOM   1711  C   LYS A1048      51.836   3.990  31.855  1.00136.24           C\\nANISOU 1711  C   LYS A1048    13159  19483  19123  -3907   3045   2785       C\\nATOM   1712  O   LYS A1048      51.813   4.012  30.619  1.00135.03           O\\nANISOU 1712  O   LYS A1048    13198  19529  18579  -4209   3556   2913       O\\nATOM   1713  CB  LYS A1048      54.036   2.964  32.467  1.00137.25           C\\nANISOU 1713  CB  LYS A1048    11720  20374  20055  -3634   3395   2361       C\\nATOM   1714  N   ALA A1049      50.743   3.782  32.587  1.00134.09           N\\nANISOU 1714  N   ALA A1049    13374  18806  18767  -3471   2557   2719       N\\nATOM   1715  CA  ALA A1049      49.423   3.607  31.993  1.00136.97           C\\nANISOU 1715  CA  ALA A1049    14488  18911  18642  -3319   2551   2790       C\\nATOM   1716  C   ALA A1049      48.555   4.853  32.093  1.00139.86           C\\nANISOU 1716  C   ALA A1049    15461  18785  18895  -3629   2088   3059       C\\nATOM   1717  O   ALA A1049      47.775   5.130  31.178  1.00144.34           O\\nANISOU 1717  O   ALA A1049    16587  19202  19054  -3792   2166   3254       O\\nATOM   1718  CB  ALA A1049      48.697   2.429  32.649  1.00134.83           C\\nANISOU 1718  CB  ALA A1049    14339  18543  18349  -2619   2376   2514       C\\nATOM   1719  N   ILE A1050      48.667   5.615  33.186  1.00147.00           N\\nANISOU 1719  N   ILE A1050    16279  19419  20157  -3696   1573   3052       N\\nATOM   1720  CA  ILE A1050      47.884   6.843  33.320  1.00137.76           C\\nANISOU 1720  CA  ILE A1050    15661  17727  18955  -3954   1109   3250       C\\nATOM   1721  C   ILE A1050      48.527   8.029  32.621  1.00135.31           C\\nANISOU 1721  C   ILE A1050    15376  17334  18700  -4696   1193   3602       C\\nATOM   1722  O   ILE A1050      47.861   9.054  32.425  1.00132.09           O\\nANISOU 1722  O   ILE A1050    15513  16449  18227  -4950    855   3834       O\\nATOM   1723  CB  ILE A1050      47.649   7.192  34.802  1.00112.75           C\\nANISOU 1723  CB  ILE A1050    12459  14272  16111  -3710    512   3036       C\\nATOM   1724  N   GLY A1051      49.800   7.923  32.236  1.00128.26           N\\nANISOU 1724  N   GLY A1051    13902  16884  17947  -5058   1630   3652       N\\nATOM   1725  CA  GLY A1051      50.479   8.964  31.501  1.00126.01           C\\nANISOU 1725  CA  GLY A1051    13606  16592  17681  -5844   1802   4017       C\\nATOM   1726  C   GLY A1051      51.114  10.046  32.350  1.00125.68           C\\nANISOU 1726  C   GLY A1051    13328  16279  18144  -6255   1362   4067       C\\nATOM   1727  O   GLY A1051      52.053  10.703  31.888  1.00131.62           O\\nANISOU 1727  O   GLY A1051    13814  17166  19028  -6906   1590   4283       O\\nATOM   1728  N   ARG A1052      50.638  10.250  33.572  1.00125.39           N\\nANISOU 1728  N   ARG A1052    13398  15875  18368  -5892    754   3830       N\\nATOM   1729  CA  ARG A1052      51.137  11.295  34.452  1.00130.48           C\\nANISOU 1729  CA  ARG A1052    13895  16207  19473  -6249    261   3810       C\\nATOM   1730  C   ARG A1052      51.879  10.681  35.633  1.00133.64           C\\nANISOU 1730  C   ARG A1052    13610  16936  20230  -5922     98   3432       C\\nATOM   1731  O   ARG A1052      51.880   9.465  35.836  1.00139.15           O\\nANISOU 1731  O   ARG A1052    14025  18014  20831  -5363    306   3204       O\\nATOM   1732  CB  ARG A1052      49.986  12.174  34.954  1.00127.22           C\\nANISOU 1732  CB  ARG A1052    14202  15072  19066  -6123   -369   3798       C\\nATOM   1733  CG  ARG A1052      49.063  11.466  35.933  1.00118.27           C\\nANISOU 1733  CG  ARG A1052    13210  13879  17849  -5343   -664   3404       C\\nATOM   1734  CD  ARG A1052      47.922  12.363  36.372  1.00115.96           C\\nANISOU 1734  CD  ARG A1052    13565  12916  17579  -5212  -1224   3339       C\\nATOM   1735  NE  ARG A1052      47.116  11.751  37.424  1.00114.03           N\\nANISOU 1735  NE  ARG A1052    13390  12676  17262  -4541  -1477   2931       N\\nATOM   1736  CZ  ARG A1052      47.303  11.960  38.723  1.00115.93           C\\nANISOU 1736  CZ  ARG A1052    13460  12852  17737  -4403  -1881   2594       C\\nATOM   1737  NH1 ARG A1052      48.271  12.768  39.132  1.00119.81           N\\nANISOU 1737  NH1 ARG A1052    13686  13244  18594  -4875  -2117   2592       N\\nATOM   1738  NH2 ARG A1052      46.523  11.364  39.613  1.00113.10           N\\nANISOU 1738  NH2 ARG A1052    13205  12544  17222  -3834  -2048   2259       N\\nATOM   1739  N   ASN A1053      52.517  11.551  36.419  1.00125.16           N\\nANISOU 1739  N   ASN A1053    12297  15678  19580  -6291   -324   3375       N\\nATOM   1740  CA  ASN A1053      53.118  11.156  37.692  1.00123.03           C\\nANISOU 1740  CA  ASN A1053    11481  15629  19636  -6002   -663   3022       C\\nATOM   1741  C   ASN A1053      52.002  11.117  38.731  1.00122.77           C\\nANISOU 1741  C   ASN A1053    11968  15217  19462  -5447  -1194   2750       C\\nATOM   1742  O   ASN A1053      51.786  12.056  39.502  1.00122.02           O\\nANISOU 1742  O   ASN A1053    12131  14690  19541  -5602  -1734   2626       O\\nATOM   1743  CB  ASN A1053      54.234  12.115  38.089  1.00126.67           C\\nANISOU 1743  CB  ASN A1053    11485  16063  20583  -6663   -923   3047       C\\nATOM   1744  N   THR A1054      51.272   9.995  38.739  1.00124.33           N\\nANISOU 1744  N   THR A1054    12319  15587  19333  -4804  -1013   2632       N\\nATOM   1745  CA  THR A1054      50.060   9.901  39.547  1.00119.55           C\\nANISOU 1745  CA  THR A1054    12244  14668  18513  -4306  -1394   2406       C\\nATOM   1746  C   THR A1054      50.366   9.947  41.037  1.00119.71           C\\nANISOU 1746  C   THR A1054    12048  14716  18720  -4133  -1918   2083       C\\nATOM   1747  O   THR A1054      49.504  10.334  41.835  1.00120.96           O\\nANISOU 1747  O   THR A1054    12645  14548  18764  -3922  -2315   1863       O\\nATOM   1748  CB  THR A1054      49.295   8.620  39.212  1.00115.03           C\\nANISOU 1748  CB  THR A1054    11827  14310  17568  -3728  -1059   2370       C\\nATOM   1749  N   ASN A1055      51.577   9.556  41.433  1.00118.97           N\\nANISOU 1749  N   ASN A1055    11271  15030  18901  -4213  -1934   2029       N\\nATOM   1750  CA  ASN A1055      52.004   9.557  42.830  1.00116.22           C\\nANISOU 1750  CA  ASN A1055    10681  14771  18707  -4084  -2473   1748       C\\nATOM   1751  C   ASN A1055      51.115   8.687  43.711  1.00119.38           C\\nANISOU 1751  C   ASN A1055    11395  15214  18750  -3437  -2650   1539       C\\nATOM   1752  O   ASN A1055      51.131   8.822  44.935  1.00121.96           O\\nANISOU 1752  O   ASN A1055    11754  15533  19052  -3324  -3143   1293       O\\nATOM   1753  CB  ASN A1055      52.071  10.984  43.391  1.00109.11           C\\nANISOU 1753  CB  ASN A1055     9992  13444  18023  -4552  -2980   1627       C\\nATOM   1754  N   GLY A1056      50.340   7.783  43.111  1.00115.78           N\\nANISOU 1754  N   GLY A1056    11183  14819  17987  -3045  -2253   1632       N\\nATOM   1755  CA  GLY A1056      49.518   6.838  43.832  1.00115.99           C\\nANISOU 1755  CA  GLY A1056    11480  14915  17677  -2485  -2341   1489       C\\nATOM   1756  C   GLY A1056      48.027   7.076  43.671  1.00112.88           C\\nANISOU 1756  C   GLY A1056    11762  14182  16944  -2317  -2293   1431       C\\nATOM   1757  O   GLY A1056      47.247   6.120  43.742  1.00109.86           O\\nANISOU 1757  O   GLY A1056    11592  13885  16264  -1902  -2132   1408       O\\nATOM   1758  N   VAL A1057      47.618   8.323  43.454  1.00113.85           N\\nANISOU 1758  N   VAL A1057    12208  13906  17145  -2632  -2448   1405       N\\nATOM   1759  CA  VAL A1057      46.211   8.699  43.361  1.00103.36           C\\nANISOU 1759  CA  VAL A1057    11467  12226  15579  -2456  -2483   1304       C\\nATOM   1760  C   VAL A1057      45.881   9.003  41.907  1.00105.21           C\\nANISOU 1760  C   VAL A1057    11904  12256  15814  -2653  -2149   1598       C\\nATOM   1761  O   VAL A1057      46.708   9.560  41.176  1.00111.08           O\\nANISOU 1761  O   VAL A1057    12459  12960  16785  -3103  -2041   1831       O\\nATOM   1762  CB  VAL A1057      45.900   9.912  44.260  1.00 96.42           C\\nANISOU 1762  CB  VAL A1057    10853  10979  14804  -2591  -2980   1005       C\\nATOM   1763  N   ILE A1058      44.667   8.639  41.488  1.00104.59           N\\nANISOU 1763  N   ILE A1058    12209  12071  15459  -2350  -1994   1597       N\\nATOM   1764  CA  ILE A1058      44.203   8.889  40.131  1.00100.91           C\\nANISOU 1764  CA  ILE A1058    12012  11414  14916  -2498  -1744   1872       C\\nATOM   1765  C   ILE A1058      42.794   9.466  40.170  1.00 98.60           C\\nANISOU 1765  C   ILE A1058    12224  10714  14524  -2295  -1978   1737       C\\nATOM   1766  O   ILE A1058      42.091   9.405  41.182  1.00 92.24           O\\nANISOU 1766  O   ILE A1058    11523   9875  13648  -1976  -2199   1403       O\\nATOM   1767  CB  ILE A1058      44.229   7.619  39.253  1.00 94.08           C\\nANISOU 1767  CB  ILE A1058    11024  10914  13808  -2321  -1243   2041       C\\nATOM   1768  CG1 ILE A1058      43.313   6.543  39.831  1.00 82.54           C\\nANISOU 1768  CG1 ILE A1058     9675   9599  12089  -1804  -1208   1830       C\\nATOM   1769  CG2 ILE A1058      45.650   7.101  39.083  1.00 91.55           C\\nANISOU 1769  CG2 ILE A1058    10149  10986  13649  -2498   -980   2147       C\\nATOM   1770  CD1 ILE A1058      43.175   5.325  38.950  1.00 80.94           C\\nANISOU 1770  CD1 ILE A1058     9440   9653  11661  -1618   -764   1951       C\\nATOM   1771  N   THR A1059      42.391  10.038  39.038  1.00100.27           N\\nANISOU 1771  N   THR A1059    12740  10636  14723  -2488  -1928   2000       N\\nATOM   1772  CA  THR A1059      41.046  10.571  38.887  1.00100.12           C\\nANISOU 1772  CA  THR A1059    13164  10218  14658  -2267  -2166   1907       C\\nATOM   1773  C   THR A1059      40.043   9.431  38.714  1.00 93.93           C\\nANISOU 1773  C   THR A1059    12445   9697  13549  -1832  -1928   1816       C\\nATOM   1774  O   THR A1059      40.390   8.322  38.302  1.00 93.12           O\\nANISOU 1774  O   THR A1059    12152   9988  13239  -1781  -1546   1935       O\\nATOM   1775  CB  THR A1059      40.982  11.515  37.681  1.00103.74           C\\nANISOU 1775  CB  THR A1059    13952  10269  15193  -2630  -2248   2286       C\\nATOM   1776  OG1 THR A1059      42.175  12.306  37.630  1.00105.14           O\\nANISOU 1776  OG1 THR A1059    13991  10320  15636  -3159  -2321   2476       O\\nATOM   1777  CG2 THR A1059      39.778  12.440  37.771  1.00108.32           C\\nANISOU 1777  CG2 THR A1059    14955  10292  15912  -2422  -2687   2144       C\\nATOM   1778  N   LYS A1060      38.780   9.709  39.047  1.00 98.18           N\\nANISOU 1778  N   LYS A1060    13229  10001  14072  -1515  -2161   1570       N\\nATOM   1779  CA  LYS A1060      37.721   8.768  38.697  1.00 98.24           C\\nANISOU 1779  CA  LYS A1060    13319  10201  13806  -1182  -1964   1522       C\\nATOM   1780  C   LYS A1060      37.594   8.635  37.188  1.00 99.60           C\\nANISOU 1780  C   LYS A1060    13688  10335  13819  -1346  -1790   1903       C\\nATOM   1781  O   LYS A1060      37.139   7.599  36.688  1.00 95.67           O\\nANISOU 1781  O   LYS A1060    13192  10106  13053  -1183  -1519   1935       O\\nATOM   1782  CB  LYS A1060      36.389   9.207  39.307  1.00 93.38           C\\nANISOU 1782  CB  LYS A1060    12863   9359  13257   -838  -2249   1162       C\\nATOM   1783  N   ASP A1061      37.997   9.671  36.449  1.00103.09           N\\nANISOU 1783  N   ASP A1061    14329  10441  14400  -1703  -1952   2200       N\\nATOM   1784  CA  ASP A1061      38.006   9.603  34.993  1.00101.97           C\\nANISOU 1784  CA  ASP A1061    14414  10301  14028  -1942  -1780   2607       C\\nATOM   1785  C   ASP A1061      39.176   8.768  34.485  1.00100.34           C\\nANISOU 1785  C   ASP A1061    13939  10555  13629  -2196  -1275   2797       C\\nATOM   1786  O   ASP A1061      39.012   7.961  33.563  1.00 99.43           O\\nANISOU 1786  O   ASP A1061    13894  10699  13185  -2180   -958   2926       O\\nATOM   1787  CB  ASP A1061      38.055  11.015  34.413  1.00102.76           C\\nANISOU 1787  CB  ASP A1061    14862   9863  14320  -2281  -2142   2907       C\\nATOM   1788  CG  ASP A1061      37.962  11.029  32.903  1.00102.52           C\\nANISOU 1788  CG  ASP A1061    15156   9822  13974  -2555  -2021   3367       C\\nATOM   1789  OD1 ASP A1061      36.881  10.700  32.371  1.00 98.49           O\\nANISOU 1789  OD1 ASP A1061    14872   9291  13258  -2289  -2114   3362       O\\nATOM   1790  OD2 ASP A1061      38.970  11.374  32.248  1.00105.90           O\\nANISOU 1790  OD2 ASP A1061    15607  10290  14339  -3064  -1832   3728       O\\nATOM   1791  N   GLU A1062      40.362   8.948  35.075  1.00102.50           N\\nANISOU 1791  N   GLU A1062    13880  10945  14119  -2420  -1205   2776       N\\nATOM   1792  CA  GLU A1062      41.504   8.118  34.707  1.00 96.62           C\\nANISOU 1792  CA  GLU A1062    12770  10671  13271  -2592   -725   2880       C\\nATOM   1793  C   GLU A1062      41.237   6.651  35.014  1.00 88.82           C\\nANISOU 1793  C   GLU A1062    11588  10061  12098  -2156   -455   2641       C\\nATOM   1794  O   GLU A1062      41.657   5.764  34.262  1.00 83.40           O\\nANISOU 1794  O   GLU A1062    10776   9705  11208  -2174    -28   2718       O\\nATOM   1795  CB  GLU A1062      42.761   8.595  35.435  1.00 87.02           C\\nANISOU 1795  CB  GLU A1062    11163   9509  12392  -2870   -785   2852       C\\nATOM   1796  CG  GLU A1062      43.240   9.972  35.025  1.00 95.42           C\\nANISOU 1796  CG  GLU A1062    12385  10212  13658  -3416   -988   3136       C\\nATOM   1797  CD  GLU A1062      44.494  10.395  35.768  1.00 99.73           C\\nANISOU 1797  CD  GLU A1062    12491  10838  14563  -3723  -1061   3077       C\\nATOM   1798  OE1 GLU A1062      44.628  10.042  36.959  1.00 95.17           O\\nANISOU 1798  OE1 GLU A1062    11645  10382  14135  -3431  -1231   2743       O\\nATOM   1799  OE2 GLU A1062      45.347  11.075  35.159  1.00104.48           O\\nANISOU 1799  OE2 GLU A1062    13018  11399  15279  -4288   -958   3375       O\\nATOM   1800  N   ALA A1063      40.542   6.377  36.121  1.00 85.45           N\\nANISOU 1800  N   ALA A1063    11151   9581  11735  -1777   -689   2337       N\\nATOM   1801  CA  ALA A1063      40.186   5.003  36.456  1.00 86.64           C\\nANISOU 1801  CA  ALA A1063    11186  10021  11712  -1400   -477   2151       C\\nATOM   1802  C   ALA A1063      39.112   4.459  35.526  1.00 88.99           C\\nANISOU 1802  C   ALA A1063    11790  10309  11715  -1259   -345   2190       C\\nATOM   1803  O   ALA A1063      39.030   3.242  35.325  1.00 88.77           O\\nANISOU 1803  O   ALA A1063    11692  10524  11512  -1068    -60   2120       O\\nATOM   1804  CB  ALA A1063      39.719   4.914  37.909  1.00 84.46           C\\nANISOU 1804  CB  ALA A1063    10850   9716  11524  -1112   -751   1850       C\\nATOM   1805  N   GLU A1064      38.283   5.337  34.957  1.00 91.39           N\\nANISOU 1805  N   GLU A1064    12438  10307  11980  -1346   -590   2294       N\\nATOM   1806  CA  GLU A1064      37.273   4.882  34.009  1.00 91.30           C\\nANISOU 1806  CA  GLU A1064    12709  10296  11686  -1243   -529   2345       C\\nATOM   1807  C   GLU A1064      37.898   4.478  32.678  1.00 95.38           C\\nANISOU 1807  C   GLU A1064    13297  11022  11922  -1504   -156   2596       C\\nATOM   1808  O   GLU A1064      37.402   3.560  32.016  1.00 93.85           O\\nANISOU 1808  O   GLU A1064    13219  10996  11445  -1384     47   2550       O\\nATOM   1809  CB  GLU A1064      36.216   5.969  33.805  1.00 88.36           C\\nANISOU 1809  CB  GLU A1064    12660   9522  11391  -1222   -972   2387       C\\nATOM   1810  CG  GLU A1064      34.995   5.506  33.022  1.00 85.95           C\\nANISOU 1810  CG  GLU A1064    12598   9220  10839  -1054  -1023   2379       C\\nATOM   1811  CD  GLU A1064      33.877   6.532  33.012  1.00 92.64           C\\nANISOU 1811  CD  GLU A1064    13676   9668  11857   -926  -1527   2353       C\\nATOM   1812  OE1 GLU A1064      32.798   6.224  32.460  1.00 92.14           O\\nANISOU 1812  OE1 GLU A1064    13758   9602  11649   -763  -1648   2318       O\\nATOM   1813  OE2 GLU A1064      34.072   7.641  33.555  1.00 96.90           O\\nANISOU 1813  OE2 GLU A1064    14234   9879  12704   -975  -1826   2343       O\\nATOM   1814  N   LYS A1065      38.982   5.144  32.270  1.00 96.04           N\\nANISOU 1814  N   LYS A1065    13309  11119  12064  -1890    -43   2837       N\\nATOM   1815  CA  LYS A1065      39.706   4.695  31.086  1.00 95.76           C\\nANISOU 1815  CA  LYS A1065    13269  11382  11732  -2158    412   3024       C\\nATOM   1816  C   LYS A1065      40.338   3.328  31.321  1.00 92.50           C\\nANISOU 1816  C   LYS A1065    12480  11360  11306  -1927    838   2784       C\\nATOM   1817  O   LYS A1065      40.296   2.460  30.442  1.00 93.15           O\\nANISOU 1817  O   LYS A1065    12640  11673  11077  -1892   1185   2745       O\\nATOM   1818  CB  LYS A1065      40.767   5.724  30.695  1.00 97.00           C\\nANISOU 1818  CB  LYS A1065    13372  11502  11982  -2673    474   3332       C\\nATOM   1819  N   LEU A1066      40.918   3.114  32.505  1.00 86.38           N\\nANISOU 1819  N   LEU A1066    11317  10638  10865  -1755    781   2609       N\\nATOM   1820  CA  LEU A1066      41.504   1.814  32.815  1.00 89.95           C\\nANISOU 1820  CA  LEU A1066    11422  11389  11367  -1482   1095   2400       C\\nATOM   1821  C   LEU A1066      40.439   0.729  32.871  1.00 88.33           C\\nANISOU 1821  C   LEU A1066    11426  11159  10977  -1113   1097   2208       C\\nATOM   1822  O   LEU A1066      40.672  -0.401  32.428  1.00 91.55           O\\nANISOU 1822  O   LEU A1066    11755  11759  11269   -957   1433   2085       O\\nATOM   1823  CB  LEU A1066      42.265   1.875  34.139  1.00 96.43           C\\nANISOU 1823  CB  LEU A1066    11833  12240  12567  -1373    917   2292       C\\nATOM   1824  CG  LEU A1066      43.442   2.845  34.220  1.00110.23           C\\nANISOU 1824  CG  LEU A1066    13274  14038  14572  -1754    899   2439       C\\nATOM   1825  CD1 LEU A1066      44.173   2.679  35.543  1.00109.37           C\\nANISOU 1825  CD1 LEU A1066    12741  14009  14807  -1592    693   2287       C\\nATOM   1826  CD2 LEU A1066      44.392   2.653  33.043  1.00117.21           C\\nANISOU 1826  CD2 LEU A1066    13951  15231  15353  -2035   1407   2560       C\\nATOM   1827  N   PHE A1067      39.266   1.055  33.417  1.00 88.20           N\\nANISOU 1827  N   PHE A1067    11656  10901  10956   -977    731   2152       N\\nATOM   1828  CA  PHE A1067      38.202   0.064  33.527  1.00 86.10           C\\nANISOU 1828  CA  PHE A1067    11554  10620  10539   -687    725   1975       C\\nATOM   1829  C   PHE A1067      37.743  -0.409  32.155  1.00 85.87           C\\nANISOU 1829  C   PHE A1067    11803  10657  10168   -762    941   2008       C\\nATOM   1830  O   PHE A1067      37.513  -1.606  31.949  1.00 84.89           O\\nANISOU 1830  O   PHE A1067    11703  10627   9925   -580   1146   1847       O\\nATOM   1831  CB  PHE A1067      37.028   0.640  34.316  1.00 89.23           C\\nANISOU 1831  CB  PHE A1067    12101  10796  11006   -569    323   1888       C\\nATOM   1832  CG  PHE A1067      35.849  -0.282  34.400  1.00 87.05           C\\nANISOU 1832  CG  PHE A1067    11964  10525  10586   -347    317   1719       C\\nATOM   1833  CD1 PHE A1067      35.865  -1.372  35.252  1.00 83.17           C\\nANISOU 1833  CD1 PHE A1067    11332  10130  10137   -136    418   1574       C\\nATOM   1834  CD2 PHE A1067      34.724  -0.058  33.627  1.00 86.11           C\\nANISOU 1834  CD2 PHE A1067    12115  10304  10299   -373    179   1726       C\\nATOM   1835  CE1 PHE A1067      34.781  -2.221  35.329  1.00 78.20           C\\nANISOU 1835  CE1 PHE A1067    10832   9493   9387     -3    424   1440       C\\nATOM   1836  CE2 PHE A1067      33.638  -0.903  33.702  1.00 81.95           C\\nANISOU 1836  CE2 PHE A1067    11664   9800   9671   -214    168   1558       C\\nATOM   1837  CZ  PHE A1067      33.666  -1.985  34.553  1.00 78.15           C\\nANISOU 1837  CZ  PHE A1067    11043   9414   9235    -52    312   1415       C\\nATOM   1838  N   ASN A1068      37.604   0.516  31.201  1.00 90.24           N\\nANISOU 1838  N   ASN A1068    12604  11140  10543  -1046    869   2222       N\\nATOM   1839  CA  ASN A1068      37.203   0.127  29.853  1.00 83.46           C\\nANISOU 1839  CA  ASN A1068    12053  10378   9278  -1159   1045   2269       C\\nATOM   1840  C   ASN A1068      38.222  -0.816  29.228  1.00 82.78           C\\nANISOU 1840  C   ASN A1068    11803  10602   9046  -1191   1575   2173       C\\nATOM   1841  O   ASN A1068      37.856  -1.728  28.479  1.00 84.94           O\\nANISOU 1841  O   ASN A1068    12255  10985   9033  -1118   1777   2024       O\\nATOM   1842  CB  ASN A1068      37.008   1.367  28.984  1.00 87.76           C\\nANISOU 1842  CB  ASN A1068    12920  10786   9638  -1498    837   2587       C\\nATOM   1843  CG  ASN A1068      35.631   1.982  29.145  1.00 95.27           C\\nANISOU 1843  CG  ASN A1068    14135  11430  10632  -1379    315   2609       C\\nATOM   1844  OD1 ASN A1068      34.845   2.027  28.198  1.00102.99           O\\nANISOU 1844  OD1 ASN A1068    15454  12372  11305  -1446    169   2702       O\\nATOM   1845  ND2 ASN A1068      35.327   2.448  30.350  1.00 94.72           N\\nANISOU 1845  ND2 ASN A1068    13890  11159  10939  -1190     20   2495       N\\nATOM   1846  N   GLN A1069      39.507  -0.618  29.532  1.00 82.90           N\\nANISOU 1846  N   GLN A1069    11450  10766   9281  -1289   1799   2217       N\\nATOM   1847  CA  GLN A1069      40.533  -1.532  29.041  1.00 93.96           C\\nANISOU 1847  CA  GLN A1069    12588  12479  10633  -1250   2317   2059       C\\nATOM   1848  C   GLN A1069      40.355  -2.926  29.631  1.00 96.67           C\\nANISOU 1848  C   GLN A1069    12801  12800  11129   -811   2383   1749       C\\nATOM   1849  O   GLN A1069      40.472  -3.931  28.918  1.00 96.30           O\\nANISOU 1849  O   GLN A1069    12800  12887  10901   -697   2721   1539       O\\nATOM   1850  CB  GLN A1069      41.922  -0.978  29.364  1.00104.31           C\\nANISOU 1850  CB  GLN A1069    13439  13961  12234  -1436   2488   2158       C\\nATOM   1851  CG  GLN A1069      42.191   0.399  28.770  1.00112.15           C\\nANISOU 1851  CG  GLN A1069    14573  14942  13096  -1947   2442   2503       C\\nATOM   1852  CD  GLN A1069      43.505   1.002  29.237  1.00116.78           C\\nANISOU 1852  CD  GLN A1069    14664  15667  14039  -2175   2548   2595       C\\nATOM   1853  OE1 GLN A1069      44.350   0.314  29.812  1.00124.86           O\\nANISOU 1853  OE1 GLN A1069    15191  16882  15370  -1946   2730   2385       O\\nATOM   1854  NE2 GLN A1069      43.681   2.297  28.993  1.00109.98           N\\nANISOU 1854  NE2 GLN A1069    13937  14684  13167  -2636   2395   2919       N\\nATOM   1855  N   ASP A1070      40.068  -3.007  30.934  1.00 93.20           N\\nANISOU 1855  N   ASP A1070    12231  12176  11004   -577   2056   1715       N\\nATOM   1856  CA  ASP A1070      39.831  -4.304  31.560  1.00 92.78           C\\nANISOU 1856  CA  ASP A1070    12121  12049  11083   -206   2064   1494       C\\nATOM   1857  C   ASP A1070      38.580  -4.968  31.000  1.00 84.10           C\\nANISOU 1857  C   ASP A1070    11427  10832   9697   -148   2030   1376       C\\nATOM   1858  O   ASP A1070      38.532  -6.195  30.858  1.00 74.28           O\\nANISOU 1858  O   ASP A1070    10218   9558   8448     64   2204   1167       O\\nATOM   1859  CB  ASP A1070      39.714  -4.145  33.076  1.00 97.16           C\\nANISOU 1859  CB  ASP A1070    12517  12464  11936    -46   1705   1529       C\\nATOM   1860  CG  ASP A1070      40.993  -3.637  33.711  1.00101.50           C\\nANISOU 1860  CG  ASP A1070    12635  13134  12794    -83   1688   1606       C\\nATOM   1861  OD1 ASP A1070      42.082  -3.940  33.181  1.00105.37           O\\nANISOU 1861  OD1 ASP A1070    12832  13826  13379    -89   2015   1558       O\\nATOM   1862  OD2 ASP A1070      40.905  -2.936  34.743  1.00 98.07           O\\nANISOU 1862  OD2 ASP A1070    12136  12614  12514   -110   1349   1680       O\\nATOM   1863  N   VAL A1071      37.557  -4.174  30.679  1.00 85.78           N\\nANISOU 1863  N   VAL A1071    11939  10950   9704   -328   1771   1495       N\\nATOM   1864  CA  VAL A1071      36.322  -4.733  30.136  1.00 82.23           C\\nANISOU 1864  CA  VAL A1071    11829  10413   9002   -301   1681   1379       C\\nATOM   1865  C   VAL A1071      36.565  -5.310  28.749  1.00 86.97           C\\nANISOU 1865  C   VAL A1071    12623  11169   9251   -401   2023   1266       C\\nATOM   1866  O   VAL A1071      36.169  -6.443  28.455  1.00 91.66           O\\nANISOU 1866  O   VAL A1071    13352  11723   9752   -267   2137   1029       O\\nATOM   1867  CB  VAL A1071      35.214  -3.667  30.113  1.00 77.64           C\\nANISOU 1867  CB  VAL A1071    11459   9702   8338   -435   1276   1525       C\\nATOM   1868  CG1 VAL A1071      34.018  -4.169  29.323  1.00 68.20           C\\nANISOU 1868  CG1 VAL A1071    10579   8473   6862   -455   1173   1415       C\\nATOM   1869  CG2 VAL A1071      34.807  -3.308  31.524  1.00 79.71           C\\nANISOU 1869  CG2 VAL A1071    11544   9829   8913   -289    982   1517       C\\nATOM   1870  N   ASP A1072      37.208  -4.533  27.872  1.00 86.89           N\\nANISOU 1870  N   ASP A1072    12656  11340   9019   -672   2197   1425       N\\nATOM   1871  CA  ASP A1072      37.548  -5.045  26.549  1.00 93.69           C\\nANISOU 1871  CA  ASP A1072    13699  12426   9474   -799   2587   1294       C\\nATOM   1872  C   ASP A1072      38.419  -6.289  26.649  1.00 93.29           C\\nANISOU 1872  C   ASP A1072    13380  12470   9598   -530   3002    969       C\\nATOM   1873  O   ASP A1072      38.186  -7.273  25.940  1.00100.45           O\\nANISOU 1873  O   ASP A1072    14485  13404  10277   -445   3208    683       O\\nATOM   1874  CB  ASP A1072      38.246  -3.964  25.724  1.00101.72           C\\nANISOU 1874  CB  ASP A1072    14764  13660  10224  -1186   2755   1563       C\\nATOM   1875  CG  ASP A1072      37.274  -2.951  25.152  1.00105.64           C\\nANISOU 1875  CG  ASP A1072    15691  14039  10407  -1457   2355   1858       C\\nATOM   1876  OD1 ASP A1072      36.104  -3.321  24.911  1.00105.43           O\\nANISOU 1876  OD1 ASP A1072    15959  13888  10212  -1367   2080   1761       O\\nATOM   1877  OD2 ASP A1072      37.677  -1.787  24.942  1.00108.66           O\\nANISOU 1877  OD2 ASP A1072    16112  14434  10740  -1764   2286   2192       O\\nATOM   1878  N   ALA A1073      39.417  -6.269  27.537  1.00 84.98           N\\nANISOU 1878  N   ALA A1073    11874  11440   8973   -376   3089    988       N\\nATOM   1879  CA  ALA A1073      40.250  -7.451  27.738  1.00 87.42           C\\nANISOU 1879  CA  ALA A1073    11887  11783   9546    -46   3401    685       C\\nATOM   1880  C   ALA A1073      39.418  -8.640  28.199  1.00 88.42           C\\nANISOU 1880  C   ALA A1073    12207  11603   9787    254   3220    480       C\\nATOM   1881  O   ALA A1073      39.645  -9.774  27.760  1.00 91.45           O\\nANISOU 1881  O   ALA A1073    12623  11947  10175    465   3482    159       O\\nATOM   1882  CB  ALA A1073      41.357  -7.149  28.747  1.00 88.38           C\\nANISOU 1882  CB  ALA A1073    11477  11958  10146     77   3385    785       C\\nATOM   1883  N   ALA A1074      38.441  -8.397  29.079  1.00 83.01           N\\nANISOU 1883  N   ALA A1074    11651  10689   9199    259   2785    645       N\\nATOM   1884  CA  ALA A1074      37.590  -9.476  29.567  1.00 85.44           C\\nANISOU 1884  CA  ALA A1074    12143  10714   9605    456   2615    500       C\\nATOM   1885  C   ALA A1074      36.749 -10.084  28.454  1.00 93.89           C\\nANISOU 1885  C   ALA A1074    13614  11749  10313    356   2695    279       C\\nATOM   1886  O   ALA A1074      36.388 -11.263  28.528  1.00 97.64           O\\nANISOU 1886  O   ALA A1074    14228  11998  10874    520   2705     57       O\\nATOM   1887  CB  ALA A1074      36.686  -8.968  30.689  1.00 78.28           C\\nANISOU 1887  CB  ALA A1074    11263   9662   8819    417   2191    709       C\\nATOM   1888  N   VAL A1075      36.430  -9.305  27.419  1.00 95.22           N\\nANISOU 1888  N   VAL A1075    13998  12114  10069     70   2718    348       N\\nATOM   1889  CA  VAL A1075      35.614  -9.821  26.325  1.00 92.66           C\\nANISOU 1889  CA  VAL A1075    14075  11790   9341    -54   2737    139       C\\nATOM   1890  C   VAL A1075      36.457 -10.646  25.357  1.00100.97           C\\nANISOU 1890  C   VAL A1075    15170  12983  10213     22   3217   -207       C\\nATOM   1891  O   VAL A1075      35.987 -11.658  24.824  1.00101.40           O\\nANISOU 1891  O   VAL A1075    15489  12912  10125     79   3272   -531       O\\nATOM   1892  CB  VAL A1075      34.888  -8.661  25.617  1.00 82.73           C\\nANISOU 1892  CB  VAL A1075    13071  10672   7689   -380   2491    377       C\\nATOM   1893  CG1 VAL A1075      34.069  -9.171  24.446  1.00 75.94           C\\nANISOU 1893  CG1 VAL A1075    12635   9852   6368   -528   2457    166       C\\nATOM   1894  CG2 VAL A1075      33.993  -7.930  26.604  1.00 76.88           C\\nANISOU 1894  CG2 VAL A1075    12256   9765   7192   -384   2023    620       C\\nATOM   1895  N   ARG A1076      37.712 -10.240  25.115  1.00100.09           N\\nANISOU 1895  N   ARG A1076    14776  13139  10116     17   3583   -182       N\\nATOM   1896  CA  ARG A1076      38.592 -11.049  24.273  1.00106.02           C\\nANISOU 1896  CA  ARG A1076    15475  14062  10744    139   4103   -579       C\\nATOM   1897  C   ARG A1076      38.740 -12.458  24.828  1.00110.21           C\\nANISOU 1897  C   ARG A1076    15911  14258  11706    564   4141   -922       C\\nATOM   1898  O   ARG A1076      38.867 -13.421  24.062  1.00118.72           O\\nANISOU 1898  O   ARG A1076    17153  15310  12647    690   4425  -1359       O\\nATOM   1899  CB  ARG A1076      39.980 -10.411  24.143  1.00109.75           C\\nANISOU 1899  CB  ARG A1076    15519  14893  11289     84   4503   -500       C\\nATOM   1900  CG  ARG A1076      40.027  -8.904  24.227  1.00109.02           C\\nANISOU 1900  CG  ARG A1076    15378  14979  11066   -286   4338    -22       C\\nATOM   1901  CD  ARG A1076      39.706  -8.229  22.910  1.00113.54           C\\nANISOU 1901  CD  ARG A1076    16360  15831  10947   -724   4457     91       C\\nATOM   1902  NE  ARG A1076      39.657  -6.778  23.063  1.00113.48           N\\nANISOU 1902  NE  ARG A1076    16365  15872  10879  -1069   4203    591       N\\nATOM   1903  CZ  ARG A1076      39.507  -5.923  22.058  1.00114.12           C\\nANISOU 1903  CZ  ARG A1076    16787  16166  10409  -1503   4233    842       C\\nATOM   1904  NH1 ARG A1076      39.395  -6.367  20.812  1.00118.70           N\\nANISOU 1904  NH1 ARG A1076    17722  16997  10383  -1663   4528    629       N\\nATOM   1905  NH2 ARG A1076      39.471  -4.619  22.301  1.00110.17           N\\nANISOU 1905  NH2 ARG A1076    16305  15605   9949  -1786   3945   1307       N\\nATOM   1906  N   GLY A1077      38.727 -12.597  26.152  1.00104.33           N\\nANISOU 1906  N   GLY A1077    14938  13235  11468    780   3843   -732       N\\nATOM   1907  CA  GLY A1077      38.862 -13.893  26.781  1.00103.24           C\\nANISOU 1907  CA  GLY A1077    14749  12715  11761   1164   3801   -960       C\\nATOM   1908  C   GLY A1077      37.555 -14.652  26.832  1.00100.52           C\\nANISOU 1908  C   GLY A1077    14844  12012  11338   1106   3509  -1046       C\\nATOM   1909  O   GLY A1077      37.538 -15.875  26.663  1.00104.59           O\\nANISOU 1909  O   GLY A1077    15516  12220  12003   1321   3586  -1382       O\\nATOM   1910  N   ILE A1078      36.453 -13.936  27.070  1.00 99.32           N\\nANISOU 1910  N   ILE A1078    14869  11880  10988    814   3165   -762       N\\nATOM   1911  CA  ILE A1078      35.138 -14.573  27.087  1.00 95.36           C\\nANISOU 1911  CA  ILE A1078    14721  11103  10410    692   2887   -841       C\\nATOM   1912  C   ILE A1078      34.872 -15.266  25.758  1.00 94.23           C\\nANISOU 1912  C   ILE A1078    14931  10962   9909    611   3076  -1259       C\\nATOM   1913  O   ILE A1078      34.461 -16.432  25.713  1.00 91.07           O\\nANISOU 1913  O   ILE A1078    14757  10213   9633    693   3032  -1537       O\\nATOM   1914  CB  ILE A1078      34.042 -13.542  27.412  1.00 93.90           C\\nANISOU 1914  CB  ILE A1078    14585  11030  10063    404   2522   -518       C\\nATOM   1915  CG1 ILE A1078      33.993 -13.263  28.917  1.00 93.60           C\\nANISOU 1915  CG1 ILE A1078    14291  10873  10400    497   2289   -213       C\\nATOM   1916  CG2 ILE A1078      32.692 -14.024  26.911  1.00 91.88           C\\nANISOU 1916  CG2 ILE A1078    14674  10646   9590    192   2300   -673       C\\nATOM   1917  CD1 ILE A1078      33.002 -12.183  29.313  1.00 86.14           C\\nANISOU 1917  CD1 ILE A1078    13326  10053   9351    273   1966     41       C\\nATOM   1918  N   LEU A1079      35.121 -14.560  24.654  1.00 96.21           N\\nANISOU 1918  N   LEU A1079    15266  11598   9690    421   3283  -1311       N\\nATOM   1919  CA  LEU A1079      34.910 -15.148  23.339  1.00 99.06           C\\nANISOU 1919  CA  LEU A1079    15997  12035   9608    315   3475  -1730       C\\nATOM   1920  C   LEU A1079      35.911 -16.261  23.058  1.00104.43           C\\nANISOU 1920  C   LEU A1079    16609  12586  10483    653   3898  -2204       C\\nATOM   1921  O   LEU A1079      35.576 -17.237  22.375  1.00107.18           O\\nANISOU 1921  O   LEU A1079    17287  12752  10686    675   3966  -2650       O\\nATOM   1922  CB  LEU A1079      34.990 -14.061  22.271  1.00 97.08           C\\nANISOU 1922  CB  LEU A1079    15879  12261   8747     -2   3592  -1606       C\\nATOM   1923  CG  LEU A1079      34.022 -12.896  22.494  1.00 92.62           C\\nANISOU 1923  CG  LEU A1079    15381  11775   8035   -286   3126  -1146       C\\nATOM   1924  CD1 LEU A1079      34.208 -11.832  21.427  1.00 87.85           C\\nANISOU 1924  CD1 LEU A1079    14956  11583   6838   -599   3216   -967       C\\nATOM   1925  CD2 LEU A1079      32.586 -13.395  22.521  1.00 89.61           C\\nANISOU 1925  CD2 LEU A1079    15271  11148   7628   -399   2691  -1233       C\\nATOM   1926  N   ARG A1080      37.134 -16.141  23.574  1.00102.78           N\\nANISOU 1926  N   ARG A1080    15961  12455  10635    932   4161  -2150       N\\nATOM   1927  CA  ARG A1080      38.113 -17.215  23.463  1.00106.42           C\\nANISOU 1927  CA  ARG A1080    16265  12749  11422   1346   4516  -2607       C\\nATOM   1928  C   ARG A1080      37.864 -18.345  24.454  1.00114.00           C\\nANISOU 1928  C   ARG A1080    17260  13084  12971   1658   4225  -2653       C\\nATOM   1929  O   ARG A1080      38.585 -19.348  24.417  1.00121.35           O\\nANISOU 1929  O   ARG A1080    18104  13749  14255   2055   4430  -3041       O\\nATOM   1930  CB  ARG A1080      39.528 -16.662  23.652  1.00 95.46           C\\nANISOU 1930  CB  ARG A1080    14320  11699  10249   1534   4874  -2535       C\\nATOM   1931  N   ASN A1081      36.877 -18.203  25.339  1.00113.30           N\\nANISOU 1931  N   ASN A1081    17292  12754  13003   1487   3760  -2268       N\\nATOM   1932  CA  ASN A1081      36.488 -19.263  26.264  1.00110.82           C\\nANISOU 1932  CA  ASN A1081    17098  11850  13160   1666   3466  -2242       C\\nATOM   1933  C   ASN A1081      35.348 -20.052  25.630  1.00107.85           C\\nANISOU 1933  C   ASN A1081    17225  11189  12565   1437   3324  -2533       C\\nATOM   1934  O   ASN A1081      34.255 -19.516  25.418  1.00 96.74           O\\nANISOU 1934  O   ASN A1081    16004   9943  10809   1044   3098  -2372       O\\nATOM   1935  CB  ASN A1081      36.075 -18.682  27.614  1.00104.89           C\\nANISOU 1935  CB  ASN A1081    16179  11052  12621   1564   3094  -1681       C\\nATOM   1936  CG  ASN A1081      35.935 -19.745  28.696  1.00100.82           C\\nANISOU 1936  CG  ASN A1081    15751   9964  12593   1757   2830  -1573       C\\nATOM   1937  OD1 ASN A1081      35.536 -20.881  28.430  1.00 96.54           O\\nANISOU 1937  OD1 ASN A1081    15540   8975  12166   1793   2783  -1851       O\\nATOM   1938  ND2 ASN A1081      36.265 -19.375  29.927  1.00 99.41           N\\nANISOU 1938  ND2 ASN A1081    15308   9782  12683   1855   2634  -1158       N\\nATOM   1939  N   ALA A1082      35.603 -21.330  25.335  1.00104.72           N\\nANISOU 1939  N   ALA A1082    17030  10346  12412   1693   3425  -2982       N\\nATOM   1940  CA  ALA A1082      34.620 -22.148  24.633  1.00104.56           C\\nANISOU 1940  CA  ALA A1082    17500  10033  12195   1466   3305  -3342       C\\nATOM   1941  C   ALA A1082      33.348 -22.360  25.442  1.00101.54           C\\nANISOU 1941  C   ALA A1082    17302   9334  11945   1142   2845  -3001       C\\nATOM   1942  O   ALA A1082      32.300 -22.654  24.856  1.00101.98           O\\nANISOU 1942  O   ALA A1082    17693   9314  11739    801   2679  -3190       O\\nATOM   1943  CB  ALA A1082      35.231 -23.499  24.264  1.00107.82           C\\nANISOU 1943  CB  ALA A1082    18086   9944  12935   1850   3489  -3914       C\\nATOM   1944  N   LYS A1083      33.409 -22.219  26.764  1.00105.02           N\\nANISOU 1944  N   LYS A1083    17519   9623  12760   1215   2642  -2520       N\\nATOM   1945  CA  LYS A1083      32.243 -22.435  27.607  1.00 99.72           C\\nANISOU 1945  CA  LYS A1083    16986   8701  12202    885   2273  -2194       C\\nATOM   1946  C   LYS A1083      31.446 -21.163  27.871  1.00 97.98           C\\nANISOU 1946  C   LYS A1083    16574   8985  11668    541   2119  -1821       C\\nATOM   1947  O   LYS A1083      30.317 -21.253  28.366  1.00 96.09           O\\nANISOU 1947  O   LYS A1083    16414   8652  11442    209   1857  -1636       O\\nATOM   1948  CB  LYS A1083      32.666 -23.061  28.941  1.00 98.15           C\\nANISOU 1948  CB  LYS A1083    16717   8046  12528   1114   2120  -1873       C\\nATOM   1949  N   LEU A1084      31.992 -19.986  27.551  1.00 99.46           N\\nANISOU 1949  N   LEU A1084    16502   9689  11600    605   2275  -1719       N\\nATOM   1950  CA  LEU A1084      31.288 -18.729  27.771  1.00 97.55           C\\nANISOU 1950  CA  LEU A1084    16090   9867  11109    333   2100  -1390       C\\nATOM   1951  C   LEU A1084      30.919 -17.993  26.491  1.00101.44           C\\nANISOU 1951  C   LEU A1084    16699  10753  11090    121   2131  -1554       C\\nATOM   1952  O   LEU A1084      30.009 -17.161  26.521  1.00102.09           O\\nANISOU 1952  O   LEU A1084    16730  11072  10987   -136   1884  -1351       O\\nATOM   1953  CB  LEU A1084      32.124 -17.790  28.654  1.00 93.67           C\\nANISOU 1953  CB  LEU A1084    15216   9609  10766    522   2147  -1024       C\\nATOM   1954  CG  LEU A1084      32.376 -18.250  30.092  1.00 99.39           C\\nANISOU 1954  CG  LEU A1084    15814  10040  11911    678   2020   -744       C\\nATOM   1955  CD1 LEU A1084      33.068 -17.160  30.896  1.00100.96           C\\nANISOU 1955  CD1 LEU A1084    15645  10540  12174    797   2010   -411       C\\nATOM   1956  CD2 LEU A1084      31.075 -18.668  30.757  1.00 98.30           C\\nANISOU 1956  CD2 LEU A1084    15830   9700  11820    371   1756   -602       C\\nATOM   1957  N   LYS A1085      31.598 -18.269  25.378  1.00102.45           N\\nANISOU 1957  N   LYS A1085    16983  10965  10978    227   2417  -1917       N\\nATOM   1958  CA  LYS A1085      31.262 -17.597  24.126  1.00 99.55           C\\nANISOU 1958  CA  LYS A1085    16799  10990  10037    -13   2431  -2041       C\\nATOM   1959  C   LYS A1085      29.850 -17.899  23.627  1.00 99.81           C\\nANISOU 1959  C   LYS A1085    17128  10950   9847   -354   2083  -2182       C\\nATOM   1960  O   LYS A1085      29.193 -16.966  23.138  1.00 92.79           O\\nANISOU 1960  O   LYS A1085    16268  10388   8598   -594   1861  -2023       O\\nATOM   1961  CB  LYS A1085      32.301 -17.947  23.053  1.00 96.22           C\\nANISOU 1961  CB  LYS A1085    16501  10703   9355    149   2870  -2453       C\\nATOM   1962  N   PRO A1086      29.335 -19.137  23.693  1.00105.32           N\\nANISOU 1962  N   PRO A1086    18044  11220  10751   -402   1987  -2468       N\\nATOM   1963  CA  PRO A1086      27.961 -19.366  23.201  1.00106.72           C\\nANISOU 1963  CA  PRO A1086    18449  11373  10729   -778   1625  -2606       C\\nATOM   1964  C   PRO A1086      26.904 -18.527  23.902  1.00101.72           C\\nANISOU 1964  C   PRO A1086    17551  10915  10184  -1000   1260  -2201       C\\nATOM   1965  O   PRO A1086      26.130 -17.830  23.232  1.00 97.88           O\\nANISOU 1965  O   PRO A1086    17104  10733   9353  -1226    992  -2175       O\\nATOM   1966  CB  PRO A1086      27.759 -20.868  23.445  1.00108.18           C\\nANISOU 1966  CB  PRO A1086    18857  10979  11267   -780   1611  -2917       C\\nATOM   1967  CG  PRO A1086      29.125 -21.438  23.364  1.00108.60           C\\nANISOU 1967  CG  PRO A1086    18951  10834  11479   -369   2012  -3150       C\\nATOM   1968  CD  PRO A1086      30.018 -20.411  23.991  1.00103.81           C\\nANISOU 1968  CD  PRO A1086    17951  10542  10950   -127   2192  -2744       C\\nATOM   1969  N   VAL A1087      26.844 -18.575  25.235  1.00 98.45           N\\nANISOU 1969  N   VAL A1087    16867  10324  10214   -932   1231  -1899       N\\nATOM   1970  CA  VAL A1087      25.825 -17.817  25.956  1.00 96.16           C\\nANISOU 1970  CA  VAL A1087    16290  10223  10024  -1125    937  -1588       C\\nATOM   1971  C   VAL A1087      26.024 -16.321  25.749  1.00 94.05           C\\nANISOU 1971  C   VAL A1087    15830  10386   9517  -1049    881  -1337       C\\nATOM   1972  O   VAL A1087      25.055 -15.564  25.617  1.00 93.16           O\\nANISOU 1972  O   VAL A1087    15592  10501   9302  -1221    565  -1236       O\\nATOM   1973  CB  VAL A1087      25.834 -18.196  27.449  1.00 97.74           C\\nANISOU 1973  CB  VAL A1087    16281  10182  10673  -1078    978  -1328       C\\nATOM   1974  CG1 VAL A1087      27.238 -18.088  28.024  1.00102.40           C\\nANISOU 1974  CG1 VAL A1087    16780  10706  11420   -706   1259  -1166       C\\nATOM   1975  CG2 VAL A1087      24.863 -17.323  28.230  1.00 89.97           C\\nANISOU 1975  CG2 VAL A1087    14954   9465   9765  -1245    754  -1058       C\\nATOM   1976  N   TYR A1088      27.284 -15.876  25.692  1.00 89.69           N\\nANISOU 1976  N   TYR A1088    15242   9934   8902   -793   1168  -1242       N\\nATOM   1977  CA  TYR A1088      27.580 -14.457  25.515  1.00 90.57           C\\nANISOU 1977  CA  TYR A1088    15204  10393   8813   -755   1125   -975       C\\nATOM   1978  C   TYR A1088      26.959 -13.916  24.234  1.00 95.61           C\\nANISOU 1978  C   TYR A1088    16073  11277   8976   -968    892  -1053       C\\nATOM   1979  O   TYR A1088      26.470 -12.781  24.202  1.00 93.98           O\\nANISOU 1979  O   TYR A1088    15753  11275   8682  -1035    611   -805       O\\nATOM   1980  CB  TYR A1088      29.095 -14.250  25.512  1.00 93.94           C\\nANISOU 1980  CB  TYR A1088    15566  10885   9242   -509   1510   -919       C\\nATOM   1981  CG  TYR A1088      29.544 -12.810  25.574  1.00 98.44           C\\nANISOU 1981  CG  TYR A1088    15953  11742   9710   -493   1488   -591       C\\nATOM   1982  CD1 TYR A1088      29.740 -12.178  26.794  1.00 98.86           C\\nANISOU 1982  CD1 TYR A1088    15682  11781  10099   -378   1424   -304       C\\nATOM   1983  CD2 TYR A1088      29.792 -12.088  24.415  1.00103.73           C\\nANISOU 1983  CD2 TYR A1088    16808  12681   9923   -622   1523   -565       C\\nATOM   1984  CE1 TYR A1088      30.162 -10.863  26.860  1.00 99.84           C\\nANISOU 1984  CE1 TYR A1088    15661  12107  10167   -380   1378    -29       C\\nATOM   1985  CE2 TYR A1088      30.213 -10.771  24.470  1.00106.12           C\\nANISOU 1985  CE2 TYR A1088    16981  13181  10158   -650   1482   -232       C\\nATOM   1986  CZ  TYR A1088      30.395 -10.164  25.696  1.00103.83           C\\nANISOU 1986  CZ  TYR A1088    16357  12826  10268   -522   1402     20       C\\nATOM   1987  OH  TYR A1088      30.810  -8.854  25.759  1.00103.35           O\\nANISOU 1987  OH  TYR A1088    16189  12904  10176   -568   1333    326       O\\nATOM   1988  N   ASP A1089      26.969 -14.714  23.164  1.00102.12           N\\nANISOU 1988  N   ASP A1089    17248  12069   9485  -1067    973  -1406       N\\nATOM   1989  CA  ASP A1089      26.320 -14.293  21.927  1.00102.51           C\\nANISOU 1989  CA  ASP A1089    17573  12361   9018  -1301    696  -1486       C\\nATOM   1990  C   ASP A1089      24.810 -14.185  22.110  1.00 97.68           C\\nANISOU 1990  C   ASP A1089    16847  11734   8531  -1503    175  -1453       C\\nATOM   1991  O   ASP A1089      24.193 -13.208  21.669  1.00 94.27           O\\nANISOU 1991  O   ASP A1089    16405  11528   7886  -1603   -198  -1266       O\\nATOM   1992  CB  ASP A1089      26.658 -15.270  20.798  1.00107.75           C\\nANISOU 1992  CB  ASP A1089    18652  12996   9292  -1371    911  -1943       C\\nATOM   1993  CG  ASP A1089      28.153 -15.360  20.522  1.00109.36           C\\nANISOU 1993  CG  ASP A1089    18906  13282   9365  -1158   1468  -2039       C\\nATOM   1994  OD1 ASP A1089      28.859 -14.349  20.724  1.00107.83           O\\nANISOU 1994  OD1 ASP A1089    18522  13306   9142  -1077   1610  -1702       O\\nATOM   1995  OD2 ASP A1089      28.623 -16.442  20.104  1.00108.54           O\\nANISOU 1995  OD2 ASP A1089    19006  13016   9217  -1074   1762  -2478       O\\nATOM   1996  N   SER A1090      24.200 -15.124  22.768  1.00 95.52           N\\nANISOU 1996  N   SER A1090    16469  11190   8635  -1571    131  -1622       N\\nATOM   1997  CA  SER A1090      22.775 -15.087  22.914  1.00100.79           C\\nANISOU 1997  CA  SER A1090    16964  11869   9463  -1805   -311  -1652       C\\nATOM   1998  C   SER A1090      22.220 -13.982  23.739  1.00102.57           C\\nANISOU 1998  C   SER A1090    16755  12269   9949  -1733   -541  -1311       C\\nATOM   1999  O   SER A1090      21.034 -13.763  23.747  1.00106.04           O\\nANISOU 1999  O   SER A1090    16983  12810  10497  -1894   -938  -1340       O\\nATOM   2000  CB  SER A1090      22.377 -16.406  23.588  1.00 99.01           C\\nANISOU 2000  CB  SER A1090    16709  11296   9615  -1937   -227  -1860       C\\nATOM   2001  OG  SER A1090      21.208 -16.357  24.395  1.00 95.53           O\\nANISOU 2001  OG  SER A1090    15874  10901   9522  -2092   -478  -1730       O\\nATOM   2002  N   LEU A1091      23.062 -13.325  24.481  1.00 99.87           N\\nANISOU 2002  N   LEU A1091    16250  11965   9730  -1492   -315  -1031       N\\nATOM   2003  CA  LEU A1091      22.607 -12.416  25.517  1.00 95.87           C\\nANISOU 2003  CA  LEU A1091    15324  11551   9550  -1398   -463   -783       C\\nATOM   2004  C   LEU A1091      22.327 -11.026  24.968  1.00 97.76           C\\nANISOU 2004  C   LEU A1091    15525  12007   9612  -1342   -816   -587       C\\nATOM   2005  O   LEU A1091      23.032 -10.535  24.083  1.00 95.64           O\\nANISOU 2005  O   LEU A1091    15549  11818   8971  -1317   -786   -485       O\\nATOM   2006  CB  LEU A1091      23.641 -12.333  26.638  1.00 87.84           C\\nANISOU 2006  CB  LEU A1091    14159  10436   8780  -1181    -92   -597       C\\nATOM   2007  CG  LEU A1091      23.680 -13.560  27.542  1.00 82.06           C\\nANISOU 2007  CG  LEU A1091    13386   9458   8336  -1224    143   -690       C\\nATOM   2008  CD1 LEU A1091      24.786 -13.425  28.573  1.00 80.82           C\\nANISOU 2008  CD1 LEU A1091    13114   9224   8371   -989    440   -482       C\\nATOM   2009  CD2 LEU A1091      22.327 -13.769  28.206  1.00 80.36           C\\nANISOU 2009  CD2 LEU A1091    12890   9277   8367  -1435    -70   -736       C\\nATOM   2010  N   ASP A1092      21.376 -10.343  25.562  1.00 96.05           N\\nANISOU 2010  N   ASP A1092    14944  11880   9672  -1329  -1151   -538       N\\nATOM   2011  CA  ASP A1092      21.052  -8.988  25.248  1.00 94.58           C\\nANISOU 2011  CA  ASP A1092    14656  11809   9469  -1194  -1512   -321       C\\nATOM   2012  C   ASP A1092      22.222  -8.197  25.771  1.00 90.97           C\\nANISOU 2012  C   ASP A1092    14182  11304   9080   -989  -1249    -61       C\\nATOM   2013  O   ASP A1092      22.961  -8.670  26.567  1.00 94.84           O\\nANISOU 2013  O   ASP A1092    14566  11715   9754   -916   -857    -59       O\\nATOM   2014  CB  ASP A1092      19.780  -8.669  26.007  1.00101.30           C\\nANISOU 2014  CB  ASP A1092    15029  12751  10711  -1166  -1868   -406       C\\nATOM   2015  CG  ASP A1092      19.607  -7.210  26.318  1.00111.33           C\\nANISOU 2015  CG  ASP A1092    16080  14045  12176   -914  -2131   -205       C\\nATOM   2016  OD1 ASP A1092      20.277  -6.361  25.708  1.00117.45           O\\nANISOU 2016  OD1 ASP A1092    17125  14798  12702   -861  -2417     -1       O\\nATOM   2017  OD2 ASP A1092      18.756  -6.904  27.171  1.00112.11           O\\nANISOU 2017  OD2 ASP A1092    15757  14174  12666   -784  -2057   -258       O\\nATOM   2018  N   ALA A1093      22.381  -6.966  25.331  1.00 96.88           N\\nANISOU 2018  N   ALA A1093    15054  12081   9674   -916  -1505    178       N\\nATOM   2019  CA  ALA A1093      23.488  -6.122  25.778  1.00 91.46           C\\nANISOU 2019  CA  ALA A1093    14374  11336   9042   -782  -1292    431       C\\nATOM   2020  C   ALA A1093      23.421  -5.832  27.272  1.00 93.10           C\\nANISOU 2020  C   ALA A1093    14165  11492   9718   -603  -1188    414       C\\nATOM   2021  O   ALA A1093      24.464  -5.712  27.927  1.00 87.73           O\\nANISOU 2021  O   ALA A1093    13451  10765   9118   -524   -866    519       O\\nATOM   2022  CB  ALA A1093      23.503  -4.814  24.988  1.00 88.70           C\\nANISOU 2022  CB  ALA A1093    14227  10970   8505   -779  -1676    717       C\\nATOM   2023  N   VAL A1094      22.214  -5.720  27.829  1.00 97.94           N\\nANISOU 2023  N   VAL A1094    14439  12147  10627   -546  -1450    262       N\\nATOM   2024  CA  VAL A1094      22.076  -5.445  29.257  1.00 93.00           C\\nANISOU 2024  CA  VAL A1094    13427  11531  10378   -399  -1324    200       C\\nATOM   2025  C   VAL A1094      22.441  -6.680  30.072  1.00 88.59           C\\nANISOU 2025  C   VAL A1094    12819  10982   9860   -491   -879     98       C\\nATOM   2026  O   VAL A1094      23.204  -6.601  31.041  1.00 83.02           O\\nANISOU 2026  O   VAL A1094    12036  10247   9261   -400   -616    175       O\\nATOM   2027  CB  VAL A1094      20.652  -4.956  29.576  1.00 91.34           C\\nANISOU 2027  CB  VAL A1094    12822  11413  10469   -310  -1694     21       C\\nATOM   2028  CG1 VAL A1094      20.546  -4.549  31.038  1.00 87.18           C\\nANISOU 2028  CG1 VAL A1094    11914  10940  10271   -155  -1529    -81       C\\nATOM   2029  CG2 VAL A1094      20.261  -3.802  28.656  1.00 92.19           C\\nANISOU 2029  CG2 VAL A1094    13027  11445  10557   -192  -2230    148       C\\nATOM   2030  N   ARG A1095      21.898  -7.840  29.694  1.00 90.63           N\\nANISOU 2030  N   ARG A1095    13144  11253  10038   -685   -833    -66       N\\nATOM   2031  CA  ARG A1095      22.284  -9.087  30.344  1.00 90.96           C\\nANISOU 2031  CA  ARG A1095    13231  11214  10116   -790   -456   -122       C\\nATOM   2032  C   ARG A1095      23.746  -9.427  30.091  1.00 87.34           C\\nANISOU 2032  C   ARG A1095    13078  10619   9487   -715   -154      0       C\\nATOM   2033  O   ARG A1095      24.354 -10.144  30.893  1.00 79.42           O\\nANISOU 2033  O   ARG A1095    12074   9515   8587   -689    132     31       O\\nATOM   2034  CB  ARG A1095      21.389 -10.229  29.864  1.00 87.99           C\\nANISOU 2034  CB  ARG A1095    12907  10817   9709  -1046   -517   -333       C\\nATOM   2035  CG  ARG A1095      19.913  -9.890  29.887  1.00 88.08           C\\nANISOU 2035  CG  ARG A1095    12562  11010   9896  -1139   -853   -486       C\\nATOM   2036  CD  ARG A1095      19.099 -10.979  29.236  1.00 93.06           C\\nANISOU 2036  CD  ARG A1095    13265  11616  10479  -1439   -963   -697       C\\nATOM   2037  NE  ARG A1095      17.793 -10.502  28.791  1.00103.22           N\\nANISOU 2037  NE  ARG A1095    14244  13099  11877  -1501  -1404   -846       N\\nATOM   2038  CZ  ARG A1095      16.679 -10.583  29.511  1.00102.98           C\\nANISOU 2038  CZ  ARG A1095    13724  13246  12157  -1620  -1455   -997       C\\nATOM   2039  NH1 ARG A1095      16.705 -11.126  30.720  1.00101.20           N\\nANISOU 2039  NH1 ARG A1095    13324  13034  12095  -1735  -1072   -988       N\\nATOM   2040  NH2 ARG A1095      15.535 -10.122  29.020  1.00102.93           N\\nANISOU 2040  NH2 ARG A1095    13394  13427  12289  -1634  -1897  -1154       N\\nATOM   2041  N   ARG A1096      24.321  -8.920  29.001  1.00 90.45           N\\nANISOU 2041  N   ARG A1096    13718  11024   9623   -685   -218     78       N\\nATOM   2042  CA  ARG A1096      25.730  -9.168  28.728  1.00 86.04           C\\nANISOU 2042  CA  ARG A1096    13368  10402   8921   -614    110    159       C\\nATOM   2043  C   ARG A1096      26.623  -8.481  29.750  1.00 81.52           C\\nANISOU 2043  C   ARG A1096    12598   9829   8548   -445    250    350       C\\nATOM   2044  O   ARG A1096      27.697  -8.997  30.076  1.00 76.37           O\\nANISOU 2044  O   ARG A1096    11967   9110   7940   -359    548    380       O\\nATOM   2045  CB  ARG A1096      26.072  -8.706  27.313  1.00 85.80           C\\nANISOU 2045  CB  ARG A1096    13637  10453   8510   -686     38    205       C\\nATOM   2046  CG  ARG A1096      26.974  -9.657  26.568  1.00 82.89           C\\nANISOU 2046  CG  ARG A1096    13541  10054   7898   -716    389     63       C\\nATOM   2047  CD  ARG A1096      27.247  -9.180  25.159  1.00 85.44           C\\nANISOU 2047  CD  ARG A1096    14183  10531   7750   -844    350    102       C\\nATOM   2048  NE  ARG A1096      26.098  -9.355  24.282  1.00 94.36           N\\nANISOU 2048  NE  ARG A1096    15514  11710   8629  -1018     -6    -32       N\\nATOM   2049  CZ  ARG A1096      26.167  -9.297  22.957  1.00 97.59           C\\nANISOU 2049  CZ  ARG A1096    16291  12257   8531  -1179    -60    -72       C\\nATOM   2050  NH1 ARG A1096      27.333  -9.075  22.369  1.00 93.17           N\\nANISOU 2050  NH1 ARG A1096    15919  11820   7663  -1201    286      6       N\\nATOM   2051  NH2 ARG A1096      25.078  -9.465  22.222  1.00102.27           N\\nANISOU 2051  NH2 ARG A1096    17053  12899   8906  -1338   -456   -197       N\\nATOM   2052  N   ALA A1097      26.196  -7.325  30.270  1.00 83.15           N\\nANISOU 2052  N   ALA A1097    12599  10095   8899   -381     10    450       N\\nATOM   2053  CA  ALA A1097      26.963  -6.656  31.316  1.00 74.83           C\\nANISOU 2053  CA  ALA A1097    11361   9035   8036   -245    100    585       C\\nATOM   2054  C   ALA A1097      26.946  -7.446  32.617  1.00 73.67           C\\nANISOU 2054  C   ALA A1097    11047   8874   8072   -207    277    525       C\\nATOM   2055  O   ALA A1097      27.942  -7.452  33.348  1.00 74.45           O\\nANISOU 2055  O   ALA A1097    11087   8949   8253   -111    442    628       O\\nATOM   2056  CB  ALA A1097      26.423  -5.246  31.550  1.00 63.51           C\\nANISOU 2056  CB  ALA A1097     9778   7621   6732   -175   -226    643       C\\nATOM   2057  N   ALA A1098      25.832  -8.117  32.923  1.00 71.99           N\\nANISOU 2057  N   ALA A1098    10755   8685   7912   -311    230    379       N\\nATOM   2058  CA  ALA A1098      25.774  -8.940  34.125  1.00 74.69           C\\nANISOU 2058  CA  ALA A1098    11001   9011   8365   -346    407    373       C\\nATOM   2059  C   ALA A1098      26.760 -10.098  34.047  1.00 83.58           C\\nANISOU 2059  C   ALA A1098    12344   9949   9462   -326    646    434       C\\nATOM   2060  O   ALA A1098      27.358 -10.485  35.059  1.00 82.43           O\\nANISOU 2060  O   ALA A1098    12168   9750   9403   -262    768    547       O\\nATOM   2061  CB  ALA A1098      24.351  -9.450  34.338  1.00 76.99           C\\nANISOU 2061  CB  ALA A1098    11160   9381   8710   -537    335    213       C\\nATOM   2062  N   LEU A1099      26.946 -10.665  32.852  1.00 86.05           N\\nANISOU 2062  N   LEU A1099    12886  10156   9651   -363    693    343       N\\nATOM   2063  CA  LEU A1099      27.950 -11.710  32.691  1.00 84.37           C\\nANISOU 2063  CA  LEU A1099    12858   9742   9457   -276    922    336       C\\nATOM   2064  C   LEU A1099      29.360 -11.153  32.838  1.00 75.62           C\\nANISOU 2064  C   LEU A1099    11669   8675   8388    -65   1050    473       C\\nATOM   2065  O   LEU A1099      30.242 -11.829  33.380  1.00 59.72           O\\nANISOU 2065  O   LEU A1099     9651   6525   6517     79   1192    528       O\\nATOM   2066  CB  LEU A1099      27.785 -12.397  31.335  1.00 88.81           C\\nANISOU 2066  CB  LEU A1099    13687  10211   9847   -362    961    126       C\\nATOM   2067  CG  LEU A1099      28.635 -13.647  31.091  1.00 89.13           C\\nANISOU 2067  CG  LEU A1099    13929   9988   9947   -253   1195     11       C\\nATOM   2068  CD1 LEU A1099      28.246 -14.750  32.060  1.00 88.78           C\\nANISOU 2068  CD1 LEU A1099    13929   9678  10126   -318   1188     43       C\\nATOM   2069  CD2 LEU A1099      28.496 -14.118  29.655  1.00 91.08           C\\nANISOU 2069  CD2 LEU A1099    14451  10201   9955   -337   1240   -262       C\\nATOM   2070  N   ILE A1100      29.591  -9.928  32.363  1.00 70.27           N\\nANISOU 2070  N   ILE A1100    10921   8168   7612    -56    974    541       N\\nATOM   2071  CA  ILE A1100      30.888  -9.294  32.557  1.00 70.30           C\\nANISOU 2071  CA  ILE A1100    10796   8234   7680     77   1083    680       C\\nATOM   2072  C   ILE A1100      31.120  -9.006  34.034  1.00 76.98           C\\nANISOU 2072  C   ILE A1100    11428   9092   8729    165   1006    808       C\\nATOM   2073  O   ILE A1100      32.244  -9.120  34.537  1.00 80.54           O\\nANISOU 2073  O   ILE A1100    11764   9529   9310    301   1104    897       O\\nATOM   2074  CB  ILE A1100      30.983  -8.022  31.697  1.00 68.88           C\\nANISOU 2074  CB  ILE A1100    10638   8193   7340    -10    989    761       C\\nATOM   2075  CG1 ILE A1100      30.869  -8.386  30.212  1.00 75.73           C\\nANISOU 2075  CG1 ILE A1100    11771   9090   7912   -120   1082    646       C\\nATOM   2076  CG2 ILE A1100      32.279  -7.281  31.978  1.00 63.94           C\\nANISOU 2076  CG2 ILE A1100     9841   7638   6817     56   1090    917       C\\nATOM   2077  CD1 ILE A1100      30.869  -7.196  29.275  1.00 65.67           C\\nANISOU 2077  CD1 ILE A1100    10607   7938   6405   -260    954    784       C\\nATOM   2078  N   ASN A1101      30.057  -8.645  34.757  1.00 76.26           N\\nANISOU 2078  N   ASN A1101    11262   9055   8656     88    828    795       N\\nATOM   2079  CA  ASN A1101      30.161  -8.449  36.200  1.00 71.74           C\\nANISOU 2079  CA  ASN A1101    10532   8535   8191    138    773    876       C\\nATOM   2080  C   ASN A1101      30.619  -9.725  36.896  1.00 69.64           C\\nANISOU 2080  C   ASN A1101    10339   8134   7987    190    891    949       C\\nATOM   2081  O   ASN A1101      31.439  -9.679  37.821  1.00 64.42           O\\nANISOU 2081  O   ASN A1101     9588   7486   7403    297    869   1078       O\\nATOM   2082  CB  ASN A1101      28.811  -7.981  36.750  1.00 72.99           C\\nANISOU 2082  CB  ASN A1101    10589   8814   8330     34    629    774       C\\nATOM   2083  CG  ASN A1101      28.882  -7.542  38.204  1.00 79.76           C\\nANISOU 2083  CG  ASN A1101    11293   9793   9219     68    586    807       C\\nATOM   2084  OD1 ASN A1101      29.385  -8.264  39.065  1.00 88.11           O\\nANISOU 2084  OD1 ASN A1101    12391  10824  10262     80    664    919       O\\nATOM   2085  ND2 ASN A1101      28.363  -6.353  38.484  1.00 77.04           N\\nANISOU 2085  ND2 ASN A1101    10794   9569   8909     92    434    696       N\\nATOM   2086  N   MET A1102      30.111 -10.877  36.452  1.00 67.47           N\\nANISOU 2086  N   MET A1102    10246   7696   7691    110    973    875       N\\nATOM   2087  CA  MET A1102      30.457 -12.137  37.100  1.00 68.00           C\\nANISOU 2087  CA  MET A1102    10442   7546   7851    150   1035    971       C\\nATOM   2088  C   MET A1102      31.900 -12.539  36.815  1.00 75.21           C\\nANISOU 2088  C   MET A1102    11354   8314   8910    407   1126   1011       C\\nATOM   2089  O   MET A1102      32.611 -12.984  37.723  1.00 77.63           O\\nANISOU 2089  O   MET A1102    11635   8519   9341    543   1075   1172       O\\nATOM   2090  CB  MET A1102      29.492 -13.233  36.655  1.00 70.40           C\\nANISOU 2090  CB  MET A1102    10958   7659   8132    -38   1075    861       C\\nATOM   2091  CG  MET A1102      28.072 -13.024  37.150  1.00 76.57           C\\nANISOU 2091  CG  MET A1102    11663   8605   8824   -310   1005    826       C\\nATOM   2092  SD  MET A1102      27.010 -14.445  36.822  1.00 81.97           S\\nANISOU 2092  SD  MET A1102    12572   9042   9532   -608   1039    733       S\\nATOM   2093  CE  MET A1102      27.916 -15.743  37.652  1.00 80.68           C\\nANISOU 2093  CE  MET A1102    12664   8490   9502   -523   1086    972       C\\nATOM   2094  N   VAL A1103      32.352 -12.395  35.565  1.00 79.58           N\\nANISOU 2094  N   VAL A1103    11918   8879   9439    475   1257    861       N\\nATOM   2095  CA  VAL A1103      33.743 -12.721  35.251  1.00 82.54           C\\nANISOU 2095  CA  VAL A1103    12205   9184   9974    728   1400    840       C\\nATOM   2096  C   VAL A1103      34.689 -11.726  35.912  1.00 80.24           C\\nANISOU 2096  C   VAL A1103    11618   9095   9774    826   1331   1000       C\\nATOM   2097  O   VAL A1103      35.848 -12.053  36.198  1.00 82.23           O\\nANISOU 2097  O   VAL A1103    11705   9299  10238   1051   1366   1045       O\\nATOM   2098  CB  VAL A1103      33.969 -12.782  33.727  1.00 84.75           C\\nANISOU 2098  CB  VAL A1103    12570   9500  10133    729   1619    609       C\\nATOM   2099  CG1 VAL A1103      32.942 -13.689  33.066  1.00 85.19           C\\nANISOU 2099  CG1 VAL A1103    12933   9364  10070    590   1631    415       C\\nATOM   2100  CG2 VAL A1103      33.931 -11.394  33.115  1.00 83.71           C\\nANISOU 2100  CG2 VAL A1103    12339   9665   9801    582   1615    646       C\\nATOM   2101  N   PHE A1104      34.222 -10.502  36.163  1.00 72.46           N\\nANISOU 2101  N   PHE A1104    10543   8321   8669    670   1206   1064       N\\nATOM   2102  CA  PHE A1104      35.025  -9.556  36.927  1.00 74.27           C\\nANISOU 2102  CA  PHE A1104    10521   8703   8994    721   1090   1196       C\\nATOM   2103  C   PHE A1104      35.203 -10.013  38.369  1.00 79.15           C\\nANISOU 2103  C   PHE A1104    11108   9268   9696    808    920   1340       C\\nATOM   2104  O   PHE A1104      36.258  -9.779  38.969  1.00 81.90           O\\nANISOU 2104  O   PHE A1104    11250   9676  10191    937    827   1439       O\\nATOM   2105  CB  PHE A1104      34.382  -8.171  36.883  1.00 67.54           C\\nANISOU 2105  CB  PHE A1104     9633   8010   8019    545    959   1195       C\\nATOM   2106  CG  PHE A1104      35.032  -7.234  35.911  1.00 71.68           C\\nANISOU 2106  CG  PHE A1104    10068   8632   8534    483   1036   1205       C\\nATOM   2107  CD1 PHE A1104      34.785  -7.340  34.554  1.00 74.18           C\\nANISOU 2107  CD1 PHE A1104    10546   8950   8690    396   1191   1126       C\\nATOM   2108  CD2 PHE A1104      35.892  -6.243  36.356  1.00 80.86           C\\nANISOU 2108  CD2 PHE A1104    11011   9893   9821    465    944   1303       C\\nATOM   2109  CE1 PHE A1104      35.384  -6.477  33.659  1.00 78.16           C\\nANISOU 2109  CE1 PHE A1104    11011   9565   9121    278   1280   1183       C\\nATOM   2110  CE2 PHE A1104      36.492  -5.376  35.467  1.00 85.63           C\\nANISOU 2110  CE2 PHE A1104    11550  10576  10412    335   1028   1354       C\\nATOM   2111  CZ  PHE A1104      36.238  -5.493  34.115  1.00 81.25           C\\nANISOU 2111  CZ  PHE A1104    11176  10035   9661    234   1209   1314       C\\nATOM   2112  N   GLN A1105      34.192 -10.669  38.935  1.00 80.45           N\\nANISOU 2112  N   GLN A1105    11475   9341   9754    708    866   1365       N\\nATOM   2113  CA  GLN A1105      34.237 -11.118  40.319  1.00 76.17           C\\nANISOU 2113  CA  GLN A1105    10978   8769   9193    723    706   1544       C\\nATOM   2114  C   GLN A1105      34.839 -12.508  40.465  1.00 79.87           C\\nANISOU 2114  C   GLN A1105    11579   8938   9829    899    695   1660       C\\nATOM   2115  O   GLN A1105      35.670 -12.731  41.352  1.00 77.78           O\\nANISOU 2115  O   GLN A1105    11252   8640   9660   1051    517   1841       O\\nATOM   2116  CB  GLN A1105      32.830 -11.107  40.918  1.00 71.88           C\\nANISOU 2116  CB  GLN A1105    10574   8313   8426    472    687   1531       C\\nATOM   2117  CG  GLN A1105      32.752 -11.692  42.313  1.00 71.95           C\\nANISOU 2117  CG  GLN A1105    10707   8315   8315    408    569   1741       C\\nATOM   2118  CD  GLN A1105      31.379 -11.534  42.928  1.00 72.70           C\\nANISOU 2118  CD  GLN A1105    10864   8598   8159    121    622   1689       C\\nATOM   2119  OE1 GLN A1105      30.414 -11.193  42.241  1.00 76.06           O\\nANISOU 2119  OE1 GLN A1105    11232   9099   8567     -1    727   1488       O\\nATOM   2120  NE2 GLN A1105      31.282 -11.777  44.230  1.00 68.30           N\\nANISOU 2120  NE2 GLN A1105    10410   8146   7396      7    545   1865       N\\nATOM   2121  N   MET A1106      34.433 -13.446  39.607  1.00 80.28           N\\nANISOU 2121  N   MET A1106    11826   8743   9934    892    842   1548       N\\nATOM   2122  CA  MET A1106      34.803 -14.847  39.734  1.00 82.95           C\\nANISOU 2122  CA  MET A1106    12358   8697  10463   1051    807   1630       C\\nATOM   2123  C   MET A1106      35.843 -15.311  38.725  1.00 89.43           C\\nANISOU 2123  C   MET A1106    13075   9350  11554   1362    949   1444       C\\nATOM   2124  O   MET A1106      36.305 -16.452  38.830  1.00 92.75           O\\nANISOU 2124  O   MET A1106    13623   9404  12215   1580    890   1476       O\\nATOM   2125  CB  MET A1106      33.551 -15.727  39.604  1.00 79.57           C\\nANISOU 2125  CB  MET A1106    12259   8043   9930    793    855   1607       C\\nATOM   2126  CG  MET A1106      32.706 -15.755  40.856  1.00 84.73           C\\nANISOU 2126  CG  MET A1106    13038   8785  10370    512    733   1843       C\\nATOM   2127  SD  MET A1106      30.984 -16.135  40.503  1.00 86.03           S\\nANISOU 2127  SD  MET A1106    13388   8937  10364     82    862   1721       S\\nATOM   2128  CE  MET A1106      30.421 -14.540  39.929  1.00 88.27           C\\nANISOU 2128  CE  MET A1106    13356   9694  10490     13    937   1471       C\\nATOM   2129  N   GLY A1107      36.219 -14.477  37.763  1.00 83.47           N\\nANISOU 2129  N   GLY A1107    12104   8844  10768   1383   1136   1249       N\\nATOM   2130  CA  GLY A1107      37.045 -14.923  36.668  1.00 86.98           C\\nANISOU 2130  CA  GLY A1107    12460   9202  11389   1617   1365   1006       C\\nATOM   2131  C   GLY A1107      36.292 -15.824  35.707  1.00 88.79           C\\nANISOU 2131  C   GLY A1107    13014   9179  11544   1543   1521    764       C\\nATOM   2132  O   GLY A1107      35.264 -16.426  36.027  1.00 86.13           O\\nANISOU 2132  O   GLY A1107    12973   8625  11128   1354   1409    824       O\\nATOM   2133  N   GLU A1108      36.843 -15.917  34.497  1.00 89.49           N\\nANISOU 2133  N   GLU A1108    13038   9319  11644   1667   1796    468       N\\nATOM   2134  CA  GLU A1108      36.262 -16.761  33.464  1.00 87.52           C\\nANISOU 2134  CA  GLU A1108    13103   8850  11300   1613   1951    163       C\\nATOM   2135  C   GLU A1108      36.230 -18.231  33.861  1.00 85.64           C\\nANISOU 2135  C   GLU A1108    13113   8070  11356   1798   1837    124       C\\nATOM   2136  O   GLU A1108      35.365 -18.973  33.377  1.00 84.49           O\\nANISOU 2136  O   GLU A1108    13313   7661  11130   1634   1842    -46       O\\nATOM   2137  CB  GLU A1108      37.029 -16.590  32.160  1.00 95.88           C\\nANISOU 2137  CB  GLU A1108    14037  10114  12279   1733   2303   -169       C\\nATOM   2138  CG  GLU A1108      36.931 -15.181  31.598  1.00102.62           C\\nANISOU 2138  CG  GLU A1108    14756  11443  12792   1470   2402   -100       C\\nATOM   2139  CD  GLU A1108      37.375 -15.104  30.157  1.00109.37           C\\nANISOU 2139  CD  GLU A1108    15629  12514  13413   1456   2771   -421       C\\nATOM   2140  OE1 GLU A1108      37.716 -16.168  29.591  1.00113.53           O\\nANISOU 2140  OE1 GLU A1108    16260  12832  14044   1672   2970   -764       O\\nATOM   2141  OE2 GLU A1108      37.380 -13.985  29.593  1.00105.41           O\\nANISOU 2141  OE2 GLU A1108    15063  12377  12612   1221   2859   -335       O\\nATOM   2142  N   THR A1109      37.155 -18.669  34.719  1.00 90.70           N\\nANISOU 2142  N   THR A1109    13597   8510  12353   2124   1695    286       N\\nATOM   2143  CA  THR A1109      37.120 -20.042  35.207  1.00 95.84           C\\nANISOU 2143  CA  THR A1109    14532   8571  13311   2298   1506    331       C\\nATOM   2144  C   THR A1109      35.855 -20.297  36.012  1.00 92.70           C\\nANISOU 2144  C   THR A1109    14477   8003  12741   1906   1273    629       C\\nATOM   2145  O   THR A1109      35.133 -21.269  35.766  1.00 95.09           O\\nANISOU 2145  O   THR A1109    15151   7895  13084   1765   1241    533       O\\nATOM   2146  CB  THR A1109      38.349 -20.335  36.066  1.00 97.86           C\\nANISOU 2146  CB  THR A1109    14535   8674  13974   2728   1309    517       C\\nATOM   2147  OG1 THR A1109      39.538 -19.920  35.381  1.00102.45           O\\nANISOU 2147  OG1 THR A1109    14672   9535  14718   3048   1561    242       O\\nATOM   2148  CG2 THR A1109      38.427 -21.828  36.376  1.00 97.85           C\\nANISOU 2148  CG2 THR A1109    14861   7969  14349   2976   1099    531       C\\nATOM   2149  N   GLY A1110      35.567 -19.420  36.975  1.00 95.75           N\\nANISOU 2149  N   GLY A1110    14731   8720  12931   1701   1128    965       N\\nATOM   2150  CA  GLY A1110      34.456 -19.660  37.880  1.00 94.88           C\\nANISOU 2150  CA  GLY A1110    14887   8513  12649   1331    949   1253       C\\nATOM   2151  C   GLY A1110      33.103 -19.552  37.204  1.00 88.67           C\\nANISOU 2151  C   GLY A1110    14261   7826  11602    922   1075   1072       C\\nATOM   2152  O   GLY A1110      32.191 -20.329  37.497  1.00 82.42           O\\nANISOU 2152  O   GLY A1110    13765   6760  10793    635    997   1160       O\\nATOM   2153  N   VAL A1111      32.952 -18.588  36.296  1.00 85.36           N\\nANISOU 2153  N   VAL A1111    13649   7799  10986    866   1244    836       N\\nATOM   2154  CA  VAL A1111      31.676 -18.422  35.606  1.00 83.59           C\\nANISOU 2154  CA  VAL A1111    13541   7694  10525    508   1297    660       C\\nATOM   2155  C   VAL A1111      31.371 -19.646  34.751  1.00 86.94           C\\nANISOU 2155  C   VAL A1111    14292   7686  11055    469   1346    385       C\\nATOM   2156  O   VAL A1111      30.217 -20.080  34.649  1.00 84.62           O\\nANISOU 2156  O   VAL A1111    14188   7281  10681    116   1284    338       O\\nATOM   2157  CB  VAL A1111      31.689 -17.125  34.776  1.00 78.72           C\\nANISOU 2157  CB  VAL A1111    12692   7539   9679    492   1403    508       C\\nATOM   2158  CG1 VAL A1111      30.403 -16.979  33.994  1.00 82.94           C\\nANISOU 2158  CG1 VAL A1111    13340   8183   9992    166   1385    324       C\\nATOM   2159  CG2 VAL A1111      31.894 -15.925  35.684  1.00 68.67           C\\nANISOU 2159  CG2 VAL A1111    11133   6621   8339    498   1317    755       C\\nATOM   2160  N   ALA A1112      32.402 -20.242  34.147  1.00 83.83           N\\nANISOU 2160  N   ALA A1112    13946   7039  10867    828   1457    166       N\\nATOM   2161  CA  ALA A1112      32.208 -21.434  33.331  1.00 86.95           C\\nANISOU 2161  CA  ALA A1112    14676   6976  11386    838   1502   -166       C\\nATOM   2162  C   ALA A1112      31.727 -22.636  34.137  1.00 97.68           C\\nANISOU 2162  C   ALA A1112    16361   7762  12989    696   1293     31       C\\nATOM   2163  O   ALA A1112      31.408 -23.672  33.541  1.00107.07           O\\nANISOU 2163  O   ALA A1112    17878   8495  14308    634   1283   -236       O\\nATOM   2164  CB  ALA A1112      33.504 -21.784  32.597  1.00 82.87           C\\nANISOU 2164  CB  ALA A1112    14088   6331  11068   1312   1699   -487       C\\nATOM   2165  N   GLY A1113      31.670 -22.528  35.467  1.00 94.08           N\\nANISOU 2165  N   GLY A1113    15859   7311  12576    613   1121    490       N\\nATOM   2166  CA  GLY A1113      31.127 -23.580  36.301  1.00 91.96           C\\nANISOU 2166  CA  GLY A1113    15934   6547  12461    374    924    767       C\\nATOM   2167  C   GLY A1113      29.632 -23.536  36.499  1.00 88.01           C\\nANISOU 2167  C   GLY A1113    15526   6189  11726   -228    907    854       C\\nATOM   2168  O   GLY A1113      29.067 -24.463  37.088  1.00 90.55           O\\nANISOU 2168  O   GLY A1113    16155   6098  12153   -532    780   1074       O\\nATOM   2169  N   PHE A1114      28.975 -22.477  36.030  1.00 89.32           N\\nANISOU 2169  N   PHE A1114    15419   6923  11597   -417   1020    697       N\\nATOM   2170  CA  PHE A1114      27.518 -22.347  36.101  1.00 93.06           C\\nANISOU 2170  CA  PHE A1114    15868   7604  11887   -955   1007    701       C\\nATOM   2171  C   PHE A1114      26.844 -22.935  34.867  1.00 97.68           C\\nANISOU 2171  C   PHE A1114    16640   7982  12490  -1154   1008    293       C\\nATOM   2172  O   PHE A1114      25.996 -22.294  34.250  1.00100.46           O\\nANISOU 2172  O   PHE A1114    16812   8720  12638  -1379   1016     94       O\\nATOM   2173  CB  PHE A1114      27.127 -20.883  36.266  1.00 94.49           C\\nANISOU 2173  CB  PHE A1114    15638   8468  11794  -1010   1062    728       C\\nATOM   2174  CG  PHE A1114      27.602 -20.258  37.542  1.00 95.33           C\\nANISOU 2174  CG  PHE A1114    15570   8818  11834   -900   1044   1086       C\\nATOM   2175  CD1 PHE A1114      26.863 -20.382  38.706  1.00 96.26           C\\nANISOU 2175  CD1 PHE A1114    15694   9032  11847  -1255   1023   1375       C\\nATOM   2176  CD2 PHE A1114      28.773 -19.521  37.572  1.00 93.76           C\\nANISOU 2176  CD2 PHE A1114    15190   8788  11647   -478   1057   1113       C\\nATOM   2177  CE1 PHE A1114      27.293 -19.799  39.881  1.00 93.49           C\\nANISOU 2177  CE1 PHE A1114    15219   8937  11366  -1170    999   1669       C\\nATOM   2178  CE2 PHE A1114      29.209 -18.933  38.743  1.00 90.99           C\\nANISOU 2178  CE2 PHE A1114    14688   8664  11219   -396    999   1410       C\\nATOM   2179  CZ  PHE A1114      28.468 -19.072  39.900  1.00 89.90           C\\nANISOU 2179  CZ  PHE A1114    14603   8619  10937   -731    961   1678       C\\nATOM   2180  N   THR A1115      27.213 -24.163  34.496  1.00 93.63           N\\nANISOU 2180  N   THR A1115    16502   6840  12234  -1062    963    146       N\\nATOM   2181  CA  THR A1115      26.755 -24.715  33.225  1.00 97.80           C\\nANISOU 2181  CA  THR A1115    17241   7160  12760  -1192    960   -325       C\\nATOM   2182  C   THR A1115      25.237 -24.821  33.175  1.00101.53           C\\nANISOU 2182  C   THR A1115    17699   7752  13126  -1809    862   -353       C\\nATOM   2183  O   THR A1115      24.618 -24.467  32.164  1.00100.69           O\\nANISOU 2183  O   THR A1115    17515   7914  12829  -1958    838   -694       O\\nATOM   2184  CB  THR A1115      27.395 -26.081  32.984  1.00104.56           C\\nANISOU 2184  CB  THR A1115    18523   7240  13966   -980    909   -494       C\\nATOM   2185  OG1 THR A1115      26.936 -27.010  33.974  1.00111.74           O\\nANISOU 2185  OG1 THR A1115    19700   7650  15106  -1304    745   -134       O\\nATOM   2186  CG2 THR A1115      28.912 -25.975  33.059  1.00103.25           C\\nANISOU 2186  CG2 THR A1115    18273   6991  13964   -334   1002   -493       C\\nATOM   2187  N   ASN A1116      24.617 -25.292  34.259  1.00109.01           N\\nANISOU 2187  N   ASN A1116    18703   8536  14180  -2193    797     12       N\\nATOM   2188  CA  ASN A1116      23.168 -25.450  34.256  1.00114.25           C\\nANISOU 2188  CA  ASN A1116    19286   9335  14790  -2821    734    -24       C\\nATOM   2189  C   ASN A1116      22.464 -24.103  34.180  1.00108.33           C\\nANISOU 2189  C   ASN A1116    18027   9368  13766  -2910    776    -69       C\\nATOM   2190  O   ASN A1116      21.401 -23.993  33.560  1.00112.39           O\\nANISOU 2190  O   ASN A1116    18389  10096  14219  -3257    688   -317       O\\nATOM   2191  CB  ASN A1116      22.716 -26.227  35.496  1.00119.12           C\\nANISOU 2191  CB  ASN A1116    20066   9646  15546  -3254    712    417       C\\nATOM   2192  N   SER A1117      23.040 -23.071  34.794  1.00107.10           N\\nANISOU 2192  N   SER A1117    17599   9621  13474  -2592    871    149       N\\nATOM   2193  CA  SER A1117      22.434 -21.748  34.719  1.00102.31           C\\nANISOU 2193  CA  SER A1117    16531   9686  12658  -2613    880     85       C\\nATOM   2194  C   SER A1117      22.674 -21.101  33.361  1.00102.29           C\\nANISOU 2194  C   SER A1117    16484   9870  12513  -2343    814   -265       C\\nATOM   2195  O   SER A1117      21.756 -20.507  32.785  1.00100.23           O\\nANISOU 2195  O   SER A1117    15984   9960  12139  -2521    696   -453       O\\nATOM   2196  CB  SER A1117      22.981 -20.857  35.835  1.00 98.47           C\\nANISOU 2196  CB  SER A1117    15811   9527  12076  -2381    982    404       C\\nATOM   2197  OG  SER A1117      22.892 -21.504  37.092  1.00 97.73           O\\nANISOU 2197  OG  SER A1117    15842   9258  12035  -2624   1039    761       O\\nATOM   2198  N   LEU A1118      23.897 -21.215  32.836  1.00104.26           N\\nANISOU 2198  N   LEU A1118    16951   9904  12761  -1923    883   -351       N\\nATOM   2199  CA  LEU A1118      24.243 -20.548  31.585  1.00100.23           C\\nANISOU 2199  CA  LEU A1118    16425   9622  12038  -1690    875   -637       C\\nATOM   2200  C   LEU A1118      23.389 -21.046  30.427  1.00107.73           C\\nANISOU 2200  C   LEU A1118    17547  10492  12892  -1976    724  -1011       C\\nATOM   2201  O   LEU A1118      23.041 -20.274  29.525  1.00110.02           O\\nANISOU 2201  O   LEU A1118    17736  11135  12931  -1982    613  -1185       O\\nATOM   2202  CB  LEU A1118      25.722 -20.757  31.279  1.00 92.05           C\\nANISOU 2202  CB  LEU A1118    15569   8366  11040  -1233   1041   -692       C\\nATOM   2203  CG  LEU A1118      26.695 -19.998  32.171  1.00 86.98           C\\nANISOU 2203  CG  LEU A1118    14695   7910  10443   -907   1144   -375       C\\nATOM   2204  CD1 LEU A1118      28.100 -20.549  32.003  1.00 86.56           C\\nANISOU 2204  CD1 LEU A1118    14792   7548  10551   -488   1291   -444       C\\nATOM   2205  CD2 LEU A1118      26.654 -18.516  31.846  1.00 86.67           C\\nANISOU 2205  CD2 LEU A1118    14359   8413  10159   -835   1133   -349       C\\nATOM   2206  N   ARG A1119      23.046 -22.333  30.429  1.00104.44           N\\nANISOU 2206  N   ARG A1119    17422   9590  12668  -2232    680  -1129       N\\nATOM   2207  CA  ARG A1119      22.191 -22.858  29.372  1.00103.70           C\\nANISOU 2207  CA  ARG A1119    17500   9406  12496  -2554    498  -1514       C\\nATOM   2208  C   ARG A1119      20.795 -22.250  29.433  1.00102.63           C\\nANISOU 2208  C   ARG A1119    16991   9707  12297  -2952    292  -1490       C\\nATOM   2209  O   ARG A1119      20.133 -22.113  28.398  1.00102.11           O\\nANISOU 2209  O   ARG A1119    16930   9811  12055  -3119     75  -1792       O\\nATOM   2210  CB  ARG A1119      22.123 -24.383  29.466  1.00105.66           C\\nANISOU 2210  CB  ARG A1119    18150   8971  13026  -2774    474  -1635       C\\nATOM   2211  CG  ARG A1119      21.461 -25.066  28.282  1.00110.68           C\\nANISOU 2211  CG  ARG A1119    19053   9414  13586  -3068    283  -2116       C\\nATOM   2212  CD  ARG A1119      21.400 -26.576  28.478  1.00119.37           C\\nANISOU 2212  CD  ARG A1119    20574   9750  15030  -3303    239  -2220       C\\nATOM   2213  NE  ARG A1119      20.881 -26.936  29.795  1.00121.59           N\\nANISOU 2213  NE  ARG A1119    20741   9865  15590  -3652    240  -1772       N\\nATOM   2214  CZ  ARG A1119      21.609 -27.484  30.763  1.00120.23           C\\nANISOU 2214  CZ  ARG A1119    20757   9256  15669  -3483    350  -1432       C\\nATOM   2215  NH1 ARG A1119      22.893 -27.748  30.561  1.00119.50           N\\nANISOU 2215  NH1 ARG A1119    20917   8831  15658  -2927    455  -1524       N\\nATOM   2216  NH2 ARG A1119      21.053 -27.772  31.933  1.00120.62           N\\nANISOU 2216  NH2 ARG A1119    20732   9219  15878  -3878    351  -1000       N\\nATOM   2217  N   MET A1120      20.338 -21.863  30.627  1.00100.48           N\\nANISOU 2217  N   MET A1120    16375   9649  12155  -3093    347  -1158       N\\nATOM   2218  CA  MET A1120      19.012 -21.263  30.756  1.00103.10           C\\nANISOU 2218  CA  MET A1120    16260  10430  12486  -3427    184  -1176       C\\nATOM   2219  C   MET A1120      19.000 -19.818  30.272  1.00100.31           C\\nANISOU 2219  C   MET A1120    15604  10594  11915  -3129     66  -1209       C\\nATOM   2220  O   MET A1120      18.009 -19.365  29.686  1.00100.24           O\\nANISOU 2220  O   MET A1120    15342  10888  11857  -3303   -198  -1388       O\\nATOM   2221  CB  MET A1120      18.535 -21.349  32.203  1.00106.18           C\\nANISOU 2221  CB  MET A1120    16380  10910  13054  -3686    341   -856       C\\nATOM   2222  CG  MET A1120      18.420 -22.776  32.714  1.00117.71           C\\nANISOU 2222  CG  MET A1120    18166  11832  14725  -4073    415   -750       C\\nATOM   2223  SD  MET A1120      17.789 -22.885  34.401  1.00123.98           S\\nANISOU 2223  SD  MET A1120    18683  12804  15620  -4485    629   -335       S\\nATOM   2224  CE  MET A1120      17.761 -24.663  34.625  1.00131.09           C\\nANISOU 2224  CE  MET A1120    20134  12916  16760  -4951    624   -214       C\\nATOM   2225  N   LEU A1121      20.082 -19.075  30.519  1.00100.35           N\\nANISOU 2225  N   LEU A1121    15626  10687  11815  -2692    222  -1026       N\\nATOM   2226  CA  LEU A1121      20.236 -17.769  29.884  1.00100.41           C\\nANISOU 2226  CA  LEU A1121    15473  11071  11608  -2415     91  -1049       C\\nATOM   2227  C   LEU A1121      20.299 -17.911  28.369  1.00105.95           C\\nANISOU 2227  C   LEU A1121    16480  11732  12045  -2411    -85  -1340       C\\nATOM   2228  O   LEU A1121      19.794 -17.057  27.629  1.00108.90           O\\nANISOU 2228  O   LEU A1121    16728  12416  12235  -2399   -355  -1411       O\\nATOM   2229  CB  LEU A1121      21.498 -17.077  30.396  1.00 89.96           C\\nANISOU 2229  CB  LEU A1121    14156   9787  10238  -2005    306   -807       C\\nATOM   2230  CG  LEU A1121      21.578 -16.711  31.874  1.00 82.79           C\\nANISOU 2230  CG  LEU A1121    12972   8988   9494  -1956    454   -522       C\\nATOM   2231  CD1 LEU A1121      22.975 -16.220  32.204  1.00 72.92           C\\nANISOU 2231  CD1 LEU A1121    11799   7708   8200  -1566    625   -331       C\\nATOM   2232  CD2 LEU A1121      20.549 -15.649  32.207  1.00 85.66           C\\nANISOU 2232  CD2 LEU A1121    12882   9776   9890  -2027    296   -524       C\\nATOM   2233  N   GLN A1122      20.920 -18.991  27.892  1.00 98.13           N\\nANISOU 2233  N   GLN A1122    15913  10351  11023  -2411     46  -1520       N\\nATOM   2234  CA  GLN A1122      21.020 -19.232  26.459  1.00 98.26           C\\nANISOU 2234  CA  GLN A1122    16271  10336  10727  -2427    -75  -1857       C\\nATOM   2235  C   GLN A1122      19.667 -19.584  25.852  1.00 96.39           C\\nANISOU 2235  C   GLN A1122    15998  10161  10466  -2846   -440  -2111       C\\nATOM   2236  O   GLN A1122      19.425 -19.301  24.674  1.00 98.68           O\\nANISOU 2236  O   GLN A1122    16445  10634  10417  -2889   -682  -2330       O\\nATOM   2237  CB  GLN A1122      22.036 -20.346  26.201  1.00103.05           C\\nANISOU 2237  CB  GLN A1122    17309  10483  11362  -2283    189  -2053       C\\nATOM   2238  CG  GLN A1122      22.347 -20.616  24.747  1.00107.55           C\\nANISOU 2238  CG  GLN A1122    18269  11042  11552  -2252    165  -2458       C\\nATOM   2239  CD  GLN A1122      23.447 -21.645  24.581  1.00111.75           C\\nANISOU 2239  CD  GLN A1122    19160  11128  12172  -2017    475  -2696       C\\nATOM   2240  OE1 GLN A1122      24.039 -22.100  25.559  1.00115.12           O\\nANISOU 2240  OE1 GLN A1122    19540  11237  12962  -1840    666  -2506       O\\nATOM   2241  NE2 GLN A1122      23.726 -22.017  23.338  1.00113.25           N\\nANISOU 2241  NE2 GLN A1122    19714  11294  12023  -1998    511  -3131       N\\nATOM   2242  N   GLN A1123      18.773 -20.184  26.639  1.00102.08           N\\nANISOU 2242  N   GLN A1123    16506  10761  11521  -3189   -495  -2073       N\\nATOM   2243  CA  GLN A1123      17.459 -20.603  26.168  1.00103.74           C\\nANISOU 2243  CA  GLN A1123    16604  11025  11786  -3643   -839  -2321       C\\nATOM   2244  C   GLN A1123      16.362 -19.590  26.496  1.00108.72           C\\nANISOU 2244  C   GLN A1123    16638  12153  12517  -3742  -1093  -2203       C\\nATOM   2245  O   GLN A1123      15.179 -19.947  26.486  1.00110.87           O\\nANISOU 2245  O   GLN A1123    16643  12510  12973  -4152  -1332  -2352       O\\nATOM   2246  CB  GLN A1123      17.101 -21.971  26.754  1.00101.84           C\\nANISOU 2246  CB  GLN A1123    16492  10326  11878  -4039   -744  -2378       C\\nATOM   2247  CG  GLN A1123      17.964 -23.119  26.251  1.00 99.00           C\\nANISOU 2247  CG  GLN A1123    16739   9389  11487  -3971   -604  -2613       C\\nATOM   2248  CD  GLN A1123      17.609 -24.442  26.905  1.00109.60           C\\nANISOU 2248  CD  GLN A1123    18244  10191  13208  -4372   -553  -2607       C\\nATOM   2249  OE1 GLN A1123      17.694 -24.589  28.124  1.00109.83           O\\nANISOU 2249  OE1 GLN A1123    18131  10108  13491  -4423   -352  -2243       O\\nATOM   2250  NE2 GLN A1123      17.200 -25.410  26.095  1.00111.61           N\\nANISOU 2250  NE2 GLN A1123    18833  10095  13478  -4692   -754  -3005       N\\nATOM   2251  N   LYS A1124      16.728 -18.344  26.794  1.00101.10           N\\nANISOU 2251  N   LYS A1124    15436  11503  11475  -3376  -1053  -1965       N\\nATOM   2252  CA  LYS A1124      15.801 -17.264  27.128  1.00102.00           C\\nANISOU 2252  CA  LYS A1124    14979  12055  11722  -3354  -1290  -1880       C\\nATOM   2253  C   LYS A1124      14.956 -17.560  28.362  1.00106.14           C\\nANISOU 2253  C   LYS A1124    15026  12671  12629  -3642  -1145  -1813       C\\nATOM   2254  O   LYS A1124      13.969 -16.858  28.613  1.00108.27           O\\nANISOU 2254  O   LYS A1124    14746  13316  13075  -3688  -1344  -1851       O\\nATOM   2255  CB  LYS A1124      14.875 -16.927  25.950  1.00104.85           C\\nANISOU 2255  CB  LYS A1124    15253  12649  11937  -3482  -1823  -2115       C\\nATOM   2256  CG  LYS A1124      15.585 -16.569  24.655  1.00106.34           C\\nANISOU 2256  CG  LYS A1124    15931  12827  11648  -3267  -1994  -2170       C\\nATOM   2257  CD  LYS A1124      16.318 -15.246  24.762  1.00102.53           C\\nANISOU 2257  CD  LYS A1124    15411  12521  11026  -2834  -1939  -1876       C\\nATOM   2258  CE  LYS A1124      16.710 -14.725  23.392  1.00104.63           C\\nANISOU 2258  CE  LYS A1124    16088  12882  10786  -2721  -2205  -1897       C\\nATOM   2259  NZ  LYS A1124      15.510 -14.429  22.560  1.00109.17           N\\nANISOU 2259  NZ  LYS A1124    16517  13684  11279  -2897  -2828  -2043       N\\nATOM   2260  N   ARG A1125      15.311 -18.583  29.142  1.00109.81           N\\nANISOU 2260  N   ARG A1125    15685  12809  13228  -3839   -806  -1713       N\\nATOM   2261  CA  ARG A1125      14.563 -18.937  30.349  1.00105.46           C\\nANISOU 2261  CA  ARG A1125    14749  12354  12966  -4188   -611  -1603       C\\nATOM   2262  C   ARG A1125      15.011 -18.038  31.502  1.00105.15           C\\nANISOU 2262  C   ARG A1125    14454  12555  12943  -3878   -338  -1327       C\\nATOM   2263  O   ARG A1125      15.645 -18.469  32.467  1.00102.11           O\\nANISOU 2263  O   ARG A1125    14245  11977  12576  -3884    -12  -1083       O\\nATOM   2264  CB  ARG A1125      14.757 -20.408  30.687  1.00100.56           C\\nANISOU 2264  CB  ARG A1125    14519  11232  12456  -4562   -413  -1558       C\\nATOM   2265  CG  ARG A1125      14.118 -21.370  29.702  1.00104.76           C\\nANISOU 2265  CG  ARG A1125    15255  11516  13034  -4972   -689  -1879       C\\nATOM   2266  CD  ARG A1125      14.117 -22.790  30.251  1.00109.68           C\\nANISOU 2266  CD  ARG A1125    16197  11614  13861  -5418   -505  -1800       C\\nATOM   2267  NE  ARG A1125      15.435 -23.419  30.187  1.00111.71           N\\nANISOU 2267  NE  ARG A1125    17086  11317  14042  -5114   -333  -1714       N\\nATOM   2268  CZ  ARG A1125      15.756 -24.551  30.807  1.00114.79           C\\nANISOU 2268  CZ  ARG A1125    17840  11156  14619  -5338   -166  -1549       C\\nATOM   2269  NH1 ARG A1125      14.859 -25.182  31.553  1.00117.33           N\\nANISOU 2269  NH1 ARG A1125    17995  11419  15168  -5934   -115  -1411       N\\nATOM   2270  NH2 ARG A1125      16.978 -25.051  30.689  1.00114.27           N\\nANISOU 2270  NH2 ARG A1125    18294  10594  14529  -4971    -54  -1512       N\\nATOM   2271  N   TRP A1126      14.657 -16.753  31.387  1.00102.43           N\\nANISOU 2271  N   TRP A1126    13702  12620  12595  -3599   -520  -1377       N\\nATOM   2272  CA  TRP A1126      15.103 -15.775  32.375  1.00 99.11           C\\nANISOU 2272  CA  TRP A1126    13061  12418  12179  -3267   -310  -1183       C\\nATOM   2273  C   TRP A1126      14.567 -16.088  33.763  1.00100.00           C\\nANISOU 2273  C   TRP A1126    12842  12708  12447  -3564     17  -1092       C\\nATOM   2274  O   TRP A1126      15.235 -15.807  34.763  1.00 95.88           O\\nANISOU 2274  O   TRP A1126    12367  12211  11852  -3395    296   -877       O\\nATOM   2275  CB  TRP A1126      14.683 -14.363  31.959  1.00 98.18           C\\nANISOU 2275  CB  TRP A1126    12566  12644  12092  -2934   -622  -1293       C\\nATOM   2276  CG  TRP A1126      15.001 -14.027  30.537  1.00 99.97           C\\nANISOU 2276  CG  TRP A1126    13108  12760  12116  -2737   -990  -1360       C\\nATOM   2277  CD1 TRP A1126      14.127 -13.586  29.588  1.00102.49           C\\nANISOU 2277  CD1 TRP A1126    13224  13259  12460  -2750  -1458  -1549       C\\nATOM   2278  CD2 TRP A1126      16.280 -14.113  29.895  1.00100.88           C\\nANISOU 2278  CD2 TRP A1126    13796  12592  11940  -2519   -920  -1236       C\\nATOM   2279  NE1 TRP A1126      14.782 -13.387  28.397  1.00102.69           N\\nANISOU 2279  NE1 TRP A1126    13720  13132  12164  -2582  -1684  -1520       N\\nATOM   2280  CE2 TRP A1126      16.105 -13.705  28.559  1.00102.48           C\\nANISOU 2280  CE2 TRP A1126    14155  12841  11942  -2447  -1322  -1348       C\\nATOM   2281  CE3 TRP A1126      17.558 -14.494  30.321  1.00101.84           C\\nANISOU 2281  CE3 TRP A1126    14288  12451  11954  -2377   -563  -1048       C\\nATOM   2282  CZ2 TRP A1126      17.157 -13.666  27.646  1.00107.44           C\\nANISOU 2282  CZ2 TRP A1126    15302  13297  12222  -2277  -1308  -1288       C\\nATOM   2283  CZ3 TRP A1126      18.601 -14.457  29.411  1.00101.67           C\\nANISOU 2283  CZ3 TRP A1126    14713  12253  11664  -2171   -560  -1020       C\\nATOM   2284  CH2 TRP A1126      18.393 -14.051  28.088  1.00104.96           C\\nANISOU 2284  CH2 TRP A1126    15284  12756  11842  -2142   -895  -1146       C\\nATOM   2285  N   ASP A1127      13.370 -16.667  33.848  1.00105.05           N\\nANISOU 2285  N   ASP A1127    13142  13500  13273  -4040    -10  -1251       N\\nATOM   2286  CA  ASP A1127      12.801 -16.985  35.152  1.00105.65           C\\nANISOU 2286  CA  ASP A1127    12891  13805  13446  -4403    350  -1159       C\\nATOM   2287  C   ASP A1127      13.638 -18.034  35.873  1.00102.58           C\\nANISOU 2287  C   ASP A1127    13044  13002  12929  -4604    661   -828       C\\nATOM   2288  O   ASP A1127      14.085 -17.819  37.005  1.00 97.10           O\\nANISOU 2288  O   ASP A1127    12362  12413  12117  -4531    958   -598       O\\nATOM   2289  CB  ASP A1127      11.355 -17.458  34.988  1.00113.14           C\\nANISOU 2289  CB  ASP A1127    13346  15002  14642  -4937    260  -1403       C\\nATOM   2290  N   GLU A1128      13.877 -19.175  35.221  1.00105.05           N\\nANISOU 2290  N   GLU A1128    13834  12818  13263  -4840    560   -812       N\\nATOM   2291  CA  GLU A1128      14.589 -20.266  35.881  1.00101.37           C\\nANISOU 2291  CA  GLU A1128    13890  11878  12749  -5036    788   -497       C\\nATOM   2292  C   GLU A1128      16.064 -19.940  36.072  1.00 98.59           C\\nANISOU 2292  C   GLU A1128    13939  11292  12227  -4482    856   -278       C\\nATOM   2293  O   GLU A1128      16.652 -20.294  37.101  1.00 98.75           O\\nANISOU 2293  O   GLU A1128    14183  11164  12175  -4507   1075     48       O\\nATOM   2294  CB  GLU A1128      14.433 -21.557  35.083  1.00102.72           C\\nANISOU 2294  CB  GLU A1128    14465  11516  13047  -5400    625   -601       C\\nATOM   2295  CG  GLU A1128      13.004 -22.014  34.909  1.00109.16           C\\nANISOU 2295  CG  GLU A1128    14894  12518  14063  -6031    538   -807       C\\nATOM   2296  CD  GLU A1128      12.920 -23.465  34.496  1.00117.05           C\\nANISOU 2296  CD  GLU A1128    16374  12895  15205  -6501    444   -827       C\\nATOM   2297  OE1 GLU A1128      13.445 -24.324  35.236  1.00119.18           O\\nANISOU 2297  OE1 GLU A1128    17078  12716  15487  -6681    639   -499       O\\nATOM   2298  OE2 GLU A1128      12.343 -23.744  33.426  1.00122.20           O\\nANISOU 2298  OE2 GLU A1128    16997  13477  15956  -6685    137  -1171       O\\nATOM   2299  N   ALA A1129      16.686 -19.280  35.090  1.00106.39           N\\nANISOU 2299  N   ALA A1129    15026  12259  13140  -4007    658   -438       N\\nATOM   2300  CA  ALA A1129      18.089 -18.904  35.232  1.00 98.44           C\\nANISOU 2300  CA  ALA A1129    14315  11087  12002  -3503    734   -256       C\\nATOM   2301  C   ALA A1129      18.313 -18.065  36.481  1.00 99.96           C\\nANISOU 2301  C   ALA A1129    14247  11624  12110  -3345    925    -40       C\\nATOM   2302  O   ALA A1129      19.394 -18.111  37.080  1.00 91.71           O\\nANISOU 2302  O   ALA A1129    13458  10403  10986  -3100   1037    208       O\\nATOM   2303  CB  ALA A1129      18.562 -18.146  33.991  1.00 90.27           C\\nANISOU 2303  CB  ALA A1129    13335  10100  10864  -3097    524   -462       C\\nATOM   2304  N   ALA A1130      17.300 -17.301  36.894  1.00101.90           N\\nANISOU 2304  N   ALA A1130    13969  12366  12382  -3472    950   -165       N\\nATOM   2305  CA  ALA A1130      17.396 -16.557  38.143  1.00100.47           C\\nANISOU 2305  CA  ALA A1130    13541  12535  12097  -3370   1159    -30       C\\nATOM   2306  C   ALA A1130      17.236 -17.478  39.344  1.00 96.24           C\\nANISOU 2306  C   ALA A1130    13135  11951  11481  -3804   1437    243       C\\nATOM   2307  O   ALA A1130      17.958 -17.340  40.339  1.00 91.99           O\\nANISOU 2307  O   ALA A1130    12752  11434  10767  -3682   1586    498       O\\nATOM   2308  CB  ALA A1130      16.348 -15.446  38.172  1.00102.74           C\\nANISOU 2308  CB  ALA A1130    13205  13359  12471  -3324   1106   -319       C\\nATOM   2309  N   VAL A1131      16.303 -18.428  39.267  1.00 92.07           N\\nANISOU 2309  N   VAL A1131    12568  11350  11062  -4347   1484    213       N\\nATOM   2310  CA  VAL A1131      16.030 -19.294  40.409  1.00 92.71           C\\nANISOU 2310  CA  VAL A1131    12779  11404  11044  -4858   1755    513       C\\nATOM   2311  C   VAL A1131      17.210 -20.220  40.681  1.00 93.11           C\\nANISOU 2311  C   VAL A1131    13506  10845  11028  -4781   1726    899       C\\nATOM   2312  O   VAL A1131      17.533 -20.509  41.839  1.00 94.49           O\\nANISOU 2312  O   VAL A1131    13879  11018  11005  -4935   1900   1255       O\\nATOM   2313  CB  VAL A1131      14.728 -20.083  40.179  1.00 91.93           C\\nANISOU 2313  CB  VAL A1131    12455  11353  11120  -5514   1797    386       C\\nATOM   2314  N   ASN A1132      17.877 -20.696  39.626  1.00 98.73           N\\nANISOU 2314  N   ASN A1132    14580  11039  11893  -4528   1494    823       N\\nATOM   2315  CA  ASN A1132      19.028 -21.572  39.827  1.00 99.57           C\\nANISOU 2315  CA  ASN A1132    15279  10537  12016  -4371   1439   1132       C\\nATOM   2316  C   ASN A1132      20.208 -20.804  40.407  1.00 98.88           C\\nANISOU 2316  C   ASN A1132    15239  10564  11768  -3840   1452   1311       C\\nATOM   2317  O   ASN A1132      20.866 -21.282  41.338  1.00106.13           O\\nANISOU 2317  O   ASN A1132    16469  11262  12593  -3844   1482   1689       O\\nATOM   2318  CB  ASN A1132      19.417 -22.244  38.508  1.00100.70           C\\nANISOU 2318  CB  ASN A1132    15748  10141  12372  -4206   1226    906       C\\nATOM   2319  CG  ASN A1132      20.355 -23.432  38.702  1.00102.63           C\\nANISOU 2319  CG  ASN A1132    16592   9660  12743  -4136   1159   1173       C\\nATOM   2320  OD1 ASN A1132      21.259 -23.402  39.538  1.00 99.29           O\\nANISOU 2320  OD1 ASN A1132    16345   9141  12242  -3883   1185   1501       O\\nATOM   2321  ND2 ASN A1132      20.136 -24.489  37.929  1.00107.31           N\\nANISOU 2321  ND2 ASN A1132    17502   9719  13554  -4348   1034   1014       N\\nATOM   2322  N   LEU A1133      20.483 -19.606  39.881  1.00 85.10           N\\nANISOU 2322  N   LEU A1133    13195   9149   9988  -3405   1394   1062       N\\nATOM   2323  CA  LEU A1133      21.652 -18.849  40.317  1.00 79.83           C\\nANISOU 2323  CA  LEU A1133    12558   8566   9209  -2920   1377   1196       C\\nATOM   2324  C   LEU A1133      21.591 -18.470  41.792  1.00 85.06           C\\nANISOU 2324  C   LEU A1133    13112   9576   9629  -3048   1529   1445       C\\nATOM   2325  O   LEU A1133      22.638 -18.221  42.399  1.00 82.43           O\\nANISOU 2325  O   LEU A1133    12927   9198   9193  -2748   1484   1656       O\\nATOM   2326  CB  LEU A1133      21.813 -17.596  39.454  1.00 84.72           C\\nANISOU 2326  CB  LEU A1133    12879   9469   9842  -2527   1283    893       C\\nATOM   2327  CG  LEU A1133      22.459 -17.798  38.079  1.00 88.21           C\\nANISOU 2327  CG  LEU A1133    13529   9583  10405  -2245   1143    716       C\\nATOM   2328  CD1 LEU A1133      22.334 -16.537  37.242  1.00 90.94           C\\nANISOU 2328  CD1 LEU A1133    13587  10258  10710  -1997   1039    463       C\\nATOM   2329  CD2 LEU A1133      23.920 -18.203  38.219  1.00 83.43           C\\nANISOU 2329  CD2 LEU A1133    13242   8615   9844  -1895   1135    911       C\\nATOM   2330  N   ALA A1134      20.399 -18.433  42.386  1.00 84.49           N\\nANISOU 2330  N   ALA A1134    12774   9880   9449  -3501   1713   1404       N\\nATOM   2331  CA  ALA A1134      20.263 -18.129  43.804  1.00 83.30           C\\nANISOU 2331  CA  ALA A1134    12544  10115   8992  -3684   1912   1604       C\\nATOM   2332  C   ALA A1134      20.570 -19.322  44.697  1.00 95.28           C\\nANISOU 2332  C   ALA A1134    14547  11297  10359  -4027   1952   2087       C\\nATOM   2333  O   ALA A1134      20.536 -19.181  45.925  1.00100.46           O\\nANISOU 2333  O   ALA A1134    15234  12260  10675  -4222   2106   2315       O\\nATOM   2334  CB  ALA A1134      18.855 -17.614  44.103  1.00 88.70           C\\nANISOU 2334  CB  ALA A1134    12701  11389   9612  -4038   2147   1331       C\\nATOM   2335  N   LYS A1135      20.860 -20.486  44.116  1.00 88.10           N\\nANISOU 2335  N   LYS A1135    14044   9751   9678  -4109   1800   2243       N\\nATOM   2336  CA  LYS A1135      21.205 -21.680  44.871  1.00 87.20           C\\nANISOU 2336  CA  LYS A1135    14461   9179   9491  -4398   1755   2737       C\\nATOM   2337  C   LYS A1135      22.701 -21.967  44.852  1.00 86.32           C\\nANISOU 2337  C   LYS A1135    14744   8566   9488  -3866   1479   2966       C\\nATOM   2338  O   LYS A1135      23.109 -23.103  45.109  1.00102.38           O\\nANISOU 2338  O   LYS A1135    17270  10011  11619  -3979   1327   3328       O\\nATOM   2339  CB  LYS A1135      20.432 -22.884  44.332  1.00 91.82           C\\nANISOU 2339  CB  LYS A1135    15253   9320  10313  -4902   1752   2756       C\\nATOM   2340  N   SER A1136      23.523 -20.968  44.553  1.00 82.36           N\\nANISOU 2340  N   SER A1136    14022   8267   9005  -3296   1395   2765       N\\nATOM   2341  CA  SER A1136      24.959 -21.160  44.431  1.00 83.52           C\\nANISOU 2341  CA  SER A1136    14419   8004   9312  -2765   1149   2911       C\\nATOM   2342  C   SER A1136      25.684 -20.619  45.656  1.00 88.67           C\\nANISOU 2342  C   SER A1136    15092   8930   9667  -2607   1075   3205       C\\nATOM   2343  O   SER A1136      25.148 -19.816  46.424  1.00 92.03           O\\nANISOU 2343  O   SER A1136    15281   9935   9752  -2806   1240   3175       O\\nATOM   2344  CB  SER A1136      25.494 -20.477  43.171  1.00 79.24           C\\nANISOU 2344  CB  SER A1136    13626   7476   9007  -2270   1101   2495       C\\nATOM   2345  OG  SER A1136      25.423 -19.068  43.285  1.00 73.97           O\\nANISOU 2345  OG  SER A1136    12540   7401   8165  -2108   1183   2288       O\\nATOM   2346  N   ARG A1137      26.926 -21.078  45.832  1.00 91.39           N\\nANISOU 2346  N   ARG A1137    15712   8855  10158  -2229    806   3459       N\\nATOM   2347  CA  ARG A1137      27.767 -20.540  46.894  1.00 91.41           C\\nANISOU 2347  CA  ARG A1137    15721   9100   9909  -2019    652   3712       C\\nATOM   2348  C   ARG A1137      28.177 -19.101  46.613  1.00 85.85           C\\nANISOU 2348  C   ARG A1137    14558   8882   9179  -1656    695   3357       C\\nATOM   2349  O   ARG A1137      28.655 -18.413  47.521  1.00 85.58           O\\nANISOU 2349  O   ARG A1137    14453   9182   8883  -1561    604   3470       O\\nATOM   2350  CB  ARG A1137      29.009 -21.414  47.089  1.00 94.63           C\\nANISOU 2350  CB  ARG A1137    16484   8915  10557  -1666    293   4057       C\\nATOM   2351  N   TRP A1138      28.013 -18.639  45.372  1.00 85.61           N\\nANISOU 2351  N   TRP A1138    14253   8876   9400  -1476    803   2943       N\\nATOM   2352  CA  TRP A1138      28.240 -17.235  45.053  1.00 83.05           C\\nANISOU 2352  CA  TRP A1138    13523   8984   9049  -1214    846   2628       C\\nATOM   2353  C   TRP A1138      27.118 -16.360  45.596  1.00 83.65           C\\nANISOU 2353  C   TRP A1138    13343   9618   8821  -1522   1044   2460       C\\nATOM   2354  O   TRP A1138      27.378 -15.303  46.181  1.00 74.31           O\\nANISOU 2354  O   TRP A1138    11960   8813   7461  -1395   1022   2377       O\\nATOM   2355  CB  TRP A1138      28.387 -17.069  43.541  1.00 81.72           C\\nANISOU 2355  CB  TRP A1138    13205   8653   9191   -970    885   2291       C\\nATOM   2356  CG  TRP A1138      28.200 -15.675  43.038  1.00 80.37           C\\nANISOU 2356  CG  TRP A1138    12659   8893   8984   -845    952   1971       C\\nATOM   2357  CD1 TRP A1138      29.008 -14.601  43.270  1.00 79.75           C\\nANISOU 2357  CD1 TRP A1138    12375   9046   8880   -571    866   1931       C\\nATOM   2358  CD2 TRP A1138      27.151 -15.209  42.179  1.00 79.40           C\\nANISOU 2358  CD2 TRP A1138    12339   8950   8882   -990   1065   1659       C\\nATOM   2359  NE1 TRP A1138      28.520 -13.492  42.620  1.00 74.10           N\\nANISOU 2359  NE1 TRP A1138    11385   8600   8171   -543    925   1634       N\\nATOM   2360  CE2 TRP A1138      27.381 -13.840  41.944  1.00 77.74           C\\nANISOU 2360  CE2 TRP A1138    11841   9040   8657   -775   1031   1470       C\\nATOM   2361  CE3 TRP A1138      26.036 -15.814  41.592  1.00 70.14           C\\nANISOU 2361  CE3 TRP A1138    11201   7697   7754  -1292   1152   1527       C\\nATOM   2362  CZ2 TRP A1138      26.539 -13.069  41.149  1.00 75.61           C\\nANISOU 2362  CZ2 TRP A1138    11345   8968   8416   -815   1054   1185       C\\nATOM   2363  CZ3 TRP A1138      25.201 -15.044  40.801  1.00 72.99           C\\nANISOU 2363  CZ3 TRP A1138    11290   8307   8136  -1332   1174   1217       C\\nATOM   2364  CH2 TRP A1138      25.457 -13.689  40.588  1.00 72.54           C\\nANISOU 2364  CH2 TRP A1138    10974   8524   8064  -1078   1113   1063       C\\nATOM   2365  N   TYR A1139      25.867 -16.790  45.424  1.00 82.65           N\\nANISOU 2365  N   TYR A1139    13198   9549   8658  -1927   1233   2375       N\\nATOM   2366  CA  TYR A1139      24.743 -16.053  45.987  1.00 86.12           C\\nANISOU 2366  CA  TYR A1139    13337  10541   8845  -2219   1452   2182       C\\nATOM   2367  C   TYR A1139      24.771 -16.040  47.509  1.00 83.42           C\\nANISOU 2367  C   TYR A1139    13129  10492   8073  -2444   1516   2445       C\\nATOM   2368  O   TYR A1139      24.214 -15.122  48.120  1.00 85.20           O\\nANISOU 2368  O   TYR A1139    13075  11244   8055  -2528   1680   2223       O\\nATOM   2369  CB  TYR A1139      23.424 -16.647  45.483  1.00 93.06           C\\nANISOU 2369  CB  TYR A1139    14126  11418   9815  -2639   1632   2048       C\\nATOM   2370  CG  TYR A1139      22.187 -15.947  45.998  1.00 97.27           C\\nANISOU 2370  CG  TYR A1139    14256  12545  10156  -2931   1887   1793       C\\nATOM   2371  CD1 TYR A1139      21.714 -14.791  45.393  1.00 97.09           C\\nANISOU 2371  CD1 TYR A1139    13784  12829  10275  -2703   1891   1360       C\\nATOM   2372  CD2 TYR A1139      21.487 -16.449  47.086  1.00101.31           C\\nANISOU 2372  CD2 TYR A1139    14831  13310  10352  -3435   2125   1984       C\\nATOM   2373  CE1 TYR A1139      20.582 -14.152  45.862  1.00 98.45           C\\nANISOU 2373  CE1 TYR A1139    13534  13534  10340  -2906   2113   1072       C\\nATOM   2374  CE2 TYR A1139      20.357 -15.817  47.560  1.00102.23           C\\nANISOU 2374  CE2 TYR A1139    14515  14020  10307  -3689   2412   1691       C\\nATOM   2375  CZ  TYR A1139      19.909 -14.671  46.946  1.00 98.03           C\\nANISOU 2375  CZ  TYR A1139    13492  13774   9981  -3392   2400   1210       C\\nATOM   2376  OH  TYR A1139      18.781 -14.044  47.424  1.00 96.25           O\\nANISOU 2376  OH  TYR A1139    12784  14130   9656  -3586   2677    868       O\\nATOM   2377  N   ASN A1140      25.410 -17.028  48.134  1.00 84.98           N\\nANISOU 2377  N   ASN A1140    13766  10358   8165  -2531   1372   2902       N\\nATOM   2378  CA  ASN A1140      25.511 -17.069  49.585  1.00 81.09           C\\nANISOU 2378  CA  ASN A1140    13485  10139   7189  -2767   1384   3212       C\\nATOM   2379  C   ASN A1140      26.720 -16.316  50.123  1.00 81.14           C\\nANISOU 2379  C   ASN A1140    13495  10255   7081  -2354   1121   3259       C\\nATOM   2380  O   ASN A1140      26.732 -15.963  51.308  1.00 91.34           O\\nANISOU 2380  O   ASN A1140    14868  11933   7905  -2514   1139   3371       O\\nATOM   2381  CB  ASN A1140      25.564 -18.521  50.073  1.00 83.93           C\\nANISOU 2381  CB  ASN A1140    14351  10066   7474  -3090   1289   3738       C\\nATOM   2382  CG  ASN A1140      24.263 -19.268  49.834  1.00 88.69           C\\nANISOU 2382  CG  ASN A1140    14898  10646   8154  -3583   1553   3682       C\\nATOM   2383  OD1 ASN A1140      23.328 -19.182  50.631  1.00 94.13           O\\nANISOU 2383  OD1 ASN A1140    15427  11795   8542  -3964   1814   3633       O\\nATOM   2384  ND2 ASN A1140      24.203 -20.015  48.739  1.00 88.26           N\\nANISOU 2384  ND2 ASN A1140    14971  10056   8508  -3583   1485   3663       N\\nATOM   2385  N   GLN A1141      27.731 -16.058  49.292  1.00 79.05           N\\nANISOU 2385  N   GLN A1141    13135   9692   7209  -1861    889   3159       N\\nATOM   2386  CA  GLN A1141      28.944 -15.389  49.751  1.00 83.34           C\\nANISOU 2386  CA  GLN A1141    13640  10316   7710  -1493    612   3207       C\\nATOM   2387  C   GLN A1141      28.857 -13.872  49.622  1.00 86.83           C\\nANISOU 2387  C   GLN A1141    13669  11193   8130  -1321    691   2761       C\\nATOM   2388  O   GLN A1141      29.270 -13.148  50.534  1.00 90.33           O\\nANISOU 2388  O   GLN A1141    14085  11948   8290  -1274    578   2742       O\\nATOM   2389  CB  GLN A1141      30.158 -15.908  48.974  1.00 81.76           C\\nANISOU 2389  CB  GLN A1141    13505   9595   7966  -1066    339   3330       C\\nATOM   2390  N   THR A1142      28.341 -13.378  48.497  1.00 81.15           N\\nANISOU 2390  N   THR A1142    12660  10468   7708  -1228    841   2404       N\\nATOM   2391  CA  THR A1142      28.099 -11.952  48.276  1.00 75.62           C\\nANISOU 2391  CA  THR A1142    11594  10099   7040  -1081    896   1987       C\\nATOM   2392  C   THR A1142      26.654 -11.815  47.825  1.00 80.15           C\\nANISOU 2392  C   THR A1142    11953  10861   7638  -1313   1170   1698       C\\nATOM   2393  O   THR A1142      26.373 -11.645  46.629  1.00 76.21           O\\nANISOU 2393  O   THR A1142    11292  10208   7456  -1195   1180   1504       O\\nATOM   2394  CB  THR A1142      29.064 -11.368  47.245  1.00 71.01           C\\nANISOU 2394  CB  THR A1142    10854   9291   6836   -689    721   1873       C\\nATOM   2395  OG1 THR A1142      28.852 -12.004  45.979  1.00 61.90           O\\nANISOU 2395  OG1 THR A1142     9720   7819   5981   -656    792   1847       O\\nATOM   2396  CG2 THR A1142      30.507 -11.581  47.678  1.00 64.20           C\\nANISOU 2396  CG2 THR A1142    10120   8261   6011   -463    447   2144       C\\nATOM   2397  N   PRO A1143      25.702 -11.890  48.760  1.00 78.66           N\\nANISOU 2397  N   PRO A1143    11743  11039   7106  -1659   1396   1658       N\\nATOM   2398  CA  PRO A1143      24.288 -11.947  48.355  1.00 77.44           C\\nANISOU 2398  CA  PRO A1143    11332  11073   7019  -1917   1663   1400       C\\nATOM   2399  C   PRO A1143      23.754 -10.645  47.786  1.00 81.38           C\\nANISOU 2399  C   PRO A1143    11396  11793   7731  -1681   1672    913       C\\nATOM   2400  O   PRO A1143      22.964 -10.679  46.836  1.00 67.23           O\\nANISOU 2400  O   PRO A1143     9390   9947   6208  -1709   1715    723       O\\nATOM   2401  CB  PRO A1143      23.575 -12.337  49.655  1.00 74.02           C\\nANISOU 2401  CB  PRO A1143    10976  11033   6115  -2363   1931   1502       C\\nATOM   2402  CG  PRO A1143      24.484 -11.856  50.733  1.00 74.95           C\\nANISOU 2402  CG  PRO A1143    11275  11318   5883  -2235   1792   1614       C\\nATOM   2403  CD  PRO A1143      25.873 -12.037  50.213  1.00 80.85           C\\nANISOU 2403  CD  PRO A1143    12236  11590   6893  -1870   1423   1866       C\\nATOM   2404  N   ASN A1144      24.148  -9.498  48.346  1.00 79.84           N\\nANISOU 2404  N   ASN A1144    11080  11820   7435  -1453   1593    702       N\\nATOM   2405  CA  ASN A1144      23.656  -8.219  47.839  1.00 82.18           C\\nANISOU 2405  CA  ASN A1144    11000  12248   7977  -1203   1550    249       C\\nATOM   2406  C   ASN A1144      24.024  -8.031  46.372  1.00 83.32           C\\nANISOU 2406  C   ASN A1144    11122  12002   8536   -947   1323    262       C\\nATOM   2407  O   ASN A1144      23.168  -7.712  45.538  1.00 77.89           O\\nANISOU 2407  O   ASN A1144    10184  11322   8089   -907   1317     25       O\\nATOM   2408  CB  ASN A1144      24.209  -7.072  48.683  1.00 86.17           C\\nANISOU 2408  CB  ASN A1144    11466  12947   8328   -999   1448     44       C\\nATOM   2409  CG  ASN A1144      23.399  -6.831  49.942  1.00 91.58           C\\nANISOU 2409  CG  ASN A1144    12020  14149   8626  -1210   1730   -220       C\\nATOM   2410  OD1 ASN A1144      22.445  -6.054  49.938  1.00 89.43           O\\nANISOU 2410  OD1 ASN A1144    11378  14135   8467  -1137   1861   -680       O\\nATOM   2411  ND2 ASN A1144      23.778  -7.496  51.028  1.00 95.06           N\\nANISOU 2411  ND2 ASN A1144    12763  14756   8600  -1466   1818     62       N\\nATOM   2412  N   ARG A1145      25.302  -8.228  46.040  1.00 83.54           N\\nANISOU 2412  N   ARG A1145    11397  11711   8633   -780   1132    536       N\\nATOM   2413  CA  ARG A1145      25.740  -8.103  44.655  1.00 77.75           C\\nANISOU 2413  CA  ARG A1145    10673  10652   8215   -579    973    561       C\\nATOM   2414  C   ARG A1145      25.101  -9.167  43.774  1.00 76.82           C\\nANISOU 2414  C   ARG A1145    10624  10365   8200   -753   1062    630       C\\nATOM   2415  O   ARG A1145      24.721  -8.887  42.631  1.00 82.58           O\\nANISOU 2415  O   ARG A1145    11252  10993   9130   -675    981    488       O\\nATOM   2416  CB  ARG A1145      27.264  -8.189  44.587  1.00 73.67           C\\nANISOU 2416  CB  ARG A1145    10353   9896   7744   -393    814    816       C\\nATOM   2417  CG  ARG A1145      27.829  -8.227  43.179  1.00 69.75           C\\nANISOU 2417  CG  ARG A1145     9893   9104   7505   -234    729    865       C\\nATOM   2418  CD  ARG A1145      29.352  -8.232  43.189  1.00 73.59           C\\nANISOU 2418  CD  ARG A1145    10468   9428   8064    -50    612   1067       C\\nATOM   2419  NE  ARG A1145      29.897  -8.135  41.837  1.00 80.75           N\\nANISOU 2419  NE  ARG A1145    11375  10131   9175     79    594   1070       N\\nATOM   2420  CZ  ARG A1145      31.175  -7.901  41.556  1.00 82.83           C\\nANISOU 2420  CZ  ARG A1145    11612  10298   9561    237    528   1175       C\\nATOM   2421  NH1 ARG A1145      32.054  -7.734  42.535  1.00 82.57           N\\nANISOU 2421  NH1 ARG A1145    11535  10328   9508    307    415   1287       N\\nATOM   2422  NH2 ARG A1145      31.574  -7.829  40.293  1.00 85.74           N\\nANISOU 2422  NH2 ARG A1145    11982  10541  10053    302    578   1158       N\\nATOM   2423  N   ALA A1146      24.974 -10.393  44.287  1.00 78.38           N\\nANISOU 2423  N   ALA A1146    11025  10507   8249  -1011   1196    857       N\\nATOM   2424  CA  ALA A1146      24.412 -11.480  43.491  1.00 77.28           C\\nANISOU 2424  CA  ALA A1146    10992  10148   8224  -1212   1259    913       C\\nATOM   2425  C   ALA A1146      22.965 -11.191  43.114  1.00 83.69           C\\nANISOU 2425  C   ALA A1146    11482  11202   9113  -1389   1341    610       C\\nATOM   2426  O   ALA A1146      22.575 -11.340  41.951  1.00 81.20           O\\nANISOU 2426  O   ALA A1146    11127  10738   8988  -1380   1252    495       O\\nATOM   2427  CB  ALA A1146      24.519 -12.800  44.253  1.00 75.31           C\\nANISOU 2427  CB  ALA A1146    11049   9751   7813  -1491   1359   1239       C\\nATOM   2428  N   LYS A1147      22.154 -10.771  44.090  1.00 81.29           N\\nANISOU 2428  N   LYS A1147    10927  11303   8657  -1547   1506    451       N\\nATOM   2429  CA  LYS A1147      20.760 -10.442  43.804  1.00 80.52           C\\nANISOU 2429  CA  LYS A1147    10420  11486   8686  -1680   1585    116       C\\nATOM   2430  C   LYS A1147      20.649  -9.302  42.799  1.00 83.83           C\\nANISOU 2430  C   LYS A1147    10611  11866   9377  -1325   1329   -152       C\\nATOM   2431  O   LYS A1147      19.710  -9.273  41.995  1.00 68.30           O\\nANISOU 2431  O   LYS A1147     8403   9940   7609  -1375   1246   -350       O\\nATOM   2432  CB  LYS A1147      20.023 -10.088  45.098  1.00 67.35           C\\nANISOU 2432  CB  LYS A1147     8483  10311   6797  -1863   1853    -63       C\\nATOM   2433  N   ARG A1148      21.599  -8.365  42.815  1.00 85.54           N\\nANISOU 2433  N   ARG A1148    10910  11984   9606   -988   1167   -140       N\\nATOM   2434  CA  ARG A1148      21.574  -7.277  41.842  1.00 79.68           C\\nANISOU 2434  CA  ARG A1148    10031  11139   9107   -685    892   -317       C\\nATOM   2435  C   ARG A1148      21.891  -7.783  40.437  1.00 82.33           C\\nANISOU 2435  C   ARG A1148    10589  11152   9539   -673    733   -165       C\\nATOM   2436  O   ARG A1148      21.289  -7.330  39.457  1.00 90.33           O\\nANISOU 2436  O   ARG A1148    11469  12136  10717   -591    526   -312       O\\nATOM   2437  CB  ARG A1148      22.555  -6.182  42.261  1.00 70.66           C\\nANISOU 2437  CB  ARG A1148     8952   9944   7952   -403    768   -316       C\\nATOM   2438  CG  ARG A1148      21.892  -4.860  42.620  1.00 71.12           C\\nANISOU 2438  CG  ARG A1148     8676  10192   8155   -198    669   -688       C\\nATOM   2439  CD  ARG A1148      22.475  -4.260  43.892  1.00 73.19           C\\nANISOU 2439  CD  ARG A1148     8962  10601   8247   -122    743   -769       C\\nATOM   2440  NE  ARG A1148      23.934  -4.303  43.899  1.00 73.07           N\\nANISOU 2440  NE  ARG A1148     9271  10346   8145    -63    641   -461       N\\nATOM   2441  CZ  ARG A1148      24.686  -4.003  44.953  1.00 72.04           C\\nANISOU 2441  CZ  ARG A1148     9236  10306   7829    -40    656   -444       C\\nATOM   2442  NH1 ARG A1148      24.121  -3.632  46.093  1.00 77.77           N\\nANISOU 2442  NH1 ARG A1148     9809  11363   8378    -79    795   -729       N\\nATOM   2443  NH2 ARG A1148      26.005  -4.075  44.867  1.00 70.75           N\\nANISOU 2443  NH2 ARG A1148     9301   9933   7647     15    532   -167       N\\nATOM   2444  N   VAL A1149      22.824  -8.727  40.321  1.00 86.59           N\\nANISOU 2444  N   VAL A1149    11473  11454   9974   -742    812    112       N\\nATOM   2445  CA  VAL A1149      23.201  -9.252  39.011  1.00 82.53           C\\nANISOU 2445  CA  VAL A1149    11189  10655   9513   -723    713    200       C\\nATOM   2446  C   VAL A1149      22.160 -10.240  38.500  1.00 89.46           C\\nANISOU 2446  C   VAL A1149    12052  11515  10424  -1007    747    112       C\\nATOM   2447  O   VAL A1149      21.841 -10.260  37.304  1.00 88.71           O\\nANISOU 2447  O   VAL A1149    11995  11326  10387  -1003    583     17       O\\nATOM   2448  CB  VAL A1149      24.603  -9.881  39.089  1.00 69.15           C\\nANISOU 2448  CB  VAL A1149     9812   8710   7751   -638    790    459       C\\nATOM   2449  CG1 VAL A1149      24.961 -10.583  37.793  1.00 62.41           C\\nANISOU 2449  CG1 VAL A1149     9197   7590   6927   -632    765    483       C\\nATOM   2450  CG2 VAL A1149      25.636  -8.812  39.423  1.00 65.57           C\\nANISOU 2450  CG2 VAL A1149     9323   8286   7303   -385    710    522       C\\nATOM   2451  N   ILE A1150      21.606 -11.063  39.394  1.00 84.73           N\\nANISOU 2451  N   ILE A1150    11413  11014   9767  -1295    945    151       N\\nATOM   2452  CA  ILE A1150      20.566 -12.008  38.997  1.00 83.24           C\\nANISOU 2452  CA  ILE A1150    11179  10809   9639  -1639    980     64       C\\nATOM   2453  C   ILE A1150      19.315 -11.263  38.545  1.00 84.16           C\\nANISOU 2453  C   ILE A1150    10861  11211   9905  -1651    831   -246       C\\nATOM   2454  O   ILE A1150      18.622 -11.692  37.612  1.00 93.69           O\\nANISOU 2454  O   ILE A1150    12028  12360  11209  -1807    688   -369       O\\nATOM   2455  CB  ILE A1150      20.272 -12.986  40.152  1.00 84.83           C\\nANISOU 2455  CB  ILE A1150    11442  11060   9730  -2003   1240    225       C\\nATOM   2456  CG1 ILE A1150      21.486 -13.878  40.414  1.00 82.12           C\\nANISOU 2456  CG1 ILE A1150    11568  10333   9299  -1964   1285    553       C\\nATOM   2457  CG2 ILE A1150      19.059 -13.839  39.844  1.00 86.81           C\\nANISOU 2457  CG2 ILE A1150    11564  11344  10076  -2432   1287    113       C\\nATOM   2458  CD1 ILE A1150      21.367 -14.717  41.663  1.00 70.60           C\\nANISOU 2458  CD1 ILE A1150    10253   8891   7682  -2294   1484    806       C\\nATOM   2459  N   THR A1151      19.009 -10.131  39.188  1.00 79.62           N\\nANISOU 2459  N   THR A1151     9946  10934   9371  -1467    829   -404       N\\nATOM   2460  CA  THR A1151      17.920  -9.283  38.713  1.00 85.27           C\\nANISOU 2460  CA  THR A1151    10223  11875  10301  -1363    618   -716       C\\nATOM   2461  C   THR A1151      18.194  -8.785  37.302  1.00 88.73           C\\nANISOU 2461  C   THR A1151    10820  12078  10815  -1128    245   -709       C\\nATOM   2462  O   THR A1151      17.290  -8.744  36.460  1.00 89.80           O\\nANISOU 2462  O   THR A1151    10761  12268  11090  -1177     -2   -876       O\\nATOM   2463  CB  THR A1151      17.713  -8.098  39.655  1.00 85.11           C\\nANISOU 2463  CB  THR A1151     9861  12141  10338  -1127    668   -919       C\\nATOM   2464  OG1 THR A1151      17.364  -8.577  40.957  1.00 90.34           O\\nANISOU 2464  OG1 THR A1151    10377  13098  10849  -1398   1046   -947       O\\nATOM   2465  CG2 THR A1151      16.602  -7.194  39.144  1.00 80.06           C\\nANISOU 2465  CG2 THR A1151     8743  11680   9998   -942    398  -1262       C\\nATOM   2466  N   THR A1152      19.440  -8.402  37.023  1.00 89.05           N\\nANISOU 2466  N   THR A1152    11208  11880  10745   -898    191   -508       N\\nATOM   2467  CA  THR A1152      19.772  -7.948  35.679  1.00 88.03           C\\nANISOU 2467  CA  THR A1152    11283  11556  10607   -736   -114   -459       C\\nATOM   2468  C   THR A1152      19.666  -9.080  34.665  1.00 84.57           C\\nANISOU 2468  C   THR A1152    11105  10963  10066   -967   -143   -432       C\\nATOM   2469  O   THR A1152      19.276  -8.846  33.516  1.00 88.93           O\\nANISOU 2469  O   THR A1152    11704  11483  10603   -948   -442   -501       O\\nATOM   2470  CB  THR A1152      21.170  -7.335  35.670  1.00 84.93           C\\nANISOU 2470  CB  THR A1152    11169  10986  10115   -508    -96   -248       C\\nATOM   2471  OG1 THR A1152      21.238  -6.314  36.674  1.00 87.26           O\\nANISOU 2471  OG1 THR A1152    11240  11404  10511   -322    -88   -315       O\\nATOM   2472  CG2 THR A1152      21.473  -6.721  34.321  1.00 75.79           C\\nANISOU 2472  CG2 THR A1152    10215   9677   8903   -385   -386   -175       C\\nATOM   2473  N   PHE A1153      19.988 -10.311  35.069  1.00 80.31           N\\nANISOU 2473  N   PHE A1153    10763  10305   9447  -1189    130   -341       N\\nATOM   2474  CA  PHE A1153      19.838 -11.445  34.163  1.00 86.85           C\\nANISOU 2474  CA  PHE A1153    11850  10938  10209  -1417    102   -378       C\\nATOM   2475  C   PHE A1153      18.375 -11.753  33.876  1.00 94.28           C\\nANISOU 2475  C   PHE A1153    12493  12048  11280  -1692    -61   -605       C\\nATOM   2476  O   PHE A1153      18.051 -12.271  32.802  1.00 97.03           O\\nANISOU 2476  O   PHE A1153    13001  12289  11578  -1834   -250   -712       O\\nATOM   2477  CB  PHE A1153      20.524 -12.681  34.744  1.00 85.98           C\\nANISOU 2477  CB  PHE A1153    12033  10584  10052  -1564    394   -224       C\\nATOM   2478  CG  PHE A1153      21.973 -12.790  34.388  1.00 82.81           C\\nANISOU 2478  CG  PHE A1153    11993   9932   9541  -1323    479    -73       C\\nATOM   2479  CD1 PHE A1153      22.400 -12.549  33.096  1.00 87.89           C\\nANISOU 2479  CD1 PHE A1153    12840  10494  10062  -1196    348   -140       C\\nATOM   2480  CD2 PHE A1153      22.908 -13.132  35.345  1.00 77.41           C\\nANISOU 2480  CD2 PHE A1153    11425   9126   8862  -1234    685    132       C\\nATOM   2481  CE1 PHE A1153      23.735 -12.650  32.764  1.00 85.44           C\\nANISOU 2481  CE1 PHE A1153    12792  10012   9660   -991    485    -39       C\\nATOM   2482  CE2 PHE A1153      24.244 -13.233  35.021  1.00 77.07           C\\nANISOU 2482  CE2 PHE A1153    11625   8883   8776   -993    759    238       C\\nATOM   2483  CZ  PHE A1153      24.658 -12.992  33.729  1.00 80.39           C\\nANISOU 2483  CZ  PHE A1153    12194   9251   9099   -874    690    135       C\\nATOM   2484  N   ARG A1154      17.484 -11.446  34.817  1.00 88.53           N\\nANISOU 2484  N   ARG A1154    11311  11612  10713  -1783     15   -710       N\\nATOM   2485  CA  ARG A1154      16.070 -11.771  34.679  1.00 90.56           C\\nANISOU 2485  CA  ARG A1154    11175  12087  11146  -2076    -96   -944       C\\nATOM   2486  C   ARG A1154      15.287 -10.657  33.990  1.00 94.08           C\\nANISOU 2486  C   ARG A1154    11255  12736  11753  -1845   -507  -1151       C\\nATOM   2487  O   ARG A1154      14.589 -10.908  33.004  1.00 98.43           O\\nANISOU 2487  O   ARG A1154    11752  13292  12353  -1977   -823  -1290       O\\nATOM   2488  CB  ARG A1154      15.471 -12.072  36.056  1.00 91.66           C\\nANISOU 2488  CB  ARG A1154    10967  12492  11368  -2333    250   -973       C\\nATOM   2489  CG  ARG A1154      13.953 -12.110  36.087  1.00 98.75           C\\nANISOU 2489  CG  ARG A1154    11273  13741  12505  -2600    179  -1261       C\\nATOM   2490  CD  ARG A1154      13.450 -12.527  37.460  1.00 98.15           C\\nANISOU 2490  CD  ARG A1154    10903  13957  12432  -2937    616  -1264       C\\nATOM   2491  NE  ARG A1154      14.141 -11.809  38.526  1.00 96.23           N\\nANISOU 2491  NE  ARG A1154    10691  13830  12042  -2666    855  -1169       N\\nATOM   2492  CZ  ARG A1154      13.729 -10.656  39.043  1.00 99.35           C\\nANISOU 2492  CZ  ARG A1154    10627  14571  12550  -2384    862  -1413       C\\nATOM   2493  NH1 ARG A1154      12.618 -10.085  38.594  1.00102.81           N\\nANISOU 2493  NH1 ARG A1154    10503  15271  13290  -2299    634  -1752       N\\nATOM   2494  NH2 ARG A1154      14.426 -10.074  40.011  1.00 97.58           N\\nANISOU 2494  NH2 ARG A1154    10500  14418  12157  -2171   1067  -1343       N\\nATOM   2495  N   THR A1155      15.394  -9.425  34.492  1.00 91.70           N\\nANISOU 2495  N   THR A1155    10720  12575  11545  -1493   -553  -1180       N\\nATOM   2496  CA  THR A1155      14.626  -8.327  33.913  1.00 95.66           C\\nANISOU 2496  CA  THR A1155    10869  13211  12265  -1227   -991  -1368       C\\nATOM   2497  C   THR A1155      15.189  -7.887  32.570  1.00 97.84           C\\nANISOU 2497  C   THR A1155    11567  13229  12380  -1038  -1391  -1215       C\\nATOM   2498  O   THR A1155      14.426  -7.500  31.678  1.00103.63           O\\nANISOU 2498  O   THR A1155    12148  14011  13216   -975  -1852  -1325       O\\nATOM   2499  CB  THR A1155      14.590  -7.135  34.871  1.00 96.53           C\\nANISOU 2499  CB  THR A1155    10639  13482  12554   -890   -932  -1480       C\\nATOM   2500  OG1 THR A1155      15.865  -6.481  34.875  1.00 89.26           O\\nANISOU 2500  OG1 THR A1155    10139  12306  11469   -624   -926  -1243       O\\nATOM   2501  CG2 THR A1155      14.254  -7.597  36.282  1.00102.13           C\\nANISOU 2501  CG2 THR A1155    11038  14480  13285  -1108   -443  -1599       C\\nATOM   2502  N   GLY A1156      16.506  -7.938  32.402  1.00 98.59           N\\nANISOU 2502  N   GLY A1156    12176  13074  12209   -961  -1232   -958       N\\nATOM   2503  CA  GLY A1156      17.109  -7.426  31.192  1.00 97.17           C\\nANISOU 2503  CA  GLY A1156    12393  12702  11824   -813  -1538   -796       C\\nATOM   2504  C   GLY A1156      17.208  -5.922  31.139  1.00 94.99           C\\nANISOU 2504  C   GLY A1156    12028  12391  11674   -459  -1843   -727       C\\nATOM   2505  O   GLY A1156      17.414  -5.364  30.057  1.00 94.83           O\\nANISOU 2505  O   GLY A1156    12287  12241  11502   -370  -2199   -582       O\\nATOM   2506  N   THR A1157      17.055  -5.243  32.275  1.00 98.59           N\\nANISOU 2506  N   THR A1157    12130  12944  12386   -269  -1724   -831       N\\nATOM   2507  CA  THR A1157      17.188  -3.793  32.334  1.00 99.99           C\\nANISOU 2507  CA  THR A1157    12241  13012  12740     83  -2014   -798       C\\nATOM   2508  C   THR A1157      18.117  -3.396  33.475  1.00 95.58           C\\nANISOU 2508  C   THR A1157    11722  12408  12187    197  -1666   -741       C\\nATOM   2509  O   THR A1157      18.739  -4.258  34.103  1.00 99.83           O\\nANISOU 2509  O   THR A1157    12385  12993  12552     13  -1238   -673       O\\nATOM   2510  CB  THR A1157      15.819  -3.130  32.503  1.00100.53           C\\nANISOU 2510  CB  THR A1157    11744  13243  13210    283  -2359  -1106       C\\nATOM   2511  N   TRP A1158      18.225  -2.094  33.747  1.00 93.22           N\\nANISOU 2511  N   TRP A1158    11337  11987  12095    500  -1890   -770       N\\nATOM   2512  CA  TRP A1158      19.077  -1.577  34.810  1.00 93.29           C\\nANISOU 2512  CA  TRP A1158    11380  11944  12121    611  -1638   -757       C\\nATOM   2513  C   TRP A1158      18.284  -1.180  36.050  1.00100.83           C\\nANISOU 2513  C   TRP A1158    11839  13130  13343    767  -1520  -1143       C\\nATOM   2514  O   TRP A1158      18.687  -0.262  36.773  1.00104.41           O\\nANISOU 2514  O   TRP A1158    12262  13494  13913    976  -1523  -1234       O\\nATOM   2515  CB  TRP A1158      19.888  -0.380  34.315  1.00 93.24           C\\nANISOU 2515  CB  TRP A1158    11675  11603  12148    796  -1939   -534       C\\nATOM   2516  CG  TRP A1158      20.831  -0.689  33.202  1.00 90.86           C\\nANISOU 2516  CG  TRP A1158    11861  11134  11527    615  -1955   -159       C\\nATOM   2517  CD1 TRP A1158      20.661  -0.401  31.878  1.00 92.31           C\\nANISOU 2517  CD1 TRP A1158    12294  11175  11605    591  -2335     30       C\\nATOM   2518  CD2 TRP A1158      22.100  -1.341  33.312  1.00 84.64           C\\nANISOU 2518  CD2 TRP A1158    11359  10335  10467    435  -1569     52       C\\nATOM   2519  NE1 TRP A1158      21.746  -0.835  31.158  1.00 87.61           N\\nANISOU 2519  NE1 TRP A1158    12125  10516  10649    382  -2146    322       N\\nATOM   2520  CE2 TRP A1158      22.643  -1.417  32.015  1.00 81.33           C\\nANISOU 2520  CE2 TRP A1158    11324   9793   9787    307  -1675    322       C\\nATOM   2521  CE3 TRP A1158      22.829  -1.871  34.381  1.00 79.01           C\\nANISOU 2521  CE3 TRP A1158    10605   9715   9699    377  -1161     35       C\\nATOM   2522  CZ2 TRP A1158      23.881  -2.001  31.759  1.00 77.25           C\\nANISOU 2522  CZ2 TRP A1158    11088   9260   9004    149  -1343    521       C\\nATOM   2523  CZ3 TRP A1158      24.059  -2.452  34.124  1.00 69.87           C\\nANISOU 2523  CZ3 TRP A1158     9733   8502   8314    244   -903    268       C\\nATOM   2524  CH2 TRP A1158      24.572  -2.511  32.824  1.00 69.73           C\\nANISOU 2524  CH2 TRP A1158    10033   8375   8085    144   -972    482       C\\nATOM   2525  N   ASP A1159      17.156  -1.850  36.306  1.00 98.45           N\\nANISOU 2525  N   ASP A1159    11135  13138  13133    646  -1402  -1399       N\\nATOM   2526  CA  ASP A1159      16.331  -1.497  37.457  1.00 97.23           C\\nANISOU 2526  CA  ASP A1159    10456  13283  13205    769  -1227  -1814       C\\nATOM   2527  C   ASP A1159      17.098  -1.638  38.765  1.00 90.66           C\\nANISOU 2527  C   ASP A1159     9725  12569  12151    685   -774  -1819       C\\nATOM   2528  O   ASP A1159      16.820  -0.916  39.727  1.00 92.33           O\\nANISOU 2528  O   ASP A1159     9651  12933  12497    879   -679  -2146       O\\nATOM   2529  CB  ASP A1159      15.076  -2.368  37.498  1.00105.69           C\\nANISOU 2529  CB  ASP A1159    11073  14718  14366    540  -1095  -2046       C\\nATOM   2530  CG  ASP A1159      14.329  -2.379  36.182  1.00109.35           C\\nANISOU 2530  CG  ASP A1159    11447  15092  15007    573  -1581  -2031       C\\nATOM   2531  OD1 ASP A1159      14.839  -2.991  35.220  1.00106.95           O\\nANISOU 2531  OD1 ASP A1159    11588  14593  14457    378  -1693  -1714       O\\nATOM   2532  OD2 ASP A1159      13.231  -1.786  36.115  1.00113.68           O\\nANISOU 2532  OD2 ASP A1159    11472  15783  15940    804  -1860  -2361       O\\nATOM   2533  N   ALA A1160      18.061  -2.558  38.822  1.00 90.75           N\\nANISOU 2533  N   ALA A1160    10142  12514  11824    416   -516  -1483       N\\nATOM   2534  CA  ALA A1160      18.793  -2.777  40.062  1.00 83.07           C\\nANISOU 2534  CA  ALA A1160     9285  11661  10616    322   -147  -1445       C\\nATOM   2535  C   ALA A1160      19.805  -1.671  40.330  1.00 83.07           C\\nANISOU 2535  C   ALA A1160     9492  11427  10644    577   -301  -1398       C\\nATOM   2536  O   ALA A1160      20.159  -1.427  41.488  1.00 80.26           O\\nANISOU 2536  O   ALA A1160     9111  11213  10170    595    -98  -1520       O\\nATOM   2537  CB  ALA A1160      19.490  -4.133  40.023  1.00 69.19           C\\nANISOU 2537  CB  ALA A1160     7878   9858   8554     -5    110  -1098       C\\nATOM   2538  N   TYR A1161      20.270  -0.989  39.289  1.00 85.89           N\\nANISOU 2538  N   TYR A1161    10067  11436  11131    737   -663  -1221       N\\nATOM   2539  CA  TYR A1161      21.312   0.021  39.439  1.00 81.29           C\\nANISOU 2539  CA  TYR A1161     9712  10587  10590    902   -820  -1122       C\\nATOM   2540  C   TYR A1161      20.830   1.413  39.031  1.00 86.56           C\\nANISOU 2540  C   TYR A1161    10259  11009  11620   1221  -1257  -1309       C\\nATOM   2541  O   TYR A1161      19.780   1.882  39.473  1.00 90.75           O\\nANISOU 2541  O   TYR A1161    10405  11678  12398   1423  -1325  -1710       O\\nATOM   2542  CB  TYR A1161      22.541  -0.357  38.608  1.00 78.82           C\\nANISOU 2542  CB  TYR A1161     9822  10037  10089    757   -833   -681       C\\nATOM   2543  CG  TYR A1161      23.144  -1.708  38.932  1.00 79.07           C\\nANISOU 2543  CG  TYR A1161    10004  10209   9831    508   -467   -486       C\\nATOM   2544  CD1 TYR A1161      22.612  -2.876  38.400  1.00 78.87           C\\nANISOU 2544  CD1 TYR A1161     9993  10274   9701    320   -342   -427       C\\nATOM   2545  CD2 TYR A1161      24.263  -1.813  39.748  1.00 75.01           C\\nANISOU 2545  CD2 TYR A1161     9629   9697   9174    468   -297   -359       C\\nATOM   2546  CE1 TYR A1161      23.166  -4.110  38.683  1.00 74.50           C\\nANISOU 2546  CE1 TYR A1161     9613   9760   8934    118    -53   -248       C\\nATOM   2547  CE2 TYR A1161      24.824  -3.042  40.039  1.00 67.83           C\\nANISOU 2547  CE2 TYR A1161     8865   8860   8048    288    -30   -162       C\\nATOM   2548  CZ  TYR A1161      24.272  -4.189  39.504  1.00 71.43           C\\nANISOU 2548  CZ  TYR A1161     9359   9354   8428    123     94   -104       C\\nATOM   2549  OH  TYR A1161      24.829  -5.416  39.787  1.00 69.66           O\\nANISOU 2549  OH  TYR A1161     9313   9118   8037    -32    319     91       O\\nATOM   2550  N   SER A 364      17.508   3.047  36.367  1.00104.00           N\\nATOM   2551  CA  SER A 364      18.568   3.670  35.585  1.00104.92           C\\nATOM   2552  C   SER A 364      18.623   3.097  34.167  1.00111.72           C\\nATOM   2553  O   SER A 364      19.675   3.111  33.526  1.00111.66           O\\nATOM   2554  CB  SER A 364      19.919   3.488  36.282  1.00 97.65           C\\nATOM   2555  N   GLN A 365      17.486   2.600  33.682  1.00122.15           N\\nATOM   2556  CA  GLN A 365      17.397   1.937  32.386  1.00115.38           C\\nATOM   2557  C   GLN A 365      16.553   2.767  31.428  1.00110.61           C\\nATOM   2558  O   GLN A 365      15.419   3.137  31.753  1.00 98.43           O\\nATOM   2559  CB  GLN A 365      16.796   0.536  32.527  1.00106.22           C\\nATOM   2560  N   GLN A 366      17.101   3.039  30.246  1.00120.06           N\\nATOM   2561  CA  GLN A 366      16.385   3.791  29.223  1.00115.06           C\\nATOM   2562  C   GLN A 366      15.363   2.887  28.544  1.00110.82           C\\nATOM   2563  O   GLN A 366      15.719   1.836  27.999  1.00106.83           O\\nATOM   2564  CB  GLN A 366      17.364   4.363  28.199  1.00114.61           C\\nATOM   2565  N   LYS A 367      14.097   3.295  28.574  1.00106.95           N\\nATOM   2566  CA  LYS A 367      13.014   2.529  27.974  1.00112.85           C\\nATOM   2567  C   LYS A 367      12.771   2.895  26.516  1.00109.20           C\\nATOM   2568  O   LYS A 367      11.803   2.410  25.921  1.00103.35           O\\nATOM   2569  CB  LYS A 367      11.727   2.721  28.781  1.00115.42           C\\nATOM   2570  N   GLU A 368      13.626   3.733  25.930  1.00114.20           N\\nATOM   2571  CA  GLU A 368      13.436   4.206  24.566  1.00 99.97           C\\nATOM   2572  C   GLU A 368      14.152   3.361  23.525  1.00100.67           C\\nATOM   2573  O   GLU A 368      13.805   3.444  22.342  1.00 97.34           O\\nATOM   2574  CB  GLU A 368      13.920   5.655  24.437  1.00 81.44           C\\nATOM   2575  CG  GLU A 368      13.087   6.681  25.188  1.00 79.48           C\\nATOM   2576  CD  GLU A 368      11.923   7.216  24.368  1.00 87.69           C\\nATOM   2577  OE1 GLU A 368      11.484   6.529  23.419  1.00 87.57           O\\nATOM   2578  OE2 GLU A 368      11.451   8.332  24.674  1.00 90.78           O\\nATOM   2579  N   LYS A 369      15.139   2.557  23.932  1.00101.97           N\\nATOM   2580  CA  LYS A 369      15.965   1.842  22.963  1.00 93.96           C\\nATOM   2581  C   LYS A 369      15.123   0.959  22.051  1.00 87.89           C\\nATOM   2582  O   LYS A 369      15.377   0.886  20.844  1.00 84.82           O\\nATOM   2583  CB  LYS A 369      17.025   1.012  23.689  1.00 94.15           C\\nATOM   2584  N   LYS A 370      14.107   0.291  22.605  1.00 95.07           N\\nATOM   2585  CA  LYS A 370      13.254  -0.567  21.787  1.00 92.51           C\\nATOM   2586  C   LYS A 370      12.587   0.220  20.665  1.00 85.60           C\\nATOM   2587  O   LYS A 370      12.454  -0.280  19.541  1.00 77.93           O\\nATOM   2588  CB  LYS A 370      12.203  -1.254  22.662  1.00 85.65           C\\nATOM   2589  N   ALA A 371      12.167   1.454  20.944  1.00 85.70           N\\nATOM   2590  CA  ALA A 371      11.556   2.271  19.901  1.00 78.85           C\\nATOM   2591  C   ALA A 371      12.589   2.776  18.902  1.00 73.40           C\\nATOM   2592  O   ALA A 371      12.274   2.940  17.718  1.00 67.94           O\\nATOM   2593  CB  ALA A 371      10.805   3.440  20.520  1.00 20.00           C\\nATOM   2594  N   THR A 372      13.820   3.030  19.357  1.00 75.36           N\\nATOM   2595  CA  THR A 372      14.875   3.470  18.451  1.00 64.07           C\\nATOM   2596  C   THR A 372      15.326   2.343  17.535  1.00 71.79           C\\nATOM   2597  O   THR A 372      15.714   2.593  16.389  1.00 80.74           O\\nATOM   2598  CB  THR A 372      16.066   4.010  19.246  1.00 69.33           C\\nATOM   2599  OG1 THR A 372      15.634   5.071  20.104  1.00 74.68           O\\nATOM   2600  CG2 THR A 372      17.138   4.544  18.316  1.00 68.04           C\\nATOM   2601  N   GLN A 373      15.283   1.100  18.019  1.00 68.72           N\\nATOM   2602  CA  GLN A 373      15.663  -0.031  17.180  1.00 79.96           C\\nATOM   2603  C   GLN A 373      14.624  -0.283  16.095  1.00 79.40           C\\nATOM   2604  O   GLN A 373      14.972  -0.633  14.961  1.00 75.09           O\\nATOM   2605  CB  GLN A 373      15.857  -1.276  18.043  1.00 95.27           C\\nATOM   2606  CG  GLN A 373      17.006  -1.162  19.028  1.00107.01           C\\nATOM   2607  CD  GLN A 373      16.835  -2.074  20.228  1.00113.19           C\\nATOM   2608  OE1 GLN A 373      15.768  -2.652  20.438  1.00109.22           O\\nATOM   2609  NE2 GLN A 373      17.889  -2.204  21.025  1.00117.08           N\\nATOM   2610  N   MET A 374      13.345  -0.105  16.421  1.00 79.17           N\\nATOM   2611  CA  MET A 374      12.307  -0.277  15.413  1.00 76.40           C\\nATOM   2612  C   MET A 374      12.384   0.814  14.350  1.00 70.69           C\\nATOM   2613  O   MET A 374      12.182   0.543  13.160  1.00 68.25           O\\nATOM   2614  CB  MET A 374      10.934  -0.292  16.079  1.00 77.49           C\\nATOM   2615  CG  MET A 374       9.801  -0.689  15.153  1.00 81.14           C\\nATOM   2616  SD  MET A 374       8.219  -0.741  16.009  1.00 84.97           S\\nATOM   2617  CE  MET A 374       8.086   0.958  16.565  1.00103.28           C\\nATOM   2618  N   ALA A 375      12.684   2.052  14.756  1.00 72.85           N\\nATOM   2619  CA  ALA A 375      12.789   3.144  13.793  1.00 69.01           C\\nATOM   2620  C   ALA A 375      13.899   2.887  12.783  1.00 71.99           C\\nATOM   2621  O   ALA A 375      13.756   3.203  11.596  1.00 68.65           O\\nATOM   2622  CB  ALA A 375      13.021   4.464  14.513  1.00 20.00           C\\nATOM   2623  N   ALA A 376      15.014   2.312  13.234  1.00 72.30           N\\nATOM   2624  CA  ALA A 376      16.110   2.018  12.320  1.00 74.21           C\\nATOM   2625  C   ALA A 376      15.790   0.830  11.427  1.00 77.19           C\\nATOM   2626  O   ALA A 376      16.261   0.771  10.285  1.00 87.02           O\\nATOM   2627  CB  ALA A 376      17.398   1.765  13.104  1.00 74.32           C\\nATOM   2628  N   ILE A 377      15.001  -0.125  11.921  1.00 87.67           N\\nATOM   2629  CA  ILE A 377      14.633  -1.265  11.089  1.00 95.90           C\\nATOM   2630  C   ILE A 377      13.706  -0.839   9.957  1.00101.03           C\\nATOM   2631  O   ILE A 377      13.826  -1.331   8.830  1.00 92.85           O\\nATOM   2632  CB  ILE A 377      13.963  -2.361  11.939  1.00 20.00           C\\nATOM   2633  CG1 ILE A 377      14.964  -2.954  12.932  1.00 20.00           C\\nATOM   2634  CG2 ILE A 377      13.385  -3.448  11.046  1.00 20.00           C\\nATOM   2635  CD1 ILE A 377      14.332  -3.844  13.978  1.00 20.00           C\\nATOM   2636  N   VAL A 378      12.786   0.088  10.234  1.00 89.06           N\\nATOM   2637  CA  VAL A 378      11.896   0.596   9.192  1.00 75.68           C\\nATOM   2638  C   VAL A 378      12.683   1.387   8.156  1.00 75.18           C\\nATOM   2639  O   VAL A 378      12.445   1.268   6.948  1.00 76.19           O\\nATOM   2640  CB  VAL A 378      10.775   1.445   9.820  1.00 64.00           C\\nATOM   2641  CG1 VAL A 378       9.960   2.132   8.740  1.00 62.64           C\\nATOM   2642  CG2 VAL A 378       9.887   0.580  10.701  1.00 69.48           C\\nATOM   2643  N   ALA A 379      13.629   2.210   8.612  1.00 84.87           N\\nATOM   2644  CA  ALA A 379      14.470   2.963   7.688  1.00 87.10           C\\nATOM   2645  C   ALA A 379      15.330   2.035   6.842  1.00 88.96           C\\nATOM   2646  O   ALA A 379      15.578   2.310   5.662  1.00 81.40           O\\nATOM   2647  CB  ALA A 379      15.348   3.945   8.463  1.00 44.79           C\\nATOM   2648  N   GLY A 380      15.802   0.935   7.428  1.00 77.23           N\\nATOM   2649  CA  GLY A 380      16.620   0.001   6.670  1.00 80.45           C\\nATOM   2650  C   GLY A 380      15.818  -0.749   5.624  1.00 77.59           C\\nATOM   2651  O   GLY A 380      16.246  -0.884   4.475  1.00 69.34           O\\nATOM   2652  N   VAL A 381      14.642  -1.252   6.012  1.00 81.99           N\\nATOM   2653  CA  VAL A 381      13.758  -1.918   5.057  1.00 83.38           C\\nATOM   2654  C   VAL A 381      13.412  -0.978   3.910  1.00 77.79           C\\nATOM   2655  O   VAL A 381      13.311  -1.397   2.751  1.00 66.26           O\\nATOM   2656  CB  VAL A 381      12.494  -2.434   5.772  1.00 76.89           C\\nATOM   2657  CG1 VAL A 381      11.472  -2.937   4.769  1.00 69.18           C\\nATOM   2658  CG2 VAL A 381      12.858  -3.534   6.752  1.00 75.31           C\\nATOM   2659  N   PHE A 382      13.231   0.308   4.214  1.00 79.75           N\\nATOM   2660  CA  PHE A 382      13.014   1.298   3.166  1.00 68.40           C\\nATOM   2661  C   PHE A 382      14.165   1.294   2.171  1.00 73.80           C\\nATOM   2662  O   PHE A 382      13.953   1.186   0.958  1.00 78.38           O\\nATOM   2663  CB  PHE A 382      12.844   2.679   3.796  1.00 62.89           C\\nATOM   2664  CG  PHE A 382      12.514   3.767   2.815  1.00 69.81           C\\nATOM   2665  CD1 PHE A 382      11.203   4.013   2.452  1.00 78.17           C\\nATOM   2666  CD2 PHE A 382      13.513   4.560   2.276  1.00 67.00           C\\nATOM   2667  CE1 PHE A 382      10.895   5.021   1.557  1.00 75.89           C\\nATOM   2668  CE2 PHE A 382      13.211   5.566   1.380  1.00 62.38           C\\nATOM   2669  CZ  PHE A 382      11.900   5.797   1.021  1.00 65.04           C\\nATOM   2670  N   ILE A 383      15.399   1.395   2.672  1.00 79.94           N\\nATOM   2671  CA  ILE A 383      16.564   1.405   1.792  1.00 76.66           C\\nATOM   2672  C   ILE A 383      16.668   0.093   1.027  1.00 74.25           C\\nATOM   2673  O   ILE A 383      17.053   0.072  -0.148  1.00 81.52           O\\nATOM   2674  CB  ILE A 383      17.840   1.702   2.601  1.00 71.78           C\\nATOM   2675  CG1 ILE A 383      17.851   3.163   3.035  1.00 63.66           C\\nATOM   2676  CG2 ILE A 383      19.084   1.400   1.789  1.00 79.30           C\\nATOM   2677  CD1 ILE A 383      17.701   4.126   1.880  1.00 64.10           C\\nATOM   2678  N   ILE A 384      16.309  -1.019   1.668  1.00 77.47           N\\nANISOU 2678  N   ILE A 384    10269   8636  10532   1676   -785   -446       N\\nATOM   2679  CA  ILE A 384      16.346  -2.312   0.990  1.00 77.09           C\\nANISOU 2679  CA  ILE A 384    10626   8415  10249   1786   -743   -487       C\\nATOM   2680  C   ILE A 384      15.395  -2.323  -0.203  1.00 79.25           C\\nANISOU 2680  C   ILE A 384    11068   8660  10381   1476   -652   -397       C\\nATOM   2681  O   ILE A 384      15.699  -2.905  -1.252  1.00 79.85           O\\nANISOU 2681  O   ILE A 384    11325   8712  10302   1540   -544   -477       O\\nATOM   2682  CB  ILE A 384      16.026  -3.439   1.989  1.00 74.75           C\\nANISOU 2682  CB  ILE A 384    10740   7870   9793   1895   -906   -471       C\\nATOM   2683  CG1 ILE A 384      17.200  -3.648   2.941  1.00 77.41           C\\nANISOU 2683  CG1 ILE A 384    10961   8240  10210   2294  -1026   -570       C\\nATOM   2684  CG2 ILE A 384      15.704  -4.737   1.267  1.00 71.60           C\\nANISOU 2684  CG2 ILE A 384    10844   7191   9169   1898   -891   -497       C\\nATOM   2685  CD1 ILE A 384      18.443  -4.186   2.256  1.00 79.90           C\\nANISOU 2685  CD1 ILE A 384    11224   8571  10564   2673   -951   -738       C\\nATOM   2686  N   CYS A 385      14.245  -1.657  -0.076  1.00 75.66           N\\nANISOU 2686  N   CYS A 385    10540   8236   9971   1156   -704   -252       N\\nATOM   2687  CA  CYS A 385      13.214  -1.744  -1.106  1.00 79.40           C\\nANISOU 2687  CA  CYS A 385    11178   8693  10298    856   -690   -152       C\\nATOM   2688  C   CYS A 385      13.483  -0.807  -2.281  1.00 77.99           C\\nANISOU 2688  C   CYS A 385    10754   8710  10168    769   -575    -84       C\\nATOM   2689  O   CYS A 385      13.199  -1.160  -3.432  1.00 80.47           O\\nANISOU 2689  O   CYS A 385    11270   9043  10261    646   -531    -66       O\\nATOM   2690  CB  CYS A 385      11.842  -1.449  -0.500  1.00 80.67           C\\nANISOU 2690  CB  CYS A 385    11312   8841  10500    576   -801    -23       C\\nATOM   2691  SG  CYS A 385      11.235  -2.722   0.645  1.00 83.19           S\\nANISOU 2691  SG  CYS A 385    12017   8939  10653    532   -901    -25       S\\nATOM   2692  N   TRP A 386      14.018   0.384  -2.024  1.00 68.60           N\\nANISOU 2692  N   TRP A 386     9160   7658   9246    804   -535    -37       N\\nATOM   2693  CA  TRP A 386      14.213   1.350  -3.095  1.00 71.32           C\\nANISOU 2693  CA  TRP A 386     9293   8158   9646    667   -432     98       C\\nATOM   2694  C   TRP A 386      15.618   1.346  -3.677  1.00 73.91           C\\nANISOU 2694  C   TRP A 386     9483   8642   9959    842   -227     12       C\\nATOM   2695  O   TRP A 386      15.812   1.874  -4.776  1.00 77.41           O\\nANISOU 2695  O   TRP A 386     9849   9237  10328    705    -92    139       O\\nATOM   2696  CB  TRP A 386      13.885   2.767  -2.612  1.00 68.85           C\\nANISOU 2696  CB  TRP A 386     8631   7857   9670    543   -510    230       C\\nATOM   2697  CG  TRP A 386      12.415   3.071  -2.565  1.00 72.68           C\\nANISOU 2697  CG  TRP A 386     9161   8279  10174    338   -661    365       C\\nATOM   2698  CD1 TRP A 386      11.648   3.236  -1.448  1.00 67.00           C\\nANISOU 2698  CD1 TRP A 386     8370   7494   9594    332   -777    320       C\\nATOM   2699  CD2 TRP A 386      11.534   3.244  -3.684  1.00 78.89           C\\nANISOU 2699  CD2 TRP A 386    10042   9108  10823    121   -715    558       C\\nATOM   2700  NE1 TRP A 386      10.348   3.502  -1.801  1.00 70.95           N\\nANISOU 2700  NE1 TRP A 386     8865   8000  10093    139   -882    461       N\\nATOM   2701  CE2 TRP A 386      10.251   3.512  -3.168  1.00 76.55           C\\nANISOU 2701  CE2 TRP A 386     9677   8767  10641      9   -876    617       C\\nATOM   2702  CE3 TRP A 386      11.706   3.200  -5.072  1.00 78.88           C\\nANISOU 2702  CE3 TRP A 386    10168   9215  10586     17   -646    682       C\\nATOM   2703  CZ2 TRP A 386       9.146   3.736  -3.988  1.00 75.36           C\\nANISOU 2703  CZ2 TRP A 386     9547   8666  10419   -188  -1008    800       C\\nATOM   2704  CZ3 TRP A 386      10.606   3.421  -5.885  1.00 78.84           C\\nANISOU 2704  CZ3 TRP A 386    10240   9252  10462   -196   -791    875       C\\nATOM   2705  CH2 TRP A 386       9.343   3.684  -5.340  1.00 78.30           C\\nANISOU 2705  CH2 TRP A 386    10069   9128  10555   -289   -989    935       C\\nATOM   2706  N   LEU A 387      16.599   0.779  -2.986  1.00 71.16           N\\nANISOU 2706  N   LEU A 387     9082   8289   9666   1138   -199   -185       N\\nATOM   2707  CA  LEU A 387      17.963   0.908  -3.486  1.00 77.39           C\\nANISOU 2707  CA  LEU A 387     9613   9290  10501   1307     10   -275       C\\nATOM   2708  C   LEU A 387      18.178   0.130  -4.783  1.00 81.59           C\\nANISOU 2708  C   LEU A 387    10394   9919  10687   1358    212   -346       C\\nATOM   2709  O   LEU A 387      18.816   0.661  -5.701  1.00 86.35           O\\nANISOU 2709  O   LEU A 387    10786  10774  11250   1288    442   -288       O\\nATOM   2710  CB  LEU A 387      18.985   0.473  -2.436  1.00 76.08           C\\nANISOU 2710  CB  LEU A 387     9284   9129  10492   1656    -47   -481       C\\nATOM   2711  CG  LEU A 387      20.393   0.933  -2.792  1.00 73.95           C\\nANISOU 2711  CG  LEU A 387     8566   9145  10385   1779    152   -557       C\\nATOM   2712  CD1 LEU A 387      20.380   2.425  -3.067  1.00 70.62           C\\nANISOU 2712  CD1 LEU A 387     7792   8838  10202   1432    210   -352       C\\nATOM   2713  CD2 LEU A 387      21.363   0.599  -1.677  1.00 74.27           C\\nANISOU 2713  CD2 LEU A 387     8384   9220  10617   2125     25   -752       C\\nATOM   2714  N   PRO A 388      17.692  -1.112  -4.913  1.00 79.42           N\\nANISOU 2714  N   PRO A 388    10576   9454  10144   1463    148   -479       N\\nATOM   2715  CA  PRO A 388      17.785  -1.780  -6.223  1.00 83.37           C\\nANISOU 2715  CA  PRO A 388    11355  10040  10283   1481    328   -585       C\\nATOM   2716  C   PRO A 388      17.190  -0.967  -7.356  1.00 88.60           C\\nANISOU 2716  C   PRO A 388    12005  10889  10771   1117    400   -357       C\\nATOM   2717  O   PRO A 388      17.670  -1.054  -8.493  1.00 89.35           O\\nANISOU 2717  O   PRO A 388    12143  11216  10591   1123    637   -407       O\\nATOM   2718  CB  PRO A 388      17.015  -3.085  -5.998  1.00 78.09           C\\nANISOU 2718  CB  PRO A 388    11219   9031   9418   1534    148   -722       C\\nATOM   2719  CG  PRO A 388      17.214  -3.371  -4.563  1.00 73.10           C\\nANISOU 2719  CG  PRO A 388    10537   8200   9037   1742    -22   -758       C\\nATOM   2720  CD  PRO A 388      17.196  -2.039  -3.878  1.00 74.29           C\\nANISOU 2720  CD  PRO A 388    10229   8503   9495   1588    -73   -564       C\\nATOM   2721  N   PHE A 389      16.157  -0.168  -7.077  1.00 87.86           N\\nANISOU 2721  N   PHE A 389    11851  10717  10815    821    202   -105       N\\nATOM   2722  CA  PHE A 389      15.588   0.699  -8.103  1.00 88.83           C\\nANISOU 2722  CA  PHE A 389    11946  10997  10808    504    215    164       C\\nATOM   2723  C   PHE A 389      16.581   1.776  -8.524  1.00 87.11           C\\nANISOU 2723  C   PHE A 389    11342  11030  10726    460    445    317       C\\nATOM   2724  O   PHE A 389      16.791   2.009  -9.719  1.00 91.58           O\\nANISOU 2724  O   PHE A 389    11960  11831  11005    327    627    435       O\\nATOM   2725  CB  PHE A 389      14.287   1.323  -7.592  1.00 81.78           C\\nANISOU 2725  CB  PHE A 389    11019   9946  10106    271    -69    378       C\\nATOM   2726  CG  PHE A 389      13.670   2.319  -8.536  1.00 78.75           C\\nANISOU 2726  CG  PHE A 389    10580   9686   9656    -11   -125    698       C\\nATOM   2727  CD1 PHE A 389      12.947   1.897  -9.638  1.00 72.20           C\\nANISOU 2727  CD1 PHE A 389    10065   8946   8421   -182   -197    758       C\\nATOM   2728  CD2 PHE A 389      13.795   3.677  -8.309  1.00 74.32           C\\nANISOU 2728  CD2 PHE A 389     9675   9124   9438   -104   -142    940       C\\nATOM   2729  CE1 PHE A 389      12.374   2.812 -10.501  1.00 66.21           C\\nANISOU 2729  CE1 PHE A 389     9270   8308   7580   -418   -296   1089       C\\nATOM   2730  CE2 PHE A 389      13.221   4.593  -9.169  1.00 73.66           C\\nANISOU 2730  CE2 PHE A 389     9576   9102   9309   -336   -229   1275       C\\nATOM   2731  CZ  PHE A 389      12.508   4.160 -10.263  1.00 67.96           C\\nANISOU 2731  CZ  PHE A 389     9160   8501   8161   -483   -313   1367       C\\nATOM   2732  N   PHE A 390      17.211   2.438  -7.553  1.00 78.28           N\\nANISOU 2732  N   PHE A 390     9842   9876  10022    542    440    319       N\\nATOM   2733  CA  PHE A 390      18.154   3.503  -7.865  1.00 77.80           C\\nANISOU 2733  CA  PHE A 390     9387  10020  10154    435    640    473       C\\nATOM   2734  C   PHE A 390      19.520   2.977  -8.285  1.00 85.50           C\\nANISOU 2734  C   PHE A 390    10201  11281  11003    650    968    266       C\\nATOM   2735  O   PHE A 390      20.266   3.699  -8.955  1.00 80.65           O\\nANISOU 2735  O   PHE A 390     9313  10928  10401    495   1220    418       O\\nATOM   2736  CB  PHE A 390      18.290   4.441  -6.666  1.00 72.78           C\\nANISOU 2736  CB  PHE A 390     8403   9227  10023    409    479    515       C\\nATOM   2737  CG  PHE A 390      17.046   5.229  -6.384  1.00 71.97           C\\nANISOU 2737  CG  PHE A 390     8367   8891  10086    201    217    731       C\\nATOM   2738  CD1 PHE A 390      16.770   6.384  -7.095  1.00 73.92           C\\nANISOU 2738  CD1 PHE A 390     8531   9132  10422    -77    215   1066       C\\nATOM   2739  CD2 PHE A 390      16.146   4.810  -5.423  1.00 69.40           C\\nANISOU 2739  CD2 PHE A 390     8185   8358   9824    295    -21    611       C\\nATOM   2740  CE1 PHE A 390      15.624   7.110  -6.848  1.00 69.85           C\\nANISOU 2740  CE1 PHE A 390     8056   8392  10093   -202    -42   1247       C\\nATOM   2741  CE2 PHE A 390      14.995   5.533  -5.171  1.00 69.17           C\\nANISOU 2741  CE2 PHE A 390     8161   8162   9960    142   -234    777       C\\nATOM   2742  CZ  PHE A 390      14.735   6.685  -5.884  1.00 63.89           C\\nANISOU 2742  CZ  PHE A 390     7389   7471   9415    -78   -256   1080       C\\nATOM   2743  N   ILE A 391      19.865   1.744  -7.905  1.00 83.05           N\\nANISOU 2743  N   ILE A 391    10043  10926  10586   1005    976    -67       N\\nATOM   2744  CA  ILE A 391      21.044   1.100  -8.477  1.00 88.93           C\\nANISOU 2744  CA  ILE A 391    10677  11954  11158   1273   1299   -305       C\\nATOM   2745  C   ILE A 391      20.854   0.907  -9.975  1.00 91.28           C\\nANISOU 2745  C   ILE A 391    11243  12480  10960   1127   1541   -254       C\\nATOM   2746  O   ILE A 391      21.789   1.084 -10.766  1.00 94.74           O\\nANISOU 2746  O   ILE A 391    11451  13294  11253   1139   1904   -276       O\\nATOM   2747  CB  ILE A 391      21.321  -0.238  -7.761  1.00 85.00           C\\nANISOU 2747  CB  ILE A 391    10370  11271  10655   1728   1197   -664       C\\nATOM   2748  CG1 ILE A 391      21.803   0.004  -6.329  1.00 81.99           C\\nANISOU 2748  CG1 ILE A 391     9657  10782  10715   1901    995   -715       C\\nATOM   2749  CG2 ILE A 391      22.336  -1.068  -8.534  1.00 85.18           C\\nANISOU 2749  CG2 ILE A 391    10376  11551  10438   2063   1525   -960       C\\nATOM   2750  CD1 ILE A 391      22.006  -1.268  -5.531  1.00 79.71           C\\nANISOU 2750  CD1 ILE A 391     9598  10266  10423   2344    833   -991       C\\nATOM   2751  N   THR A 392      19.633   0.564 -10.388  1.00 91.03           N\\nANISOU 2751  N   THR A 392    11682  12262  10642    965   1345   -183       N\\nATOM   2752  CA  THR A 392      19.347   0.341 -11.801  1.00 92.03           C\\nANISOU 2752  CA  THR A 392    12124  12607  10236    813   1511   -151       C\\nATOM   2753  C   THR A 392      19.510   1.622 -12.611  1.00 96.64           C\\nANISOU 2753  C   THR A 392    12473  13487  10758    456   1684    247       C\\nATOM   2754  O   THR A 392      19.972   1.585 -13.759  1.00 99.51           O\\nANISOU 2754  O   THR A 392    12896  14212  10701    394   2002    256       O\\nATOM   2755  CB  THR A 392      17.934  -0.222 -11.949  1.00 85.65           C\\nANISOU 2755  CB  THR A 392    11821  11527   9195    670   1183   -144       C\\nATOM   2756  OG1 THR A 392      17.843  -1.462 -11.238  1.00 86.36           O\\nANISOU 2756  OG1 THR A 392    12169  11313   9330    965   1047   -489       O\\nATOM   2757  CG2 THR A 392      17.589  -0.458 -13.404  1.00 82.50           C\\nANISOU 2757  CG2 THR A 392    11776  11367   8203    498   1292   -131       C\\nATOM   2758  N   HIS A 393      19.187   2.742 -12.031  1.00 88.71           N\\nANISOU 2758  N   HIS A 393    11226  12324  10155    219   1485    579       N\\nATOM   2759  CA  HIS A 393      19.363   3.957 -12.738  1.00 88.98           C\\nANISOU 2759  CA  HIS A 393    11056  12550  10202   -130   1618   1001       C\\nATOM   2760  C   HIS A 393      20.809   4.181 -13.033  1.00 88.31           C\\nANISOU 2760  C   HIS A 393    10554  12829  10172   -105   2051    965       C\\nATOM   2761  O   HIS A 393      21.145   4.651 -14.071  1.00 90.40           O\\nANISOU 2761  O   HIS A 393    10759  13392  10197   -381   2313   1255       O\\nATOM   2762  CB  HIS A 393      18.863   5.074 -11.893  1.00 92.81           C\\nANISOU 2762  CB  HIS A 393    11357  12712  11192   -324   1304   1294       C\\nATOM   2763  CG  HIS A 393      17.412   5.334 -12.064  1.00 96.38           C\\nANISOU 2763  CG  HIS A 393    12141  12922  11557   -443    932   1454       C\\nATOM   2764  ND1 HIS A 393      16.815   5.355 -13.296  1.00101.35           N\\nANISOU 2764  ND1 HIS A 393    12985  13642  11882   -712    860   1815       N\\nATOM   2765  CD2 HIS A 393      16.440   5.591 -11.168  1.00 93.09           C\\nANISOU 2765  CD2 HIS A 393    11851  12212  11307   -333    611   1312       C\\nATOM   2766  CE1 HIS A 393      15.536   5.622 -13.155  1.00 98.51           C\\nANISOU 2766  CE1 HIS A 393    12830  13059  11540   -744    489   1868       C\\nATOM   2767  NE2 HIS A 393      15.282   5.762 -11.872  1.00 93.35           N\\nANISOU 2767  NE2 HIS A 393    12117  12180  11171   -533    357   1563       N\\nATOM   2768  N   ILE A 394      21.675   3.869 -12.094  1.00 95.53           N\\nANISOU 2768  N   ILE A 394    11157  13746  11395    209   2124    635       N\\nATOM   2769  CA  ILE A 394      23.103   4.065 -12.304  1.00100.46           C\\nANISOU 2769  CA  ILE A 394    11300  14765  12104    258   2532    556       C\\nATOM   2770  C   ILE A 394      23.590   3.234 -13.480  1.00110.00           C\\nANISOU 2770  C   ILE A 394    12669  16389  12736    410   2939    349       C\\nATOM   2771  O   ILE A 394      24.530   3.628 -14.181  1.00116.65           O\\nANISOU 2771  O   ILE A 394    13187  17679  13455    283   3367    434       O\\nATOM   2772  CB  ILE A 394      23.876   3.735 -11.014  1.00 95.87           C\\nANISOU 2772  CB  ILE A 394    10335  14092  12001    599   2436    239       C\\nATOM   2773  N   LEU A 395      22.959   2.084 -13.726  1.00109.05           N\\nANISOU 2773  N   LEU A 395    13051  16136  12246    661   2828     65       N\\nATOM   2774  CA  LEU A 395      23.384   1.213 -14.816  1.00115.80           C\\nANISOU 2774  CA  LEU A 395    14119  17349  12533    853   3195   -221       C\\nATOM   2775  C   LEU A 395      22.911   1.731 -16.169  1.00123.98           C\\nANISOU 2775  C   LEU A 395    15434  18666  13007    451   3352    106       C\\nATOM   2776  O   LEU A 395      23.622   1.591 -17.170  1.00132.70           O\\nANISOU 2776  O   LEU A 395    16488  20259  13673    459   3812     22       O\\nATOM   2777  CB  LEU A 395      22.873  -0.208 -14.578  1.00113.04           C\\nANISOU 2777  CB  LEU A 395    14254  16684  12011   1243   2983   -662       C\\nATOM   2778  CG  LEU A 395      23.285  -0.827 -13.242  1.00107.58           C\\nANISOU 2778  CG  LEU A 395    13379  15684  11813   1666   2788   -952       C\\nATOM   2779  CD1 LEU A 395      22.874  -2.287 -13.174  1.00109.94           C\\nANISOU 2779  CD1 LEU A 395    14213  15663  11896   2035   2631  -1369       C\\nATOM   2780  CD2 LEU A 395      24.782  -0.681 -13.009  1.00102.89           C\\nANISOU 2780  CD2 LEU A 395    12151  15454  11490   1927   3132  -1110       C\\nATOM   2781  N   ASN A 396      21.713   2.324 -16.219  1.00120.69           N\\nANISOU 2781  N   ASN A 396    15306  17974  12576    116   2975    478       N\\nATOM   2782  CA  ASN A 396      21.242   2.943 -17.454  1.00120.58           C\\nANISOU 2782  CA  ASN A 396    15547  18214  12053   -278   3052    871       C\\nATOM   2783  C   ASN A 396      22.194   4.031 -17.930  1.00122.42           C\\nANISOU 2783  C   ASN A 396    15355  18837  12322   -573   3455   1241       C\\nATOM   2784  O   ASN A 396      22.387   4.205 -19.139  1.00125.81           O\\nANISOU 2784  O   ASN A 396    15933  19697  12171   -784   3770   1420       O\\nATOM   2785  CB  ASN A 396      19.841   3.523 -17.251  1.00116.75           C\\nANISOU 2785  CB  ASN A 396    15328  17340  11693   -546   2527   1239       C\\nATOM   2786  CG  ASN A 396      18.760   2.676 -17.888  1.00117.94           C\\nANISOU 2786  CG  ASN A 396    16062  17433  11316   -534   2274   1087       C\\nATOM   2787  OD1 ASN A 396      18.987   1.516 -18.228  1.00121.59           O\\nANISOU 2787  OD1 ASN A 396    16780  18007  11413   -276   2424    626       O\\nATOM   2788  ND2 ASN A 396      17.576   3.253 -18.057  1.00116.24           N\\nANISOU 2788  ND2 ASN A 396    16052  17032  11079   -807   1870   1457       N\\nATOM   2789  N   ILE A 397      22.806   4.760 -16.997  1.00128.30           N\\nANISOU 2789  N   ILE A 397    15581  19448  13721   -619   3450   1356       N\\nATOM   2790  CA  ILE A 397      23.706   5.849 -17.357  1.00131.63           C\\nANISOU 2790  CA  ILE A 397    15568  20182  14265   -972   3805   1730       C\\nATOM   2791  C   ILE A 397      25.103   5.322 -17.667  1.00137.13           C\\nANISOU 2791  C   ILE A 397    15858  21427  14818   -764   4380   1392       C\\nATOM   2792  O   ILE A 397      25.789   5.839 -18.556  1.00140.52           O\\nANISOU 2792  O   ILE A 397    16093  22338  14959  -1056   4838   1642       O\\nATOM   2793  CB  ILE A 397      23.731   6.896 -16.228  1.00123.72           C\\nANISOU 2793  CB  ILE A 397    14191  18774  14042  -1149   3517   1971       C\\nATOM   2794  CG1 ILE A 397      22.331   7.473 -16.007  1.00113.56           C\\nANISOU 2794  CG1 ILE A 397    13280  16985  12883  -1327   2987   2301       C\\nATOM   2795  CG2 ILE A 397      24.735   8.002 -16.530  1.00125.40           C\\nANISOU 2795  CG2 ILE A 397    13930  19262  14453  -1557   3873   2337       C\\nATOM   2796  CD1 ILE A 397      22.251   8.459 -14.860  1.00102.21           C\\nANISOU 2796  CD1 ILE A 397    11537  15104  12195  -1449   2680   2462       C\\nATOM   2797  N   HIS A 398      25.537   4.278 -16.959  1.00136.75           N\\nANISOU 2797  N   HIS A 398    15674  21329  14958   -248   4372    832       N\\nATOM   2798  CA  HIS A 398      26.930   3.846 -17.033  1.00140.25           C\\nANISOU 2798  CA  HIS A 398    15599  22260  15431     23   4867    485       C\\nATOM   2799  C   HIS A 398      27.250   3.199 -18.376  1.00154.68           C\\nANISOU 2799  C   HIS A 398    17644  24638  16490    117   5371    293       C\\nATOM   2800  O   HIS A 398      28.121   3.674 -19.114  1.00162.37           O\\nANISOU 2800  O   HIS A 398    18256  26184  17254   -111   5901    448       O\\nATOM   2801  CB  HIS A 398      27.240   2.881 -15.886  1.00132.50           C\\nANISOU 2801  CB  HIS A 398    14462  21019  14861    602   4649    -39       C\\nATOM   2802  N   CYS A 399      26.570   2.103 -18.707  1.00157.99           N\\nANISOU 2802  N   CYS A 399    18652  24908  16468    436   5229    -65       N\\nATOM   2803  CA  CYS A 399      26.929   1.309 -19.875  1.00171.19           C\\nANISOU 2803  CA  CYS A 399    20554  27077  17414    635   5693   -403       C\\nATOM   2804  C   CYS A 399      25.915   1.388 -21.006  1.00172.38           C\\nANISOU 2804  C   CYS A 399    21379  27292  16826    306   5614   -163       C\\nATOM   2805  O   CYS A 399      26.152   0.799 -22.069  1.00171.94           O\\nANISOU 2805  O   CYS A 399    21574  27683  16070    417   5999   -433       O\\nATOM   2806  CB  CYS A 399      27.145  -0.157 -19.472  1.00177.68           C\\nANISOU 2806  CB  CYS A 399    21527  27720  18264   1324   5648  -1118       C\\nATOM   2807  SG  CYS A 399      25.689  -1.129 -18.956  1.00177.65           S\\nANISOU 2807  SG  CYS A 399    22318  26935  18245   1520   4957  -1341       S\\nATOM   2808  N   ASP A 400      24.802   2.093 -20.815  1.00169.42           N\\nANISOU 2808  N   ASP A 400    21292  26506  16572    -73   5118    313       N\\nATOM   2809  CA  ASP A 400      23.708   2.176 -21.779  1.00172.19           C\\nANISOU 2809  CA  ASP A 400    22278  26866  16282   -369   4909    565       C\\nATOM   2810  C   ASP A 400      23.130   0.810 -22.126  1.00178.49           C\\nANISOU 2810  C   ASP A 400    23661  27552  16606    -24   4760      1       C\\nATOM   2811  O   ASP A 400      22.354   0.694 -23.084  1.00180.90           O\\nANISOU 2811  O   ASP A 400    24500  27979  16254   -230   4642     91       O\\nATOM   2812  CB  ASP A 400      24.139   2.903 -23.061  1.00174.58           C\\nANISOU 2812  CB  ASP A 400    22570  27804  15958   -772   5382    965       C\\nATOM   2813  N   CYS A 401      23.494  -0.229 -21.377  1.00180.63           N\\nANISOU 2813  N   CYS A 401    23862  27575  17194    489   4738   -576       N\\nATOM   2814  CA  CYS A 401      22.923  -1.551 -21.583  1.00179.00           C\\nANISOU 2814  CA  CYS A 401    24242  27130  16641    806   4543  -1120       C\\nATOM   2815  C   CYS A 401      21.440  -1.519 -21.252  1.00170.63           C\\nANISOU 2815  C   CYS A 401    23622  25538  15671    556   3881   -897       C\\nATOM   2816  O   CYS A 401      21.063  -1.243 -20.109  1.00166.40           O\\nANISOU 2816  O   CYS A 401    22893  24541  15789    548   3513   -729       O\\nATOM   2817  CB  CYS A 401      23.624  -2.583 -20.701  1.00179.14           C\\nANISOU 2817  CB  CYS A 401    24079  26891  17096   1410   4598  -1700       C\\nATOM   2818  SG  CYS A 401      25.421  -2.457 -20.478  1.00183.37           S\\nANISOU 2818  SG  CYS A 401    23801  27930  17940   1774   5237  -1908       S\\nATOM   2819  N   ASN A 402      20.597  -1.793 -22.244  1.00163.09           N\\nANISOU 2819  N   ASN A 402    23235  24683  14049    348   3727   -908       N\\nATOM   2820  CA  ASN A 402      19.171  -1.877 -21.964  1.00152.09           C\\nANISOU 2820  CA  ASN A 402    22222  22828  12736    126   3092   -755       C\\nATOM   2821  C   ASN A 402      18.914  -3.031 -21.004  1.00144.87           C\\nANISOU 2821  C   ASN A 402    21476  21352  12215    479   2819  -1242       C\\nATOM   2822  O   ASN A 402      19.334  -4.167 -21.242  1.00148.09           O\\nANISOU 2822  O   ASN A 402    22151  21737  12380    836   2997  -1823       O\\nATOM   2823  CB  ASN A 402      18.364  -2.039 -23.255  1.00153.00           C\\nANISOU 2823  CB  ASN A 402    22907  23202  12025   -153   2955   -727       C\\nATOM   2824  CG  ASN A 402      18.644  -3.344 -23.970  1.00154.48           C\\nANISOU 2824  CG  ASN A 402    23550  23525  11619    142   3169  -1424       C\\nATOM   2825  OD1 ASN A 402      18.048  -4.376 -23.657  1.00152.23           O\\nANISOU 2825  OD1 ASN A 402    23645  22801  11394    294   2842  -1846       O\\nATOM   2826  ND2 ASN A 402      19.540  -3.303 -24.949  1.00156.47           N\\nANISOU 2826  ND2 ASN A 402    23784  24383  11285    209   3730  -1554       N\\nATOM   2827  N   ILE A 403      18.259  -2.719 -19.893  1.00137.95           N\\nANISOU 2827  N   ILE A 403    20445  20015  11956    389   2403   -999       N\\nATOM   2828  CA  ILE A 403      18.056  -3.664 -18.801  1.00126.08           C\\nANISOU 2828  CA  ILE A 403    19041  17968  10897    679   2150  -1342       C\\nATOM   2829  C   ILE A 403      16.725  -4.370 -19.025  1.00123.67           C\\nANISOU 2829  C   ILE A 403    19300  17348  10341    476   1691  -1463       C\\nATOM   2830  O   ILE A 403      15.774  -3.737 -19.506  1.00123.23           O\\nANISOU 2830  O   ILE A 403    19345  17396  10082     73   1419  -1099       O\\nATOM   2831  CB  ILE A 403      18.121  -2.936 -17.448  1.00116.57           C\\nANISOU 2831  CB  ILE A 403    17344  16498  10450    680   1990  -1029       C\\nATOM   2832  CG1 ILE A 403      19.571  -2.545 -17.154  1.00117.76           C\\nANISOU 2832  CG1 ILE A 403    16950  16923  10871    944   2430  -1064       C\\nATOM   2833  CG2 ILE A 403      17.524  -3.771 -16.324  1.00111.83           C\\nANISOU 2833  CG2 ILE A 403    16927  15326  10238    834   1619  -1235       C\\nATOM   2834  CD1 ILE A 403      19.744  -1.682 -15.938  1.00115.05           C\\nANISOU 2834  CD1 ILE A 403    16103  16396  11214    903   2293   -760       C\\nATOM   2835  N   PRO A 404      16.628  -5.671 -18.745  1.00118.90           N\\nANISOU 2835  N   PRO A 404    19074  16363   9738    731   1581  -1960       N\\nATOM   2836  CA  PRO A 404      15.360  -6.387 -18.918  1.00118.90           C\\nANISOU 2836  CA  PRO A 404    19598  16036   9542    479   1130  -2089       C\\nATOM   2837  C   PRO A 404      14.199  -5.600 -18.342  1.00114.46           C\\nANISOU 2837  C   PRO A 404    18849  15327   9312     80    700  -1589       C\\nATOM   2838  O   PRO A 404      14.149  -5.345 -17.130  1.00111.06           O\\nANISOU 2838  O   PRO A 404    18106  14611   9479    144    589  -1414       O\\nATOM   2839  CB  PRO A 404      15.590  -7.690 -18.142  1.00118.42           C\\nANISOU 2839  CB  PRO A 404    19799  15435   9759    841   1069  -2563       C\\nATOM   2840  CG  PRO A 404      17.050  -7.938 -18.305  1.00121.83           C\\nANISOU 2840  CG  PRO A 404    20054  16085  10152   1347   1569  -2883       C\\nATOM   2841  CD  PRO A 404      17.718  -6.580 -18.344  1.00119.79           C\\nANISOU 2841  CD  PRO A 404    19169  16331  10014   1271   1867  -2444       C\\nATOM   2842  N   PRO A 405      13.257  -5.175 -19.187  1.00111.48           N\\nANISOU 2842  N   PRO A 405    18639  15168   8549   -316    448  -1354       N\\nATOM   2843  CA  PRO A 405      12.126  -4.381 -18.686  1.00109.02           C\\nANISOU 2843  CA  PRO A 405    18100  14751   8571   -653     36   -886       C\\nATOM   2844  C   PRO A 405      11.320  -5.093 -17.621  1.00107.40           C\\nANISOU 2844  C   PRO A 405    17974  14039   8792   -700   -301  -1012       C\\nATOM   2845  O   PRO A 405      10.656  -4.425 -16.820  1.00106.74           O\\nANISOU 2845  O   PRO A 405    17562  13840   9155   -851   -528   -666       O\\nATOM   2846  CB  PRO A 405      11.292  -4.119 -19.948  1.00110.35           C\\nANISOU 2846  CB  PRO A 405    18539  15248   8141  -1009   -207   -731       C\\nATOM   2847  CG  PRO A 405      11.691  -5.197 -20.899  1.00113.76           C\\nANISOU 2847  CG  PRO A 405    19491  15789   7942   -900    -38  -1264       C\\nATOM   2848  CD  PRO A 405      13.141  -5.456 -20.627  1.00117.16           C\\nANISOU 2848  CD  PRO A 405    19780  16246   8490   -452    496  -1536       C\\nATOM   2849  N   VAL A 406      11.356  -6.428 -17.580  1.00111.87           N\\nANISOU 2849  N   VAL A 406    18978  14290   9236   -579   -329  -1496       N\\nATOM   2850  CA  VAL A 406      10.738  -7.139 -16.469  1.00102.56           C\\nANISOU 2850  CA  VAL A 406    17881  12600   8486   -624   -592  -1581       C\\nATOM   2851  C   VAL A 406      11.508  -6.882 -15.181  1.00104.10           C\\nANISOU 2851  C   VAL A 406    17697  12610   9246   -300   -398  -1479       C\\nATOM   2852  O   VAL A 406      10.926  -6.894 -14.090  1.00102.17           O\\nANISOU 2852  O   VAL A 406    17313  12081   9424   -395   -602  -1324       O\\nATOM   2853  CB  VAL A 406      10.640  -8.644 -16.776  1.00 94.49           C\\nANISOU 2853  CB  VAL A 406    17480  11217   7203   -584   -680  -2114       C\\nATOM   2854  N   LEU A 407      12.818  -6.639 -15.277  1.00103.82           N\\nANISOU 2854  N   LEU A 407    17468  12769   9209     74     -3  -1567       N\\nATOM   2855  CA  LEU A 407      13.592  -6.296 -14.089  1.00100.38           C\\nANISOU 2855  CA  LEU A 407    16623  12220   9296    369    146  -1462       C\\nATOM   2856  C   LEU A 407      13.390  -4.838 -13.698  1.00 94.26           C\\nANISOU 2856  C   LEU A 407    15315  11675   8824    182    114   -975       C\\nATOM   2857  O   LEU A 407      13.200  -4.533 -12.516  1.00 88.29           O\\nANISOU 2857  O   LEU A 407    14299  10718   8529    200     -8   -812       O\\nATOM   2858  CB  LEU A 407      15.077  -6.584 -14.317  1.00101.90           C\\nANISOU 2858  CB  LEU A 407    16737  12562   9418    837    561  -1755       C\\nATOM   2859  N   TYR A 408      13.370  -3.956 -14.650  1.00 94.06           N\\nANISOU 2859  N   TYR A 408    15152  12055   8531      5    218   -738       N\\nATOM   2860  CA  TYR A 408      13.143  -2.599 -14.299  1.00 92.67           C\\nANISOU 2860  CA  TYR A 408    14536  12021   8655   -189    141   -264       C\\nATOM   2861  C   TYR A 408      11.764  -2.493 -13.713  1.00 95.64           C\\nANISOU 2861  C   TYR A 408    14901  12179   9258   -462   -278    -65       C\\nATOM   2862  O   TYR A 408      11.578  -1.795 -12.766  1.00 92.85           O\\nANISOU 2862  O   TYR A 408    14175  11751   9352   -489   -366    194       O\\nATOM   2863  CB  TYR A 408      13.263  -1.746 -15.521  1.00 92.66           C\\nANISOU 2863  CB  TYR A 408    14496  12449   8263   -369    283     -7       C\\nATOM   2864  CG  TYR A 408      13.909  -0.444 -15.274  1.00 92.93           C\\nANISOU 2864  CG  TYR A 408    14043  12651   8617   -377    472    359       C\\nATOM   2865  CD1 TYR A 408      13.694   0.227 -14.129  1.00 88.51           C\\nANISOU 2865  CD1 TYR A 408    13122  11858   8651   -379    316    564       C\\nATOM   2866  CD2 TYR A 408      14.725   0.122 -16.199  1.00 98.66           C\\nANISOU 2866  CD2 TYR A 408    14681  13767   9040   -406    819    487       C\\nATOM   2867  CE1 TYR A 408      14.287   1.434 -13.904  1.00 87.26           C\\nANISOU 2867  CE1 TYR A 408    12549  11797   8809   -413    462    866       C\\nATOM   2868  CE2 TYR A 408      15.323   1.331 -15.973  1.00 98.99           C\\nANISOU 2868  CE2 TYR A 408    14288  13921   9401   -474    985    837       C\\nATOM   2869  CZ  TYR A 408      15.086   1.974 -14.814  1.00 95.40           C\\nANISOU 2869  CZ  TYR A 408    13502  13174   9570   -479    786   1014       C\\nATOM   2870  OH  TYR A 408      15.640   3.178 -14.533  1.00 98.94           O\\nANISOU 2870  OH  TYR A 408    13550  13681  10361   -572    923   1329       O\\nATOM   2871  N   SER A 409      10.781  -3.173 -14.278  1.00105.38           N\\nANISOU 2871  N   SER A 409    16521  13320  10198   -667   -536   -211       N\\nATOM   2872  CA  SER A 409       9.431  -3.119 -13.727  1.00100.18           C\\nANISOU 2872  CA  SER A 409    15802  12496   9765   -940   -916    -53       C\\nATOM   2873  C   SER A 409       9.363  -3.750 -12.341  1.00 91.59           C\\nANISOU 2873  C   SER A 409    14684  11035   9081   -825   -948   -193       C\\nATOM   2874  O   SER A 409       8.543  -3.336 -11.513  1.00 85.61           O\\nANISOU 2874  O   SER A 409    13671  10195   8661   -967  -1137      4       O\\nATOM   2875  CB  SER A 409       8.447  -3.811 -14.672  1.00102.06           C\\nANISOU 2875  CB  SER A 409    16434  12778   9567  -1245  -1202   -175       C\\nATOM   2876  OG  SER A 409       8.493  -3.239 -15.967  1.00105.65           O\\nANISOU 2876  OG  SER A 409    16956  13611   9576  -1354  -1197    -26       O\\nATOM   2877  N   ALA A 410      10.216  -4.740 -12.069  1.00 90.76           N\\nANISOU 2877  N   ALA A 410    14837  10715   8935   -552   -765   -524       N\\nATOM   2878  CA  ALA A 410      10.196  -5.405 -10.769  1.00 84.55           C\\nANISOU 2878  CA  ALA A 410    14089   9558   8478   -436   -813   -622       C\\nATOM   2879  C   ALA A 410      10.716  -4.488  -9.669  1.00 85.46           C\\nANISOU 2879  C   ALA A 410    13726   9716   9028   -244   -702   -420       C\\nATOM   2880  O   ALA A 410      10.097  -4.365  -8.607  1.00 76.26           O\\nANISOU 2880  O   ALA A 410    12411   8410   8155   -337   -841   -294       O\\nATOM   2881  CB  ALA A 410      11.018  -6.693 -10.829  1.00 79.54           C\\nANISOU 2881  CB  ALA A 410    13883   8649   7690   -141   -680  -1016       C\\nATOM   2882  N   PHE A 411      11.858  -3.837  -9.904  1.00 82.88           N\\nANISOU 2882  N   PHE A 411    13149   9606   8736      5   -442   -403       N\\nATOM   2883  CA  PHE A 411      12.446  -2.977  -8.883  1.00 81.51           C\\nANISOU 2883  CA  PHE A 411    12529   9464   8975    175   -355   -259       C\\nATOM   2884  C   PHE A 411      11.593  -1.745  -8.614  1.00 76.95           C\\nANISOU 2884  C   PHE A 411    11608   8991   8637    -75   -511     73       C\\nATOM   2885  O   PHE A 411      11.658  -1.179  -7.516  1.00 76.38           O\\nANISOU 2885  O   PHE A 411    11240   8854   8929      0   -536    155       O\\nATOM   2886  CB  PHE A 411      13.859  -2.567  -9.293  1.00 88.89           C\\nANISOU 2886  CB  PHE A 411    13244  10633   9898    438    -44   -321       C\\nATOM   2887  CG  PHE A 411      14.856  -3.688  -9.233  1.00 94.35           C\\nANISOU 2887  CG  PHE A 411    14147  11212  10488    811    121   -674       C\\nATOM   2888  CD1 PHE A 411      14.562  -4.860  -8.555  1.00 93.62           C\\nANISOU 2888  CD1 PHE A 411    14407  10746  10418    926    -36   -865       C\\nATOM   2889  CD2 PHE A 411      16.092  -3.568  -9.846  1.00 94.90           C\\nANISOU 2889  CD2 PHE A 411    14052  11548  10457   1055    438   -805       C\\nATOM   2890  CE1 PHE A 411      15.480  -5.891  -8.497  1.00 91.66           C\\nANISOU 2890  CE1 PHE A 411    14375  10339  10112   1324     82  -1184       C\\nATOM   2891  CE2 PHE A 411      17.013  -4.595  -9.790  1.00 91.21           C\\nANISOU 2891  CE2 PHE A 411    13738  10988   9931   1464    585  -1156       C\\nATOM   2892  CZ  PHE A 411      16.707  -5.757  -9.115  1.00 90.35           C\\nANISOU 2892  CZ  PHE A 411    14011  10453   9865   1623    389  -1349       C\\nATOM   2893  N   THR A 412      10.799  -1.310  -9.596  1.00 86.37           N\\nANISOU 2893  N   THR A 412    12841  10347   9628   -346   -634    251       N\\nATOM   2894  CA  THR A 412       9.854  -0.225  -9.353  1.00 83.78           C\\nANISOU 2894  CA  THR A 412    12208  10075   9551   -541   -831    553       C\\nATOM   2895  C   THR A 412       8.712  -0.693  -8.459  1.00 78.58           C\\nANISOU 2895  C   THR A 412    11565   9242   9050   -678  -1053    522       C\\nATOM   2896  O   THR A 412       8.335  -0.005  -7.503  1.00 75.36           O\\nANISOU 2896  O   THR A 412    10841   8797   8997   -662  -1111    634       O\\nATOM   2897  CB  THR A 412       9.310   0.315 -10.677  1.00 83.99           C\\nANISOU 2897  CB  THR A 412    12287  10328   9297   -765   -948    775       C\\nATOM   2898  OG1 THR A 412      10.397   0.624 -11.557  1.00 88.79           O\\nANISOU 2898  OG1 THR A 412    12926  11134   9675   -676   -690    805       O\\nATOM   2899  CG2 THR A 412       8.491   1.578 -10.436  1.00 76.49           C\\nANISOU 2899  CG2 THR A 412    10981   9411   8671   -879  -1149   1106       C\\nATOM   2900  N   TRP A 413       8.148  -1.866  -8.758  1.00 79.97           N\\nANISOU 2900  N   TRP A 413    12110   9314   8961   -831  -1168    357       N\\nATOM   2901  CA  TRP A 413       7.078  -2.406  -7.927  1.00 79.43           C\\nANISOU 2901  CA  TRP A 413    12060   9094   9024  -1024  -1347    342       C\\nATOM   2902  C   TRP A 413       7.576  -2.703  -6.520  1.00 73.46           C\\nANISOU 2902  C   TRP A 413    11258   8138   8517   -819  -1224    254       C\\nATOM   2903  O   TRP A 413       6.853  -2.491  -5.539  1.00 70.81           O\\nANISOU 2903  O   TRP A 413    10714   7782   8407   -915  -1295    340       O\\nATOM   2904  CB  TRP A 413       6.498  -3.667  -8.569  1.00 85.80           C\\nANISOU 2904  CB  TRP A 413    13317   9783   9501  -1268  -1494    166       C\\nATOM   2905  CG  TRP A 413       5.728  -3.398  -9.828  1.00 91.51           C\\nANISOU 2905  CG  TRP A 413    14070  10739   9962  -1534  -1703    261       C\\nATOM   2906  CD1 TRP A 413       5.242  -2.195 -10.250  1.00 85.59           C\\nANISOU 2906  CD1 TRP A 413    12966  10256   9299  -1598  -1823    542       C\\nATOM   2907  CD2 TRP A 413       5.358  -4.354 -10.833  1.00 96.72           C\\nANISOU 2907  CD2 TRP A 413    15160  11373  10216  -1760  -1855     72       C\\nATOM   2908  NE1 TRP A 413       4.589  -2.343 -11.449  1.00 88.41           N\\nANISOU 2908  NE1 TRP A 413    13492  10790   9309  -1846  -2056    571       N\\nATOM   2909  CE2 TRP A 413       4.646  -3.658 -11.829  1.00 95.02           C\\nANISOU 2909  CE2 TRP A 413    14808  11468   9826  -1963  -2077    265       C\\nATOM   2910  CE3 TRP A 413       5.558  -5.731 -10.985  1.00100.43           C\\nANISOU 2910  CE3 TRP A 413    16143  11559  10456  -1802  -1850   -252       C\\nATOM   2911  CZ2 TRP A 413       4.135  -4.290 -12.963  1.00 98.69           C\\nANISOU 2911  CZ2 TRP A 413    15618  12022   9858  -2226  -2299    130       C\\nATOM   2912  CZ3 TRP A 413       5.049  -6.356 -12.111  1.00103.40           C\\nANISOU 2912  CZ3 TRP A 413    16876  11980  10432  -2067  -2053   -417       C\\nATOM   2913  CH2 TRP A 413       4.347  -5.636 -13.085  1.00102.66           C\\nANISOU 2913  CH2 TRP A 413    16621  12251  10133  -2286  -2277   -233       C\\nATOM   2914  N   LEU A 414       8.817  -3.184  -6.402  1.00 75.32           N\\nANISOU 2914  N   LEU A 414    11667   8256   8695   -521  -1041     79       N\\nATOM   2915  CA  LEU A 414       9.384  -3.467  -5.087  1.00 69.21           C\\nANISOU 2915  CA  LEU A 414    10863   7310   8123   -291   -967     10       C\\nATOM   2916  C   LEU A 414       9.434  -2.210  -4.226  1.00 77.59           C\\nANISOU 2916  C   LEU A 414    11447   8517   9516   -215   -939    159       C\\nATOM   2917  O   LEU A 414       9.179  -2.265  -3.016  1.00 79.71           O\\nANISOU 2917  O   LEU A 414    11637   8710   9938   -194   -969    169       O\\nATOM   2918  CB  LEU A 414      10.778  -4.078  -5.238  1.00 67.92           C\\nANISOU 2918  CB  LEU A 414    10893   7049   7867     71   -800   -201       C\\nATOM   2919  CG  LEU A 414      11.552  -4.368  -3.947  1.00 71.97           C\\nANISOU 2919  CG  LEU A 414    11370   7408   8567    375   -760   -268       C\\nATOM   2920  CD1 LEU A 414      10.756  -5.279  -3.035  1.00 56.68           C\\nANISOU 2920  CD1 LEU A 414     9726   5197   6611    226   -906   -242       C\\nATOM   2921  CD2 LEU A 414      12.904  -4.980  -4.260  1.00 76.87           C\\nANISOU 2921  CD2 LEU A 414    12133   7966   9108    768   -617   -490       C\\nATOM   2922  N   GLY A 415       9.747  -1.065  -4.832  1.00 76.07           N\\nANISOU 2922  N   GLY A 415    10960   8524   9421   -187   -885    275       N\\nATOM   2923  CA  GLY A 415       9.745   0.179  -4.081  1.00 72.96           C\\nANISOU 2923  CA  GLY A 415    10144   8207   9369   -132   -886    390       C\\nATOM   2924  C   GLY A 415       8.357   0.581  -3.618  1.00 74.19           C\\nANISOU 2924  C   GLY A 415    10131   8394   9665   -339  -1044    507       C\\nATOM   2925  O   GLY A 415       8.180   1.043  -2.488  1.00 75.00           O\\nANISOU 2925  O   GLY A 415    10010   8487   9999   -269  -1044    489       O\\nATOM   2926  N   TYR A 416       7.355   0.423  -4.485  1.00 71.29           N\\nANISOU 2926  N   TYR A 416     9841   8097   9148   -588  -1184    609       N\\nATOM   2927  CA  TYR A 416       5.978   0.695  -4.089  1.00 65.72           C\\nANISOU 2927  CA  TYR A 416     8925   7466   8580   -782  -1337    704       C\\nATOM   2928  C   TYR A 416       5.494  -0.288  -3.030  1.00 74.23           C\\nANISOU 2928  C   TYR A 416    10136   8452   9617   -880  -1320    595       C\\nATOM   2929  O   TYR A 416       4.629   0.058  -2.215  1.00 72.94           O\\nANISOU 2929  O   TYR A 416     9706   8378   9627   -957  -1345    631       O\\nATOM   2930  CB  TYR A 416       5.065   0.646  -5.312  1.00 62.97           C\\nANISOU 2930  CB  TYR A 416     8626   7243   8059  -1034  -1533    831       C\\nATOM   2931  CG  TYR A 416       5.257   1.800  -6.266  1.00 72.57           C\\nANISOU 2931  CG  TYR A 416     9671   8573   9328   -975  -1592   1030       C\\nATOM   2932  CD1 TYR A 416       5.334   3.107  -5.802  1.00 77.77           C\\nANISOU 2932  CD1 TYR A 416     9966   9229  10353   -816  -1582   1149       C\\nATOM   2933  CD2 TYR A 416       5.362   1.584  -7.633  1.00 70.98           C\\nANISOU 2933  CD2 TYR A 416     9709   8467   8795  -1089  -1663   1103       C\\nATOM   2934  CE1 TYR A 416       5.505   4.166  -6.675  1.00 81.18           C\\nANISOU 2934  CE1 TYR A 416    10288   9707  10852   -788  -1652   1381       C\\nATOM   2935  CE2 TYR A 416       5.537   2.637  -8.513  1.00 78.84           C\\nANISOU 2935  CE2 TYR A 416    10587   9572   9796  -1063  -1716   1345       C\\nATOM   2936  CZ  TYR A 416       5.608   3.925  -8.030  1.00 78.01           C\\nANISOU 2936  CZ  TYR A 416    10131   9419  10091   -919  -1715   1507       C\\nATOM   2937  OH  TYR A 416       5.781   4.974  -8.906  1.00 66.59           O\\nANISOU 2937  OH  TYR A 416     8612   8022   8665   -917  -1783   1795       O\\nATOM   2938  N   VAL A 417       6.036  -1.510  -3.031  1.00 75.00           N\\nANISOU 2938  N   VAL A 417    10650   8367   9481   -873  -1268    468       N\\nATOM   2939  CA  VAL A 417       5.682  -2.503  -2.019  1.00 75.22           C\\nANISOU 2939  CA  VAL A 417    10882   8250   9450   -979  -1253    416       C\\nATOM   2940  C   VAL A 417       6.049  -2.017  -0.621  1.00 75.65           C\\nANISOU 2940  C   VAL A 417    10726   8332   9686   -769  -1144    400       C\\nATOM   2941  O   VAL A 417       5.383  -2.367   0.363  1.00 73.28           O\\nANISOU 2941  O   VAL A 417    10419   8044   9381   -909  -1125    429       O\\nATOM   2942  CB  VAL A 417       6.357  -3.847  -2.359  1.00 69.42           C\\nANISOU 2942  CB  VAL A 417    10679   7234   8461   -938  -1241    282       C\\nATOM   2943  CG1 VAL A 417       6.474  -4.740  -1.133  1.00 66.88           C\\nANISOU 2943  CG1 VAL A 417    10605   6693   8112   -911  -1204    262       C\\nATOM   2944  CG2 VAL A 417       5.575  -4.550  -3.446  1.00 68.97           C\\nANISOU 2944  CG2 VAL A 417    10878   7133   8193  -1268  -1387    262       C\\nATOM   2945  N   ASN A 418       7.086  -1.184  -0.510  1.00 69.14           N\\nANISOU 2945  N   ASN A 418     9719   7544   9007   -464  -1071    354       N\\nATOM   2946  CA  ASN A 418       7.506  -0.674   0.790  1.00 59.69           C\\nANISOU 2946  CA  ASN A 418     8331   6385   7962   -263  -1004    296       C\\nATOM   2947  C   ASN A 418       6.365   0.000   1.544  1.00 72.46           C\\nANISOU 2947  C   ASN A 418     9629   8176   9728   -397  -1007    338       C\\nATOM   2948  O   ASN A 418       6.372   0.033   2.780  1.00 78.40           O\\nANISOU 2948  O   ASN A 418    10330   8974  10483   -321   -946    277       O\\nATOM   2949  CB  ASN A 418       8.666   0.302   0.607  1.00 65.48           C\\nANISOU 2949  CB  ASN A 418     8842   7154   8882      6   -958    240       C\\nATOM   2950  CG  ASN A 418       9.105   0.938   1.907  1.00 70.06           C\\nANISOU 2950  CG  ASN A 418     9208   7784   9627    195   -932    141       C\\nATOM   2951  OD1 ASN A 418       9.915   0.373   2.644  1.00 72.31           O\\nANISOU 2951  OD1 ASN A 418     9648   8008   9820    376   -923     50       O\\nATOM   2952  ND2 ASN A 418       8.575   2.123   2.197  1.00 73.88           N\\nANISOU 2952  ND2 ASN A 418     9344   8372  10354    175   -946    143       N\\nATOM   2953  N   SER A 419       5.371   0.528   0.828  1.00 73.71           N\\nANISOU 2953  N   SER A 419     9563   8456   9988   -577  -1081    433       N\\nATOM   2954  CA  SER A 419       4.257   1.208   1.479  1.00 74.87           C\\nANISOU 2954  CA  SER A 419     9342   8795  10311   -653  -1075    444       C\\nATOM   2955  C   SER A 419       3.387   0.269   2.304  1.00 71.13           C\\nANISOU 2955  C   SER A 419     8963   8398   9665   -899  -1010    455       C\\nATOM   2956  O   SER A 419       2.578   0.748   3.105  1.00 79.35           O\\nANISOU 2956  O   SER A 419     9691   9646  10814   -930   -935    423       O\\nATOM   2957  CB  SER A 419       3.402   1.927   0.433  1.00 76.98           C\\nANISOU 2957  CB  SER A 419     9339   9174  10737   -757  -1215    564       C\\nATOM   2958  OG  SER A 419       4.102   3.028  -0.124  1.00 76.00           O\\nANISOU 2958  OG  SER A 419     9078   8985  10813   -542  -1256    597       O\\nATOM   2959  N   ALA A 420       3.532  -1.043   2.146  1.00 64.52           N\\nANISOU 2959  N   ALA A 420     8553   7392   8567  -1076  -1023    494       N\\nATOM   2960  CA  ALA A 420       2.711  -1.998   2.873  1.00 70.62           C\\nANISOU 2960  CA  ALA A 420     9465   8194   9173  -1382   -964    556       C\\nATOM   2961  C   ALA A 420       3.486  -2.802   3.908  1.00 76.87           C\\nANISOU 2961  C   ALA A 420    10638   8808   9762  -1279   -878    546       C\\nATOM   2962  O   ALA A 420       2.886  -3.634   4.598  1.00 79.00           O\\nANISOU 2962  O   ALA A 420    11085   9071   9862  -1550   -815    643       O\\nATOM   2963  CB  ALA A 420       2.026  -2.954   1.892  1.00 69.09           C\\nANISOU 2963  CB  ALA A 420     9496   7901   8853  -1760  -1092    637       C\\nATOM   2964  N   VAL A 421       4.793  -2.590   4.035  1.00 77.91           N\\nANISOU 2964  N   VAL A 421    10893   8806   9904   -910   -888    455       N\\nATOM   2965  CA  VAL A 421       5.579  -3.412   4.946  1.00 79.27           C\\nANISOU 2965  CA  VAL A 421    11443   8799   9879   -770   -869    464       C\\nATOM   2966  C   VAL A 421       5.680  -2.792   6.335  1.00 78.59           C\\nANISOU 2966  C   VAL A 421    11159   8929   9775   -616   -776    415       C\\nATOM   2967  O   VAL A 421       5.844  -3.521   7.319  1.00 80.37           O\\nANISOU 2967  O   VAL A 421    11677   9096   9766   -626   -753    490       O\\nATOM   2968  CB  VAL A 421       6.980  -3.686   4.367  1.00 73.59           C\\nANISOU 2968  CB  VAL A 421    10961   7841   9160   -437   -947    375       C\\nATOM   2969  CG1 VAL A 421       6.871  -4.312   2.991  1.00 71.39           C\\nANISOU 2969  CG1 VAL A 421    10910   7375   8838   -578  -1015    377       C\\nATOM   2970  CG2 VAL A 421       7.810  -2.409   4.324  1.00 65.73           C\\nANISOU 2970  CG2 VAL A 421     9584   7002   8387   -121   -934    246       C\\nATOM   2971  N   ASN A 422       5.581  -1.466   6.440  1.00 74.03           N\\nANISOU 2971  N   ASN A 422    10123   8582   9422   -475   -738    288       N\\nATOM   2972  CA  ASN A 422       5.742  -0.820   7.742  1.00 73.83           C\\nANISOU 2972  CA  ASN A 422     9929   8759   9366   -304   -662    170       C\\nATOM   2973  C   ASN A 422       4.697  -1.265   8.756  1.00 74.68           C\\nANISOU 2973  C   ASN A 422    10063   9076   9236   -564   -510    254       C\\nATOM   2974  O   ASN A 422       5.081  -1.611   9.887  1.00 76.59           O\\nANISOU 2974  O   ASN A 422    10516   9367   9218   -484   -475    261       O\\nATOM   2975  CB  ASN A 422       5.757   0.700   7.560  1.00 72.41           C\\nANISOU 2975  CB  ASN A 422     9279   8717   9517   -120   -663     -7       C\\nATOM   2976  CG  ASN A 422       7.075   1.199   7.026  1.00 70.46           C\\nANISOU 2976  CG  ASN A 422     9018   8305   9448    152   -777    -94       C\\nATOM   2977  OD1 ASN A 422       8.006   0.419   6.829  1.00 69.93           O\\nANISOU 2977  OD1 ASN A 422     9248   8068   9254    251   -842    -54       O\\nATOM   2978  ND2 ASN A 422       7.166   2.500   6.780  1.00 74.23           N\\nANISOU 2978  ND2 ASN A 422     9142   8823  10239    275   -798   -213       N\\nATOM   2979  N   PRO A 423       3.396  -1.299   8.444  1.00 74.98           N\\nANISOU 2979  N   PRO A 423     9889   9275   9326   -884   -418    332       N\\nATOM   2980  CA  PRO A 423       2.439  -1.829   9.431  1.00 79.39           C\\nANISOU 2980  CA  PRO A 423    10466  10068   9629  -1180   -229    435       C\\nATOM   2981  C   PRO A 423       2.722  -3.267   9.832  1.00 83.90           C\\nANISOU 2981  C   PRO A 423    11615  10404   9861  -1378   -249    663       C\\nATOM   2982  O   PRO A 423       2.406  -3.662  10.961  1.00 90.16           O\\nANISOU 2982  O   PRO A 423    12538  11363  10356  -1521    -99    763       O\\nATOM   2983  CB  PRO A 423       1.089  -1.697   8.713  1.00 72.48           C\\nANISOU 2983  CB  PRO A 423     9227   9375   8937  -1503   -180    488       C\\nATOM   2984  CG  PRO A 423       1.299  -0.620   7.719  1.00 68.97           C\\nANISOU 2984  CG  PRO A 423     8463   8890   8854  -1250   -321    353       C\\nATOM   2985  CD  PRO A 423       2.703  -0.792   7.246  1.00 69.67           C\\nANISOU 2985  CD  PRO A 423     8902   8634   8934   -993   -481    335       C\\nATOM   2986  N   ILE A 424       3.313  -4.062   8.939  1.00 83.26           N\\nANISOU 2986  N   ILE A 424    11907   9927   9801  -1380   -427    747       N\\nATOM   2987  CA  ILE A 424       3.682  -5.430   9.285  1.00 83.10           C\\nANISOU 2987  CA  ILE A 424    12489   9580   9504  -1500   -487    952       C\\nATOM   2988  C   ILE A 424       4.819  -5.441  10.300  1.00 81.27           C\\nANISOU 2988  C   ILE A 424    12492   9304   9083  -1119   -542    931       C\\nATOM   2989  O   ILE A 424       4.919  -6.359  11.125  1.00 80.08           O\\nANISOU 2989  O   ILE A 424    12773   9025   8629  -1213   -546   1138       O\\nATOM   2990  CB  ILE A 424       4.040  -6.206   8.002  1.00 78.55           C\\nANISOU 2990  CB  ILE A 424    12237   8582   9027  -1536   -666    971       C\\nATOM   2991  CG1 ILE A 424       2.825  -6.276   7.073  1.00 73.56           C\\nANISOU 2991  CG1 ILE A 424    11398   8028   8524  -1971   -654   1003       C\\nATOM   2992  CG2 ILE A 424       4.560  -7.600   8.325  1.00 80.22           C\\nANISOU 2992  CG2 ILE A 424    13116   8357   9008  -1567   -766   1149       C\\nATOM   2993  CD1 ILE A 424       3.095  -6.975   5.758  1.00 71.89           C\\nANISOU 2993  CD1 ILE A 424    11502   7446   8367  -2028   -834    970       C\\nATOM   2994  N   ILE A 425       5.680  -4.422  10.275  1.00 72.91           N\\nANISOU 2994  N   ILE A 425    11155   8352   8197   -705   -607    699       N\\nATOM   2995  CA  ILE A 425       6.795  -4.363  11.215  1.00 77.19           C\\nANISOU 2995  CA  ILE A 425    11857   8894   8577   -341   -708    646       C\\nATOM   2996  C   ILE A 425       6.320  -3.961  12.608  1.00 86.64           C\\nANISOU 2996  C   ILE A 425    12947  10469   9504   -403   -561    636       C\\nATOM   2997  O   ILE A 425       6.863  -4.432  13.615  1.00 84.58           O\\nANISOU 2997  O   ILE A 425    13008  10207   8921   -280   -633    733       O\\nATOM   2998  CB  ILE A 425       7.877  -3.406  10.689  1.00 71.65           C\\nANISOU 2998  CB  ILE A 425    10863   8188   8172     58   -830    392       C\\nATOM   2999  CG1 ILE A 425       8.343  -3.850   9.303  1.00 71.05           C\\nANISOU 2999  CG1 ILE A 425    10906   7796   8294    111   -926    402       C\\nATOM   3000  CG2 ILE A 425       9.062  -3.360  11.634  1.00 68.37           C\\nANISOU 3000  CG2 ILE A 425    10565   7798   7613    422   -980    318       C\\nATOM   3001  CD1 ILE A 425       9.377  -2.939   8.685  1.00 69.86           C\\nANISOU 3001  CD1 ILE A 425    10448   7667   8427    435  -1000    194       C\\nATOM   3002  N   TYR A 426       5.302  -3.102  12.695  1.00 80.85           N\\nANISOU 3002  N   TYR A 426    11769  10077   8874   -571   -359    514       N\\nATOM   3003  CA  TYR A 426       4.811  -2.668  13.999  1.00 87.40           C\\nANISOU 3003  CA  TYR A 426    12467  11316   9424   -609   -172    444       C\\nATOM   3004  C   TYR A 426       4.159  -3.813  14.767  1.00 95.75           C\\nANISOU 3004  C   TYR A 426    13906  12427  10045   -980    -30    771       C\\nATOM   3005  O   TYR A 426       4.175  -3.815  16.004  1.00 99.16           O\\nANISOU 3005  O   TYR A 426    14463  13130  10085   -961     67    794       O\\nATOM   3006  CB  TYR A 426       3.826  -1.511  13.828  1.00 86.99           C\\nANISOU 3006  CB  TYR A 426    11825  11596   9630   -664     22    214       C\\nATOM   3007  CG  TYR A 426       4.370  -0.345  13.027  1.00 85.70           C\\nANISOU 3007  CG  TYR A 426    11311  11332   9920   -350   -120    -55       C\\nATOM   3008  CD1 TYR A 426       5.706   0.027  13.118  1.00 83.30           C\\nANISOU 3008  CD1 TYR A 426    11097  10869   9684      2   -327   -201       C\\nATOM   3009  CD2 TYR A 426       3.547   0.381  12.176  1.00 83.93           C\\nANISOU 3009  CD2 TYR A 426    10656  11172  10061   -422    -61   -137       C\\nATOM   3010  CE1 TYR A 426       6.206   1.093  12.385  1.00 79.72           C\\nANISOU 3010  CE1 TYR A 426    10330  10311   9648    224   -438   -408       C\\nATOM   3011  CE2 TYR A 426       4.037   1.447  11.441  1.00 82.37           C\\nANISOU 3011  CE2 TYR A 426    10186  10845  10265   -163   -196   -323       C\\nATOM   3012  CZ  TYR A 426       5.368   1.799  11.548  1.00 77.29           C\\nANISOU 3012  CZ  TYR A 426     9656  10030   9679    135   -368   -452       C\\nATOM   3013  OH  TYR A 426       5.859   2.858  10.815  1.00 65.48           O\\nANISOU 3013  OH  TYR A 426     7898   8395   8588    330   -485   -601       O\\nATOM   3014  N   THR A 427       3.583  -4.790  14.059  1.00 94.12           N\\nANISOU 3014  N   THR A 427    13912  11967   9880  -1346    -21   1029       N\\nATOM   3015  CA  THR A 427       2.981  -5.936  14.735  1.00 94.73           C\\nANISOU 3015  CA  THR A 427    14395  12024   9574  -1766    104   1385       C\\nATOM   3016  C   THR A 427       4.036  -6.873  15.301  1.00 93.77           C\\nANISOU 3016  C   THR A 427    14923  11553   9151  -1581   -115   1608       C\\nATOM   3017  O   THR A 427       3.779  -7.565  16.293  1.00107.23           O\\nANISOU 3017  O   THR A 427    16989  13325  10429  -1808    -22   1896       O\\nATOM   3018  CB  THR A 427       2.076  -6.711  13.777  1.00 92.02           C\\nANISOU 3018  CB  THR A 427    14101  11462   9402  -2246    135   1572       C\\nATOM   3019  OG1 THR A 427       2.869  -7.267  12.722  1.00 87.69           O\\nANISOU 3019  OG1 THR A 427    13873  10378   9067  -2083   -148   1577       O\\nATOM   3020  CG2 THR A 427       1.028  -5.801  13.182  1.00 92.49           C\\nANISOU 3020  CG2 THR A 427    13488  11881   9771  -2397    298   1371       C\\nATOM   3021  N   THR A 428       5.216  -6.918  14.687  1.00 86.78           N\\nANISOU 3021  N   THR A 428    14188  10309   8477  -1167   -404   1497       N\\nATOM   3022  CA  THR A 428       6.250  -7.850  15.112  1.00 80.90           C\\nANISOU 3022  CA  THR A 428    14030   9197   7512   -924   -656   1699       C\\nATOM   3023  C   THR A 428       7.087  -7.298  16.260  1.00 88.26           C\\nANISOU 3023  C   THR A 428    14945  10410   8178   -536   -758   1595       C\\nATOM   3024  O   THR A 428       7.228  -7.954  17.297  1.00 98.04           O\\nANISOU 3024  O   THR A 428    16618  11653   8981   -567   -810   1867       O\\nATOM   3025  CB  THR A 428       7.162  -8.200  13.934  1.00 75.14           C\\nANISOU 3025  CB  THR A 428    13433   7992   7124   -626   -905   1599       C\\nATOM   3026  OG1 THR A 428       6.369  -8.438  12.764  1.00 66.95           O\\nANISOU 3026  OG1 THR A 428    12310   6784   6344   -965   -819   1592       O\\nATOM   3027  CG2 THR A 428       7.977  -9.450  14.258  1.00 74.10           C\\nANISOU 3027  CG2 THR A 428    13971   7385   6798   -439  -1156   1861       C\\nATOM   3028  N   PHE A 429       7.642  -6.097  16.092  1.00 82.80           N\\nANISOU 3028  N   PHE A 429    13778   9948   7733   -194   -807   1216       N\\nATOM   3029  CA  PHE A 429       8.628  -5.569  17.024  1.00 85.65           C\\nANISOU 3029  CA  PHE A 429    14115  10520   7909    205   -988   1057       C\\nATOM   3030  C   PHE A 429       8.031  -4.731  18.145  1.00 88.27           C\\nANISOU 3030  C   PHE A 429    14208  11398   7933    109   -780    904       C\\nATOM   3031  O   PHE A 429       8.759  -4.373  19.077  1.00 94.52           O\\nANISOU 3031  O   PHE A 429    15046  12401   8467    386   -940    780       O\\nATOM   3032  CB  PHE A 429       9.666  -4.731  16.274  1.00 81.51           C\\nANISOU 3032  CB  PHE A 429    13220   9923   7826    606  -1176    717       C\\nATOM   3033  CG  PHE A 429      10.610  -5.545  15.451  1.00 86.84           C\\nANISOU 3033  CG  PHE A 429    14151  10141   8702    848  -1415    814       C\\nATOM   3034  CD1 PHE A 429      11.723  -6.132  16.031  1.00 95.71           C\\nANISOU 3034  CD1 PHE A 429    15590  11131   9647   1208  -1714    909       C\\nATOM   3035  CD2 PHE A 429      10.383  -5.736  14.099  1.00 90.50           C\\nANISOU 3035  CD2 PHE A 429    14539  10330   9515    740  -1348    797       C\\nATOM   3036  CE1 PHE A 429      12.597  -6.891  15.275  1.00100.77           C\\nANISOU 3036  CE1 PHE A 429    16434  11359  10493   1488  -1918    962       C\\nATOM   3037  CE2 PHE A 429      11.253  -6.492  13.334  1.00 94.15           C\\nANISOU 3037  CE2 PHE A 429    15239  10395  10137    990  -1533    835       C\\nATOM   3038  CZ  PHE A 429      12.362  -7.070  13.923  1.00 99.97           C\\nANISOU 3038  CZ  PHE A 429    16261  10992  10733   1381  -1805    907       C\\nATOM   3039  N   ASN A 430       6.743  -4.409  18.090  1.00 83.72           N\\nANISOU 3039  N   ASN A 430    13363  11080   7368   -257   -438    882       N\\nATOM   3040  CA  ASN A 430       6.116  -3.571  19.103  1.00 88.98           C\\nANISOU 3040  CA  ASN A 430    13756  12293   7759   -315   -190    673       C\\nATOM   3041  C   ASN A 430       4.910  -4.295  19.678  1.00 94.26           C\\nANISOU 3041  C   ASN A 430    14603  13185   8026   -804    139    994       C\\nATOM   3042  O   ASN A 430       3.949  -4.578  18.954  1.00 90.37           O\\nANISOU 3042  O   ASN A 430    13952  12628   7755  -1162    332   1116       O\\nATOM   3043  CB  ASN A 430       5.708  -2.218  18.523  1.00 82.34           C\\nANISOU 3043  CB  ASN A 430    12274  11632   7378   -219    -60    251       C\\nATOM   3044  CG  ASN A 430       5.177  -1.278  19.577  1.00 86.94           C\\nANISOU 3044  CG  ASN A 430    12575  12746   7711   -183    175    -57       C\\nATOM   3045  OD1 ASN A 430       3.978  -1.247  19.844  1.00 86.57           O\\nANISOU 3045  OD1 ASN A 430    12339  13023   7531   -474    525    -28       O\\nATOM   3046  ND2 ASN A 430       6.069  -0.510  20.193  1.00 93.49           N\\nANISOU 3046  ND2 ASN A 430    13362  13689   8473    174    -14   -380       N\\nATOM   3047  N   ILE A 431       4.963  -4.590  20.979  1.00 96.66           N\\nANISOU 3047  N   ILE A 431    15226  13779   7721   -842    197   1137       N\\nATOM   3048  CA  ILE A 431       3.848  -5.262  21.638  1.00 92.58           C\\nANISOU 3048  CA  ILE A 431    14883  13536   6757  -1346    552   1472       C\\nATOM   3049  C   ILE A 431       2.630  -4.348  21.695  1.00 98.55           C\\nANISOU 3049  C   ILE A 431    15013  14819   7614  -1537    984   1175       C\\nATOM   3050  O   ILE A 431       1.488  -4.806  21.569  1.00 98.81           O\\nANISOU 3050  O   ILE A 431    14936  14997   7611  -2018   1303   1397       O\\nATOM   3051  CB  ILE A 431       4.263  -5.738  23.042  1.00 91.00           C\\nANISOU 3051  CB  ILE A 431    15200  13558   5818  -1318    503   1710       C\\nATOM   3052  N   GLU A 432       2.851  -3.043  21.881  1.00 96.20           N\\nANISOU 3052  N   GLU A 432    14279  14803   7470  -1163    992    657       N\\nATOM   3053  CA  GLU A 432       1.733  -2.109  21.979  1.00 93.30           C\\nANISOU 3053  CA  GLU A 432    13305  14920   7225  -1248   1385    325       C\\nATOM   3054  C   GLU A 432       1.005  -1.971  20.646  1.00 90.82           C\\nANISOU 3054  C   GLU A 432    12560  14400   7549  -1408   1437    316       C\\nATOM   3055  O   GLU A 432      -0.230  -1.927  20.610  1.00 84.30           O\\nANISOU 3055  O   GLU A 432    11363  13912   6757  -1725   1791    333       O\\nATOM   3056  CB  GLU A 432       2.229  -0.750  22.471  1.00 88.42           C\\nANISOU 3056  CB  GLU A 432    12394  14544   6659   -774   1324   -250       C\\nATOM   3057  N   PHE A 433       1.747  -1.901  19.538  1.00 90.26           N\\nANISOU 3057  N   PHE A 433    12509  13817   7970  -1197   1087    288       N\\nATOM   3058  CA  PHE A 433       1.098  -1.850  18.232  1.00 93.03           C\\nANISOU 3058  CA  PHE A 433    12520  13969   8860  -1363   1090    317       C\\nATOM   3059  C   PHE A 433       0.366  -3.155  17.929  1.00 92.59           C\\nANISOU 3059  C   PHE A 433    12717  13789   8674  -1909   1194    776       C\\nATOM   3060  O   PHE A 433      -0.768  -3.136  17.438  1.00 86.48           O\\nANISOU 3060  O   PHE A 433    11554  13195   8111  -2229   1396    805       O\\nATOM   3061  CB  PHE A 433       2.125  -1.540  17.137  1.00 94.23           C\\nANISOU 3061  CB  PHE A 433    12696  13628   9479  -1036    712    208       C\\nATOM   3062  CG  PHE A 433       2.253  -0.070  16.807  1.00 90.02           C\\nANISOU 3062  CG  PHE A 433    11657  13176   9371   -672    669   -233       C\\nATOM   3063  CD1 PHE A 433       1.220   0.604  16.178  1.00 82.18           C\\nANISOU 3063  CD1 PHE A 433    10137  12335   8753   -746    821   -367       C\\nATOM   3064  CD2 PHE A 433       3.413   0.630  17.106  1.00 88.82           C\\nANISOU 3064  CD2 PHE A 433    11559  12920   9269   -265    446   -498       C\\nATOM   3065  CE1 PHE A 433       1.331   1.949  15.867  1.00 78.56           C\\nANISOU 3065  CE1 PHE A 433     9265  11877   8709   -401    756   -738       C\\nATOM   3066  CE2 PHE A 433       3.531   1.976  16.796  1.00 82.75           C\\nANISOU 3066  CE2 PHE A 433    10368  12155   8919     24    394   -882       C\\nATOM   3067  CZ  PHE A 433       2.487   2.635  16.177  1.00 81.74           C\\nANISOU 3067  CZ  PHE A 433     9768  12128   9161    -34    550   -991       C\\nATOM   3068  N   ARG A 434       0.991  -4.296  18.232  1.00 96.08           N\\nANISOU 3068  N   ARG A 434    13805  13913   8786  -2025   1037   1134       N\\nATOM   3069  CA  ARG A 434       0.385  -5.588  17.918  1.00 91.88           C\\nANISOU 3069  CA  ARG A 434    13600  13146   8164  -2562   1089   1576       C\\nATOM   3070  C   ARG A 434      -0.930  -5.778  18.663  1.00 88.38           C\\nANISOU 3070  C   ARG A 434    12942  13229   7411  -3068   1532   1730       C\\nATOM   3071  O   ARG A 434      -1.944  -6.162  18.068  1.00 89.59           O\\nANISOU 3071  O   ARG A 434    12864  13413   7764  -3530   1674   1870       O\\nATOM   3072  CB  ARG A 434       1.360  -6.718  18.249  1.00 91.99           C\\nANISOU 3072  CB  ARG A 434    14390  12689   7871  -2520    823   1923       C\\nATOM   3073  N   LYS A 435      -0.934  -5.515  19.973  1.00 92.30           N\\nANISOU 3073  N   LYS A 435    13491  14183   7397  -3005   1759   1697       N\\nATOM   3074  CA  LYS A 435      -2.157  -5.679  20.753  1.00 95.80           C\\nANISOU 3074  CA  LYS A 435    13709  15207   7485  -3485   2243   1837       C\\nATOM   3075  C   LYS A 435      -3.199  -4.633  20.385  1.00 95.39           C\\nANISOU 3075  C   LYS A 435    12798  15636   7810  -3466   2525   1447       C\\nATOM   3076  O   LYS A 435      -4.399  -4.865  20.566  1.00100.11           O\\nANISOU 3076  O   LYS A 435    13054  16654   8329  -3942   2904   1572       O\\nATOM   3077  CB  LYS A 435      -1.843  -5.617  22.249  1.00100.45           C\\nANISOU 3077  CB  LYS A 435    14594  16206   7366  -3383   2418   1871       C\\nATOM   3078  N   ALA A 436      -2.763  -3.482  19.869  1.00 97.48           N\\nANISOU 3078  N   ALA A 436    12695  15840   8503  -2926   2339    989       N\\nATOM   3079  CA  ALA A 436      -3.711  -2.457  19.446  1.00 99.12           C\\nANISOU 3079  CA  ALA A 436    12109  16422   9131  -2835   2542    627       C\\nATOM   3080  C   ALA A 436      -4.463  -2.884  18.193  1.00 98.71           C\\nANISOU 3080  C   ALA A 436    11791  16164   9549  -3194   2456    809       C\\nATOM   3081  O   ALA A 436      -5.682  -2.702  18.103  1.00 98.79           O\\nANISOU 3081  O   ALA A 436    11222  16613   9701  -3464   2744    764       O\\nATOM   3082  CB  ALA A 436      -2.984  -1.133  19.210  1.00 94.08           C\\nANISOU 3082  CB  ALA A 436    11230  15675   8839  -2179   2321    134       C\\nATOM   3083  N   PHE A 437      -3.753  -3.456  17.217  1.00 90.64           N\\nANISOU 3083  N   PHE A 437    11168  14510   8763  -3193   2056    991       N\\nATOM   3084  CA  PHE A 437      -4.405  -3.888  15.985  1.00 89.75           C\\nANISOU 3084  CA  PHE A 437    10864  14185   9052  -3536   1925   1136       C\\nATOM   3085  C   PHE A 437      -5.403  -5.004  16.256  1.00 98.61           C\\nANISOU 3085  C   PHE A 437    12055  15479   9935  -4263   2173   1518       C\\nATOM   3086  O   PHE A 437      -6.491  -5.031  15.669  1.00 97.68           O\\nANISOU 3086  O   PHE A 437    11436  15585  10092  -4617   2265   1534       O\\nATOM   3087  CB  PHE A 437      -3.365  -4.353  14.965  1.00 85.17           C\\nANISOU 3087  CB  PHE A 437    10775  12904   8681  -3381   1477   1231       C\\nATOM   3088  CG  PHE A 437      -2.480  -3.255  14.437  1.00 86.40           C\\nANISOU 3088  CG  PHE A 437    10779  12886   9165  -2763   1230    890       C\\nATOM   3089  CD1 PHE A 437      -2.661  -1.937  14.822  1.00 90.40           C\\nANISOU 3089  CD1 PHE A 437    10767  13767   9814  -2388   1365    522       C\\nATOM   3090  CD2 PHE A 437      -1.469  -3.548  13.540  1.00 80.59           C\\nANISOU 3090  CD2 PHE A 437    10422  11598   8603  -2569    873    931       C\\nATOM   3091  CE1 PHE A 437      -1.838  -0.938  14.328  1.00 85.90           C\\nANISOU 3091  CE1 PHE A 437    10090  12981   9568  -1879   1127    241       C\\nATOM   3092  CE2 PHE A 437      -0.645  -2.555  13.044  1.00 80.08           C\\nANISOU 3092  CE2 PHE A 437    10206  11388   8833  -2065    672    655       C\\nATOM   3093  CZ  PHE A 437      -0.831  -1.248  13.438  1.00 81.28           C\\nANISOU 3093  CZ  PHE A 437     9867  11875   9140  -1744    789    329       C\\nATOM   3094  N   LEU A 438      -5.047  -5.938  17.144  1.00 97.43           N\\nANISOU 3094  N   LEU A 438    12520  15222   9276  -4511   2262   1848       N\\nATOM   3095  CA  LEU A 438      -5.930  -7.059  17.446  1.00 99.16           C\\nANISOU 3095  CA  LEU A 438    12887  15540   9250  -5265   2497   2270       C\\nATOM   3096  C   LEU A 438      -7.187  -6.605  18.176  1.00104.88           C\\nANISOU 3096  C   LEU A 438    12926  17091   9832  -5548   3020   2189       C\\nATOM   3097  O   LEU A 438      -8.233  -7.257  18.066  1.00112.28           O\\nANISOU 3097  O   LEU A 438    13646  18228  10786  -6211   3228   2440       O\\nATOM   3098  CB  LEU A 438      -5.179  -8.106  18.269  1.00101.79           C\\nANISOU 3098  CB  LEU A 438    14093  15526   9057  -5410   2445   2676       C\\nATOM   3099  N   LYS A 439      -7.108  -5.501  18.923  1.00104.77           N\\nANISOU 3099  N   LYS A 439    12553  17573   9684  -5064   3242   1817       N\\nATOM   3100  CA  LYS A 439      -8.295  -4.960  19.574  1.00111.86           C\\nANISOU 3100  CA  LYS A 439    12728  19296  10480  -5232   3763   1648       C\\nATOM   3101  C   LYS A 439      -9.200  -4.234  18.588  1.00113.57           C\\nANISOU 3101  C   LYS A 439    12089  19730  11334  -5165   3740   1359       C\\nATOM   3102  O   LYS A 439     -10.419  -4.192  18.788  1.00116.22           O\\nANISOU 3102  O   LYS A 439    11788  20658  11710  -5514   4113   1349       O\\nATOM   3103  CB  LYS A 439      -7.894  -4.019  20.711  1.00111.35           C\\nANISOU 3103  CB  LYS A 439    12602  19665  10042  -4703   3997   1288       C\\nATOM   3104  N   ILE A 440      -8.629  -3.664  17.526  1.00111.11           N\\nANISOU 3104  N   ILE A 440    11741  18958  11519  -4713   3295   1139       N\\nATOM   3105  CA  ILE A 440      -9.451  -3.036  16.502  1.00110.51           C\\nANISOU 3105  CA  ILE A 440    10923  19028  12037  -4650   3192    931       C\\nATOM   3106  C   ILE A 440     -10.182  -4.088  15.675  1.00112.85           C\\nANISOU 3106  C   ILE A 440    11191  19185  12503  -5352   3077   1285       C\\nATOM   3107  O   ILE A 440     -11.326  -3.874  15.259  1.00112.91           O\\nANISOU 3107  O   ILE A 440    10465  19613  12823  -5584   3184   1219       O\\nATOM   3108  CB  ILE A 440      -8.581  -2.115  15.629  1.00104.69           C\\nANISOU 3108  CB  ILE A 440    10219  17834  11725  -3988   2753    640       C\\nATOM   3109  CG1 ILE A 440      -7.927  -1.040  16.500  1.00107.61           C\\nANISOU 3109  CG1 ILE A 440    10580  18352  11953  -3351   2868    257       C\\nATOM   3110  CG2 ILE A 440      -9.411  -1.469  14.537  1.00101.39           C\\nANISOU 3110  CG2 ILE A 440     9088  17539  11896  -3905   2594    477       C\\nATOM   3111  CD1 ILE A 440      -7.131  -0.015  15.728  1.00100.57           C\\nANISOU 3111  CD1 ILE A 440     9658  17052  11502  -2734   2483    -35       C\\nATOM   3112  N   LEU A 441      -9.554  -5.245  15.440  1.00112.02           N\\nANISOU 3112  N   LEU A 441    11866  18490  12207  -5698   2844   1648       N\\nATOM   3113  CA  LEU A 441     -10.167  -6.342  14.697  1.00113.38           C\\nANISOU 3113  CA  LEU A 441    12136  18432  12510  -6402   2704   1969       C\\nATOM   3114  C   LEU A 441     -10.959  -7.287  15.593  1.00125.26           C\\nANISOU 3114  C   LEU A 441    13779  20090  13724  -6864   2989   2236       C\\nATOM   3115  O   LEU A 441     -11.000  -8.499  15.335  1.00130.59           O\\nANISOU 3115  O   LEU A 441    14979  20276  14364  -7284   2800   2536       O\\nATOM   3116  CB  LEU A 441      -9.096  -7.115  13.924  1.00105.56           C\\nANISOU 3116  CB  LEU A 441    11981  16582  11546  -6372   2234   2137       C\\nATOM   3117  CG  LEU A 441      -8.272  -6.304  12.915  1.00100.01           C\\nANISOU 3117  CG  LEU A 441    11276  15521  11203  -5710   1825   1833       C\\nATOM   3118  CD1 LEU A 441      -7.049  -7.083  12.435  1.00 92.92           C\\nANISOU 3118  CD1 LEU A 441    11249  13839  10218  -5600   1460   1975       C\\nATOM   3119  CD2 LEU A 441      -9.133  -5.880  11.735  1.00101.27           C\\nANISOU 3119  CD2 LEU A 441    10791  15843  11843  -5803   1635   1687       C\\nATOM   3120  N   HIS A 442     -11.587  -6.766  16.640  1.00118.20           N\\nANISOU 3120  N   HIS A 442    12431  19851  12628  -6779   3439   2114       N\\nATOM   3121  CA  HIS A 442     -12.365  -7.591  17.554  1.00126.48           C\\nANISOU 3121  CA  HIS A 442    13562  21110  13385  -7224   3754   2376       C\\nATOM   3122  C   HIS A 442     -13.375  -6.752  18.337  1.00131.96           C\\nANISOU 3122  C   HIS A 442    13462  22622  14057  -7071   4227   2114       C\\nATOM   3123  O   HIS A 442     -14.028  -5.864  17.785  1.00131.46           O\\nANISOU 3123  O   HIS A 442    12638  22887  14424  -6809   4221   1787       O\\nATOM   3124  CB  HIS A 442     -11.436  -8.335  18.515  1.00127.27           C\\nANISOU 3124  CB  HIS A 442    14545  20900  12913  -7295   3807   2692       C\\nCONECT    1    2\\nCONECT    2    1    5    3\\nCONECT    3    2    4    6\\nCONECT    4    3\\nCONECT    5    2\\nCONECT    6    7    3\\nCONECT    7    6   10    8\\nCONECT    8    7    9   11\\nCONECT    9    8\\nCONECT   10    7\\nCONECT   58   59   53\\nCONECT   59   58   62   60\\nCONECT   60   59   61   63\\nCONECT   61   60\\nCONECT   62   59\\nCONECT  194  195  185\\nCONECT  195  194  198  196\\nCONECT  196  195  197  199\\nCONECT  197  196\\nCONECT  198  195\\nCONECT  199  200  196\\nCONECT  200  199  203  201\\nCONECT  201  200  202  204\\nCONECT  202  201\\nCONECT  203  200\\nCONECT  451  452  444\\nCONECT  452  451  455  453\\nCONECT  453  452  454  456\\nCONECT  454  453\\nCONECT  455  452\\nCONECT  467  468  465\\nCONECT  468  467  471  469\\nCONECT  469  468  470  472\\nCONECT  470  469\\nCONECT  471  468\\nCONECT  486  487  474\\nCONECT  487  486  490  488\\nCONECT  488  487  489  491\\nCONECT  489  488\\nCONECT  490  487\\nCONECT  542 1057  541\\nCONECT  772  778  773  766\\nCONECT  773  772  776  774\\nCONECT  774  773  775\\nCONECT  775  774\\nCONECT  776  773  777\\nCONECT  777  776  778\\nCONECT  778  772  777\\nCONECT  779  780\\nCONECT  780  779  783  781\\nCONECT  781  780  782  784\\nCONECT  782  781\\nCONECT  783  780\\nCONECT  784  785  781\\nCONECT  785  784  788  786\\nCONECT  786  785  787  789\\nCONECT  787  786\\nCONECT  788  785\\nCONECT  801  802  791\\nCONECT  802  801  805  803\\nCONECT  803  802  804  806\\nCONECT  804  803\\nCONECT  805  802\\nCONECT  812  813  808\\nCONECT  813  812  816  814\\nCONECT  814  813  815  817\\nCONECT  815  814\\nCONECT  816  813\\nCONECT  817  818  814\\nCONECT  818  817  821  819\\nCONECT  819  818  820  822\\nCONECT  820  819\\nCONECT  821  818\\nCONECT 1018 1019 1012\\nCONECT 1019 1018 1022 1020\\nCONECT 1020 1019 1021 1023\\nCONECT 1021 1020\\nCONECT 1022 1019\\nCONECT 1028 1029 1025\\nCONECT 1029 1028 1032 1030\\nCONECT 1030 1029 1031 1033\\nCONECT 1031 1030\\nCONECT 1032 1029\\nCONECT 1033 1034 1030\\nCONECT 1034 1033 1037 1035\\nCONECT 1035 1034 1036 1038\\nCONECT 1036 1035\\nCONECT 1037 1034\\nCONECT 1038 1039 1035\\nCONECT 1039 1038 1042 1040\\nCONECT 1040 1039 1041 1043\\nCONECT 1041 1040\\nCONECT 1042 1039\\nCONECT 1057  542 1056\\nCONECT 1282 1283 1276\\nCONECT 1283 1282 1286 1284\\nCONECT 1284 1283 1285 1289\\nCONECT 1285 1284\\nCONECT 1286 1283 1287\\nCONECT 1287 1286 1288\\nCONECT 1288 1287\\nCONECT 1332 1333 1326\\nCONECT 1333 1332 1336 1334\\nCONECT 1334 1333 1335 1337\\nCONECT 1335 1334\\nCONECT 1336 1333\\nCONECT 1337 1338 1334\\nCONECT 1338 1337 1341 1339\\nCONECT 1339 1338 1340 1342\\nCONECT 1340 1339\\nCONECT 1341 1338\\nCONECT 1364 1365 1355\\nCONECT 1365 1364 1368 1366\\nCONECT 1366 1365 1367 1369\\nCONECT 1367 1366\\nCONECT 1368 1365\\nCONECT 1369 1370 1366\\nCONECT 1370 1369 1373 1371\\nCONECT 1371 1370 1372 1374\\nCONECT 1372 1371\\nCONECT 1373 1370\\nCONECT 1493 1494 1487\\nCONECT 1494 1493 1497 1495\\nCONECT 1495 1494 1496 1498\\nCONECT 1496 1495\\nCONECT 1497 1494\\nCONECT 1518 1519 1508\\nCONECT 1519 1518 1522 1520\\nCONECT 1520 1519 1521 1523\\nCONECT 1521 1520\\nCONECT 1522 1519\\nCONECT 1538 1539 1533\\nCONECT 1539 1538 1542 1540\\nCONECT 1540 1539 1541 1543\\nCONECT 1541 1540\\nCONECT 1542 1539\\nCONECT 1612 1613 1604\\nCONECT 1613 1612 1616 1614\\nCONECT 1614 1613 1615 1617\\nCONECT 1615 1614\\nCONECT 1616 1613\\nCONECT 1617 1618 1614\\nCONECT 1618 1617 1621 1619\\nCONECT 1619 1618 1620 1622\\nCONECT 1620 1619\\nCONECT 1621 1618\\nCONECT 1629 1630 1624\\nCONECT 1630 1629 1633 1631\\nCONECT 1631 1630 1632 1634\\nCONECT 1632 1631\\nCONECT 1633 1630\\nCONECT 1634 1635 1631\\nCONECT 1635 1634 1638 1636\\nCONECT 1636 1635 1637 1639\\nCONECT 1637 1636\\nCONECT 1638 1635\\nCONECT 1646 1647 1641\\nCONECT 1647 1646 1650 1648\\nCONECT 1648 1647 1649 1651\\nCONECT 1649 1648\\nCONECT 1650 1647\\nCONECT 1659 1660 1653\\nCONECT 1660 1659 1663 1661\\nCONECT 1661 1660 1662 1664\\nCONECT 1662 1661\\nCONECT 1663 1660\\nCONECT 1683 1684 1676\\nCONECT 1684 1683 1687 1685\\nCONECT 1685 1684 1686 1688\\nCONECT 1686 1685\\nCONECT 1687 1684\\nCONECT 1688 1689 1685\\nCONECT 1689 1688 1692 1690\\nCONECT 1690 1689 1691 1693\\nCONECT 1691 1690\\nCONECT 1692 1689\\nCONECT 1709 1710 1703\\nCONECT 1710 1709 1713 1711\\nCONECT 1711 1710 1712 1714\\nCONECT 1712 1711\\nCONECT 1713 1710\\nCONECT 1719 1720 1716\\nCONECT 1720 1719 1723 1721\\nCONECT 1721 1720 1722 1724\\nCONECT 1722 1721\\nCONECT 1723 1720\\nCONECT 1739 1740 1730\\nCONECT 1740 1739 1743 1741\\nCONECT 1741 1740 1742 1744\\nCONECT 1742 1741\\nCONECT 1743 1740\\nCONECT 1744 1745 1741\\nCONECT 1745 1744 1748 1746\\nCONECT 1746 1745 1747 1749\\nCONECT 1747 1746\\nCONECT 1748 1745\\nCONECT 1749 1750 1746\\nCONECT 1750 1749 1753 1751\\nCONECT 1751 1750 1752 1754\\nCONECT 1752 1751\\nCONECT 1753 1750\\nCONECT 1758 1759 1756\\nCONECT 1759 1758 1762 1760\\nCONECT 1760 1759 1761 1763\\nCONECT 1761 1760\\nCONECT 1762 1759\\nCONECT 1778 1779 1773\\nCONECT 1779 1778 1782 1780\\nCONECT 1780 1779 1781 1783\\nCONECT 1781 1780\\nCONECT 1782 1779\\nCONECT 1814 1815 1807\\nCONECT 1815 1814 1818 1816\\nCONECT 1816 1815 1817 1819\\nCONECT 1817 1816\\nCONECT 1818 1815\\nCONECT 1926 1927 1920\\nCONECT 1927 1926 1930 1928\\nCONECT 1928 1927 1929 1931\\nCONECT 1929 1928\\nCONECT 1930 1927\\nCONECT 1944 1945 1941\\nCONECT 1945 1944 1948 1946\\nCONECT 1946 1945 1947 1949\\nCONECT 1947 1946\\nCONECT 1948 1945\\nCONECT 1957 1958 1951\\nCONECT 1958 1957 1961 1959\\nCONECT 1959 1958 1960 1962\\nCONECT 1960 1959\\nCONECT 1961 1958\\nCONECT 2187 2188 2182\\nCONECT 2188 2187 2191 2189\\nCONECT 2189 2188 2190 2192\\nCONECT 2190 2189\\nCONECT 2191 2188\\nCONECT 2285 2286 2273\\nCONECT 2286 2285 2289 2287\\nCONECT 2287 2286 2288 2290\\nCONECT 2288 2287\\nCONECT 2289 2286\\nCONECT 2309 2310 2306\\nCONECT 2310 2309 2313 2311\\nCONECT 2311 2310 2312 2314\\nCONECT 2312 2311\\nCONECT 2313 2310\\nCONECT 2335 2336 2332\\nCONECT 2336 2335 2339 2337\\nCONECT 2337 2336 2338 2340\\nCONECT 2338 2337\\nCONECT 2339 2336\\nCONECT 2346 2347 2342\\nCONECT 2347 2346 2350 2348\\nCONECT 2348 2347 2349 2351\\nCONECT 2349 2348\\nCONECT 2350 2347\\nCONECT 2385 2386 2379\\nCONECT 2386 2385 2389 2387\\nCONECT 2387 2386 2388 2390\\nCONECT 2388 2387\\nCONECT 2389 2386\\nCONECT 2428 2429 2425\\nCONECT 2429 2428 2432 2430\\nCONECT 2430 2429 2431 2433\\nCONECT 2431 2430\\nCONECT 2432 2429\\nCONECT 2506 2507 2504\\nCONECT 2507 2506 2510 2508\\nCONECT 2508 2507 2509 2511\\nCONECT 2509 2508\\nCONECT 2510 2507\\nCONECT 2538 2539 2535\\nCONECT 2539 2538 2542 2540\\nCONECT 2540 2539 2541\\nCONECT 2541 2540\\nCONECT 2542 2539 2543\\nCONECT 2543 2542 2544 2545\\nCONECT 2544 2543 2546\\nCONECT 2545 2543 2547\\nCONECT 2546 2544 2548\\nCONECT 2547 2545 2548\\nCONECT 2548 2546 2547 2549\\nCONECT 2549 2548\\nCONECT 2550 2551\\nCONECT 2551 2550 2554 2552\\nCONECT 2552 2551 2553 2555\\nCONECT 2553 2552\\nCONECT 2554 2551\\nCONECT 2555 2556 2552\\nCONECT 2556 2555 2559 2557\\nCONECT 2557 2556 2558 2560\\nCONECT 2558 2557\\nCONECT 2559 2556\\nCONECT 2560 2561 2557\\nCONECT 2561 2560 2564 2562\\nCONECT 2562 2561 2563 2565\\nCONECT 2563 2562\\nCONECT 2564 2561\\nCONECT 2565 2566 2562\\nCONECT 2566 2565 2569 2567\\nCONECT 2567 2566 2568 2570\\nCONECT 2568 2567\\nCONECT 2569 2566\\nCONECT 2579 2580 2572\\nCONECT 2580 2579 2583 2581\\nCONECT 2581 2580 2582 2584\\nCONECT 2582 2581\\nCONECT 2583 2580\\nCONECT 2584 2585 2581\\nCONECT 2585 2584 2588 2586\\nCONECT 2586 2585 2587 2589\\nCONECT 2587 2586\\nCONECT 2588 2585\\nCONECT 2768 2769 2760\\nCONECT 2769 2768 2772 2770\\nCONECT 2770 2769 2771 2773\\nCONECT 2771 2770\\nCONECT 2772 2769\\nCONECT 2797 2798 2791\\nCONECT 2798 2797 2801 2799\\nCONECT 2799 2798 2800 2802\\nCONECT 2800 2799\\nCONECT 2801 2798\\nCONECT 2807 2818 2806\\nCONECT 2808 2809 2804\\nCONECT 2809 2808 2812 2810\\nCONECT 2810 2809 2811 2813\\nCONECT 2811 2810\\nCONECT 2812 2809\\nCONECT 2818 2807 2817\\nCONECT 2849 2850 2844\\nCONECT 2850 2849 2853 2851\\nCONECT 2851 2850 2852 2854\\nCONECT 2852 2851\\nCONECT 2853 2850\\nCONECT 2854 2855 2851\\nCONECT 2855 2854 2858 2856\\nCONECT 2856 2855 2857 2859\\nCONECT 2857 2856\\nCONECT 2858 2855\\nCONECT 3047 3048 3041\\nCONECT 3048 3047 3051 3049\\nCONECT 3049 3048 3050 3052\\nCONECT 3050 3049\\nCONECT 3051 3048\\nCONECT 3052 3053 3049\\nCONECT 3053 3052 3056 3054\\nCONECT 3054 3053 3055 3057\\nCONECT 3055 3054\\nCONECT 3056 3053\\nCONECT 3068 3069 3059\\nCONECT 3069 3068 3072 3070\\nCONECT 3070 3069 3071 3073\\nCONECT 3071 3070\\nCONECT 3072 3069\\nCONECT 3073 3074 3070\\nCONECT 3074 3073 3077 3075\\nCONECT 3075 3074 3076 3078\\nCONECT 3076 3075\\nCONECT 3077 3074\\nCONECT 3094 3095 3085\\nCONECT 3095 3094 3098 3096\\nCONECT 3096 3095 3097 3099\\nCONECT 3097 3096\\nCONECT 3098 3095\\nCONECT 3099 3100 3096\\nCONECT 3100 3099 3103 3101\\nCONECT 3101 3100 3102 3104\\nCONECT 3102 3101\\nCONECT 3103 3100\\nCONECT 3120 3121 3114\\nCONECT 3121 3120 3124 3122\\nCONECT 3122 3121 3123\\nCONECT 3123 3122\\nCONECT 3124 3121\\nEND\\n\",\"pdb\");\n",
       "\tviewer_1716802976377794.setStyle({\"model\": 0},{\"cartoon\": {}});\n",
       "\tviewer_1716802976377794.addSurface(null,{\"opacity\": 1, \"color\": \"lightgray\"});\n",
       "\tviewer_1716802976377794.addModels(\"HETATM    1 C18  UNL   1        7.832   6.691 -12.018  1.00  0.00           C  \\nHETATM    2 C19  UNL   1        9.368   6.654 -12.071  1.00  0.00           C  \\nHETATM    3 C20  UNL   1        9.972   5.608 -13.005  1.00  0.00           C  \\nHETATM    4 C21  UNL   1       11.334   5.730 -13.375  1.00  0.00           C  \\nHETATM    5 C22  UNL   1       11.940   4.833 -14.261  1.00  0.00           C  \\nHETATM    6 C23  UNL   1       11.171   3.816 -14.786  1.00  0.00           C  \\nHETATM    7 C24  UNL   1        9.823   3.679 -14.439  1.00  0.00           C  \\nHETATM    8 C25  UNL   1        9.214   4.558 -13.551  1.00  0.00           C  \\nHETATM    9 C26  UNL   1        9.232   2.514 -15.184  1.00  0.00           C  \\nHETATM   10 C27  UNL   1       10.425   2.052 -15.980  1.00  0.00           C  \\nHETATM   11 C28  UNL   1       11.526   2.785 -15.746  1.00  0.00           C  \\nHETATM   12 N5   UNL   1        8.742   1.468 -14.245  1.00  0.00           N1+\\nHETATM   13 C29  UNL   1        7.291   1.106 -14.333  1.00  0.00           C  \\nHETATM   14 C30  UNL   1        6.421   2.209 -13.718  1.00  0.00           C  \\nHETATM   15 C31  UNL   1        5.146   1.645 -13.082  1.00  0.00           C  \\nHETATM   16 C32  UNL   1        4.691   0.369 -13.775  1.00  0.00           C  \\nHETATM   17 O3   UNL   1        5.685  -0.659 -13.764  1.00  0.00           O  \\nHETATM   18 C33  UNL   1        7.032  -0.225 -13.617  1.00  0.00           C  \\nHETATM   19 C34  UNL   1        9.978   6.653 -10.648  1.00  0.00           C  \\nHETATM   20 C35  UNL   1       10.751   7.908 -10.205  1.00  0.00           C  \\nHETATM   21 C36  UNL   1       10.928   7.924  -8.693  1.00  0.00           C  \\nHETATM   22 C37  UNL   1       10.998   6.721  -7.973  1.00  0.00           C  \\nHETATM   23 C38  UNL   1       11.134   6.724  -6.585  1.00  0.00           C  \\nHETATM   24 C39  UNL   1       11.197   7.931  -5.880  1.00  0.00           C  \\nHETATM   25 C40  UNL   1       11.098   9.150  -6.579  1.00  0.00           C  \\nHETATM   26 C41  UNL   1       10.978   9.134  -7.982  1.00  0.00           C  \\nHETATM   27 C42  UNL   1       11.160  10.465  -5.849  1.00  0.00           C  \\nHETATM   28 N6   UNL   1       10.910  10.329  -4.383  1.00  0.00           N1+\\nHETATM   29 C43  UNL   1       11.722   9.234  -3.773  1.00  0.00           C  \\nHETATM   30 C44  UNL   1       11.299   7.895  -4.372  1.00  0.00           C  \\nHETATM   31 O4   UNL   1       12.016   8.010 -10.855  1.00  0.00           O  \\nCONECT    1    2\\nCONECT    2    1    3   19\\nCONECT    3    2    4    4    8\\nCONECT   19    2   20\\nCONECT    4    3    3    5\\nCONECT    8    3    7    7\\nCONECT    5    4    6    6\\nCONECT    6    5    5    7   11\\nCONECT    7    6    8    8    9\\nCONECT   11    6   10   10\\nCONECT    9    7   10   12\\nCONECT   10    9   11   11\\nCONECT   12    9   13\\nCONECT   13   12   14   18\\nCONECT   14   13   15\\nCONECT   18   13   17\\nCONECT   15   14   16\\nCONECT   16   15   17\\nCONECT   17   16   18\\nCONECT   20   19   21   31\\nCONECT   21   20   22   22   26\\nCONECT   31   20\\nCONECT   22   21   21   23\\nCONECT   26   21   25   25\\nCONECT   23   22   24   24\\nCONECT   24   23   23   25   30\\nCONECT   25   24   26   26   27\\nCONECT   30   24   29\\nCONECT   27   25   28\\nCONECT   28   27   29\\nCONECT   29   28   30\\nEND\",\"pdb\");\n",
       "\tviewer_1716802976377794.setStyle({\"model\": 1},{\"stick\": {\"color\": \"cyan\"}});\n",
       "\tviewer_1716802976377794.zoomTo();\n",
       "viewer_1716802976377794.render();\n",
       "});\n",
       "</script>"
      ]
     },
     "metadata": {},
     "output_type": "display_data"
    }
   ],
   "source": [
    "# we will use Py3DMol to visualize the protein and ligand together\n",
    "import py3Dmol as p3d\n",
    "\n",
    "def show_ligand_and_protein(ligand):\n",
    "    view = p3d.view(width=800, height=600)\n",
    "\n",
    "    # add the protein\n",
    "    view.addModels(open(\"./files/DRD2.pdb\").read(), \"pdb\")\n",
    "    view.setStyle({\"model\": 0}, {\"cartoon\": {}})\n",
    "    view.addSurface(None, {\"opacity\" : 1, \"color\": \"lightgray\"})\n",
    "\n",
    "    # add the ligand\n",
    "    # (we have to get the PDB-text for Py3DMol)\n",
    "    pdb = bam.utils.pdb.encode_pdb(ligand)\n",
    "    view.addModels(pdb, \"pdb\")\n",
    "    view.setStyle({\"model\": 1}, {\"stick\": {\"color\" : \"cyan\"}})\n",
    "    view.zoomTo()\n",
    "    view.show()\n",
    "\n",
    "show_ligand_and_protein(ligand)"
   ]
  },
  {
   "cell_type": "markdown",
   "metadata": {},
   "source": [
    "Okey, cool, there is a molecule in the pocket where Risperidone is supposed to bind! Now that we have a system that appears to be working we can think of turning it into a simple \"screening\" tool of sorts, by for instance, simply repeatedly running the procedure above from random starting ligands. Below is some example code that would do the trick. The code is super inefficient though since we are running each optimization sequentially, any real application of this kind should definitely use a parallel approach here!"
   ]
  },
  {
   "cell_type": "code",
   "execution_count": 22,
   "metadata": {},
   "outputs": [
    {
     "name": "stdout",
     "output_type": "stream",
     "text": [
      "Run 1 done with score -8.9\n",
      "Run 2 done with score -8.3\n"
     ]
    }
   ],
   "source": [
    "# how many times we will run the procedure\n",
    "n_runs = 2\n",
    "\n",
    "# define a function that will run the optimization\n",
    "# (this is super down-scaled of course, so we don't have to wait so long...)\n",
    "def _run(i):\n",
    "    starting = sampler.random(n_fragments)\n",
    "    metadata[\"best_score\"] = np.inf \n",
    "    metadata[\"ligand\"] = None\n",
    "    \n",
    "    out = optimize.minimize(score, starting.flatten(), method=\"Nelder-Mead\", options={\"maxiter\" : 1})\n",
    "\n",
    "    print(f\"Run {i+1} done with score {out.fun}\")\n",
    "    results.append(dict(metadata))\n",
    "    return results[-1]\n",
    "\n",
    "results = [_run(i) for i in range(n_runs)]"
   ]
  },
  {
   "cell_type": "markdown",
   "metadata": {},
   "source": [
    "We can inspect the ligands that were produces:"
   ]
  },
  {
   "cell_type": "code",
   "execution_count": 25,
   "metadata": {},
   "outputs": [
    {
     "data": {
      "image/png": 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",
      "text/plain": [
       "<Figure size 800x500 with 2 Axes>"
      ]
     },
     "metadata": {},
     "output_type": "display_data"
    }
   ],
   "source": [
    "import matplotlib.pyplot as plt\n",
    "\n",
    "ligands = [get_ligand(i[\"ligand\"]) for i in results]\n",
    "fig, axs = plt.subplots(2, len(ligands) // 2, figsize=(8, 5))\n",
    "\n",
    "# draw all ligands\n",
    "for idx, l in enumerate(ligands):\n",
    "    if l is not None:\n",
    "        ax = axs.flat[idx]\n",
    "        ax.imshow(l.chem2dview().draw())\n",
    "        ax.axis(\"off\")\n",
    "        ax.set_title(f\"Score: {results[idx]['best_score']:.2f}\")"
   ]
  },
  {
   "cell_type": "markdown",
   "metadata": {},
   "source": [
    "Okey, cool! And just like this we have got some new candidate ligands! Of course, this entire example is not a fully developed ligand screening pipeline, it's just a toy example, but it's still quite nice to see that it works and with a relatively moderate amount of code too!"
   ]
  },
  {
   "cell_type": "markdown",
   "metadata": {},
   "source": [
    "Let's end this tutorial by visualizing the two other ligands that we just made also with the protein:"
   ]
  },
  {
   "cell_type": "code",
   "execution_count": 26,
   "metadata": {},
   "outputs": [
    {
     "data": {
      "application/3dmoljs_load.v0": "<div id=\"3dmolviewer_1716807258080235\"  style=\"position: relative; width: 800px; height: 600px;\">\n        <p id=\"3dmolwarning_1716807258080235\" style=\"background-color:#ffcccc;color:black\">You appear to be running in JupyterLab (or JavaScript failed to load for some other reason).  You need to install the 3dmol extension: <br>\n        <tt>jupyter labextension install jupyterlab_3dmol</tt></p>\n        </div>\n<script>\n\nvar loadScriptAsync = function(uri){\n  return new Promise((resolve, reject) => {\n    //this is to ignore the existence of requirejs amd\n    var savedexports, savedmodule;\n    if (typeof exports !== 'undefined') savedexports = exports;\n    else exports = {}\n    if (typeof module !== 'undefined') savedmodule = module;\n    else module = {}\n\n    var tag = document.createElement('script');\n    tag.src = uri;\n    tag.async = true;\n    tag.onload = () => {\n        exports = savedexports;\n        module = savedmodule;\n        resolve();\n    };\n  var firstScriptTag = document.getElementsByTagName('script')[0];\n  firstScriptTag.parentNode.insertBefore(tag, firstScriptTag);\n});\n};\n\nif(typeof $3Dmolpromise === 'undefined') {\n$3Dmolpromise = null;\n  $3Dmolpromise = loadScriptAsync('https://cdnjs.cloudflare.com/ajax/libs/3Dmol/2.0.3/3Dmol-min.js');\n}\n\nvar viewer_1716807258080235 = null;\nvar warn = document.getElementById(\"3dmolwarning_1716807258080235\");\nif(warn) {\n    warn.parentNode.removeChild(warn);\n}\n$3Dmolpromise.then(function() {\nviewer_1716807258080235 = $3Dmol.createViewer(document.getElementById(\"3dmolviewer_1716807258080235\"),{backgroundColor:\"white\"});\nviewer_1716807258080235.zoomTo();\n\tviewer_1716807258080235.addModels(\"HEADER    MEMBRANE PROTEIN                        02-MAR-18   6CM4              \\nTITLE     STRUCTURE OF THE D2 DOPAMINE RECEPTOR BOUND TO THE ATYPICAL           \\nTITLE    2 ANTIPSYCHOTIC DRUG RISPERIDONE                                       \\nCOMPND    MOL_ID: 1;                                                            \\nCOMPND   2 MOLECULE: D(2) DOPAMINE RECEPTOR, ENDOLYSIN CHIMERA;                 \\nCOMPND   3 CHAIN: A;                                                            \\nCOMPND   4 SYNONYM: DOPAMINE D2 RECEPTOR, LYSIS PROTEIN, LYSOZYME, MURAMIDASE,  \\nCOMPND   5 DOPAMINE D2 RECEPTOR;                                                \\nCOMPND   6 EC: 3.2.1.17;                                                        \\nCOMPND   7 ENGINEERED: YES                                                      \\nSOURCE    MOL_ID: 1;                                                            \\nSOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, ENTEROBACTERIA PHAGE T4;          \\nSOURCE   3 ORGANISM_COMMON: HUMAN, BACTERIOPHAGE T4;                            \\nSOURCE   4 ORGANISM_TAXID: 9606, 10665;                                         \\nSOURCE   5 GENE: DRD2, E, T4TP126;                                              \\nSOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            \\nSOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             \\nSOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;                                       \\nSOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          \\nSOURCE  10 EXPRESSION_SYSTEM_PLASMID: PFASTBAC1-HM                              \\nKEYWDS    GPCR, D2, DOPAMINE RECEPTOR, ANTIPSYCHOTIC, RISPERIDONE, MEMBRANE     \\nKEYWDS   2 PROTEIN                                                              \\nEXPDTA    X-RAY DIFFRACTION                                                     \\nAUTHOR    S.WANG,T.CHE,A.LEVIT,B.K.SHOICHET,D.WACKER,B.L.ROTH                   \\nREVDAT   6   04-OCT-23 6CM4    1       REMARK                                   \\nREVDAT   5   27-NOV-19 6CM4    1       REMARK                                   \\nREVDAT   4   20-FEB-19 6CM4    1       REMARK                                   \\nREVDAT   3   11-APR-18 6CM4    1       DBREF                                    \\nREVDAT   2   21-MAR-18 6CM4    1       JRNL                                     \\nREVDAT   1   14-MAR-18 6CM4    0                                                \\nSPRSDE     14-MAR-18 6CM4      6C38                                             \\nJRNL        AUTH   S.WANG,T.CHE,A.LEVIT,B.K.SHOICHET,D.WACKER,B.L.ROTH          \\nJRNL        TITL   STRUCTURE OF THE D2 DOPAMINE RECEPTOR BOUND TO THE ATYPICAL  \\nJRNL        TITL 2 ANTIPSYCHOTIC DRUG RISPERIDONE.                              \\nJRNL        REF    NATURE                        V. 555   269 2018              \\nJRNL        REFN                   ESSN 1476-4687                               \\nJRNL        PMID   29466326                                                     \\nJRNL        DOI    10.1038/NATURE25758                                          \\nREMARK   2                                                                      \\nREMARK   2 RESOLUTION.    2.87 ANGSTROMS.                                       \\nREMARK   3                                                                      \\nREMARK   3 REFINEMENT.                                                          \\nREMARK   3   PROGRAM     : PHENIX (1.12_2829: ???)                              \\nREMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            \\nREMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           \\nREMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            \\nREMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              \\nREMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               \\nREMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           \\nREMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  \\nREMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  \\nREMARK   3                                                                      \\nREMARK   3    REFINEMENT TARGET : ML                                            \\nREMARK   3                                                                      \\nREMARK   3  DATA USED IN REFINEMENT.                                            \\nREMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.87                           \\nREMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.55                          \\nREMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.360                          \\nREMARK   3   COMPLETENESS FOR RANGE        (%) : 95.2                           \\nREMARK   3   NUMBER OF REFLECTIONS             : 12814                          \\nREMARK   3                                                                      \\nREMARK   3  FIT TO DATA USED IN REFINEMENT.                                     \\nREMARK   3   R VALUE     (WORKING + TEST SET) : 0.227                           \\nREMARK   3   R VALUE            (WORKING SET) : 0.226                           \\nREMARK   3   FREE R VALUE                     : 0.249                           \\nREMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.850                           \\nREMARK   3   FREE R VALUE TEST SET COUNT      : 622                             \\nREMARK   3                                                                      \\nREMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           \\nREMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        \\nREMARK   3     1 29.5504 -  4.5475    0.98     3287   157  0.2103 0.2188        \\nREMARK   3     2  4.5475 -  3.6116    0.99     3151   170  0.2090 0.2511        \\nREMARK   3     3  3.6116 -  3.1556    0.99     3111   162  0.2730 0.3034        \\nREMARK   3     4  3.1556 -  2.8674    0.84     2643   133  0.3166 0.3214        \\nREMARK   3                                                                      \\nREMARK   3  BULK SOLVENT MODELLING.                                             \\nREMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       \\nREMARK   3   SOLVENT RADIUS     : 1.11                                          \\nREMARK   3   SHRINKAGE RADIUS   : 0.90                                          \\nREMARK   3   K_SOL              : NULL                                          \\nREMARK   3   B_SOL              : NULL                                          \\nREMARK   3                                                                      \\nREMARK   3  ERROR ESTIMATES.                                                    \\nREMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.390            \\nREMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.640           \\nREMARK   3                                                                      \\nREMARK   3  B VALUES.                                                           \\nREMARK   3   FROM WILSON PLOT           (A**2) : NULL                           \\nREMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           \\nREMARK   3   OVERALL ANISOTROPIC B VALUE.                                       \\nREMARK   3    B11 (A**2) : NULL                                                 \\nREMARK   3    B22 (A**2) : NULL                                                 \\nREMARK   3    B33 (A**2) : NULL                                                 \\nREMARK   3    B12 (A**2) : NULL                                                 \\nREMARK   3    B13 (A**2) : NULL                                                 \\nREMARK   3    B23 (A**2) : NULL                                                 \\nREMARK   3                                                                      \\nREMARK   3  TWINNING INFORMATION.                                               \\nREMARK   3   FRACTION: NULL                                                     \\nREMARK   3   OPERATOR: NULL                                                     \\nREMARK   3                                                                      \\nREMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       \\nREMARK   3                 RMSD          COUNT                                  \\nREMARK   3   BOND      :  0.003           3283                                  \\nREMARK   3   ANGLE     :  0.516           4483                                  \\nREMARK   3   CHIRALITY :  0.037            544                                  \\nREMARK   3   PLANARITY :  0.003            549                                  \\nREMARK   3   DIHEDRAL  : 10.862           1928                                  \\nREMARK   3                                                                      \\nREMARK   3  TLS DETAILS                                                         \\nREMARK   3   NUMBER OF TLS GROUPS  : 3                                          \\nREMARK   3   TLS GROUP : 1                                                      \\nREMARK   3    SELECTION: CHAIN 'A' AND (RESID 36 THROUGH 222 )                  \\nREMARK   3    ORIGIN FOR THE GROUP (A):   7.6595   9.9883   1.8227              \\nREMARK   3    T TENSOR                                                          \\nREMARK   3      T11:   0.3906 T22:   0.3948                                     \\nREMARK   3      T33:   0.4097 T12:  -0.0409                                     \\nREMARK   3      T13:   0.0298 T23:   0.0323                                     \\nREMARK   3    L TENSOR                                                          \\nREMARK   3      L11:   4.8704 L22:   2.9655                                     \\nREMARK   3      L33:   4.7317 L12:   0.7811                                     \\nREMARK   3      L13:   2.8181 L23:   1.4507                                     \\nREMARK   3    S TENSOR                                                          \\nREMARK   3      S11:   0.0593 S12:  -0.1051 S13:   0.0093                       \\nREMARK   3      S21:   0.1418 S22:  -0.1464 S23:   0.1356                       \\nREMARK   3      S31:   0.4299 S32:  -0.3974 S33:  -0.0137                       \\nREMARK   3   TLS GROUP : 2                                                      \\nREMARK   3    SELECTION: CHAIN 'A' AND (RESID 1002 THROUGH 1161 )               \\nREMARK   3    ORIGIN FOR THE GROUP (A):  32.7700  -7.7446  36.3658              \\nREMARK   3    T TENSOR                                                          \\nREMARK   3      T11:   0.6968 T22:   0.5198                                     \\nREMARK   3      T33:   0.5000 T12:   0.0363                                     \\nREMARK   3      T13:   0.0872 T23:   0.1084                                     \\nREMARK   3    L TENSOR                                                          \\nREMARK   3      L11:   6.6697 L22:   6.8821                                     \\nREMARK   3      L33:   6.4568 L12:   1.6541                                     \\nREMARK   3      L13:   1.9941 L23:   1.4205                                     \\nREMARK   3    S TENSOR                                                          \\nREMARK   3      S11:  -0.2551 S12:   0.1211 S13:  -0.2547                       \\nREMARK   3      S21:  -0.3908 S22:  -0.0566 S23:  -0.4642                       \\nREMARK   3      S31:   0.4711 S32:   0.2364 S33:   0.3147                       \\nREMARK   3   TLS GROUP : 3                                                      \\nREMARK   3    SELECTION: CHAIN 'A' AND (RESID 384 THROUGH 460 )                 \\nREMARK   3    ORIGIN FOR THE GROUP (A):   9.8885  -1.6530  -1.3224              \\nREMARK   3    T TENSOR                                                          \\nREMARK   3      T11:   0.6392 T22:   0.3770                                     \\nREMARK   3      T33:   0.5276 T12:   0.0087                                     \\nREMARK   3      T13:  -0.0908 T23:   0.0140                                     \\nREMARK   3    L TENSOR                                                          \\nREMARK   3      L11:   6.0244 L22:   5.3813                                     \\nREMARK   3      L33:   6.7255 L12:   0.3578                                     \\nREMARK   3      L13:   1.1698 L23:   0.5209                                     \\nREMARK   3    S TENSOR                                                          \\nREMARK   3      S11:  -0.0948 S12:   0.3307 S13:   0.0832                       \\nREMARK   3      S21:  -0.4022 S22:   0.2772 S23:  -0.0581                       \\nREMARK   3      S31:   1.2902 S32:  -0.0417 S33:  -0.2847                       \\nREMARK   3                                                                      \\nREMARK   3  NCS DETAILS                                                         \\nREMARK   3   NUMBER OF NCS GROUPS : NULL                                        \\nREMARK   3                                                                      \\nREMARK   3  OTHER REFINEMENT REMARKS: NULL                                      \\nREMARK   4                                                                      \\nREMARK   4 6CM4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         \\nREMARK 100                                                                      \\nREMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-MAR-18.                  \\nREMARK 100 THE DEPOSITION ID IS D_1000232947.                                   \\nREMARK 200                                                                      \\nREMARK 200 EXPERIMENTAL DETAILS                                                 \\nREMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  \\nREMARK 200  DATE OF DATA COLLECTION        : 13-AUG-17                          \\nREMARK 200  TEMPERATURE           (KELVIN) : 100                                \\nREMARK 200  PH                             : NULL                               \\nREMARK 200  NUMBER OF CRYSTALS USED        : 1                                  \\nREMARK 200                                                                      \\nREMARK 200  SYNCHROTRON              (Y/N) : Y                                  \\nREMARK 200  RADIATION SOURCE               : APS                                \\nREMARK 200  BEAMLINE                       : 23-ID-B                            \\nREMARK 200  X-RAY GENERATOR MODEL          : NULL                               \\nREMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  \\nREMARK 200  WAVELENGTH OR RANGE        (A) : 1.033                              \\nREMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL CRYO-COOLED         \\nREMARK 200                                   SI(111)                            \\nREMARK 200  OPTICS                         : NULL                               \\nREMARK 200                                                                      \\nREMARK 200  DETECTOR TYPE                  : PIXEL                              \\nREMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER X 16M                \\nREMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000                           \\nREMARK 200  DATA SCALING SOFTWARE          : HKL-3000                           \\nREMARK 200                                                                      \\nREMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 12826                              \\nREMARK 200  RESOLUTION RANGE HIGH      (A) : 2.867                              \\nREMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             \\nREMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               \\nREMARK 200                                                                      \\nREMARK 200 OVERALL.                                                             \\nREMARK 200  COMPLETENESS FOR RANGE     (%) : 97.3                               \\nREMARK 200  DATA REDUNDANCY                : 5.500                              \\nREMARK 200  R MERGE                    (I) : 0.13400                            \\nREMARK 200  R SYM                      (I) : NULL                               \\nREMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.2000                            \\nREMARK 200                                                                      \\nREMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     \\nREMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90                     \\nREMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.99                     \\nREMARK 200  COMPLETENESS FOR SHELL     (%) : 86.9                               \\nREMARK 200  DATA REDUNDANCY IN SHELL       : 2.50                               \\nREMARK 200  R MERGE FOR SHELL          (I) : 0.73800                            \\nREMARK 200  R SYM FOR SHELL            (I) : NULL                               \\nREMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.000                              \\nREMARK 200                                                                      \\nREMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              \\nREMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        \\nREMARK 200 SOFTWARE USED: PHASER                                                \\nREMARK 200 STARTING MODEL: PDB ENTRIES 5WIU & 2RH1                              \\nREMARK 200                                                                      \\nREMARK 200 REMARK: NULL                                                         \\nREMARK 280                                                                      \\nREMARK 280 CRYSTAL                                                              \\nREMARK 280 SOLVENT CONTENT, VS   (%): 57.13                                     \\nREMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.87                     \\nREMARK 280                                                                      \\nREMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM TRIS-HCL, PH 7.8, 230 MM          \\nREMARK 280  LITHIUM NITRATE, 25% PEG400, 4% 1,3-BUTANEDIOL, LIPIDIC CUBIC       \\nREMARK 280  PHASE, TEMPERATURE 293K                                             \\nREMARK 290                                                                      \\nREMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            \\nREMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       \\nREMARK 290                                                                      \\nREMARK 290      SYMOP   SYMMETRY                                                \\nREMARK 290     NNNMMM   OPERATOR                                                \\nREMARK 290       1555   X,Y,Z                                                   \\nREMARK 290       2555   -X+1/2,-Y,Z+1/2                                         \\nREMARK 290       3555   -X,Y+1/2,-Z+1/2                                         \\nREMARK 290       4555   X+1/2,-Y+1/2,-Z                                         \\nREMARK 290                                                                      \\nREMARK 290     WHERE NNN -> OPERATOR NUMBER                                     \\nREMARK 290           MMM -> TRANSLATION VECTOR                                  \\nREMARK 290                                                                      \\nREMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            \\nREMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             \\nREMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                \\nREMARK 290 RELATED MOLECULES.                                                   \\nREMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            \\nREMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            \\nREMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            \\nREMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       25.48950            \\nREMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            \\nREMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       75.65350            \\nREMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            \\nREMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       36.26150            \\nREMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       75.65350            \\nREMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       25.48950            \\nREMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       36.26150            \\nREMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            \\nREMARK 290                                                                      \\nREMARK 290 REMARK: NULL                                                         \\nREMARK 300                                                                      \\nREMARK 300 BIOMOLECULE: 1                                                       \\nREMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                \\nREMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  \\nREMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               \\nREMARK 300 BURIED SURFACE AREA.                                                 \\nREMARK 350                                                                      \\nREMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           \\nREMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                \\nREMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          \\nREMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          \\nREMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               \\nREMARK 350                                                                      \\nREMARK 350 BIOMOLECULE: 1                                                       \\nREMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         \\nREMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  \\nREMARK 350 SOFTWARE USED: PISA                                                  \\nREMARK 350 TOTAL BURIED SURFACE AREA: 1850 ANGSTROM**2                          \\nREMARK 350 SURFACE AREA OF THE COMPLEX: 20460 ANGSTROM**2                       \\nREMARK 350 CHANGE IN SOLVENT FREE ENERGY: 12.0 KCAL/MOL                         \\nREMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     \\nREMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            \\nREMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            \\nREMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            \\nREMARK 465                                                                      \\nREMARK 465 MISSING RESIDUES                                                     \\nREMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       \\nREMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               \\nREMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                \\nREMARK 465                                                                      \\nREMARK 465   M RES C SSSEQI                                                     \\nREMARK 465     MET A   140                                                      \\nREMARK 465     LEU A   141                                                      \\nREMARK 465     TYR A   142                                                      \\nREMARK 465     ASN A   143                                                      \\nREMARK 465     LYS A   362                                                      \\nREMARK 465     LEU A   363                                                      \\nREMARK 465     CYS A   443                                                      \\nREMARK 470                                                                      \\nREMARK 470 MISSING ATOM                                                         \\nREMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           \\nREMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          \\nREMARK 470 I=INSERTION CODE):                                                   \\nREMARK 470   M RES CSSEQI  ATOMS                                                \\nREMARK 470     ASN A  35    CG   OD1  ND2                                       \\nREMARK 470     TYR A  36    CG   CD1  CD2  CE1  CE2  CZ   OH                    \\nREMARK 470     LEU A  43    CG   CD1  CD2                                       \\nREMARK 470     GLU A  62    CG   CD   OE1  OE2                                  \\nREMARK 470     LYS A  63    CG   CD   CE   NZ                                   \\nREMARK 470     VAL A  96    CG1  CG2                                            \\nREMARK 470     GLU A  99    CG   CD   OE1  OE2                                  \\nREMARK 470     LYS A 101    CG   CD   CE   NZ                                   \\nREMARK 470     THR A 144    OG1  CG2                                            \\nREMARK 470     ARG A 145    CG   CD   NE   CZ   NH1  NH2                        \\nREMARK 470     SER A 147    OG                                                  \\nREMARK 470     LYS A 149    CG   CD   CE   NZ                                   \\nREMARK 470     ARG A 150    CG   CD   NE   CZ   NH1  NH2                        \\nREMARK 470     ASN A 176    CG   OD1  ND2                                       \\nREMARK 470     ASP A 178    CG   OD1  OD2                                       \\nREMARK 470     GLN A 179    CG   CD   OE1  NE2                                  \\nREMARK 470     ASN A 180    CG   OD1  ND2                                       \\nREMARK 470     LYS A 211    CE   NZ                                             \\nREMARK 470     ARG A 217    CG   CD   NE   CZ   NH1  NH2                        \\nREMARK 470     ARG A 218    CG   CD   NE   CZ   NH1  NH2                        \\nREMARK 470     LYS A 221    CG   CD   CE   NZ                                   \\nREMARK 470     ARG A 222    CG   CD   NE   CZ   NH1  NH2                        \\nREMARK 470     LYS A1016    CG   CD   CE   NZ                                   \\nREMARK 470     LYS A1019    CG   CD   CE   NZ                                   \\nREMARK 470     GLU A1022    CG   CD   OE1  OE2                                  \\nREMARK 470     LEU A1032    CG   CD1  CD2                                       \\nREMARK 470     LEU A1033    CG   CD1  CD2                                       \\nREMARK 470     LYS A1035    CG   CD   CE   NZ                                   \\nREMARK 470     SER A1036    OG                                                  \\nREMARK 470     SER A1038    OG                                                  \\nREMARK 470     ASN A1040    CG   OD1  ND2                                       \\nREMARK 470     SER A1044    OG                                                  \\nREMARK 470     GLU A1045    CG   CD   OE1  OE2                                  \\nREMARK 470     LYS A1048    CG   CD   CE   NZ                                   \\nREMARK 470     ILE A1050    CG1  CG2  CD1                                       \\nREMARK 470     ASN A1053    CG   OD1  ND2                                       \\nREMARK 470     THR A1054    OG1  CG2                                            \\nREMARK 470     ASN A1055    CG   OD1  ND2                                       \\nREMARK 470     VAL A1057    CG1  CG2                                            \\nREMARK 470     LYS A1060    CG   CD   CE   NZ                                   \\nREMARK 470     LYS A1065    CG   CD   CE   NZ                                   \\nREMARK 470     ARG A1080    CG   CD   NE   CZ   NH1  NH2                        \\nREMARK 470     LYS A1083    CG   CD   CE   NZ                                   \\nREMARK 470     LYS A1085    CG   CD   CE   NZ                                   \\nREMARK 470     ASN A1116    CG   OD1  ND2                                       \\nREMARK 470     ASP A1127    CG   OD1  OD2                                       \\nREMARK 470     VAL A1131    CG1  CG2                                            \\nREMARK 470     LYS A1135    CG   CD   CE   NZ                                   \\nREMARK 470     ARG A1137    CG   CD   NE   CZ   NH1  NH2                        \\nREMARK 470     GLN A1141    CG   CD   OE1  NE2                                  \\nREMARK 470     LYS A1147    CG   CD   CE   NZ                                   \\nREMARK 470     THR A1157    OG1  CG2                                            \\nREMARK 470     SER A 364    OG                                                  \\nREMARK 470     GLN A 365    CG   CD   OE1  NE2                                  \\nREMARK 470     GLN A 366    CG   CD   OE1  NE2                                  \\nREMARK 470     LYS A 367    CG   CD   CE   NZ                                   \\nREMARK 470     LYS A 369    CG   CD   CE   NZ                                   \\nREMARK 470     LYS A 370    CG   CD   CE   NZ                                   \\nREMARK 470     ILE A 394    CG1  CG2  CD1                                       \\nREMARK 470     HIS A 398    CG   ND1  CD2  CE1  NE2                             \\nREMARK 470     ASP A 400    CG   OD1  OD2                                       \\nREMARK 470     VAL A 406    CG1  CG2                                            \\nREMARK 470     LEU A 407    CG   CD1  CD2                                       \\nREMARK 470     ILE A 431    CG1  CG2  CD1                                       \\nREMARK 470     GLU A 432    CG   CD   OE1  OE2                                  \\nREMARK 470     ARG A 434    CG   CD   NE   CZ   NH1  NH2                        \\nREMARK 470     LYS A 435    CG   CD   CE   NZ                                   \\nREMARK 470     LEU A 438    CG   CD1  CD2                                       \\nREMARK 470     LYS A 439    CG   CD   CE   NZ                                   \\nREMARK 470     HIS A 442    CG   ND1  CD2  CE1  NE2                             \\nREMARK 500                                                                      \\nREMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         \\nREMARK 500 SUBTOPIC: TORSION ANGLES                                             \\nREMARK 500                                                                      \\nREMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            \\nREMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               \\nREMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             \\nREMARK 500                                                                      \\nREMARK 500 STANDARD TABLE:                                                      \\nREMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    \\nREMARK 500                                                                      \\nREMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           \\nREMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            \\nREMARK 500                                                                      \\nREMARK 500  M RES CSSEQI        PSI       PHI                                   \\nREMARK 500    GLN A  66       70.23   -104.22                                   \\nREMARK 500    VAL A  87      -52.46   -121.67                                   \\nREMARK 500    PHE A 198      -60.72   -124.56                                   \\nREMARK 500    ASN A1055       17.81     58.75                                   \\nREMARK 500    PHE A1114       49.44    -89.78                                   \\nREMARK 500    ASP A 400       11.47     57.92                                   \\nREMARK 500    LEU A 441       33.98    -88.55                                   \\nREMARK 500                                                                      \\nREMARK 500 REMARK: NULL                                                         \\nREMARK 610                                                                      \\nREMARK 610 MISSING HETEROATOM                                                   \\nREMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           \\nREMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          \\nREMARK 610 I=INSERTION CODE):                                                   \\nREMARK 610   M RES C SSEQI                                                      \\nREMARK 610     OLA A 2005                                                       \\nREMARK 610     OLA A 2006                                                       \\nDBREF  6CM4 A   35   222  UNP    P14416   DRD2_HUMAN      35    222             \\nDBREF  6CM4 A 1002  1161  UNP    D9IEF7   D9IEF7_BPT4      2    161             \\nDBREF  6CM4 A  362   443  UNP    P14416   DRD2_HUMAN     362    443             \\nSEQADV 6CM4 ALA A  122  UNP  P14416    ILE   122 CONFLICT                       \\nSEQADV 6CM4 THR A 1054  UNP  D9IEF7    CYS    54 CONFLICT                       \\nSEQADV 6CM4 ALA A 1097  UNP  D9IEF7    CYS    97 CONFLICT                       \\nSEQADV 6CM4 ALA A  375  UNP  P14416    LEU   375 CONFLICT                       \\nSEQADV 6CM4 ALA A  379  UNP  P14416    LEU   379 CONFLICT                       \\nSEQRES   1 A  430  ASN TYR TYR ALA THR LEU LEU THR LEU LEU ILE ALA VAL\\nSEQRES   2 A  430  ILE VAL PHE GLY ASN VAL LEU VAL CYS MET ALA VAL SER\\nSEQRES   3 A  430  ARG GLU LYS ALA LEU GLN THR THR THR ASN TYR LEU ILE\\nSEQRES   4 A  430  VAL SER LEU ALA VAL ALA ASP LEU LEU VAL ALA THR LEU\\nSEQRES   5 A  430  VAL MET PRO TRP VAL VAL TYR LEU GLU VAL VAL GLY GLU\\nSEQRES   6 A  430  TRP LYS PHE SER ARG ILE HIS CYS ASP ILE PHE VAL THR\\nSEQRES   7 A  430  LEU ASP VAL MET MET CYS THR ALA SER ALA LEU ASN LEU\\nSEQRES   8 A  430  CYS ALA ILE SER ILE ASP ARG TYR THR ALA VAL ALA MET\\nSEQRES   9 A  430  PRO MET LEU TYR ASN THR ARG TYR SER SER LYS ARG ARG\\nSEQRES  10 A  430  VAL THR VAL MET ILE SER ILE VAL TRP VAL LEU SER PHE\\nSEQRES  11 A  430  THR ILE SER CYS PRO LEU LEU PHE GLY LEU ASN ASN ALA\\nSEQRES  12 A  430  ASP GLN ASN GLU CYS ILE ILE ALA ASN PRO ALA PHE VAL\\nSEQRES  13 A  430  VAL TYR SER SER ILE VAL SER PHE TYR VAL PRO PHE ILE\\nSEQRES  14 A  430  VAL THR LEU LEU VAL TYR ILE LYS ILE TYR ILE VAL LEU\\nSEQRES  15 A  430  ARG ARG ARG ARG LYS ARG ASN ILE PHE GLU MET LEU ARG\\nSEQRES  16 A  430  ILE ASP GLU GLY LEU ARG LEU LYS ILE TYR LYS ASP THR\\nSEQRES  17 A  430  GLU GLY TYR TYR THR ILE GLY ILE GLY HIS LEU LEU THR\\nSEQRES  18 A  430  LYS SER PRO SER LEU ASN ALA ALA LYS SER GLU LEU ASP\\nSEQRES  19 A  430  LYS ALA ILE GLY ARG ASN THR ASN GLY VAL ILE THR LYS\\nSEQRES  20 A  430  ASP GLU ALA GLU LYS LEU PHE ASN GLN ASP VAL ASP ALA\\nSEQRES  21 A  430  ALA VAL ARG GLY ILE LEU ARG ASN ALA LYS LEU LYS PRO\\nSEQRES  22 A  430  VAL TYR ASP SER LEU ASP ALA VAL ARG ARG ALA ALA LEU\\nSEQRES  23 A  430  ILE ASN MET VAL PHE GLN MET GLY GLU THR GLY VAL ALA\\nSEQRES  24 A  430  GLY PHE THR ASN SER LEU ARG MET LEU GLN GLN LYS ARG\\nSEQRES  25 A  430  TRP ASP GLU ALA ALA VAL ASN LEU ALA LYS SER ARG TRP\\nSEQRES  26 A  430  TYR ASN GLN THR PRO ASN ARG ALA LYS ARG VAL ILE THR\\nSEQRES  27 A  430  THR PHE ARG THR GLY THR TRP ASP ALA TYR LYS LEU SER\\nSEQRES  28 A  430  GLN GLN LYS GLU LYS LYS ALA THR GLN MET ALA ALA ILE\\nSEQRES  29 A  430  VAL ALA GLY VAL PHE ILE ILE CYS TRP LEU PRO PHE PHE\\nSEQRES  30 A  430  ILE THR HIS ILE LEU ASN ILE HIS CYS ASP CYS ASN ILE\\nSEQRES  31 A  430  PRO PRO VAL LEU TYR SER ALA PHE THR TRP LEU GLY TYR\\nSEQRES  32 A  430  VAL ASN SER ALA VAL ASN PRO ILE ILE TYR THR THR PHE\\nSEQRES  33 A  430  ASN ILE GLU PHE ARG LYS ALA PHE LEU LYS ILE LEU HIS\\nSEQRES  34 A  430  CYS\\nHET    8NU  A2001      30                                                       \\nHET    PEG  A2002       7                                                       \\nHET    PEG  A2003       7                                                       \\nHET    PEG  A2004       7                                                       \\nHET    OLA  A2005      13                                                       \\nHET    OLA  A2006      12                                                       \\nHET    OLA  A2007      20                                                       \\nHETNAM     8NU 3-[2-[4-(6-FLUORANYL-1,2-BENZOXAZOL-3-YL)PIPERIDIN-1-            \\nHETNAM   2 8NU  YL]ETHYL]-2-METHYL-6,7,8,9-TETRAHYDROPYRIDO[1,2-                \\nHETNAM   3 8NU  A]PYRIMIDIN-4-ONE                                               \\nHETNAM     PEG DI(HYDROXYETHYL)ETHER                                            \\nHETNAM     OLA OLEIC ACID                                                       \\nFORMUL   2  8NU    C23 H27 F N4 O2                                              \\nFORMUL   3  PEG    3(C4 H10 O3)                                                 \\nFORMUL   6  OLA    3(C18 H34 O2)                                                \\nFORMUL   9  HOH   *16(H2 O)                                                     \\nHELIX    1   1 ASN A   35  GLU A   62  1                                  28\\nHELIX    2   2 LYS A   63  GLN A   66  1                                   4\\nHELIX    3   3 THR A   67  LEU A   86  1                                  20\\nHELIX    4   4 VAL A   87  GLY A   98  1                                  12\\nHELIX    5   5 SER A  103  MET A  138  1                                  36\\nHELIX    6   6 TYR A  146  CYS A  168  1                                  23\\nHELIX    7   7 PRO A  169  ASN A  176  1                                   8\\nHELIX    8   8 CYS A  182  ASN A  186  1                                   5\\nHELIX    9   9 ALA A  188  VAL A  196  1                                   9\\nHELIX   10  10 PHE A  198  GLU A 1011  1                                  35\\nHELIX   11  11 SER A 1038  GLY A 1051  1                                  14\\nHELIX   12  12 THR A 1059  ASN A 1081  1                                  23\\nHELIX   13  13 LEU A 1084  LEU A 1091  1                                   8\\nHELIX   14  14 ASP A 1092  ALA A 1112  1                                  21\\nHELIX   15  15 PHE A 1114  GLN A 1123  1                                  10\\nHELIX   16  16 ARG A 1125  ALA A 1134  1                                  10\\nHELIX   17  17 SER A 1136  GLN A 1141  1                                   6\\nHELIX   18  18 THR A 1142  GLY A 1156  1                                  15\\nHELIX   19  19 GLU A  368  CYS A  399  1                                  32\\nHELIX   20  20 PRO A  404  ASN A  418  1                                  15\\nHELIX   21  21 VAL A  421  PHE A  429  1                                   9\\nHELIX   22  22 ASN A  430  LEU A  441  1                                  12\\nSHEET    1   1 1 ARG A1014  LYS A1019  0\\nSHEET    2   2 1 TYR A1025  GLY A1028  0\\nSHEET    3   3 1 HIS A1031  THR A1034  0\\nSSBOND   1 CYS A  107    CYS A  182                          1555   1555  2.03\\nSSBOND   2 CYS A  399    CYS A  401                          1555   1555  2.04\\nCRYST1   50.979   72.523  151.307  90.00  90.00  90.00 P 21 21 21    4          \\nORIGX1      1.000000  0.000000  0.000000        0.00000                         \\nORIGX2      0.000000  1.000000  0.000000        0.00000                         \\nORIGX3      0.000000  0.000000  1.000000        0.00000                         \\nSCALE1      0.019616  0.000000  0.000000        0.00000                         \\nSCALE2      0.000000  0.013789  0.000000        0.00000                         \\nSCALE3      0.000000  0.000000  0.006609        0.00000                         \\nATOM      1  N   ASN A  35      -5.317  -8.666 -16.658  1.00108.95           N\\nATOM      2  CA  ASN A  35      -3.999  -9.279 -16.550  1.00112.41           C\\nATOM      3  C   ASN A  35      -3.770  -9.829 -15.148  1.00103.98           C\\nATOM      4  O   ASN A  35      -4.596  -9.642 -14.253  1.00111.14           O\\nATOM      5  CB  ASN A  35      -2.903  -8.271 -16.904  1.00115.88           C\\nATOM      6  N   TYR A  36      -2.640 -10.512 -14.962  1.00122.79           N\\nANISOU    6  N   TYR A  36    17290  13079  16284  -1997  -3163  -3043       N\\nATOM      7  CA  TYR A  36      -2.284 -11.046 -13.653  1.00105.49           C\\nANISOU    7  CA  TYR A  36    15314  10451  14315  -2168  -3210  -2776       C\\nATOM      8  C   TYR A  36      -1.522 -10.036 -12.804  1.00100.38           C\\nANISOU    8  C   TYR A  36    14564  10022  13555  -2013  -2870  -2480       C\\nATOM      9  O   TYR A  36      -1.767  -9.933 -11.597  1.00 95.60           O\\nANISOU    9  O   TYR A  36    13979   9308  13038  -2297  -2774  -2120       O\\nATOM     10  CB  TYR A  36      -1.455 -12.323 -13.811  1.00 98.01           C\\nANISOU   10  CB  TYR A  36    14721   8957  13564  -1967  -3571  -3071       C\\nATOM     11  N   TYR A  37      -0.606  -9.280 -13.416  1.00105.86           N\\nANISOU   11  N   TYR A  37    15140  11047  14036  -1589  -2687  -2627       N\\nATOM     12  CA  TYR A  37       0.202  -8.334 -12.652  1.00101.50           C\\nANISOU   12  CA  TYR A  37    14496  10678  13392  -1434  -2394  -2372       C\\nATOM     13  C   TYR A  37      -0.596  -7.105 -12.233  1.00 97.18           C\\nANISOU   13  C   TYR A  37    13669  10521  12732  -1638  -2109  -2055       C\\nATOM     14  O   TYR A  37      -0.269  -6.474 -11.221  1.00 92.55           O\\nANISOU   14  O   TYR A  37    13035   9983  12145  -1663  -1908  -1774       O\\nATOM     15  CB  TYR A  37       1.435  -7.931 -13.459  1.00105.43           C\\nANISOU   15  CB  TYR A  37    14938  11423  13698   -962  -2294  -2627       C\\nATOM     16  CG  TYR A  37       2.442  -9.052 -13.603  1.00112.39           C\\nANISOU   16  CG  TYR A  37    16060  11928  14715   -688  -2547  -2949       C\\nATOM     17  CD1 TYR A  37       2.745  -9.880 -12.528  1.00116.25           C\\nANISOU   17  CD1 TYR A  37    16804  11893  15472   -778  -2740  -2820       C\\nATOM     18  CD2 TYR A  37       3.084  -9.291 -14.814  1.00112.70           C\\nANISOU   18  CD2 TYR A  37    16070  12145  14606   -332  -2615  -3395       C\\nATOM     19  CE1 TYR A  37       3.662 -10.907 -12.650  1.00117.63           C\\nANISOU   19  CE1 TYR A  37    17203  11682  15808   -489  -3027  -3136       C\\nATOM     20  CE2 TYR A  37       4.002 -10.320 -14.944  1.00114.52           C\\nANISOU   20  CE2 TYR A  37    16488  12042  14980    -35  -2866  -3754       C\\nATOM     21  CZ  TYR A  37       4.287 -11.123 -13.860  1.00116.82           C\\nANISOU   21  CZ  TYR A  37    17037  11766  15584    -99  -3089  -3627       C\\nATOM     22  OH  TYR A  37       5.200 -12.147 -13.987  1.00116.76           O\\nANISOU   22  OH  TYR A  37    17222  11387  15756    236  -3393  -4004       O\\nATOM     23  N   ALA A  38      -1.639  -6.750 -12.985  1.00 96.22           N\\nANISOU   23  N   ALA A  38    13359  10676  12525  -1764  -2113  -2120       N\\nATOM     24  CA  ALA A  38      -2.506  -5.655 -12.566  1.00 90.24           C\\nANISOU   24  CA  ALA A  38    12324  10255  11709  -1946  -1899  -1864       C\\nATOM     25  C   ALA A  38      -3.348  -6.039 -11.356  1.00 93.14           C\\nANISOU   25  C   ALA A  38    12686  10447  12255  -2375  -1898  -1620       C\\nATOM     26  O   ALA A  38      -3.625  -5.191 -10.500  1.00 89.27           O\\nANISOU   26  O   ALA A  38    12015  10164  11737  -2476  -1673  -1375       O\\nATOM     27  CB  ALA A  38      -3.409  -5.222 -13.721  1.00 92.04           C\\nANISOU   27  CB  ALA A  38    12349  10812  11811  -1948  -1956  -2018       C\\nATOM     28  N   THR A  39      -3.759  -7.307 -11.265  1.00101.53           N\\nANISOU   28  N   THR A  39    13946  11141  13491  -2646  -2152  -1687       N\\nATOM     29  CA  THR A  39      -4.521  -7.761 -10.105  1.00 98.62           C\\nANISOU   29  CA  THR A  39    13594  10616  13261  -3121  -2155  -1423       C\\nATOM     30  C   THR A  39      -3.673  -7.706  -8.839  1.00 94.46           C\\nANISOU   30  C   THR A  39    13228   9915  12749  -3111  -2033  -1154       C\\nATOM     31  O   THR A  39      -4.127  -7.220  -7.795  1.00 90.19           O\\nANISOU   31  O   THR A  39    12545   9551  12174  -3363  -1831   -884       O\\nATOM     32  CB  THR A  39      -5.041  -9.178 -10.345  1.00 96.91           C\\nANISOU   32  CB  THR A  39    13602   9983  13235  -3430  -2502  -1538       C\\nATOM     33  OG1 THR A  39      -5.673  -9.242 -11.631  1.00 99.65           O\\nANISOU   33  OG1 THR A  39    13821  10489  13554  -3372  -2644  -1841       O\\nATOM     34  CG2 THR A  39      -6.044  -9.566  -9.272  1.00 85.14           C\\nANISOU   34  CG2 THR A  39    12068   8436  11847  -4016  -2487  -1245       C\\nATOM     35  N   LEU A  40      -2.434  -8.202  -8.915  1.00 91.92           N\\nANISOU   35  N   LEU A  40    13187   9271  12469  -2807  -2162  -1251       N\\nATOM     36  CA  LEU A  40      -1.537  -8.138  -7.766  1.00 89.55           C\\nANISOU   36  CA  LEU A  40    13043   8803  12179  -2751  -2081  -1015       C\\nATOM     37  C   LEU A  40      -1.335  -6.702  -7.304  1.00 83.76           C\\nANISOU   37  C   LEU A  40    12038   8512  11276  -2605  -1722   -856       C\\nATOM     38  O   LEU A  40      -1.301  -6.429  -6.098  1.00 87.36           O\\nANISOU   38  O   LEU A  40    12497   8987  11709  -2775  -1584   -580       O\\nATOM     39  CB  LEU A  40      -0.191  -8.777  -8.104  1.00 87.94           C\\nANISOU   39  CB  LEU A  40    13114   8249  12051  -2357  -2285  -1222       C\\nATOM     40  CG  LEU A  40      -0.166 -10.273  -8.417  1.00 86.57           C\\nANISOU   40  CG  LEU A  40    13274   7524  12094  -2433  -2707  -1405       C\\nATOM     41  CD1 LEU A  40       1.260 -10.798  -8.334  1.00 81.27           C\\nANISOU   41  CD1 LEU A  40    12855   6507  11518  -2029  -2890  -1557       C\\nATOM     42  CD2 LEU A  40      -1.085 -11.041  -7.480  1.00 87.43           C\\nANISOU   42  CD2 LEU A  40    13549   7331  12340  -3007  -2857  -1101       C\\nATOM     43  N   LEU A  41      -1.202  -5.770  -8.248  1.00 77.53           N\\nANISOU   43  N   LEU A  41    11027   8075  10356  -2302  -1588  -1023       N\\nATOM     44  CA  LEU A  41      -1.025  -4.372  -7.871  1.00 83.20           C\\nANISOU   44  CA  LEU A  41    11504   9166  10941  -2162  -1296   -879       C\\nATOM     45  C   LEU A  41      -2.242  -3.847  -7.120  1.00 91.88           C\\nANISOU   45  C   LEU A  41    12365  10511  12032  -2501  -1145   -694       C\\nATOM     46  O   LEU A  41      -2.101  -3.145  -6.111  1.00 94.79           O\\nANISOU   46  O   LEU A  41    12646  11017  12354  -2528   -951   -503       O\\nATOM     47  CB  LEU A  41      -0.739  -3.520  -9.108  1.00 84.35           C\\nANISOU   47  CB  LEU A  41    11487   9616  10946  -1830  -1231  -1064       C\\nATOM     48  CG  LEU A  41       0.684  -3.615  -9.668  1.00 84.82           C\\nANISOU   48  CG  LEU A  41    11682   9604  10941  -1449  -1257  -1222       C\\nATOM     49  CD1 LEU A  41       0.863  -2.686 -10.856  1.00 82.66           C\\nANISOU   49  CD1 LEU A  41    11233   9703  10473  -1206  -1167  -1345       C\\nATOM     50  CD2 LEU A  41       1.708  -3.304  -8.588  1.00 84.95           C\\nANISOU   50  CD2 LEU A  41    11768   9527  10981  -1340  -1134  -1042       C\\nATOM     51  N   THR A  42      -3.447  -4.187  -7.587  1.00 91.95           N\\nANISOU   51  N   THR A  42    12247  10603  12085  -2760  -1237   -778       N\\nATOM     52  CA  THR A  42      -4.651  -3.758  -6.883  1.00 87.42           C\\nANISOU   52  CA  THR A  42    11395  10312  11509  -3092  -1095   -650       C\\nATOM     53  C   THR A  42      -4.741  -4.405  -5.507  1.00 89.21           C\\nANISOU   53  C   THR A  42    11759  10370  11767  -3467  -1059   -402       C\\nATOM     54  O   THR A  42      -5.141  -3.757  -4.533  1.00 90.48           O\\nANISOU   54  O   THR A  42    11720  10805  11853  -3617   -841   -252       O\\nATOM     55  CB  THR A  42      -5.894  -4.085  -7.708  1.00 81.63           C\\nANISOU   55  CB  THR A  42    10483   9703  10829  -3302  -1229   -812       C\\nATOM     56  OG1 THR A  42      -5.719  -3.600  -9.045  1.00 80.89           O\\nANISOU   56  OG1 THR A  42    10326   9737  10673  -2956  -1306  -1030       O\\nATOM     57  CG2 THR A  42      -7.122  -3.427  -7.095  1.00 73.78           C\\nANISOU   57  CG2 THR A  42     9102   9107   9822  -3566  -1057   -743       C\\nATOM     58  N   LEU A  43      -4.372  -5.685  -5.408  1.00 89.32           N\\nANISOU   58  N   LEU A  43    12123   9933  11882  -3624  -1291   -363       N\\nATOM     59  CA  LEU A  43      -4.291  -6.324  -4.100  1.00 89.41           C\\nANISOU   59  CA  LEU A  43    12339   9733  11900  -3975  -1300    -78       C\\nATOM     60  C   LEU A  43      -3.297  -5.599  -3.203  1.00 85.76           C\\nANISOU   60  C   LEU A  43    11923   9332  11330  -3737  -1117     75       C\\nATOM     61  O   LEU A  43      -3.540  -5.429  -2.003  1.00 86.73           O\\nANISOU   61  O   LEU A  43    12007   9591  11355  -4009   -965    311       O\\nATOM     62  CB  LEU A  43      -3.907  -7.795  -4.254  1.00 92.73           C\\nANISOU   62  CB  LEU A  43    13182   9571  12480  -4106  -1657    -74       C\\nATOM     63  N   LEU A  44      -2.173  -5.155  -3.773  1.00 83.60           N\\nANISOU   63  N   LEU A  44    11715   8995  11055  -3246  -1124    -66       N\\nATOM     64  CA  LEU A  44      -1.214  -4.375  -3.000  1.00 85.11           C\\nANISOU   64  CA  LEU A  44    11914   9267  11155  -3006   -957     53       C\\nATOM     65  C   LEU A  44      -1.839  -3.078  -2.502  1.00 85.13           C\\nANISOU   65  C   LEU A  44    11557   9754  11035  -3039   -660    109       C\\nATOM     66  O   LEU A  44      -1.633  -2.688  -1.347  1.00 86.93           O\\nANISOU   66  O   LEU A  44    11776  10082  11172  -3118   -515    286       O\\nATOM     67  CB  LEU A  44       0.031  -4.082  -3.838  1.00 87.56           C\\nANISOU   67  CB  LEU A  44    12295   9491  11483  -2502  -1005   -135       C\\nATOM     68  CG  LEU A  44       1.048  -3.125  -3.207  1.00 86.61           C\\nANISOU   68  CG  LEU A  44    12129   9496  11281  -2230   -831    -46       C\\nATOM     69  CD1 LEU A  44       1.618  -3.719  -1.930  1.00 87.91           C\\nANISOU   69  CD1 LEU A  44    12554   9391  11458  -2363   -905    175       C\\nATOM     70  CD2 LEU A  44       2.164  -2.764  -4.177  1.00 83.34           C\\nANISOU   70  CD2 LEU A  44    11712   9091  10864  -1783   -849   -246       C\\nATOM     71  N   ILE A  45      -2.611  -2.400  -3.356  1.00 82.86           N\\nANISOU   71  N   ILE A  45    10974   9766  10745  -2965   -594    -59       N\\nATOM     72  CA  ILE A  45      -3.287  -1.172  -2.940  1.00 83.78           C\\nANISOU   72  CA  ILE A  45    10732  10317  10784  -2961   -364    -56       C\\nATOM     73  C   ILE A  45      -4.154  -1.429  -1.715  1.00 85.75           C\\nANISOU   73  C   ILE A  45    10876  10734  10969  -3402   -243     98       C\\nATOM     74  O   ILE A  45      -4.169  -0.633  -0.767  1.00 85.46           O\\nANISOU   74  O   ILE A  45    10685  10954  10832  -3395    -44    165       O\\nATOM     75  CB  ILE A  45      -4.118  -0.594  -4.101  1.00 80.09           C\\nANISOU   75  CB  ILE A  45     9986  10096  10350  -2847   -391   -260       C\\nATOM     76  CG1 ILE A  45      -3.232  -0.296  -5.309  1.00 82.72           C\\nANISOU   76  CG1 ILE A  45    10426  10322  10681  -2446   -492   -386       C\\nATOM     77  CG2 ILE A  45      -4.845   0.666  -3.657  1.00 71.03           C\\nANISOU   77  CG2 ILE A  45     8464   9363   9163  -2807   -205   -292       C\\nATOM     78  CD1 ILE A  45      -3.998   0.221  -6.511  1.00 85.25           C\\nANISOU   78  CD1 ILE A  45    10525  10865  11002  -2340   -563   -559       C\\nATOM     79  N   ALA A  46      -4.887  -2.544  -1.711  1.00 89.24           N\\nANISOU   79  N   ALA A  46    11398  11053  11455  -3812   -363    150       N\\nATOM     80  CA  ALA A  46      -5.719  -2.875  -0.560  1.00 84.99           C\\nANISOU   80  CA  ALA A  46    10762  10712  10819  -4309   -240    325       C\\nATOM     81  C   ALA A  46      -4.868  -3.120   0.678  1.00 86.02           C\\nANISOU   81  C   ALA A  46    11172  10680  10833  -4395   -199    583       C\\nATOM     82  O   ALA A  46      -5.201  -2.653   1.773  1.00 82.61           O\\nANISOU   82  O   ALA A  46    10575  10580  10232  -4584     19    688       O\\nATOM     83  CB  ALA A  46      -6.581  -4.096  -0.869  1.00 77.37           C\\nANISOU   83  CB  ALA A  46     9868   9590   9938  -4771   -418    360       C\\nATOM     84  N   VAL A  47      -3.758  -3.841   0.522  1.00 84.11           N\\nANISOU   84  N   VAL A  47    11343   9946  10669  -4238   -419    662       N\\nATOM     85  CA  VAL A  47      -2.894  -4.117   1.664  1.00 83.65           C\\nANISOU   85  CA  VAL A  47    11575   9696  10512  -4292   -436    908       C\\nATOM     86  C   VAL A  47      -2.272  -2.829   2.191  1.00 82.63           C\\nANISOU   86  C   VAL A  47    11279   9847  10269  -3948   -212    871       C\\nATOM     87  O   VAL A  47      -2.139  -2.644   3.406  1.00 89.41           O\\nANISOU   87  O   VAL A  47    12171  10845  10957  -4107    -91   1051       O\\nATOM     88  CB  VAL A  47      -1.826  -5.156   1.281  1.00 85.45           C\\nANISOU   88  CB  VAL A  47    12252   9322  10892  -4129   -768    941       C\\nATOM     89  CG1 VAL A  47      -0.873  -5.397   2.438  1.00 84.04           C\\nANISOU   89  CG1 VAL A  47    12375   8931  10627  -4135   -829   1190       C\\nATOM     90  CG2 VAL A  47      -2.490  -6.457   0.863  1.00 89.97           C\\nANISOU   90  CG2 VAL A  47    13015   9574  11594  -4506  -1029    979       C\\nATOM     91  N   ILE A  48      -1.893  -1.915   1.294  1.00 78.76           N\\nANISOU   91  N   ILE A  48    10618   9450   9859  -3495   -165    645       N\\nATOM     92  CA  ILE A  48      -1.320  -0.643   1.730  1.00 77.79           C\\nANISOU   92  CA  ILE A  48    10338   9559   9659  -3180     16    603       C\\nATOM     93  C   ILE A  48      -2.344   0.158   2.522  1.00 82.81           C\\nANISOU   93  C   ILE A  48    10623  10681  10158  -3375    261    582       C\\nATOM     94  O   ILE A  48      -2.025   0.749   3.560  1.00 85.46           O\\nANISOU   94  O   ILE A  48    10924  11187  10359  -3347    400    647       O\\nATOM     95  CB  ILE A  48      -0.797   0.158   0.525  1.00 76.69           C\\nANISOU   95  CB  ILE A  48    10090   9420   9628  -2722     -7    395       C\\nATOM     96  CG1 ILE A  48       0.350  -0.582  -0.162  1.00 81.09           C\\nANISOU   96  CG1 ILE A  48    10957   9571  10283  -2498   -216    373       C\\nATOM     97  CG2 ILE A  48      -0.339   1.535   0.969  1.00 73.83           C\\nANISOU   97  CG2 ILE A  48     9552   9290   9212  -2449    157    360       C\\nATOM     98  CD1 ILE A  48       0.859   0.105  -1.411  1.00 83.26           C\\nANISOU   98  CD1 ILE A  48    11128   9896  10613  -2110   -227    183       C\\nATOM     99  N   VAL A  49      -3.590   0.189   2.047  1.00 85.62           N\\nANISOU   99  N   VAL A  49    10696  11290  10545  -3560    309    458       N\\nATOM    100  CA  VAL A  49      -4.628   0.950   2.736  1.00 86.41           C\\nANISOU  100  CA  VAL A  49    10399  11901  10530  -3713    539    369       C\\nATOM    101  C   VAL A  49      -5.028   0.256   4.033  1.00 86.76           C\\nANISOU  101  C   VAL A  49    10505  12094  10367  -4215    646    582       C\\nATOM    102  O   VAL A  49      -5.154   0.896   5.083  1.00 84.97           O\\nANISOU  102  O   VAL A  49    10110  12216   9958  -4262    848    578       O\\nATOM    103  CB  VAL A  49      -5.837   1.166   1.811  1.00 85.12           C\\nANISOU  103  CB  VAL A  49     9887  11980  10477  -3747    531    151       C\\nATOM    104  CG1 VAL A  49      -7.004   1.745   2.592  1.00 88.42           C\\nANISOU  104  CG1 VAL A  49     9863  12953  10781  -3956    756     30       C\\nATOM    105  CG2 VAL A  49      -5.456   2.084   0.662  1.00 80.88           C\\nANISOU  105  CG2 VAL A  49     9274  11370  10087  -3251    439    -34       C\\nATOM    106  N   PHE A  50      -5.229  -1.063   3.980  1.00 87.95           N\\nANISOU  106  N   PHE A  50    10908  11980  10529  -4611    497    773       N\\nATOM    107  CA  PHE A  50      -5.635  -1.794   5.177  1.00 89.88           C\\nANISOU  107  CA  PHE A  50    11255  12333  10561  -5041    554   1009       C\\nATOM    108  C   PHE A  50      -4.604  -1.654   6.289  1.00 92.06           C\\nANISOU  108  C   PHE A  50    11792  12524  10663  -4962    580   1197       C\\nATOM    109  O   PHE A  50      -4.957  -1.394   7.445  1.00 93.62           O\\nANISOU  109  O   PHE A  50    11871  13085  10613  -5087    752   1242       O\\nATOM    110  CB  PHE A  50      -5.857  -3.269   4.846  1.00 88.37           C\\nANISOU  110  CB  PHE A  50    11370  11743  10463  -5313    300   1176       C\\nATOM    111  CG  PHE A  50      -6.166  -4.119   6.048  1.00 91.54           C\\nANISOU  111  CG  PHE A  50    11945  12184  10651  -5658    293   1438       C\\nATOM    112  CD1 PHE A  50      -7.465  -4.232   6.518  1.00 92.88           C\\nANISOU  112  CD1 PHE A  50    11823  12793  10672  -5976    452   1419       C\\nATOM    113  CD2 PHE A  50      -5.157  -4.805   6.708  1.00 90.81           C\\nANISOU  113  CD2 PHE A  50    12302  11702  10500  -5665    108   1698       C\\nATOM    114  CE1 PHE A  50      -7.752  -5.011   7.623  1.00 96.10           C\\nANISOU  114  CE1 PHE A  50    12394  13265  10853  -6335    441   1672       C\\nATOM    115  CE2 PHE A  50      -5.439  -5.583   7.816  1.00 94.85           C\\nANISOU  115  CE2 PHE A  50    12982  12260  10797  -6003     73   1952       C\\nATOM    116  CZ  PHE A  50      -6.737  -5.688   8.272  1.00 98.38           C\\nANISOU  116  CZ  PHE A  50    13146  13159  11074  -6358    245   1949       C\\nATOM    117  N   GLY A  51      -3.324  -1.822   5.959  1.00 89.17           N\\nANISOU  117  N   GLY A  51    11775  11692  10415  -4731    395   1283       N\\nATOM    118  CA  GLY A  51      -2.301  -1.796   6.988  1.00 84.51           C\\nANISOU  118  CA  GLY A  51    11458  10976   9676  -4664    370   1475       C\\nATOM    119  C   GLY A  51      -2.075  -0.415   7.573  1.00 79.23           C\\nANISOU  119  C   GLY A  51    10517  10705   8881  -4366    607   1313       C\\nATOM    120  O   GLY A  51      -1.800  -0.278   8.767  1.00 79.21           O\\nANISOU  120  O   GLY A  51    10593  10866   8639  -4497    694   1454       O\\nATOM    121  N   ASN A  52      -2.183   0.626   6.746  1.00 74.87           N\\nANISOU  121  N   ASN A  52     9661  10300   8487  -3969    686   1017       N\\nATOM    122  CA  ASN A  52      -1.869   1.971   7.213  1.00 72.04           C\\nANISOU  122  CA  ASN A  52     9081  10223   8066  -3641    847    847       C\\nATOM    123  C   ASN A  52      -3.057   2.680   7.841  1.00 76.56           C\\nANISOU  123  C   ASN A  52     9223  11393   8475  -3813   1107    674       C\\nATOM    124  O   ASN A  52      -2.860   3.566   8.681  1.00 76.05           O\\nANISOU  124  O   ASN A  52     9026  11599   8272  -3672   1243    574       O\\nATOM    125  CB  ASN A  52      -1.305   2.809   6.069  1.00 68.61           C\\nANISOU  125  CB  ASN A  52     8565   9624   7879  -3132    768    642       C\\nATOM    126  CG  ASN A  52       0.113   2.416   5.715  1.00 79.96           C\\nANISOU  126  CG  ASN A  52    10362  10592   9427  -2882    569    754       C\\nATOM    127  OD1 ASN A  52       1.065   2.835   6.370  1.00 77.35           O\\nANISOU  127  OD1 ASN A  52    10144  10206   9041  -2704    566    802       O\\nATOM    128  ND2 ASN A  52       0.261   1.600   4.681  1.00 80.13           N\\nANISOU  128  ND2 ASN A  52    10547  10294   9604  -2861    393    767       N\\nATOM    129  N   VAL A  53      -4.286   2.318   7.468  1.00 82.38           N\\nANISOU  129  N   VAL A  53     9715  12360   9224  -4106   1170    606       N\\nATOM    130  CA  VAL A  53      -5.441   2.817   8.209  1.00 86.81           C\\nANISOU  130  CA  VAL A  53     9853  13535   9597  -4309   1419    435       C\\nATOM    131  C   VAL A  53      -5.398   2.300   9.643  1.00 91.28           C\\nANISOU  131  C   VAL A  53    10607  14230   9845  -4566   1474    633       C\\nATOM    132  O   VAL A  53      -5.768   3.009  10.588  1.00 98.44           O\\nANISOU  132  O   VAL A  53    11273  15582  10548  -4528   1653    471       O\\nATOM    133  CB  VAL A  53      -6.751   2.433   7.494  1.00 83.17           C\\nANISOU  133  CB  VAL A  53     9126  13231   9243  -4473   1406    307       C\\nATOM    134  CG1 VAL A  53      -7.949   2.691   8.387  1.00 78.74           C\\nANISOU  134  CG1 VAL A  53     8217  13227   8475  -4616   1596    143       C\\nATOM    135  CG2 VAL A  53      -6.893   3.217   6.198  1.00 79.84           C\\nANISOU  135  CG2 VAL A  53     8453  12777   9107  -4129   1341     45       C\\nATOM    136  N   LEU A  54      -4.923   1.065   9.827  1.00 86.53           N\\nANISOU  136  N   LEU A  54    10442  13233   9201  -4813   1292    968       N\\nATOM    137  CA  LEU A  54      -4.726   0.529  11.172  1.00 88.26           C\\nANISOU  137  CA  LEU A  54    10891  13520   9123  -5054   1288   1196       C\\nATOM    138  C   LEU A  54      -3.747   1.383  11.968  1.00 86.94           C\\nANISOU  138  C   LEU A  54    10787  13428   8817  -4810   1356   1171       C\\nATOM    139  O   LEU A  54      -4.002   1.722  13.130  1.00 94.33           O\\nANISOU  139  O   LEU A  54    11611  14759   9469  -4901   1496   1127       O\\nATOM    140  CB  LEU A  54      -4.224  -0.914  11.097  1.00 90.28           C\\nANISOU  140  CB  LEU A  54    11637  13240   9427  -5281   1006   1548       C\\nATOM    141  CG  LEU A  54      -5.198  -2.030  10.729  1.00 92.89           C\\nANISOU  141  CG  LEU A  54    11990  13500   9806  -5638    909   1650       C\\nATOM    142  CD1 LEU A  54      -4.459  -3.354  10.614  1.00 97.20           C\\nANISOU  142  CD1 LEU A  54    13055  13428  10449  -5757    575   1961       C\\nATOM    143  CD2 LEU A  54      -6.301  -2.128  11.763  1.00 96.43           C\\nANISOU  143  CD2 LEU A  54    12213  14478   9948  -5990   1090   1654       C\\nATOM    144  N   VAL A  55      -2.613   1.737  11.356  1.00 84.36           N\\nANISOU  144  N   VAL A  55    10638  12737   8678  -4508   1252   1188       N\\nATOM    145  CA  VAL A  55      -1.593   2.518  12.053  1.00 89.47           C\\nANISOU  145  CA  VAL A  55    11371  13417   9208  -4276   1291   1178       C\\nATOM    146  C   VAL A  55      -2.164   3.838  12.551  1.00 92.31           C\\nANISOU  146  C   VAL A  55    11279  14347   9446  -4112   1550    831       C\\nATOM    147  O   VAL A  55      -1.801   4.314  13.634  1.00 95.44           O\\nANISOU  147  O   VAL A  55    11689  14966   9606  -4066   1624    802       O\\nATOM    148  CB  VAL A  55      -0.374   2.741  11.133  1.00 85.96           C\\nANISOU  148  CB  VAL A  55    11134  12447   9082  -3803   1074   1151       C\\nATOM    149  CG1 VAL A  55       0.679   3.587  11.829  1.00 76.85           C\\nANISOU  149  CG1 VAL A  55    10045  11292   7864  -3476   1063   1092       C\\nATOM    150  CG2 VAL A  55       0.217   1.408  10.697  1.00 86.37           C\\nANISOU  150  CG2 VAL A  55    11619  11948   9251  -3934    799   1439       C\\nATOM    151  N   CYS A  56      -3.075   4.442  11.786  1.00 85.56           N\\nANISOU  151  N   CYS A  56    10018  13731   8759  -3998   1660    538       N\\nATOM    152  CA  CYS A  56      -3.627   5.737  12.175  1.00 80.56           C\\nANISOU  152  CA  CYS A  56     8941  13592   8075  -3762   1850    148       C\\nATOM    153  C   CYS A  56      -4.603   5.598  13.334  1.00 86.48           C\\nANISOU  153  C   CYS A  56     9514  14821   8522  -4005   1984     66       C\\nATOM    154  O   CYS A  56      -4.495   6.313  14.337  1.00 84.77           O\\nANISOU  154  O   CYS A  56     9186  14923   8102  -3899   2089   -102       O\\nATOM    155  CB  CYS A  56      -4.301   6.398  10.975  1.00 67.26           C\\nANISOU  155  CB  CYS A  56     6920  11917   6720  -3468   1818   -150       C\\nATOM    156  SG  CYS A  56      -3.139   6.859   9.688  1.00 71.11           S\\nANISOU  156  SG  CYS A  56     7652  11761   7605  -2939   1540   -134       S\\nATOM    157  N   MET A  57      -5.565   4.680  13.217  1.00 89.30           N\\nANISOU  157  N   MET A  57     9839  15250   8838  -4343   1978    170       N\\nATOM    158  CA  MET A  57      -6.547   4.508  14.283  1.00 99.11           C\\nANISOU  158  CA  MET A  57    10893  16987   9777  -4621   2115     99       C\\nATOM    159  C   MET A  57      -5.891   4.028  15.570  1.00100.31           C\\nANISOU  159  C   MET A  57    11370  17145   9601  -4843   2094    365       C\\nATOM    160  O   MET A  57      -6.282   4.448  16.665  1.00109.98           O\\nANISOU  160  O   MET A  57    12410  18838  10541  -4909   2235    210       O\\nATOM    161  CB  MET A  57      -7.633   3.529  13.845  1.00106.16           C\\nANISOU  161  CB  MET A  57    11719  17920  10695  -4975   2095    198       C\\nATOM    162  CG  MET A  57      -8.458   4.012  12.672  1.00104.93           C\\nANISOU  162  CG  MET A  57    11195  17843  10830  -4777   2113    -94       C\\nATOM    163  SD  MET A  57      -9.729   2.811  12.239  1.00106.23           S\\nANISOU  163  SD  MET A  57    11291  18073  11000  -5226   2085     28       S\\nATOM    164  CE  MET A  57      -8.718   1.360  11.965  1.00104.77           C\\nANISOU  164  CE  MET A  57    11736  17203  10870  -5491   1838    545       C\\nATOM    165  N   ALA A  58      -4.891   3.151  15.458  1.00 91.70           N\\nANISOU  165  N   ALA A  58    10761  15535   8547  -4945   1896    749       N\\nATOM    166  CA  ALA A  58      -4.253   2.590  16.647  1.00 94.86           C\\nANISOU  166  CA  ALA A  58    11502  15887   8653  -5159   1819   1033       C\\nATOM    167  C   ALA A  58      -3.578   3.673  17.478  1.00 93.98           C\\nANISOU  167  C   ALA A  58    11323  16005   8380  -4887   1912    851       C\\nATOM    168  O   ALA A  58      -3.795   3.769  18.691  1.00 97.13           O\\nANISOU  168  O   ALA A  58    11671  16787   8447  -5049   2002    828       O\\nATOM    169  CB  ALA A  58      -3.240   1.521  16.244  1.00 92.30           C\\nANISOU  169  CB  ALA A  58    11700  14899   8471  -5223   1532   1429       C\\nATOM    170  N   VAL A  59      -2.740   4.492  16.841  1.00 96.30           N\\nANISOU  170  N   VAL A  59    11619  16077   8895  -4483   1883    717       N\\nATOM    171  CA  VAL A  59      -2.102   5.595  17.551  1.00 91.92           C\\nANISOU  171  CA  VAL A  59    10983  15733   8211  -4197   1959    504       C\\nATOM    172  C   VAL A  59      -3.144   6.585  18.045  1.00 91.74           C\\nANISOU  172  C   VAL A  59    10460  16322   8077  -4097   2177     56       C\\nATOM    173  O   VAL A  59      -2.990   7.184  19.117  1.00 99.07           O\\nANISOU  173  O   VAL A  59    11313  17573   8756  -4030   2251   -105       O\\nATOM    174  CB  VAL A  59      -1.062   6.271  16.638  1.00 84.96           C\\nANISOU  174  CB  VAL A  59    10179  14491   7608  -3805   1881    441       C\\nATOM    175  CG1 VAL A  59      -0.446   7.484  17.318  1.00 88.37           C\\nANISOU  175  CG1 VAL A  59    10505  15150   7923  -3491   1949    173       C\\nATOM    176  CG2 VAL A  59       0.009   5.267  16.235  1.00 77.23           C\\nANISOU  176  CG2 VAL A  59     9704  12913   6729  -3889   1637    864       C\\nATOM    177  N   SER A  60      -4.229   6.759  17.291  1.00 95.26           N\\nANISOU  177  N   SER A  60    10557  16933   8706  -4072   2257   -169       N\\nATOM    178  CA  SER A  60      -5.247   7.733  17.658  1.00 98.05           C\\nANISOU  178  CA  SER A  60    10416  17831   9007  -3917   2417   -638       C\\nATOM    179  C   SER A  60      -6.057   7.307  18.875  1.00104.36           C\\nANISOU  179  C   SER A  60    11113  19121   9420  -4286   2535   -633       C\\nATOM    180  O   SER A  60      -6.732   8.148  19.479  1.00107.43           O\\nANISOU  180  O   SER A  60    11125  20003   9691  -4157   2661  -1033       O\\nATOM    181  CB  SER A  60      -6.183   7.974  16.473  1.00 97.14           C\\nANISOU  181  CB  SER A  60     9973  17730   9205  -3784   2427   -864       C\\nATOM    182  OG  SER A  60      -7.148   8.967  16.770  1.00 99.99           O\\nANISOU  182  OG  SER A  60     9859  18573   9559  -3574   2531  -1349       O\\nATOM    183  N   ARG A  61      -6.003   6.030  19.255  1.00 98.78           N\\nANISOU  183  N   ARG A  61    10729  18286   8518  -4738   2478   -202       N\\nATOM    184  CA  ARG A  61      -6.880   5.512  20.291  1.00103.46           C\\nANISOU  184  CA  ARG A  61    11212  19353   8745  -5156   2589   -162       C\\nATOM    185  C   ARG A  61      -6.159   4.772  21.410  1.00107.55           C\\nANISOU  185  C   ARG A  61    12131  19803   8928  -5464   2513    219       C\\nATOM    186  O   ARG A  61      -6.808   4.395  22.392  1.00117.52           O\\nANISOU  186  O   ARG A  61    13311  21498   9842  -5828   2609    262       O\\nATOM    187  CB  ARG A  61      -7.937   4.590  19.664  1.00104.53           C\\nANISOU  187  CB  ARG A  61    11265  19502   8951  -5497   2593    -37       C\\nATOM    188  CG  ARG A  61      -8.730   5.267  18.557  1.00 96.67           C\\nANISOU  188  CG  ARG A  61     9865  18588   8277  -5209   2647   -407       C\\nATOM    189  CD  ARG A  61     -10.016   4.534  18.248  1.00108.57           C\\nANISOU  189  CD  ARG A  61    11174  20320   9758  -5564   2702   -387       C\\nATOM    190  NE  ARG A  61      -9.801   3.362  17.409  1.00109.71           N\\nANISOU  190  NE  ARG A  61    11662  19943  10079  -5797   2536     11       N\\nATOM    191  CZ  ARG A  61     -10.778   2.566  16.987  1.00115.93           C\\nANISOU  191  CZ  ARG A  61    12357  20800  10890  -6123   2537     93       C\\nATOM    192  NH1 ARG A  61     -12.034   2.820  17.330  1.00116.46           N\\nANISOU  192  NH1 ARG A  61    11988  21459  10801  -6264   2710   -185       N\\nATOM    193  NH2 ARG A  61     -10.501   1.519  16.223  1.00119.11           N\\nANISOU  193  NH2 ARG A  61    13096  20686  11475  -6303   2354    434       N\\nATOM    194  N   GLU A  62      -4.853   4.558  21.301  1.00 96.97           N\\nANISOU  194  N   GLU A  62    11215  17953   7675  -5333   2333    491       N\\nATOM    195  CA  GLU A  62      -4.083   3.859  22.320  1.00101.43           C\\nANISOU  195  CA  GLU A  62    12192  18393   7956  -5580   2207    858       C\\nATOM    196  C   GLU A  62      -3.184   4.851  23.046  1.00102.22           C\\nANISOU  196  C   GLU A  62    12307  18603   7928  -5257   2227    678       C\\nATOM    197  O   GLU A  62      -2.426   5.591  22.409  1.00 92.57           O\\nANISOU  197  O   GLU A  62    11100  17116   6955  -4842   2178    531       O\\nATOM    198  CB  GLU A  62      -3.246   2.737  21.703  1.00100.84           C\\nANISOU  198  CB  GLU A  62    12621  17618   8074  -5678   1928   1315       C\\nATOM    199  N   LYS A  63      -3.269   4.854  24.378  1.00108.00           N\\nANISOU  199  N   LYS A  63    13040  19738   8259  -5463   2293    691       N\\nATOM    200  CA  LYS A  63      -2.467   5.770  25.183  1.00106.16           C\\nANISOU  200  CA  LYS A  63    12820  19652   7864  -5180   2305    504       C\\nATOM    201  C   LYS A  63      -0.976   5.535  24.970  1.00 98.83           C\\nANISOU  201  C   LYS A  63    12367  18125   7059  -4996   2054    800       C\\nATOM    202  O   LYS A  63      -0.243   6.439  24.552  1.00 90.24           O\\nANISOU  202  O   LYS A  63    11250  16879   6157  -4571   2024    584       O\\nATOM    203  CB  LYS A  63      -2.833   5.616  26.660  1.00114.28           C\\nANISOU  203  CB  LYS A  63    13807  21206   8408  -5502   2401    526       C\\nATOM    204  N   ALA A  64      -0.510   4.312  25.239  1.00108.15           N\\nANISOU  204  N   ALA A  64    13988  18956   8148  -5308   1844   1286       N\\nATOM    205  CA  ALA A  64       0.917   4.011  25.200  1.00103.75           C\\nANISOU  205  CA  ALA A  64    13892  17853   7678  -5142   1563   1569       C\\nATOM    206  C   ALA A  64       1.513   4.169  23.805  1.00 99.33           C\\nANISOU  206  C   ALA A  64    13405  16779   7558  -4812   1452   1552       C\\nATOM    207  O   ALA A  64       2.735   4.041  23.649  1.00 84.58           O\\nANISOU  207  O   ALA A  64    11875  14464   5799  -4615   1215   1732       O\\nATOM    208  CB  ALA A  64       1.164   2.590  25.719  1.00103.60           C\\nANISOU  208  CB  ALA A  64    14310  17538   7516  -5540   1320   2073       C\\nATOM    209  N   LEU A  65       0.685   4.450  22.798  1.00 91.85           N\\nANISOU  209  N   LEU A  65    12140  15902   6858  -4745   1606   1334       N\\nATOM    210  CA  LEU A  65       1.126   4.676  21.429  1.00 92.45           C\\nANISOU  210  CA  LEU A  65    12233  15560   7334  -4450   1535   1288       C\\nATOM    211  C   LEU A  65       1.071   6.143  21.021  1.00 91.55           C\\nANISOU  211  C   LEU A  65    11741  15700   7344  -4047   1715    824       C\\nATOM    212  O   LEU A  65       1.216   6.447  19.835  1.00 98.95           O\\nANISOU  212  O   LEU A  65    12606  16387   8603  -3825   1705    736       O\\nATOM    213  CB  LEU A  65       0.282   3.842  20.465  1.00 91.67           C\\nANISOU  213  CB  LEU A  65    12087  15284   7459  -4662   1529   1402       C\\nATOM    214  CG  LEU A  65       0.533   2.337  20.472  1.00 96.52           C\\nANISOU  214  CG  LEU A  65    13133  15448   8091  -4973   1266   1854       C\\nATOM    215  CD1 LEU A  65      -0.389   1.627  19.490  1.00101.66           C\\nANISOU  215  CD1 LEU A  65    13694  15972   8962  -5162   1269   1895       C\\nATOM    216  CD2 LEU A  65       1.987   2.059  20.143  1.00 88.49           C\\nANISOU  216  CD2 LEU A  65    12531  13837   7256  -4733    974   2071       C\\nATOM    217  N   GLN A  66       0.870   7.056  21.966  1.00 97.64           N\\nANISOU  217  N   GLN A  66    12271  16951   7878  -3940   1858    509       N\\nATOM    218  CA  GLN A  66       0.729   8.476  21.643  1.00 91.59           C\\nANISOU  218  CA  GLN A  66    11125  16421   7256  -3531   1991      9       C\\nATOM    219  C   GLN A  66       2.014   9.220  22.003  1.00 88.27           C\\nANISOU  219  C   GLN A  66    10883  15873   6783  -3219   1872    -76       C\\nATOM    220  O   GLN A  66       2.081  10.015  22.940  1.00 95.43           O\\nANISOU  220  O   GLN A  66    11654  17116   7488  -3077   1921   -364       O\\nATOM    221  CB  GLN A  66      -0.488   9.060  22.354  1.00 94.21           C\\nANISOU  221  CB  GLN A  66    11011  17366   7418  -3569   2200   -377       C\\nATOM    222  CG  GLN A  66      -1.806   8.615  21.747  1.00 90.38           C\\nANISOU  222  CG  GLN A  66    10255  17032   7053  -3778   2313   -412       C\\nATOM    223  CD  GLN A  66      -3.010   9.067  22.544  1.00 98.45           C\\nANISOU  223  CD  GLN A  66    10853  18690   7865  -3861   2497   -767       C\\nATOM    224  OE1 GLN A  66      -2.887   9.506  23.689  1.00102.35           O\\nANISOU  224  OE1 GLN A  66    11295  19524   8070  -3847   2548   -921       O\\nATOM    225  NE2 GLN A  66      -4.187   8.960  21.941  1.00101.41           N\\nANISOU  225  NE2 GLN A  66    10914  19243   8376  -3945   2588   -913       N\\nATOM    226  N   THR A  67       3.049   8.942  21.221  1.00 81.40           N\\nANISOU  226  N   THR A  67    10313  14420   6193  -3058   1648    159       N\\nATOM    227  CA  THR A  67       4.366   9.523  21.416  1.00 80.16           C\\nANISOU  227  CA  THR A  67    10341  13928   6189  -2690   1412    112       C\\nATOM    228  C   THR A  67       4.724  10.396  20.219  1.00 81.81           C\\nANISOU  228  C   THR A  67    10385  13739   6959  -2223   1303   -122       C\\nATOM    229  O   THR A  67       4.047  10.388  19.187  1.00 83.11           O\\nANISOU  229  O   THR A  67    10366  13821   7392  -2189   1372   -182       O\\nATOM    230  CB  THR A  67       5.424   8.430  21.618  1.00 74.28           C\\nANISOU  230  CB  THR A  67    10089  12752   5384  -2838   1150    588       C\\nATOM    231  OG1 THR A  67       5.732   7.823  20.359  1.00 77.15           O\\nANISOU  231  OG1 THR A  67    10579  12565   6169  -2749   1000    784       O\\nATOM    232  CG2 THR A  67       4.909   7.358  22.566  1.00 76.90           C\\nANISOU  232  CG2 THR A  67    10631  13398   5190  -3391   1228    928       C\\nATOM    233  N   THR A  68       5.803  11.165  20.370  1.00 86.60           N\\nANISOU  233  N   THR A  68    11062  14111   7731  -1884   1119   -244       N\\nATOM    234  CA  THR A  68       6.274  11.984  19.259  1.00 81.90           C\\nANISOU  234  CA  THR A  68    10353  13120   7646  -1492    990   -405       C\\nATOM    235  C   THR A  68       6.614  11.116  18.055  1.00 76.38           C\\nANISOU  235  C   THR A  68     9828  11956   7236  -1519    883    -94       C\\nATOM    236  O   THR A  68       6.157  11.379  16.939  1.00 74.99           O\\nANISOU  236  O   THR A  68     9479  11652   7360  -1401    915   -182       O\\nATOM    237  CB  THR A  68       7.490  12.816  19.681  1.00 80.77           C\\nANISOU  237  CB  THR A  68    10291  12786   7611  -1198    788   -526       C\\nATOM    238  OG1 THR A  68       8.582  11.948  20.014  1.00 75.97           O\\nANISOU  238  OG1 THR A  68    10037  11917   6911  -1290    604   -182       O\\nATOM    239  CG2 THR A  68       7.155  13.692  20.878  1.00 83.25           C\\nANISOU  239  CG2 THR A  68    10436  13561   7636  -1147    872   -884       C\\nATOM    240  N   THR A  69       7.412  10.066  18.270  1.00 78.37           N\\nANISOU  240  N   THR A  69    10426  11955   7395  -1662    733    255       N\\nATOM    241  CA  THR A  69       7.811   9.195  17.168  1.00 78.88           C\\nANISOU  241  CA  THR A  69    10662  11578   7732  -1656    605    503       C\\nATOM    242  C   THR A  69       6.596   8.584  16.482  1.00 78.27           C\\nANISOU  242  C   THR A  69    10482  11594   7664  -1890    759    558       C\\nATOM    243  O   THR A  69       6.522   8.550  15.247  1.00 73.15           O\\nANISOU  243  O   THR A  69     9763  10702   7330  -1761    732    539       O\\nATOM    244  CB  THR A  69       8.748   8.097  17.676  1.00 76.37           C\\nANISOU  244  CB  THR A  69    10733  11000   7285  -1777    388    839       C\\nATOM    245  OG1 THR A  69       9.982   8.680  18.112  1.00 72.19           O\\nANISOU  245  OG1 THR A  69    10268  10338   6821  -1513    212    771       O\\nATOM    246  CG2 THR A  69       9.035   7.083  16.582  1.00 74.02           C\\nANISOU  246  CG2 THR A  69    10604  10273   7247  -1776    252   1050       C\\nATOM    247  N   ASN A  70       5.625   8.114  17.269  1.00 82.86           N\\nANISOU  247  N   ASN A  70    11039  12561   7884  -2256    925    618       N\\nATOM    248  CA  ASN A  70       4.436   7.496  16.698  1.00 81.91           C\\nANISOU  248  CA  ASN A  70    10800  12565   7757  -2530   1069    672       C\\nATOM    249  C   ASN A  70       3.562   8.494  15.947  1.00 81.00           C\\nANISOU  249  C   ASN A  70    10269  12649   7860  -2327   1221    314       C\\nATOM    250  O   ASN A  70       2.805   8.084  15.063  1.00 74.10           O\\nANISOU  250  O   ASN A  70     9290  11736   7128  -2431   1271    335       O\\nATOM    251  CB  ASN A  70       3.629   6.801  17.798  1.00 79.20           C\\nANISOU  251  CB  ASN A  70    10505  12647   6942  -3020   1221    832       C\\nATOM    252  CG  ASN A  70       4.333   5.581  18.348  1.00 78.28           C\\nANISOU  252  CG  ASN A  70    10856  12250   6638  -3286   1014   1268       C\\nATOM    253  OD1 ASN A  70       5.224   5.030  17.706  1.00 74.09           O\\nANISOU  253  OD1 ASN A  70    10588  11183   6379  -3127    762   1443       O\\nATOM    254  ND2 ASN A  70       3.941   5.152  19.542  1.00 73.15           N\\nANISOU  254  ND2 ASN A  70    10308  11972   5512  -3692   1103   1439       N\\nATOM    255  N   TYR A  71       3.640   9.786  16.274  1.00 84.07           N\\nANISOU  255  N   TYR A  71    10427  13227   8291  -2033   1261    -20       N\\nATOM    256  CA  TYR A  71       2.933  10.782  15.475  1.00 77.80           C\\nANISOU  256  CA  TYR A  71     9275  12516   7768  -1780   1321   -352       C\\nATOM    257  C   TYR A  71       3.632  11.001  14.143  1.00 70.85           C\\nANISOU  257  C   TYR A  71     8477  11134   7310  -1497   1135   -290       C\\nATOM    258  O   TYR A  71       2.978  11.216  13.117  1.00 65.56           O\\nANISOU  258  O   TYR A  71     7626  10422   6864  -1416   1148   -386       O\\nATOM    259  CB  TYR A  71       2.809  12.094  16.246  1.00 74.68           C\\nANISOU  259  CB  TYR A  71     8632  12431   7314  -1540   1370   -746       C\\nATOM    260  CG  TYR A  71       1.783  12.035  17.350  1.00 80.29           C\\nANISOU  260  CG  TYR A  71     9123  13772   7611  -1796   1612   -924       C\\nATOM    261  CD1 TYR A  71       0.690  11.189  17.253  1.00 82.22           C\\nANISOU  261  CD1 TYR A  71     9248  14311   7681  -2164   1796   -825       C\\nATOM    262  CD2 TYR A  71       1.912  12.814  18.492  1.00 84.10           C\\nANISOU  262  CD2 TYR A  71     9504  14589   7861  -1688   1658  -1202       C\\nATOM    263  CE1 TYR A  71      -0.250  11.123  18.258  1.00 91.89           C\\nANISOU  263  CE1 TYR A  71    10236  16183   8495  -2441   2045   -986       C\\nATOM    264  CE2 TYR A  71       0.976  12.756  19.503  1.00 85.39           C\\nANISOU  264  CE2 TYR A  71     9439  15406   7599  -1932   1905  -1392       C\\nATOM    265  CZ  TYR A  71      -0.103  11.907  19.381  1.00 94.33           C\\nANISOU  265  CZ  TYR A  71    10434  16859   8548  -2320   2110  -1275       C\\nATOM    266  OH  TYR A  71      -1.045  11.839  20.381  1.00 99.85           O\\nANISOU  266  OH  TYR A  71    10911  18103   8926  -2541   2275  -1429       O\\nATOM    267  N   LEU A  72       4.963  10.950  14.139  1.00 66.28           N\\nANISOU  267  N   LEU A  72     8155  10205   6825  -1355    960   -134       N\\nATOM    268  CA  LEU A  72       5.688  10.938  12.880  1.00 65.47           C\\nANISOU  268  CA  LEU A  72     8142   9678   7057  -1158    810    -34       C\\nATOM    269  C   LEU A  72       5.520   9.612  12.156  1.00 66.26           C\\nANISOU  269  C   LEU A  72     8411   9590   7173  -1363    790    218       C\\nATOM    270  O   LEU A  72       5.755   9.545  10.947  1.00 70.26           O\\nANISOU  270  O   LEU A  72     8925   9843   7928  -1232    713    248       O\\nATOM    271  CB  LEU A  72       7.166  11.237  13.129  1.00 68.98           C\\nANISOU  271  CB  LEU A  72     8763   9860   7585   -964    640     32       C\\nATOM    272  CG  LEU A  72       7.464  12.668  13.586  1.00 71.02           C\\nANISOU  272  CG  LEU A  72     8861  10200   7924   -721    600   -231       C\\nATOM    273  CD1 LEU A  72       8.795  12.745  14.308  1.00 68.45           C\\nANISOU  273  CD1 LEU A  72     8719   9732   7557   -638    454   -157       C\\nATOM    274  CD2 LEU A  72       7.449  13.618  12.399  1.00 69.98           C\\nANISOU  274  CD2 LEU A  72     8565   9884   8138   -488    531   -351       C\\nATOM    275  N   ILE A  73       5.112   8.562  12.866  1.00 69.01           N\\nANISOU  275  N   ILE A  73     8906  10062   7254  -1697    844    397       N\\nATOM    276  CA  ILE A  73       4.844   7.288  12.214  1.00 67.68           C\\nANISOU  276  CA  ILE A  73     8907   9691   7118  -1917    795    618       C\\nATOM    277  C   ILE A  73       3.522   7.340  11.460  1.00 71.94           C\\nANISOU  277  C   ILE A  73     9183  10422   7728  -2023    929    489       C\\nATOM    278  O   ILE A  73       3.411   6.809  10.350  1.00 75.02           O\\nANISOU  278  O   ILE A  73     9617  10582   8307  -2015    856    546       O\\nATOM    279  CB  ILE A  73       4.880   6.148  13.249  1.00 69.17           C\\nANISOU  279  CB  ILE A  73     9379   9898   7006  -2275    759    894       C\\nATOM    280  CG1 ILE A  73       6.327   5.743  13.542  1.00 66.13           C\\nANISOU  280  CG1 ILE A  73     9319   9150   6659  -2128    522   1069       C\\nATOM    281  CG2 ILE A  73       4.072   4.944  12.777  1.00 68.47           C\\nANISOU  281  CG2 ILE A  73     9386   9730   6900  -2615    755   1076       C\\nATOM    282  CD1 ILE A  73       6.453   4.548  14.461  1.00 67.07           C\\nANISOU  282  CD1 ILE A  73     9782   9188   6514  -2462    402   1387       C\\nATOM    283  N   VAL A  74       2.507   7.996  12.029  1.00 70.79           N\\nANISOU  283  N   VAL A  74     8739  10720   7436  -2102   1115    280       N\\nATOM    284  CA  VAL A  74       1.244   8.128  11.308  1.00 74.58           C\\nANISOU  284  CA  VAL A  74     8921  11407   8009  -2166   1221    118       C\\nATOM    285  C   VAL A  74       1.392   9.116  10.161  1.00 73.54           C\\nANISOU  285  C   VAL A  74     8633  11099   8211  -1776   1127    -73       C\\nATOM    286  O   VAL A  74       0.708   8.995   9.137  1.00 75.63           O\\nANISOU  286  O   VAL A  74     8769  11334   8631  -1776   1112   -121       O\\nATOM    287  CB  VAL A  74       0.095   8.527  12.256  1.00 73.62           C\\nANISOU  287  CB  VAL A  74     8477  11862   7633  -2350   1446    -95       C\\nATOM    288  CG1 VAL A  74       0.133   7.692  13.523  1.00 69.23           C\\nANISOU  288  CG1 VAL A  74     8110  11512   6684  -2747   1535    127       C\\nATOM    289  CG2 VAL A  74       0.126  10.011  12.581  1.00 69.08           C\\nANISOU  289  CG2 VAL A  74     7641  11478   7130  -1988   1471   -451       C\\nATOM    290  N   SER A  75       2.276  10.106  10.306  1.00 69.43           N\\nANISOU  290  N   SER A  75     8129  10455   7797  -1464   1043   -169       N\\nATOM    291  CA  SER A  75       2.644  10.933   9.164  1.00 66.75           C\\nANISOU  291  CA  SER A  75     7729   9871   7764  -1146    912   -253       C\\nATOM    292  C   SER A  75       3.278  10.082   8.075  1.00 68.29           C\\nANISOU  292  C   SER A  75     8151   9714   8082  -1158    801    -30       C\\nATOM    293  O   SER A  75       3.025  10.291   6.882  1.00 67.91           O\\nANISOU  293  O   SER A  75     8025   9564   8214  -1048    739    -65       O\\nATOM    294  CB  SER A  75       3.595  12.044   9.605  1.00 65.59           C\\nANISOU  294  CB  SER A  75     7599   9627   7697   -876    823   -350       C\\nATOM    295  OG  SER A  75       4.148  12.722   8.492  1.00 65.64           O\\nANISOU  295  OG  SER A  75     7609   9355   7975   -636    678   -344       O\\nATOM    296  N   LEU A  76       4.099   9.107   8.470  1.00 69.61           N\\nANISOU  296  N   LEU A  76     8600   9702   8145  -1281    755    185       N\\nATOM    297  CA  LEU A  76       4.653   8.169   7.503  1.00 70.39           C\\nANISOU  297  CA  LEU A  76     8904   9490   8352  -1284    641    344       C\\nATOM    298  C   LEU A  76       3.555   7.304   6.898  1.00 71.56           C\\nANISOU  298  C   LEU A  76     9015   9685   8488  -1514    675    369       C\\nATOM    299  O   LEU A  76       3.587   6.994   5.700  1.00 67.72           O\\nANISOU  299  O   LEU A  76     8556   9030   8146  -1442    597    372       O\\nATOM    300  CB  LEU A  76       5.725   7.307   8.170  1.00 71.65           C\\nANISOU  300  CB  LEU A  76     9365   9437   8421  -1339    541    534       C\\nATOM    301  CG  LEU A  76       6.488   6.311   7.296  1.00 73.93           C\\nANISOU  301  CG  LEU A  76     9872   9386   8833  -1283    387    648       C\\nATOM    302  CD1 LEU A  76       7.050   6.993   6.057  1.00 66.82           C\\nANISOU  302  CD1 LEU A  76     8859   8395   8135  -1003    352    542       C\\nATOM    303  CD2 LEU A  76       7.598   5.643   8.104  1.00 66.32           C\\nANISOU  303  CD2 LEU A  76     9178   8218   7804  -1274    247    796       C\\nATOM    304  N   ALA A  77       2.567   6.918   7.708  1.00 76.17           N\\nANISOU  304  N   ALA A  77     9525  10531   8886  -1810    794    379       N\\nATOM    305  CA  ALA A  77       1.468   6.103   7.203  1.00 75.85           C\\nANISOU  305  CA  ALA A  77     9422  10562   8836  -2078    825    401       C\\nATOM    306  C   ALA A  77       0.603   6.875   6.217  1.00 76.40           C\\nANISOU  306  C   ALA A  77     9182  10781   9066  -1929    853    183       C\\nATOM    307  O   ALA A  77       0.034   6.277   5.295  1.00 74.94           O\\nANISOU  307  O   ALA A  77     8980  10529   8965  -2027    802    189       O\\nATOM    308  CB  ALA A  77       0.618   5.589   8.364  1.00 77.54           C\\nANISOU  308  CB  ALA A  77     9590  11086   8784  -2476    967    470       C\\nATOM    309  N   VAL A  78       0.484   8.192   6.395  1.00 72.57           N\\nANISOU  309  N   VAL A  78     8462  10479   8634  -1687    898    -17       N\\nATOM    310  CA  VAL A  78      -0.263   9.001   5.438  1.00 73.72           C\\nANISOU  310  CA  VAL A  78     8340  10714   8956  -1502    861   -213       C\\nATOM    311  C   VAL A  78       0.492   9.092   4.118  1.00 73.77           C\\nANISOU  311  C   VAL A  78     8495  10392   9143  -1286    699   -137       C\\nATOM    312  O   VAL A  78      -0.108   9.025   3.037  1.00 75.36           O\\nANISOU  312  O   VAL A  78     8606  10583   9444  -1265    631   -185       O\\nATOM    313  CB  VAL A  78      -0.556  10.391   6.030  1.00 69.67           C\\nANISOU  313  CB  VAL A  78     7563  10433   8477  -1281    899   -460       C\\nATOM    314  CG1 VAL A  78      -1.042  11.346   4.951  1.00 67.83           C\\nANISOU  314  CG1 VAL A  78     7129  10169   8475  -1016    769   -625       C\\nATOM    315  CG2 VAL A  78      -1.591  10.281   7.138  1.00 54.88           C\\nANISOU  315  CG2 VAL A  78     5447   9002   6402  -1505   1086   -609       C\\nATOM    316  N   ALA A  79       1.819   9.239   4.180  1.00 71.40           N\\nANISOU  316  N   ALA A  79     8408   9854   8865  -1136    637    -25       N\\nATOM    317  CA  ALA A  79       2.617   9.243   2.959  1.00 72.25           C\\nANISOU  317  CA  ALA A  79     8642   9715   9095   -969    515     48       C\\nATOM    318  C   ALA A  79       2.382   7.976   2.148  1.00 78.12           C\\nANISOU  318  C   ALA A  79     9512  10348   9824  -1122    472    118       C\\nATOM    319  O   ALA A  79       2.254   8.030   0.919  1.00 82.23           O\\nANISOU  319  O   ALA A  79    10005  10818  10420  -1035    394     87       O\\nATOM    320  CB  ALA A  79       4.097   9.398   3.301  1.00 67.24           C\\nANISOU  320  CB  ALA A  79     8191   8894   8464   -836    476    149       C\\nATOM    321  N   ASP A  80       2.306   6.826   2.820  1.00 70.96           N\\nANISOU  321  N   ASP A  80     8756   9392   8812  -1362    499    214       N\\nATOM    322  CA  ASP A  80       2.041   5.580   2.113  1.00 74.85           C\\nANISOU  322  CA  ASP A  80     9387   9736   9318  -1522    420    263       C\\nATOM    323  C   ASP A  80       0.578   5.468   1.707  1.00 70.40           C\\nANISOU  323  C   ASP A  80     8610   9377   8763  -1703    452    165       C\\nATOM    324  O   ASP A  80       0.275   4.919   0.641  1.00 75.04           O\\nANISOU  324  O   ASP A  80     9225   9874   9413  -1725    358    129       O\\nATOM    325  CB  ASP A  80       2.453   4.386   2.975  1.00 85.13           C\\nANISOU  325  CB  ASP A  80    10957  10859  10529  -1735    379    424       C\\nATOM    326  CG  ASP A  80       3.955   4.316   3.193  1.00 91.73           C\\nANISOU  326  CG  ASP A  80    12008  11459  11389  -1526    293    497       C\\nATOM    327  OD1 ASP A  80       4.707   4.814   2.326  1.00 90.12           O\\nANISOU  327  OD1 ASP A  80    11774  11187  11279  -1257    253    424       O\\nATOM    328  OD2 ASP A  80       4.383   3.762   4.231  1.00 93.76           O\\nANISOU  328  OD2 ASP A  80    12452  11616  11555  -1644    259    631       O\\nATOM    329  N   LEU A  81      -0.340   5.974   2.535  1.00 74.65           N\\nANISOU  329  N   LEU A  81     8912  10218   9233  -1827    580     91       N\\nATOM    330  CA  LEU A  81      -1.751   5.961   2.159  1.00 71.55           C\\nANISOU  330  CA  LEU A  81     8249  10074   8865  -1978    612    -40       C\\nATOM    331  C   LEU A  81      -2.001   6.765   0.893  1.00 74.65           C\\nANISOU  331  C   LEU A  81     8488  10471   9406  -1709    505   -178       C\\nATOM    332  O   LEU A  81      -2.886   6.418   0.105  1.00 69.21           O\\nANISOU  332  O   LEU A  81     7680   9851   8766  -1803    444   -254       O\\nATOM    333  CB  LEU A  81      -2.611   6.504   3.297  1.00 69.87           C\\nANISOU  333  CB  LEU A  81     7752  10250   8545  -2106    782   -153       C\\nATOM    334  CG  LEU A  81      -3.075   5.485   4.331  1.00 74.99           C\\nANISOU  334  CG  LEU A  81     8452  11043   8999  -2544    901    -27       C\\nATOM    335  CD1 LEU A  81      -3.852   6.179   5.437  1.00 74.69           C\\nANISOU  335  CD1 LEU A  81     8087  11477   8814  -2632   1099   -186       C\\nATOM    336  CD2 LEU A  81      -3.924   4.409   3.669  1.00 73.03           C\\nANISOU  336  CD2 LEU A  81     8197  10767   8785  -2854    842     14       C\\nATOM    337  N   LEU A  82      -1.237   7.838   0.678  1.00 69.87           N\\nANISOU  337  N   LEU A  82     7892   9789   8867  -1397    460   -196       N\\nATOM    338  CA  LEU A  82      -1.409   8.637  -0.529  1.00 65.99           C\\nANISOU  338  CA  LEU A  82     7299   9280   8492  -1167    327   -272       C\\nATOM    339  C   LEU A  82      -0.757   7.982  -1.740  1.00 70.21           C\\nANISOU  339  C   LEU A  82     8057   9596   9025  -1131    218   -180       C\\nATOM    340  O   LEU A  82      -1.178   8.231  -2.875  1.00 71.57           O\\nANISOU  340  O   LEU A  82     8160   9794   9239  -1047    101   -233       O\\nATOM    341  CB  LEU A  82      -0.848  10.040  -0.313  1.00 59.37           C\\nANISOU  341  CB  LEU A  82     6407   8421   7728   -892    291   -300       C\\nATOM    342  CG  LEU A  82      -1.644  10.851   0.706  1.00 62.33           C\\nANISOU  342  CG  LEU A  82     6510   9044   8130   -856    360   -482       C\\nATOM    343  CD1 LEU A  82      -1.091  12.261   0.855  1.00 55.10           C\\nANISOU  343  CD1 LEU A  82     5564   8044   7327   -570    267   -530       C\\nATOM    344  CD2 LEU A  82      -3.114  10.883   0.314  1.00 64.42           C\\nANISOU  344  CD2 LEU A  82     6475   9550   8451   -907    325   -667       C\\nATOM    345  N   VAL A  83       0.261   7.147  -1.524  1.00 71.76           N\\nANISOU  345  N   VAL A  83     8510   9592   9162  -1179    238    -64       N\\nATOM    346  CA  VAL A  83       0.813   6.355  -2.620  1.00 69.53           C\\nANISOU  346  CA  VAL A  83     8414   9139   8867  -1147    140    -43       C\\nATOM    347  C   VAL A  83      -0.238   5.394  -3.158  1.00 73.89           C\\nANISOU  347  C   VAL A  83     8937   9715   9422  -1353     76   -116       C\\nATOM    348  O   VAL A  83      -0.404   5.247  -4.375  1.00 79.13           O\\nANISOU  348  O   VAL A  83     9606  10373  10087  -1289    -32   -185       O\\nATOM    349  CB  VAL A  83       2.078   5.608  -2.159  1.00 61.51           C\\nANISOU  349  CB  VAL A  83     7653   7900   7818  -1130    147     49       C\\nATOM    350  CG1 VAL A  83       2.537   4.623  -3.222  1.00 56.33           C\\nANISOU  350  CG1 VAL A  83     7164   7084   7153  -1094     37      1       C\\nATOM    351  CG2 VAL A  83       3.187   6.592  -1.827  1.00 55.01           C\\nANISOU  351  CG2 VAL A  83     6836   7065   7001   -921    189    106       C\\nATOM    352  N   ALA A  84      -0.973   4.732  -2.264  1.00 63.07           N\\nANISOU  352  N   ALA A  84     7532   8393   8036  -1628    136   -100       N\\nATOM    353  CA  ALA A  84      -1.979   3.777  -2.713  1.00 68.51           C\\nANISOU  353  CA  ALA A  84     8190   9097   8744  -1877     65   -159       C\\nATOM    354  C   ALA A  84      -3.109   4.458  -3.475  1.00 67.78           C\\nANISOU  354  C   ALA A  84     7803   9251   8701  -1831     21   -306       C\\nATOM    355  O   ALA A  84      -3.668   3.871  -4.408  1.00 63.21           O\\nANISOU  355  O   ALA A  84     7217   8653   8146  -1911   -101   -386       O\\nATOM    356  CB  ALA A  84      -2.540   3.003  -1.520  1.00 70.03           C\\nANISOU  356  CB  ALA A  84     8393   9327   8888  -2241    149    -72       C\\nATOM    357  N   THR A  85      -3.449   5.692  -3.108  1.00 59.88           N\\nANISOU  357  N   THR A  85     6561   8463   7726  -1685     85   -362       N\\nATOM    358  CA  THR A  85      -4.630   6.368  -3.632  1.00 70.05           C\\nANISOU  358  CA  THR A  85     7536   9994   9087  -1632     16   -521       C\\nATOM    359  C   THR A  85      -4.329   7.352  -4.758  1.00 73.23           C\\nANISOU  359  C   THR A  85     7938  10354   9531  -1316   -140   -540       C\\nATOM    360  O   THR A  85      -5.144   7.493  -5.674  1.00 73.60           O\\nANISOU  360  O   THR A  85     7844  10501   9619  -1283   -285   -640       O\\nATOM    361  CB  THR A  85      -5.355   7.103  -2.501  1.00 66.86           C\\nANISOU  361  CB  THR A  85     6829   9873   8704  -1660    148   -625       C\\nATOM    362  OG1 THR A  85      -4.432   7.958  -1.812  1.00 68.22           O\\nANISOU  362  OG1 THR A  85     7080   9977   8864  -1454    215   -567       O\\nATOM    363  CG2 THR A  85      -5.948   6.109  -1.519  1.00 61.69           C\\nANISOU  363  CG2 THR A  85     6117   9358   7964  -2054    299   -604       C\\nATOM    364  N   LEU A  86      -3.186   8.043  -4.718  1.00 62.95           N\\nANISOU  364  N   LEU A  86     6792   8914   8211  -1106   -129   -431       N\\nATOM    365  CA  LEU A  86      -2.875   9.074  -5.699  1.00 69.96           C\\nANISOU  365  CA  LEU A  86     7691   9770   9119   -857   -279   -398       C\\nATOM    366  C   LEU A  86      -1.823   8.663  -6.718  1.00 73.74           C\\nANISOU  366  C   LEU A  86     8430  10102   9484   -805   -327   -290       C\\nATOM    367  O   LEU A  86      -1.627   9.386  -7.700  1.00 78.44           O\\nANISOU  367  O   LEU A  86     9050  10709  10044   -662   -458   -237       O\\nATOM    368  CB  LEU A  86      -2.400  10.356  -5.000  1.00 71.90           C\\nANISOU  368  CB  LEU A  86     7888   9995   9438   -669   -260   -361       C\\nATOM    369  CG  LEU A  86      -3.358  11.015  -4.012  1.00 70.39           C\\nANISOU  369  CG  LEU A  86     7407   9983   9357   -640   -226   -527       C\\nATOM    370  CD1 LEU A  86      -2.805  12.358  -3.572  1.00 66.08           C\\nANISOU  370  CD1 LEU A  86     6851   9355   8902   -408   -280   -511       C\\nATOM    371  CD2 LEU A  86      -4.735  11.169  -4.633  1.00 73.10           C\\nANISOU  371  CD2 LEU A  86     7488  10505   9781   -625   -371   -694       C\\nATOM    372  N   VAL A  87      -1.137   7.538  -6.512  1.00 71.08           N\\nANISOU  372  N   VAL A  87     8285   9640   9081   -916   -240   -262       N\\nATOM    373  CA  VAL A  87      -0.068   7.087  -7.395  1.00 73.29           C\\nANISOU  373  CA  VAL A  87     8777   9820   9251   -840   -268   -222       C\\nATOM    374  C   VAL A  87      -0.364   5.702  -7.963  1.00 77.64           C\\nANISOU  374  C   VAL A  87     9430  10309   9760   -973   -330   -334       C\\nATOM    375  O   VAL A  87      -0.313   5.497  -9.179  1.00 73.98           O\\nANISOU  375  O   VAL A  87     9018   9892   9199   -916   -433   -399       O\\nATOM    376  CB  VAL A  87       1.295   7.094  -6.673  1.00 71.74           C\\nANISOU  376  CB  VAL A  87     8723   9494   9039   -769   -152   -126       C\\nATOM    377  CG1 VAL A  87       2.408   6.688  -7.635  1.00 74.66           C\\nANISOU  377  CG1 VAL A  87     9249   9829   9290   -667   -171   -133       C\\nATOM    378  CG2 VAL A  87       1.561   8.458  -6.054  1.00 66.12           C\\nANISOU  378  CG2 VAL A  87     7914   8818   8388   -656   -114    -33       C\\nATOM    379  N   MET A  88      -0.666   4.743  -7.091  1.00 80.11           N\\nANISOU  379  N   MET A  88     9788  10515  10136  -1166   -284   -354       N\\nATOM    380  CA  MET A  88      -0.910   3.374  -7.543  1.00 77.27           C\\nANISOU  380  CA  MET A  88     9560  10025   9773  -1313   -382   -456       C\\nATOM    381  C   MET A  88      -2.014   3.257  -8.587  1.00 74.77           C\\nANISOU  381  C   MET A  88     9120   9842   9447  -1377   -521   -585       C\\nATOM    382  O   MET A  88      -1.856   2.434  -9.508  1.00 75.54           O\\nANISOU  382  O   MET A  88     9351   9858   9492  -1370   -641   -704       O\\nATOM    383  CB  MET A  88      -1.213   2.478  -6.335  1.00 80.86           C\\nANISOU  383  CB  MET A  88    10082  10339  10303  -1575   -337   -400       C\\nATOM    384  CG  MET A  88      -0.060   2.322  -5.349  1.00 81.25           C\\nANISOU  384  CG  MET A  88    10311  10211  10350  -1521   -256   -278       C\\nATOM    385  SD  MET A  88       1.427   1.569  -6.040  1.00 83.45           S\\nANISOU  385  SD  MET A  88    10860  10245  10603  -1297   -355   -350       S\\nATOM    386  CE  MET A  88       0.780   0.002  -6.622  1.00 86.55           C\\nANISOU  386  CE  MET A  88    11408  10421  11056  -1493   -560   -493       C\\nATOM    387  N   PRO A  89      -3.134   3.998  -8.521  1.00 73.85           N\\nANISOU  387  N   PRO A  89     8745   9932   9382  -1424   -534   -603       N\\nATOM    388  CA  PRO A  89      -4.103   3.930  -9.629  1.00 74.48           C\\nANISOU  388  CA  PRO A  89     8707  10146   9448  -1448   -704   -735       C\\nATOM    389  C   PRO A  89      -3.480   4.213 -10.985  1.00 73.67           C\\nANISOU  389  C   PRO A  89     8725  10074   9192  -1237   -816   -758       C\\nATOM    390  O   PRO A  89      -3.834   3.559 -11.972  1.00 74.04           O\\nANISOU  390  O   PRO A  89     8817  10141   9174  -1277   -962   -893       O\\nATOM    391  CB  PRO A  89      -5.142   4.990  -9.248  1.00 73.14           C\\nANISOU  391  CB  PRO A  89     8221  10200   9368  -1431   -703   -747       C\\nATOM    392  CG  PRO A  89      -5.085   5.041  -7.779  1.00 71.74           C\\nANISOU  392  CG  PRO A  89     7982  10016   9258  -1543   -514   -680       C\\nATOM    393  CD  PRO A  89      -3.645   4.834  -7.418  1.00 67.98           C\\nANISOU  393  CD  PRO A  89     7787   9325   8719  -1455   -417   -550       C\\nATOM    394  N   TRP A  90      -2.552   5.170 -11.056  1.00 69.93           N\\nANISOU  394  N   TRP A  90     8302   9624   8643  -1037   -753   -630       N\\nATOM    395  CA  TRP A  90      -1.831   5.402 -12.301  1.00 70.06           C\\nANISOU  395  CA  TRP A  90     8440   9716   8463   -885   -824   -623       C\\nATOM    396  C   TRP A  90      -0.927   4.229 -12.652  1.00 73.43           C\\nANISOU  396  C   TRP A  90     9074  10033   8794   -879   -795   -740       C\\nATOM    397  O   TRP A  90      -0.713   3.948 -13.836  1.00 80.52           O\\nANISOU  397  O   TRP A  90    10046  11036   9511   -815   -885   -849       O\\nATOM    398  CB  TRP A  90      -0.996   6.677 -12.206  1.00 72.68           C\\nANISOU  398  CB  TRP A  90     8778  10094   8744   -730   -758   -431       C\\nATOM    399  CG  TRP A  90      -1.743   7.924 -11.827  1.00 78.23           C\\nANISOU  399  CG  TRP A  90     9301  10853   9571   -681   -825   -337       C\\nATOM    400  CD1 TRP A  90      -2.061   8.338 -10.567  1.00 78.70           C\\nANISOU  400  CD1 TRP A  90     9229  10858   9814   -696   -738   -319       C\\nATOM    401  CD2 TRP A  90      -2.229   8.939 -12.716  1.00 88.37           C\\nANISOU  401  CD2 TRP A  90    10523  12253  10801   -588  -1022   -264       C\\nATOM    402  NE1 TRP A  90      -2.729   9.539 -10.616  1.00 79.87           N\\nANISOU  402  NE1 TRP A  90     9218  11075  10052   -589   -872   -284       N\\nATOM    403  CE2 TRP A  90      -2.844   9.929 -11.925  1.00 85.91           C\\nANISOU  403  CE2 TRP A  90    10036  11918  10690   -521  -1067   -232       C\\nATOM    404  CE3 TRP A  90      -2.213   9.101 -14.106  1.00 93.09           C\\nANISOU  404  CE3 TRP A  90    11205  12978  11187   -553  -1185   -228       C\\nATOM    405  CZ2 TRP A  90      -3.436  11.064 -12.476  1.00 91.05           C\\nANISOU  405  CZ2 TRP A  90    10603  12614  11379   -398  -1303   -166       C\\nATOM    406  CZ3 TRP A  90      -2.801  10.229 -14.651  1.00 88.71           C\\nANISOU  406  CZ3 TRP A  90    10584  12483  10637   -467  -1412   -117       C\\nATOM    407  CH2 TRP A  90      -3.404  11.195 -13.838  1.00 91.05           C\\nANISOU  407  CH2 TRP A  90    10716  12700  11179   -380  -1486    -87       C\\nATOM    408  N   VAL A  91      -0.382   3.540 -11.646  1.00 69.25           N\\nANISOU  408  N   VAL A  91     8640   9297   8374   -930   -690   -736       N\\nATOM    409  CA  VAL A  91       0.555   2.453 -11.912  1.00 71.26           C\\nANISOU  409  CA  VAL A  91     9090   9406   8578   -872   -701   -873       C\\nATOM    410  C   VAL A  91      -0.181   1.188 -12.341  1.00 81.86           C\\nANISOU  410  C   VAL A  91    10506  10626   9969  -1010   -867  -1076       C\\nATOM    411  O   VAL A  91       0.272   0.468 -13.239  1.00 84.97           O\\nANISOU  411  O   VAL A  91    11020  11005  10261   -913   -961  -1279       O\\nATOM    412  CB  VAL A  91       1.447   2.203 -10.683  1.00 66.23           C\\nANISOU  412  CB  VAL A  91     8549   8562   8051   -856   -583   -782       C\\nATOM    413  CG1 VAL A  91       2.331   0.984 -10.905  1.00 66.75           C\\nANISOU  413  CG1 VAL A  91     8812   8434   8116   -769   -652   -961       C\\nATOM    414  CG2 VAL A  91       2.295   3.427 -10.395  1.00 71.66           C\\nANISOU  414  CG2 VAL A  91     9171   9373   8685   -712   -442   -614       C\\nATOM    415  N   VAL A  92      -1.320   0.890 -11.713  1.00 76.99           N\\nANISOU  415  N   VAL A  92     9808   9938   9507  -1247   -911  -1047       N\\nATOM    416  CA  VAL A  92      -2.100  -0.267 -12.139  1.00 83.11           C\\nANISOU  416  CA  VAL A  92    10641  10591  10346  -1426  -1092  -1225       C\\nATOM    417  C   VAL A  92      -2.714  -0.014 -13.513  1.00 85.39           C\\nANISOU  417  C   VAL A  92    10837  11112  10496  -1365  -1232  -1373       C\\nATOM    418  O   VAL A  92      -2.760  -0.914 -14.362  1.00 87.20           O\\nANISOU  418  O   VAL A  92    11179  11274  10677  -1366  -1396  -1596       O\\nATOM    419  CB  VAL A  92      -3.160  -0.626 -11.077  1.00 86.97           C\\nANISOU  419  CB  VAL A  92    11035  10994  11015  -1752  -1083  -1133       C\\nATOM    420  CG1 VAL A  92      -4.059   0.557 -10.774  1.00 88.40           C\\nANISOU  420  CG1 VAL A  92    10916  11464  11208  -1788   -990  -1030       C\\nATOM    421  CG2 VAL A  92      -3.984  -1.823 -11.526  1.00 90.14           C\\nANISOU  421  CG2 VAL A  92    11495  11253  11500  -1988  -1291  -1301       C\\nATOM    422  N   TYR A  93      -3.173   1.217 -13.762  1.00 86.77           N\\nANISOU  422  N   TYR A  93    10817  11548  10602  -1298  -1201  -1261       N\\nATOM    423  CA  TYR A  93      -3.600   1.598 -15.106  1.00 83.84           C\\nANISOU  423  CA  TYR A  93    10389  11409  10056  -1209  -1354  -1357       C\\nATOM    424  C   TYR A  93      -2.477   1.379 -16.111  1.00 80.40           C\\nANISOU  424  C   TYR A  93    10133  11042   9375  -1017  -1359  -1466       C\\nATOM    425  O   TYR A  93      -2.706   0.878 -17.219  1.00 74.40           O\\nANISOU  425  O   TYR A  93     9423  10381   8465   -997  -1517  -1669       O\\nATOM    426  CB  TYR A  93      -4.062   3.059 -15.102  1.00 86.78           C\\nANISOU  426  CB  TYR A  93    10567  11993  10412  -1130  -1345  -1178       C\\nATOM    427  CG  TYR A  93      -4.289   3.683 -16.465  1.00 96.56           C\\nANISOU  427  CG  TYR A  93    11788  13469  11430  -1012  -1516  -1193       C\\nATOM    428  CD1 TYR A  93      -5.528   3.603 -17.096  1.00 94.66           C\\nANISOU  428  CD1 TYR A  93    11412  13349  11207  -1088  -1737  -1310       C\\nATOM    429  CD2 TYR A  93      -3.274   4.383 -17.106  1.00 98.40           C\\nANISOU  429  CD2 TYR A  93    12135  13829  11423   -849  -1468  -1073       C\\nATOM    430  CE1 TYR A  93      -5.739   4.185 -18.334  1.00 95.59           C\\nANISOU  430  CE1 TYR A  93    11537  13682  11100   -983  -1926  -1302       C\\nATOM    431  CE2 TYR A  93      -3.475   4.965 -18.343  1.00 97.04           C\\nANISOU  431  CE2 TYR A  93    11974  13889  11007   -780  -1636  -1042       C\\nATOM    432  CZ  TYR A  93      -4.707   4.864 -18.952  1.00 96.39           C\\nANISOU  432  CZ  TYR A  93    11785  13900  10937   -837  -1876  -1153       C\\nATOM    433  OH  TYR A  93      -4.903   5.446 -20.182  1.00 95.53           O\\nANISOU  433  OH  TYR A  93    11712  14022  10562   -771  -2074  -1102       O\\nATOM    434  N   LEU A  94      -1.250   1.724 -15.722  1.00 88.56           N\\nANISOU  434  N   LEU A  94    11244  12051  10355   -879  -1185  -1358       N\\nATOM    435  CA  LEU A  94      -0.090   1.590 -16.592  1.00 90.25           C\\nANISOU  435  CA  LEU A  94    11571  12398  10320   -698  -1144  -1470       C\\nATOM    436  C   LEU A  94       0.187   0.143 -16.984  1.00 86.74           C\\nANISOU  436  C   LEU A  94    11276  11802   9879   -668  -1251  -1798       C\\nATOM    437  O   LEU A  94       0.806  -0.096 -18.027  1.00 79.60           O\\nANISOU  437  O   LEU A  94    10426  11091   8726   -524  -1274  -1999       O\\nATOM    438  CB  LEU A  94       1.131   2.192 -15.893  1.00 91.19           C\\nANISOU  438  CB  LEU A  94    11704  12504  10440   -587   -935  -1297       C\\nATOM    439  CG  LEU A  94       2.362   2.481 -16.745  1.00 96.59           C\\nANISOU  439  CG  LEU A  94    12420  13445  10836   -422   -839  -1342       C\\nATOM    440  CD1 LEU A  94       1.952   3.241 -17.987  1.00 95.48           C\\nANISOU  440  CD1 LEU A  94    12233  13639  10407   -435   -921  -1281       C\\nATOM    441  CD2 LEU A  94       3.366   3.277 -15.931  1.00 94.01           C\\nANISOU  441  CD2 LEU A  94    12057  13105  10556   -364   -648  -1120       C\\nATOM    442  N   GLU A  95      -0.244  -0.827 -16.175  1.00 91.64           N\\nANISOU  442  N   GLU A  95    11967  12086  10767   -809  -1328  -1863       N\\nATOM    443  CA  GLU A  95      -0.007  -2.228 -16.505  1.00 89.73           C\\nANISOU  443  CA  GLU A  95    11897  11617  10578   -779  -1491  -2179       C\\nATOM    444  C   GLU A  95      -1.104  -2.803 -17.392  1.00 87.68           C\\nANISOU  444  C   GLU A  95    11631  11388  10293   -904  -1724  -2391       C\\nATOM    445  O   GLU A  95      -0.812  -3.568 -18.317  1.00 89.77           O\\nANISOU  445  O   GLU A  95    12002  11667  10441   -784  -1865  -2717       O\\nATOM    446  CB  GLU A  95       0.121  -3.065 -15.229  1.00 87.59           C\\nANISOU  446  CB  GLU A  95    11758  10917  10607   -899  -1515  -2120       C\\nATOM    447  CG  GLU A  95       0.439  -4.539 -15.480  1.00 93.67           C\\nANISOU  447  CG  GLU A  95    12747  11357  11487   -851  -1741  -2438       C\\nATOM    448  CD  GLU A  95       1.851  -4.758 -16.002  1.00102.62           C\\nANISOU  448  CD  GLU A  95    13952  12557  12482   -504  -1707  -2681       C\\nATOM    449  OE1 GLU A  95       2.722  -3.902 -15.740  1.00104.20           O\\nANISOU  449  OE1 GLU A  95    14062  12957  12571   -357  -1484  -2527       O\\nATOM    450  OE2 GLU A  95       2.093  -5.788 -16.670  1.00107.64           O\\nANISOU  450  OE2 GLU A  95    14717  13056  13125   -376  -1910  -3051       O\\nATOM    451  N   VAL A  96      -2.362  -2.449 -17.129  1.00 78.94           N\\nANISOU  451  N   VAL A  96    10382  10316   9297  -1131  -1774  -2245       N\\nATOM    452  CA  VAL A  96      -3.462  -2.952 -17.947  1.00 80.52           C\\nANISOU  452  CA  VAL A  96    10543  10563   9488  -1267  -2011  -2444       C\\nATOM    453  C   VAL A  96      -3.331  -2.439 -19.375  1.00 85.05           C\\nANISOU  453  C   VAL A  96    11087  11511   9717  -1081  -2072  -2578       C\\nATOM    454  O   VAL A  96      -3.404  -3.209 -20.340  1.00 82.90           O\\nANISOU  454  O   VAL A  96    10906  11266   9327  -1037  -2258  -2893       O\\nATOM    455  CB  VAL A  96      -4.816  -2.561 -17.328  1.00 77.18           C\\nANISOU  455  CB  VAL A  96     9907  10166   9251  -1538  -2032  -2265       C\\nATOM    456  N   VAL A  97      -3.117  -1.130 -19.528  1.00 87.40           N\\nANISOU  456  N   VAL A  97    11271  12099   9836   -979  -1932  -2336       N\\nATOM    457  CA  VAL A  97      -2.995  -0.529 -20.854  1.00 88.86           C\\nANISOU  457  CA  VAL A  97    11446  12664   9653   -847  -1994  -2384       C\\nATOM    458  C   VAL A  97      -1.719  -0.983 -21.554  1.00 90.16           C\\nANISOU  458  C   VAL A  97    11752  12956   9548   -647  -1919  -2608       C\\nATOM    459  O   VAL A  97      -1.694  -1.122 -22.783  1.00 92.93           O\\nANISOU  459  O   VAL A  97    12140  13588   9583   -572  -2028  -2817       O\\nATOM    460  CB  VAL A  97      -3.061   1.005 -20.740  1.00 86.80           C\\nANISOU  460  CB  VAL A  97    11060  12617   9305   -817  -1897  -2025       C\\nATOM    461  CG1 VAL A  97      -2.893   1.659 -22.106  1.00 88.76           C\\nANISOU  461  CG1 VAL A  97    11335  13252   9139   -721  -1981  -2009       C\\nATOM    462  CG2 VAL A  97      -4.372   1.434 -20.086  1.00 86.16           C\\nANISOU  462  CG2 VAL A  97    10792  12448   9495   -970  -1990  -1884       C\\nATOM    463  N   GLY A  98      -0.650  -1.230 -20.800  1.00 88.15           N\\nANISOU  463  N   GLY A  98    11562  12531   9400   -550  -1740  -2596       N\\nATOM    464  CA  GLY A  98       0.613  -1.604 -21.402  1.00 89.34           C\\nANISOU  464  CA  GLY A  98    11789  12846   9310   -334  -1652  -2837       C\\nATOM    465  C   GLY A  98       1.360  -0.469 -22.059  1.00 91.48           C\\nANISOU  465  C   GLY A  98    11987  13570   9202   -247  -1473  -2660       C\\nATOM    466  O   GLY A  98       2.307  -0.717 -22.810  1.00 93.59           O\\nANISOU  466  O   GLY A  98    12270  14114   9177    -92  -1395  -2892       O\\nATOM    467  N   GLU A  99       0.962   0.772 -21.797  1.00 93.52           N\\nANISOU  467  N   GLU A  99    12159  13918   9455   -352  -1418  -2264       N\\nATOM    468  CA  GLU A  99       1.609   1.938 -22.378  1.00 95.54           C\\nANISOU  468  CA  GLU A  99    12373  14557   9372   -328  -1286  -2022       C\\nATOM    469  C   GLU A  99       1.259   3.151 -21.529  1.00 92.97           C\\nANISOU  469  C   GLU A  99    11976  14105   9244   -422  -1241  -1593       C\\nATOM    470  O   GLU A  99       0.253   3.163 -20.815  1.00 85.82           O\\nANISOU  470  O   GLU A  99    11021  12937   8648   -506  -1345  -1519       O\\nATOM    471  CB  GLU A  99       1.181   2.153 -23.835  1.00 94.86           C\\nANISOU  471  CB  GLU A  99    12308  14866   8868   -355  -1437  -2092       C\\nATOM    472  N   TRP A 100       2.110   4.174 -21.614  1.00 89.68           N\\nANISOU  472  N   TRP A 100    11539  13894   8642   -414  -1089  -1330       N\\nATOM    473  CA  TRP A 100       1.871   5.446 -20.932  1.00 88.27           C\\nANISOU  473  CA  TRP A 100    11308  13606   8625   -483  -1080   -935       C\\nATOM    474  C   TRP A 100       0.892   6.302 -21.742  1.00 91.37           C\\nANISOU  474  C   TRP A 100    11702  14149   8867   -556  -1315   -744       C\\nATOM    475  O   TRP A 100       1.217   7.382 -22.236  1.00 95.09           O\\nANISOU  475  O   TRP A 100    12204  14809   9115   -605  -1334   -453       O\\nATOM    476  CB  TRP A 100       3.188   6.177 -20.702  1.00 86.77           C\\nANISOU  476  CB  TRP A 100    11107  13540   8322   -471   -861   -729       C\\nATOM    477  CG  TRP A 100       4.148   5.471 -19.784  1.00 92.86           C\\nANISOU  477  CG  TRP A 100    11859  14140   9283   -376   -663   -888       C\\nATOM    478  CD1 TRP A 100       4.731   4.252 -19.983  1.00 99.53           C\\nANISOU  478  CD1 TRP A 100    12726  15011  10078   -261   -605  -1253       C\\nATOM    479  CD2 TRP A 100       4.655   5.958 -18.534  1.00 93.04           C\\nANISOU  479  CD2 TRP A 100    11841  13932   9577   -369   -533   -700       C\\nATOM    480  NE1 TRP A 100       5.558   3.944 -18.928  1.00 99.78           N\\nANISOU  480  NE1 TRP A 100    12740  14828  10345   -179   -465  -1286       N\\nATOM    481  CE2 TRP A 100       5.530   4.975 -18.027  1.00 94.10           C\\nANISOU  481  CE2 TRP A 100    11981  13965   9809   -254   -408   -944       C\\nATOM    482  CE3 TRP A 100       4.449   7.125 -17.792  1.00 92.42           C\\nANISOU  482  CE3 TRP A 100    11726  13714   9675   -431   -538   -373       C\\nATOM    483  CZ2 TRP A 100       6.198   5.125 -16.811  1.00 92.35           C\\nANISOU  483  CZ2 TRP A 100    11733  13525   9830   -217   -285   -845       C\\nATOM    484  CZ3 TRP A 100       5.114   7.273 -16.583  1.00 87.83           C\\nANISOU  484  CZ3 TRP A 100    11114  12928   9330   -397   -398   -300       C\\nATOM    485  CH2 TRP A 100       5.977   6.279 -16.107  1.00 90.94           C\\nANISOU  485  CH2 TRP A 100    11517  13244   9792   -299   -271   -522       C\\nATOM    486  N   LYS A 101      -0.329   5.791 -21.877  1.00 95.15           N\\nANISOU  486  N   LYS A 101    12148  14527   9477   -577  -1521   -906       N\\nATOM    487  CA  LYS A 101      -1.365   6.446 -22.678  1.00 96.45           C\\nANISOU  487  CA  LYS A 101    12300  14824   9522   -619  -1798   -787       C\\nATOM    488  C   LYS A 101      -2.121   7.498 -21.869  1.00 98.53           C\\nANISOU  488  C   LYS A 101    12457  14876  10104   -621  -1907   -529       C\\nATOM    489  O   LYS A 101      -3.351   7.502 -21.813  1.00100.15           O\\nANISOU  489  O   LYS A 101    12553  15004  10495   -628  -2120   -595       O\\nATOM    490  CB  LYS A 101      -2.319   5.405 -23.251  1.00 91.01           C\\nANISOU  490  CB  LYS A 101    11597  14158   8826   -638  -1991  -1116       C\\nATOM    491  N   PHE A 102      -1.377   8.397 -21.223  1.00 92.76           N\\nANISOU  491  N   PHE A 102    11736  14060   9449   -605  -1768   -264       N\\nATOM    492  CA  PHE A 102      -1.943   9.593 -20.620  1.00 93.22           C\\nANISOU  492  CA  PHE A 102    11716  13947   9756   -575  -1904    -18       C\\nATOM    493  C   PHE A 102      -1.857  10.735 -21.628  1.00 91.71           C\\nANISOU  493  C   PHE A 102    11641  13918   9287   -599  -2119    289       C\\nATOM    494  O   PHE A 102      -1.422  10.558 -22.768  1.00103.07           O\\nANISOU  494  O   PHE A 102    13204  15642  10313   -665  -2138    313       O\\nATOM    495  CB  PHE A 102      -1.202   9.983 -19.340  1.00 94.22           C\\nANISOU  495  CB  PHE A 102    11808  13862  10129   -551  -1677     95       C\\nATOM    496  CG  PHE A 102      -0.815   8.827 -18.469  1.00 91.97           C\\nANISOU  496  CG  PHE A 102    11490  13455  10000   -556  -1432   -141       C\\nATOM    497  CD1 PHE A 102      -1.737   8.243 -17.618  1.00 88.34           C\\nANISOU  497  CD1 PHE A 102    10903  12822   9841   -574  -1444   -314       C\\nATOM    498  CD2 PHE A 102       0.483   8.344 -18.477  1.00 88.17           C\\nANISOU  498  CD2 PHE A 102    11097  13037   9364   -553  -1204   -181       C\\nATOM    499  CE1 PHE A 102      -1.375   7.184 -16.805  1.00 84.23           C\\nANISOU  499  CE1 PHE A 102    10394  12156   9452   -611  -1257   -481       C\\nATOM    500  CE2 PHE A 102       0.849   7.286 -17.667  1.00 83.36           C\\nANISOU  500  CE2 PHE A 102    10485  12270   8917   -538  -1037   -386       C\\nATOM    501  CZ  PHE A 102      -0.082   6.706 -16.830  1.00 81.83           C\\nANISOU  501  CZ  PHE A 102    10213  11865   9014   -578  -1075   -513       C\\nATOM    502  N   SER A 103      -2.265  11.924 -21.210  1.00 88.70           N\\nANISOU  502  N   SER A 103    11226  13356   9120   -550  -2299    526       N\\nATOM    503  CA  SER A 103      -1.855  13.135 -21.896  1.00 82.43           C\\nANISOU  503  CA  SER A 103    10589  12620   8110   -603  -2476    904       C\\nATOM    504  C   SER A 103      -0.586  13.661 -21.237  1.00 83.13           C\\nANISOU  504  C   SER A 103    10732  12623   8230   -660  -2230   1106       C\\nATOM    505  O   SER A 103      -0.135  13.148 -20.210  1.00 83.31           O\\nANISOU  505  O   SER A 103    10661  12526   8466   -622  -1957    945       O\\nATOM    506  CB  SER A 103      -2.969  14.182 -21.869  1.00 79.20           C\\nANISOU  506  CB  SER A 103    10137  12018   7939   -498  -2879   1043       C\\nATOM    507  OG  SER A 103      -3.335  14.521 -20.542  1.00 76.16           O\\nANISOU  507  OG  SER A 103     9579  11344   8016   -372  -2840    955       O\\nATOM    508  N   ARG A 104       0.009  14.689 -21.845  1.00 84.27           N\\nANISOU  508  N   ARG A 104    11037  12833   8148   -776  -2344   1478       N\\nATOM    509  CA  ARG A 104       1.252  15.212 -21.290  1.00 80.60           C\\nANISOU  509  CA  ARG A 104    10612  12312   7701   -868  -2123   1679       C\\nATOM    510  C   ARG A 104       1.025  15.830 -19.921  1.00 77.44           C\\nANISOU  510  C   ARG A 104    10113  11518   7794   -740  -2150   1682       C\\nATOM    511  O   ARG A 104       1.913  15.783 -19.064  1.00 78.86           O\\nANISOU  511  O   ARG A 104    10250  11620   8096   -755  -1890   1666       O\\nATOM    512  CB  ARG A 104       1.881  16.231 -22.235  1.00 80.66           C\\nANISOU  512  CB  ARG A 104    10815  12469   7362  -1078  -2266   2114       C\\nATOM    513  CG  ARG A 104       3.382  16.383 -22.031  1.00 90.20           C\\nANISOU  513  CG  ARG A 104    12038  13815   8417  -1248  -1948   2260       C\\nATOM    514  CD  ARG A 104       3.766  17.736 -21.446  1.00101.17           C\\nANISOU  514  CD  ARG A 104    13504  14894  10041  -1329  -2089   2624       C\\nATOM    515  NE  ARG A 104       3.451  18.831 -22.359  1.00106.68           N\\nANISOU  515  NE  ARG A 104    14414  15562  10556  -1484  -2476   3046       N\\nATOM    516  CZ  ARG A 104       2.650  19.849 -22.059  1.00108.76           C\\nANISOU  516  CZ  ARG A 104    14758  15416  11150  -1381  -2885   3220       C\\nATOM    517  NH1 ARG A 104       2.092  19.927 -20.857  1.00104.63           N\\nANISOU  517  NH1 ARG A 104    14088  14533  11136  -1126  -2918   2984       N\\nATOM    518  NH2 ARG A 104       2.417  20.795 -22.961  1.00112.28           N\\nANISOU  518  NH2 ARG A 104    15433  15822  11408  -1532  -3275   3626       N\\nATOM    519  N   ILE A 105      -0.160  16.392 -19.688  1.00 79.98           N\\nANISOU  519  N   ILE A 105    10379  11613   8397   -597  -2469   1666       N\\nATOM    520  CA  ILE A 105      -0.435  17.000 -18.394  1.00 78.38           C\\nANISOU  520  CA  ILE A 105    10057  11079   8646   -452  -2502   1613       C\\nATOM    521  C   ILE A 105      -0.797  15.939 -17.359  1.00 74.85           C\\nANISOU  521  C   ILE A 105     9401  10617   8423   -355  -2239   1232       C\\nATOM    522  O   ILE A 105      -0.422  16.063 -16.189  1.00 73.96           O\\nANISOU  522  O   ILE A 105     9211  10343   8549   -307  -2066   1171       O\\nATOM    523  CB  ILE A 105      -1.528  18.076 -18.534  1.00 77.26           C\\nANISOU  523  CB  ILE A 105     9910  10715   8730   -308  -2966   1710       C\\nATOM    524  CG1 ILE A 105      -1.691  18.858 -17.227  1.00 76.93           C\\nANISOU  524  CG1 ILE A 105     9750  10345   9133   -142  -3017   1643       C\\nATOM    525  CG2 ILE A 105      -2.847  17.465 -18.989  1.00 71.80           C\\nANISOU  525  CG2 ILE A 105     9083  10142   8055   -199  -3143   1458       C\\nATOM    526  CD1 ILE A 105      -0.522  19.761 -16.903  1.00 63.79           C\\nANISOU  526  CD1 ILE A 105     8244   8504   7489   -248  -2982   1938       C\\nATOM    527  N   HIS A 106      -1.425  14.862 -17.789  1.00 78.10           N\\nANISOU  527  N   HIS A 106     9732  11194   8747   -350  -2214    984       N\\nATOM    528  CA  HIS A 106      -1.751  13.780 -16.889  1.00 72.04           C\\nANISOU  528  CA  HIS A 106     8805  10412   8157   -326  -1967    668       C\\nATOM    529  C   HIS A 106      -0.480  13.081 -16.470  1.00 75.28           C\\nANISOU  529  C   HIS A 106     9289  10863   8451   -409  -1617    644       C\\nATOM    530  O   HIS A 106      -0.345  12.663 -15.351  1.00 70.37           O\\nANISOU  530  O   HIS A 106     8580  10125   8032   -389  -1418    503       O\\nATOM    531  CB  HIS A 106      -2.690  12.806 -17.558  1.00 69.03           C\\nANISOU  531  CB  HIS A 106     8344  10182   7701   -344  -2050    426       C\\nATOM    532  CG  HIS A 106      -4.109  13.257 -17.558  1.00 86.66           C\\nANISOU  532  CG  HIS A 106    10420  12382  10122   -239  -2375    359       C\\nATOM    533  ND1 HIS A 106      -4.497  14.469 -17.043  1.00 93.53           N\\nANISOU  533  ND1 HIS A 106    11265  13098  11175   -109  -2634    518       N\\nATOM    534  CD2 HIS A 106      -5.234  12.662 -18.003  1.00 92.54           C\\nANISOU  534  CD2 HIS A 106    11011  13228  10921   -235  -2507    125       C\\nATOM    535  CE1 HIS A 106      -5.801  14.602 -17.170  1.00 95.16           C\\nANISOU  535  CE1 HIS A 106    11292  13325  11539     -1  -2912    369       C\\nATOM    536  NE2 HIS A 106      -6.273  13.520 -17.751  1.00 94.46           N\\nANISOU  536  NE2 HIS A 106    11111  13409  11371    -89  -2829    134       N\\nATOM    537  N   CYS A 107       0.459  12.953 -17.384  1.00 74.40           N\\nANISOU  537  N   CYS A 107     9326  10942   8001   -501  -1547    768       N\\nATOM    538  CA  CYS A 107       1.750  12.355 -17.073  1.00 74.41           C\\nANISOU  538  CA  CYS A 107     9366  11008   7898   -548  -1239    725       C\\nATOM    539  C   CYS A 107       2.520  13.220 -16.082  1.00 69.26           C\\nANISOU  539  C   CYS A 107     8705  10174   7436   -541  -1146    902       C\\nATOM    540  O   CYS A 107       3.036  12.718 -15.076  1.00 62.15           O\\nANISOU  540  O   CYS A 107     7754   9173   6688   -508   -936    780       O\\nATOM    541  CB  CYS A 107       2.542  12.149 -18.368  1.00 77.98           C\\nANISOU  541  CB  CYS A 107     9930  11782   7918   -646  -1190    790       C\\nATOM    542  SG  CYS A 107       4.200  11.445 -18.193  1.00 79.49           S\\nANISOU  542  SG  CYS A 107    10119  12137   7945   -673   -832    689       S\\nATOM    543  N   ASP A 108       2.590  14.530 -16.341  1.00 68.64           N\\nANISOU  543  N   ASP A 108     8692  10029   7359   -576  -1335   1195       N\\nATOM    544  CA  ASP A 108       3.289  15.433 -15.430  1.00 67.61           C\\nANISOU  544  CA  ASP A 108     8561   9699   7427   -578  -1293   1358       C\\nATOM    545  C   ASP A 108       2.673  15.405 -14.037  1.00 65.65           C\\nANISOU  545  C   ASP A 108     8180   9208   7557   -435  -1270   1167       C\\nATOM    546  O   ASP A 108       3.393  15.362 -13.033  1.00 66.27           O\\nANISOU  546  O   ASP A 108     8226   9190   7765   -423  -1086   1133       O\\nATOM    547  CB  ASP A 108       3.280  16.856 -15.990  1.00 70.02           C\\nANISOU  547  CB  ASP A 108     8985   9912   7707   -648  -1582   1705       C\\nATOM    548  CG  ASP A 108       4.274  17.047 -17.124  1.00 81.41           C\\nANISOU  548  CG  ASP A 108    10562  11623   8747   -867  -1532   1967       C\\nATOM    549  OD1 ASP A 108       5.293  16.329 -17.150  1.00 84.41           O\\nANISOU  549  OD1 ASP A 108    10904  12225   8943   -940  -1226   1879       O\\nATOM    550  OD2 ASP A 108       4.043  17.922 -17.986  1.00 86.93           O\\nANISOU  550  OD2 ASP A 108    11397  12326   9305   -971  -1808   2260       O\\nATOM    551  N   ILE A 109       1.341  15.424 -13.956  1.00 63.48           N\\nANISOU  551  N   ILE A 109     7808   8870   7442   -332  -1455   1030       N\\nATOM    552  CA  ILE A 109       0.665  15.365 -12.662  1.00 61.96           C\\nANISOU  552  CA  ILE A 109     7449   8532   7562   -218  -1412    821       C\\nATOM    553  C   ILE A 109       1.015  14.072 -11.937  1.00 63.72           C\\nANISOU  553  C   ILE A 109     7629   8811   7771   -268  -1106    623       C\\nATOM    554  O   ILE A 109       1.341  14.076 -10.743  1.00 59.23           O\\nANISOU  554  O   ILE A 109     7010   8137   7359   -241   -960    564       O\\nATOM    555  CB  ILE A 109      -0.856  15.511 -12.845  1.00 58.03           C\\nANISOU  555  CB  ILE A 109     6805   8039   7204   -115  -1656    674       C\\nATOM    556  CG1 ILE A 109      -1.212  16.937 -13.262  1.00 58.42           C\\nANISOU  556  CG1 ILE A 109     6896   7940   7362    -12  -2018    855       C\\nATOM    557  CG2 ILE A 109      -1.588  15.133 -11.573  1.00 56.04           C\\nANISOU  557  CG2 ILE A 109     6336   7761   7197    -50  -1535    405       C\\nATOM    558  CD1 ILE A 109      -2.681  17.131 -13.524  1.00 59.89           C\\nANISOU  558  CD1 ILE A 109     6917   8142   7695    126  -2302    693       C\\nATOM    559  N   PHE A 110       0.949  12.945 -12.648  1.00 61.78           N\\nANISOU  559  N   PHE A 110     7422   8717   7335   -338  -1034    516       N\\nATOM    560  CA  PHE A 110       1.250  11.658 -12.031  1.00 58.79           C\\nANISOU  560  CA  PHE A 110     7039   8336   6961   -385   -808    335       C\\nATOM    561  C   PHE A 110       2.679  11.622 -11.510  1.00 63.91           C\\nANISOU  561  C   PHE A 110     7771   8939   7574   -390   -613    414       C\\nATOM    562  O   PHE A 110       2.921  11.236 -10.361  1.00 59.44           O\\nANISOU  562  O   PHE A 110     7180   8260   7146   -384   -476    340       O\\nATOM    563  CB  PHE A 110       0.997  10.530 -13.034  1.00 61.38           C\\nANISOU  563  CB  PHE A 110     7419   8803   7098   -442   -823    194       C\\nATOM    564  CG  PHE A 110       1.692   9.234 -12.700  1.00 68.94           C\\nANISOU  564  CG  PHE A 110     8447   9728   8016   -477   -636     42       C\\nATOM    565  CD1 PHE A 110       1.579   8.662 -11.444  1.00 75.18           C\\nANISOU  565  CD1 PHE A 110     9204  10361   8999   -508   -525    -42       C\\nATOM    566  CD2 PHE A 110       2.437   8.573 -13.660  1.00 71.59           C\\nANISOU  566  CD2 PHE A 110     8887  10201   8115   -474   -595    -28       C\\nATOM    567  CE1 PHE A 110       2.216   7.472 -11.150  1.00 77.40           C\\nANISOU  567  CE1 PHE A 110     9585  10560   9264   -531   -416   -161       C\\nATOM    568  CE2 PHE A 110       3.070   7.383 -13.372  1.00 74.90           C\\nANISOU  568  CE2 PHE A 110     9372  10553   8534   -462   -477   -203       C\\nATOM    569  CZ  PHE A 110       2.960   6.833 -12.116  1.00 77.70           C\\nANISOU  569  CZ  PHE A 110     9724  10690   9110   -489   -407   -255       C\\nATOM    570  N   VAL A 111       3.641  12.034 -12.340  1.00 65.60           N\\nANISOU  570  N   VAL A 111     8072   9264   7587   -416   -603    568       N\\nATOM    571  CA  VAL A 111       5.043  11.987 -11.930  1.00 66.54           C\\nANISOU  571  CA  VAL A 111     8228   9388   7667   -424   -420    620       C\\nATOM    572  C   VAL A 111       5.288  12.924 -10.757  1.00 60.65           C\\nANISOU  572  C   VAL A 111     7442   8452   7150   -393   -417    727       C\\nATOM    573  O   VAL A 111       6.026  12.590  -9.822  1.00 56.21           O\\nANISOU  573  O   VAL A 111     6872   7814   6670   -370   -270    674       O\\nATOM    574  CB  VAL A 111       5.960  12.317 -13.119  1.00 69.81           C\\nANISOU  574  CB  VAL A 111     8700  10035   7791   -499   -401    765       C\\nATOM    575  CG1 VAL A 111       7.405  12.336 -12.671  1.00 60.98           C\\nANISOU  575  CG1 VAL A 111     7563   8955   6651   -512   -214    801       C\\nATOM    576  CG2 VAL A 111       5.758  11.308 -14.235  1.00 72.95           C\\nANISOU  576  CG2 VAL A 111     9130  10652   7937   -508   -394    597       C\\nATOM    577  N   THR A 112       4.669  14.106 -10.784  1.00 59.23           N\\nANISOU  577  N   THR A 112     7242   8180   7083   -374   -610    861       N\\nATOM    578  CA  THR A 112       4.789  15.036  -9.664  1.00 65.31           C\\nANISOU  578  CA  THR A 112     7970   8754   8090   -319   -646    910       C\\nATOM    579  C   THR A 112       4.286  14.407  -8.371  1.00 66.52           C\\nANISOU  579  C   THR A 112     8031   8833   8410   -256   -532    693       C\\nATOM    580  O   THR A 112       4.970  14.440  -7.343  1.00 76.31           O\\nANISOU  580  O   THR A 112     9268   9991   9734   -241   -417    676       O\\nATOM    581  CB  THR A 112       4.019  16.321  -9.963  1.00 64.71           C\\nANISOU  581  CB  THR A 112     7889   8561   8139   -269   -933   1031       C\\nATOM    582  OG1 THR A 112       4.645  17.010 -11.052  1.00 63.73           O\\nANISOU  582  OG1 THR A 112     7888   8484   7843   -379  -1048   1304       O\\nATOM    583  CG2 THR A 112       3.995  17.223  -8.744  1.00 62.38           C\\nANISOU  583  CG2 THR A 112     7534   8052   8116   -171   -994    998       C\\nATOM    584  N   LEU A 113       3.086  13.825  -8.407  1.00 61.29           N\\nANISOU  584  N   LEU A 113     7289   8219   7778   -245   -569    534       N\\nATOM    585  CA  LEU A 113       2.533  13.195  -7.214  1.00 68.29           C\\nANISOU  585  CA  LEU A 113     8081   9085   8780   -248   -453    353       C\\nATOM    586  C   LEU A 113       3.348  11.975  -6.799  1.00 67.53           C\\nANISOU  586  C   LEU A 113     8081   8983   8595   -321   -257    312       C\\nATOM    587  O   LEU A 113       3.573  11.752  -5.604  1.00 68.67           O\\nANISOU  587  O   LEU A 113     8216   9064   8811   -332   -149    267       O\\nATOM    588  CB  LEU A 113       1.075  12.808  -7.454  1.00 70.65           C\\nANISOU  588  CB  LEU A 113     8249   9477   9119   -266   -536    201       C\\nATOM    589  CG  LEU A 113       0.073  13.960  -7.517  1.00 65.91           C\\nANISOU  589  CG  LEU A 113     7497   8872   8673   -146   -751    162       C\\nATOM    590  CD1 LEU A 113      -1.287  13.451  -7.958  1.00 61.41           C\\nANISOU  590  CD1 LEU A 113     6776   8439   8118   -174   -840      2       C\\nATOM    591  CD2 LEU A 113      -0.016  14.648  -6.165  1.00 61.76           C\\nANISOU  591  CD2 LEU A 113     6853   8287   8324    -59   -710     69       C\\nATOM    592  N   ASP A 114       3.794  11.174  -7.768  1.00 63.91           N\\nANISOU  592  N   ASP A 114     7718   8590   7975   -359   -233    311       N\\nATOM    593  CA  ASP A 114       4.598   9.999  -7.445  1.00 66.05           C\\nANISOU  593  CA  ASP A 114     8086   8820   8191   -384   -102    240       C\\nATOM    594  C   ASP A 114       5.885  10.392  -6.734  1.00 66.08           C\\nANISOU  594  C   ASP A 114     8124   8760   8225   -333    -12    324       C\\nATOM    595  O   ASP A 114       6.262   9.778  -5.730  1.00 69.96           O\\nANISOU  595  O   ASP A 114     8658   9151   8773   -337     64    278       O\\nATOM    596  CB  ASP A 114       4.901   9.208  -8.720  1.00 75.01           C\\nANISOU  596  CB  ASP A 114     9296  10059   9148   -388   -118    174       C\\nATOM    597  CG  ASP A 114       5.951   8.133  -8.509  1.00 75.49           C\\nANISOU  597  CG  ASP A 114     9451  10063   9168   -352    -25     76       C\\nATOM    598  OD1 ASP A 114       5.746   7.255  -7.648  1.00 74.37           O\\nANISOU  598  OD1 ASP A 114     9364   9766   9125   -388     -9     -2       O\\nATOM    599  OD2 ASP A 114       6.981   8.161  -9.214  1.00 76.15           O\\nANISOU  599  OD2 ASP A 114     9549  10268   9116   -291     20     74       O\\nATOM    600  N   VAL A 115       6.568  11.421  -7.235  1.00 71.45           N\\nANISOU  600  N   VAL A 115     8790   9494   8864   -306    -41    464       N\\nATOM    601  CA  VAL A 115       7.809  11.865  -6.610  1.00 70.24           C\\nANISOU  601  CA  VAL A 115     8641   9297   8749   -279     30    542       C\\nATOM    602  C   VAL A 115       7.535  12.461  -5.234  1.00 69.24           C\\nANISOU  602  C   VAL A 115     8477   9030   8802   -253     19    542       C\\nATOM    603  O   VAL A 115       8.282  12.220  -4.279  1.00 70.91           O\\nANISOU  603  O   VAL A 115     8710   9175   9059   -230     93    521       O\\nATOM    604  CB  VAL A 115       8.536  12.862  -7.531  1.00 65.07           C\\nANISOU  604  CB  VAL A 115     7975   8750   7999   -319     -9    719       C\\nATOM    605  CG1 VAL A 115       9.683  13.529  -6.804  1.00 60.52           C\\nANISOU  605  CG1 VAL A 115     7374   8118   7505   -321     36    809       C\\nATOM    606  CG2 VAL A 115       9.043  12.156  -8.778  1.00 62.56           C\\nANISOU  606  CG2 VAL A 115     7676   8649   7446   -346     53    680       C\\nATOM    607  N   MET A 116       6.454  13.232  -5.103  1.00 72.12           N\\nANISOU  607  N   MET A 116     8773   9364   9266   -239    -88    539       N\\nATOM    608  CA  MET A 116       6.164  13.889  -3.832  1.00 68.31           C\\nANISOU  608  CA  MET A 116     8226   8792   8936   -191   -103    487       C\\nATOM    609  C   MET A 116       5.814  12.877  -2.746  1.00 67.37           C\\nANISOU  609  C   MET A 116     8106   8685   8808   -232     19    357       C\\nATOM    610  O   MET A 116       6.435  12.860  -1.677  1.00 67.14           O\\nANISOU  610  O   MET A 116     8105   8604   8802   -221     83    349       O\\nATOM    611  CB  MET A 116       5.031  14.896  -4.005  1.00 66.63           C\\nANISOU  611  CB  MET A 116     7912   8564   8843   -129   -269    455       C\\nATOM    612  CG  MET A 116       4.669  15.602  -2.718  1.00 65.54           C\\nANISOU  612  CG  MET A 116     7676   8370   8856    -46   -291    332       C\\nATOM    613  SD  MET A 116       3.209  16.636  -2.880  1.00 73.08           S\\nANISOU  613  SD  MET A 116     8464   9323   9980     85   -509    199       S\\nATOM    614  CE  MET A 116       3.000  17.178  -1.184  1.00 75.15           C\\nANISOU  614  CE  MET A 116     8597   9592  10365    186   -462    -23       C\\nATOM    615  N   MET A 117       4.820  12.023  -3.000  1.00 57.68           N\\nANISOU  615  N   MET A 117     6854   7527   7535   -303     36    271       N\\nATOM    616  CA  MET A 117       4.373  11.084  -1.977  1.00 63.01           C\\nANISOU  616  CA  MET A 117     7536   8218   8187   -406    135    188       C\\nATOM    617  C   MET A 117       5.457  10.093  -1.578  1.00 71.53           C\\nANISOU  617  C   MET A 117     8783   9196   9201   -439    202    236       C\\nATOM    618  O   MET A 117       5.388   9.526  -0.482  1.00 77.20           O\\nANISOU  618  O   MET A 117     9549   9888   9894   -524    260    225       O\\nATOM    619  CB  MET A 117       3.132  10.337  -2.457  1.00 61.50           C\\nANISOU  619  CB  MET A 117     7283   8115   7968   -518    120    103       C\\nATOM    620  CG  MET A 117       1.975  11.258  -2.770  1.00 64.85           C\\nANISOU  620  CG  MET A 117     7509   8654   8476   -463     28     19       C\\nATOM    621  SD  MET A 117       1.790  12.509  -1.489  1.00 62.59           S\\nANISOU  621  SD  MET A 117     7071   8409   8301   -354     37    -66       S\\nATOM    622  CE  MET A 117       0.518  13.548  -2.206  1.00 56.74           C\\nANISOU  622  CE  MET A 117     6109   7754   7697   -221   -153   -189       C\\nATOM    623  N   CYS A 118       6.449   9.867  -2.434  1.00 70.60           N\\nANISOU  623  N   CYS A 118     8747   9036   9042   -373    183    282       N\\nATOM    624  CA  CYS A 118       7.576   9.023  -2.062  1.00 70.67           C\\nANISOU  624  CA  CYS A 118     8885   8946   9021   -346    211    289       C\\nATOM    625  C   CYS A 118       8.689   9.813  -1.387  1.00 68.27           C\\nANISOU  625  C   CYS A 118     8564   8615   8761   -260    228    351       C\\nATOM    626  O   CYS A 118       9.435   9.249  -0.578  1.00 62.32           O\\nANISOU  626  O   CYS A 118     7898   7774   8009   -239    233    351       O\\nATOM    627  CB  CYS A 118       8.121   8.295  -3.295  1.00 71.86           C\\nANISOU  627  CB  CYS A 118     9091   9112   9101   -295    188    239       C\\nATOM    628  SG  CYS A 118       6.974   7.093  -4.021  1.00 68.74           S\\nANISOU  628  SG  CYS A 118     8755   8698   8664   -398    132    131       S\\nATOM    629  N   THR A 119       8.819  11.105  -1.703  1.00 71.90           N\\nANISOU  629  N   THR A 119     8925   9128   9267   -218    203    409       N\\nATOM    630  CA  THR A 119       9.769  11.947  -0.985  1.00 68.93           C\\nANISOU  630  CA  THR A 119     8523   8711   8956   -165    196    461       C\\nATOM    631  C   THR A 119       9.300  12.212   0.440  1.00 62.52           C\\nANISOU  631  C   THR A 119     7704   7861   8191   -175    201    411       C\\nATOM    632  O   THR A 119      10.125  12.295   1.357  1.00 61.89           O\\nANISOU  632  O   THR A 119     7656   7732   8127   -144    202    417       O\\nATOM    633  CB  THR A 119       9.981  13.271  -1.728  1.00 67.89           C\\nANISOU  633  CB  THR A 119     8314   8606   8874   -156    129    558       C\\nATOM    634  OG1 THR A 119      10.268  13.009  -3.105  1.00 63.88           O\\nANISOU  634  OG1 THR A 119     7808   8202   8260   -182    139    610       O\\nATOM    635  CG2 THR A 119      11.148  14.045  -1.129  1.00 64.40           C\\nANISOU  635  CG2 THR A 119     7848   8113   8507   -132    108    616       C\\nATOM    636  N   ALA A 120       7.987  12.343   0.642  1.00 61.79           N\\nANISOU  636  N   ALA A 120     7547   7824   8105   -218    203    341       N\\nATOM    637  CA  ALA A 120       7.457  12.486   1.992  1.00 59.49           C\\nANISOU  637  CA  ALA A 120     7220   7579   7805   -246    240    258       C\\nATOM    638  C   ALA A 120       7.815  11.283   2.852  1.00 61.28           C\\nANISOU  638  C   ALA A 120     7585   7779   7919   -337    300    286       C\\nATOM    639  O   ALA A 120       8.114  11.433   4.041  1.00 62.06           O\\nANISOU  639  O   ALA A 120     7711   7891   7976   -343    316    271       O\\nATOM    640  CB  ALA A 120       5.943  12.676   1.947  1.00 60.06           C\\nANISOU  640  CB  ALA A 120     7153   7780   7886   -287    251    145       C\\nATOM    641  N   SER A 121       7.784  10.080   2.268  1.00 59.91           N\\nANISOU  641  N   SER A 121     7518   7552   7694   -409    305    325       N\\nATOM    642  CA  SER A 121       8.208   8.889   2.998  1.00 65.17           C\\nANISOU  642  CA  SER A 121     8361   8120   8282   -489    296    378       C\\nATOM    643  C   SER A 121       9.662   9.003   3.431  1.00 68.85           C\\nANISOU  643  C   SER A 121     8900   8486   8775   -361    241    416       C\\nATOM    644  O   SER A 121      10.014   8.643   4.561  1.00 69.48           O\\nANISOU  644  O   SER A 121     9088   8521   8792   -399    214    457       O\\nATOM    645  CB  SER A 121       8.013   7.640   2.137  1.00 61.09           C\\nANISOU  645  CB  SER A 121     7954   7505   7753   -550    254    383       C\\nATOM    646  OG  SER A 121       6.661   7.485   1.747  1.00 71.73           O\\nANISOU  646  OG  SER A 121     9221   8952   9081   -688    290    343       O\\nATOM    647  N   ALA A 122      10.522   9.500   2.544  1.00 66.20           N\\nANISOU  647  N   ALA A 122     8498   8140   8516   -228    219    409       N\\nATOM    648  CA  ALA A 122      11.932   9.632   2.882  1.00 64.09           C\\nANISOU  648  CA  ALA A 122     8247   7817   8288   -115    169    424       C\\nATOM    649  C   ALA A 122      12.144  10.731   3.911  1.00 67.35           C\\nANISOU  649  C   ALA A 122     8599   8264   8729    -99    162    428       C\\nATOM    650  O   ALA A 122      12.870  10.544   4.893  1.00 67.60           O\\nANISOU  650  O   ALA A 122     8699   8245   8739    -68    109    438       O\\nATOM    651  CB  ALA A 122      12.746   9.905   1.621  1.00 62.95           C\\nANISOU  651  CB  ALA A 122     8005   7723   8189    -24    175    411       C\\nATOM    652  N   LEU A 123      11.511  11.886   3.707  1.00 62.65           N\\nANISOU  652  N   LEU A 123     7879   7737   8186   -107    182    403       N\\nATOM    653  CA  LEU A 123      11.661  12.982   4.654  1.00 64.73           C\\nANISOU  653  CA  LEU A 123     8084   8013   8499    -71    145    360       C\\nATOM    654  C   LEU A 123      11.002  12.677   5.993  1.00 68.58           C\\nANISOU  654  C   LEU A 123     8623   8569   8865   -134    179    297       C\\nATOM    655  O   LEU A 123      11.397  13.259   7.008  1.00 65.26           O\\nANISOU  655  O   LEU A 123     8197   8165   8435    -96    140    244       O\\nATOM    656  CB  LEU A 123      11.095  14.271   4.056  1.00 60.03           C\\nANISOU  656  CB  LEU A 123     7361   7429   8020    -42    106    331       C\\nATOM    657  CG  LEU A 123      12.060  15.137   3.236  1.00 62.40           C\\nANISOU  657  CG  LEU A 123     7610   7663   8437    -13     31    421       C\\nATOM    658  CD1 LEU A 123      12.857  14.325   2.223  1.00 59.85           C\\nANISOU  658  CD1 LEU A 123     7308   7374   8057    -33     81    508       C\\nATOM    659  CD2 LEU A 123      11.293  16.248   2.540  1.00 58.42           C\\nANISOU  659  CD2 LEU A 123     7032   7125   8039     -7    -54    431       C\\nATOM    660  N   ASN A 124      10.015  11.778   6.022  1.00 64.20           N\\nANISOU  660  N   ASN A 124     8115   8078   8200   -253    250    303       N\\nATOM    661  CA  ASN A 124       9.452  11.343   7.295  1.00 68.55           C\\nANISOU  661  CA  ASN A 124     8724   8742   8580   -376    301    282       C\\nATOM    662  C   ASN A 124      10.430  10.450   8.047  1.00 72.49           C\\nANISOU  662  C   ASN A 124     9424   9133   8985   -402    229    393       C\\nATOM    663  O   ASN A 124      10.617  10.600   9.260  1.00 78.80           O\\nANISOU  663  O   ASN A 124    10273  10006   9661   -433    215    382       O\\nATOM    664  CB  ASN A 124       8.129  10.616   7.067  1.00 63.03           C\\nANISOU  664  CB  ASN A 124     8004   8152   7791   -549    391    281       C\\nATOM    665  CG  ASN A 124       6.940  11.540   7.141  1.00 59.12           C\\nANISOU  665  CG  ASN A 124     7283   7866   7312   -543    463    113       C\\nATOM    666  OD1 ASN A 124       6.864  12.399   8.016  1.00 58.74           O\\nANISOU  666  OD1 ASN A 124     7141   7941   7236   -481    474    -16       O\\nATOM    667  ND2 ASN A 124       6.000  11.373   6.218  1.00 59.97           N\\nANISOU  667  ND2 ASN A 124     7292   8020   7473   -588    490     83       N\\nATOM    668  N   LEU A 125      11.062   9.508   7.343  1.00 66.29           N\\nANISOU  668  N   LEU A 125     8756   8179   8253   -373    162    480       N\\nATOM    669  CA  LEU A 125      12.084   8.682   7.972  1.00 65.46           C\\nANISOU  669  CA  LEU A 125     8836   7929   8106   -343     35    565       C\\nATOM    670  C   LEU A 125      13.243   9.524   8.477  1.00 65.97           C\\nANISOU  670  C   LEU A 125     8840   7991   8234   -191    -37    522       C\\nATOM    671  O   LEU A 125      13.922   9.139   9.436  1.00 61.15           O\\nANISOU  671  O   LEU A 125     8360   7325   7547   -177   -149    572       O\\nATOM    672  CB  LEU A 125      12.583   7.629   6.988  1.00 62.70           C\\nANISOU  672  CB  LEU A 125     8578   7397   7847   -276    -48    593       C\\nATOM    673  CG  LEU A 125      11.555   6.553   6.663  1.00 64.43           C\\nANISOU  673  CG  LEU A 125     8919   7557   8006   -451    -38    646       C\\nATOM    674  CD1 LEU A 125      12.089   5.633   5.597  1.00 62.96           C\\nANISOU  674  CD1 LEU A 125     8802   7188   7932   -337   -140    608       C\\nATOM    675  CD2 LEU A 125      11.214   5.779   7.920  1.00 61.82           C\\nANISOU  675  CD2 LEU A 125     8799   7183   7505   -650   -100    783       C\\nATOM    676  N   CYS A 126      13.482  10.673   7.849  1.00 67.22           N\\nANISOU  676  N   CYS A 126     8812   8199   8530    -94      0    444       N\\nATOM    677  CA  CYS A 126      14.522  11.568   8.333  1.00 68.85           C\\nANISOU  677  CA  CYS A 126     8945   8402   8814     11    -78    401       C\\nATOM    678  C   CYS A 126      14.084  12.257   9.617  1.00 71.84           C\\nANISOU  678  C   CYS A 126     9323   8885   9086    -30    -78    330       C\\nATOM    679  O   CYS A 126      14.848  12.331  10.588  1.00 74.42           O\\nANISOU  679  O   CYS A 126     9709   9205   9362      8   -177    320       O\\nATOM    680  CB  CYS A 126      14.866  12.592   7.257  1.00 64.79           C\\nANISOU  680  CB  CYS A 126     8252   7891   8474     72    -60    375       C\\nATOM    681  SG  CYS A 126      16.409  13.441   7.561  1.00 69.06           S\\nANISOU  681  SG  CYS A 126     8693   8402   9146    160   -175    353       S\\nATOM    682  N   ALA A 127      12.849  12.762   9.642  1.00 60.58           N\\nANISOU  682  N   ALA A 127     7817   7582   7618    -95     24    250       N\\nATOM    683  CA  ALA A 127      12.322  13.375  10.854  1.00 61.10           C\\nANISOU  683  CA  ALA A 127     7852   7809   7555   -121     44    122       C\\nATOM    684  C   ALA A 127      12.220  12.369  11.990  1.00 65.12           C\\nANISOU  684  C   ALA A 127     8538   8411   7794   -256     52    201       C\\nATOM    685  O   ALA A 127      12.407  12.729  13.158  1.00 65.71           O\\nANISOU  685  O   ALA A 127     8640   8603   7724   -258     16    127       O\\nATOM    686  CB  ALA A 127      10.957  13.996  10.570  1.00 60.25           C\\nANISOU  686  CB  ALA A 127     7585   7843   7462   -141    147    -17       C\\nATOM    687  N   ILE A 128      11.925  11.108  11.673  1.00 64.09           N\\nANISOU  687  N   ILE A 128     8546   8221   7582   -384     77    357       N\\nATOM    688  CA  ILE A 128      11.829  10.083  12.705  1.00 61.38           C\\nANISOU  688  CA  ILE A 128     8417   7924   6982   -558     46    492       C\\nATOM    689  C   ILE A 128      13.184   9.868  13.370  1.00 64.99           C\\nANISOU  689  C   ILE A 128     9025   8241   7426   -455   -148    563       C\\nATOM    690  O   ILE A 128      13.286   9.807  14.600  1.00 69.74           O\\nANISOU  690  O   ILE A 128     9740   8959   7800   -534   -198    591       O\\nATOM    691  CB  ILE A 128      11.271   8.779  12.108  1.00 62.32           C\\nANISOU  691  CB  ILE A 128     8673   7934   7072   -722     61    653       C\\nATOM    692  CG1 ILE A 128       9.772   8.923  11.836  1.00 63.83           C\\nANISOU  692  CG1 ILE A 128     8711   8345   7195   -888    252    582       C\\nATOM    693  CG2 ILE A 128      11.548   7.604  13.028  1.00 64.88           C\\nANISOU  693  CG2 ILE A 128     9290   8172   7190   -886    -69    860       C\\nATOM    694  CD1 ILE A 128       9.120   7.668  11.294  1.00 68.59           C\\nANISOU  694  CD1 ILE A 128     9440   8852   7770  -1092    259    730       C\\nATOM    695  N   SER A 129      14.244   9.756  12.565  1.00 66.20           N\\nANISOU  695  N   SER A 129     9164   8178   7810   -278   -262    578       N\\nATOM    696  CA  SER A 129      15.586   9.611  13.121  1.00 63.02           C\\nANISOU  696  CA  SER A 129     8848   7658   7438   -147   -463    607       C\\nATOM    697  C   SER A 129      15.949  10.799  13.998  1.00 65.47           C\\nANISOU  697  C   SER A 129     9055   8109   7713    -86   -487    474       C\\nATOM    698  O   SER A 129      16.527  10.629  15.078  1.00 65.88           O\\nANISOU  698  O   SER A 129     9234   8177   7619    -82   -631    506       O\\nATOM    699  CB  SER A 129      16.603   9.467  11.995  1.00 65.36           C\\nANISOU  699  CB  SER A 129     9050   7784   7998     39   -538    582       C\\nATOM    700  OG  SER A 129      16.749  10.693  11.302  1.00 65.87           O\\nANISOU  700  OG  SER A 129     8871   7922   8235    114   -445    460       O\\nATOM    701  N   ILE A 130      15.624  12.011  13.546  1.00 64.82           N\\nANISOU  701  N   ILE A 130     8755   8106   7766    -35   -383    319       N\\nATOM    702  CA  ILE A 130      15.959  13.208  14.313  1.00 68.76           C\\nANISOU  702  CA  ILE A 130     9156   8695   8276     36   -439    156       C\\nATOM    703  C   ILE A 130      15.205  13.216  15.636  1.00 70.22           C\\nANISOU  703  C   ILE A 130     9425   9110   8144    -76   -395     92       C\\nATOM    704  O   ILE A 130      15.775  13.502  16.695  1.00 76.17           O\\nANISOU  704  O   ILE A 130    10235   9933   8773    -45   -514     30       O\\nATOM    705  CB  ILE A 130      15.668  14.473  13.488  1.00 69.26           C\\nANISOU  705  CB  ILE A 130     9002   8739   8574    105   -379     19       C\\nATOM    706  CG1 ILE A 130      16.553  14.504  12.241  1.00 65.51           C\\nANISOU  706  CG1 ILE A 130     8440   8094   8355    174   -420    103       C\\nATOM    707  CG2 ILE A 130      15.878  15.716  14.329  1.00 65.28           C\\nANISOU  707  CG2 ILE A 130     8415   8293   8097    175   -469   -180       C\\nATOM    708  CD1 ILE A 130      16.380  15.745  11.402  1.00 62.56           C\\nANISOU  708  CD1 ILE A 130     7895   7673   8203    202   -405     32       C\\nATOM    709  N   ASP A 131      13.909  12.904  15.595  1.00 70.28           N\\nANISOU  709  N   ASP A 131     9426   9280   7998   -221   -219     94       N\\nATOM    710  CA  ASP A 131      13.155  12.749  16.833  1.00 71.28           C\\nANISOU  710  CA  ASP A 131     9617   9702   7763   -378   -141     50       C\\nATOM    711  C   ASP A 131      13.708  11.611  17.677  1.00 75.20           C\\nANISOU  711  C   ASP A 131    10397  10170   8008   -506   -269    283       C\\nATOM    712  O   ASP A 131      13.639  11.660  18.910  1.00 73.14           O\\nANISOU  712  O   ASP A 131    10222  10134   7432   -599   -289    255       O\\nATOM    713  CB  ASP A 131      11.678  12.515  16.525  1.00 70.71           C\\nANISOU  713  CB  ASP A 131     9449   9834   7586   -540     79     22       C\\nATOM    714  CG  ASP A 131      10.820  12.477  17.775  1.00 76.68           C\\nANISOU  714  CG  ASP A 131    10201  10991   7942   -727    206    -66       C\\nATOM    715  OD1 ASP A 131      10.819  13.472  18.528  1.00 78.05           O\\nANISOU  715  OD1 ASP A 131    10254  11363   8039   -619    204   -327       O\\nATOM    716  OD2 ASP A 131      10.140  11.455  18.001  1.00 79.31           O\\nANISOU  716  OD2 ASP A 131    10647  11456   8030   -996    304    118       O\\nATOM    717  N   ARG A 132      14.264  10.581  17.036  1.00 72.55           N\\nANISOU  717  N   ARG A 132    10215   9556   7796   -504   -380    502       N\\nATOM    718  CA  ARG A 132      14.921   9.521  17.791  1.00 74.39           C\\nANISOU  718  CA  ARG A 132    10739   9679   7847   -579   -584    726       C\\nATOM    719  C   ARG A 132      16.221  10.003  18.417  1.00 74.84           C\\nANISOU  719  C   ARG A 132    10811   9673   7954   -388   -804    656       C\\nATOM    720  O   ARG A 132      16.614   9.507  19.479  1.00 74.70           O\\nANISOU  720  O   ARG A 132    11012   9686   7686   -458   -973    778       O\\nATOM    721  CB  ARG A 132      15.175   8.307  16.894  1.00 71.71           C\\nANISOU  721  CB  ARG A 132    10547   9024   7674   -578   -687    923       C\\nATOM    722  CG  ARG A 132      13.976   7.378  16.715  1.00 69.10           C\\nANISOU  722  CG  ARG A 132    10338   8727   7188   -858   -567   1086       C\\nATOM    723  CD  ARG A 132      13.493   6.832  18.055  1.00 75.91           C\\nANISOU  723  CD  ARG A 132    11433   9782   7627  -1155   -591   1269       C\\nATOM    724  NE  ARG A 132      12.518   7.717  18.686  1.00 77.94           N\\nANISOU  724  NE  ARG A 132    11497  10480   7636  -1291   -337   1099       N\\nATOM    725  CZ  ARG A 132      12.271   7.756  19.990  1.00 77.58           C\\nANISOU  725  CZ  ARG A 132    11552  10740   7186  -1484   -317   1141       C\\nATOM    726  NH1 ARG A 132      12.931   6.960  20.822  1.00 76.41           N\\nANISOU  726  NH1 ARG A 132    11728  10477   6827  -1585   -559   1394       N\\nATOM    727  NH2 ARG A 132      11.366   8.602  20.464  1.00 79.78           N\\nANISOU  727  NH2 ARG A 132    11599  11452   7261  -1565    -71    912       N\\nATOM    728  N   TYR A 133      16.902  10.960  17.786  1.00 73.32           N\\nANISOU  728  N   TYR A 133    10393   9395   8070   -171   -822    476       N\\nATOM    729  CA  TYR A 133      18.124  11.492  18.379  1.00 72.55           C\\nANISOU  729  CA  TYR A 133    10271   9257   8037    -13  -1032    389       C\\nATOM    730  C   TYR A 133      17.813  12.311  19.624  1.00 76.41           C\\nANISOU  730  C   TYR A 133    10753  10016   8263    -65  -1020    228       C\\nATOM    731  O   TYR A 133      18.475  12.161  20.658  1.00 82.66           O\\nANISOU  731  O   TYR A 133    11685  10852   8869    -54  -1214    255       O\\nATOM    732  CB  TYR A 133      18.894  12.340  17.365  1.00 65.57           C\\nANISOU  732  CB  TYR A 133     9133   8238   7542    169  -1045    254       C\\nATOM    733  CG  TYR A 133      20.160  12.957  17.931  1.00 69.03           C\\nANISOU  733  CG  TYR A 133     9504   8648   8079    305  -1262    149       C\\nATOM    734  CD1 TYR A 133      21.367  12.268  17.901  1.00 73.59           C\\nANISOU  734  CD1 TYR A 133    10124   9075   8760    424  -1482    232       C\\nATOM    735  CD2 TYR A 133      20.148  14.224  18.502  1.00 67.30           C\\nANISOU  735  CD2 TYR A 133     9162   8546   7862    326  -1271    -61       C\\nATOM    736  CE1 TYR A 133      22.526  12.825  18.419  1.00 73.44           C\\nANISOU  736  CE1 TYR A 133    10011   9052   8839    539  -1690    123       C\\nATOM    737  CE2 TYR A 133      21.303  14.789  19.022  1.00 69.25           C\\nANISOU  737  CE2 TYR A 133     9341   8760   8209    429  -1488   -164       C\\nATOM    738  CZ  TYR A 133      22.488  14.084  18.977  1.00 74.54           C\\nANISOU  738  CZ  TYR A 133    10039   9309   8975    524  -1689    -64       C\\nATOM    739  OH  TYR A 133      23.637  14.640  19.490  1.00 78.51           O\\nANISOU  739  OH  TYR A 133    10443   9800   9586    618  -1914   -178       O\\nATOM    740  N   THR A 134      16.813  13.190  19.544  1.00 70.79           N\\nANISOU  740  N   THR A 134     9871   9496   7530   -102   -814     34       N\\nATOM    741  CA  THR A 134      16.526  14.064  20.674  1.00 74.84           C\\nANISOU  741  CA  THR A 134    10337  10284   7814   -106   -805   -201       C\\nATOM    742  C   THR A 134      16.021  13.276  21.876  1.00 73.81           C\\nANISOU  742  C   THR A 134    10425  10433   7188   -319   -780    -82       C\\nATOM    743  O   THR A 134      16.266  13.672  23.021  1.00 83.45           O\\nANISOU  743  O   THR A 134    11696  11863   8150   -318   -870   -208       O\\nATOM    744  CB  THR A 134      15.517  15.137  20.270  1.00 81.04           C\\nANISOU  744  CB  THR A 134    10877  11199   8715    -61   -617   -471       C\\nATOM    745  OG1 THR A 134      14.231  14.541  20.084  1.00 85.24           O\\nANISOU  745  OG1 THR A 134    11407  11920   9060   -236   -387   -405       O\\nATOM    746  CG2 THR A 134      15.945  15.803  18.969  1.00 80.96           C\\nANISOU  746  CG2 THR A 134    10697  10893   9169     91   -653   -505       C\\nATOM    747  N   ALA A 135      15.341  12.151  21.642  1.00 74.49           N\\nANISOU  747  N   ALA A 135    10655  10530   7120   -527   -674    172       N\\nATOM    748  CA  ALA A 135      14.858  11.340  22.756  1.00 76.81           C\\nANISOU  748  CA  ALA A 135    11182  11087   6918   -800   -658    350       C\\nATOM    749  C   ALA A 135      16.008  10.654  23.480  1.00 76.81           C\\nANISOU  749  C   ALA A 135    11471  10921   6791   -787   -978    571       C\\nATOM    750  O   ALA A 135      15.979  10.505  24.707  1.00 82.26           O\\nANISOU  750  O   ALA A 135    12330  11871   7053   -935  -1044    623       O\\nATOM    751  CB  ALA A 135      13.849  10.307  22.259  1.00 69.76           C\\nANISOU  751  CB  ALA A 135    10373  10203   5930  -1063   -492    588       C\\nATOM    752  N   VAL A 136      17.029  10.233  22.739  1.00 76.95           N\\nANISOU  752  N   VAL A 136    11539  10534   7164   -603  -1189    688       N\\nATOM    753  CA  VAL A 136      18.154   9.535  23.350  1.00 82.31           C\\nANISOU  753  CA  VAL A 136    12472  11024   7777   -545  -1537    878       C\\nATOM    754  C   VAL A 136      19.136  10.524  23.967  1.00 82.04           C\\nANISOU  754  C   VAL A 136    12325  11053   7795   -336  -1708    644       C\\nATOM    755  O   VAL A 136      19.554  10.367  25.120  1.00 81.48           O\\nANISOU  755  O   VAL A 136    12446  11103   7411   -382  -1911    704       O\\nATOM    756  CB  VAL A 136      18.839   8.630  22.309  1.00 77.31           C\\nANISOU  756  CB  VAL A 136    11904   9961   7508   -406  -1706   1045       C\\nATOM    757  CG1 VAL A 136      20.246   8.278  22.755  1.00 77.43           C\\nANISOU  757  CG1 VAL A 136    12049   9764   7606   -210  -2095   1106       C\\nATOM    758  CG2 VAL A 136      18.017   7.366  22.083  1.00 72.64           C\\nANISOU  758  CG2 VAL A 136    11557   9266   6777   -655  -1667   1340       C\\nATOM    759  N   ALA A 137      19.501  11.568  23.224  1.00 77.79           N\\nANISOU  759  N   ALA A 137    11484  10437   7637   -128  -1644    384       N\\nATOM    760  CA  ALA A 137      20.609  12.434  23.603  1.00 80.22           C\\nANISOU  760  CA  ALA A 137    11669  10715   8097     69  -1852    182       C\\nATOM    761  C   ALA A 137      20.209  13.605  24.491  1.00 87.12           C\\nANISOU  761  C   ALA A 137    12440  11898   8765     54  -1780   -115       C\\nATOM    762  O   ALA A 137      21.094  14.243  25.073  1.00 87.55           O\\nANISOU  762  O   ALA A 137    12447  11955   8861    179  -1994   -277       O\\nATOM    763  CB  ALA A 137      21.304  12.975  22.349  1.00 74.40           C\\nANISOU  763  CB  ALA A 137    10663   9730   7877    260  -1849     74       C\\nATOM    764  N   MET A 138      18.922  13.910  24.616  1.00 85.65           N\\nANISOU  764  N   MET A 138    12198  11978   8368    -81  -1504   -224       N\\nATOM    765  CA  MET A 138      18.517  15.099  25.348  1.00 91.36           C\\nANISOU  765  CA  MET A 138    12776  12989   8948    -40  -1439   -587       C\\nATOM    766  C   MET A 138      17.450  14.760  26.377  1.00 93.65           C\\nANISOU  766  C   MET A 138    13184  13730   8670   -264  -1268   -595       C\\nATOM    767  O   MET A 138      16.648  13.844  26.169  1.00 90.32           O\\nANISOU  767  O   MET A 138    12865  13389   8064   -478  -1095   -353       O\\nATOM    768  CB  MET A 138      18.001  16.181  24.387  1.00 94.18           C\\nANISOU  768  CB  MET A 138    12839  13259   9687     83  -1276   -847       C\\nATOM    769  CG  MET A 138      19.095  16.769  23.500  1.00 98.65           C\\nANISOU  769  CG  MET A 138    13264  13452  10767    263  -1446   -874       C\\nATOM    770  SD  MET A 138      18.521  18.077  22.402  1.00105.80           S\\nANISOU  770  SD  MET A 138    13881  14215  12101    371  -1319  -1121       S\\nATOM    771  CE  MET A 138      20.031  18.481  21.533  1.00105.56           C\\nANISOU  771  CE  MET A 138    13744  13805  12559    477  -1542  -1039       C\\nATOM    772  N   PRO A 139      17.425  15.482  27.515  1.00104.46           N\\nANISOU  772  N   PRO A 139    14532  15425   9735   -241  -1315   -880       N\\nATOM    773  CA  PRO A 139      16.509  15.224  28.635  1.00105.59           C\\nANISOU  773  CA  PRO A 139    14765  16095   9259   -469  -1152   -923       C\\nATOM    774  C   PRO A 139      15.042  15.103  28.221  1.00104.65           C\\nANISOU  774  C   PRO A 139    14492  16238   9033   -630   -782   -969       C\\nATOM    775  O   PRO A 139      14.317  16.097  28.261  1.00106.02           O\\nANISOU  775  O   PRO A 139    14394  16653   9234   -519   -617  -1385       O\\nATOM    776  CB  PRO A 139      16.714  16.446  29.535  1.00103.32           C\\nANISOU  776  CB  PRO A 139    14347  16058   8852   -301  -1242  -1390       C\\nATOM    777  CG  PRO A 139      18.112  16.868  29.263  1.00100.62           C\\nANISOU  777  CG  PRO A 139    14009  15289   8934    -72  -1575  -1406       C\\nATOM    778  CD  PRO A 139      18.340  16.603  27.805  1.00 97.12           C\\nANISOU  778  CD  PRO A 139    13483  14389   9030     -4  -1545  -1193       C\\nATOM    779  N   THR A 144       8.716  17.350  27.929  1.00103.31           N\\nANISOU  779  N   THR A 144    12885  17966   8400   -718    631  -2535       N\\nATOM    780  CA  THR A 144       7.590  18.233  28.208  1.00111.55           C\\nANISOU  780  CA  THR A 144    13533  19499   9351   -578    832  -3111       C\\nATOM    781  C   THR A 144       6.396  17.895  27.318  1.00111.78           C\\nANISOU  781  C   THR A 144    13322  19627   9521   -685   1084  -3075       C\\nATOM    782  O   THR A 144       6.556  17.666  26.122  1.00115.16           O\\nANISOU  782  O   THR A 144    13802  19541  10411   -631   1006  -2812       O\\nATOM    783  CB  THR A 144       7.971  19.712  28.006  1.00112.47           C\\nANISOU  783  CB  THR A 144    13477  19327   9931   -104    597  -3618       C\\nATOM    784  N   ARG A 145       5.198  17.868  27.907  1.00112.87           N\\nANISOU  784  N   ARG A 145    13181  20279   9425   -824   1334  -3251       N\\nATOM    785  CA  ARG A 145       4.002  17.509  27.151  1.00114.09           C\\nANISOU  785  CA  ARG A 145    13078  20551   9719   -950   1551  -3212       C\\nATOM    786  C   ARG A 145       3.581  18.596  26.170  1.00118.73           C\\nANISOU  786  C   ARG A 145    13352  20930  10830   -531   1477  -3651       C\\nATOM    787  O   ARG A 145       2.846  18.305  25.221  1.00119.01           O\\nANISOU  787  O   ARG A 145    13234  20913  11072   -582   1585  -3578       O\\nATOM    788  CB  ARG A 145       2.846  17.198  28.104  1.00118.50           C\\nANISOU  788  CB  ARG A 145    13396  21689   9937  -1221   1786  -3270       C\\nATOM    789  N   TYR A 146       4.024  19.834  26.375  1.00121.59           N\\nANISOU  789  N   TYR A 146    13630  21133  11434   -123   1259  -4089       N\\nATOM    790  CA  TYR A 146       3.700  20.948  25.491  1.00117.64           C\\nANISOU  790  CA  TYR A 146    12880  20335  11482    295   1102  -4485       C\\nATOM    791  C   TYR A 146       4.829  21.280  24.526  1.00108.31           C\\nANISOU  791  C   TYR A 146    11951  18428  10772    498    805  -4303       C\\nATOM    792  O   TYR A 146       4.573  21.530  23.344  1.00100.71           O\\nANISOU  792  O   TYR A 146    10911  17078  10275    638    718  -4241       O\\nATOM    793  CB  TYR A 146       3.345  22.185  26.325  1.00124.08           C\\nANISOU  793  CB  TYR A 146    13429  21323  12394    606    974  -5030       C\\nATOM    794  CG  TYR A 146       3.156  23.462  25.533  1.00125.41           C\\nANISOU  794  CG  TYR A 146    13400  21084  13165   1062    702  -5422       C\\nATOM    795  CD1 TYR A 146       1.920  23.794  24.993  1.00128.22           C\\nANISOU  795  CD1 TYR A 146    13405  21556  13758   1181    740  -5641       C\\nATOM    796  CD2 TYR A 146       4.211  24.347  25.345  1.00125.84           C\\nANISOU  796  CD2 TYR A 146    13634  20614  13563   1355    362  -5554       C\\nATOM    797  CE1 TYR A 146       1.746  24.966  24.276  1.00131.82           C\\nANISOU  797  CE1 TYR A 146    13721  21595  14769   1588    432  -5955       C\\nATOM    798  CE2 TYR A 146       4.047  25.515  24.631  1.00128.03           C\\nANISOU  798  CE2 TYR A 146    13776  20456  14413   1732     64  -5846       C\\nATOM    799  CZ  TYR A 146       2.815  25.821  24.099  1.00132.64           C\\nANISOU  799  CZ  TYR A 146    14037  21147  15214   1852     92  -6034       C\\nATOM    800  OH  TYR A 146       2.656  26.988  23.388  1.00136.93           O\\nANISOU  800  OH  TYR A 146    14484  21222  16320   2213   -261  -6277       O\\nATOM    801  N   SER A 147       6.076  21.287  25.005  1.00108.97           N\\nANISOU  801  N   SER A 147    12336  18257  10810    490    611  -4125       N\\nATOM    802  CA  SER A 147       7.206  21.602  24.138  1.00104.01           C\\nANISOU  802  CA  SER A 147    11926  16901  10691    633    308  -3860       C\\nATOM    803  C   SER A 147       7.407  20.541  23.065  1.00103.85           C\\nANISOU  803  C   SER A 147    12083  16559  10818    407    370  -3277       C\\nATOM    804  O   SER A 147       7.842  20.861  21.953  1.00 99.45           O\\nANISOU  804  O   SER A 147    11570  15480  10738    539    199  -3123       O\\nATOM    805  CB  SER A 147       8.481  21.758  24.972  1.00101.67           C\\nANISOU  805  CB  SER A 147    11877  16479  10273    647     99  -3814       C\\nATOM    806  N   SER A 148       7.103  19.279  23.375  1.00100.58           N\\nANISOU  806  N   SER A 148    11778  16447   9991     56    598  -2950       N\\nATOM    807  CA  SER A 148       7.325  18.214  22.404  1.00 97.98           C\\nANISOU  807  CA  SER A 148    11636  15794   9798   -147    625  -2427       C\\nATOM    808  C   SER A 148       6.273  18.239  21.303  1.00 88.88           C\\nANISOU  808  C   SER A 148    10254  14611   8905   -117    745  -2472       C\\nATOM    809  O   SER A 148       6.602  18.071  20.125  1.00 80.56           O\\nANISOU  809  O   SER A 148     9283  13109   8218    -74    646  -2217       O\\nATOM    810  CB  SER A 148       7.339  16.858  23.106  1.00103.00           C\\nANISOU  810  CB  SER A 148    12497  16702   9935   -541    771  -2055       C\\nATOM    811  OG  SER A 148       6.089  16.599  23.719  1.00106.17           O\\nANISOU  811  OG  SER A 148    12692  17721   9926   -754   1057  -2228       O\\nATOM    812  N   LYS A 149       5.003  18.446  21.667  1.00 92.05           N\\nANISOU  812  N   LYS A 149    10349  15519   9108   -139    955  -2812       N\\nATOM    813  CA  LYS A 149       3.946  18.506  20.661  1.00 84.26           C\\nANISOU  813  CA  LYS A 149     9110  14536   8369    -93   1046  -2895       C\\nATOM    814  C   LYS A 149       4.192  19.638  19.673  1.00 88.93           C\\nANISOU  814  C   LYS A 149     9627  14634   9529    289    781  -3067       C\\nATOM    815  O   LYS A 149       3.943  19.488  18.470  1.00 93.01           O\\nANISOU  815  O   LYS A 149    10125  14862  10350    308    742  -2887       O\\nATOM    816  CB  LYS A 149       2.585  18.670  21.333  1.00 79.97           C\\nANISOU  816  CB  LYS A 149     8188  14678   7518   -142   1299  -3315       C\\nATOM    817  N   ARG A 150       4.688  20.778  20.160  1.00 87.49           N\\nANISOU  817  N   ARG A 150     9416  14340   9487    578    575  -3405       N\\nATOM    818  CA  ARG A 150       5.060  21.865  19.261  1.00 81.69           C\\nANISOU  818  CA  ARG A 150     8671  13071   9295    893    273  -3505       C\\nATOM    819  C   ARG A 150       6.223  21.474  18.359  1.00 80.21           C\\nANISOU  819  C   ARG A 150     8786  12341   9349    799    130  -2998       C\\nATOM    820  O   ARG A 150       6.317  21.964  17.230  1.00 82.46           O\\nANISOU  820  O   ARG A 150     9071  12222  10039    928    -38  -2909       O\\nATOM    821  CB  ARG A 150       5.411  23.117  20.063  1.00 80.33           C\\nANISOU  821  CB  ARG A 150     8437  12868   9215   1187     52  -3965       C\\nATOM    822  N   ARG A 151       7.111  20.595  18.831  1.00 78.36           N\\nANISOU  822  N   ARG A 151     8802  12110   8862    578    185  -2672       N\\nATOM    823  CA  ARG A 151       8.234  20.166  18.003  1.00 72.71           C\\nANISOU  823  CA  ARG A 151     8328  10937   8361    507     62  -2239       C\\nATOM    824  C   ARG A 151       7.780  19.202  16.916  1.00 79.91           C\\nANISOU  824  C   ARG A 151     9266  11777   9319    342    198  -1915       C\\nATOM    825  O   ARG A 151       8.310  19.226  15.799  1.00 80.42           O\\nANISOU  825  O   ARG A 151     9410  11464   9683    376     87  -1687       O\\nATOM    826  CB  ARG A 151       9.319  19.528  18.870  1.00 74.01           C\\nANISOU  826  CB  ARG A 151     8732  11123   8264    367     34  -2034       C\\nATOM    827  CG  ARG A 151      10.576  19.134  18.110  1.00 82.30           C\\nANISOU  827  CG  ARG A 151     9986  11745   9540    333   -108  -1658       C\\nATOM    828  CD  ARG A 151      11.637  18.577  19.045  1.00 87.06           C\\nANISOU  828  CD  ARG A 151    10798  12374   9905    242   -184  -1509       C\\nATOM    829  NE  ARG A 151      11.097  17.537  19.917  1.00 91.56           N\\nANISOU  829  NE  ARG A 151    11463  13317  10010     18     -7  -1413       N\\nATOM    830  CZ  ARG A 151      11.047  16.249  19.600  1.00 88.57           C\\nANISOU  830  CZ  ARG A 151    11241  12910   9500   -194     83  -1059       C\\nATOM    831  NH1 ARG A 151      10.538  15.370  20.453  1.00 83.32           N\\nANISOU  831  NH1 ARG A 151    10680  12574   8402   -440    216   -953       N\\nATOM    832  NH2 ARG A 151      11.506  15.837  18.428  1.00 87.56           N\\nANISOU  832  NH2 ARG A 151    11174  12429   9667   -175     27   -816       N\\nATOM    833  N   VAL A 152       6.797  18.350  17.218  1.00 81.56           N\\nANISOU  833  N   VAL A 152     9402  12365   9221    140    437  -1897       N\\nATOM    834  CA  VAL A 152       6.288  17.429  16.204  1.00 81.36           C\\nANISOU  834  CA  VAL A 152     9394  12272   9245    -25    549  -1623       C\\nATOM    835  C   VAL A 152       5.564  18.196  15.104  1.00 80.65           C\\nANISOU  835  C   VAL A 152     9093  12045   9504    168    481  -1785       C\\nATOM    836  O   VAL A 152       5.709  17.888  13.915  1.00 78.73           O\\nANISOU  836  O   VAL A 152     8921  11517   9474    149    431  -1543       O\\nATOM    837  CB  VAL A 152       5.377  16.364  16.843  1.00 80.98           C\\nANISOU  837  CB  VAL A 152     9312  12669   8787   -333    803  -1562       C\\nATOM    838  CG1 VAL A 152       5.106  15.241  15.863  1.00 82.24           C\\nANISOU  838  CG1 VAL A 152     9570  12682   8997   -541    871  -1224       C\\nATOM    839  CG2 VAL A 152       6.004  15.810  18.104  1.00 83.35           C\\nANISOU  839  CG2 VAL A 152     9819  13145   8703   -511    831  -1443       C\\nATOM    840  N   THR A 153       4.781  19.211  15.482  1.00 84.22           N\\nANISOU  840  N   THR A 153     9285  12700  10015    371    455  -2213       N\\nATOM    841  CA  THR A 153       4.057  20.004  14.492  1.00 78.54           C\\nANISOU  841  CA  THR A 153     8369  11830   9642    587    332  -2387       C\\nATOM    842  C   THR A 153       5.011  20.696  13.525  1.00 75.61           C\\nANISOU  842  C   THR A 153     8160  10910   9657    737     57  -2208       C\\nATOM    843  O   THR A 153       4.738  20.779  12.322  1.00 76.21           O\\nANISOU  843  O   THR A 153     8221  10766   9967    773    -25  -2073       O\\nATOM    844  CB  THR A 153       3.168  21.031  15.195  1.00 80.46           C\\nANISOU  844  CB  THR A 153     8306  12365   9901    832    300  -2933       C\\nATOM    845  OG1 THR A 153       2.144  20.354  15.937  1.00 82.11           O\\nANISOU  845  OG1 THR A 153     8305  13162   9733    652    595  -3096       O\\nATOM    846  CG2 THR A 153       2.527  21.976  14.186  1.00 77.79           C\\nANISOU  846  CG2 THR A 153     7796  11785   9977   1109     80  -3121       C\\nATOM    847  N   VAL A 154       6.141  21.193  14.030  1.00 73.65           N\\nANISOU  847  N   VAL A 154     8065  10459   9460    799    -90  -2194       N\\nATOM    848  CA  VAL A 154       7.112  21.843  13.156  1.00 71.40           C\\nANISOU  848  CA  VAL A 154     7922   9692   9516    880   -337  -2000       C\\nATOM    849  C   VAL A 154       7.787  20.821  12.246  1.00 67.73           C\\nANISOU  849  C   VAL A 154     7638   9069   9028    675   -255  -1548       C\\nATOM    850  O   VAL A 154       8.007  21.079  11.057  1.00 61.81           O\\nANISOU  850  O   VAL A 154     6927   8041   8515    690   -370  -1361       O\\nATOM    851  CB  VAL A 154       8.137  22.627  13.993  1.00 65.37           C\\nANISOU  851  CB  VAL A 154     7244   8781   8811    974   -518  -2127       C\\nATOM    852  CG1 VAL A 154       9.256  23.154  13.108  1.00 56.93           C\\nANISOU  852  CG1 VAL A 154     6321   7254   8055    968   -742  -1864       C\\nATOM    853  CG2 VAL A 154       7.453  23.767  14.722  1.00 60.75           C\\nANISOU  853  CG2 VAL A 154     6475   8294   8312   1228   -654  -2627       C\\nATOM    854  N   MET A 155       8.122  19.645  12.784  1.00 69.04           N\\nANISOU  854  N   MET A 155     7921   9413   8899    483    -75  -1374       N\\nATOM    855  CA  MET A 155       8.784  18.630  11.972  1.00 68.64           C\\nANISOU  855  CA  MET A 155     8035   9207   8837    329    -24  -1003       C\\nATOM    856  C   MET A 155       7.875  18.134  10.856  1.00 64.55           C\\nANISOU  856  C   MET A 155     7452   8706   8368    269     63   -905       C\\nATOM    857  O   MET A 155       8.316  17.979   9.712  1.00 59.62           O\\nANISOU  857  O   MET A 155     6898   7863   7894    252      8   -690       O\\nATOM    858  CB  MET A 155       9.241  17.467  12.851  1.00 72.37           C\\nANISOU  858  CB  MET A 155     8663   9833   9001    158     94   -859       C\\nATOM    859  CG  MET A 155      10.407  17.803  13.768  1.00 80.64           C\\nANISOU  859  CG  MET A 155     9815  10814  10011    208    -29   -884       C\\nATOM    860  SD  MET A 155      11.031  16.373  14.674  1.00 89.65           S\\nANISOU  860  SD  MET A 155    11184  12069  10810     19     37   -657       S\\nATOM    861  CE  MET A 155      12.405  17.110  15.553  1.00 99.07           C\\nANISOU  861  CE  MET A 155    12443  13153  12047    140   -171   -742       C\\nATOM    862  N   ILE A 156       6.602  17.886  11.166  1.00 67.34           N\\nANISOU  862  N   ILE A 156     7652   9352   8582    227    200  -1075       N\\nATOM    863  CA  ILE A 156       5.685  17.372  10.156  1.00 68.91           C\\nANISOU  863  CA  ILE A 156     7773   9590   8821    157    271  -1001       C\\nATOM    864  C   ILE A 156       5.469  18.403   9.059  1.00 69.08           C\\nANISOU  864  C   ILE A 156     7705   9384   9158    345     81  -1053       C\\nATOM    865  O   ILE A 156       5.484  18.072   7.867  1.00 70.31           O\\nANISOU  865  O   ILE A 156     7916   9392   9407    300     52   -852       O\\nATOM    866  CB  ILE A 156       4.357  16.945  10.806  1.00 70.36           C\\nANISOU  866  CB  ILE A 156     7765  10184   8786     48    458  -1197       C\\nATOM    867  CG1 ILE A 156       4.590  15.773  11.761  1.00 67.02           C\\nANISOU  867  CG1 ILE A 156     7488   9956   8020   -215    628  -1044       C\\nATOM    868  CG2 ILE A 156       3.332  16.571   9.742  1.00 64.85           C\\nANISOU  868  CG2 ILE A 156     6940   9528   8171     -3    496  -1169       C\\nATOM    869  CD1 ILE A 156       3.333  15.249  12.401  1.00 60.59           C\\nANISOU  869  CD1 ILE A 156     6493   9587   6942   -411    838  -1180       C\\nATOM    870  N   SER A 157       5.271  19.668   9.439  1.00 67.59           N\\nANISOU  870  N   SER A 157     7393   9155   9133    558    -76  -1325       N\\nATOM    871  CA  SER A 157       5.081  20.719   8.446  1.00 66.91           C\\nANISOU  871  CA  SER A 157     7261   8799   9364    734   -321  -1352       C\\nATOM    872  C   SER A 157       6.261  20.789   7.488  1.00 65.20           C\\nANISOU  872  C   SER A 157     7252   8247   9275    664   -437  -1006       C\\nATOM    873  O   SER A 157       6.079  20.905   6.271  1.00 70.97           O\\nANISOU  873  O   SER A 157     8005   8831  10130    658   -531   -845       O\\nATOM    874  CB  SER A 157       4.876  22.064   9.138  1.00 53.19           C\\nANISOU  874  CB  SER A 157     5403   7001   7805    983   -525  -1706       C\\nATOM    875  OG  SER A 157       3.770  22.013  10.019  1.00 59.25           O\\nANISOU  875  OG  SER A 157     5930   8154   8428   1059   -395  -2076       O\\nATOM    876  N   ILE A 158       7.481  20.701   8.019  1.00 63.38           N\\nANISOU  876  N   ILE A 158     7159   7930   8993    600   -428   -895       N\\nATOM    877  CA  ILE A 158       8.662  20.757   7.168  1.00 62.29           C\\nANISOU  877  CA  ILE A 158     7167   7544   8955    516   -512   -595       C\\nATOM    878  C   ILE A 158       8.684  19.577   6.207  1.00 66.42           C\\nANISOU  878  C   ILE A 158     7754   8134   9350    369   -356   -352       C\\nATOM    879  O   ILE A 158       9.069  19.717   5.042  1.00 76.92           O\\nANISOU  879  O   ILE A 158     9134   9324  10767    323   -426   -148       O\\nATOM    880  CB  ILE A 158       9.935  20.815   8.030  1.00 62.52           C\\nANISOU  880  CB  ILE A 158     7286   7519   8948    483   -529   -568       C\\nATOM    881  CG1 ILE A 158       9.969  22.114   8.833  1.00 61.54           C\\nANISOU  881  CG1 ILE A 158     7112   7280   8990    635   -734   -823       C\\nATOM    882  CG2 ILE A 158      11.177  20.683   7.165  1.00 56.51           C\\nANISOU  882  CG2 ILE A 158     6625   6594   8253    369   -564   -273       C\\nATOM    883  CD1 ILE A 158      11.102  22.178   9.819  1.00 68.44           C\\nANISOU  883  CD1 ILE A 158     8055   8136   9811    610   -764   -846       C\\nATOM    884  N   VAL A 159       8.260  18.399   6.670  1.00 61.58           N\\nANISOU  884  N   VAL A 159     7145   7737   8515    280   -157   -371       N\\nATOM    885  CA  VAL A 159       8.270  17.217   5.808  1.00 61.95           C\\nANISOU  885  CA  VAL A 159     7267   7816   8456    152    -40   -177       C\\nATOM    886  C   VAL A 159       7.403  17.448   4.578  1.00 58.47           C\\nANISOU  886  C   VAL A 159     6754   7353   8111    173    -97   -152       C\\nATOM    887  O   VAL A 159       7.847  17.270   3.437  1.00 64.62           O\\nANISOU  887  O   VAL A 159     7599   8038   8915    129   -128     32       O\\nATOM    888  CB  VAL A 159       7.811  15.973   6.589  1.00 61.71           C\\nANISOU  888  CB  VAL A 159     7270   7984   8194     28    136   -202       C\\nATOM    889  CG1 VAL A 159       7.571  14.812   5.641  1.00 58.85           C\\nANISOU  889  CG1 VAL A 159     6974   7622   7763    -90    212    -53       C\\nATOM    890  CG2 VAL A 159       8.840  15.593   7.634  1.00 64.69           C\\nANISOU  890  CG2 VAL A 159     7772   8351   8457     -6    154   -157       C\\nATOM    891  N   TRP A 160       6.156  17.865   4.792  1.00 55.67           N\\nANISOU  891  N   TRP A 160     6244   7112   7797    249   -122   -357       N\\nATOM    892  CA  TRP A 160       5.209  17.964   3.688  1.00 61.87           C\\nANISOU  892  CA  TRP A 160     6946   7902   8658    275   -191   -352       C\\nATOM    893  C   TRP A 160       5.414  19.222   2.854  1.00 68.14           C\\nANISOU  893  C   TRP A 160     7758   8458   9675    394   -447   -287       C\\nATOM    894  O   TRP A 160       5.155  19.201   1.645  1.00 72.46           O\\nANISOU  894  O   TRP A 160     8331   8951  10250    369   -527   -148       O\\nATOM    895  CB  TRP A 160       3.778  17.893   4.226  1.00 54.20           C\\nANISOU  895  CB  TRP A 160     5762   7176   7654    313   -130   -618       C\\nATOM    896  CG  TRP A 160       3.447  16.528   4.729  1.00 59.47           C\\nANISOU  896  CG  TRP A 160     6436   8074   8087    111    106   -599       C\\nATOM    897  CD1 TRP A 160       3.428  16.111   6.027  1.00 64.43           C\\nANISOU  897  CD1 TRP A 160     7047   8894   8538     21    258   -694       C\\nATOM    898  CD2 TRP A 160       3.129  15.380   3.933  1.00 65.48           C\\nANISOU  898  CD2 TRP A 160     7253   8873   8755    -53    190   -456       C\\nATOM    899  NE1 TRP A 160       3.105  14.776   6.089  1.00 64.83           N\\nANISOU  899  NE1 TRP A 160     7153   9080   8400   -211    420   -586       N\\nATOM    900  CE2 TRP A 160       2.917  14.305   4.817  1.00 67.13           C\\nANISOU  900  CE2 TRP A 160     7487   9263   8758   -251    374   -455       C\\nATOM    901  CE3 TRP A 160       2.997  15.161   2.558  1.00 66.76           C\\nANISOU  901  CE3 TRP A 160     7455   8935   8975    -62    110   -331       C\\nATOM    902  CZ2 TRP A 160       2.575  13.030   4.371  1.00 70.04           C\\nANISOU  902  CZ2 TRP A 160     7926   9666   9019   -454    457   -337       C\\nATOM    903  CZ3 TRP A 160       2.659  13.895   2.117  1.00 69.12           C\\nANISOU  903  CZ3 TRP A 160     7807   9302   9154   -239    209   -252       C\\nATOM    904  CH2 TRP A 160       2.451  12.846   3.021  1.00 68.25           C\\nANISOU  904  CH2 TRP A 160     7727   9325   8880   -431    370   -257       C\\nATOM    905  N   VAL A 161       5.874  20.317   3.463  1.00 67.95           N\\nANISOU  905  N   VAL A 161     7737   8280   9802    507   -599   -373       N\\nATOM    906  CA  VAL A 161       6.140  21.520   2.680  1.00 69.19           C\\nANISOU  906  CA  VAL A 161     7952   8155  10182    576   -883   -262       C\\nATOM    907  C   VAL A 161       7.379  21.323   1.823  1.00 65.64           C\\nANISOU  907  C   VAL A 161     7665   7597   9678    402   -867     76       C\\nATOM    908  O   VAL A 161       7.447  21.799   0.684  1.00 71.00           O\\nANISOU  908  O   VAL A 161     8411   8144  10420    354  -1023    278       O\\nATOM    909  CB  VAL A 161       6.273  22.747   3.599  1.00 68.92           C\\nANISOU  909  CB  VAL A 161     7883   7953  10351    740  -1087   -473       C\\nATOM    910  CG1 VAL A 161       6.754  23.958   2.810  1.00 55.10           C\\nANISOU  910  CG1 VAL A 161     6251   5845   8841    751  -1414   -291       C\\nATOM    911  CG2 VAL A 161       4.941  23.041   4.271  1.00 68.37           C\\nANISOU  911  CG2 VAL A 161     7604   8033  10340    947  -1123   -858       C\\nATOM    912  N   LEU A 162       8.370  20.607   2.346  1.00 57.34           N\\nANISOU  912  N   LEU A 162     6669   6627   8492    302   -683    137       N\\nATOM    913  CA  LEU A 162       9.567  20.343   1.562  1.00 62.34           C\\nANISOU  913  CA  LEU A 162     7399   7226   9060    152   -640    403       C\\nATOM    914  C   LEU A 162       9.274  19.375   0.424  1.00 64.44           C\\nANISOU  914  C   LEU A 162     7686   7633   9165     68   -521    527       C\\nATOM    915  O   LEU A 162       9.756  19.565  -0.698  1.00 73.70           O\\nANISOU  915  O   LEU A 162     8910   8787  10307    -32   -568    735       O\\nATOM    916  CB  LEU A 162      10.668  19.803   2.467  1.00 66.33           C\\nANISOU  916  CB  LEU A 162     7929   7786   9485    111   -507    389       C\\nATOM    917  CG  LEU A 162      12.083  19.741   1.909  1.00 71.44           C\\nANISOU  917  CG  LEU A 162     8616   8419  10108    -16   -484    596       C\\nATOM    918  CD1 LEU A 162      12.409  21.020   1.165  1.00 63.78           C\\nANISOU  918  CD1 LEU A 162     7665   7275   9293    -96   -691    765       C\\nATOM    919  CD2 LEU A 162      13.044  19.530   3.061  1.00 75.47           C\\nANISOU  919  CD2 LEU A 162     9125   8941  10610      0   -439    519       C\\nATOM    920  N   SER A 163       8.481  18.334   0.691  1.00 62.39           N\\nANISOU  920  N   SER A 163     7390   7531   8786     86   -371    399       N\\nATOM    921  CA  SER A 163       8.099  17.410  -0.371  1.00 64.81           C\\nANISOU  921  CA  SER A 163     7718   7951   8957     15   -289    475       C\\nATOM    922  C   SER A 163       7.384  18.143  -1.499  1.00 65.90           C\\nANISOU  922  C   SER A 163     7840   8039   9160     33   -467    552       C\\nATOM    923  O   SER A 163       7.634  17.874  -2.680  1.00 71.94           O\\nANISOU  923  O   SER A 163     8662   8855   9817    -51   -466    710       O\\nATOM    924  CB  SER A 163       7.213  16.302   0.193  1.00 64.78           C\\nANISOU  924  CB  SER A 163     7674   8087   8852      4   -146    321       C\\nATOM    925  OG  SER A 163       7.785  15.740   1.357  1.00 61.15           O\\nANISOU  925  OG  SER A 163     7254   7650   8329    -18    -31    269       O\\nATOM    926  N   PHE A 164       6.497  19.078  -1.153  1.00 60.59           N\\nANISOU  926  N   PHE A 164     7089   7277   8655    156   -639    427       N\\nATOM    927  CA  PHE A 164       5.825  19.887  -2.164  1.00 61.72           C\\nANISOU  927  CA  PHE A 164     7234   7322   8893    201   -880    505       C\\nATOM    928  C   PHE A 164       6.833  20.691  -2.972  1.00 65.16           C\\nANISOU  928  C   PHE A 164     7806   7601   9350     94  -1027    793       C\\nATOM    929  O   PHE A 164       6.879  20.597  -4.203  1.00 65.92           O\\nANISOU  929  O   PHE A 164     7974   7746   9327    -10  -1074    992       O\\nATOM    930  CB  PHE A 164       4.803  20.813  -1.496  1.00 57.42           C\\nANISOU  930  CB  PHE A 164     6564   6683   8568    400  -1076    267       C\\nATOM    931  CG  PHE A 164       4.135  21.779  -2.443  1.00 61.42           C\\nANISOU  931  CG  PHE A 164     7089   7023   9226    488  -1405    340       C\\nATOM    932  CD1 PHE A 164       3.067  21.374  -3.232  1.00 63.79           C\\nANISOU  932  CD1 PHE A 164     7317   7446   9476    519  -1453    302       C\\nATOM    933  CD2 PHE A 164       4.563  23.097  -2.528  1.00 60.79           C\\nANISOU  933  CD2 PHE A 164     7109   6640   9350    534  -1703    451       C\\nATOM    934  CE1 PHE A 164       2.450  22.259  -4.099  1.00 64.22           C\\nANISOU  934  CE1 PHE A 164     7400   7336   9667    615  -1799    378       C\\nATOM    935  CE2 PHE A 164       3.946  23.988  -3.393  1.00 65.28           C\\nANISOU  935  CE2 PHE A 164     7729   7008  10065    614  -2062    545       C\\nATOM    936  CZ  PHE A 164       2.889  23.566  -4.178  1.00 64.54           C\\nANISOU  936  CZ  PHE A 164     7564   7051   9906    666  -2113    510       C\\nATOM    937  N   THR A 165       7.667  21.477  -2.285  1.00 60.91           N\\nANISOU  937  N   THR A 165     7302   6899   8944     90  -1100    820       N\\nATOM    938  CA  THR A 165       8.590  22.366  -2.984  1.00 68.08           C\\nANISOU  938  CA  THR A 165     8326   7648   9893    -59  -1264   1109       C\\nATOM    939  C   THR A 165       9.585  21.592  -3.836  1.00 67.06           C\\nANISOU  939  C   THR A 165     8237   7731   9511   -266  -1055   1321       C\\nATOM    940  O   THR A 165      10.068  22.114  -4.846  1.00 74.56           O\\nANISOU  940  O   THR A 165     9269   8666  10395   -439  -1158   1596       O\\nATOM    941  CB  THR A 165       9.335  23.256  -1.988  1.00 72.21           C\\nANISOU  941  CB  THR A 165     8862   7963  10613    -43  -1373   1067       C\\nATOM    942  OG1 THR A 165      10.064  22.439  -1.068  1.00 84.36           O\\nANISOU  942  OG1 THR A 165    10343   9656  12055    -52  -1111    946       O\\nATOM    943  CG2 THR A 165       8.362  24.133  -1.215  1.00 69.54           C\\nANISOU  943  CG2 THR A 165     8475   7415  10531    191  -1616    813       C\\nATOM    944  N   ILE A 166       9.898  20.352  -3.455  1.00 69.64           N\\nANISOU  944  N   ILE A 166     8506   8267   9687   -255   -775   1193       N\\nATOM    945  CA  ILE A 166      10.825  19.548  -4.247  1.00 72.15           C\\nANISOU  945  CA  ILE A 166     8831   8805   9778   -397   -585   1317       C\\nATOM    946  C   ILE A 166      10.150  19.043  -5.520  1.00 72.60           C\\nANISOU  946  C   ILE A 166     8918   9016   9653   -435   -578   1379       C\\nATOM    947  O   ILE A 166      10.751  19.045  -6.601  1.00 74.34           O\\nANISOU  947  O   ILE A 166     9167   9388   9690   -588   -548   1564       O\\nATOM    948  CB  ILE A 166      11.383  18.389  -3.402  1.00 64.44           C\\nANISOU  948  CB  ILE A 166     7804   7945   8737   -337   -355   1141       C\\nATOM    949  CG1 ILE A 166      12.401  18.911  -2.386  1.00 65.09           C\\nANISOU  949  CG1 ILE A 166     7859   7927   8946   -345   -368   1133       C\\nATOM    950  CG2 ILE A 166      12.008  17.326  -4.294  1.00 61.90           C\\nANISOU  950  CG2 ILE A 166     7469   7861   8189   -405   -177   1168       C\\nATOM    951  CD1 ILE A 166      12.979  17.825  -1.505  1.00 55.41           C\\nANISOU  951  CD1 ILE A 166     6604   6788   7663   -276   -195    979       C\\nATOM    952  N   SER A 167       8.896  18.605  -5.414  1.00 66.08           N\\nANISOU  952  N   SER A 167     8070   8185   8852   -311   -603   1216       N\\nATOM    953  CA  SER A 167       8.168  18.066  -6.554  1.00 69.77           C\\nANISOU  953  CA  SER A 167     8557   8794   9156   -335   -616   1237       C\\nATOM    954  C   SER A 167       7.500  19.138  -7.404  1.00 70.97           C\\nANISOU  954  C   SER A 167     8769   8841   9355   -354   -900   1407       C\\nATOM    955  O   SER A 167       7.132  18.860  -8.553  1.00 69.63           O\\nANISOU  955  O   SER A 167     8642   8809   9005   -415   -942   1493       O\\nATOM    956  CB  SER A 167       7.104  17.078  -6.070  1.00 67.68           C\\nANISOU  956  CB  SER A 167     8226   8582   8907   -228   -531    989       C\\nATOM    957  OG  SER A 167       6.153  17.737  -5.251  1.00 68.82           O\\nANISOU  957  OG  SER A 167     8295   8591   9261   -104   -663    859       O\\nATOM    958  N   CYS A 168       7.324  20.345  -6.871  1.00 72.75           N\\nANISOU  958  N   CYS A 168     9009   8812   9819   -293  -1126   1446       N\\nATOM    959  CA  CYS A 168       6.648  21.393  -7.631  1.00 73.51           C\\nANISOU  959  CA  CYS A 168     9186   8743  10001   -284  -1466   1607       C\\nATOM    960  C   CYS A 168       7.347  21.747  -8.942  1.00 77.62           C\\nANISOU  960  C   CYS A 168     9848   9341  10301   -524  -1540   1966       C\\nATOM    961  O   CYS A 168       6.638  22.045  -9.918  1.00 81.68           O\\nANISOU  961  O   CYS A 168    10442   9849  10744   -540  -1760   2098       O\\nATOM    962  CB  CYS A 168       6.478  22.640  -6.754  1.00 74.94           C\\nANISOU  962  CB  CYS A 168     9371   8593  10510   -158  -1727   1556       C\\nATOM    963  SG  CYS A 168       5.411  23.906  -7.472  1.00 83.98           S\\nANISOU  963  SG  CYS A 168    10608   9450  11852    -51  -2231   1669       S\\nATOM    964  N   PRO A 169       8.683  21.755  -9.044  1.00 78.38           N\\nANISOU  964  N   PRO A 169     9970   9541  10269   -727  -1380   2136       N\\nATOM    965  CA  PRO A 169       9.296  22.005 -10.360  1.00 83.73           C\\nANISOU  965  CA  PRO A 169    10752  10394  10669   -996  -1410   2471       C\\nATOM    966  C   PRO A 169       8.894  21.001 -11.428  1.00 84.95           C\\nANISOU  966  C   PRO A 169    10900  10878  10501  -1015  -1280   2429       C\\nATOM    967  O   PRO A 169       8.857  21.362 -12.611  1.00 84.19           O\\nANISOU  967  O   PRO A 169    10915  10894  10178  -1189  -1413   2692       O\\nATOM    968  CB  PRO A 169      10.799  21.935 -10.063  1.00 82.55           C\\nANISOU  968  CB  PRO A 169    10540  10383  10443  -1178  -1179   2547       C\\nATOM    969  CG  PRO A 169      10.912  22.332  -8.645  1.00 76.42           C\\nANISOU  969  CG  PRO A 169     9712   9325   9998  -1032  -1220   2380       C\\nATOM    970  CD  PRO A 169       9.698  21.762  -7.973  1.00 74.69           C\\nANISOU  970  CD  PRO A 169     9435   9030   9916   -740  -1219   2057       C\\nATOM    971  N   LEU A 170       8.584  19.755 -11.051  1.00 79.08           N\\nANISOU  971  N   LEU A 170    10044  10281   9723   -856  -1047   2113       N\\nATOM    972  CA  LEU A 170       8.270  18.731 -12.044  1.00 73.43           C\\nANISOU  972  CA  LEU A 170     9322   9863   8714   -871   -932   2033       C\\nATOM    973  C   LEU A 170       7.035  19.090 -12.860  1.00 76.56           C\\nANISOU  973  C   LEU A 170     9801  10208   9081   -835  -1215   2109       C\\nATOM    974  O   LEU A 170       6.917  18.677 -14.020  1.00 77.86           O\\nANISOU  974  O   LEU A 170    10015  10626   8942   -927  -1211   2171       O\\nATOM    975  CB  LEU A 170       8.080  17.380 -11.356  1.00 67.28           C\\nANISOU  975  CB  LEU A 170     8435   9155   7972   -710   -697   1684       C\\nATOM    976  CG  LEU A 170       9.176  16.975 -10.366  1.00 66.79           C\\nANISOU  976  CG  LEU A 170     8297   9091   7988   -692   -470   1577       C\\nATOM    977  CD1 LEU A 170       8.737  15.773  -9.563  1.00 66.74           C\\nANISOU  977  CD1 LEU A 170     8235   9057   8068   -536   -332   1276       C\\nATOM    978  CD2 LEU A 170      10.488  16.689 -11.074  1.00 61.58           C\\nANISOU  978  CD2 LEU A 170     7607   8724   7065   -840   -287   1659       C\\nATOM    979  N   LEU A 171       6.108  19.856 -12.280  1.00 72.91           N\\nANISOU  979  N   LEU A 171     9340   9439   8925   -685  -1477   2076       N\\nATOM    980  CA  LEU A 171       4.945  20.322 -13.024  1.00 75.80           C\\nANISOU  980  CA  LEU A 171     9768   9727   9306   -622  -1806   2146       C\\nATOM    981  C   LEU A 171       5.311  21.339 -14.094  1.00 79.71           C\\nANISOU  981  C   LEU A 171    10460  10190   9637   -830  -2066   2561       C\\nATOM    982  O   LEU A 171       4.541  21.531 -15.041  1.00 84.88           O\\nANISOU  982  O   LEU A 171    11203  10874  10173   -833  -2320   2673       O\\nATOM    983  CB  LEU A 171       3.917  20.942 -12.075  1.00 74.05           C\\nANISOU  983  CB  LEU A 171     9460   9199   9478   -376  -2034   1961       C\\nATOM    984  CG  LEU A 171       2.918  20.015 -11.385  1.00 69.74           C\\nANISOU  984  CG  LEU A 171     8717   8733   9050   -185  -1900   1574       C\\nATOM    985  CD1 LEU A 171       2.056  20.807 -10.416  1.00 68.86           C\\nANISOU  985  CD1 LEU A 171     8486   8373   9305     44  -2112   1385       C\\nATOM    986  CD2 LEU A 171       2.059  19.311 -12.420  1.00 65.45           C\\nANISOU  986  CD2 LEU A 171     8160   8395   8313   -188  -1959   1520       C\\nATOM    987  N   PHE A 172       6.460  21.995 -13.967  1.00 68.04           N\\nANISOU  987  N   PHE A 172     9054   8656   8140  -1028  -2027   2807       N\\nATOM    988  CA  PHE A 172       6.795  23.074 -14.882  1.00 78.77           C\\nANISOU  988  CA  PHE A 172    10620   9942   9366  -1280  -2310   3252       C\\nATOM    989  C   PHE A 172       8.096  22.777 -15.619  1.00 85.91           C\\nANISOU  989  C   PHE A 172    11542  11237   9862  -1615  -2028   3473       C\\nATOM    990  O   PHE A 172       9.011  23.607 -15.641  1.00 88.20           O\\nANISOU  990  O   PHE A 172    11911  11460  10141  -1873  -2078   3779       O\\nATOM    991  CB  PHE A 172       6.876  24.399 -14.118  1.00 84.73           C\\nANISOU  991  CB  PHE A 172    11461  10224  10509  -1254  -2621   3391       C\\nATOM    992  CG  PHE A 172       5.617  24.738 -13.360  1.00 85.93           C\\nANISOU  992  CG  PHE A 172    11551  10035  11063   -893  -2895   3113       C\\nATOM    993  CD1 PHE A 172       4.602  25.461 -13.964  1.00 86.94           C\\nANISOU  993  CD1 PHE A 172    11803   9937  11293   -793  -3356   3232       C\\nATOM    994  CD2 PHE A 172       5.447  24.323 -12.046  1.00 83.56           C\\nANISOU  994  CD2 PHE A 172    11054   9673  11022   -654  -2699   2721       C\\nATOM    995  CE1 PHE A 172       3.443  25.769 -13.275  1.00 83.30           C\\nANISOU  995  CE1 PHE A 172    11232   9212  11208   -436  -3605   2923       C\\nATOM    996  CE2 PHE A 172       4.288  24.629 -11.350  1.00 82.96           C\\nANISOU  996  CE2 PHE A 172    10876   9366  11280   -334  -2919   2431       C\\nATOM    997  CZ  PHE A 172       3.286  25.353 -11.967  1.00 83.10           C\\nANISOU  997  CZ  PHE A 172    10978   9179  11417   -212  -3367   2511       C\\nATOM    998  N   GLY A 173       8.179  21.592 -16.224  1.00 92.00           N\\nANISOU  998  N   GLY A 173    12224  12431  10302  -1618  -1741   3296       N\\nATOM    999  CA  GLY A 173       9.333  21.223 -17.023  1.00 99.29           C\\nANISOU  999  CA  GLY A 173    13120  13810  10797  -1900  -1463   3431       C\\nATOM   1000  C   GLY A 173      10.629  21.114 -16.255  1.00105.40           C\\nANISOU 1000  C   GLY A 173    13746  14661  11642  -1983  -1167   3370       C\\nATOM   1001  O   GLY A 173      11.703  21.225 -16.853  1.00109.34           O\\nANISOU 1001  O   GLY A 173    14209  15498  11836  -2275   -998   3563       O\\nATOM   1002  N   LEU A 174      10.558  20.899 -14.940  1.00100.46           N\\nANISOU 1002  N   LEU A 174    13015  13761  11393  -1742  -1102   3100       N\\nATOM   1003  CA  LEU A 174      11.734  20.873 -14.068  1.00103.35           C\\nANISOU 1003  CA  LEU A 174    13246  14141  11880  -1788   -879   3034       C\\nATOM   1004  C   LEU A 174      12.539  22.163 -14.183  1.00110.64           C\\nANISOU 1004  C   LEU A 174    14250  14960  12828  -2107  -1028   3434       C\\nATOM   1005  O   LEU A 174      13.746  22.179 -13.930  1.00113.38           O\\nANISOU 1005  O   LEU A 174    14470  15481  13128  -2273   -823   3467       O\\nATOM   1006  CB  LEU A 174      12.615  19.654 -14.361  1.00 97.67           C\\nANISOU 1006  CB  LEU A 174    12350  13885  10875  -1796   -492   2806       C\\nATOM   1007  CG  LEU A 174      13.534  19.118 -13.264  1.00 92.37           C\\nANISOU 1007  CG  LEU A 174    11502  13215  10381  -1682   -254   2560       C\\nATOM   1008  CD1 LEU A 174      12.928  19.339 -11.890  1.00 88.80           C\\nANISOU 1008  CD1 LEU A 174    11078  12307  10354  -1450   -387   2419       C\\nATOM   1009  CD2 LEU A 174      13.792  17.638 -13.505  1.00 90.06           C\\nANISOU 1009  CD2 LEU A 174    11076  13252   9891  -1525     22   2210       C\\nATOM   1010  N   ASN A 175      11.863  23.254 -14.556  1.00127.08           N\\nANISOU 1010  N   ASN A 175    16542  16739  15004  -2196  -1417   3738       N\\nATOM   1011  CA  ASN A 175      12.511  24.539 -14.814  1.00131.09           C\\nANISOU 1011  CA  ASN A 175    17185  17092  15530  -2547  -1637   4178       C\\nATOM   1012  C   ASN A 175      13.737  24.358 -15.706  1.00135.52           C\\nANISOU 1012  C   ASN A 175    17627  18169  15696  -2875  -1339   4267       C\\nATOM   1013  O   ASN A 175      14.777  24.991 -15.516  1.00141.49           O\\nANISOU 1013  O   ASN A 175    18317  18930  16514  -3096  -1295   4368       O\\nATOM   1014  CB  ASN A 175      12.876  25.244 -13.504  1.00127.19           C\\nANISOU 1014  CB  ASN A 175    16665  16177  15484  -2475  -1748   4122       C\\nATOM   1015  CG  ASN A 175      11.656  25.790 -12.774  1.00121.37           C\\nANISOU 1015  CG  ASN A 175    16035  14913  15169  -2144  -2109   3974       C\\nATOM   1016  OD1 ASN A 175      10.689  26.228 -13.400  1.00120.30           O\\nANISOU 1016  OD1 ASN A 175    16064  14605  15041  -2092  -2430   4105       O\\nATOM   1017  ND2 ASN A 175      11.697  25.764 -11.445  1.00115.08           N\\nANISOU 1017  ND2 ASN A 175    15127  13886  14713  -1906  -2061   3672       N\\nATOM   1018  N   ASN A 176      13.611  23.469 -16.686  1.00138.51           N\\nANISOU 1018  N   ASN A 176    17960  19005  15662  -2893  -1141   4194       N\\nATOM   1019  CA  ASN A 176      14.702  23.139 -17.593  1.00128.90           C\\nANISOU 1019  CA  ASN A 176    16590  18346  14041  -3148   -837   4194       C\\nATOM   1020  C   ASN A 176      14.143  23.135 -19.012  1.00130.29           C\\nANISOU 1020  C   ASN A 176    16893  18756  13854  -3256   -934   4312       C\\nATOM   1021  O   ASN A 176      13.054  23.656 -19.280  1.00128.25           O\\nANISOU 1021  O   ASN A 176    16856  18174  13701  -3186  -1280   4456       O\\nATOM   1022  CB  ASN A 176      15.347  21.804 -17.188  1.00114.40           C\\nANISOU 1022  CB  ASN A 176    14490  16909  12066  -3004   -416   3849       C\\nATOM   1023  N   ALA A 177      14.888  22.541 -19.940  1.00131.35           N\\nANISOU 1023  N   ALA A 177    16876  19466  13564  -3410   -639   4223       N\\nATOM   1024  CA  ALA A 177      14.518  22.512 -21.354  1.00133.06           C\\nANISOU 1024  CA  ALA A 177    17193  19978  13388  -3547   -695   4324       C\\nATOM   1025  C   ALA A 177      13.850  21.175 -21.665  1.00139.43           C\\nANISOU 1025  C   ALA A 177    17953  21060  13966  -3279   -543   3999       C\\nATOM   1026  O   ALA A 177      14.499  20.218 -22.087  1.00134.42           O\\nANISOU 1026  O   ALA A 177    17113  20932  13028  -3260   -210   3722       O\\nATOM   1027  CB  ALA A 177      15.744  22.740 -22.230  1.00132.82           C\\nANISOU 1027  CB  ALA A 177    17018  20431  13018  -3895   -487   4415       C\\nATOM   1028  N   ASP A 178      12.535  21.113 -21.456  1.00139.56           N\\nANISOU 1028  N   ASP A 178    18147  20737  14141  -3057   -814   4002       N\\nATOM   1029  CA  ASP A 178      11.738  19.985 -21.927  1.00140.00           C\\nANISOU 1029  CA  ASP A 178    18203  21034  13957  -2843   -761   3735       C\\nATOM   1030  C   ASP A 178      10.328  20.465 -22.235  1.00139.46           C\\nANISOU 1030  C   ASP A 178    18375  20618  13994  -2746  -1185   3897       C\\nATOM   1031  O   ASP A 178       9.372  20.082 -21.554  1.00142.64           O\\nANISOU 1031  O   ASP A 178    18808  20766  14622  -2479  -1336   3761       O\\nATOM   1032  CB  ASP A 178      11.711  18.857 -20.894  1.00137.06           C\\nANISOU 1032  CB  ASP A 178    17675  20675  13728  -2556   -547   3368       C\\nATOM   1033  N   GLN A 179      10.191  21.295 -23.270  1.00143.02           N\\nANISOU 1033  N   GLN A 179    18983  21074  14284  -2960  -1392   4178       N\\nATOM   1034  CA  GLN A 179       8.987  22.105 -23.424  1.00133.33           C\\nANISOU 1034  CA  GLN A 179    17987  19403  13269  -2879  -1859   4383       C\\nATOM   1035  C   GLN A 179       7.753  21.243 -23.675  1.00128.51           C\\nANISOU 1035  C   GLN A 179    17406  18844  12578  -2605  -1987   4153       C\\nATOM   1036  O   GLN A 179       6.787  21.279 -22.902  1.00124.40           O\\nANISOU 1036  O   GLN A 179    16911  17946  12410  -2345  -2237   4071       O\\nATOM   1037  CB  GLN A 179       9.188  23.117 -24.553  1.00132.56           C\\nANISOU 1037  CB  GLN A 179    18056  19342  12970  -3191  -2041   4737       C\\nATOM   1038  N   ASN A 180       7.766  20.455 -24.749  1.00126.77           N\\nANISOU 1038  N   ASN A 180    17160  19104  11903  -2656  -1831   4014       N\\nATOM   1039  CA  ASN A 180       6.565  19.780 -25.230  1.00115.92           C\\nANISOU 1039  CA  ASN A 180    15839  17790  10414  -2448  -2017   3825       C\\nATOM   1040  C   ASN A 180       6.535  18.292 -24.886  1.00111.57           C\\nANISOU 1040  C   ASN A 180    15109  17542   9741  -2253  -1745   3379       C\\nATOM   1041  O   ASN A 180       5.949  17.498 -25.625  1.00103.18           O\\nANISOU 1041  O   ASN A 180    14050  16740   8415  -2166  -1771   3154       O\\nATOM   1042  CB  ASN A 180       6.419  19.972 -26.739  1.00115.56           C\\nANISOU 1042  CB  ASN A 180    15926  18028   9952  -2620  -2110   3964       C\\nATOM   1043  N   GLU A 181       7.135  17.896 -23.764  1.00104.62           N\\nANISOU 1043  N   GLU A 181    14065  16578   9107  -2156  -1490   3195       N\\nATOM   1044  CA  GLU A 181       7.136  16.494 -23.369  1.00106.80           C\\nANISOU 1044  CA  GLU A 181    14149  16965   9465  -1902  -1204   2656       C\\nATOM   1045  C   GLU A 181       6.948  16.366 -21.867  1.00100.72           C\\nANISOU 1045  C   GLU A 181    13266  15721   9281  -1661  -1157   2456       C\\nATOM   1046  O   GLU A 181       7.211  17.295 -21.099  1.00102.83           O\\nANISOU 1046  O   GLU A 181    13557  15677   9838  -1708  -1233   2688       O\\nATOM   1047  CB  GLU A 181       8.426  15.780 -23.782  1.00111.20           C\\nANISOU 1047  CB  GLU A 181    14562  18052   9639  -2014   -799   2478       C\\nATOM   1048  CG  GLU A 181       8.455  15.363 -25.237  1.00118.18           C\\nANISOU 1048  CG  GLU A 181    15491  19499   9912  -2150   -768   2439       C\\nATOM   1049  CD  GLU A 181       9.558  14.373 -25.529  1.00125.80           C\\nANISOU 1049  CD  GLU A 181    16244  20936  10620  -2119   -359   2054       C\\nATOM   1050  OE1 GLU A 181       9.649  13.356 -24.809  1.00127.00           O\\nANISOU 1050  OE1 GLU A 181    16258  20997  10999  -1858   -200   1630       O\\nATOM   1051  OE2 GLU A 181      10.339  14.618 -26.473  1.00132.18           O\\nANISOU 1051  OE2 GLU A 181    16999  22090  11133  -2311   -210   2123       O\\nATOM   1052  N   CYS A 182       6.490  15.185 -21.461  1.00 85.77           N\\nANISOU 1052  N   CYS A 182    11262  13784   7544  -1421  -1042   2020       N\\nATOM   1053  CA  CYS A 182       6.326  14.886 -20.051  1.00 85.01           C\\nANISOU 1053  CA  CYS A 182    11057  13309   7934  -1219   -963   1809       C\\nATOM   1054  C   CYS A 182       7.659  15.034 -19.325  1.00 85.25           C\\nANISOU 1054  C   CYS A 182    10998  13354   8038  -1280   -699   1848       C\\nATOM   1055  O   CYS A 182       8.737  14.991 -19.927  1.00 87.66           O\\nANISOU 1055  O   CYS A 182    11266  14030   8011  -1441   -506   1910       O\\nATOM   1056  CB  CYS A 182       5.770  13.473 -19.864  1.00 85.07           C\\nANISOU 1056  CB  CYS A 182    10980  13320   8021  -1022   -869   1364       C\\nATOM   1057  SG  CYS A 182       5.430  13.056 -18.147  1.00 88.55           S\\nANISOU 1057  SG  CYS A 182    11313  13325   9006   -826   -793   1143       S\\nATOM   1058  N   ILE A 183       7.575  15.222 -18.009  1.00 86.69           N\\nANISOU 1058  N   ILE A 183    11127  13162   8650  -1153   -694   1796       N\\nATOM   1059  CA  ILE A 183       8.782  15.505 -17.243  1.00 88.06           C\\nANISOU 1059  CA  ILE A 183    11221  13307   8931  -1209   -498   1856       C\\nATOM   1060  C   ILE A 183       9.631  14.253 -17.070  1.00 90.76           C\\nANISOU 1060  C   ILE A 183    11430  13873   9183  -1113   -193   1518       C\\nATOM   1061  O   ILE A 183      10.856  14.349 -16.944  1.00 89.70           O\\nANISOU 1061  O   ILE A 183    11199  13916   8966  -1199     -1   1550       O\\nATOM   1062  CB  ILE A 183       8.428  16.141 -15.888  1.00 82.65           C\\nANISOU 1062  CB  ILE A 183    10529  12169   8706  -1098   -610   1893       C\\nATOM   1063  CG1 ILE A 183       9.689  16.703 -15.236  1.00 81.90           C\\nANISOU 1063  CG1 ILE A 183    10377  12044   8696  -1203   -475   2026       C\\nATOM   1064  CG2 ILE A 183       7.755  15.134 -14.972  1.00 80.02           C\\nANISOU 1064  CG2 ILE A 183    10121  11657   8626   -869   -543   1542       C\\nATOM   1065  CD1 ILE A 183      10.562  17.486 -16.201  1.00 77.13           C\\nANISOU 1065  CD1 ILE A 183     9815  11711   7778  -1501   -472   2363       C\\nATOM   1066  N   ILE A 184       9.020  13.066 -17.078  1.00 86.05           N\\nANISOU 1066  N   ILE A 184    10817  13266   8612   -938   -167   1182       N\\nATOM   1067  CA  ILE A 184       9.808  11.848 -16.945  1.00 81.50           C\\nANISOU 1067  CA  ILE A 184    10141  12849   7978   -818     61    843       C\\nATOM   1068  C   ILE A 184      10.649  11.603 -18.187  1.00 77.44           C\\nANISOU 1068  C   ILE A 184     9566  12848   7010   -918    205    786       C\\nATOM   1069  O   ILE A 184      11.589  10.802 -18.148  1.00 77.18           O\\nANISOU 1069  O   ILE A 184     9408  13014   6904   -822    403    514       O\\nATOM   1070  CB  ILE A 184       8.907  10.636 -16.645  1.00 80.64           C\\nANISOU 1070  CB  ILE A 184    10060  12549   8030   -635      7    515       C\\nATOM   1071  CG1 ILE A 184       9.694   9.574 -15.876  1.00 78.25           C\\nANISOU 1071  CG1 ILE A 184     9688  12171   7873   -478    168    222       C\\nATOM   1072  CG2 ILE A 184       8.346  10.052 -17.932  1.00 83.92           C\\nANISOU 1072  CG2 ILE A 184    10523  13226   8137   -643    -67    367       C\\nATOM   1073  CD1 ILE A 184       8.861   8.383 -15.456  1.00 80.33           C\\nANISOU 1073  CD1 ILE A 184    10011  12185   8326   -346     90    -54       C\\nATOM   1074  N   ALA A 185      10.335  12.279 -19.291  1.00 80.23           N\\nANISOU 1074  N   ALA A 185     9999  13442   7044  -1105     98   1028       N\\nATOM   1075  CA  ALA A 185      11.162  12.234 -20.487  1.00 83.51           C\\nANISOU 1075  CA  ALA A 185    10349  14420   6960  -1262    251   1031       C\\nATOM   1076  C   ALA A 185      12.352  13.177 -20.411  1.00 83.75           C\\nANISOU 1076  C   ALA A 185    10288  14647   6887  -1499    393   1327       C\\nATOM   1077  O   ALA A 185      13.207  13.143 -21.301  1.00 89.61           O\\nANISOU 1077  O   ALA A 185    10921  15924   7202  -1661    576   1320       O\\nATOM   1078  CB  ALA A 185      10.320  12.565 -21.723  1.00 73.89           C\\nANISOU 1078  CB  ALA A 185     9279  13403   5395  -1401     57   1201       C\\nATOM   1079  N   ASN A 186      12.425  14.011 -19.384  1.00 87.95           N\\nANISOU 1079  N   ASN A 186    10846  14788   7782  -1536    315   1567       N\\nATOM   1080  CA  ASN A 186      13.545  14.931 -19.235  1.00 90.37           C\\nANISOU 1080  CA  ASN A 186    11066  15232   8039  -1784    421   1852       C\\nATOM   1081  C   ASN A 186      14.781  14.156 -18.795  1.00 93.04           C\\nANISOU 1081  C   ASN A 186    11153  15806   8392  -1671    718   1526       C\\nATOM   1082  O   ASN A 186      14.734  13.472 -17.765  1.00 90.82           O\\nANISOU 1082  O   ASN A 186    10830  15214   8462  -1399    737   1252       O\\nATOM   1083  CB  ASN A 186      13.200  16.017 -18.220  1.00 86.22           C\\nANISOU 1083  CB  ASN A 186    10651  14175   7934  -1820    209   2150       C\\nATOM   1084  CG  ASN A 186      14.162  17.185 -18.259  1.00 89.29           C\\nANISOU 1084  CG  ASN A 186    11013  14659   8255  -2152    225   2537       C\\nATOM   1085  OD1 ASN A 186      15.380  17.008 -18.241  1.00 95.97           O\\nANISOU 1085  OD1 ASN A 186    11655  15837   8971  -2255    479   2464       O\\nATOM   1086  ND2 ASN A 186      13.616  18.393 -18.314  1.00 87.60           N\\nANISOU 1086  ND2 ASN A 186    10997  14142   8145  -2325    -71   2943       N\\nATOM   1087  N   PRO A 187      15.895  14.232 -19.527  1.00 95.07           N\\nANISOU 1087  N   PRO A 187    11229  16621   8273  -1873    941   1541       N\\nATOM   1088  CA  PRO A 187      17.095  13.486 -19.110  1.00 94.27           C\\nANISOU 1088  CA  PRO A 187    10845  16765   8209  -1726   1203   1183       C\\nATOM   1089  C   PRO A 187      17.587  13.857 -17.721  1.00 93.98           C\\nANISOU 1089  C   PRO A 187    10749  16330   8627  -1662   1185   1242       C\\nATOM   1090  O   PRO A 187      18.317  13.067 -17.109  1.00 94.56           O\\nANISOU 1090  O   PRO A 187    10638  16436   8855  -1433   1319    896       O\\nATOM   1091  CB  PRO A 187      18.127  13.845 -20.190  1.00 87.30           C\\nANISOU 1091  CB  PRO A 187     9769  16534   6867  -2026   1406   1271       C\\nATOM   1092  CG  PRO A 187      17.630  15.128 -20.784  1.00 81.91           C\\nANISOU 1092  CG  PRO A 187     9311  15710   6102  -2368   1189   1793       C\\nATOM   1093  CD  PRO A 187      16.135  15.035 -20.737  1.00 89.48           C\\nANISOU 1093  CD  PRO A 187    10552  16349   7098  -2256    952   1890       C\\nATOM   1094  N   ALA A 188      17.198  15.020 -17.198  1.00 89.90           N\\nANISOU 1094  N   ALA A 188    10393  15427   8337  -1837    994   1648       N\\nATOM   1095  CA  ALA A 188      17.621  15.462 -15.877  1.00 87.20           C\\nANISOU 1095  CA  ALA A 188    10012  14708   8411  -1788    952   1704       C\\nATOM   1096  C   ALA A 188      16.681  15.017 -14.764  1.00 83.84           C\\nANISOU 1096  C   ALA A 188     9732  13727   8396  -1473    795   1536       C\\nATOM   1097  O   ALA A 188      16.983  15.253 -13.591  1.00 75.80           O\\nANISOU 1097  O   ALA A 188     8687  12406   7707  -1395    761   1530       O\\nATOM   1098  CB  ALA A 188      17.750  16.987 -15.848  1.00 80.85           C\\nANISOU 1098  CB  ALA A 188     9302  13764   7654  -2142    804   2201       C\\nATOM   1099  N   PHE A 189      15.554  14.386 -15.094  1.00 80.92           N\\nANISOU 1099  N   PHE A 189     9504  13244   7997  -1314    698   1400       N\\nATOM   1100  CA  PHE A 189      14.640  13.936 -14.051  1.00 78.27           C\\nANISOU 1100  CA  PHE A 189     9281  12440   8018  -1065    570   1248       C\\nATOM   1101  C   PHE A 189      15.276  12.851 -13.193  1.00 80.35           C\\nANISOU 1101  C   PHE A 189     9430  12648   8450   -824    697    901       C\\nATOM   1102  O   PHE A 189      15.128  12.856 -11.964  1.00 75.11           O\\nANISOU 1102  O   PHE A 189     8806  11626   8105   -710    633    876       O\\nATOM   1103  CB  PHE A 189      13.335  13.437 -14.671  1.00 80.58           C\\nANISOU 1103  CB  PHE A 189     9715  12675   8225   -983    445   1165       C\\nATOM   1104  CG  PHE A 189      12.426  12.754 -13.693  1.00 85.91           C\\nANISOU 1104  CG  PHE A 189    10465  12965   9214   -760    358    965       C\\nATOM   1105  CD1 PHE A 189      11.690  13.490 -12.780  1.00 86.83           C\\nANISOU 1105  CD1 PHE A 189    10658  12708   9625   -749    203   1115       C\\nATOM   1106  CD2 PHE A 189      12.306  11.375 -13.683  1.00 84.50           C\\nANISOU 1106  CD2 PHE A 189    10274  12804   9028   -575    421    619       C\\nATOM   1107  CE1 PHE A 189      10.853  12.861 -11.873  1.00 82.22           C\\nANISOU 1107  CE1 PHE A 189    10115  11841   9283   -588    152    936       C\\nATOM   1108  CE2 PHE A 189      11.471  10.742 -12.779  1.00 79.97           C\\nANISOU 1108  CE2 PHE A 189     9777  11887   8720   -435    339    479       C\\nATOM   1109  CZ  PHE A 189      10.745  11.486 -11.874  1.00 75.49           C\\nANISOU 1109  CZ  PHE A 189     9262  11015   8404   -457    224    645       C\\nATOM   1110  N   VAL A 190      15.990  11.913 -13.820  1.00 82.64           N\\nANISOU 1110  N   VAL A 190     9581  13296   8524   -736    857    620       N\\nATOM   1111  CA  VAL A 190      16.608  10.825 -13.066  1.00 79.80           C\\nANISOU 1111  CA  VAL A 190     9129  12855   8338   -476    921    274       C\\nATOM   1112  C   VAL A 190      17.619  11.375 -12.070  1.00 73.96           C\\nANISOU 1112  C   VAL A 190     8263  12038   7801   -501    965    362       C\\nATOM   1113  O   VAL A 190      17.647  10.963 -10.905  1.00 69.81           O\\nANISOU 1113  O   VAL A 190     7780  11184   7561   -328    899    257       O\\nATOM   1114  CB  VAL A 190      17.246   9.799 -14.024  1.00 76.29           C\\nANISOU 1114  CB  VAL A 190     8531  12834   7621   -350   1058    -85       C\\nATOM   1115  CG1 VAL A 190      18.329   8.997 -13.321  1.00 73.98           C\\nANISOU 1115  CG1 VAL A 190     8071  12543   7496   -111   1121   -401       C\\nATOM   1116  CG2 VAL A 190      16.181   8.863 -14.570  1.00 70.22           C\\nANISOU 1116  CG2 VAL A 190     7922  11973   6787   -219    957   -292       C\\nATOM   1117  N   VAL A 191      18.449  12.327 -12.502  1.00 74.89           N\\nANISOU 1117  N   VAL A 191     8232  12459   7764   -745   1062    574       N\\nATOM   1118  CA  VAL A 191      19.440  12.910 -11.603  1.00 69.99           C\\nANISOU 1118  CA  VAL A 191     7472  11783   7337   -800   1089    659       C\\nATOM   1119  C   VAL A 191      18.756  13.666 -10.472  1.00 71.73           C\\nANISOU 1119  C   VAL A 191     7882  11494   7879   -818    904    880       C\\nATOM   1120  O   VAL A 191      19.167  13.580  -9.308  1.00 74.22           O\\nANISOU 1120  O   VAL A 191     8168  11584   8449   -696    866    802       O\\nATOM   1121  CB  VAL A 191      20.401  13.820 -12.387  1.00 69.86           C\\nANISOU 1121  CB  VAL A 191     7256  12216   7071  -1128   1224    873       C\\nATOM   1122  CG1 VAL A 191      21.588  14.210 -11.518  1.00 61.69           C\\nANISOU 1122  CG1 VAL A 191     6014  11194   6229  -1167   1269    875       C\\nATOM   1123  CG2 VAL A 191      20.860  13.135 -13.669  1.00 71.25           C\\nANISOU 1123  CG2 VAL A 191     7250  12975   6848  -1136   1419    651       C\\nATOM   1124  N   TYR A 192      17.698  14.409 -10.792  1.00 73.30           N\\nANISOU 1124  N   TYR A 192     8269  11519   8064   -952    769   1133       N\\nATOM   1125  CA  TYR A 192      17.008  15.209  -9.786  1.00 69.49           C\\nANISOU 1125  CA  TYR A 192     7937  10591   7877   -952    585   1300       C\\nATOM   1126  C   TYR A 192      16.386  14.323  -8.714  1.00 69.05           C\\nANISOU 1126  C   TYR A 192     7966  10230   8040   -683    540   1063       C\\nATOM   1127  O   TYR A 192      16.743  14.407  -7.534  1.00 70.50           O\\nANISOU 1127  O   TYR A 192     8135  10210   8443   -602    510   1018       O\\nATOM   1128  CB  TYR A 192      15.946  16.079 -10.460  1.00 70.53           C\\nANISOU 1128  CB  TYR A 192     8235  10616   7948  -1102    419   1566       C\\nATOM   1129  CG  TYR A 192      15.223  17.022  -9.524  1.00 71.79           C\\nANISOU 1129  CG  TYR A 192     8522  10343   8412  -1083    204   1704       C\\nATOM   1130  CD1 TYR A 192      15.814  18.212  -9.114  1.00 72.52           C\\nANISOU 1130  CD1 TYR A 192     8604  10305   8647  -1251    105   1926       C\\nATOM   1131  CD2 TYR A 192      13.943  16.733  -9.066  1.00 75.40           C\\nANISOU 1131  CD2 TYR A 192     9093  10543   9014   -904     92   1589       C\\nATOM   1132  CE1 TYR A 192      15.157  19.082  -8.265  1.00 72.60           C\\nANISOU 1132  CE1 TYR A 192     8724   9917   8942  -1200   -114   1996       C\\nATOM   1133  CE2 TYR A 192      13.275  17.600  -8.217  1.00 78.40           C\\nANISOU 1133  CE2 TYR A 192     9549  10580   9658   -860    -96   1656       C\\nATOM   1134  CZ  TYR A 192      13.887  18.772  -7.820  1.00 72.16           C\\nANISOU 1134  CZ  TYR A 192     8758   9648   9013   -988   -206   1843       C\\nATOM   1135  OH  TYR A 192      13.226  19.632  -6.973  1.00 63.34           O\\nANISOU 1135  OH  TYR A 192     7711   8188   8168   -909   -415   1853       O\\nATOM   1136  N   SER A 193      15.457  13.449  -9.114  1.00 72.61           N\\nANISOU 1136  N   SER A 193     8511  10659   8417   -566    526    916       N\\nATOM   1137  CA  SER A 193      14.715  12.654  -8.139  1.00 77.34           C\\nANISOU 1137  CA  SER A 193     9213  10968   9205   -382    469    746       C\\nATOM   1138  C   SER A 193      15.615  11.681  -7.386  1.00 75.22           C\\nANISOU 1138  C   SER A 193     8884  10678   9019   -217    535    524       C\\nATOM   1139  O   SER A 193      15.294  11.286  -6.260  1.00 76.80           O\\nANISOU 1139  O   SER A 193     9170  10614   9397   -116    473    460       O\\nATOM   1140  CB  SER A 193      13.580  11.897  -8.830  1.00 79.11           C\\nANISOU 1140  CB  SER A 193     9536  11195   9327   -336    430    640       C\\nATOM   1141  OG  SER A 193      14.075  10.934  -9.741  1.00 69.99           O\\nANISOU 1141  OG  SER A 193     8324  10300   7968   -274    524    442       O\\nATOM   1142  N   SER A 194      16.739  11.283  -7.980  1.00 71.25           N\\nANISOU 1142  N   SER A 194     8226  10467   8381   -186    646    398       N\\nATOM   1143  CA  SER A 194      17.664  10.407  -7.271  1.00 72.26           C\\nANISOU 1143  CA  SER A 194     8279  10561   8614      6    663    171       C\\nATOM   1144  C   SER A 194      18.401  11.166  -6.177  1.00 76.18           C\\nANISOU 1144  C   SER A 194     8709  10947   9290    -29    635    286       C\\nATOM   1145  O   SER A 194      18.423  10.741  -5.014  1.00 72.02           O\\nANISOU 1145  O   SER A 194     8263  10164   8939     99    550    218       O\\nATOM   1146  CB  SER A 194      18.661   9.784  -8.246  1.00 72.31           C\\nANISOU 1146  CB  SER A 194     8087  10955   8432     84    784    -57       C\\nATOM   1147  OG  SER A 194      17.998   9.092  -9.286  1.00 80.43           O\\nANISOU 1147  OG  SER A 194     9180  12101   9277    122    797   -194       O\\nATOM   1148  N   ILE A 195      19.005  12.300  -6.530  1.00 77.08           N\\nANISOU 1148  N   ILE A 195     8687  11249   9349   -226    688    474       N\\nATOM   1149  CA  ILE A 195      19.847  13.021  -5.580  1.00 70.51           C\\nANISOU 1149  CA  ILE A 195     7763  10342   8685   -272    652    555       C\\nATOM   1150  C   ILE A 195      18.988  13.748  -4.552  1.00 66.52           C\\nANISOU 1150  C   ILE A 195     7438   9466   8370   -304    511    708       C\\nATOM   1151  O   ILE A 195      19.129  13.541  -3.341  1.00 74.63           O\\nANISOU 1151  O   ILE A 195     8511  10286   9557   -186    438    633       O\\nATOM   1152  CB  ILE A 195      20.787  13.987  -6.321  1.00 68.49           C\\nANISOU 1152  CB  ILE A 195     7299  10412   8313   -520    744    715       C\\nATOM   1153  CG1 ILE A 195      21.784  13.200  -7.177  1.00 66.22           C\\nANISOU 1153  CG1 ILE A 195     6764  10568   7828   -459    911    488       C\\nATOM   1154  CG2 ILE A 195      21.510  14.892  -5.337  1.00 63.89           C\\nANISOU 1154  CG2 ILE A 195     6643   9700   7932   -613    668    829       C\\nATOM   1155  CD1 ILE A 195      22.738  14.064  -7.971  1.00 56.97           C\\nANISOU 1155  CD1 ILE A 195     5348   9813   6484   -752   1041    642       C\\nATOM   1156  N   VAL A 196      18.073  14.597  -5.019  1.00 62.66           N\\nANISOU 1156  N   VAL A 196     7052   8902   7854   -450    454    905       N\\nATOM   1157  CA  VAL A 196      17.332  15.463  -4.105  1.00 67.97           C\\nANISOU 1157  CA  VAL A 196     7847   9264   8715   -469    309   1012       C\\nATOM   1158  C   VAL A 196      16.343  14.656  -3.269  1.00 67.07           C\\nANISOU 1158  C   VAL A 196     7868   8944   8670   -296    275    861       C\\nATOM   1159  O   VAL A 196      16.268  14.814  -2.046  1.00 61.49           O\\nANISOU 1159  O   VAL A 196     7206   8054   8102   -231    210    818       O\\nATOM   1160  CB  VAL A 196      16.626  16.582  -4.888  1.00 64.23           C\\nANISOU 1160  CB  VAL A 196     7440   8750   8216   -643    212   1244       C\\nATOM   1161  CG1 VAL A 196      15.849  17.474  -3.945  1.00 52.97           C\\nANISOU 1161  CG1 VAL A 196     6116   7001   7009   -610     37   1287       C\\nATOM   1162  CG2 VAL A 196      17.638  17.392  -5.674  1.00 71.96           C\\nANISOU 1162  CG2 VAL A 196     8304   9935   9102   -883    238   1445       C\\nATOM   1163  N   SER A 197      15.571  13.778  -3.911  1.00 68.31           N\\nANISOU 1163  N   SER A 197     8091   9151   8712   -244    315    780       N\\nATOM   1164  CA  SER A 197      14.505  13.073  -3.211  1.00 64.29           C\\nANISOU 1164  CA  SER A 197     7706   8466   8256   -150    280    676       C\\nATOM   1165  C   SER A 197      14.986  11.839  -2.460  1.00 64.86           C\\nANISOU 1165  C   SER A 197     7819   8478   8346    -22    301    516       C\\nATOM   1166  O   SER A 197      14.304  11.401  -1.528  1.00 71.84           O\\nANISOU 1166  O   SER A 197     8812   9202   9284      7    262    476       O\\nATOM   1167  CB  SER A 197      13.401  12.668  -4.191  1.00 64.34           C\\nANISOU 1167  CB  SER A 197     7768   8525   8155   -175    281    661       C\\nATOM   1168  OG  SER A 197      12.416  13.677  -4.297  1.00 65.40           O\\nANISOU 1168  OG  SER A 197     7921   8583   8345   -241    188    775       O\\nATOM   1169  N   PHE A 198      16.134  11.265  -2.824  1.00 56.65           N\\nANISOU 1169  N   PHE A 198     6693   7571   7259     50    348    422       N\\nATOM   1170  CA  PHE A 198      16.563  10.006  -2.225  1.00 61.84           C\\nANISOU 1170  CA  PHE A 198     7413   8131   7953    205    308    258       C\\nATOM   1171  C   PHE A 198      17.951  10.080  -1.597  1.00 66.94           C\\nANISOU 1171  C   PHE A 198     7945   8814   8677    293    283    207       C\\nATOM   1172  O   PHE A 198      18.076   9.853  -0.391  1.00 63.30           O\\nANISOU 1172  O   PHE A 198     7574   8170   8306    352    191    202       O\\nATOM   1173  CB  PHE A 198      16.518   8.887  -3.269  1.00 62.27           C\\nANISOU 1173  CB  PHE A 198     7477   8279   7904    290    331     91       C\\nATOM   1174  CG  PHE A 198      16.836   7.525  -2.714  1.00 71.87           C\\nANISOU 1174  CG  PHE A 198     8800   9318   9188    461    226    -82       C\\nATOM   1175  CD1 PHE A 198      15.889   6.822  -1.986  1.00 73.26           C\\nANISOU 1175  CD1 PHE A 198     9194   9229   9414    432    130    -54       C\\nATOM   1176  CD2 PHE A 198      18.074   6.944  -2.927  1.00 66.14           C\\nANISOU 1176  CD2 PHE A 198     7955   8695   8481    641    204   -273       C\\nATOM   1177  CE1 PHE A 198      16.173   5.566  -1.481  1.00 70.07           C\\nANISOU 1177  CE1 PHE A 198     8932   8611   9079    560    -15   -171       C\\nATOM   1178  CE2 PHE A 198      18.365   5.687  -2.423  1.00 70.55           C\\nANISOU 1178  CE2 PHE A 198     8637   9036   9134    826     45   -436       C\\nATOM   1179  CZ  PHE A 198      17.412   4.997  -1.700  1.00 69.64           C\\nANISOU 1179  CZ  PHE A 198     8787   8602   9070    775    -79   -363       C\\nATOM   1180  N   TYR A 199      18.996  10.380  -2.373  1.00 67.17           N\\nANISOU 1180  N   TYR A 199     7766   9103   8654    290    360    166       N\\nATOM   1181  CA  TYR A 199      20.356  10.230  -1.861  1.00 67.05           C\\nANISOU 1181  CA  TYR A 199     7598   9159   8719    402    329     58       C\\nATOM   1182  C   TYR A 199      20.656  11.224  -0.746  1.00 67.17           C\\nANISOU 1182  C   TYR A 199     7604   9058   8859    323    261    193       C\\nATOM   1183  O   TYR A 199      21.379  10.897   0.202  1.00 60.26           O\\nANISOU 1183  O   TYR A 199     6716   8098   8082    445    161    112       O\\nATOM   1184  CB  TYR A 199      21.367  10.375  -2.997  1.00 71.88           C\\nANISOU 1184  CB  TYR A 199     7935  10155   9221    380    457    -32       C\\nATOM   1185  CG  TYR A 199      21.372   9.197  -3.942  1.00 81.30           C\\nANISOU 1185  CG  TYR A 199     9102  11489  10299    540    498   -275       C\\nATOM   1186  CD1 TYR A 199      21.185   7.907  -3.469  1.00 86.13           C\\nANISOU 1186  CD1 TYR A 199     9871  11856  10998    769    359   -463       C\\nATOM   1187  CD2 TYR A 199      21.545   9.374  -5.307  1.00 83.10           C\\nANISOU 1187  CD2 TYR A 199     9165  12088  10320    449    652   -315       C\\nATOM   1188  CE1 TYR A 199      21.177   6.825  -4.325  1.00 85.63           C\\nANISOU 1188  CE1 TYR A 199     9799  11878  10859    933    355   -719       C\\nATOM   1189  CE2 TYR A 199      21.538   8.297  -6.171  1.00 80.51           C\\nANISOU 1189  CE2 TYR A 199     8809  11905   9875    615    680   -585       C\\nATOM   1190  CZ  TYR A 199      21.352   7.026  -5.674  1.00 76.43           C\\nANISOU 1190  CZ  TYR A 199     8448  11104   9487    871    522   -803       C\\nATOM   1191  OH  TYR A 199      21.344   5.950  -6.531  1.00 69.70           O\\nANISOU 1191  OH  TYR A 199     7579  10355   8547   1053    510  -1106       O\\nATOM   1192  N   VAL A 200      20.116  12.435  -0.831  1.00 65.74           N\\nANISOU 1192  N   VAL A 200     7439   8856   8685    133    281    383       N\\nATOM   1193  CA  VAL A 200      20.375  13.434   0.206  1.00 71.58           C\\nANISOU 1193  CA  VAL A 200     8173   9468   9555     66    193    476       C\\nATOM   1194  C   VAL A 200      19.616  13.076   1.483  1.00 70.25           C\\nANISOU 1194  C   VAL A 200     8210   9046   9435    156     95    445       C\\nATOM   1195  O   VAL A 200      20.203  13.156   2.571  1.00 66.48           O\\nANISOU 1195  O   VAL A 200     7736   8490   9035    213      0    407       O\\nATOM   1196  CB  VAL A 200      20.038  14.854  -0.281  1.00 71.46           C\\nANISOU 1196  CB  VAL A 200     8129   9461   9562   -148    192    671       C\\nATOM   1197  CG1 VAL A 200      20.109  15.848   0.873  1.00 70.31           C\\nANISOU 1197  CG1 VAL A 200     8017   9123   9575   -187     60    720       C\\nATOM   1198  CG2 VAL A 200      20.992  15.264  -1.393  1.00 67.72           C\\nANISOU 1198  CG2 VAL A 200     7444   9277   9011   -300    285    742       C\\nATOM   1199  N   PRO A 201      18.333  12.691   1.432  1.00 68.63           N\\nANISOU 1199  N   PRO A 201     8167   8739   9171    150    111    459       N\\nATOM   1200  CA  PRO A 201      17.717  12.147   2.655  1.00 67.01           C\\nANISOU 1200  CA  PRO A 201     8135   8363   8962    204     43    424       C\\nATOM   1201  C   PRO A 201      18.416  10.898   3.166  1.00 63.12           C\\nANISOU 1201  C   PRO A 201     7712   7811   8461    342    -32    331       C\\nATOM   1202  O   PRO A 201      18.541  10.711   4.383  1.00 64.72           O\\nANISOU 1202  O   PRO A 201     8019   7903   8669    376   -131    332       O\\nATOM   1203  CB  PRO A 201      16.275  11.860   2.217  1.00 66.92           C\\nANISOU 1203  CB  PRO A 201     8227   8319   8879    142     97    446       C\\nATOM   1204  CG  PRO A 201      16.022  12.833   1.137  1.00 66.63           C\\nANISOU 1204  CG  PRO A 201     8086   8379   8852     55    144    523       C\\nATOM   1205  CD  PRO A 201      17.319  12.916   0.383  1.00 66.70           C\\nANISOU 1205  CD  PRO A 201     7946   8542   8857     61    178    525       C\\nATOM   1206  N   PHE A 202      18.884  10.041   2.258  1.00 56.10           N\\nANISOU 1206  N   PHE A 202     6771   6992   7551    435    -11    238       N\\nATOM   1207  CA  PHE A 202      19.593   8.829   2.655  1.00 63.87           C\\nANISOU 1207  CA  PHE A 202     7821   7882   8566    610   -137    119       C\\nATOM   1208  C   PHE A 202      20.816   9.156   3.509  1.00 70.36           C\\nANISOU 1208  C   PHE A 202     8539   8718   9475    697   -242     86       C\\nATOM   1209  O   PHE A 202      20.977   8.621   4.613  1.00 72.54           O\\nANISOU 1209  O   PHE A 202     8969   8826   9768    771   -400     91       O\\nATOM   1210  CB  PHE A 202      19.992   8.047   1.402  1.00 62.85           C\\nANISOU 1210  CB  PHE A 202     7591   7872   8416    726    -97    -41       C\\nATOM   1211  CG  PHE A 202      20.499   6.659   1.671  1.00 70.17           C\\nANISOU 1211  CG  PHE A 202     8620   8639   9403    941   -273   -200       C\\nATOM   1212  CD1 PHE A 202      20.468   6.114   2.942  1.00 73.47           C\\nANISOU 1212  CD1 PHE A 202     9254   8795   9864    982   -462   -139       C\\nATOM   1213  CD2 PHE A 202      21.014   5.899   0.638  1.00 76.10           C\\nANISOU 1213  CD2 PHE A 202     9257   9501  10156   1108   -271   -423       C\\nATOM   1214  CE1 PHE A 202      20.939   4.847   3.177  1.00 78.88           C\\nANISOU 1214  CE1 PHE A 202    10067   9279  10625   1182   -682   -264       C\\nATOM   1215  CE2 PHE A 202      21.485   4.628   0.866  1.00 75.62           C\\nANISOU 1215  CE2 PHE A 202     9296   9248  10187   1343   -483   -603       C\\nATOM   1216  CZ  PHE A 202      21.447   4.100   2.137  1.00 79.28           C\\nANISOU 1216  CZ  PHE A 202    10003   9395  10724   1380   -707   -507       C\\nATOM   1217  N   ILE A 203      21.692  10.031   3.011  1.00 69.89           N\\nANISOU 1217  N   ILE A 203     8223   8871   9462    667   -169     66       N\\nATOM   1218  CA  ILE A 203      22.931  10.333   3.726  1.00 70.07           C\\nANISOU 1218  CA  ILE A 203     8101   8940   9583    743   -275      9       C\\nATOM   1219  C   ILE A 203      22.628  10.977   5.074  1.00 68.51           C\\nANISOU 1219  C   ILE A 203     8043   8585   9403    671   -375    114       C\\nATOM   1220  O   ILE A 203      23.185  10.584   6.106  1.00 61.96           O\\nANISOU 1220  O   ILE A 203     7279   7659   8605    783   -545     72       O\\nATOM   1221  CB  ILE A 203      23.843  11.227   2.870  1.00 67.00           C\\nANISOU 1221  CB  ILE A 203     7390   8840   9226    648   -158     -7       C\\nATOM   1222  CG1 ILE A 203      24.189  10.534   1.555  1.00 68.52           C\\nANISOU 1222  CG1 ILE A 203     7420   9264   9349    728    -43   -152       C\\nATOM   1223  CG2 ILE A 203      25.111  11.566   3.623  1.00 62.39           C\\nANISOU 1223  CG2 ILE A 203     6625   8319   8761    704   -276    -75       C\\nATOM   1224  CD1 ILE A 203      24.882  11.438   0.566  1.00 75.16           C\\nANISOU 1224  CD1 ILE A 203     7956  10453  10148    555    118   -121       C\\nATOM   1225  N   VAL A 204      21.738  11.974   5.082  1.00 68.09           N\\nANISOU 1225  N   VAL A 204     8035   8512   9324    499   -292    232       N\\nATOM   1226  CA  VAL A 204      21.439  12.706   6.313  1.00 64.98           C\\nANISOU 1226  CA  VAL A 204     7739   8013   8938    443   -378    276       C\\nATOM   1227  C   VAL A 204      20.881  11.767   7.375  1.00 65.55           C\\nANISOU 1227  C   VAL A 204     8061   7945   8902    504   -469    277       C\\nATOM   1228  O   VAL A 204      21.332  11.764   8.527  1.00 66.60           O\\nANISOU 1228  O   VAL A 204     8259   8027   9017    550   -610    260       O\\nATOM   1229  CB  VAL A 204      20.471  13.865   6.027  1.00 56.49           C\\nANISOU 1229  CB  VAL A 204     6664   6928   7872    291   -296    354       C\\nATOM   1230  CG1 VAL A 204      19.900  14.399   7.325  1.00 59.98           C\\nANISOU 1230  CG1 VAL A 204     7227   7276   8289    274   -375    333       C\\nATOM   1231  CG2 VAL A 204      21.185  14.972   5.267  1.00 55.27           C\\nANISOU 1231  CG2 VAL A 204     6299   6869   7831    182   -275    403       C\\nATOM   1232  N   THR A 205      19.886  10.960   7.005  1.00 66.29           N\\nANISOU 1232  N   THR A 205     8302   7982   8903    478   -403    312       N\\nATOM   1233  CA  THR A 205      19.340   9.991   7.947  1.00 66.07           C\\nANISOU 1233  CA  THR A 205     8524   7824   8753    475   -492    356       C\\nATOM   1234  C   THR A 205      20.407   9.003   8.395  1.00 73.22           C\\nANISOU 1234  C   THR A 205     9501   8627   9694    637   -693    319       C\\nATOM   1235  O   THR A 205      20.450   8.611   9.567  1.00 73.97           O\\nANISOU 1235  O   THR A 205     9780   8626   9698    635   -843    376       O\\nATOM   1236  CB  THR A 205      18.162   9.258   7.313  1.00 64.13           C\\nANISOU 1236  CB  THR A 205     8398   7536   8434    391   -397    399       C\\nATOM   1237  OG1 THR A 205      17.159  10.210   6.937  1.00 70.05           O\\nANISOU 1237  OG1 THR A 205     9065   8385   9167    268   -244    415       O\\nATOM   1238  CG2 THR A 205      17.567   8.265   8.291  1.00 59.18           C\\nANISOU 1238  CG2 THR A 205     8038   6780   7668    317   -492    485       C\\nATOM   1239  N   LEU A 206      21.282   8.594   7.476  1.00 71.22           N\\nANISOU 1239  N   LEU A 206     9095   8407   9557    784   -714    211       N\\nATOM   1240  CA  LEU A 206      22.343   7.663   7.839  1.00 69.37           C\\nANISOU 1240  CA  LEU A 206     8891   8070   9395    992   -940    126       C\\nATOM   1241  C   LEU A 206      23.325   8.302   8.810  1.00 67.69           C\\nANISOU 1241  C   LEU A 206     8584   7907   9228   1046  -1074    104       C\\nATOM   1242  O   LEU A 206      23.847   7.629   9.705  1.00 63.83           O\\nANISOU 1242  O   LEU A 206     8237   7281   8736   1166  -1318    106       O\\nATOM   1243  CB  LEU A 206      23.069   7.177   6.586  1.00 68.74           C\\nANISOU 1243  CB  LEU A 206     8603   8086   9429   1162   -911    -54       C\\nATOM   1244  CG  LEU A 206      24.254   6.253   6.864  1.00 66.60           C\\nANISOU 1244  CG  LEU A 206     8300   7728   9276   1438  -1170   -212       C\\nATOM   1245  CD1 LEU A 206      23.779   4.999   7.577  1.00 68.61           C\\nANISOU 1245  CD1 LEU A 206     8929   7645   9495   1492  -1416   -131       C\\nATOM   1246  CD2 LEU A 206      24.981   5.908   5.578  1.00 65.91           C\\nANISOU 1246  CD2 LEU A 206     7933   7826   9284   1614  -1102   -453       C\\nATOM   1247  N   LEU A 207      23.592   9.597   8.647  1.00 71.05           N\\nANISOU 1247  N   LEU A 207     8784   8507   9703    951   -950     91       N\\nATOM   1248  CA  LEU A 207      24.489  10.279   9.572  1.00 68.27           C\\nANISOU 1248  CA  LEU A 207     8336   8199   9405    979  -1088     58       C\\nATOM   1249  C   LEU A 207      23.856  10.418  10.949  1.00 68.21           C\\nANISOU 1249  C   LEU A 207     8586   8088   9244    897  -1186    154       C\\nATOM   1250  O   LEU A 207      24.552  10.352  11.967  1.00 66.32           O\\nANISOU 1250  O   LEU A 207     8392   7815   8989    976  -1395    132       O\\nATOM   1251  CB  LEU A 207      24.875  11.645   9.012  1.00 63.44           C\\nANISOU 1251  CB  LEU A 207     7441   7765   8897    855   -953     35       C\\nATOM   1252  CG  LEU A 207      25.757  11.605   7.765  1.00 58.28           C\\nANISOU 1252  CG  LEU A 207     6481   7306   8356    900   -859    -62       C\\nATOM   1253  CD1 LEU A 207      25.869  12.987   7.135  1.00 58.28           C\\nANISOU 1253  CD1 LEU A 207     6266   7458   8418    685   -713     -2       C\\nATOM   1254  CD2 LEU A 207      27.133  11.057   8.115  1.00 60.06           C\\nANISOU 1254  CD2 LEU A 207     6537   7593   8688   1106  -1049   -219       C\\nATOM   1255  N   VAL A 208      22.536  10.604  11.000  1.00 65.76           N\\nANISOU 1255  N   VAL A 208     8427   7760   8800    740  -1039    244       N\\nATOM   1256  CA  VAL A 208      21.850  10.728  12.283  1.00 70.01           C\\nANISOU 1256  CA  VAL A 208     9179   8279   9143    643  -1090    309       C\\nATOM   1257  C   VAL A 208      21.897   9.408  13.042  1.00 72.90           C\\nANISOU 1257  C   VAL A 208     9821   8505   9370    686  -1284    405       C\\nATOM   1258  O   VAL A 208      22.211   9.371  14.237  1.00 72.29           O\\nANISOU 1258  O   VAL A 208     9878   8422   9167    690  -1459    437       O\\nATOM   1259  CB  VAL A 208      20.403  11.205  12.072  1.00 62.31           C\\nANISOU 1259  CB  VAL A 208     8243   7366   8066    475   -875    344       C\\nATOM   1260  CG1 VAL A 208      19.616  11.100  13.361  1.00 57.35           C\\nANISOU 1260  CG1 VAL A 208     7821   6784   7185    363   -898    391       C\\nATOM   1261  CG2 VAL A 208      20.388  12.634  11.560  1.00 55.34           C\\nANISOU 1261  CG2 VAL A 208     7134   6567   7324    438   -769    263       C\\nATOM   1262  N   TYR A 209      21.584   8.304  12.360  1.00 67.17           N\\nANISOU 1262  N   TYR A 209     9206   7651   8663    711  -1285    458       N\\nATOM   1263  CA  TYR A 209      21.578   7.010  13.032  1.00 62.85           C\\nANISOU 1263  CA  TYR A 209     8966   6907   8008    728  -1515    581       C\\nATOM   1264  C   TYR A 209      22.975   6.598  13.468  1.00 67.38           C\\nANISOU 1264  C   TYR A 209     9528   7379   8695    962  -1822    518       C\\nATOM   1265  O   TYR A 209      23.130   5.942  14.504  1.00 76.08           O\\nANISOU 1265  O   TYR A 209    10894   8346   9666    963  -2077    640       O\\nATOM   1266  CB  TYR A 209      20.960   5.946  12.126  1.00 60.49           C\\nANISOU 1266  CB  TYR A 209     8784   6452   7749    710  -1483    623       C\\nATOM   1267  CG  TYR A 209      19.452   5.927  12.179  1.00 66.56           C\\nANISOU 1267  CG  TYR A 209     9685   7270   8334    437  -1286    750       C\\nATOM   1268  CD1 TYR A 209      18.788   5.544  13.335  1.00 66.30           C\\nANISOU 1268  CD1 TYR A 209     9921   7223   8047    229  -1351    931       C\\nATOM   1269  CD2 TYR A 209      18.693   6.292  11.078  1.00 67.85           C\\nANISOU 1269  CD2 TYR A 209     9692   7530   8559    372  -1040    687       C\\nATOM   1270  CE1 TYR A 209      17.408   5.526  13.397  1.00 71.51           C\\nANISOU 1270  CE1 TYR A 209    10651   7990   8531    -39  -1153   1024       C\\nATOM   1271  CE2 TYR A 209      17.312   6.271  11.129  1.00 67.87           C\\nANISOU 1271  CE2 TYR A 209     9776   7601   8410    135   -874    776       C\\nATOM   1272  CZ  TYR A 209      16.675   5.892  12.292  1.00 73.98           C\\nANISOU 1272  CZ  TYR A 209    10778   8387   8944    -71   -920    933       C\\nATOM   1273  OH  TYR A 209      15.301   5.875  12.350  1.00 78.65           O\\nANISOU 1273  OH  TYR A 209    11400   9107   9378   -325   -736    998       O\\nATOM   1274  N   ILE A 210      24.002   6.972  12.702  1.00 65.59           N\\nANISOU 1274  N   ILE A 210     8989   7235   8698   1151  -1815    332       N\\nATOM   1275  CA  ILE A 210      25.373   6.731  13.144  1.00 66.53           C\\nANISOU 1275  CA  ILE A 210     9020   7316   8943   1384  -2102    228       C\\nATOM   1276  C   ILE A 210      25.669   7.536  14.402  1.00 68.90           C\\nANISOU 1276  C   ILE A 210     9347   7706   9128   1318  -2205    265       C\\nATOM   1277  O   ILE A 210      26.296   7.036  15.343  1.00 66.82           O\\nANISOU 1277  O   ILE A 210     9234   7337   8820   1429  -2518    299       O\\nATOM   1278  CB  ILE A 210      26.368   7.053  12.015  1.00 68.77           C\\nANISOU 1278  CB  ILE A 210     8898   7760   9473   1556  -2020      2       C\\nATOM   1279  CG1 ILE A 210      26.237   6.043  10.879  1.00 66.91           C\\nANISOU 1279  CG1 ILE A 210     8656   7435   9331   1685  -1991    -87       C\\nATOM   1280  CG2 ILE A 210      27.792   7.062  12.545  1.00 69.56           C\\nANISOU 1280  CG2 ILE A 210     8822   7898   9711   1774  -2291   -139       C\\nATOM   1281  CD1 ILE A 210      27.237   6.254   9.771  1.00 66.26           C\\nANISOU 1281  CD1 ILE A 210     8158   7579   9440   1852  -1900   -335       C\\nATOM   1282  N   LYS A 211      25.221   8.797  14.439  1.00 68.09           N\\nANISOU 1282  N   LYS A 211     9108   7786   8977   1147  -1974    247       N\\nATOM   1283  CA  LYS A 211      25.368   9.607  15.645  1.00 72.77           C\\nANISOU 1283  CA  LYS A 211     9739   8468   9442   1077  -2066    245       C\\nATOM   1284  C   LYS A 211      24.551   9.044  16.798  1.00 75.75           C\\nANISOU 1284  C   LYS A 211    10492   8790   9501    949  -2158    418       C\\nATOM   1285  O   LYS A 211      24.918   9.225  17.965  1.00 75.16           O\\nANISOU 1285  O   LYS A 211    10526   8758   9275    949  -2353    430       O\\nATOM   1286  CB  LYS A 211      24.956  11.053  15.367  1.00 72.52           C\\nANISOU 1286  CB  LYS A 211     9503   8598   9455    934  -1825    165       C\\nATOM   1287  CG  LYS A 211      26.059  11.921  14.784  1.00 76.74           C\\nANISOU 1287  CG  LYS A 211     9682   9223  10251    997  -1830     21       C\\nATOM   1288  CD  LYS A 211      27.081  12.304  15.845  1.00 80.50           C\\nANISOU 1288  CD  LYS A 211    10106   9734  10746   1072  -2092    -66       C\\nATOM   1289  N   ILE A 212      23.444   8.363  16.492  1.00 76.82           N\\nANISOU 1289  N   ILE A 212    10821   8858   9510    813  -2022    555       N\\nATOM   1290  CA  ILE A 212      22.634   7.738  17.534  1.00 75.49           C\\nANISOU 1290  CA  ILE A 212    11004   8670   9009    629  -2092    753       C\\nATOM   1291  C   ILE A 212      23.351   6.523  18.110  1.00 78.85           C\\nANISOU 1291  C   ILE A 212    11697   8862   9401    741  -2475    889       C\\nATOM   1292  O   ILE A 212      23.426   6.348  19.332  1.00 81.23           O\\nANISOU 1292  O   ILE A 212    12234   9186   9445    664  -2673   1015       O\\nATOM   1293  CB  ILE A 212      21.244   7.368  16.983  1.00 72.94           C\\nANISOU 1293  CB  ILE A 212    10775   8353   8584    420  -1838    858       C\\nATOM   1294  CG1 ILE A 212      20.367   8.618  16.858  1.00 72.24           C\\nANISOU 1294  CG1 ILE A 212    10488   8519   8442    291  -1522    738       C\\nATOM   1295  CG2 ILE A 212      20.575   6.319  17.861  1.00 71.22           C\\nANISOU 1295  CG2 ILE A 212    10941   8062   8058    211  -1961   1112       C\\nATOM   1296  CD1 ILE A 212      18.962   8.339  16.351  1.00 65.08           C\\nANISOU 1296  CD1 ILE A 212     9627   7664   7437     90  -1276    811       C\\nATOM   1297  N   TYR A 213      23.890   5.666  17.237  1.00 80.40           N\\nANISOU 1297  N   TYR A 213    11866   8833   9849    936  -2607    855       N\\nATOM   1298  CA  TYR A 213      24.609   4.484  17.706  1.00 74.91           C\\nANISOU 1298  CA  TYR A 213    11423   7857   9182   1095  -3032    956       C\\nATOM   1299  C   TYR A 213      25.796   4.871  18.580  1.00 76.60           C\\nANISOU 1299  C   TYR A 213    11566   8127   9414   1272  -3314    873       C\\nATOM   1300  O   TYR A 213      26.091   4.197  19.574  1.00 75.58           O\\nANISOU 1300  O   TYR A 213    11741   7846   9129   1288  -3670   1037       O\\nATOM   1301  CB  TYR A 213      25.070   3.642  16.515  1.00 69.47           C\\nANISOU 1301  CB  TYR A 213    10637   6949   8811   1339  -3122    828       C\\nATOM   1302  CG  TYR A 213      25.850   2.401  16.899  1.00 82.87           C\\nANISOU 1302  CG  TYR A 213    12578   8305  10605   1567  -3612    881       C\\nATOM   1303  CD1 TYR A 213      25.198   1.248  17.317  1.00 88.00           C\\nANISOU 1303  CD1 TYR A 213    13681   8643  11110   1422  -3838   1153       C\\nATOM   1304  CD2 TYR A 213      27.237   2.376  16.828  1.00 83.04           C\\nANISOU 1304  CD2 TYR A 213    12370   8305  10877   1924  -3876    656       C\\nATOM   1305  CE1 TYR A 213      25.906   0.107  17.664  1.00 88.45           C\\nANISOU 1305  CE1 TYR A 213    13945   8382  11281   1597  -4262   1171       C\\nATOM   1306  CE2 TYR A 213      27.955   1.241  17.174  1.00 84.14           C\\nANISOU 1306  CE2 TYR A 213    12701   8139  11130   2144  -4318    655       C\\nATOM   1307  CZ  TYR A 213      27.286   0.109  17.589  1.00 88.74           C\\nANISOU 1307  CZ  TYR A 213    13713   8432  11572   1950  -4461    892       C\\nATOM   1308  OH  TYR A 213      27.998  -1.023  17.933  1.00 93.97           O\\nANISOU 1308  OH  TYR A 213    14524   8828  12351   2091  -4813    843       O\\nATOM   1309  N   ILE A 214      26.491   5.955  18.226  1.00 79.22           N\\nANISOU 1309  N   ILE A 214    11503   8668   9929   1388  -3184    634       N\\nATOM   1310  CA  ILE A 214      27.667   6.368  18.988  1.00 79.71           C\\nANISOU 1310  CA  ILE A 214    11448   8796  10043   1553  -3456    525       C\\nATOM   1311  C   ILE A 214      27.278   6.769  20.407  1.00 82.99           C\\nANISOU 1311  C   ILE A 214    12112   9325  10094   1359  -3536    663       C\\nATOM   1312  O   ILE A 214      27.993   6.468  21.373  1.00 77.18           O\\nANISOU 1312  O   ILE A 214    11526   8534   9267   1459  -3903    709       O\\nATOM   1313  CB  ILE A 214      28.405   7.505  18.256  1.00 74.49           C\\nANISOU 1313  CB  ILE A 214    10301   8350   9651   1642  -3272    259       C\\nATOM   1314  CG1 ILE A 214      28.993   6.995  16.944  1.00 73.37           C\\nANISOU 1314  CG1 ILE A 214     9897   8156   9825   1855  -3239    102       C\\nATOM   1315  CG2 ILE A 214      29.508   8.085  19.125  1.00 79.54           C\\nANISOU 1315  CG2 ILE A 214    10802   9091  10328   1753  -3532    141       C\\nATOM   1316  CD1 ILE A 214      29.840   8.022  16.221  1.00 79.87           C\\nANISOU 1316  CD1 ILE A 214    10233   9224  10891   1906  -3079   -130       C\\nATOM   1317  N   VAL A 215      26.138   7.447  20.558  1.00 80.48           N\\nANISOU 1317  N   VAL A 215    11834   9193   9553   1092  -3207    710       N\\nATOM   1318  CA  VAL A 215      25.693   7.866  21.883  1.00 80.01           C\\nANISOU 1318  CA  VAL A 215    11978   9313   9108    905  -3241    790       C\\nATOM   1319  C   VAL A 215      25.303   6.658  22.722  1.00 86.31           C\\nANISOU 1319  C   VAL A 215    13235   9978   9582    774  -3480   1098       C\\nATOM   1320  O   VAL A 215      25.668   6.557  23.900  1.00 89.76           O\\nANISOU 1320  O   VAL A 215    13882  10466   9758    750  -3755   1189       O\\nATOM   1321  CB  VAL A 215      24.532   8.868  21.764  1.00 69.82           C\\nANISOU 1321  CB  VAL A 215    10575   8272   7681    685  -2829    710       C\\nATOM   1322  CG1 VAL A 215      23.873   9.073  23.115  1.00 70.46           C\\nANISOU 1322  CG1 VAL A 215    10891   8582   7299    474  -2833    787       C\\nATOM   1323  CG2 VAL A 215      25.035  10.188  21.201  1.00 70.96           C\\nANISOU 1323  CG2 VAL A 215    10323   8520   8117    791  -2692    435       C\\nATOM   1324  N   LEU A 216      24.556   5.722  22.131  1.00 88.27           N\\nANISOU 1324  N   LEU A 216    13660  10047   9830    664  -3400   1278       N\\nATOM   1325  CA  LEU A 216      24.129   4.539  22.870  1.00 81.42           C\\nANISOU 1325  CA  LEU A 216    13257   9014   8666    480  -3641   1616       C\\nATOM   1326  C   LEU A 216      25.314   3.682  23.294  1.00 84.21           C\\nANISOU 1326  C   LEU A 216    13802   9063   9129    728  -4180   1700       C\\nATOM   1327  O   LEU A 216      25.268   3.046  24.353  1.00 81.69           O\\nANISOU 1327  O   LEU A 216    13836   8687   8514    577  -4427   1947       O\\nATOM   1328  CB  LEU A 216      23.148   3.725  22.025  1.00 83.40           C\\nANISOU 1328  CB  LEU A 216    13629   9094   8967    318  -3470   1765       C\\nATOM   1329  CG  LEU A 216      21.846   4.440  21.657  1.00 89.34           C\\nANISOU 1329  CG  LEU A 216    14218  10142   9584     56  -2973   1707       C\\nATOM   1330  CD1 LEU A 216      21.017   3.625  20.676  1.00 88.79           C\\nANISOU 1330  CD1 LEU A 216    14221   9881   9633    -62  -2839   1814       C\\nATOM   1331  CD2 LEU A 216      21.046   4.736  22.911  1.00 97.88           C\\nANISOU 1331  CD2 LEU A 216    15482  11550  10159   -274  -2870   1850       C\\nATOM   1332  N   ARG A 217      26.382   3.651  22.492  1.00 81.94           N\\nANISOU 1332  N   ARG A 217    13237   8618   9279   1094  -4322   1464       N\\nATOM   1333  CA  ARG A 217      27.561   2.877  22.871  1.00 83.41           C\\nANISOU 1333  CA  ARG A 217    13486   8566   9641   1348  -4750   1435       C\\nATOM   1334  C   ARG A 217      28.345   3.556  23.985  1.00 85.61           C\\nANISOU 1334  C   ARG A 217    13711   9042   9775   1403  -4934   1364       C\\nATOM   1335  O   ARG A 217      28.952   2.873  24.816  1.00 80.30           O\\nANISOU 1335  O   ARG A 217    13221   8234   9057   1442  -5229   1443       O\\nATOM   1336  CB  ARG A 217      28.460   2.641  21.658  1.00 74.00           C\\nANISOU 1336  CB  ARG A 217    11946   7228   8942   1710  -4789   1141       C\\nATOM   1337  N   ARG A 218      28.347   4.891  24.021  1.00 77.47           N\\nANISOU 1337  N   ARG A 218    12427   8320   8687   1399  -4771   1198       N\\nATOM   1338  CA  ARG A 218      28.948   5.589  25.152  1.00 79.95           C\\nANISOU 1338  CA  ARG A 218    12725   8839   8812   1411  -4955   1127       C\\nATOM   1339  C   ARG A 218      28.170   5.328  26.435  1.00 82.04           C\\nANISOU 1339  C   ARG A 218    13403   9226   8543   1087  -4970   1402       C\\nATOM   1340  O   ARG A 218      28.765   5.243  27.517  1.00 84.60           O\\nANISOU 1340  O   ARG A 218    13838   9600   8707   1097  -5207   1432       O\\nATOM   1341  CB  ARG A 218      29.022   7.089  24.868  1.00 75.14           C\\nANISOU 1341  CB  ARG A 218    11692   8536   8320   1397  -4623    823       C\\nATOM   1342  N   ARG A 219      26.847   5.179  26.326  1.00 85.99           N\\nANISOU 1342  N   ARG A 219    14111   9803   8758    785  -4704   1599       N\\nATOM   1343  CA  ARG A 219      26.016   4.885  27.490  1.00 84.46           C\\nANISOU 1343  CA  ARG A 219    14260   9795   8035    425  -4645   1858       C\\nATOM   1344  C   ARG A 219      26.340   3.511  28.066  1.00 86.08           C\\nANISOU 1344  C   ARG A 219    14765   9710   8230    380  -4920   2118       C\\nATOM   1345  O   ARG A 219      26.501   3.361  29.283  1.00 90.06           O\\nANISOU 1345  O   ARG A 219    15467  10337   8414    256  -5076   2247       O\\nATOM   1346  CB  ARG A 219      24.539   4.978  27.102  1.00 85.75           C\\nANISOU 1346  CB  ARG A 219    14494  10127   7961    100  -4243   1970       C\\nATOM   1347  CG  ARG A 219      23.566   4.985  28.270  1.00 97.90           C\\nANISOU 1347  CG  ARG A 219    16277  12019   8900   -302  -4086   2160       C\\nATOM   1348  CD  ARG A 219      22.137   5.191  27.780  1.00103.51           C\\nANISOU 1348  CD  ARG A 219    16923  12951   9455   -597  -3619   2177       C\\nATOM   1349  NE  ARG A 219      22.015   6.380  26.940  1.00103.98           N\\nANISOU 1349  NE  ARG A 219    16513  13152   9842   -422  -3259   1780       N\\nATOM   1350  CZ  ARG A 219      21.746   7.599  27.400  1.00102.81           C\\nANISOU 1350  CZ  ARG A 219    16138  13388   9536   -439  -3032   1497       C\\nATOM   1351  NH1 ARG A 219      21.567   7.793  28.700  1.00112.25           N\\nANISOU 1351  NH1 ARG A 219    17509  14920  10223   -616  -3093   1534       N\\nATOM   1352  NH2 ARG A 219      21.656   8.624  26.563  1.00 90.07           N\\nANISOU 1352  NH2 ARG A 219    14137  11821   8266   -282  -2765   1173       N\\nATOM   1353  N   ARG A 220      26.443   2.493  27.205  1.00 85.93           N\\nANISOU 1353  N   ARG A 220    14788   9305   8558    483  -5002   2177       N\\nATOM   1354  CA  ARG A 220      26.753   1.145  27.680  1.00 92.53           C\\nANISOU 1354  CA  ARG A 220    15922   9808   9426    451  -5313   2391       C\\nATOM   1355  C   ARG A 220      28.118   1.092  28.355  1.00 98.18           C\\nANISOU 1355  C   ARG A 220    16600  10438  10265    730  -5700   2278       C\\nATOM   1356  O   ARG A 220      28.296   0.384  29.353  1.00 99.06           O\\nANISOU 1356  O   ARG A 220    17008  10452  10178    616  -5960   2492       O\\nATOM   1357  CB  ARG A 220      26.686   0.149  26.522  1.00 94.83           C\\nANISOU 1357  CB  ARG A 220    16221   9701  10109    561  -5350   2378       C\\nATOM   1358  CG  ARG A 220      25.281  -0.055  25.969  1.00100.75           C\\nANISOU 1358  CG  ARG A 220    17071  10487  10720    234  -5015   2543       C\\nATOM   1359  CD  ARG A 220      25.299  -0.715  24.596  1.00102.73           C\\nANISOU 1359  CD  ARG A 220    17220  10409  11403    417  -5011   2417       C\\nATOM   1360  NE  ARG A 220      23.971  -0.712  23.986  1.00105.76           N\\nANISOU 1360  NE  ARG A 220    17640  10872  11673    124  -4663   2533       N\\nATOM   1361  CZ  ARG A 220      23.743  -0.876  22.687  1.00111.13           C\\nANISOU 1361  CZ  ARG A 220    18166  11401  12658    249  -4533   2393       C\\nATOM   1362  NH1 ARG A 220      24.756  -1.052  21.850  1.00115.91           N\\nANISOU 1362  NH1 ARG A 220    18552  11801  13687    664  -4699   2115       N\\nATOM   1363  NH2 ARG A 220      22.500  -0.857  22.220  1.00109.07           N\\nANISOU 1363  NH2 ARG A 220    17943  11230  12267    -44  -4223   2509       N\\nATOM   1364  N   LYS A 221      29.096   1.832  27.826  1.00 87.90           N\\nANISOU 1364  N   LYS A 221    14922   9183   9293   1081  -5746   1943       N\\nATOM   1365  CA  LYS A 221      30.396   1.903  28.485  1.00 91.01           C\\nANISOU 1365  CA  LYS A 221    15227   9552   9800   1332  -6088   1803       C\\nATOM   1366  C   LYS A 221      30.311   2.643  29.815  1.00 92.81           C\\nANISOU 1366  C   LYS A 221    15563  10123   9576   1152  -6111   1881       C\\nATOM   1367  O   LYS A 221      31.080   2.348  30.738  1.00 97.14           O\\nANISOU 1367  O   LYS A 221    16229  10626  10054   1227  -6434   1922       O\\nATOM   1368  CB  LYS A 221      31.420   2.575  27.569  1.00 88.24           C\\nANISOU 1368  CB  LYS A 221    14391   9229   9907   1702  -6082   1409       C\\nATOM   1369  N   ARG A 222      29.386   3.599  29.935  1.00 89.90           N\\nANISOU 1369  N   ARG A 222    15156  10111   8890    923  -5782   1877       N\\nATOM   1370  CA  ARG A 222      29.220   4.328  31.190  1.00 91.86           C\\nANISOU 1370  CA  ARG A 222    15494  10740   8669    746  -5774   1897       C\\nATOM   1371  C   ARG A 222      28.375   3.544  32.190  1.00 96.10           C\\nANISOU 1371  C   ARG A 222    16450  11352   8712    379  -5763   2271       C\\nATOM   1372  O   ARG A 222      28.677   3.536  33.390  1.00100.34           O\\nANISOU 1372  O   ARG A 222    17145  12050   8928    306  -5948   2359       O\\nATOM   1373  CB  ARG A 222      28.596   5.698  30.923  1.00 87.62           C\\nANISOU 1373  CB  ARG A 222    14726  10572   7995    668  -5443   1670       C\\nATOM   1374  N   ASN A1002      27.322   2.874  31.712  1.00 85.72           N\\nANISOU 1374  N   ASN A1002    12716   9421  10431    154  -1889   1403       N\\nATOM   1375  CA  ASN A1002      26.456   2.104  32.601  1.00 78.54           C\\nANISOU 1375  CA  ASN A1002    11488   8720   9636    336  -1772   1042       C\\nATOM   1376  C   ASN A1002      27.206   0.951  33.259  1.00 74.17           C\\nANISOU 1376  C   ASN A1002    10829   8409   8943    253  -1283    980       C\\nATOM   1377  O   ASN A1002      26.974   0.646  34.435  1.00 77.99           O\\nANISOU 1377  O   ASN A1002    11066   9013   9552    361  -1151    748       O\\nATOM   1378  CB  ASN A1002      25.242   1.584  31.828  1.00 72.27           C\\nANISOU 1378  CB  ASN A1002    10694   8018   8747    370  -1959    956       C\\nATOM   1379  CG  ASN A1002      24.296   2.693  31.414  1.00 85.39           C\\nANISOU 1379  CG  ASN A1002    12363   9440  10641    548  -2522    954       C\\nATOM   1380  OD1 ASN A1002      24.569   3.871  31.643  1.00 91.93           O\\nANISOU 1380  OD1 ASN A1002    13249   9977  11701    641  -2774   1033       O\\nATOM   1381  ND2 ASN A1002      23.179   2.324  30.796  1.00 95.12           N\\nANISOU 1381  ND2 ASN A1002    13533  10764  11844    599  -2763    857       N\\nATOM   1382  N   ILE A1003      28.104   0.295  32.520  1.00 69.88           N\\nANISOU 1382  N   ILE A1003    10476   7942   8134     67  -1017   1180       N\\nATOM   1383  CA  ILE A1003      28.844  -0.824  33.094  1.00 75.25           C\\nANISOU 1383  CA  ILE A1003    11058   8796   8739     40   -607   1126       C\\nATOM   1384  C   ILE A1003      29.846  -0.336  34.137  1.00 79.70           C\\nANISOU 1384  C   ILE A1003    11473   9334   9474     69   -527   1154       C\\nATOM   1385  O   ILE A1003      30.117  -1.035  35.121  1.00 81.90           O\\nANISOU 1385  O   ILE A1003    11597   9734   9788    131   -334   1048       O\\nATOM   1386  CB  ILE A1003      29.526  -1.644  31.981  1.00 76.66           C\\nANISOU 1386  CB  ILE A1003    11445   9056   8624   -116   -342   1259       C\\nATOM   1387  CG1 ILE A1003      30.131  -2.927  32.553  1.00 83.23           C\\nANISOU 1387  CG1 ILE A1003    12171  10007   9446    -76     25   1164       C\\nATOM   1388  CG2 ILE A1003      30.599  -0.830  31.276  1.00 75.86           C\\nANISOU 1388  CG2 ILE A1003    11492   8897   8434   -279   -312   1524       C\\nATOM   1389  CD1 ILE A1003      30.765  -3.812  31.509  1.00 89.05           C\\nANISOU 1389  CD1 ILE A1003    13083  10813   9939   -170    311   1194       C\\nATOM   1390  N   PHE A1004      30.403   0.862  33.954  1.00 72.73           N\\nANISOU 1390  N   PHE A1004    10657   8281   8697      0   -708   1309       N\\nATOM   1391  CA  PHE A1004      31.300   1.419  34.961  1.00 72.86           C\\nANISOU 1391  CA  PHE A1004    10523   8260   8901      1   -698   1302       C\\nATOM   1392  C   PHE A1004      30.561   1.658  36.271  1.00 75.78           C\\nANISOU 1392  C   PHE A1004    10709   8641   9442    194   -837   1009       C\\nATOM   1393  O   PHE A1004      31.045   1.293  37.349  1.00 75.51           O\\nANISOU 1393  O   PHE A1004    10525   8740   9424    231   -703    911       O\\nATOM   1394  CB  PHE A1004      31.920   2.718  34.446  1.00 74.85           C\\nANISOU 1394  CB  PHE A1004    10908   8273   9256   -164   -904   1525       C\\nATOM   1395  CG  PHE A1004      32.831   3.387  35.431  1.00 80.49           C\\nANISOU 1395  CG  PHE A1004    11471   8921  10192   -205   -951   1497       C\\nATOM   1396  CD1 PHE A1004      34.093   2.876  35.685  1.00 79.31           C\\nANISOU 1396  CD1 PHE A1004    11166   8951  10018   -317   -675   1584       C\\nATOM   1397  CD2 PHE A1004      32.429   4.533  36.100  1.00 83.97           C\\nANISOU 1397  CD2 PHE A1004    11907   9110  10888   -118  -1297   1351       C\\nATOM   1398  CE1 PHE A1004      34.938   3.492  36.589  1.00 82.95           C\\nANISOU 1398  CE1 PHE A1004    11465   9368  10684   -377   -769   1550       C\\nATOM   1399  CE2 PHE A1004      33.269   5.154  37.007  1.00 85.07           C\\nANISOU 1399  CE2 PHE A1004    11928   9181  11215   -183  -1370   1289       C\\nATOM   1400  CZ  PHE A1004      34.525   4.633  37.251  1.00 84.25           C\\nANISOU 1400  CZ  PHE A1004    11666   9282  11062   -331  -1119   1402       C\\nATOM   1401  N   GLU A1005      29.376   2.270  36.194  1.00 75.34           N\\nANISOU 1401  N   GLU A1005    10654   8467   9503    325  -1114    852       N\\nATOM   1402  CA  GLU A1005      28.576   2.488  37.395  1.00 80.23           C\\nANISOU 1402  CA  GLU A1005    11062   9155  10266    516  -1188    504       C\\nATOM   1403  C   GLU A1005      28.115   1.169  38.000  1.00 86.02           C\\nANISOU 1403  C   GLU A1005    11656  10202  10825    527   -889    366       C\\nATOM   1404  O   GLU A1005      28.046   1.030  39.227  1.00 90.45           O\\nANISOU 1404  O   GLU A1005    12070  10923  11372    580   -788    167       O\\nATOM   1405  CB  GLU A1005      27.375   3.375  37.076  1.00 77.92           C\\nANISOU 1405  CB  GLU A1005    10741   8676  10189    694  -1544    334       C\\nATOM   1406  CG  GLU A1005      27.742   4.831  36.890  1.00 84.80           C\\nANISOU 1406  CG  GLU A1005    11751   9159  11311    720  -1903    409       C\\nATOM   1407  CD  GLU A1005      28.491   5.393  38.081  1.00 89.89           C\\nANISOU 1407  CD  GLU A1005    12315   9761  12076    724  -1883    248       C\\nATOM   1408  OE1 GLU A1005      27.991   5.262  39.219  1.00 89.61           O\\nANISOU 1408  OE1 GLU A1005    12069   9916  12064    880  -1796   -120       O\\nATOM   1409  OE2 GLU A1005      29.591   5.949  37.880  1.00 88.50           O\\nANISOU 1409  OE2 GLU A1005    12285   9394  11947    539  -1944    483       O\\nATOM   1410  N   MET A1006      27.798   0.187  37.153  1.00 78.13           N\\nANISOU 1410  N   MET A1006    10736   9284   9667    448   -755    474       N\\nATOM   1411  CA  MET A1006      27.337  -1.104  37.657  1.00 72.09           C\\nANISOU 1411  CA  MET A1006     9881   8748   8762    410   -494    376       C\\nATOM   1412  C   MET A1006      28.381  -1.755  38.553  1.00 75.65           C\\nANISOU 1412  C   MET A1006    10336   9295   9114    362   -262    468       C\\nATOM   1413  O   MET A1006      28.038  -2.402  39.549  1.00 76.42           O\\nANISOU 1413  O   MET A1006    10345   9565   9126    348   -119    363       O\\nATOM   1414  CB  MET A1006      26.994  -2.033  36.497  1.00 63.48           C\\nANISOU 1414  CB  MET A1006     8926   7661   7531    307   -419    476       C\\nATOM   1415  CG  MET A1006      26.279  -3.292  36.913  1.00 70.23           C\\nANISOU 1415  CG  MET A1006     9703   8684   8298    231   -215    360       C\\nATOM   1416  SD  MET A1006      26.609  -4.663  35.798  1.00 70.93           S\\nANISOU 1416  SD  MET A1006    10037   8714   8198     86    -29    502       S\\nATOM   1417  CE  MET A1006      25.235  -5.747  36.183  1.00 79.60           C\\nANISOU 1417  CE  MET A1006    11010   9948   9288    -46     55    311       C\\nATOM   1418  N   LEU A1007      29.660  -1.591  38.223  1.00 74.32           N\\nANISOU 1418  N   LEU A1007    10257   9030   8951    321   -234    678       N\\nATOM   1419  CA  LEU A1007      30.716  -2.231  38.992  1.00 72.19           C\\nANISOU 1419  CA  LEU A1007     9955   8841   8633    310    -74    777       C\\nATOM   1420  C   LEU A1007      31.310  -1.346  40.078  1.00 77.91           C\\nANISOU 1420  C   LEU A1007    10574   9585   9442    343   -217    715       C\\nATOM   1421  O   LEU A1007      31.846  -1.881  41.054  1.00 81.18           O\\nANISOU 1421  O   LEU A1007    10944  10120   9781    352   -154    740       O\\nATOM   1422  CB  LEU A1007      31.835  -2.718  38.066  1.00 71.02           C\\nANISOU 1422  CB  LEU A1007     9882   8633   8470    261     76    992       C\\nATOM   1423  CG  LEU A1007      31.556  -4.102  37.475  1.00 67.80           C\\nANISOU 1423  CG  LEU A1007     9585   8237   7941    251    288   1010       C\\nATOM   1424  CD1 LEU A1007      30.727  -4.015  36.198  1.00 65.13           C\\nANISOU 1424  CD1 LEU A1007     9386   7844   7514    183    249    974       C\\nATOM   1425  CD2 LEU A1007      32.848  -4.848  37.236  1.00 68.79           C\\nANISOU 1425  CD2 LEU A1007     9698   8348   8090    287    481   1140       C\\nATOM   1426  N   ARG A1008      31.232  -0.018  39.954  1.00 81.15           N\\nANISOU 1426  N   ARG A1008    10972   9855  10007    355   -447    635       N\\nATOM   1427  CA  ARG A1008      31.610   0.793  41.106  1.00 79.83           C\\nANISOU 1427  CA  ARG A1008    10721   9701   9912    383   -602    485       C\\nATOM   1428  C   ARG A1008      30.583   0.693  42.224  1.00 79.95           C\\nANISOU 1428  C   ARG A1008    10660   9903   9815    473   -581    181       C\\nATOM   1429  O   ARG A1008      30.878   1.089  43.357  1.00 82.62           O\\nANISOU 1429  O   ARG A1008    10953  10337  10104    486   -655     22       O\\nATOM   1430  CB  ARG A1008      31.814   2.257  40.711  1.00 75.25           C\\nANISOU 1430  CB  ARG A1008    10178   8848   9565    361   -878    461       C\\nATOM   1431  CG  ARG A1008      30.548   3.009  40.384  1.00 84.73           C\\nANISOU 1431  CG  ARG A1008    11405   9893  10893    488  -1070    258       C\\nATOM   1432  CD  ARG A1008      30.759   4.502  40.562  1.00 91.79           C\\nANISOU 1432  CD  ARG A1008    12342  10481  12053    509  -1399    147       C\\nATOM   1433  NE  ARG A1008      30.802   4.870  41.973  1.00 97.78           N\\nANISOU 1433  NE  ARG A1008    12996  11338  12815    587  -1451   -187       N\\nATOM   1434  CZ  ARG A1008      29.731   5.209  42.684  1.00100.58           C\\nANISOU 1434  CZ  ARG A1008    13254  11756  13206    785  -1504   -595       C\\nATOM   1435  NH1 ARG A1008      28.534   5.231  42.111  1.00 94.43           N\\nANISOU 1435  NH1 ARG A1008    12420  10935  12522    941  -1541   -707       N\\nATOM   1436  NH2 ARG A1008      29.857   5.526  43.966  1.00105.64           N\\nANISOU 1436  NH2 ARG A1008    13834  12529  13777    825  -1520   -917       N\\nATOM   1437  N   ILE A1009      29.394   0.171  41.926  1.00 74.25           N\\nANISOU 1437  N   ILE A1009     9910   9267   9034    507   -473     81       N\\nATOM   1438  CA  ILE A1009      28.416  -0.151  42.956  1.00 75.30           C\\nANISOU 1438  CA  ILE A1009     9929   9661   9019    531   -350   -186       C\\nATOM   1439  C   ILE A1009      28.680  -1.535  43.536  1.00 78.79           C\\nANISOU 1439  C   ILE A1009    10438  10305   9194    403   -107     -8       C\\nATOM   1440  O   ILE A1009      28.534  -1.752  44.743  1.00 85.17           O\\nANISOU 1440  O   ILE A1009    11227  11348   9787    355    -20   -120       O\\nATOM   1441  CB  ILE A1009      26.996  -0.039  42.373  1.00 72.07           C\\nANISOU 1441  CB  ILE A1009     9394   9267   8722    603   -364   -387       C\\nATOM   1442  CG1 ILE A1009      26.670   1.415  42.030  1.00 73.75           C\\nANISOU 1442  CG1 ILE A1009     9547   9243   9230    783   -675   -591       C\\nATOM   1443  CG2 ILE A1009      25.968  -0.620  43.332  1.00 70.49           C\\nANISOU 1443  CG2 ILE A1009     9027   9408   8349    556   -136   -634       C\\nATOM   1444  CD1 ILE A1009      25.423   1.572  41.190  1.00 76.17           C\\nANISOU 1444  CD1 ILE A1009     9730   9499   9713    890   -796   -718       C\\nATOM   1445  N   ASP A1010      29.079  -2.490  42.694  1.00 72.06           N\\nANISOU 1445  N   ASP A1010     9694   9350   8336    343     -7    269       N\\nATOM   1446  CA  ASP A1010      29.286  -3.870  43.127  1.00 72.56           C\\nANISOU 1446  CA  ASP A1010     9858   9501   8210    243    179    457       C\\nATOM   1447  C   ASP A1010      30.708  -4.106  43.629  1.00 75.95           C\\nANISOU 1447  C   ASP A1010    10352   9894   8612    272    117    675       C\\nATOM   1448  O   ASP A1010      30.908  -4.550  44.763  1.00 79.91           O\\nANISOU 1448  O   ASP A1010    10905  10541   8916    226    124    730       O\\nATOM   1449  CB  ASP A1010      28.966  -4.834  41.979  1.00 68.87           C\\nANISOU 1449  CB  ASP A1010     9481   8902   7784    190    300    582       C\\nATOM   1450  CG  ASP A1010      27.482  -4.951  41.709  1.00 73.05           C\\nANISOU 1450  CG  ASP A1010     9921   9528   8308    113    358    385       C\\nATOM   1451  OD1 ASP A1010      26.693  -4.307  42.432  1.00 67.48           O\\nANISOU 1451  OD1 ASP A1010     9046   9009   7582    124    341    140       O\\nATOM   1452  OD2 ASP A1010      27.105  -5.691  40.773  1.00 78.54           O\\nANISOU 1452  OD2 ASP A1010    10691  10123   9026     43    418    440       O\\nATOM   1453  N   GLU A1011      31.702  -3.824  42.788  1.00 76.16           N\\nANISOU 1453  N   GLU A1011    10363   9749   8825    334     50    808       N\\nATOM   1454  CA  GLU A1011      33.088  -4.089  43.149  1.00 80.16           C\\nANISOU 1454  CA  GLU A1011    10842  10236   9377    379    -14    997       C\\nATOM   1455  C   GLU A1011      33.663  -2.965  44.003  1.00 86.62           C\\nANISOU 1455  C   GLU A1011    11560  11131  10222    377   -238    897       C\\nATOM   1456  O   GLU A1011      34.212  -3.213  45.081  1.00 98.58           O\\nANISOU 1456  O   GLU A1011    13076  12768  11614    380   -345    952       O\\nATOM   1457  CB  GLU A1011      33.926  -4.284  41.885  1.00 82.54           C\\nANISOU 1457  CB  GLU A1011    11111  10383   9867    418     68   1140       C\\nATOM   1458  CG  GLU A1011      35.344  -4.765  42.134  1.00 89.74           C\\nANISOU 1458  CG  GLU A1011    11913  11291  10894    502     40   1313       C\\nATOM   1459  CD  GLU A1011      35.393  -6.223  42.539  1.00 95.34           C\\nANISOU 1459  CD  GLU A1011    12731  11959  11534    586    111   1445       C\\nATOM   1460  OE1 GLU A1011      35.895  -6.518  43.646  1.00 99.56           O\\nANISOU 1460  OE1 GLU A1011    13255  12559  12013    632    -51   1549       O\\nATOM   1461  OE2 GLU A1011      34.920  -7.072  41.751  1.00 94.59           O\\nANISOU 1461  OE2 GLU A1011    12763  11742  11436    596    295   1450       O\\nATOM   1462  N   GLY A1012      33.549  -1.725  43.534  1.00 83.15           N\\nANISOU 1462  N   GLY A1012    11062  10592   9938    362   -351    758       N\\nATOM   1463  CA  GLY A1012      34.064  -0.590  44.272  1.00 80.42           C\\nANISOU 1463  CA  GLY A1012    10644  10253   9660    339   -589    621       C\\nATOM   1464  C   GLY A1012      35.145   0.176  43.536  1.00 76.41           C\\nANISOU 1464  C   GLY A1012    10041   9573   9418    270   -701    745       C\\nATOM   1465  O   GLY A1012      36.026  -0.422  42.909  1.00 75.35           O\\nANISOU 1465  O   GLY A1012     9829   9430   9369    254   -588    972       O\\nATOM   1466  N   LEU A1013      35.090   1.505  43.610  1.00 72.47           N\\nANISOU 1466  N   LEU A1013     9539   8928   9066    216   -914    581       N\\nATOM   1467  CA  LEU A1013      36.059   2.381  42.960  1.00 75.06           C\\nANISOU 1467  CA  LEU A1013     9799   9069   9653     69  -1037    711       C\\nATOM   1468  C   LEU A1013      37.076   2.842  43.998  1.00 85.43           C\\nANISOU 1468  C   LEU A1013    10980  10447  11031    -12  -1266    645       C\\nATOM   1469  O   LEU A1013      36.730   3.569  44.935  1.00 92.30           O\\nANISOU 1469  O   LEU A1013    11906  11301  11864      3  -1478    364       O\\nATOM   1470  CB  LEU A1013      35.362   3.575  42.309  1.00 76.93           C\\nANISOU 1470  CB  LEU A1013    10164   9014  10053     35  -1188    614       C\\nATOM   1471  CG  LEU A1013      36.264   4.677  41.743  1.00 81.85           C\\nANISOU 1471  CG  LEU A1013    10778   9382  10939   -188  -1361    759       C\\nATOM   1472  CD1 LEU A1013      37.119   4.145  40.607  1.00 83.65           C\\nANISOU 1472  CD1 LEU A1013    10936   9672  11176   -345  -1119   1104       C\\nATOM   1473  CD2 LEU A1013      35.444   5.879  41.290  1.00 79.42           C\\nANISOU 1473  CD2 LEU A1013    10661   8711  10803   -183  -1600    657       C\\nATOM   1474  N   ARG A1014      38.324   2.416  43.830  1.00 82.30           N\\nANISOU 1474  N   ARG A1014    10388  10143  10740    -92  -1229    865       N\\nATOM   1475  CA  ARG A1014      39.431   2.846  44.673  1.00 87.70           C\\nANISOU 1475  CA  ARG A1014    10885  10900  11537   -200  -1487    834       C\\nATOM   1476  C   ARG A1014      40.374   3.720  43.858  1.00 91.11           C\\nANISOU 1476  C   ARG A1014    11154  11170  12293   -454  -1533    970       C\\nATOM   1477  O   ARG A1014      40.854   3.301  42.800  1.00 93.58           O\\nANISOU 1477  O   ARG A1014    11348  11510  12699   -513  -1278   1201       O\\nATOM   1478  CB  ARG A1014      40.189   1.647  45.242  1.00 89.70           C\\nANISOU 1478  CB  ARG A1014    10969  11409  11702    -83  -1465    977       C\\nATOM   1479  CG  ARG A1014      39.445   0.867  46.311  1.00 95.14           C\\nANISOU 1479  CG  ARG A1014    11845  12266  12037     80  -1493    888       C\\nATOM   1480  CD  ARG A1014      40.338   0.658  47.527  1.00103.70           C\\nANISOU 1480  CD  ARG A1014    12817  13547  13039     82  -1799    903       C\\nATOM   1481  NE  ARG A1014      39.801  -0.327  48.462  1.00107.67           N\\nANISOU 1481  NE  ARG A1014    13522  14230  13160    204  -1802    939       N\\nATOM   1482  CZ  ARG A1014      40.399  -0.677  49.597  1.00111.85           C\\nANISOU 1482  CZ  ARG A1014    14048  14948  13504    219  -2094    997       C\\nATOM   1483  NH1 ARG A1014      41.553  -0.119  49.939  1.00113.46           N\\nANISOU 1483  NH1 ARG A1014    14008  15196  13905    140  -2424    984       N\\nATOM   1484  NH2 ARG A1014      39.844  -1.584  50.391  1.00112.62           N\\nANISOU 1484  NH2 ARG A1014    14392  15192  13208    282  -2078   1085       N\\nATOM   1485  N   LEU A1015      40.648   4.926  44.357  1.00 92.65           N\\nANISOU 1485  N   LEU A1015    11353  11202  12646   -633  -1845    811       N\\nATOM   1486  CA  LEU A1015      41.453   5.897  43.627  1.00 98.42           C\\nANISOU 1486  CA  LEU A1015    11974  11728  13694   -955  -1914    952       C\\nATOM   1487  C   LEU A1015      42.928   5.886  44.013  1.00100.85           C\\nANISOU 1487  C   LEU A1015    11893  12218  14209  -1148  -2036   1034       C\\nATOM   1488  O   LEU A1015      43.750   6.434  43.268  1.00 98.40           O\\nANISOU 1488  O   LEU A1015    11399  11829  14161  -1460  -1984   1214       O\\nATOM   1489  CB  LEU A1015      40.885   7.309  43.827  1.00 99.65           C\\nANISOU 1489  CB  LEU A1015    12381  11497  13985  -1071  -2220    736       C\\nATOM   1490  CG  LEU A1015      39.471   7.567  43.292  1.00 99.54           C\\nANISOU 1490  CG  LEU A1015    12694  11242  13885   -893  -2166    655       C\\nATOM   1491  CD1 LEU A1015      39.000   8.964  43.667  1.00 99.18           C\\nANISOU 1491  CD1 LEU A1015    12859  10780  14044   -939  -2532    377       C\\nATOM   1492  CD2 LEU A1015      39.410   7.369  41.782  1.00 97.70           C\\nANISOU 1492  CD2 LEU A1015    12526  10927  13670   -996  -1904   1008       C\\nATOM   1493  N   LYS A1016      43.285   5.285  45.145  1.00105.59           N\\nANISOU 1493  N   LYS A1016    12353  13074  14693   -995  -2209    921       N\\nATOM   1494  CA  LYS A1016      44.673   5.127  45.549  1.00101.07           C\\nANISOU 1494  CA  LYS A1016    11354  12717  14330  -1119  -2373    997       C\\nATOM   1495  C   LYS A1016      45.057   3.654  45.506  1.00 97.42           C\\nANISOU 1495  C   LYS A1016    10673  12549  13792   -837  -2171   1168       C\\nATOM   1496  O   LYS A1016      44.204   2.765  45.581  1.00 93.98           O\\nANISOU 1496  O   LYS A1016    10480  12152  13076   -558  -2006   1179       O\\nATOM   1497  CB  LYS A1016      44.913   5.693  46.953  1.00 96.36           C\\nANISOU 1497  CB  LYS A1016    10775  12159  13680  -1180  -2856    730       C\\nATOM   1498  N   ILE A1017      46.361   3.401  45.382  1.00 93.92           N\\nANISOU 1498  N   ILE A1017     9745  12296  13643   -915  -2196   1291       N\\nATOM   1499  CA  ILE A1017      46.835   2.030  45.257  1.00 95.27           C\\nANISOU 1499  CA  ILE A1017     9663  12692  13845   -609  -2025   1434       C\\nATOM   1500  C   ILE A1017      46.498   1.247  46.517  1.00 93.58           C\\nANISOU 1500  C   ILE A1017     9634  12578  13344   -317  -2322   1390       C\\nATOM   1501  O   ILE A1017      46.630   1.745  47.643  1.00 98.49           O\\nANISOU 1501  O   ILE A1017    10306  13255  13861   -400  -2751   1258       O\\nATOM   1502  CB  ILE A1017      48.346   2.013  44.968  1.00 99.88           C\\nANISOU 1502  CB  ILE A1017     9604  13484  14862   -733  -2035   1517       C\\nATOM   1503  CG1 ILE A1017      48.641   2.776  43.677  1.00 99.15           C\\nANISOU 1503  CG1 ILE A1017     9368  13325  14980  -1097  -1674   1598       C\\nATOM   1504  CG2 ILE A1017      48.859   0.586  44.863  1.00102.32           C\\nANISOU 1504  CG2 ILE A1017     9624  13983  15272   -342  -1894   1617       C\\nATOM   1505  CD1 ILE A1017      50.072   2.657  43.214  1.00100.19           C\\nANISOU 1505  CD1 ILE A1017     8808  13728  15530  -1237  -1535   1668       C\\nATOM   1506  N   TYR A1018      46.040   0.013  46.328  1.00 96.96           N\\nANISOU 1506  N   TYR A1018    10204  13021  13613     -4  -2100   1503       N\\nATOM   1507  CA  TYR A1018      45.693  -0.867  47.432  1.00100.96           C\\nANISOU 1507  CA  TYR A1018    10937  13603  13821    241  -2341   1544       C\\nATOM   1508  C   TYR A1018      45.961  -2.303  47.006  1.00113.96           C\\nANISOU 1508  C   TYR A1018    12472  15250  15576    569  -2149   1734       C\\nATOM   1509  O   TYR A1018      46.224  -2.587  45.835  1.00121.07           O\\nANISOU 1509  O   TYR A1018    13172  16106  16722    616  -1774   1767       O\\nATOM   1510  CB  TYR A1018      44.232  -0.693  47.850  1.00 93.06           C\\nANISOU 1510  CB  TYR A1018    10474  12514  12372    220  -2278   1421       C\\nATOM   1511  CG  TYR A1018      43.253  -1.208  46.822  1.00 94.64           C\\nANISOU 1511  CG  TYR A1018    10901  12566  12493    308  -1824   1465       C\\nATOM   1512  CD1 TYR A1018      43.069  -0.541  45.617  1.00 98.44           C\\nANISOU 1512  CD1 TYR A1018    11346  12911  13146    160  -1544   1428       C\\nATOM   1513  CD2 TYR A1018      42.513  -2.358  47.053  1.00 92.36           C\\nANISOU 1513  CD2 TYR A1018    10884  12266  11944    505  -1704   1563       C\\nATOM   1514  CE1 TYR A1018      42.179  -1.007  44.669  1.00 97.08           C\\nANISOU 1514  CE1 TYR A1018    11389  12624  12873    230  -1183   1460       C\\nATOM   1515  CE2 TYR A1018      41.614  -2.831  46.111  1.00 95.41           C\\nANISOU 1515  CE2 TYR A1018    11463  12519  12271    556  -1325   1577       C\\nATOM   1516  CZ  TYR A1018      41.450  -2.147  44.923  1.00 96.24           C\\nANISOU 1516  CZ  TYR A1018    11515  12518  12534    430  -1079   1511       C\\nATOM   1517  OH  TYR A1018      40.562  -2.611  43.980  1.00 94.30           O\\nANISOU 1517  OH  TYR A1018    11469  12159  12201    471   -755   1517       O\\nATOM   1518  N   LYS A1019      45.882  -3.212  47.972  1.00112.29           N\\nANISOU 1518  N   LYS A1019    12428  15075  15161    787  -2416   1854       N\\nATOM   1519  CA  LYS A1019      46.124  -4.629  47.736  1.00114.49           C\\nANISOU 1519  CA  LYS A1019    12662  15272  15567   1129  -2330   2040       C\\nATOM   1520  C   LYS A1019      44.796  -5.365  47.616  1.00112.47           C\\nANISOU 1520  C   LYS A1019    12933  14846  14954   1191  -2067   2094       C\\nATOM   1521  O   LYS A1019      43.893  -5.162  48.435  1.00114.99           O\\nANISOU 1521  O   LYS A1019    13645  15200  14846   1061  -2176   2073       O\\nATOM   1522  CB  LYS A1019      46.964  -5.233  48.863  1.00116.93           C\\nANISOU 1522  CB  LYS A1019    12829  15675  15923   1330  -2866   2206       C\\nATOM   1523  N   ASP A1020      44.677  -6.212  46.597  1.00112.39           N\\nANISOU 1523  N   ASP A1020    12914  14672  15118   1369  -1707   2129       N\\nATOM   1524  CA  ASP A1020      43.491  -7.038  46.453  1.00108.38           C\\nANISOU 1524  CA  ASP A1020    12868  13981  14329   1415  -1485   2186       C\\nATOM   1525  C   ASP A1020      43.556  -8.206  47.436  1.00111.34           C\\nANISOU 1525  C   ASP A1020    13459  14255  14590   1619  -1796   2432       C\\nATOM   1526  O   ASP A1020      44.475  -8.316  48.253  1.00111.64           O\\nANISOU 1526  O   ASP A1020    13307  14376  14734   1741  -2219   2559       O\\nATOM   1527  CB  ASP A1020      43.344  -7.520  45.010  1.00103.84           C\\nANISOU 1527  CB  ASP A1020    12244  13254  13957   1507  -1026   2105       C\\nATOM   1528  CG  ASP A1020      44.444  -8.477  44.594  1.00108.01           C\\nANISOU 1528  CG  ASP A1020    12440  13694  14903   1844  -1010   2150       C\\nATOM   1529  OD1 ASP A1020      45.525  -8.453  45.217  1.00113.64           O\\nANISOU 1529  OD1 ASP A1020    12802  14515  15861   1981  -1346   2220       O\\nATOM   1530  OD2 ASP A1020      44.228  -9.253  43.639  1.00105.75           O\\nANISOU 1530  OD2 ASP A1020    12227  13235  14718   1987   -677   2082       O\\nATOM   1531  N   THR A1021      42.571  -9.101  47.357  1.00111.86           N\\nANISOU 1531  N   THR A1021    13936  14124  14441   1634  -1618   2524       N\\nATOM   1532  CA  THR A1021      42.498 -10.201  48.311  1.00111.37           C\\nANISOU 1532  CA  THR A1021    14180  13918  14216   1754  -1913   2816       C\\nATOM   1533  C   THR A1021      43.592 -11.242  48.108  1.00113.87           C\\nANISOU 1533  C   THR A1021    14272  14000  14994   2154  -2104   2966       C\\nATOM   1534  O   THR A1021      43.713 -12.150  48.936  1.00122.97           O\\nANISOU 1534  O   THR A1021    15669  14982  16073   2291  -2453   3261       O\\nATOM   1535  CB  THR A1021      41.130 -10.879  48.236  1.00106.11           C\\nANISOU 1535  CB  THR A1021    14000  13085  13230   1600  -1650   2877       C\\nATOM   1536  OG1 THR A1021      40.997 -11.555  46.980  1.00101.52           O\\nANISOU 1536  OG1 THR A1021    13390  12234  12949   1746  -1308   2783       O\\nATOM   1537  CG2 THR A1021      40.020  -9.844  48.372  1.00105.59           C\\nANISOU 1537  CG2 THR A1021    14074  13265  12778   1259  -1443   2671       C\\nATOM   1538  N   GLU A1022      44.388 -11.136  47.045  1.00109.65           N\\nANISOU 1538  N   GLU A1022    13282  13452  14927   2346  -1889   2772       N\\nATOM   1539  CA  GLU A1022      45.477 -12.070  46.790  1.00109.91           C\\nANISOU 1539  CA  GLU A1022    13002  13289  15472   2780  -2033   2824       C\\nATOM   1540  C   GLU A1022      46.850 -11.447  47.014  1.00110.30           C\\nANISOU 1540  C   GLU A1022    12423  13602  15882   2906  -2315   2766       C\\nATOM   1541  O   GLU A1022      47.866 -12.107  46.769  1.00114.91           O\\nANISOU 1541  O   GLU A1022    12609  14084  16969   3299  -2431   2752       O\\nATOM   1542  CB  GLU A1022      45.376 -12.625  45.367  1.00110.94           C\\nANISOU 1542  CB  GLU A1022    13056  13217  15878   2939  -1526   2594       C\\nATOM   1543  N   GLY A1023      46.907 -10.195  47.471  1.00108.89           N\\nANISOU 1543  N   GLY A1023    12123  13753  15498   2586  -2436   2704       N\\nATOM   1544  CA  GLY A1023      48.156  -9.536  47.793  1.00110.44           C\\nANISOU 1544  CA  GLY A1023    11736  14212  16013   2619  -2755   2653       C\\nATOM   1545  C   GLY A1023      48.709  -8.632  46.710  1.00113.05           C\\nANISOU 1545  C   GLY A1023    11548  14751  16654   2465  -2360   2382       C\\nATOM   1546  O   GLY A1023      49.639  -7.862  46.986  1.00112.39           O\\nANISOU 1546  O   GLY A1023    10982  14921  16798   2361  -2597   2323       O\\nATOM   1547  N   TYR A1024      48.174  -8.700  45.495  1.00108.30           N\\nANISOU 1547  N   TYR A1024    11043  14058  16046   2411  -1784   2230       N\\nATOM   1548  CA  TYR A1024      48.663  -7.880  44.398  1.00113.34           C\\nANISOU 1548  CA  TYR A1024    11259  14900  16907   2217  -1372   2019       C\\nATOM   1549  C   TYR A1024      48.186  -6.439  44.545  1.00111.52           C\\nANISOU 1549  C   TYR A1024    11170  14816  16386   1738  -1381   1979       C\\nATOM   1550  O   TYR A1024      47.084  -6.173  45.033  1.00110.91           O\\nANISOU 1550  O   TYR A1024    11615  14645  15882   1574  -1459   2021       O\\nATOM   1551  CB  TYR A1024      48.188  -8.447  43.060  1.00116.94           C\\nANISOU 1551  CB  TYR A1024    11856  15216  17360   2297   -787   1879       C\\nATOM   1552  CG  TYR A1024      48.578  -9.890  42.820  1.00122.30           C\\nANISOU 1552  CG  TYR A1024    12446  15674  18349   2790   -744   1850       C\\nATOM   1553  CD1 TYR A1024      49.830 -10.364  43.189  1.00128.61           C\\nANISOU 1553  CD1 TYR A1024    12689  16530  19645   3150  -1024   1848       C\\nATOM   1554  CD2 TYR A1024      47.689 -10.779  42.227  1.00118.01           C\\nANISOU 1554  CD2 TYR A1024    12364  14836  17638   2906   -460   1804       C\\nATOM   1555  CE1 TYR A1024      50.188 -11.681  42.970  1.00131.77           C\\nANISOU 1555  CE1 TYR A1024    13011  16664  20391   3655  -1019   1793       C\\nATOM   1556  CE2 TYR A1024      48.037 -12.096  42.004  1.00120.38           C\\nANISOU 1556  CE2 TYR A1024    12621  14859  18257   3363   -444   1744       C\\nATOM   1557  CZ  TYR A1024      49.287 -12.542  42.377  1.00129.11           C\\nANISOU 1557  CZ  TYR A1024    13187  15991  19879   3758   -723   1736       C\\nATOM   1558  OH  TYR A1024      49.639 -13.855  42.158  1.00133.04           O\\nANISOU 1558  OH  TYR A1024    13642  16152  20756   4269   -742   1651       O\\nATOM   1559  N   TYR A1025      49.029  -5.504  44.113  1.00117.71           N\\nANISOU 1559  N   TYR A1025    11469  15821  17433   1507  -1294   1881       N\\nATOM   1560  CA  TYR A1025      48.682  -4.087  44.152  1.00110.35           C\\nANISOU 1560  CA  TYR A1025    10659  14955  16314   1049  -1319   1834       C\\nATOM   1561  C   TYR A1025      47.758  -3.760  42.985  1.00104.43           C\\nANISOU 1561  C   TYR A1025    10246  14092  15339    855   -821   1781       C\\nATOM   1562  O   TYR A1025      48.115  -3.979  41.822  1.00101.17           O\\nANISOU 1562  O   TYR A1025     9617  13740  15082    859   -384   1729       O\\nATOM   1563  CB  TYR A1025      49.939  -3.221  44.101  1.00111.84           C\\nANISOU 1563  CB  TYR A1025    10220  15385  16890    814  -1427   1782       C\\nATOM   1564  CG  TYR A1025      50.892  -3.432  45.257  1.00115.51           C\\nANISOU 1564  CG  TYR A1025    10303  15992  17595    978  -1998   1822       C\\nATOM   1565  CD1 TYR A1025      50.776  -2.688  46.423  1.00114.38           C\\nANISOU 1565  CD1 TYR A1025    10332  15875  17252    775  -2517   1825       C\\nATOM   1566  CD2 TYR A1025      51.915  -4.369  45.177  1.00120.42           C\\nANISOU 1566  CD2 TYR A1025    10384  16722  18646   1352  -2046   1830       C\\nATOM   1567  CE1 TYR A1025      51.647  -2.875  47.481  1.00116.89           C\\nANISOU 1567  CE1 TYR A1025    10328  16345  17742    906  -3095   1869       C\\nATOM   1568  CE2 TYR A1025      52.791  -4.563  46.228  1.00124.27           C\\nANISOU 1568  CE2 TYR A1025    10509  17338  19372   1522  -2643   1887       C\\nATOM   1569  CZ  TYR A1025      52.653  -3.813  47.377  1.00124.31           C\\nANISOU 1569  CZ  TYR A1025    10724  17386  19121   1279  -3180   1923       C\\nATOM   1570  OH  TYR A1025      53.523  -4.004  48.428  1.00131.17           O\\nANISOU 1570  OH  TYR A1025    11258  18402  20177   1430  -3829   1986       O\\nATOM   1571  N   THR A1026      46.569  -3.247  43.288  1.00104.70           N\\nANISOU 1571  N   THR A1026    10799  13985  14997    692   -893   1776       N\\nATOM   1572  CA  THR A1026      45.596  -2.892  42.268  1.00105.81           C\\nANISOU 1572  CA  THR A1026    11282  14002  14919    524   -528   1739       C\\nATOM   1573  C   THR A1026      45.108  -1.467  42.499  1.00102.55           C\\nANISOU 1573  C   THR A1026    11058  13525  14382    179   -701   1694       C\\nATOM   1574  O   THR A1026      45.449  -0.819  43.493  1.00 98.86           O\\nANISOU 1574  O   THR A1026    10500  13102  13962     75  -1083   1653       O\\nATOM   1575  CB  THR A1026      44.400  -3.858  42.255  1.00102.47           C\\nANISOU 1575  CB  THR A1026    11323  13413  14198    735   -413   1745       C\\nATOM   1576  OG1 THR A1026      43.497  -3.517  43.312  1.00 98.43           O\\nANISOU 1576  OG1 THR A1026    11152  12846  13400    677   -704   1728       O\\nATOM   1577  CG2 THR A1026      44.861  -5.301  42.437  1.00103.30           C\\nANISOU 1577  CG2 THR A1026    11315  13487  14447   1108   -410   1798       C\\nATOM   1578  N   ILE A1027      44.296  -0.982  41.560  1.00 99.57           N\\nANISOU 1578  N   ILE A1027    10963  13018  13850     15   -450   1686       N\\nATOM   1579  CA  ILE A1027      43.734   0.361  41.638  1.00 94.27           C\\nANISOU 1579  CA  ILE A1027    10513  12198  13107   -265   -621   1637       C\\nATOM   1580  C   ILE A1027      42.483   0.419  40.770  1.00 89.78           C\\nANISOU 1580  C   ILE A1027    10350  11463  12301   -276   -407   1635       C\\nATOM   1581  O   ILE A1027      42.233  -0.483  39.962  1.00 86.52           O\\nANISOU 1581  O   ILE A1027    10008  11080  11787   -145    -97   1677       O\\nATOM   1582  CB  ILE A1027      44.771   1.417  41.213  1.00 89.65           C\\nANISOU 1582  CB  ILE A1027     9615  11643  12803   -620   -639   1700       C\\nATOM   1583  CG1 ILE A1027      44.397   2.796  41.761  1.00 84.69           C\\nANISOU 1583  CG1 ILE A1027     9187  10803  12189   -869   -988   1614       C\\nATOM   1584  CG2 ILE A1027      44.914   1.453  39.698  1.00 80.58           C\\nANISOU 1584  CG2 ILE A1027     8450  10512  11654   -794   -204   1829       C\\nATOM   1585  CD1 ILE A1027      45.403   3.866  41.434  1.00 82.74           C\\nANISOU 1585  CD1 ILE A1027     8667  10528  12241  -1282  -1056   1694       C\\nATOM   1586  N   GLY A1028      41.681   1.469  40.938  1.00 90.15           N\\nANISOU 1586  N   GLY A1028    10659  11318  12274   -414   -605   1560       N\\nATOM   1587  CA  GLY A1028      40.491   1.617  40.118  1.00 84.64           C\\nANISOU 1587  CA  GLY A1028    10306  10458  11396   -412   -482   1559       C\\nATOM   1588  C   GLY A1028      39.429   0.607  40.504  1.00 83.32           C\\nANISOU 1588  C   GLY A1028    10333  10329  10994   -142   -422   1455       C\\nATOM   1589  O   GLY A1028      39.140   0.390  41.685  1.00 81.04           O\\nANISOU 1589  O   GLY A1028    10066  10102  10624    -17   -599   1333       O\\nATOM   1590  N   ILE A1029      38.832  -0.021  39.494  1.00 90.61           N\\nANISOU 1590  N   ILE A1029    11415  11232  11782    -90   -168   1506       N\\nATOM   1591  CA  ILE A1029      37.857  -1.077  39.728  1.00 88.98           C\\nANISOU 1591  CA  ILE A1029    11375  11052  11381    109    -82   1426       C\\nATOM   1592  C   ILE A1029      38.467  -2.405  39.306  1.00 96.86           C\\nANISOU 1592  C   ILE A1029    12278  12138  12386    239    180   1504       C\\nATOM   1593  O   ILE A1029      38.305  -2.841  38.160  1.00 98.47           O\\nANISOU 1593  O   ILE A1029    12577  12322  12515    224    426   1527       O\\nATOM   1594  CB  ILE A1029      36.538  -0.812  38.980  1.00 75.33           C\\nANISOU 1594  CB  ILE A1029     9908   9202   9511     82    -63   1368       C\\nATOM   1595  CG1 ILE A1029      35.978   0.560  39.350  1.00 71.56           C\\nANISOU 1595  CG1 ILE A1029     9501   8581   9108     11   -352   1261       C\\nATOM   1596  CG2 ILE A1029      35.522  -1.900  39.298  1.00 63.88           C\\nANISOU 1596  CG2 ILE A1029     8583   7799   7889    229     23   1272       C\\nATOM   1597  CD1 ILE A1029      34.589   0.806  38.813  1.00 68.30           C\\nANISOU 1597  CD1 ILE A1029     9287   8054   8610     55   -413   1168       C\\nATOM   1598  N   GLY A1030      39.179  -3.050  40.226  1.00 99.15           N\\nANISOU 1598  N   GLY A1030    12396  12511  12765    380    101   1529       N\\nATOM   1599  CA  GLY A1030      39.787  -4.335  39.947  1.00 98.18           C\\nANISOU 1599  CA  GLY A1030    12171  12410  12722    571    291   1577       C\\nATOM   1600  C   GLY A1030      40.760  -4.288  38.789  1.00 94.57           C\\nANISOU 1600  C   GLY A1030    11485  12025  12421    523    562   1598       C\\nATOM   1601  O   GLY A1030      40.506  -4.869  37.728  1.00 95.69           O\\nANISOU 1601  O   GLY A1030    11749  12138  12469    550    849   1553       O\\nATOM   1602  N   HIS A1031      41.878  -3.592  38.977  1.00 87.03           N\\nANISOU 1602  N   HIS A1031    10189  11192  11687    421    486   1644       N\\nATOM   1603  CA  HIS A1031      42.893  -3.436  37.938  1.00 89.86           C\\nANISOU 1603  CA  HIS A1031    10256  11692  12196    312    785   1660       C\\nATOM   1604  C   HIS A1031      44.259  -3.687  38.565  1.00 92.16           C\\nANISOU 1604  C   HIS A1031    10046  12138  12831    439    693   1664       C\\nATOM   1605  O   HIS A1031      44.848  -2.781  39.162  1.00 95.75           O\\nANISOU 1605  O   HIS A1031    10270  12666  13443    260    450   1711       O\\nATOM   1606  CB  HIS A1031      42.821  -2.053  37.308  1.00 89.34           C\\nANISOU 1606  CB  HIS A1031    10256  11621  12066    -69    797   1742       C\\nATOM   1607  CG  HIS A1031      43.762  -1.865  36.161  1.00 92.70           C\\nANISOU 1607  CG  HIS A1031    10434  12232  12556   -271   1167   1789       C\\nATOM   1608  ND1 HIS A1031      43.332  -1.784  34.855  1.00 93.45           N\\nANISOU 1608  ND1 HIS A1031    10789  12339  12379   -440   1471   1824       N\\nATOM   1609  CD2 HIS A1031      45.109  -1.748  36.123  1.00 96.67           C\\nANISOU 1609  CD2 HIS A1031    10434  12956  13341   -356   1297   1798       C\\nATOM   1610  CE1 HIS A1031      44.375  -1.621  34.061  1.00 97.80           C\\nANISOU 1610  CE1 HIS A1031    11037  13125  12996   -641   1814   1858       C\\nATOM   1611  NE2 HIS A1031      45.465  -1.597  34.805  1.00100.11           N\\nANISOU 1611  NE2 HIS A1031    10830  13554  13654   -592   1731   1833       N\\nATOM   1612  N   LEU A1032      44.761  -4.912  38.422  1.00 91.24           N\\nANISOU 1612  N   LEU A1032     9754  12051  12863    756    853   1596       N\\nATOM   1613  CA  LEU A1032      46.058  -5.267  38.982  1.00 95.11           C\\nANISOU 1613  CA  LEU A1032     9720  12682  13737    952    730   1587       C\\nATOM   1614  C   LEU A1032      47.161  -4.499  38.265  1.00 99.71           C\\nANISOU 1614  C   LEU A1032     9815  13531  14540    697    975   1562       C\\nATOM   1615  O   LEU A1032      47.347  -4.649  37.054  1.00 96.96           O\\nANISOU 1615  O   LEU A1032     9403  13297  14140    624   1442   1479       O\\nATOM   1616  CB  LEU A1032      46.290  -6.772  38.868  1.00 93.50           C\\nANISOU 1616  CB  LEU A1032     9457  12381  13686   1392    849   1495       C\\nATOM   1617  N   LEU A1033      47.887  -3.667  39.013  1.00 97.35           N\\nANISOU 1617  N   LEU A1033     9181  13349  14459    521    666   1628       N\\nATOM   1618  CA  LEU A1033      49.025  -2.964  38.434  1.00104.31           C\\nANISOU 1618  CA  LEU A1033     9528  14502  15604    230    883   1619       C\\nATOM   1619  C   LEU A1033      50.158  -3.934  38.121  1.00112.65           C\\nANISOU 1619  C   LEU A1033     9983  15786  17034    550   1131   1473       C\\nATOM   1620  O   LEU A1033      50.737  -3.897  37.029  1.00115.99           O\\nANISOU 1620  O   LEU A1033    10102  16446  17521    410   1635   1381       O\\nATOM   1621  CB  LEU A1033      49.494  -1.861  39.381  1.00103.46           C\\nANISOU 1621  CB  LEU A1033     9213  14430  15668    -55    434   1699       C\\nATOM   1622  N   THR A1034      50.477  -4.818  39.064  1.00114.71           N\\nANISOU 1622  N   THR A1034    10071  15980  17534    990    782   1443       N\\nATOM   1623  CA  THR A1034      51.514  -5.822  38.866  1.00119.05           C\\nANISOU 1623  CA  THR A1034    10043  16677  18514   1403    933   1278       C\\nATOM   1624  C   THR A1034      51.333  -6.919  39.904  1.00116.13           C\\nANISOU 1624  C   THR A1034     9831  16045  18250   1915    470   1326       C\\nATOM   1625  O   THR A1034      50.615  -6.756  40.893  1.00112.94           O\\nANISOU 1625  O   THR A1034     9869  15449  17593   1873     24   1499       O\\nATOM   1626  CB  THR A1034      52.919  -5.218  38.968  1.00123.11           C\\nANISOU 1626  CB  THR A1034     9729  17558  19489   1237    901   1232       C\\nATOM   1627  OG1 THR A1034      53.898  -6.241  38.746  1.00127.31           O\\nANISOU 1627  OG1 THR A1034     9644  18240  20490   1707   1059   1022       O\\nATOM   1628  CG2 THR A1034      53.135  -4.617  40.344  1.00124.58           C\\nANISOU 1628  CG2 THR A1034     9836  17714  19783   1140    210   1384       C\\nATOM   1629  N   LYS A1035      51.998  -8.046  39.660  1.00124.24           N\\nANISOU 1629  N   LYS A1035    10499  17061  19647   2398    588   1165       N\\nATOM   1630  CA  LYS A1035      52.071  -9.132  40.624  1.00115.60           C\\nANISOU 1630  CA  LYS A1035     9471  15694  18757   2910    100   1245       C\\nATOM   1631  C   LYS A1035      53.350  -9.089  41.448  1.00124.45           C\\nANISOU 1631  C   LYS A1035     9878  17011  20395   3112   -361   1270       C\\nATOM   1632  O   LYS A1035      53.591 -10.004  42.241  1.00126.86           O\\nANISOU 1632  O   LYS A1035    10167  17100  20932   3572   -826   1360       O\\nATOM   1633  CB  LYS A1035      51.953 -10.483  39.911  1.00108.04           C\\nANISOU 1633  CB  LYS A1035     8621  14489  17940   3381    417   1046       C\\nATOM   1634  N   SER A1036      54.169  -8.044  41.282  1.00124.75           N\\nANISOU 1634  N   SER A1036     9333  17441  20626   2756   -279   1212       N\\nATOM   1635  CA  SER A1036      55.429  -7.892  41.994  1.00130.16           C\\nANISOU 1635  CA  SER A1036     9248  18374  21834   2880   -717   1205       C\\nATOM   1636  C   SER A1036      55.191  -7.369  43.411  1.00127.51           C\\nANISOU 1636  C   SER A1036     9199  17961  21290   2719  -1470   1465       C\\nATOM   1637  O   SER A1036      54.249  -6.611  43.652  1.00124.62           O\\nANISOU 1637  O   SER A1036     9437  17497  20415   2316  -1507   1585       O\\nATOM   1638  CB  SER A1036      56.351  -6.937  41.243  1.00133.68           C\\nANISOU 1638  CB  SER A1036     8966  19280  22547   2465   -307   1043       C\\nATOM   1639  N   PRO A1037      56.041  -7.758  44.369  1.00132.59           N\\nANISOU 1639  N   PRO A1037     9408  18656  22314   3043  -2094   1531       N\\nATOM   1640  CA  PRO A1037      55.818  -7.332  45.758  1.00131.46           C\\nANISOU 1640  CA  PRO A1037     9590  18465  21895   2895  -2836   1763       C\\nATOM   1641  C   PRO A1037      56.251  -5.907  46.050  1.00131.07           C\\nANISOU 1641  C   PRO A1037     9233  18724  21845   2324  -3004   1723       C\\nATOM   1642  O   PRO A1037      55.767  -5.327  47.031  1.00128.15           O\\nANISOU 1642  O   PRO A1037     9314  18300  21079   2075  -3470   1849       O\\nATOM   1643  CB  PRO A1037      56.658  -8.330  46.564  1.00137.89           C\\nANISOU 1643  CB  PRO A1037    10022  19225  23144   3474  -3467   1855       C\\nATOM   1644  CG  PRO A1037      57.788  -8.659  45.647  1.00141.32           C\\nANISOU 1644  CG  PRO A1037     9525  19887  24282   3748  -3098   1581       C\\nATOM   1645  CD  PRO A1037      57.205  -8.654  44.250  1.00138.32           C\\nANISOU 1645  CD  PRO A1037     9352  19476  23728   3597  -2186   1384       C\\nATOM   1646  N   SER A1038      57.142  -5.329  45.249  1.00134.97           N\\nANISOU 1646  N   SER A1038     8987  19535  22758   2087  -2636   1539       N\\nATOM   1647  CA  SER A1038      57.615  -3.977  45.512  1.00138.82           C\\nANISOU 1647  CA  SER A1038     9165  20272  23307   1497  -2818   1510       C\\nATOM   1648  C   SER A1038      56.508  -2.965  45.234  1.00142.03           C\\nANISOU 1648  C   SER A1038    10304  20506  23157    966  -2548   1556       C\\nATOM   1649  O   SER A1038      55.905  -2.966  44.156  1.00142.81           O\\nANISOU 1649  O   SER A1038    10685  20515  23061    864  -1905   1526       O\\nATOM   1650  CB  SER A1038      58.845  -3.669  44.659  1.00137.97           C\\nANISOU 1650  CB  SER A1038     8060  20560  23801   1331  -2429   1322       C\\nATOM   1651  N   LEU A1039      56.235  -2.105  46.219  1.00148.93           N\\nANISOU 1651  N   LEU A1039    11491  21326  23772    647  -3071   1607       N\\nATOM   1652  CA  LEU A1039      55.237  -1.059  46.027  1.00137.41           C\\nANISOU 1652  CA  LEU A1039    10670  19674  21866    176  -2887   1609       C\\nATOM   1653  C   LEU A1039      55.728  -0.005  45.042  1.00134.86           C\\nANISOU 1653  C   LEU A1039     9968  19484  21790   -372  -2464   1547       C\\nATOM   1654  O   LEU A1039      54.942   0.522  44.246  1.00128.51           O\\nANISOU 1654  O   LEU A1039     9617  18504  20707   -648  -2029   1577       O\\nATOM   1655  CB  LEU A1039      54.882  -0.422  47.371  1.00133.76           C\\nANISOU 1655  CB  LEU A1039    10606  19126  21088      8  -3557   1606       C\\nATOM   1656  CG  LEU A1039      53.969   0.807  47.351  1.00123.44           C\\nANISOU 1656  CG  LEU A1039     9880  17606  19417   -461  -3487   1537       C\\nATOM   1657  CD1 LEU A1039      52.634   0.486  46.697  1.00115.73           C\\nANISOU 1657  CD1 LEU A1039     9575  16373  18024   -334  -3002   1586       C\\nATOM   1658  CD2 LEU A1039      53.766   1.349  48.759  1.00121.51           C\\nANISOU 1658  CD2 LEU A1039     9948  17332  18887   -575  -4163   1451       C\\nATOM   1659  N   ASN A1040      57.027   0.309  45.078  1.00140.78           N\\nANISOU 1659  N   ASN A1040     9881  20545  23065   -557  -2602   1481       N\\nATOM   1660  CA  ASN A1040      57.584   1.273  44.135  1.00137.59           C\\nANISOU 1660  CA  ASN A1040     9069  20297  22910  -1145  -2171   1458       C\\nATOM   1661  C   ASN A1040      57.424   0.803  42.695  1.00142.78           C\\nANISOU 1661  C   ASN A1040     9696  21027  23528  -1086  -1335   1468       C\\nATOM   1662  O   ASN A1040      57.214   1.623  41.793  1.00129.49           O\\nANISOU 1662  O   ASN A1040     8176  19309  21715  -1595   -895   1536       O\\nATOM   1663  CB  ASN A1040      59.058   1.528  44.452  1.00137.97           C\\nANISOU 1663  CB  ASN A1040     8117  20728  23578  -1326  -2453   1368       C\\nATOM   1664  N   ALA A1041      57.513  -0.508  42.459  1.00141.43           N\\nANISOU 1664  N   ALA A1041     9359  20933  23447   -478  -1132   1401       N\\nATOM   1665  CA  ALA A1041      57.326  -1.032  41.111  1.00146.42           C\\nANISOU 1665  CA  ALA A1041    10009  21635  23988   -388   -344   1347       C\\nATOM   1666  C   ALA A1041      55.865  -0.980  40.683  1.00137.93           C\\nANISOU 1666  C   ALA A1041     9919  20195  22294   -425   -117   1454       C\\nATOM   1667  O   ALA A1041      55.576  -0.783  39.497  1.00137.36           O\\nANISOU 1667  O   ALA A1041    10016  20159  22015   -671    490   1467       O\\nATOM   1668  CB  ALA A1041      57.852  -2.465  41.023  1.00155.04           C\\nANISOU 1668  CB  ALA A1041    10644  22857  25406    310   -239   1186       C\\nATOM   1669  N   ALA A1042      54.935  -1.157  41.626  1.00140.82           N\\nANISOU 1669  N   ALA A1042    10925  20238  22341   -200   -595   1527       N\\nATOM   1670  CA  ALA A1042      53.519  -1.060  41.288  1.00132.90           C\\nANISOU 1670  CA  ALA A1042    10790  18913  20795   -244   -420   1604       C\\nATOM   1671  C   ALA A1042      53.142   0.352  40.863  1.00133.14           C\\nANISOU 1671  C   ALA A1042    11109  18838  20640   -869   -326   1693       C\\nATOM   1672  O   ALA A1042      52.205   0.531  40.075  1.00130.01           O\\nANISOU 1672  O   ALA A1042    11253  18260  19885   -986      1   1755       O\\nATOM   1673  CB  ALA A1042      52.662  -1.505  42.472  1.00126.18           C\\nANISOU 1673  CB  ALA A1042    10481  17801  19659     81   -937   1646       C\\nATOM   1674  N   LYS A1043      53.853   1.361  41.370  1.00137.98           N\\nANISOU 1674  N   LYS A1043    11384  19531  21510  -1275   -652   1703       N\\nATOM   1675  CA  LYS A1043      53.613   2.736  40.950  1.00131.35           C\\nANISOU 1675  CA  LYS A1043    10799  18530  20579  -1894   -598   1802       C\\nATOM   1676  C   LYS A1043      54.204   3.022  39.577  1.00133.43           C\\nANISOU 1676  C   LYS A1043    10730  19015  20952  -2291     34   1891       C\\nATOM   1677  O   LYS A1043      53.705   3.899  38.864  1.00133.13           O\\nANISOU 1677  O   LYS A1043    11108  18782  20694  -2733    227   2044       O\\nATOM   1678  CB  LYS A1043      54.192   3.713  41.976  1.00128.92           C\\nANISOU 1678  CB  LYS A1043    10263  18193  20526  -2230  -1186   1758       C\\nATOM   1679  CG  LYS A1043      53.569   3.618  43.359  1.00124.36           C\\nANISOU 1679  CG  LYS A1043    10090  17422  19739  -1936  -1811   1654       C\\nATOM   1680  CD  LYS A1043      54.054   4.744  44.258  1.00124.45           C\\nANISOU 1680  CD  LYS A1043     9973  17371  19941  -2345  -2374   1565       C\\nATOM   1681  CE  LYS A1043      53.301   4.761  45.577  1.00122.13           C\\nANISOU 1681  CE  LYS A1043    10189  16897  19319  -2105  -2935   1426       C\\nATOM   1682  NZ  LYS A1043      53.698   5.919  46.425  1.00124.65           N\\nANISOU 1682  NZ  LYS A1043    10461  17121  19779  -2520  -3485   1275       N\\nATOM   1683  N   SER A1044      55.263   2.305  39.194  1.00130.51           N\\nANISOU 1683  N   SER A1044     9619  19057  20914  -2142    357   1795       N\\nATOM   1684  CA  SER A1044      55.858   2.511  37.879  1.00137.15           C\\nANISOU 1684  CA  SER A1044    10108  20197  21806  -2533   1041   1845       C\\nATOM   1685  C   SER A1044      54.904   2.086  36.770  1.00136.57           C\\nANISOU 1685  C   SER A1044    10643  20016  21232  -2427   1563   1899       C\\nATOM   1686  O   SER A1044      54.789   2.771  35.747  1.00141.22           O\\nANISOU 1686  O   SER A1044    11441  20628  21589  -2937   1967   2067       O\\nATOM   1687  CB  SER A1044      57.179   1.749  37.775  1.00143.25           C\\nANISOU 1687  CB  SER A1044     9888  21468  23072  -2311   1285   1648       C\\nATOM   1688  N   GLU A1045      54.211   0.960  36.954  1.00136.81           N\\nANISOU 1688  N   GLU A1045    10988  19917  21076  -1800   1534   1777       N\\nATOM   1689  CA  GLU A1045      53.243   0.521  35.955  1.00129.18           C\\nANISOU 1689  CA  GLU A1045    10619  18832  19631  -1695   1960   1797       C\\nATOM   1690  C   GLU A1045      52.010   1.415  35.939  1.00128.34           C\\nANISOU 1690  C   GLU A1045    11333  18313  19118  -1974   1718   2002       C\\nATOM   1691  O   GLU A1045      51.383   1.582  34.887  1.00126.75           O\\nANISOU 1691  O   GLU A1045    11575  18053  18531  -2171   2069   2109       O\\nATOM   1692  CB  GLU A1045      52.847  -0.934  36.210  1.00121.20           C\\nANISOU 1692  CB  GLU A1045     9714  17751  18586   -982   1950   1604       C\\nATOM   1693  N   LEU A1046      51.650   1.998  37.088  1.00131.91           N\\nANISOU 1693  N   LEU A1046    11988  18485  19645  -1980   1106   2037       N\\nATOM   1694  CA  LEU A1046      50.490   2.885  37.146  1.00126.43           C\\nANISOU 1694  CA  LEU A1046    12012  17383  18643  -2189    846   2169       C\\nATOM   1695  C   LEU A1046      50.730   4.156  36.342  1.00134.52           C\\nANISOU 1695  C   LEU A1046    13116  18345  19652  -2860    993   2395       C\\nATOM   1696  O   LEU A1046      49.873   4.579  35.558  1.00138.35           O\\nANISOU 1696  O   LEU A1046    14165  18604  19797  -3036   1114   2555       O\\nATOM   1697  CB  LEU A1046      50.156   3.227  38.600  1.00114.87           C\\nANISOU 1697  CB  LEU A1046    10689  15684  17273  -2043    195   2081       C\\nATOM   1698  CG  LEU A1046      49.189   4.395  38.827  1.00103.62           C\\nANISOU 1698  CG  LEU A1046     9857  13838  15674  -2297   -138   2146       C\\nATOM   1699  CD1 LEU A1046      47.828   4.107  38.217  1.00 96.31           C\\nANISOU 1699  CD1 LEU A1046     9556  12698  14341  -2097     22   2183       C\\nATOM   1700  CD2 LEU A1046      49.056   4.722  40.308  1.00 99.47           C\\nANISOU 1700  CD2 LEU A1046     9379  13170  15245  -2171   -734   1980       C\\nATOM   1701  N   ASP A1047      51.893   4.784  36.529  1.00127.49           N\\nANISOU 1701  N   ASP A1047    11667  17635  19137  -3262    951   2433       N\\nATOM   1702  CA  ASP A1047      52.188   6.012  35.801  1.00131.96           C\\nANISOU 1702  CA  ASP A1047    12311  18112  19714  -3978   1078   2692       C\\nATOM   1703  C   ASP A1047      52.444   5.742  34.324  1.00130.92           C\\nANISOU 1703  C   ASP A1047    12130  18291  19323  -4228   1792   2837       C\\nATOM   1704  O   ASP A1047      52.172   6.607  33.483  1.00133.98           O\\nANISOU 1704  O   ASP A1047    12921  18510  19475  -4745   1927   3128       O\\nATOM   1705  CB  ASP A1047      53.382   6.723  36.435  1.00141.47           C\\nANISOU 1705  CB  ASP A1047    12895  19442  21416  -4390    835   2678       C\\nATOM   1706  CG  ASP A1047      53.050   7.320  37.791  1.00139.91           C\\nANISOU 1706  CG  ASP A1047    12900  18874  21385  -4305     95   2555       C\\nATOM   1707  OD1 ASP A1047      51.910   7.125  38.263  1.00133.93           O\\nANISOU 1707  OD1 ASP A1047    12719  17809  20359  -3898   -178   2466       O\\nATOM   1708  OD2 ASP A1047      53.925   7.988  38.382  1.00142.42           O\\nANISOU 1708  OD2 ASP A1047    12791  19231  22093  -4666   -203   2522       O\\nATOM   1709  N   LYS A1048      52.958   4.557  33.986  1.00136.15           N\\nANISOU 1709  N   LYS A1048    12332  19393  20008  -3866   2239   2634       N\\nATOM   1710  CA  LYS A1048      53.156   4.211  32.584  1.00137.23           C\\nANISOU 1710  CA  LYS A1048    12447  19868  19828  -4059   2961   2691       C\\nATOM   1711  C   LYS A1048      51.836   3.990  31.855  1.00136.24           C\\nANISOU 1711  C   LYS A1048    13159  19483  19123  -3907   3045   2785       C\\nATOM   1712  O   LYS A1048      51.813   4.012  30.619  1.00135.03           O\\nANISOU 1712  O   LYS A1048    13198  19529  18579  -4209   3556   2913       O\\nATOM   1713  CB  LYS A1048      54.036   2.964  32.467  1.00137.25           C\\nANISOU 1713  CB  LYS A1048    11720  20374  20055  -3634   3395   2361       C\\nATOM   1714  N   ALA A1049      50.743   3.782  32.587  1.00134.09           N\\nANISOU 1714  N   ALA A1049    13374  18806  18767  -3471   2557   2719       N\\nATOM   1715  CA  ALA A1049      49.423   3.607  31.993  1.00136.97           C\\nANISOU 1715  CA  ALA A1049    14488  18911  18642  -3319   2551   2790       C\\nATOM   1716  C   ALA A1049      48.555   4.853  32.093  1.00139.86           C\\nANISOU 1716  C   ALA A1049    15461  18785  18895  -3629   2088   3059       C\\nATOM   1717  O   ALA A1049      47.775   5.130  31.178  1.00144.34           O\\nANISOU 1717  O   ALA A1049    16587  19202  19054  -3792   2166   3254       O\\nATOM   1718  CB  ALA A1049      48.697   2.429  32.649  1.00134.83           C\\nANISOU 1718  CB  ALA A1049    14339  18543  18349  -2619   2376   2514       C\\nATOM   1719  N   ILE A1050      48.667   5.615  33.186  1.00147.00           N\\nANISOU 1719  N   ILE A1050    16279  19419  20157  -3696   1573   3052       N\\nATOM   1720  CA  ILE A1050      47.884   6.843  33.320  1.00137.76           C\\nANISOU 1720  CA  ILE A1050    15661  17727  18955  -3954   1109   3250       C\\nATOM   1721  C   ILE A1050      48.527   8.029  32.621  1.00135.31           C\\nANISOU 1721  C   ILE A1050    15376  17334  18700  -4696   1193   3602       C\\nATOM   1722  O   ILE A1050      47.861   9.054  32.425  1.00132.09           O\\nANISOU 1722  O   ILE A1050    15513  16449  18227  -4950    855   3834       O\\nATOM   1723  CB  ILE A1050      47.649   7.192  34.802  1.00112.75           C\\nANISOU 1723  CB  ILE A1050    12459  14272  16111  -3710    512   3036       C\\nATOM   1724  N   GLY A1051      49.800   7.923  32.236  1.00128.26           N\\nANISOU 1724  N   GLY A1051    13902  16884  17947  -5058   1630   3652       N\\nATOM   1725  CA  GLY A1051      50.479   8.964  31.501  1.00126.01           C\\nANISOU 1725  CA  GLY A1051    13606  16592  17681  -5844   1802   4017       C\\nATOM   1726  C   GLY A1051      51.114  10.046  32.350  1.00125.68           C\\nANISOU 1726  C   GLY A1051    13328  16279  18144  -6255   1362   4067       C\\nATOM   1727  O   GLY A1051      52.053  10.703  31.888  1.00131.62           O\\nANISOU 1727  O   GLY A1051    13814  17166  19028  -6906   1590   4283       O\\nATOM   1728  N   ARG A1052      50.638  10.250  33.572  1.00125.39           N\\nANISOU 1728  N   ARG A1052    13398  15875  18368  -5892    754   3830       N\\nATOM   1729  CA  ARG A1052      51.137  11.295  34.452  1.00130.48           C\\nANISOU 1729  CA  ARG A1052    13895  16207  19473  -6249    261   3810       C\\nATOM   1730  C   ARG A1052      51.879  10.681  35.633  1.00133.64           C\\nANISOU 1730  C   ARG A1052    13610  16936  20230  -5922     98   3432       C\\nATOM   1731  O   ARG A1052      51.880   9.465  35.836  1.00139.15           O\\nANISOU 1731  O   ARG A1052    14025  18014  20831  -5363    306   3204       O\\nATOM   1732  CB  ARG A1052      49.986  12.174  34.954  1.00127.22           C\\nANISOU 1732  CB  ARG A1052    14202  15072  19066  -6123   -369   3798       C\\nATOM   1733  CG  ARG A1052      49.063  11.466  35.933  1.00118.27           C\\nANISOU 1733  CG  ARG A1052    13210  13879  17849  -5343   -664   3404       C\\nATOM   1734  CD  ARG A1052      47.922  12.363  36.372  1.00115.96           C\\nANISOU 1734  CD  ARG A1052    13565  12916  17579  -5212  -1224   3339       C\\nATOM   1735  NE  ARG A1052      47.116  11.751  37.424  1.00114.03           N\\nANISOU 1735  NE  ARG A1052    13390  12676  17262  -4541  -1477   2931       N\\nATOM   1736  CZ  ARG A1052      47.303  11.960  38.723  1.00115.93           C\\nANISOU 1736  CZ  ARG A1052    13460  12852  17737  -4403  -1881   2594       C\\nATOM   1737  NH1 ARG A1052      48.271  12.768  39.132  1.00119.81           N\\nANISOU 1737  NH1 ARG A1052    13686  13244  18594  -4875  -2117   2592       N\\nATOM   1738  NH2 ARG A1052      46.523  11.364  39.613  1.00113.10           N\\nANISOU 1738  NH2 ARG A1052    13205  12544  17222  -3834  -2048   2259       N\\nATOM   1739  N   ASN A1053      52.517  11.551  36.419  1.00125.16           N\\nANISOU 1739  N   ASN A1053    12297  15678  19580  -6291   -324   3375       N\\nATOM   1740  CA  ASN A1053      53.118  11.156  37.692  1.00123.03           C\\nANISOU 1740  CA  ASN A1053    11481  15629  19636  -6002   -663   3022       C\\nATOM   1741  C   ASN A1053      52.002  11.117  38.731  1.00122.77           C\\nANISOU 1741  C   ASN A1053    11968  15217  19462  -5447  -1194   2750       C\\nATOM   1742  O   ASN A1053      51.786  12.056  39.502  1.00122.02           O\\nANISOU 1742  O   ASN A1053    12131  14690  19541  -5602  -1734   2626       O\\nATOM   1743  CB  ASN A1053      54.234  12.115  38.089  1.00126.67           C\\nANISOU 1743  CB  ASN A1053    11485  16063  20583  -6663   -923   3047       C\\nATOM   1744  N   THR A1054      51.272   9.995  38.739  1.00124.33           N\\nANISOU 1744  N   THR A1054    12319  15587  19333  -4804  -1013   2632       N\\nATOM   1745  CA  THR A1054      50.060   9.901  39.547  1.00119.55           C\\nANISOU 1745  CA  THR A1054    12244  14668  18513  -4306  -1394   2406       C\\nATOM   1746  C   THR A1054      50.366   9.947  41.037  1.00119.71           C\\nANISOU 1746  C   THR A1054    12048  14716  18720  -4133  -1918   2083       C\\nATOM   1747  O   THR A1054      49.504  10.334  41.835  1.00120.96           O\\nANISOU 1747  O   THR A1054    12645  14548  18764  -3922  -2315   1863       O\\nATOM   1748  CB  THR A1054      49.295   8.620  39.212  1.00115.03           C\\nANISOU 1748  CB  THR A1054    11827  14310  17568  -3728  -1059   2370       C\\nATOM   1749  N   ASN A1055      51.577   9.556  41.433  1.00118.97           N\\nANISOU 1749  N   ASN A1055    11271  15030  18901  -4213  -1934   2029       N\\nATOM   1750  CA  ASN A1055      52.004   9.557  42.830  1.00116.22           C\\nANISOU 1750  CA  ASN A1055    10681  14771  18707  -4084  -2473   1748       C\\nATOM   1751  C   ASN A1055      51.115   8.687  43.711  1.00119.38           C\\nANISOU 1751  C   ASN A1055    11395  15214  18750  -3437  -2650   1539       C\\nATOM   1752  O   ASN A1055      51.131   8.822  44.935  1.00121.96           O\\nANISOU 1752  O   ASN A1055    11754  15533  19052  -3324  -3143   1293       O\\nATOM   1753  CB  ASN A1055      52.071  10.984  43.391  1.00109.11           C\\nANISOU 1753  CB  ASN A1055     9992  13444  18023  -4552  -2980   1627       C\\nATOM   1754  N   GLY A1056      50.340   7.783  43.111  1.00115.78           N\\nANISOU 1754  N   GLY A1056    11183  14819  17987  -3045  -2253   1632       N\\nATOM   1755  CA  GLY A1056      49.518   6.838  43.832  1.00115.99           C\\nANISOU 1755  CA  GLY A1056    11480  14915  17677  -2485  -2341   1489       C\\nATOM   1756  C   GLY A1056      48.027   7.076  43.671  1.00112.88           C\\nANISOU 1756  C   GLY A1056    11762  14182  16944  -2317  -2293   1431       C\\nATOM   1757  O   GLY A1056      47.247   6.120  43.742  1.00109.86           O\\nANISOU 1757  O   GLY A1056    11592  13885  16264  -1902  -2132   1408       O\\nATOM   1758  N   VAL A1057      47.618   8.323  43.454  1.00113.85           N\\nANISOU 1758  N   VAL A1057    12208  13906  17145  -2632  -2448   1405       N\\nATOM   1759  CA  VAL A1057      46.211   8.699  43.361  1.00103.36           C\\nANISOU 1759  CA  VAL A1057    11467  12226  15579  -2456  -2483   1304       C\\nATOM   1760  C   VAL A1057      45.881   9.003  41.907  1.00105.21           C\\nANISOU 1760  C   VAL A1057    11904  12256  15814  -2653  -2149   1598       C\\nATOM   1761  O   VAL A1057      46.708   9.560  41.176  1.00111.08           O\\nANISOU 1761  O   VAL A1057    12459  12960  16785  -3103  -2041   1831       O\\nATOM   1762  CB  VAL A1057      45.900   9.912  44.260  1.00 96.42           C\\nANISOU 1762  CB  VAL A1057    10853  10979  14804  -2591  -2980   1005       C\\nATOM   1763  N   ILE A1058      44.667   8.639  41.488  1.00104.59           N\\nANISOU 1763  N   ILE A1058    12209  12071  15459  -2350  -1994   1597       N\\nATOM   1764  CA  ILE A1058      44.203   8.889  40.131  1.00100.91           C\\nANISOU 1764  CA  ILE A1058    12012  11414  14916  -2498  -1744   1872       C\\nATOM   1765  C   ILE A1058      42.794   9.466  40.170  1.00 98.60           C\\nANISOU 1765  C   ILE A1058    12224  10714  14524  -2295  -1978   1737       C\\nATOM   1766  O   ILE A1058      42.091   9.405  41.182  1.00 92.24           O\\nANISOU 1766  O   ILE A1058    11523   9875  13648  -1976  -2199   1403       O\\nATOM   1767  CB  ILE A1058      44.229   7.619  39.253  1.00 94.08           C\\nANISOU 1767  CB  ILE A1058    11024  10914  13808  -2321  -1243   2041       C\\nATOM   1768  CG1 ILE A1058      43.313   6.543  39.831  1.00 82.54           C\\nANISOU 1768  CG1 ILE A1058     9675   9599  12089  -1804  -1208   1830       C\\nATOM   1769  CG2 ILE A1058      45.650   7.101  39.083  1.00 91.55           C\\nANISOU 1769  CG2 ILE A1058    10149  10986  13649  -2498   -980   2147       C\\nATOM   1770  CD1 ILE A1058      43.175   5.325  38.950  1.00 80.94           C\\nANISOU 1770  CD1 ILE A1058     9440   9653  11661  -1618   -764   1951       C\\nATOM   1771  N   THR A1059      42.391  10.038  39.038  1.00100.27           N\\nANISOU 1771  N   THR A1059    12740  10636  14723  -2488  -1928   2000       N\\nATOM   1772  CA  THR A1059      41.046  10.571  38.887  1.00100.12           C\\nANISOU 1772  CA  THR A1059    13164  10218  14658  -2267  -2166   1907       C\\nATOM   1773  C   THR A1059      40.043   9.431  38.714  1.00 93.93           C\\nANISOU 1773  C   THR A1059    12445   9697  13549  -1832  -1928   1816       C\\nATOM   1774  O   THR A1059      40.390   8.322  38.302  1.00 93.12           O\\nANISOU 1774  O   THR A1059    12152   9988  13239  -1781  -1546   1935       O\\nATOM   1775  CB  THR A1059      40.982  11.515  37.681  1.00103.74           C\\nANISOU 1775  CB  THR A1059    13952  10269  15193  -2630  -2248   2286       C\\nATOM   1776  OG1 THR A1059      42.175  12.306  37.630  1.00105.14           O\\nANISOU 1776  OG1 THR A1059    13991  10320  15636  -3159  -2321   2476       O\\nATOM   1777  CG2 THR A1059      39.778  12.440  37.771  1.00108.32           C\\nANISOU 1777  CG2 THR A1059    14955  10292  15912  -2422  -2687   2144       C\\nATOM   1778  N   LYS A1060      38.780   9.709  39.047  1.00 98.18           N\\nANISOU 1778  N   LYS A1060    13229  10001  14072  -1515  -2161   1570       N\\nATOM   1779  CA  LYS A1060      37.721   8.768  38.697  1.00 98.24           C\\nANISOU 1779  CA  LYS A1060    13319  10201  13806  -1182  -1964   1522       C\\nATOM   1780  C   LYS A1060      37.594   8.635  37.188  1.00 99.60           C\\nANISOU 1780  C   LYS A1060    13688  10335  13819  -1346  -1790   1903       C\\nATOM   1781  O   LYS A1060      37.139   7.599  36.688  1.00 95.67           O\\nANISOU 1781  O   LYS A1060    13192  10106  13053  -1183  -1519   1935       O\\nATOM   1782  CB  LYS A1060      36.389   9.207  39.307  1.00 93.38           C\\nANISOU 1782  CB  LYS A1060    12863   9359  13257   -838  -2249   1162       C\\nATOM   1783  N   ASP A1061      37.997   9.671  36.449  1.00103.09           N\\nANISOU 1783  N   ASP A1061    14329  10441  14400  -1703  -1952   2200       N\\nATOM   1784  CA  ASP A1061      38.006   9.603  34.993  1.00101.97           C\\nANISOU 1784  CA  ASP A1061    14414  10301  14028  -1942  -1780   2607       C\\nATOM   1785  C   ASP A1061      39.176   8.768  34.485  1.00100.34           C\\nANISOU 1785  C   ASP A1061    13939  10555  13629  -2196  -1275   2797       C\\nATOM   1786  O   ASP A1061      39.012   7.961  33.563  1.00 99.43           O\\nANISOU 1786  O   ASP A1061    13894  10699  13185  -2180   -958   2926       O\\nATOM   1787  CB  ASP A1061      38.055  11.015  34.413  1.00102.76           C\\nANISOU 1787  CB  ASP A1061    14862   9863  14320  -2281  -2142   2907       C\\nATOM   1788  CG  ASP A1061      37.962  11.029  32.903  1.00102.52           C\\nANISOU 1788  CG  ASP A1061    15156   9822  13974  -2555  -2021   3367       C\\nATOM   1789  OD1 ASP A1061      36.881  10.700  32.371  1.00 98.49           O\\nANISOU 1789  OD1 ASP A1061    14872   9291  13258  -2289  -2114   3362       O\\nATOM   1790  OD2 ASP A1061      38.970  11.374  32.248  1.00105.90           O\\nANISOU 1790  OD2 ASP A1061    15607  10290  14339  -3064  -1832   3728       O\\nATOM   1791  N   GLU A1062      40.362   8.948  35.075  1.00102.50           N\\nANISOU 1791  N   GLU A1062    13880  10945  14119  -2420  -1205   2776       N\\nATOM   1792  CA  GLU A1062      41.504   8.118  34.707  1.00 96.62           C\\nANISOU 1792  CA  GLU A1062    12770  10671  13271  -2592   -725   2880       C\\nATOM   1793  C   GLU A1062      41.237   6.651  35.014  1.00 88.82           C\\nANISOU 1793  C   GLU A1062    11588  10061  12098  -2156   -455   2641       C\\nATOM   1794  O   GLU A1062      41.657   5.764  34.262  1.00 83.40           O\\nANISOU 1794  O   GLU A1062    10776   9705  11208  -2174    -28   2718       O\\nATOM   1795  CB  GLU A1062      42.761   8.595  35.435  1.00 87.02           C\\nANISOU 1795  CB  GLU A1062    11163   9509  12392  -2870   -785   2852       C\\nATOM   1796  CG  GLU A1062      43.240   9.972  35.025  1.00 95.42           C\\nANISOU 1796  CG  GLU A1062    12385  10212  13658  -3416   -988   3136       C\\nATOM   1797  CD  GLU A1062      44.494  10.395  35.768  1.00 99.73           C\\nANISOU 1797  CD  GLU A1062    12491  10838  14563  -3723  -1061   3077       C\\nATOM   1798  OE1 GLU A1062      44.628  10.042  36.959  1.00 95.17           O\\nANISOU 1798  OE1 GLU A1062    11645  10382  14135  -3431  -1231   2743       O\\nATOM   1799  OE2 GLU A1062      45.347  11.075  35.159  1.00104.48           O\\nANISOU 1799  OE2 GLU A1062    13018  11399  15279  -4288   -958   3375       O\\nATOM   1800  N   ALA A1063      40.542   6.377  36.121  1.00 85.45           N\\nANISOU 1800  N   ALA A1063    11151   9581  11735  -1777   -689   2337       N\\nATOM   1801  CA  ALA A1063      40.186   5.003  36.456  1.00 86.64           C\\nANISOU 1801  CA  ALA A1063    11186  10021  11712  -1400   -477   2151       C\\nATOM   1802  C   ALA A1063      39.112   4.459  35.526  1.00 88.99           C\\nANISOU 1802  C   ALA A1063    11790  10309  11715  -1259   -345   2190       C\\nATOM   1803  O   ALA A1063      39.030   3.242  35.325  1.00 88.77           O\\nANISOU 1803  O   ALA A1063    11692  10524  11512  -1068    -60   2120       O\\nATOM   1804  CB  ALA A1063      39.719   4.914  37.909  1.00 84.46           C\\nANISOU 1804  CB  ALA A1063    10850   9716  11524  -1112   -751   1850       C\\nATOM   1805  N   GLU A1064      38.283   5.337  34.957  1.00 91.39           N\\nANISOU 1805  N   GLU A1064    12438  10307  11980  -1346   -590   2294       N\\nATOM   1806  CA  GLU A1064      37.273   4.882  34.009  1.00 91.30           C\\nANISOU 1806  CA  GLU A1064    12709  10296  11686  -1243   -529   2345       C\\nATOM   1807  C   GLU A1064      37.898   4.478  32.678  1.00 95.38           C\\nANISOU 1807  C   GLU A1064    13297  11022  11922  -1504   -156   2596       C\\nATOM   1808  O   GLU A1064      37.402   3.560  32.016  1.00 93.85           O\\nANISOU 1808  O   GLU A1064    13219  10996  11445  -1384     47   2550       O\\nATOM   1809  CB  GLU A1064      36.216   5.969  33.805  1.00 88.36           C\\nANISOU 1809  CB  GLU A1064    12660   9522  11391  -1222   -972   2387       C\\nATOM   1810  CG  GLU A1064      34.995   5.506  33.022  1.00 85.95           C\\nANISOU 1810  CG  GLU A1064    12598   9220  10839  -1054  -1023   2379       C\\nATOM   1811  CD  GLU A1064      33.877   6.532  33.012  1.00 92.64           C\\nANISOU 1811  CD  GLU A1064    13676   9668  11857   -926  -1527   2353       C\\nATOM   1812  OE1 GLU A1064      32.798   6.224  32.460  1.00 92.14           O\\nANISOU 1812  OE1 GLU A1064    13758   9602  11649   -763  -1648   2318       O\\nATOM   1813  OE2 GLU A1064      34.072   7.641  33.555  1.00 96.90           O\\nANISOU 1813  OE2 GLU A1064    14234   9879  12704   -975  -1826   2343       O\\nATOM   1814  N   LYS A1065      38.982   5.144  32.270  1.00 96.04           N\\nANISOU 1814  N   LYS A1065    13309  11119  12064  -1890    -43   2837       N\\nATOM   1815  CA  LYS A1065      39.706   4.695  31.086  1.00 95.76           C\\nANISOU 1815  CA  LYS A1065    13269  11382  11732  -2158    412   3024       C\\nATOM   1816  C   LYS A1065      40.338   3.328  31.321  1.00 92.50           C\\nANISOU 1816  C   LYS A1065    12480  11360  11306  -1927    838   2784       C\\nATOM   1817  O   LYS A1065      40.296   2.460  30.442  1.00 93.15           O\\nANISOU 1817  O   LYS A1065    12640  11673  11077  -1892   1185   2745       O\\nATOM   1818  CB  LYS A1065      40.767   5.724  30.695  1.00 97.00           C\\nANISOU 1818  CB  LYS A1065    13372  11502  11982  -2673    474   3332       C\\nATOM   1819  N   LEU A1066      40.918   3.114  32.505  1.00 86.38           N\\nANISOU 1819  N   LEU A1066    11317  10638  10865  -1755    781   2609       N\\nATOM   1820  CA  LEU A1066      41.504   1.814  32.815  1.00 89.95           C\\nANISOU 1820  CA  LEU A1066    11422  11389  11367  -1482   1095   2400       C\\nATOM   1821  C   LEU A1066      40.439   0.729  32.871  1.00 88.33           C\\nANISOU 1821  C   LEU A1066    11426  11159  10977  -1113   1097   2208       C\\nATOM   1822  O   LEU A1066      40.672  -0.401  32.428  1.00 91.55           O\\nANISOU 1822  O   LEU A1066    11755  11759  11269   -957   1433   2085       O\\nATOM   1823  CB  LEU A1066      42.265   1.875  34.139  1.00 96.43           C\\nANISOU 1823  CB  LEU A1066    11833  12240  12567  -1373    917   2292       C\\nATOM   1824  CG  LEU A1066      43.442   2.845  34.220  1.00110.23           C\\nANISOU 1824  CG  LEU A1066    13274  14038  14572  -1754    899   2439       C\\nATOM   1825  CD1 LEU A1066      44.173   2.679  35.543  1.00109.37           C\\nANISOU 1825  CD1 LEU A1066    12741  14009  14807  -1592    693   2287       C\\nATOM   1826  CD2 LEU A1066      44.392   2.653  33.043  1.00117.21           C\\nANISOU 1826  CD2 LEU A1066    13951  15231  15353  -2035   1407   2560       C\\nATOM   1827  N   PHE A1067      39.266   1.055  33.417  1.00 88.20           N\\nANISOU 1827  N   PHE A1067    11656  10901  10956   -977    731   2152       N\\nATOM   1828  CA  PHE A1067      38.202   0.064  33.527  1.00 86.10           C\\nANISOU 1828  CA  PHE A1067    11554  10620  10539   -687    725   1975       C\\nATOM   1829  C   PHE A1067      37.743  -0.409  32.155  1.00 85.87           C\\nANISOU 1829  C   PHE A1067    11803  10657  10168   -762    941   2008       C\\nATOM   1830  O   PHE A1067      37.513  -1.606  31.949  1.00 84.89           O\\nANISOU 1830  O   PHE A1067    11703  10627   9925   -580   1146   1847       O\\nATOM   1831  CB  PHE A1067      37.028   0.640  34.316  1.00 89.23           C\\nANISOU 1831  CB  PHE A1067    12101  10796  11006   -569    323   1888       C\\nATOM   1832  CG  PHE A1067      35.849  -0.282  34.400  1.00 87.05           C\\nANISOU 1832  CG  PHE A1067    11964  10525  10586   -347    317   1719       C\\nATOM   1833  CD1 PHE A1067      35.865  -1.372  35.252  1.00 83.17           C\\nANISOU 1833  CD1 PHE A1067    11332  10130  10137   -136    418   1574       C\\nATOM   1834  CD2 PHE A1067      34.724  -0.058  33.627  1.00 86.11           C\\nANISOU 1834  CD2 PHE A1067    12115  10304  10299   -373    179   1726       C\\nATOM   1835  CE1 PHE A1067      34.781  -2.221  35.329  1.00 78.20           C\\nANISOU 1835  CE1 PHE A1067    10832   9493   9387     -3    424   1440       C\\nATOM   1836  CE2 PHE A1067      33.638  -0.903  33.702  1.00 81.95           C\\nANISOU 1836  CE2 PHE A1067    11664   9800   9671   -214    168   1558       C\\nATOM   1837  CZ  PHE A1067      33.666  -1.985  34.553  1.00 78.15           C\\nANISOU 1837  CZ  PHE A1067    11043   9414   9235    -52    312   1415       C\\nATOM   1838  N   ASN A1068      37.604   0.516  31.201  1.00 90.24           N\\nANISOU 1838  N   ASN A1068    12604  11140  10543  -1046    869   2222       N\\nATOM   1839  CA  ASN A1068      37.203   0.127  29.853  1.00 83.46           C\\nANISOU 1839  CA  ASN A1068    12053  10378   9278  -1159   1045   2269       C\\nATOM   1840  C   ASN A1068      38.222  -0.816  29.228  1.00 82.78           C\\nANISOU 1840  C   ASN A1068    11803  10602   9046  -1191   1575   2173       C\\nATOM   1841  O   ASN A1068      37.856  -1.728  28.479  1.00 84.94           O\\nANISOU 1841  O   ASN A1068    12255  10985   9033  -1118   1777   2024       O\\nATOM   1842  CB  ASN A1068      37.008   1.367  28.984  1.00 87.76           C\\nANISOU 1842  CB  ASN A1068    12920  10786   9638  -1498    837   2587       C\\nATOM   1843  CG  ASN A1068      35.631   1.982  29.145  1.00 95.27           C\\nANISOU 1843  CG  ASN A1068    14135  11430  10632  -1379    315   2609       C\\nATOM   1844  OD1 ASN A1068      34.845   2.027  28.198  1.00102.99           O\\nANISOU 1844  OD1 ASN A1068    15454  12372  11305  -1446    169   2702       O\\nATOM   1845  ND2 ASN A1068      35.327   2.448  30.350  1.00 94.72           N\\nANISOU 1845  ND2 ASN A1068    13890  11159  10939  -1190     20   2495       N\\nATOM   1846  N   GLN A1069      39.507  -0.618  29.532  1.00 82.90           N\\nANISOU 1846  N   GLN A1069    11450  10766   9281  -1289   1799   2217       N\\nATOM   1847  CA  GLN A1069      40.533  -1.532  29.041  1.00 93.96           C\\nANISOU 1847  CA  GLN A1069    12588  12479  10633  -1250   2317   2059       C\\nATOM   1848  C   GLN A1069      40.355  -2.926  29.631  1.00 96.67           C\\nANISOU 1848  C   GLN A1069    12801  12800  11129   -811   2383   1749       C\\nATOM   1849  O   GLN A1069      40.472  -3.931  28.918  1.00 96.30           O\\nANISOU 1849  O   GLN A1069    12800  12887  10901   -697   2721   1539       O\\nATOM   1850  CB  GLN A1069      41.922  -0.978  29.364  1.00104.31           C\\nANISOU 1850  CB  GLN A1069    13439  13961  12234  -1436   2488   2158       C\\nATOM   1851  CG  GLN A1069      42.191   0.399  28.770  1.00112.15           C\\nANISOU 1851  CG  GLN A1069    14573  14942  13096  -1947   2442   2503       C\\nATOM   1852  CD  GLN A1069      43.505   1.002  29.237  1.00116.78           C\\nANISOU 1852  CD  GLN A1069    14664  15667  14039  -2175   2548   2595       C\\nATOM   1853  OE1 GLN A1069      44.350   0.314  29.812  1.00124.86           O\\nANISOU 1853  OE1 GLN A1069    15191  16882  15370  -1946   2730   2385       O\\nATOM   1854  NE2 GLN A1069      43.681   2.297  28.993  1.00109.98           N\\nANISOU 1854  NE2 GLN A1069    13937  14684  13167  -2636   2395   2919       N\\nATOM   1855  N   ASP A1070      40.068  -3.007  30.934  1.00 93.20           N\\nANISOU 1855  N   ASP A1070    12231  12176  11004   -577   2056   1715       N\\nATOM   1856  CA  ASP A1070      39.831  -4.304  31.560  1.00 92.78           C\\nANISOU 1856  CA  ASP A1070    12121  12049  11083   -206   2064   1494       C\\nATOM   1857  C   ASP A1070      38.580  -4.968  31.000  1.00 84.10           C\\nANISOU 1857  C   ASP A1070    11427  10832   9697   -148   2030   1376       C\\nATOM   1858  O   ASP A1070      38.532  -6.195  30.858  1.00 74.28           O\\nANISOU 1858  O   ASP A1070    10218   9558   8448     64   2204   1167       O\\nATOM   1859  CB  ASP A1070      39.714  -4.145  33.076  1.00 97.16           C\\nANISOU 1859  CB  ASP A1070    12517  12464  11936    -46   1705   1529       C\\nATOM   1860  CG  ASP A1070      40.993  -3.637  33.711  1.00101.50           C\\nANISOU 1860  CG  ASP A1070    12635  13134  12794    -83   1688   1606       C\\nATOM   1861  OD1 ASP A1070      42.082  -3.940  33.181  1.00105.37           O\\nANISOU 1861  OD1 ASP A1070    12832  13826  13379    -89   2015   1558       O\\nATOM   1862  OD2 ASP A1070      40.905  -2.936  34.743  1.00 98.07           O\\nANISOU 1862  OD2 ASP A1070    12136  12614  12514   -110   1349   1680       O\\nATOM   1863  N   VAL A1071      37.557  -4.174  30.679  1.00 85.78           N\\nANISOU 1863  N   VAL A1071    11939  10950   9704   -328   1771   1495       N\\nATOM   1864  CA  VAL A1071      36.322  -4.733  30.136  1.00 82.23           C\\nANISOU 1864  CA  VAL A1071    11829  10413   9002   -301   1681   1379       C\\nATOM   1865  C   VAL A1071      36.565  -5.310  28.749  1.00 86.97           C\\nANISOU 1865  C   VAL A1071    12623  11169   9251   -401   2023   1266       C\\nATOM   1866  O   VAL A1071      36.169  -6.443  28.455  1.00 91.66           O\\nANISOU 1866  O   VAL A1071    13352  11723   9752   -267   2137   1029       O\\nATOM   1867  CB  VAL A1071      35.214  -3.667  30.113  1.00 77.64           C\\nANISOU 1867  CB  VAL A1071    11459   9702   8338   -435   1276   1525       C\\nATOM   1868  CG1 VAL A1071      34.018  -4.169  29.323  1.00 68.20           C\\nANISOU 1868  CG1 VAL A1071    10579   8473   6862   -455   1173   1415       C\\nATOM   1869  CG2 VAL A1071      34.807  -3.308  31.524  1.00 79.71           C\\nANISOU 1869  CG2 VAL A1071    11544   9829   8913   -289    982   1517       C\\nATOM   1870  N   ASP A1072      37.208  -4.533  27.872  1.00 86.89           N\\nANISOU 1870  N   ASP A1072    12656  11340   9019   -672   2197   1425       N\\nATOM   1871  CA  ASP A1072      37.548  -5.045  26.549  1.00 93.69           C\\nANISOU 1871  CA  ASP A1072    13699  12426   9474   -799   2587   1294       C\\nATOM   1872  C   ASP A1072      38.419  -6.289  26.649  1.00 93.29           C\\nANISOU 1872  C   ASP A1072    13380  12470   9598   -530   3002    969       C\\nATOM   1873  O   ASP A1072      38.186  -7.273  25.940  1.00100.45           O\\nANISOU 1873  O   ASP A1072    14485  13404  10277   -445   3208    683       O\\nATOM   1874  CB  ASP A1072      38.246  -3.964  25.724  1.00101.72           C\\nANISOU 1874  CB  ASP A1072    14764  13660  10224  -1186   2755   1563       C\\nATOM   1875  CG  ASP A1072      37.274  -2.951  25.152  1.00105.64           C\\nANISOU 1875  CG  ASP A1072    15691  14039  10407  -1457   2355   1858       C\\nATOM   1876  OD1 ASP A1072      36.104  -3.321  24.911  1.00105.43           O\\nANISOU 1876  OD1 ASP A1072    15959  13888  10212  -1367   2080   1761       O\\nATOM   1877  OD2 ASP A1072      37.677  -1.787  24.942  1.00108.66           O\\nANISOU 1877  OD2 ASP A1072    16112  14434  10740  -1764   2286   2192       O\\nATOM   1878  N   ALA A1073      39.417  -6.269  27.537  1.00 84.98           N\\nANISOU 1878  N   ALA A1073    11874  11440   8973   -376   3089    988       N\\nATOM   1879  CA  ALA A1073      40.250  -7.451  27.738  1.00 87.42           C\\nANISOU 1879  CA  ALA A1073    11887  11783   9546    -46   3401    685       C\\nATOM   1880  C   ALA A1073      39.418  -8.640  28.199  1.00 88.42           C\\nANISOU 1880  C   ALA A1073    12207  11603   9787    254   3220    480       C\\nATOM   1881  O   ALA A1073      39.645  -9.774  27.760  1.00 91.45           O\\nANISOU 1881  O   ALA A1073    12623  11947  10175    465   3482    159       O\\nATOM   1882  CB  ALA A1073      41.357  -7.149  28.747  1.00 88.38           C\\nANISOU 1882  CB  ALA A1073    11477  11958  10146     77   3385    785       C\\nATOM   1883  N   ALA A1074      38.441  -8.397  29.079  1.00 83.01           N\\nANISOU 1883  N   ALA A1074    11651  10689   9199    259   2785    645       N\\nATOM   1884  CA  ALA A1074      37.590  -9.476  29.567  1.00 85.44           C\\nANISOU 1884  CA  ALA A1074    12143  10714   9605    456   2615    500       C\\nATOM   1885  C   ALA A1074      36.749 -10.084  28.454  1.00 93.89           C\\nANISOU 1885  C   ALA A1074    13614  11749  10313    356   2695    279       C\\nATOM   1886  O   ALA A1074      36.388 -11.263  28.528  1.00 97.64           O\\nANISOU 1886  O   ALA A1074    14228  11998  10874    520   2705     57       O\\nATOM   1887  CB  ALA A1074      36.686  -8.968  30.689  1.00 78.28           C\\nANISOU 1887  CB  ALA A1074    11263   9662   8819    417   2191    709       C\\nATOM   1888  N   VAL A1075      36.430  -9.305  27.419  1.00 95.22           N\\nANISOU 1888  N   VAL A1075    13998  12114  10069     70   2718    348       N\\nATOM   1889  CA  VAL A1075      35.614  -9.821  26.325  1.00 92.66           C\\nANISOU 1889  CA  VAL A1075    14075  11790   9341    -54   2737    139       C\\nATOM   1890  C   VAL A1075      36.457 -10.646  25.357  1.00100.97           C\\nANISOU 1890  C   VAL A1075    15170  12983  10213     22   3217   -207       C\\nATOM   1891  O   VAL A1075      35.987 -11.658  24.824  1.00101.40           O\\nANISOU 1891  O   VAL A1075    15489  12912  10125     79   3272   -531       O\\nATOM   1892  CB  VAL A1075      34.888  -8.661  25.617  1.00 82.73           C\\nANISOU 1892  CB  VAL A1075    13071  10672   7689   -380   2491    377       C\\nATOM   1893  CG1 VAL A1075      34.069  -9.171  24.446  1.00 75.94           C\\nANISOU 1893  CG1 VAL A1075    12635   9852   6368   -528   2457    166       C\\nATOM   1894  CG2 VAL A1075      33.993  -7.930  26.604  1.00 76.88           C\\nANISOU 1894  CG2 VAL A1075    12256   9765   7192   -384   2023    620       C\\nATOM   1895  N   ARG A1076      37.712 -10.240  25.115  1.00100.09           N\\nANISOU 1895  N   ARG A1076    14776  13139  10116     17   3583   -182       N\\nATOM   1896  CA  ARG A1076      38.592 -11.049  24.273  1.00106.02           C\\nANISOU 1896  CA  ARG A1076    15475  14062  10744    139   4103   -579       C\\nATOM   1897  C   ARG A1076      38.740 -12.458  24.828  1.00110.21           C\\nANISOU 1897  C   ARG A1076    15911  14258  11706    564   4141   -922       C\\nATOM   1898  O   ARG A1076      38.867 -13.421  24.062  1.00118.72           O\\nANISOU 1898  O   ARG A1076    17153  15310  12647    690   4425  -1359       O\\nATOM   1899  CB  ARG A1076      39.980 -10.411  24.143  1.00109.75           C\\nANISOU 1899  CB  ARG A1076    15519  14893  11289     84   4503   -500       C\\nATOM   1900  CG  ARG A1076      40.027  -8.904  24.227  1.00109.02           C\\nANISOU 1900  CG  ARG A1076    15378  14979  11066   -286   4338    -22       C\\nATOM   1901  CD  ARG A1076      39.706  -8.229  22.910  1.00113.54           C\\nANISOU 1901  CD  ARG A1076    16360  15831  10947   -724   4457     91       C\\nATOM   1902  NE  ARG A1076      39.657  -6.778  23.063  1.00113.48           N\\nANISOU 1902  NE  ARG A1076    16365  15872  10879  -1069   4203    591       N\\nATOM   1903  CZ  ARG A1076      39.507  -5.923  22.058  1.00114.12           C\\nANISOU 1903  CZ  ARG A1076    16787  16166  10409  -1503   4233    842       C\\nATOM   1904  NH1 ARG A1076      39.395  -6.367  20.812  1.00118.70           N\\nANISOU 1904  NH1 ARG A1076    17722  16997  10383  -1663   4528    629       N\\nATOM   1905  NH2 ARG A1076      39.471  -4.619  22.301  1.00110.17           N\\nANISOU 1905  NH2 ARG A1076    16305  15605   9949  -1786   3945   1307       N\\nATOM   1906  N   GLY A1077      38.727 -12.597  26.152  1.00104.33           N\\nANISOU 1906  N   GLY A1077    14938  13235  11468    780   3843   -732       N\\nATOM   1907  CA  GLY A1077      38.862 -13.893  26.781  1.00103.24           C\\nANISOU 1907  CA  GLY A1077    14749  12715  11761   1164   3801   -960       C\\nATOM   1908  C   GLY A1077      37.555 -14.652  26.832  1.00100.52           C\\nANISOU 1908  C   GLY A1077    14844  12012  11338   1106   3509  -1046       C\\nATOM   1909  O   GLY A1077      37.538 -15.875  26.663  1.00104.59           O\\nANISOU 1909  O   GLY A1077    15516  12220  12003   1321   3586  -1382       O\\nATOM   1910  N   ILE A1078      36.453 -13.936  27.070  1.00 99.32           N\\nANISOU 1910  N   ILE A1078    14869  11880  10988    814   3165   -762       N\\nATOM   1911  CA  ILE A1078      35.138 -14.573  27.087  1.00 95.36           C\\nANISOU 1911  CA  ILE A1078    14721  11103  10410    692   2887   -841       C\\nATOM   1912  C   ILE A1078      34.872 -15.266  25.758  1.00 94.23           C\\nANISOU 1912  C   ILE A1078    14931  10962   9909    611   3076  -1259       C\\nATOM   1913  O   ILE A1078      34.461 -16.432  25.713  1.00 91.07           O\\nANISOU 1913  O   ILE A1078    14757  10213   9633    693   3032  -1537       O\\nATOM   1914  CB  ILE A1078      34.042 -13.542  27.412  1.00 93.90           C\\nANISOU 1914  CB  ILE A1078    14585  11030  10063    404   2522   -518       C\\nATOM   1915  CG1 ILE A1078      33.993 -13.263  28.917  1.00 93.60           C\\nANISOU 1915  CG1 ILE A1078    14291  10873  10400    497   2289   -213       C\\nATOM   1916  CG2 ILE A1078      32.692 -14.024  26.911  1.00 91.88           C\\nANISOU 1916  CG2 ILE A1078    14674  10646   9590    192   2300   -673       C\\nATOM   1917  CD1 ILE A1078      33.002 -12.183  29.313  1.00 86.14           C\\nANISOU 1917  CD1 ILE A1078    13326  10053   9351    273   1966     41       C\\nATOM   1918  N   LEU A1079      35.121 -14.560  24.654  1.00 96.21           N\\nANISOU 1918  N   LEU A1079    15266  11598   9690    421   3283  -1311       N\\nATOM   1919  CA  LEU A1079      34.910 -15.148  23.339  1.00 99.06           C\\nANISOU 1919  CA  LEU A1079    15997  12035   9608    315   3475  -1730       C\\nATOM   1920  C   LEU A1079      35.911 -16.261  23.058  1.00104.43           C\\nANISOU 1920  C   LEU A1079    16609  12586  10483    653   3898  -2204       C\\nATOM   1921  O   LEU A1079      35.576 -17.237  22.375  1.00107.18           O\\nANISOU 1921  O   LEU A1079    17287  12752  10686    675   3966  -2650       O\\nATOM   1922  CB  LEU A1079      34.990 -14.061  22.271  1.00 97.08           C\\nANISOU 1922  CB  LEU A1079    15879  12261   8747     -2   3592  -1606       C\\nATOM   1923  CG  LEU A1079      34.022 -12.896  22.494  1.00 92.62           C\\nANISOU 1923  CG  LEU A1079    15381  11775   8035   -286   3126  -1146       C\\nATOM   1924  CD1 LEU A1079      34.208 -11.832  21.427  1.00 87.85           C\\nANISOU 1924  CD1 LEU A1079    14956  11583   6838   -599   3216   -967       C\\nATOM   1925  CD2 LEU A1079      32.586 -13.395  22.521  1.00 89.61           C\\nANISOU 1925  CD2 LEU A1079    15271  11148   7628   -399   2691  -1233       C\\nATOM   1926  N   ARG A1080      37.134 -16.141  23.574  1.00102.78           N\\nANISOU 1926  N   ARG A1080    15961  12455  10635    932   4161  -2150       N\\nATOM   1927  CA  ARG A1080      38.113 -17.215  23.463  1.00106.42           C\\nANISOU 1927  CA  ARG A1080    16265  12749  11422   1346   4516  -2607       C\\nATOM   1928  C   ARG A1080      37.864 -18.345  24.454  1.00114.00           C\\nANISOU 1928  C   ARG A1080    17260  13084  12971   1658   4225  -2653       C\\nATOM   1929  O   ARG A1080      38.585 -19.348  24.417  1.00121.35           O\\nANISOU 1929  O   ARG A1080    18104  13749  14255   2055   4430  -3041       O\\nATOM   1930  CB  ARG A1080      39.528 -16.662  23.652  1.00 95.46           C\\nANISOU 1930  CB  ARG A1080    14320  11699  10249   1534   4874  -2535       C\\nATOM   1931  N   ASN A1081      36.877 -18.203  25.339  1.00113.30           N\\nANISOU 1931  N   ASN A1081    17292  12754  13003   1487   3760  -2268       N\\nATOM   1932  CA  ASN A1081      36.488 -19.263  26.264  1.00110.82           C\\nANISOU 1932  CA  ASN A1081    17098  11850  13160   1666   3466  -2242       C\\nATOM   1933  C   ASN A1081      35.348 -20.052  25.630  1.00107.85           C\\nANISOU 1933  C   ASN A1081    17225  11189  12565   1437   3324  -2533       C\\nATOM   1934  O   ASN A1081      34.255 -19.516  25.418  1.00 96.74           O\\nANISOU 1934  O   ASN A1081    16004   9943  10809   1044   3098  -2372       O\\nATOM   1935  CB  ASN A1081      36.075 -18.682  27.614  1.00104.89           C\\nANISOU 1935  CB  ASN A1081    16179  11052  12621   1564   3094  -1681       C\\nATOM   1936  CG  ASN A1081      35.935 -19.745  28.696  1.00100.82           C\\nANISOU 1936  CG  ASN A1081    15751   9964  12593   1757   2830  -1573       C\\nATOM   1937  OD1 ASN A1081      35.536 -20.881  28.430  1.00 96.54           O\\nANISOU 1937  OD1 ASN A1081    15540   8975  12166   1793   2783  -1851       O\\nATOM   1938  ND2 ASN A1081      36.265 -19.375  29.927  1.00 99.41           N\\nANISOU 1938  ND2 ASN A1081    15308   9782  12683   1855   2634  -1158       N\\nATOM   1939  N   ALA A1082      35.603 -21.330  25.335  1.00104.72           N\\nANISOU 1939  N   ALA A1082    17030  10346  12412   1693   3425  -2982       N\\nATOM   1940  CA  ALA A1082      34.620 -22.148  24.633  1.00104.56           C\\nANISOU 1940  CA  ALA A1082    17500  10033  12195   1466   3305  -3342       C\\nATOM   1941  C   ALA A1082      33.348 -22.360  25.442  1.00101.54           C\\nANISOU 1941  C   ALA A1082    17302   9334  11945   1142   2845  -3001       C\\nATOM   1942  O   ALA A1082      32.300 -22.654  24.856  1.00101.98           O\\nANISOU 1942  O   ALA A1082    17693   9314  11739    801   2679  -3190       O\\nATOM   1943  CB  ALA A1082      35.231 -23.499  24.264  1.00107.82           C\\nANISOU 1943  CB  ALA A1082    18086   9944  12935   1850   3489  -3914       C\\nATOM   1944  N   LYS A1083      33.409 -22.219  26.764  1.00105.02           N\\nANISOU 1944  N   LYS A1083    17519   9623  12760   1215   2642  -2520       N\\nATOM   1945  CA  LYS A1083      32.243 -22.435  27.607  1.00 99.72           C\\nANISOU 1945  CA  LYS A1083    16986   8701  12202    885   2273  -2194       C\\nATOM   1946  C   LYS A1083      31.446 -21.163  27.871  1.00 97.98           C\\nANISOU 1946  C   LYS A1083    16574   8985  11668    541   2119  -1821       C\\nATOM   1947  O   LYS A1083      30.317 -21.253  28.366  1.00 96.09           O\\nANISOU 1947  O   LYS A1083    16414   8652  11442    209   1857  -1636       O\\nATOM   1948  CB  LYS A1083      32.666 -23.061  28.941  1.00 98.15           C\\nANISOU 1948  CB  LYS A1083    16717   8046  12528   1114   2120  -1873       C\\nATOM   1949  N   LEU A1084      31.992 -19.986  27.551  1.00 99.46           N\\nANISOU 1949  N   LEU A1084    16502   9689  11600    605   2275  -1719       N\\nATOM   1950  CA  LEU A1084      31.288 -18.729  27.771  1.00 97.55           C\\nANISOU 1950  CA  LEU A1084    16090   9867  11109    333   2100  -1390       C\\nATOM   1951  C   LEU A1084      30.919 -17.993  26.491  1.00101.44           C\\nANISOU 1951  C   LEU A1084    16699  10753  11090    121   2131  -1554       C\\nATOM   1952  O   LEU A1084      30.009 -17.161  26.521  1.00102.09           O\\nANISOU 1952  O   LEU A1084    16730  11072  10987   -136   1884  -1351       O\\nATOM   1953  CB  LEU A1084      32.124 -17.790  28.654  1.00 93.67           C\\nANISOU 1953  CB  LEU A1084    15216   9609  10766    522   2147  -1024       C\\nATOM   1954  CG  LEU A1084      32.376 -18.250  30.092  1.00 99.39           C\\nANISOU 1954  CG  LEU A1084    15814  10040  11911    678   2020   -744       C\\nATOM   1955  CD1 LEU A1084      33.068 -17.160  30.896  1.00100.96           C\\nANISOU 1955  CD1 LEU A1084    15645  10540  12174    797   2010   -411       C\\nATOM   1956  CD2 LEU A1084      31.075 -18.668  30.757  1.00 98.30           C\\nANISOU 1956  CD2 LEU A1084    15830   9700  11820    371   1756   -602       C\\nATOM   1957  N   LYS A1085      31.598 -18.269  25.378  1.00102.45           N\\nANISOU 1957  N   LYS A1085    16983  10965  10978    227   2417  -1917       N\\nATOM   1958  CA  LYS A1085      31.262 -17.597  24.126  1.00 99.55           C\\nANISOU 1958  CA  LYS A1085    16799  10990  10037    -13   2431  -2041       C\\nATOM   1959  C   LYS A1085      29.850 -17.899  23.627  1.00 99.81           C\\nANISOU 1959  C   LYS A1085    17128  10950   9847   -354   2083  -2182       C\\nATOM   1960  O   LYS A1085      29.193 -16.966  23.138  1.00 92.79           O\\nANISOU 1960  O   LYS A1085    16268  10388   8598   -594   1861  -2023       O\\nATOM   1961  CB  LYS A1085      32.301 -17.947  23.053  1.00 96.22           C\\nANISOU 1961  CB  LYS A1085    16501  10703   9355    149   2870  -2453       C\\nATOM   1962  N   PRO A1086      29.335 -19.137  23.693  1.00105.32           N\\nANISOU 1962  N   PRO A1086    18044  11220  10751   -402   1987  -2468       N\\nATOM   1963  CA  PRO A1086      27.961 -19.366  23.201  1.00106.72           C\\nANISOU 1963  CA  PRO A1086    18449  11373  10729   -778   1625  -2606       C\\nATOM   1964  C   PRO A1086      26.904 -18.527  23.902  1.00101.72           C\\nANISOU 1964  C   PRO A1086    17551  10915  10184  -1000   1260  -2201       C\\nATOM   1965  O   PRO A1086      26.130 -17.830  23.232  1.00 97.88           O\\nANISOU 1965  O   PRO A1086    17104  10733   9353  -1226    992  -2175       O\\nATOM   1966  CB  PRO A1086      27.759 -20.868  23.445  1.00108.18           C\\nANISOU 1966  CB  PRO A1086    18857  10979  11267   -780   1611  -2917       C\\nATOM   1967  CG  PRO A1086      29.125 -21.438  23.364  1.00108.60           C\\nANISOU 1967  CG  PRO A1086    18951  10834  11479   -369   2012  -3150       C\\nATOM   1968  CD  PRO A1086      30.018 -20.411  23.991  1.00103.81           C\\nANISOU 1968  CD  PRO A1086    17951  10542  10950   -127   2192  -2744       C\\nATOM   1969  N   VAL A1087      26.844 -18.575  25.235  1.00 98.45           N\\nANISOU 1969  N   VAL A1087    16867  10324  10214   -932   1231  -1899       N\\nATOM   1970  CA  VAL A1087      25.825 -17.817  25.956  1.00 96.16           C\\nANISOU 1970  CA  VAL A1087    16290  10223  10024  -1125    937  -1588       C\\nATOM   1971  C   VAL A1087      26.024 -16.321  25.749  1.00 94.05           C\\nANISOU 1971  C   VAL A1087    15830  10386   9517  -1049    881  -1337       C\\nATOM   1972  O   VAL A1087      25.055 -15.564  25.617  1.00 93.16           O\\nANISOU 1972  O   VAL A1087    15592  10501   9302  -1221    565  -1236       O\\nATOM   1973  CB  VAL A1087      25.834 -18.196  27.449  1.00 97.74           C\\nANISOU 1973  CB  VAL A1087    16281  10182  10673  -1078    978  -1328       C\\nATOM   1974  CG1 VAL A1087      27.238 -18.088  28.024  1.00102.40           C\\nANISOU 1974  CG1 VAL A1087    16780  10706  11420   -706   1259  -1166       C\\nATOM   1975  CG2 VAL A1087      24.863 -17.323  28.230  1.00 89.97           C\\nANISOU 1975  CG2 VAL A1087    14954   9465   9765  -1245    754  -1058       C\\nATOM   1976  N   TYR A1088      27.284 -15.876  25.692  1.00 89.69           N\\nANISOU 1976  N   TYR A1088    15242   9934   8902   -793   1168  -1242       N\\nATOM   1977  CA  TYR A1088      27.580 -14.457  25.515  1.00 90.57           C\\nANISOU 1977  CA  TYR A1088    15204  10393   8813   -755   1125   -975       C\\nATOM   1978  C   TYR A1088      26.959 -13.916  24.234  1.00 95.61           C\\nANISOU 1978  C   TYR A1088    16073  11277   8976   -968    892  -1053       C\\nATOM   1979  O   TYR A1088      26.470 -12.781  24.202  1.00 93.98           O\\nANISOU 1979  O   TYR A1088    15753  11275   8682  -1035    611   -805       O\\nATOM   1980  CB  TYR A1088      29.095 -14.250  25.512  1.00 93.94           C\\nANISOU 1980  CB  TYR A1088    15566  10885   9242   -509   1510   -919       C\\nATOM   1981  CG  TYR A1088      29.544 -12.810  25.574  1.00 98.44           C\\nANISOU 1981  CG  TYR A1088    15953  11742   9710   -493   1488   -591       C\\nATOM   1982  CD1 TYR A1088      29.740 -12.178  26.794  1.00 98.86           C\\nANISOU 1982  CD1 TYR A1088    15682  11781  10099   -378   1424   -304       C\\nATOM   1983  CD2 TYR A1088      29.792 -12.088  24.415  1.00103.73           C\\nANISOU 1983  CD2 TYR A1088    16808  12681   9923   -622   1523   -565       C\\nATOM   1984  CE1 TYR A1088      30.162 -10.863  26.860  1.00 99.84           C\\nANISOU 1984  CE1 TYR A1088    15661  12107  10167   -380   1378    -29       C\\nATOM   1985  CE2 TYR A1088      30.213 -10.771  24.470  1.00106.12           C\\nANISOU 1985  CE2 TYR A1088    16981  13181  10158   -650   1482   -232       C\\nATOM   1986  CZ  TYR A1088      30.395 -10.164  25.696  1.00103.83           C\\nANISOU 1986  CZ  TYR A1088    16357  12826  10268   -522   1402     20       C\\nATOM   1987  OH  TYR A1088      30.810  -8.854  25.759  1.00103.35           O\\nANISOU 1987  OH  TYR A1088    16189  12904  10176   -568   1333    326       O\\nATOM   1988  N   ASP A1089      26.969 -14.714  23.164  1.00102.12           N\\nANISOU 1988  N   ASP A1089    17248  12069   9485  -1067    973  -1406       N\\nATOM   1989  CA  ASP A1089      26.320 -14.293  21.927  1.00102.51           C\\nANISOU 1989  CA  ASP A1089    17573  12361   9018  -1301    696  -1486       C\\nATOM   1990  C   ASP A1089      24.810 -14.185  22.110  1.00 97.68           C\\nANISOU 1990  C   ASP A1089    16847  11734   8531  -1503    175  -1453       C\\nATOM   1991  O   ASP A1089      24.193 -13.208  21.669  1.00 94.27           O\\nANISOU 1991  O   ASP A1089    16405  11528   7886  -1603   -198  -1266       O\\nATOM   1992  CB  ASP A1089      26.658 -15.270  20.798  1.00107.75           C\\nANISOU 1992  CB  ASP A1089    18652  12996   9292  -1371    911  -1943       C\\nATOM   1993  CG  ASP A1089      28.153 -15.360  20.522  1.00109.36           C\\nANISOU 1993  CG  ASP A1089    18906  13282   9365  -1158   1468  -2039       C\\nATOM   1994  OD1 ASP A1089      28.859 -14.349  20.724  1.00107.83           O\\nANISOU 1994  OD1 ASP A1089    18522  13306   9142  -1077   1610  -1702       O\\nATOM   1995  OD2 ASP A1089      28.623 -16.442  20.104  1.00108.54           O\\nANISOU 1995  OD2 ASP A1089    19006  13016   9217  -1074   1762  -2478       O\\nATOM   1996  N   SER A1090      24.200 -15.124  22.768  1.00 95.52           N\\nANISOU 1996  N   SER A1090    16469  11190   8635  -1571    131  -1622       N\\nATOM   1997  CA  SER A1090      22.775 -15.087  22.914  1.00100.79           C\\nANISOU 1997  CA  SER A1090    16964  11869   9463  -1805   -311  -1652       C\\nATOM   1998  C   SER A1090      22.220 -13.982  23.739  1.00102.57           C\\nANISOU 1998  C   SER A1090    16755  12269   9949  -1733   -541  -1311       C\\nATOM   1999  O   SER A1090      21.034 -13.763  23.747  1.00106.04           O\\nANISOU 1999  O   SER A1090    16983  12810  10497  -1894   -938  -1340       O\\nATOM   2000  CB  SER A1090      22.377 -16.406  23.588  1.00 99.01           C\\nANISOU 2000  CB  SER A1090    16709  11296   9615  -1937   -227  -1860       C\\nATOM   2001  OG  SER A1090      21.208 -16.357  24.395  1.00 95.53           O\\nANISOU 2001  OG  SER A1090    15874  10901   9522  -2092   -478  -1730       O\\nATOM   2002  N   LEU A1091      23.062 -13.325  24.481  1.00 99.87           N\\nANISOU 2002  N   LEU A1091    16250  11965   9730  -1492   -315  -1031       N\\nATOM   2003  CA  LEU A1091      22.607 -12.416  25.517  1.00 95.87           C\\nANISOU 2003  CA  LEU A1091    15324  11551   9550  -1398   -463   -783       C\\nATOM   2004  C   LEU A1091      22.327 -11.026  24.968  1.00 97.76           C\\nANISOU 2004  C   LEU A1091    15525  12007   9612  -1342   -816   -587       C\\nATOM   2005  O   LEU A1091      23.032 -10.535  24.083  1.00 95.64           O\\nANISOU 2005  O   LEU A1091    15549  11818   8971  -1317   -786   -485       O\\nATOM   2006  CB  LEU A1091      23.641 -12.333  26.638  1.00 87.84           C\\nANISOU 2006  CB  LEU A1091    14159  10436   8780  -1181    -92   -597       C\\nATOM   2007  CG  LEU A1091      23.680 -13.560  27.542  1.00 82.06           C\\nANISOU 2007  CG  LEU A1091    13386   9458   8336  -1224    143   -690       C\\nATOM   2008  CD1 LEU A1091      24.786 -13.425  28.573  1.00 80.82           C\\nANISOU 2008  CD1 LEU A1091    13114   9224   8371   -989    440   -482       C\\nATOM   2009  CD2 LEU A1091      22.327 -13.769  28.206  1.00 80.36           C\\nANISOU 2009  CD2 LEU A1091    12890   9277   8367  -1435    -70   -736       C\\nATOM   2010  N   ASP A1092      21.376 -10.343  25.562  1.00 96.05           N\\nANISOU 2010  N   ASP A1092    14944  11880   9672  -1329  -1151   -538       N\\nATOM   2011  CA  ASP A1092      21.052  -8.988  25.248  1.00 94.58           C\\nANISOU 2011  CA  ASP A1092    14656  11809   9469  -1194  -1512   -321       C\\nATOM   2012  C   ASP A1092      22.222  -8.197  25.771  1.00 90.97           C\\nANISOU 2012  C   ASP A1092    14182  11304   9080   -989  -1249    -61       C\\nATOM   2013  O   ASP A1092      22.961  -8.670  26.567  1.00 94.84           O\\nANISOU 2013  O   ASP A1092    14566  11715   9754   -916   -857    -59       O\\nATOM   2014  CB  ASP A1092      19.780  -8.669  26.007  1.00101.30           C\\nANISOU 2014  CB  ASP A1092    15029  12751  10711  -1166  -1868   -406       C\\nATOM   2015  CG  ASP A1092      19.607  -7.210  26.318  1.00111.33           C\\nANISOU 2015  CG  ASP A1092    16080  14045  12176   -914  -2131   -205       C\\nATOM   2016  OD1 ASP A1092      20.277  -6.361  25.708  1.00117.45           O\\nANISOU 2016  OD1 ASP A1092    17125  14798  12702   -861  -2417     -1       O\\nATOM   2017  OD2 ASP A1092      18.756  -6.904  27.171  1.00112.11           O\\nANISOU 2017  OD2 ASP A1092    15757  14174  12666   -784  -2057   -258       O\\nATOM   2018  N   ALA A1093      22.381  -6.966  25.331  1.00 96.88           N\\nANISOU 2018  N   ALA A1093    15054  12081   9674   -916  -1505    178       N\\nATOM   2019  CA  ALA A1093      23.488  -6.122  25.778  1.00 91.46           C\\nANISOU 2019  CA  ALA A1093    14374  11336   9042   -782  -1292    431       C\\nATOM   2020  C   ALA A1093      23.421  -5.832  27.272  1.00 93.10           C\\nANISOU 2020  C   ALA A1093    14165  11492   9718   -603  -1188    414       C\\nATOM   2021  O   ALA A1093      24.464  -5.712  27.927  1.00 87.73           O\\nANISOU 2021  O   ALA A1093    13451  10765   9118   -524   -866    519       O\\nATOM   2022  CB  ALA A1093      23.503  -4.814  24.988  1.00 88.70           C\\nANISOU 2022  CB  ALA A1093    14227  10970   8505   -779  -1676    717       C\\nATOM   2023  N   VAL A1094      22.214  -5.720  27.829  1.00 97.94           N\\nANISOU 2023  N   VAL A1094    14439  12147  10627   -546  -1450    262       N\\nATOM   2024  CA  VAL A1094      22.076  -5.445  29.257  1.00 93.00           C\\nANISOU 2024  CA  VAL A1094    13427  11531  10378   -399  -1324    200       C\\nATOM   2025  C   VAL A1094      22.441  -6.680  30.072  1.00 88.59           C\\nANISOU 2025  C   VAL A1094    12819  10982   9860   -491   -879     98       C\\nATOM   2026  O   VAL A1094      23.204  -6.601  31.041  1.00 83.02           O\\nANISOU 2026  O   VAL A1094    12036  10247   9261   -400   -616    175       O\\nATOM   2027  CB  VAL A1094      20.652  -4.956  29.576  1.00 91.34           C\\nANISOU 2027  CB  VAL A1094    12822  11413  10469   -310  -1694     21       C\\nATOM   2028  CG1 VAL A1094      20.546  -4.549  31.038  1.00 87.18           C\\nANISOU 2028  CG1 VAL A1094    11914  10940  10271   -155  -1529    -81       C\\nATOM   2029  CG2 VAL A1094      20.261  -3.802  28.656  1.00 92.19           C\\nANISOU 2029  CG2 VAL A1094    13027  11445  10557   -192  -2230    148       C\\nATOM   2030  N   ARG A1095      21.898  -7.840  29.694  1.00 90.63           N\\nANISOU 2030  N   ARG A1095    13144  11253  10038   -685   -833    -66       N\\nATOM   2031  CA  ARG A1095      22.284  -9.087  30.344  1.00 90.96           C\\nANISOU 2031  CA  ARG A1095    13231  11214  10116   -790   -456   -122       C\\nATOM   2032  C   ARG A1095      23.746  -9.427  30.091  1.00 87.34           C\\nANISOU 2032  C   ARG A1095    13078  10619   9487   -715   -154      0       C\\nATOM   2033  O   ARG A1095      24.354 -10.144  30.893  1.00 79.42           O\\nANISOU 2033  O   ARG A1095    12074   9515   8587   -689    132     31       O\\nATOM   2034  CB  ARG A1095      21.389 -10.229  29.864  1.00 87.99           C\\nANISOU 2034  CB  ARG A1095    12907  10817   9709  -1046   -517   -333       C\\nATOM   2035  CG  ARG A1095      19.913  -9.890  29.887  1.00 88.08           C\\nANISOU 2035  CG  ARG A1095    12562  11010   9896  -1139   -853   -486       C\\nATOM   2036  CD  ARG A1095      19.099 -10.979  29.236  1.00 93.06           C\\nANISOU 2036  CD  ARG A1095    13265  11616  10479  -1439   -963   -697       C\\nATOM   2037  NE  ARG A1095      17.793 -10.502  28.791  1.00103.22           N\\nANISOU 2037  NE  ARG A1095    14244  13099  11877  -1501  -1404   -846       N\\nATOM   2038  CZ  ARG A1095      16.679 -10.583  29.511  1.00102.98           C\\nANISOU 2038  CZ  ARG A1095    13724  13246  12157  -1620  -1455   -997       C\\nATOM   2039  NH1 ARG A1095      16.705 -11.126  30.720  1.00101.20           N\\nANISOU 2039  NH1 ARG A1095    13324  13034  12095  -1735  -1072   -988       N\\nATOM   2040  NH2 ARG A1095      15.535 -10.122  29.020  1.00102.93           N\\nANISOU 2040  NH2 ARG A1095    13394  13427  12289  -1634  -1897  -1154       N\\nATOM   2041  N   ARG A1096      24.321  -8.920  29.001  1.00 90.45           N\\nANISOU 2041  N   ARG A1096    13718  11024   9623   -685   -218     78       N\\nATOM   2042  CA  ARG A1096      25.730  -9.168  28.728  1.00 86.04           C\\nANISOU 2042  CA  ARG A1096    13368  10402   8921   -614    110    159       C\\nATOM   2043  C   ARG A1096      26.623  -8.481  29.750  1.00 81.52           C\\nANISOU 2043  C   ARG A1096    12598   9829   8548   -445    250    350       C\\nATOM   2044  O   ARG A1096      27.697  -8.997  30.076  1.00 76.37           O\\nANISOU 2044  O   ARG A1096    11967   9110   7940   -359    548    380       O\\nATOM   2045  CB  ARG A1096      26.072  -8.706  27.313  1.00 85.80           C\\nANISOU 2045  CB  ARG A1096    13637  10453   8510   -686     38    205       C\\nATOM   2046  CG  ARG A1096      26.974  -9.657  26.568  1.00 82.89           C\\nANISOU 2046  CG  ARG A1096    13541  10054   7898   -716    389     63       C\\nATOM   2047  CD  ARG A1096      27.247  -9.180  25.159  1.00 85.44           C\\nANISOU 2047  CD  ARG A1096    14183  10531   7750   -844    350    102       C\\nATOM   2048  NE  ARG A1096      26.098  -9.355  24.282  1.00 94.36           N\\nANISOU 2048  NE  ARG A1096    15514  11710   8629  -1018     -6    -32       N\\nATOM   2049  CZ  ARG A1096      26.167  -9.297  22.957  1.00 97.59           C\\nANISOU 2049  CZ  ARG A1096    16291  12257   8531  -1179    -60    -72       C\\nATOM   2050  NH1 ARG A1096      27.333  -9.075  22.369  1.00 93.17           N\\nANISOU 2050  NH1 ARG A1096    15919  11820   7663  -1201    286      6       N\\nATOM   2051  NH2 ARG A1096      25.078  -9.465  22.222  1.00102.27           N\\nANISOU 2051  NH2 ARG A1096    17053  12899   8906  -1338   -456   -197       N\\nATOM   2052  N   ALA A1097      26.196  -7.325  30.270  1.00 83.15           N\\nANISOU 2052  N   ALA A1097    12599  10095   8899   -381     10    450       N\\nATOM   2053  CA  ALA A1097      26.963  -6.656  31.316  1.00 74.83           C\\nANISOU 2053  CA  ALA A1097    11361   9035   8036   -245    100    585       C\\nATOM   2054  C   ALA A1097      26.946  -7.446  32.617  1.00 73.67           C\\nANISOU 2054  C   ALA A1097    11047   8874   8072   -207    277    525       C\\nATOM   2055  O   ALA A1097      27.942  -7.452  33.348  1.00 74.45           O\\nANISOU 2055  O   ALA A1097    11087   8949   8253   -111    442    628       O\\nATOM   2056  CB  ALA A1097      26.423  -5.246  31.550  1.00 63.51           C\\nANISOU 2056  CB  ALA A1097     9778   7621   6732   -175   -226    643       C\\nATOM   2057  N   ALA A1098      25.832  -8.117  32.923  1.00 71.99           N\\nANISOU 2057  N   ALA A1098    10755   8685   7912   -311    230    379       N\\nATOM   2058  CA  ALA A1098      25.774  -8.940  34.125  1.00 74.69           C\\nANISOU 2058  CA  ALA A1098    11001   9011   8365   -346    407    373       C\\nATOM   2059  C   ALA A1098      26.760 -10.098  34.047  1.00 83.58           C\\nANISOU 2059  C   ALA A1098    12344   9949   9462   -326    646    434       C\\nATOM   2060  O   ALA A1098      27.358 -10.485  35.059  1.00 82.43           O\\nANISOU 2060  O   ALA A1098    12168   9750   9403   -262    768    547       O\\nATOM   2061  CB  ALA A1098      24.351  -9.450  34.338  1.00 76.99           C\\nANISOU 2061  CB  ALA A1098    11160   9381   8710   -537    335    213       C\\nATOM   2062  N   LEU A1099      26.946 -10.665  32.852  1.00 86.05           N\\nANISOU 2062  N   LEU A1099    12886  10156   9651   -363    693    343       N\\nATOM   2063  CA  LEU A1099      27.950 -11.710  32.691  1.00 84.37           C\\nANISOU 2063  CA  LEU A1099    12858   9742   9457   -276    922    336       C\\nATOM   2064  C   LEU A1099      29.360 -11.153  32.838  1.00 75.62           C\\nANISOU 2064  C   LEU A1099    11669   8675   8388    -65   1050    473       C\\nATOM   2065  O   LEU A1099      30.242 -11.829  33.380  1.00 59.72           O\\nANISOU 2065  O   LEU A1099     9651   6525   6517     79   1192    528       O\\nATOM   2066  CB  LEU A1099      27.785 -12.397  31.335  1.00 88.81           C\\nANISOU 2066  CB  LEU A1099    13687  10211   9847   -362    961    126       C\\nATOM   2067  CG  LEU A1099      28.635 -13.647  31.091  1.00 89.13           C\\nANISOU 2067  CG  LEU A1099    13929   9988   9947   -253   1195     11       C\\nATOM   2068  CD1 LEU A1099      28.246 -14.750  32.060  1.00 88.78           C\\nANISOU 2068  CD1 LEU A1099    13929   9678  10126   -318   1188     43       C\\nATOM   2069  CD2 LEU A1099      28.496 -14.118  29.655  1.00 91.08           C\\nANISOU 2069  CD2 LEU A1099    14451  10201   9955   -337   1240   -262       C\\nATOM   2070  N   ILE A1100      29.591  -9.928  32.363  1.00 70.27           N\\nANISOU 2070  N   ILE A1100    10921   8168   7612    -56    974    541       N\\nATOM   2071  CA  ILE A1100      30.888  -9.294  32.557  1.00 70.30           C\\nANISOU 2071  CA  ILE A1100    10796   8234   7680     77   1083    680       C\\nATOM   2072  C   ILE A1100      31.120  -9.006  34.034  1.00 76.98           C\\nANISOU 2072  C   ILE A1100    11428   9092   8729    165   1006    808       C\\nATOM   2073  O   ILE A1100      32.244  -9.120  34.537  1.00 80.54           O\\nANISOU 2073  O   ILE A1100    11764   9529   9310    301   1104    897       O\\nATOM   2074  CB  ILE A1100      30.983  -8.022  31.697  1.00 68.88           C\\nANISOU 2074  CB  ILE A1100    10638   8193   7340    -10    989    761       C\\nATOM   2075  CG1 ILE A1100      30.869  -8.386  30.212  1.00 75.73           C\\nANISOU 2075  CG1 ILE A1100    11771   9090   7912   -120   1082    646       C\\nATOM   2076  CG2 ILE A1100      32.279  -7.281  31.978  1.00 63.94           C\\nANISOU 2076  CG2 ILE A1100     9841   7638   6817     56   1090    917       C\\nATOM   2077  CD1 ILE A1100      30.869  -7.196  29.275  1.00 65.67           C\\nANISOU 2077  CD1 ILE A1100    10607   7938   6405   -260    954    784       C\\nATOM   2078  N   ASN A1101      30.057  -8.645  34.757  1.00 76.26           N\\nANISOU 2078  N   ASN A1101    11262   9055   8656     88    828    795       N\\nATOM   2079  CA  ASN A1101      30.161  -8.449  36.200  1.00 71.74           C\\nANISOU 2079  CA  ASN A1101    10532   8535   8191    138    773    876       C\\nATOM   2080  C   ASN A1101      30.619  -9.725  36.896  1.00 69.64           C\\nANISOU 2080  C   ASN A1101    10339   8134   7987    190    891    949       C\\nATOM   2081  O   ASN A1101      31.439  -9.679  37.821  1.00 64.42           O\\nANISOU 2081  O   ASN A1101     9588   7486   7403    297    869   1078       O\\nATOM   2082  CB  ASN A1101      28.811  -7.981  36.750  1.00 72.99           C\\nANISOU 2082  CB  ASN A1101    10589   8814   8330     34    629    774       C\\nATOM   2083  CG  ASN A1101      28.882  -7.542  38.204  1.00 79.76           C\\nANISOU 2083  CG  ASN A1101    11293   9793   9219     68    586    807       C\\nATOM   2084  OD1 ASN A1101      29.385  -8.264  39.065  1.00 88.11           O\\nANISOU 2084  OD1 ASN A1101    12391  10824  10262     80    664    919       O\\nATOM   2085  ND2 ASN A1101      28.363  -6.353  38.484  1.00 77.04           N\\nANISOU 2085  ND2 ASN A1101    10794   9569   8909     92    434    696       N\\nATOM   2086  N   MET A1102      30.111 -10.877  36.452  1.00 67.47           N\\nANISOU 2086  N   MET A1102    10246   7696   7691    110    973    875       N\\nATOM   2087  CA  MET A1102      30.457 -12.137  37.100  1.00 68.00           C\\nANISOU 2087  CA  MET A1102    10442   7546   7851    150   1035    971       C\\nATOM   2088  C   MET A1102      31.900 -12.539  36.815  1.00 75.21           C\\nANISOU 2088  C   MET A1102    11354   8314   8910    407   1126   1011       C\\nATOM   2089  O   MET A1102      32.611 -12.984  37.723  1.00 77.63           O\\nANISOU 2089  O   MET A1102    11635   8519   9341    543   1075   1172       O\\nATOM   2090  CB  MET A1102      29.492 -13.233  36.655  1.00 70.40           C\\nANISOU 2090  CB  MET A1102    10958   7659   8132    -38   1075    861       C\\nATOM   2091  CG  MET A1102      28.072 -13.024  37.150  1.00 76.57           C\\nANISOU 2091  CG  MET A1102    11663   8605   8824   -310   1005    826       C\\nATOM   2092  SD  MET A1102      27.010 -14.445  36.822  1.00 81.97           S\\nANISOU 2092  SD  MET A1102    12572   9042   9532   -608   1039    733       S\\nATOM   2093  CE  MET A1102      27.916 -15.743  37.652  1.00 80.68           C\\nANISOU 2093  CE  MET A1102    12664   8490   9502   -523   1086    972       C\\nATOM   2094  N   VAL A1103      32.352 -12.395  35.565  1.00 79.58           N\\nANISOU 2094  N   VAL A1103    11918   8879   9439    475   1257    861       N\\nATOM   2095  CA  VAL A1103      33.743 -12.721  35.251  1.00 82.54           C\\nANISOU 2095  CA  VAL A1103    12205   9184   9974    728   1400    840       C\\nATOM   2096  C   VAL A1103      34.689 -11.726  35.912  1.00 80.24           C\\nANISOU 2096  C   VAL A1103    11618   9095   9774    826   1331   1000       C\\nATOM   2097  O   VAL A1103      35.848 -12.053  36.198  1.00 82.23           O\\nANISOU 2097  O   VAL A1103    11705   9299  10238   1051   1366   1045       O\\nATOM   2098  CB  VAL A1103      33.969 -12.782  33.727  1.00 84.75           C\\nANISOU 2098  CB  VAL A1103    12570   9500  10133    729   1619    609       C\\nATOM   2099  CG1 VAL A1103      32.942 -13.689  33.066  1.00 85.19           C\\nANISOU 2099  CG1 VAL A1103    12933   9364  10070    590   1631    415       C\\nATOM   2100  CG2 VAL A1103      33.931 -11.394  33.115  1.00 83.71           C\\nANISOU 2100  CG2 VAL A1103    12339   9665   9801    582   1615    646       C\\nATOM   2101  N   PHE A1104      34.222 -10.502  36.163  1.00 72.46           N\\nANISOU 2101  N   PHE A1104    10543   8321   8669    670   1206   1064       N\\nATOM   2102  CA  PHE A1104      35.025  -9.556  36.927  1.00 74.27           C\\nANISOU 2102  CA  PHE A1104    10521   8703   8994    721   1090   1196       C\\nATOM   2103  C   PHE A1104      35.203 -10.013  38.369  1.00 79.15           C\\nANISOU 2103  C   PHE A1104    11108   9268   9696    808    920   1340       C\\nATOM   2104  O   PHE A1104      36.258  -9.779  38.969  1.00 81.90           O\\nANISOU 2104  O   PHE A1104    11250   9676  10191    937    827   1439       O\\nATOM   2105  CB  PHE A1104      34.382  -8.171  36.883  1.00 67.54           C\\nANISOU 2105  CB  PHE A1104     9633   8010   8019    545    959   1195       C\\nATOM   2106  CG  PHE A1104      35.032  -7.234  35.911  1.00 71.68           C\\nANISOU 2106  CG  PHE A1104    10068   8632   8534    483   1036   1205       C\\nATOM   2107  CD1 PHE A1104      34.785  -7.340  34.554  1.00 74.18           C\\nANISOU 2107  CD1 PHE A1104    10546   8950   8690    396   1191   1126       C\\nATOM   2108  CD2 PHE A1104      35.892  -6.243  36.356  1.00 80.86           C\\nANISOU 2108  CD2 PHE A1104    11011   9893   9821    465    944   1303       C\\nATOM   2109  CE1 PHE A1104      35.384  -6.477  33.659  1.00 78.16           C\\nANISOU 2109  CE1 PHE A1104    11011   9565   9121    278   1280   1183       C\\nATOM   2110  CE2 PHE A1104      36.492  -5.376  35.467  1.00 85.63           C\\nANISOU 2110  CE2 PHE A1104    11550  10576  10412    335   1028   1354       C\\nATOM   2111  CZ  PHE A1104      36.238  -5.493  34.115  1.00 81.25           C\\nANISOU 2111  CZ  PHE A1104    11176  10035   9661    234   1209   1314       C\\nATOM   2112  N   GLN A1105      34.192 -10.669  38.935  1.00 80.45           N\\nANISOU 2112  N   GLN A1105    11475   9341   9754    708    866   1365       N\\nATOM   2113  CA  GLN A1105      34.237 -11.118  40.319  1.00 76.17           C\\nANISOU 2113  CA  GLN A1105    10978   8769   9193    723    706   1544       C\\nATOM   2114  C   GLN A1105      34.839 -12.508  40.465  1.00 79.87           C\\nANISOU 2114  C   GLN A1105    11579   8938   9829    899    695   1660       C\\nATOM   2115  O   GLN A1105      35.670 -12.731  41.352  1.00 77.78           O\\nANISOU 2115  O   GLN A1105    11252   8640   9660   1051    517   1841       O\\nATOM   2116  CB  GLN A1105      32.830 -11.107  40.918  1.00 71.88           C\\nANISOU 2116  CB  GLN A1105    10574   8313   8426    472    687   1531       C\\nATOM   2117  CG  GLN A1105      32.752 -11.692  42.313  1.00 71.95           C\\nANISOU 2117  CG  GLN A1105    10707   8315   8315    408    569   1741       C\\nATOM   2118  CD  GLN A1105      31.379 -11.534  42.928  1.00 72.70           C\\nANISOU 2118  CD  GLN A1105    10864   8598   8159    121    622   1689       C\\nATOM   2119  OE1 GLN A1105      30.414 -11.193  42.241  1.00 76.06           O\\nANISOU 2119  OE1 GLN A1105    11232   9099   8567     -1    727   1488       O\\nATOM   2120  NE2 GLN A1105      31.282 -11.777  44.230  1.00 68.30           N\\nANISOU 2120  NE2 GLN A1105    10410   8146   7396      7    545   1865       N\\nATOM   2121  N   MET A1106      34.433 -13.446  39.607  1.00 80.28           N\\nANISOU 2121  N   MET A1106    11826   8743   9934    892    842   1548       N\\nATOM   2122  CA  MET A1106      34.803 -14.847  39.734  1.00 82.95           C\\nANISOU 2122  CA  MET A1106    12358   8697  10463   1051    807   1630       C\\nATOM   2123  C   MET A1106      35.843 -15.311  38.725  1.00 89.43           C\\nANISOU 2123  C   MET A1106    13075   9350  11554   1362    949   1444       C\\nATOM   2124  O   MET A1106      36.305 -16.452  38.830  1.00 92.75           O\\nANISOU 2124  O   MET A1106    13623   9404  12215   1580    890   1476       O\\nATOM   2125  CB  MET A1106      33.551 -15.727  39.604  1.00 79.57           C\\nANISOU 2125  CB  MET A1106    12259   8043   9930    793    855   1607       C\\nATOM   2126  CG  MET A1106      32.706 -15.755  40.856  1.00 84.73           C\\nANISOU 2126  CG  MET A1106    13038   8785  10370    512    733   1843       C\\nATOM   2127  SD  MET A1106      30.984 -16.135  40.503  1.00 86.03           S\\nANISOU 2127  SD  MET A1106    13388   8937  10364     82    862   1721       S\\nATOM   2128  CE  MET A1106      30.421 -14.540  39.929  1.00 88.27           C\\nANISOU 2128  CE  MET A1106    13356   9694  10490     13    937   1471       C\\nATOM   2129  N   GLY A1107      36.219 -14.477  37.763  1.00 83.47           N\\nANISOU 2129  N   GLY A1107    12104   8844  10768   1383   1136   1249       N\\nATOM   2130  CA  GLY A1107      37.045 -14.923  36.668  1.00 86.98           C\\nANISOU 2130  CA  GLY A1107    12460   9202  11389   1617   1365   1006       C\\nATOM   2131  C   GLY A1107      36.292 -15.824  35.707  1.00 88.79           C\\nANISOU 2131  C   GLY A1107    13014   9179  11544   1543   1521    764       C\\nATOM   2132  O   GLY A1107      35.264 -16.426  36.027  1.00 86.13           O\\nANISOU 2132  O   GLY A1107    12973   8625  11128   1354   1409    824       O\\nATOM   2133  N   GLU A1108      36.843 -15.917  34.497  1.00 89.49           N\\nANISOU 2133  N   GLU A1108    13038   9319  11644   1667   1796    468       N\\nATOM   2134  CA  GLU A1108      36.262 -16.761  33.464  1.00 87.52           C\\nANISOU 2134  CA  GLU A1108    13103   8850  11300   1613   1951    163       C\\nATOM   2135  C   GLU A1108      36.230 -18.231  33.861  1.00 85.64           C\\nANISOU 2135  C   GLU A1108    13113   8070  11356   1798   1837    124       C\\nATOM   2136  O   GLU A1108      35.365 -18.973  33.377  1.00 84.49           O\\nANISOU 2136  O   GLU A1108    13313   7661  11130   1634   1842    -46       O\\nATOM   2137  CB  GLU A1108      37.029 -16.590  32.160  1.00 95.88           C\\nANISOU 2137  CB  GLU A1108    14037  10114  12279   1733   2303   -169       C\\nATOM   2138  CG  GLU A1108      36.931 -15.181  31.598  1.00102.62           C\\nANISOU 2138  CG  GLU A1108    14756  11443  12792   1470   2402   -100       C\\nATOM   2139  CD  GLU A1108      37.375 -15.104  30.157  1.00109.37           C\\nANISOU 2139  CD  GLU A1108    15629  12514  13413   1456   2771   -421       C\\nATOM   2140  OE1 GLU A1108      37.716 -16.168  29.591  1.00113.53           O\\nANISOU 2140  OE1 GLU A1108    16260  12832  14044   1672   2970   -764       O\\nATOM   2141  OE2 GLU A1108      37.380 -13.985  29.593  1.00105.41           O\\nANISOU 2141  OE2 GLU A1108    15063  12377  12612   1221   2859   -335       O\\nATOM   2142  N   THR A1109      37.155 -18.669  34.719  1.00 90.70           N\\nANISOU 2142  N   THR A1109    13597   8510  12353   2124   1695    286       N\\nATOM   2143  CA  THR A1109      37.120 -20.042  35.207  1.00 95.84           C\\nANISOU 2143  CA  THR A1109    14532   8571  13311   2298   1506    331       C\\nATOM   2144  C   THR A1109      35.855 -20.297  36.012  1.00 92.70           C\\nANISOU 2144  C   THR A1109    14477   8003  12741   1906   1273    629       C\\nATOM   2145  O   THR A1109      35.133 -21.269  35.766  1.00 95.09           O\\nANISOU 2145  O   THR A1109    15151   7895  13084   1765   1241    533       O\\nATOM   2146  CB  THR A1109      38.349 -20.335  36.066  1.00 97.86           C\\nANISOU 2146  CB  THR A1109    14535   8674  13974   2728   1309    517       C\\nATOM   2147  OG1 THR A1109      39.538 -19.920  35.381  1.00102.45           O\\nANISOU 2147  OG1 THR A1109    14672   9535  14718   3048   1561    242       O\\nATOM   2148  CG2 THR A1109      38.427 -21.828  36.376  1.00 97.85           C\\nANISOU 2148  CG2 THR A1109    14861   7969  14349   2976   1099    531       C\\nATOM   2149  N   GLY A1110      35.567 -19.420  36.975  1.00 95.75           N\\nANISOU 2149  N   GLY A1110    14731   8720  12931   1701   1128    965       N\\nATOM   2150  CA  GLY A1110      34.456 -19.660  37.880  1.00 94.88           C\\nANISOU 2150  CA  GLY A1110    14887   8513  12649   1331    949   1253       C\\nATOM   2151  C   GLY A1110      33.103 -19.552  37.204  1.00 88.67           C\\nANISOU 2151  C   GLY A1110    14261   7826  11602    922   1075   1072       C\\nATOM   2152  O   GLY A1110      32.191 -20.329  37.497  1.00 82.42           O\\nANISOU 2152  O   GLY A1110    13765   6760  10793    635    997   1160       O\\nATOM   2153  N   VAL A1111      32.952 -18.588  36.296  1.00 85.36           N\\nANISOU 2153  N   VAL A1111    13649   7799  10986    866   1244    836       N\\nATOM   2154  CA  VAL A1111      31.676 -18.422  35.606  1.00 83.59           C\\nANISOU 2154  CA  VAL A1111    13541   7694  10525    508   1297    660       C\\nATOM   2155  C   VAL A1111      31.371 -19.646  34.751  1.00 86.94           C\\nANISOU 2155  C   VAL A1111    14292   7686  11055    469   1346    385       C\\nATOM   2156  O   VAL A1111      30.217 -20.080  34.649  1.00 84.62           O\\nANISOU 2156  O   VAL A1111    14188   7281  10681    116   1284    338       O\\nATOM   2157  CB  VAL A1111      31.689 -17.125  34.776  1.00 78.72           C\\nANISOU 2157  CB  VAL A1111    12692   7539   9679    492   1403    508       C\\nATOM   2158  CG1 VAL A1111      30.403 -16.979  33.994  1.00 82.94           C\\nANISOU 2158  CG1 VAL A1111    13340   8183   9992    166   1385    324       C\\nATOM   2159  CG2 VAL A1111      31.894 -15.925  35.684  1.00 68.67           C\\nANISOU 2159  CG2 VAL A1111    11133   6621   8339    498   1317    755       C\\nATOM   2160  N   ALA A1112      32.402 -20.242  34.147  1.00 83.83           N\\nANISOU 2160  N   ALA A1112    13946   7039  10867    828   1457    166       N\\nATOM   2161  CA  ALA A1112      32.208 -21.434  33.331  1.00 86.95           C\\nANISOU 2161  CA  ALA A1112    14676   6976  11386    838   1502   -166       C\\nATOM   2162  C   ALA A1112      31.727 -22.636  34.137  1.00 97.68           C\\nANISOU 2162  C   ALA A1112    16361   7762  12989    696   1293     31       C\\nATOM   2163  O   ALA A1112      31.408 -23.672  33.541  1.00107.07           O\\nANISOU 2163  O   ALA A1112    17878   8495  14308    634   1283   -236       O\\nATOM   2164  CB  ALA A1112      33.504 -21.784  32.597  1.00 82.87           C\\nANISOU 2164  CB  ALA A1112    14088   6331  11068   1312   1699   -487       C\\nATOM   2165  N   GLY A1113      31.670 -22.528  35.467  1.00 94.08           N\\nANISOU 2165  N   GLY A1113    15859   7311  12576    613   1121    490       N\\nATOM   2166  CA  GLY A1113      31.127 -23.580  36.301  1.00 91.96           C\\nANISOU 2166  CA  GLY A1113    15934   6547  12461    374    924    767       C\\nATOM   2167  C   GLY A1113      29.632 -23.536  36.499  1.00 88.01           C\\nANISOU 2167  C   GLY A1113    15526   6189  11726   -228    907    854       C\\nATOM   2168  O   GLY A1113      29.067 -24.463  37.088  1.00 90.55           O\\nANISOU 2168  O   GLY A1113    16155   6098  12153   -532    780   1074       O\\nATOM   2169  N   PHE A1114      28.975 -22.477  36.030  1.00 89.32           N\\nANISOU 2169  N   PHE A1114    15419   6923  11597   -417   1020    697       N\\nATOM   2170  CA  PHE A1114      27.518 -22.347  36.101  1.00 93.06           C\\nANISOU 2170  CA  PHE A1114    15868   7604  11887   -955   1007    701       C\\nATOM   2171  C   PHE A1114      26.844 -22.935  34.867  1.00 97.68           C\\nANISOU 2171  C   PHE A1114    16640   7982  12490  -1154   1008    293       C\\nATOM   2172  O   PHE A1114      25.996 -22.294  34.250  1.00100.46           O\\nANISOU 2172  O   PHE A1114    16812   8720  12638  -1379   1016     94       O\\nATOM   2173  CB  PHE A1114      27.127 -20.883  36.266  1.00 94.49           C\\nANISOU 2173  CB  PHE A1114    15638   8468  11794  -1010   1062    728       C\\nATOM   2174  CG  PHE A1114      27.602 -20.258  37.542  1.00 95.33           C\\nANISOU 2174  CG  PHE A1114    15570   8818  11834   -900   1044   1086       C\\nATOM   2175  CD1 PHE A1114      26.863 -20.382  38.706  1.00 96.26           C\\nANISOU 2175  CD1 PHE A1114    15694   9032  11847  -1255   1023   1375       C\\nATOM   2176  CD2 PHE A1114      28.773 -19.521  37.572  1.00 93.76           C\\nANISOU 2176  CD2 PHE A1114    15190   8788  11647   -478   1057   1113       C\\nATOM   2177  CE1 PHE A1114      27.293 -19.799  39.881  1.00 93.49           C\\nANISOU 2177  CE1 PHE A1114    15219   8937  11366  -1170    999   1669       C\\nATOM   2178  CE2 PHE A1114      29.209 -18.933  38.743  1.00 90.99           C\\nANISOU 2178  CE2 PHE A1114    14688   8664  11219   -396    999   1410       C\\nATOM   2179  CZ  PHE A1114      28.468 -19.072  39.900  1.00 89.90           C\\nANISOU 2179  CZ  PHE A1114    14603   8619  10937   -731    961   1678       C\\nATOM   2180  N   THR A1115      27.213 -24.163  34.496  1.00 93.63           N\\nANISOU 2180  N   THR A1115    16502   6840  12234  -1062    963    146       N\\nATOM   2181  CA  THR A1115      26.755 -24.715  33.225  1.00 97.80           C\\nANISOU 2181  CA  THR A1115    17241   7160  12760  -1192    960   -325       C\\nATOM   2182  C   THR A1115      25.237 -24.821  33.175  1.00101.53           C\\nANISOU 2182  C   THR A1115    17699   7752  13126  -1809    862   -353       C\\nATOM   2183  O   THR A1115      24.618 -24.467  32.164  1.00100.69           O\\nANISOU 2183  O   THR A1115    17515   7914  12829  -1958    838   -694       O\\nATOM   2184  CB  THR A1115      27.395 -26.081  32.984  1.00104.56           C\\nANISOU 2184  CB  THR A1115    18523   7240  13966   -980    909   -494       C\\nATOM   2185  OG1 THR A1115      26.936 -27.010  33.974  1.00111.74           O\\nANISOU 2185  OG1 THR A1115    19700   7650  15106  -1304    745   -134       O\\nATOM   2186  CG2 THR A1115      28.912 -25.975  33.059  1.00103.25           C\\nANISOU 2186  CG2 THR A1115    18273   6991  13964   -334   1002   -493       C\\nATOM   2187  N   ASN A1116      24.617 -25.292  34.259  1.00109.01           N\\nANISOU 2187  N   ASN A1116    18703   8536  14180  -2193    797     12       N\\nATOM   2188  CA  ASN A1116      23.168 -25.450  34.256  1.00114.25           C\\nANISOU 2188  CA  ASN A1116    19286   9335  14790  -2821    734    -24       C\\nATOM   2189  C   ASN A1116      22.464 -24.103  34.180  1.00108.33           C\\nANISOU 2189  C   ASN A1116    18027   9368  13766  -2910    776    -69       C\\nATOM   2190  O   ASN A1116      21.401 -23.993  33.560  1.00112.39           O\\nANISOU 2190  O   ASN A1116    18389  10096  14219  -3257    688   -317       O\\nATOM   2191  CB  ASN A1116      22.716 -26.227  35.496  1.00119.12           C\\nANISOU 2191  CB  ASN A1116    20066   9646  15546  -3254    712    417       C\\nATOM   2192  N   SER A1117      23.040 -23.071  34.794  1.00107.10           N\\nANISOU 2192  N   SER A1117    17599   9621  13474  -2592    871    149       N\\nATOM   2193  CA  SER A1117      22.434 -21.748  34.719  1.00102.31           C\\nANISOU 2193  CA  SER A1117    16531   9686  12658  -2613    880     85       C\\nATOM   2194  C   SER A1117      22.674 -21.101  33.361  1.00102.29           C\\nANISOU 2194  C   SER A1117    16484   9870  12513  -2343    814   -265       C\\nATOM   2195  O   SER A1117      21.756 -20.507  32.785  1.00100.23           O\\nANISOU 2195  O   SER A1117    15984   9960  12139  -2521    696   -453       O\\nATOM   2196  CB  SER A1117      22.981 -20.857  35.835  1.00 98.47           C\\nANISOU 2196  CB  SER A1117    15811   9527  12076  -2381    982    404       C\\nATOM   2197  OG  SER A1117      22.892 -21.504  37.092  1.00 97.73           O\\nANISOU 2197  OG  SER A1117    15842   9258  12035  -2624   1039    761       O\\nATOM   2198  N   LEU A1118      23.897 -21.215  32.836  1.00104.26           N\\nANISOU 2198  N   LEU A1118    16951   9904  12761  -1923    883   -351       N\\nATOM   2199  CA  LEU A1118      24.243 -20.548  31.585  1.00100.23           C\\nANISOU 2199  CA  LEU A1118    16425   9622  12038  -1690    875   -637       C\\nATOM   2200  C   LEU A1118      23.389 -21.046  30.427  1.00107.73           C\\nANISOU 2200  C   LEU A1118    17547  10492  12892  -1976    724  -1011       C\\nATOM   2201  O   LEU A1118      23.041 -20.274  29.525  1.00110.02           O\\nANISOU 2201  O   LEU A1118    17736  11135  12931  -1982    613  -1185       O\\nATOM   2202  CB  LEU A1118      25.722 -20.757  31.279  1.00 92.05           C\\nANISOU 2202  CB  LEU A1118    15569   8366  11040  -1233   1041   -692       C\\nATOM   2203  CG  LEU A1118      26.695 -19.998  32.171  1.00 86.98           C\\nANISOU 2203  CG  LEU A1118    14695   7910  10443   -907   1144   -375       C\\nATOM   2204  CD1 LEU A1118      28.100 -20.549  32.003  1.00 86.56           C\\nANISOU 2204  CD1 LEU A1118    14792   7548  10551   -488   1291   -444       C\\nATOM   2205  CD2 LEU A1118      26.654 -18.516  31.846  1.00 86.67           C\\nANISOU 2205  CD2 LEU A1118    14359   8413  10159   -835   1133   -349       C\\nATOM   2206  N   ARG A1119      23.046 -22.333  30.429  1.00104.44           N\\nANISOU 2206  N   ARG A1119    17422   9590  12668  -2232    680  -1129       N\\nATOM   2207  CA  ARG A1119      22.191 -22.858  29.372  1.00103.70           C\\nANISOU 2207  CA  ARG A1119    17500   9406  12496  -2554    498  -1514       C\\nATOM   2208  C   ARG A1119      20.795 -22.250  29.433  1.00102.63           C\\nANISOU 2208  C   ARG A1119    16991   9707  12297  -2952    292  -1490       C\\nATOM   2209  O   ARG A1119      20.133 -22.113  28.398  1.00102.11           O\\nANISOU 2209  O   ARG A1119    16930   9811  12055  -3119     75  -1792       O\\nATOM   2210  CB  ARG A1119      22.123 -24.383  29.466  1.00105.66           C\\nANISOU 2210  CB  ARG A1119    18150   8971  13026  -2774    474  -1635       C\\nATOM   2211  CG  ARG A1119      21.461 -25.066  28.282  1.00110.68           C\\nANISOU 2211  CG  ARG A1119    19053   9414  13586  -3068    283  -2116       C\\nATOM   2212  CD  ARG A1119      21.400 -26.576  28.478  1.00119.37           C\\nANISOU 2212  CD  ARG A1119    20574   9750  15030  -3303    239  -2220       C\\nATOM   2213  NE  ARG A1119      20.881 -26.936  29.795  1.00121.59           N\\nANISOU 2213  NE  ARG A1119    20741   9865  15590  -3652    240  -1772       N\\nATOM   2214  CZ  ARG A1119      21.609 -27.484  30.763  1.00120.23           C\\nANISOU 2214  CZ  ARG A1119    20757   9256  15669  -3483    350  -1432       C\\nATOM   2215  NH1 ARG A1119      22.893 -27.748  30.561  1.00119.50           N\\nANISOU 2215  NH1 ARG A1119    20917   8831  15658  -2927    455  -1524       N\\nATOM   2216  NH2 ARG A1119      21.053 -27.772  31.933  1.00120.62           N\\nANISOU 2216  NH2 ARG A1119    20732   9219  15878  -3878    351  -1000       N\\nATOM   2217  N   MET A1120      20.338 -21.863  30.627  1.00100.48           N\\nANISOU 2217  N   MET A1120    16375   9649  12155  -3093    347  -1158       N\\nATOM   2218  CA  MET A1120      19.012 -21.263  30.756  1.00103.10           C\\nANISOU 2218  CA  MET A1120    16260  10430  12486  -3427    184  -1176       C\\nATOM   2219  C   MET A1120      19.000 -19.818  30.272  1.00100.31           C\\nANISOU 2219  C   MET A1120    15604  10594  11915  -3129     66  -1209       C\\nATOM   2220  O   MET A1120      18.009 -19.365  29.686  1.00100.24           O\\nANISOU 2220  O   MET A1120    15342  10888  11857  -3303   -198  -1388       O\\nATOM   2221  CB  MET A1120      18.535 -21.349  32.203  1.00106.18           C\\nANISOU 2221  CB  MET A1120    16380  10910  13054  -3686    341   -856       C\\nATOM   2222  CG  MET A1120      18.420 -22.776  32.714  1.00117.71           C\\nANISOU 2222  CG  MET A1120    18166  11832  14725  -4073    415   -750       C\\nATOM   2223  SD  MET A1120      17.789 -22.885  34.401  1.00123.98           S\\nANISOU 2223  SD  MET A1120    18683  12804  15620  -4485    629   -335       S\\nATOM   2224  CE  MET A1120      17.761 -24.663  34.625  1.00131.09           C\\nANISOU 2224  CE  MET A1120    20134  12916  16760  -4951    624   -214       C\\nATOM   2225  N   LEU A1121      20.082 -19.075  30.519  1.00100.35           N\\nANISOU 2225  N   LEU A1121    15626  10687  11815  -2692    222  -1026       N\\nATOM   2226  CA  LEU A1121      20.236 -17.769  29.884  1.00100.41           C\\nANISOU 2226  CA  LEU A1121    15473  11071  11608  -2415     91  -1049       C\\nATOM   2227  C   LEU A1121      20.299 -17.911  28.369  1.00105.95           C\\nANISOU 2227  C   LEU A1121    16480  11732  12045  -2411    -85  -1340       C\\nATOM   2228  O   LEU A1121      19.794 -17.057  27.629  1.00108.90           O\\nANISOU 2228  O   LEU A1121    16728  12416  12235  -2399   -355  -1411       O\\nATOM   2229  CB  LEU A1121      21.498 -17.077  30.396  1.00 89.96           C\\nANISOU 2229  CB  LEU A1121    14156   9787  10238  -2005    306   -807       C\\nATOM   2230  CG  LEU A1121      21.578 -16.711  31.874  1.00 82.79           C\\nANISOU 2230  CG  LEU A1121    12972   8988   9494  -1956    454   -522       C\\nATOM   2231  CD1 LEU A1121      22.975 -16.220  32.204  1.00 72.92           C\\nANISOU 2231  CD1 LEU A1121    11799   7708   8200  -1566    625   -331       C\\nATOM   2232  CD2 LEU A1121      20.549 -15.649  32.207  1.00 85.66           C\\nANISOU 2232  CD2 LEU A1121    12882   9776   9890  -2027    296   -524       C\\nATOM   2233  N   GLN A1122      20.920 -18.991  27.892  1.00 98.13           N\\nANISOU 2233  N   GLN A1122    15913  10351  11023  -2411     46  -1520       N\\nATOM   2234  CA  GLN A1122      21.020 -19.232  26.459  1.00 98.26           C\\nANISOU 2234  CA  GLN A1122    16271  10336  10727  -2427    -75  -1857       C\\nATOM   2235  C   GLN A1122      19.667 -19.584  25.852  1.00 96.39           C\\nANISOU 2235  C   GLN A1122    15998  10161  10466  -2846   -440  -2111       C\\nATOM   2236  O   GLN A1122      19.425 -19.301  24.674  1.00 98.68           O\\nANISOU 2236  O   GLN A1122    16445  10634  10417  -2889   -682  -2330       O\\nATOM   2237  CB  GLN A1122      22.036 -20.346  26.201  1.00103.05           C\\nANISOU 2237  CB  GLN A1122    17309  10483  11362  -2283    189  -2053       C\\nATOM   2238  CG  GLN A1122      22.347 -20.616  24.747  1.00107.55           C\\nANISOU 2238  CG  GLN A1122    18269  11042  11552  -2252    165  -2458       C\\nATOM   2239  CD  GLN A1122      23.447 -21.645  24.581  1.00111.75           C\\nANISOU 2239  CD  GLN A1122    19160  11128  12172  -2017    475  -2696       C\\nATOM   2240  OE1 GLN A1122      24.039 -22.100  25.559  1.00115.12           O\\nANISOU 2240  OE1 GLN A1122    19540  11237  12962  -1840    666  -2506       O\\nATOM   2241  NE2 GLN A1122      23.726 -22.017  23.338  1.00113.25           N\\nANISOU 2241  NE2 GLN A1122    19714  11294  12023  -1998    511  -3131       N\\nATOM   2242  N   GLN A1123      18.773 -20.184  26.639  1.00102.08           N\\nANISOU 2242  N   GLN A1123    16506  10761  11521  -3189   -495  -2073       N\\nATOM   2243  CA  GLN A1123      17.459 -20.603  26.168  1.00103.74           C\\nANISOU 2243  CA  GLN A1123    16604  11025  11786  -3643   -839  -2321       C\\nATOM   2244  C   GLN A1123      16.362 -19.590  26.496  1.00108.72           C\\nANISOU 2244  C   GLN A1123    16638  12153  12517  -3742  -1093  -2203       C\\nATOM   2245  O   GLN A1123      15.179 -19.947  26.486  1.00110.87           O\\nANISOU 2245  O   GLN A1123    16643  12510  12973  -4152  -1332  -2352       O\\nATOM   2246  CB  GLN A1123      17.101 -21.971  26.754  1.00101.84           C\\nANISOU 2246  CB  GLN A1123    16492  10326  11878  -4039   -744  -2378       C\\nATOM   2247  CG  GLN A1123      17.964 -23.119  26.251  1.00 99.00           C\\nANISOU 2247  CG  GLN A1123    16739   9389  11487  -3971   -604  -2613       C\\nATOM   2248  CD  GLN A1123      17.609 -24.442  26.905  1.00109.60           C\\nANISOU 2248  CD  GLN A1123    18244  10191  13208  -4372   -553  -2607       C\\nATOM   2249  OE1 GLN A1123      17.694 -24.589  28.124  1.00109.83           O\\nANISOU 2249  OE1 GLN A1123    18131  10108  13491  -4423   -352  -2243       O\\nATOM   2250  NE2 GLN A1123      17.200 -25.410  26.095  1.00111.61           N\\nANISOU 2250  NE2 GLN A1123    18833  10095  13478  -4692   -754  -3005       N\\nATOM   2251  N   LYS A1124      16.728 -18.344  26.794  1.00101.10           N\\nANISOU 2251  N   LYS A1124    15436  11503  11475  -3376  -1053  -1965       N\\nATOM   2252  CA  LYS A1124      15.801 -17.264  27.128  1.00102.00           C\\nANISOU 2252  CA  LYS A1124    14979  12055  11722  -3354  -1290  -1880       C\\nATOM   2253  C   LYS A1124      14.956 -17.560  28.362  1.00106.14           C\\nANISOU 2253  C   LYS A1124    15026  12671  12629  -3642  -1145  -1813       C\\nATOM   2254  O   LYS A1124      13.969 -16.858  28.613  1.00108.27           O\\nANISOU 2254  O   LYS A1124    14746  13316  13075  -3688  -1344  -1851       O\\nATOM   2255  CB  LYS A1124      14.875 -16.927  25.950  1.00104.85           C\\nANISOU 2255  CB  LYS A1124    15253  12649  11937  -3482  -1823  -2115       C\\nATOM   2256  CG  LYS A1124      15.585 -16.569  24.655  1.00106.34           C\\nANISOU 2256  CG  LYS A1124    15931  12827  11648  -3267  -1994  -2170       C\\nATOM   2257  CD  LYS A1124      16.318 -15.246  24.762  1.00102.53           C\\nANISOU 2257  CD  LYS A1124    15411  12521  11026  -2834  -1939  -1876       C\\nATOM   2258  CE  LYS A1124      16.710 -14.725  23.392  1.00104.63           C\\nANISOU 2258  CE  LYS A1124    16088  12882  10786  -2721  -2205  -1897       C\\nATOM   2259  NZ  LYS A1124      15.510 -14.429  22.560  1.00109.17           N\\nANISOU 2259  NZ  LYS A1124    16517  13684  11279  -2897  -2828  -2043       N\\nATOM   2260  N   ARG A1125      15.311 -18.583  29.142  1.00109.81           N\\nANISOU 2260  N   ARG A1125    15685  12809  13228  -3839   -806  -1713       N\\nATOM   2261  CA  ARG A1125      14.563 -18.937  30.349  1.00105.46           C\\nANISOU 2261  CA  ARG A1125    14749  12354  12966  -4188   -611  -1603       C\\nATOM   2262  C   ARG A1125      15.011 -18.038  31.502  1.00105.15           C\\nANISOU 2262  C   ARG A1125    14454  12555  12943  -3878   -338  -1327       C\\nATOM   2263  O   ARG A1125      15.645 -18.469  32.467  1.00102.11           O\\nANISOU 2263  O   ARG A1125    14245  11977  12576  -3884    -12  -1083       O\\nATOM   2264  CB  ARG A1125      14.757 -20.408  30.687  1.00100.56           C\\nANISOU 2264  CB  ARG A1125    14519  11232  12456  -4562   -413  -1558       C\\nATOM   2265  CG  ARG A1125      14.118 -21.370  29.702  1.00104.76           C\\nANISOU 2265  CG  ARG A1125    15255  11516  13034  -4972   -689  -1879       C\\nATOM   2266  CD  ARG A1125      14.117 -22.790  30.251  1.00109.68           C\\nANISOU 2266  CD  ARG A1125    16197  11614  13861  -5418   -505  -1800       C\\nATOM   2267  NE  ARG A1125      15.435 -23.419  30.187  1.00111.71           N\\nANISOU 2267  NE  ARG A1125    17086  11317  14042  -5114   -333  -1714       N\\nATOM   2268  CZ  ARG A1125      15.756 -24.551  30.807  1.00114.79           C\\nANISOU 2268  CZ  ARG A1125    17840  11156  14619  -5338   -166  -1549       C\\nATOM   2269  NH1 ARG A1125      14.859 -25.182  31.553  1.00117.33           N\\nANISOU 2269  NH1 ARG A1125    17995  11419  15168  -5934   -115  -1411       N\\nATOM   2270  NH2 ARG A1125      16.978 -25.051  30.689  1.00114.27           N\\nANISOU 2270  NH2 ARG A1125    18294  10594  14529  -4971    -54  -1512       N\\nATOM   2271  N   TRP A1126      14.657 -16.753  31.387  1.00102.43           N\\nANISOU 2271  N   TRP A1126    13702  12620  12595  -3599   -520  -1377       N\\nATOM   2272  CA  TRP A1126      15.103 -15.775  32.375  1.00 99.11           C\\nANISOU 2272  CA  TRP A1126    13061  12418  12179  -3267   -310  -1183       C\\nATOM   2273  C   TRP A1126      14.567 -16.088  33.763  1.00100.00           C\\nANISOU 2273  C   TRP A1126    12842  12708  12447  -3564     17  -1092       C\\nATOM   2274  O   TRP A1126      15.235 -15.807  34.763  1.00 95.88           O\\nANISOU 2274  O   TRP A1126    12367  12211  11852  -3395    296   -877       O\\nATOM   2275  CB  TRP A1126      14.683 -14.363  31.959  1.00 98.18           C\\nANISOU 2275  CB  TRP A1126    12566  12644  12092  -2934   -622  -1293       C\\nATOM   2276  CG  TRP A1126      15.001 -14.027  30.537  1.00 99.97           C\\nANISOU 2276  CG  TRP A1126    13108  12760  12116  -2737   -990  -1360       C\\nATOM   2277  CD1 TRP A1126      14.127 -13.586  29.588  1.00102.49           C\\nANISOU 2277  CD1 TRP A1126    13224  13259  12460  -2750  -1458  -1549       C\\nATOM   2278  CD2 TRP A1126      16.280 -14.113  29.895  1.00100.88           C\\nANISOU 2278  CD2 TRP A1126    13796  12592  11940  -2519   -920  -1236       C\\nATOM   2279  NE1 TRP A1126      14.782 -13.387  28.397  1.00102.69           N\\nANISOU 2279  NE1 TRP A1126    13720  13132  12164  -2582  -1684  -1520       N\\nATOM   2280  CE2 TRP A1126      16.105 -13.705  28.559  1.00102.48           C\\nANISOU 2280  CE2 TRP A1126    14155  12841  11942  -2447  -1322  -1348       C\\nATOM   2281  CE3 TRP A1126      17.558 -14.494  30.321  1.00101.84           C\\nANISOU 2281  CE3 TRP A1126    14288  12451  11954  -2377   -563  -1048       C\\nATOM   2282  CZ2 TRP A1126      17.157 -13.666  27.646  1.00107.44           C\\nANISOU 2282  CZ2 TRP A1126    15302  13297  12222  -2277  -1308  -1288       C\\nATOM   2283  CZ3 TRP A1126      18.601 -14.457  29.411  1.00101.67           C\\nANISOU 2283  CZ3 TRP A1126    14713  12253  11664  -2171   -560  -1020       C\\nATOM   2284  CH2 TRP A1126      18.393 -14.051  28.088  1.00104.96           C\\nANISOU 2284  CH2 TRP A1126    15284  12756  11842  -2142   -895  -1146       C\\nATOM   2285  N   ASP A1127      13.370 -16.667  33.848  1.00105.05           N\\nANISOU 2285  N   ASP A1127    13142  13500  13273  -4040    -10  -1251       N\\nATOM   2286  CA  ASP A1127      12.801 -16.985  35.152  1.00105.65           C\\nANISOU 2286  CA  ASP A1127    12891  13805  13446  -4403    350  -1159       C\\nATOM   2287  C   ASP A1127      13.638 -18.034  35.873  1.00102.58           C\\nANISOU 2287  C   ASP A1127    13044  13002  12929  -4604    661   -828       C\\nATOM   2288  O   ASP A1127      14.085 -17.819  37.005  1.00 97.10           O\\nANISOU 2288  O   ASP A1127    12362  12413  12117  -4531    958   -598       O\\nATOM   2289  CB  ASP A1127      11.355 -17.458  34.988  1.00113.14           C\\nANISOU 2289  CB  ASP A1127    13346  15002  14642  -4937    260  -1403       C\\nATOM   2290  N   GLU A1128      13.877 -19.175  35.221  1.00105.05           N\\nANISOU 2290  N   GLU A1128    13834  12818  13263  -4840    560   -812       N\\nATOM   2291  CA  GLU A1128      14.589 -20.266  35.881  1.00101.37           C\\nANISOU 2291  CA  GLU A1128    13890  11878  12749  -5036    788   -497       C\\nATOM   2292  C   GLU A1128      16.064 -19.940  36.072  1.00 98.59           C\\nANISOU 2292  C   GLU A1128    13939  11292  12227  -4482    856   -278       C\\nATOM   2293  O   GLU A1128      16.652 -20.294  37.101  1.00 98.75           O\\nANISOU 2293  O   GLU A1128    14183  11164  12175  -4507   1075     48       O\\nATOM   2294  CB  GLU A1128      14.433 -21.557  35.083  1.00102.72           C\\nANISOU 2294  CB  GLU A1128    14465  11516  13047  -5400    625   -601       C\\nATOM   2295  CG  GLU A1128      13.004 -22.014  34.909  1.00109.16           C\\nANISOU 2295  CG  GLU A1128    14894  12518  14063  -6031    538   -807       C\\nATOM   2296  CD  GLU A1128      12.920 -23.465  34.496  1.00117.05           C\\nANISOU 2296  CD  GLU A1128    16374  12895  15205  -6501    444   -827       C\\nATOM   2297  OE1 GLU A1128      13.445 -24.324  35.236  1.00119.18           O\\nANISOU 2297  OE1 GLU A1128    17078  12716  15487  -6681    639   -499       O\\nATOM   2298  OE2 GLU A1128      12.343 -23.744  33.426  1.00122.20           O\\nANISOU 2298  OE2 GLU A1128    16997  13477  15956  -6685    137  -1171       O\\nATOM   2299  N   ALA A1129      16.686 -19.280  35.090  1.00106.39           N\\nANISOU 2299  N   ALA A1129    15026  12259  13140  -4007    658   -438       N\\nATOM   2300  CA  ALA A1129      18.089 -18.904  35.232  1.00 98.44           C\\nANISOU 2300  CA  ALA A1129    14315  11087  12002  -3503    734   -256       C\\nATOM   2301  C   ALA A1129      18.313 -18.065  36.481  1.00 99.96           C\\nANISOU 2301  C   ALA A1129    14247  11624  12110  -3345    925    -40       C\\nATOM   2302  O   ALA A1129      19.394 -18.111  37.080  1.00 91.71           O\\nANISOU 2302  O   ALA A1129    13458  10403  10986  -3100   1037    208       O\\nATOM   2303  CB  ALA A1129      18.562 -18.146  33.991  1.00 90.27           C\\nANISOU 2303  CB  ALA A1129    13335  10100  10864  -3097    524   -462       C\\nATOM   2304  N   ALA A1130      17.300 -17.301  36.894  1.00101.90           N\\nANISOU 2304  N   ALA A1130    13969  12366  12382  -3472    950   -165       N\\nATOM   2305  CA  ALA A1130      17.396 -16.557  38.143  1.00100.47           C\\nANISOU 2305  CA  ALA A1130    13541  12535  12097  -3370   1159    -30       C\\nATOM   2306  C   ALA A1130      17.236 -17.478  39.344  1.00 96.24           C\\nANISOU 2306  C   ALA A1130    13135  11951  11481  -3804   1437    243       C\\nATOM   2307  O   ALA A1130      17.958 -17.340  40.339  1.00 91.99           O\\nANISOU 2307  O   ALA A1130    12752  11434  10767  -3682   1586    498       O\\nATOM   2308  CB  ALA A1130      16.348 -15.446  38.172  1.00102.74           C\\nANISOU 2308  CB  ALA A1130    13205  13359  12471  -3324   1106   -319       C\\nATOM   2309  N   VAL A1131      16.303 -18.428  39.267  1.00 92.07           N\\nANISOU 2309  N   VAL A1131    12568  11350  11062  -4347   1484    213       N\\nATOM   2310  CA  VAL A1131      16.030 -19.294  40.409  1.00 92.71           C\\nANISOU 2310  CA  VAL A1131    12779  11404  11044  -4858   1755    513       C\\nATOM   2311  C   VAL A1131      17.210 -20.220  40.681  1.00 93.11           C\\nANISOU 2311  C   VAL A1131    13506  10845  11028  -4781   1726    899       C\\nATOM   2312  O   VAL A1131      17.533 -20.509  41.839  1.00 94.49           O\\nANISOU 2312  O   VAL A1131    13879  11018  11005  -4935   1900   1255       O\\nATOM   2313  CB  VAL A1131      14.728 -20.083  40.179  1.00 91.93           C\\nANISOU 2313  CB  VAL A1131    12455  11353  11120  -5514   1797    386       C\\nATOM   2314  N   ASN A1132      17.877 -20.696  39.626  1.00 98.73           N\\nANISOU 2314  N   ASN A1132    14580  11039  11893  -4528   1494    823       N\\nATOM   2315  CA  ASN A1132      19.028 -21.572  39.827  1.00 99.57           C\\nANISOU 2315  CA  ASN A1132    15279  10537  12016  -4371   1439   1132       C\\nATOM   2316  C   ASN A1132      20.208 -20.804  40.407  1.00 98.88           C\\nANISOU 2316  C   ASN A1132    15239  10564  11768  -3840   1452   1311       C\\nATOM   2317  O   ASN A1132      20.866 -21.282  41.338  1.00106.13           O\\nANISOU 2317  O   ASN A1132    16469  11262  12593  -3844   1482   1689       O\\nATOM   2318  CB  ASN A1132      19.417 -22.244  38.508  1.00100.70           C\\nANISOU 2318  CB  ASN A1132    15748  10141  12372  -4206   1226    906       C\\nATOM   2319  CG  ASN A1132      20.355 -23.432  38.702  1.00102.63           C\\nANISOU 2319  CG  ASN A1132    16592   9660  12743  -4136   1159   1173       C\\nATOM   2320  OD1 ASN A1132      21.259 -23.402  39.538  1.00 99.29           O\\nANISOU 2320  OD1 ASN A1132    16345   9141  12242  -3883   1185   1501       O\\nATOM   2321  ND2 ASN A1132      20.136 -24.489  37.929  1.00107.31           N\\nANISOU 2321  ND2 ASN A1132    17502   9719  13554  -4348   1034   1014       N\\nATOM   2322  N   LEU A1133      20.483 -19.606  39.881  1.00 85.10           N\\nANISOU 2322  N   LEU A1133    13195   9149   9988  -3405   1394   1062       N\\nATOM   2323  CA  LEU A1133      21.652 -18.849  40.317  1.00 79.83           C\\nANISOU 2323  CA  LEU A1133    12558   8566   9209  -2920   1377   1196       C\\nATOM   2324  C   LEU A1133      21.591 -18.470  41.792  1.00 85.06           C\\nANISOU 2324  C   LEU A1133    13112   9576   9629  -3048   1529   1445       C\\nATOM   2325  O   LEU A1133      22.638 -18.221  42.399  1.00 82.43           O\\nANISOU 2325  O   LEU A1133    12927   9198   9193  -2748   1484   1656       O\\nATOM   2326  CB  LEU A1133      21.813 -17.596  39.454  1.00 84.72           C\\nANISOU 2326  CB  LEU A1133    12879   9469   9842  -2527   1283    893       C\\nATOM   2327  CG  LEU A1133      22.459 -17.798  38.079  1.00 88.21           C\\nANISOU 2327  CG  LEU A1133    13529   9583  10405  -2245   1143    716       C\\nATOM   2328  CD1 LEU A1133      22.334 -16.537  37.242  1.00 90.94           C\\nANISOU 2328  CD1 LEU A1133    13587  10258  10710  -1997   1039    463       C\\nATOM   2329  CD2 LEU A1133      23.920 -18.203  38.219  1.00 83.43           C\\nANISOU 2329  CD2 LEU A1133    13242   8615   9844  -1895   1135    911       C\\nATOM   2330  N   ALA A1134      20.399 -18.433  42.386  1.00 84.49           N\\nANISOU 2330  N   ALA A1134    12774   9880   9449  -3501   1713   1404       N\\nATOM   2331  CA  ALA A1134      20.263 -18.129  43.804  1.00 83.30           C\\nANISOU 2331  CA  ALA A1134    12544  10115   8992  -3684   1912   1604       C\\nATOM   2332  C   ALA A1134      20.570 -19.322  44.697  1.00 95.28           C\\nANISOU 2332  C   ALA A1134    14547  11297  10359  -4027   1952   2087       C\\nATOM   2333  O   ALA A1134      20.536 -19.181  45.925  1.00100.46           O\\nANISOU 2333  O   ALA A1134    15234  12260  10675  -4222   2106   2315       O\\nATOM   2334  CB  ALA A1134      18.855 -17.614  44.103  1.00 88.70           C\\nANISOU 2334  CB  ALA A1134    12701  11389   9612  -4038   2147   1331       C\\nATOM   2335  N   LYS A1135      20.860 -20.486  44.116  1.00 88.10           N\\nANISOU 2335  N   LYS A1135    14044   9751   9678  -4109   1800   2243       N\\nATOM   2336  CA  LYS A1135      21.205 -21.680  44.871  1.00 87.20           C\\nANISOU 2336  CA  LYS A1135    14461   9179   9491  -4398   1755   2737       C\\nATOM   2337  C   LYS A1135      22.701 -21.967  44.852  1.00 86.32           C\\nANISOU 2337  C   LYS A1135    14744   8566   9488  -3866   1479   2966       C\\nATOM   2338  O   LYS A1135      23.109 -23.103  45.109  1.00102.38           O\\nANISOU 2338  O   LYS A1135    17270  10011  11619  -3979   1327   3328       O\\nATOM   2339  CB  LYS A1135      20.432 -22.884  44.332  1.00 91.82           C\\nANISOU 2339  CB  LYS A1135    15253   9320  10313  -4902   1752   2756       C\\nATOM   2340  N   SER A1136      23.523 -20.968  44.553  1.00 82.36           N\\nANISOU 2340  N   SER A1136    14022   8267   9005  -3296   1395   2765       N\\nATOM   2341  CA  SER A1136      24.959 -21.160  44.431  1.00 83.52           C\\nANISOU 2341  CA  SER A1136    14419   8004   9312  -2765   1149   2911       C\\nATOM   2342  C   SER A1136      25.684 -20.619  45.656  1.00 88.67           C\\nANISOU 2342  C   SER A1136    15092   8930   9667  -2607   1075   3205       C\\nATOM   2343  O   SER A1136      25.148 -19.816  46.424  1.00 92.03           O\\nANISOU 2343  O   SER A1136    15281   9935   9752  -2806   1240   3175       O\\nATOM   2344  CB  SER A1136      25.494 -20.477  43.171  1.00 79.24           C\\nANISOU 2344  CB  SER A1136    13626   7476   9007  -2270   1101   2495       C\\nATOM   2345  OG  SER A1136      25.423 -19.068  43.285  1.00 73.97           O\\nANISOU 2345  OG  SER A1136    12540   7401   8165  -2108   1183   2288       O\\nATOM   2346  N   ARG A1137      26.926 -21.078  45.832  1.00 91.39           N\\nANISOU 2346  N   ARG A1137    15712   8855  10158  -2229    806   3459       N\\nATOM   2347  CA  ARG A1137      27.767 -20.540  46.894  1.00 91.41           C\\nANISOU 2347  CA  ARG A1137    15721   9100   9909  -2019    652   3712       C\\nATOM   2348  C   ARG A1137      28.177 -19.101  46.613  1.00 85.85           C\\nANISOU 2348  C   ARG A1137    14558   8882   9179  -1656    695   3357       C\\nATOM   2349  O   ARG A1137      28.655 -18.413  47.521  1.00 85.58           O\\nANISOU 2349  O   ARG A1137    14453   9182   8883  -1561    604   3470       O\\nATOM   2350  CB  ARG A1137      29.009 -21.414  47.089  1.00 94.63           C\\nANISOU 2350  CB  ARG A1137    16484   8915  10557  -1666    293   4057       C\\nATOM   2351  N   TRP A1138      28.013 -18.639  45.372  1.00 85.61           N\\nANISOU 2351  N   TRP A1138    14253   8876   9400  -1476    803   2943       N\\nATOM   2352  CA  TRP A1138      28.240 -17.235  45.053  1.00 83.05           C\\nANISOU 2352  CA  TRP A1138    13523   8984   9049  -1214    846   2628       C\\nATOM   2353  C   TRP A1138      27.118 -16.360  45.596  1.00 83.65           C\\nANISOU 2353  C   TRP A1138    13343   9618   8821  -1522   1044   2460       C\\nATOM   2354  O   TRP A1138      27.378 -15.303  46.181  1.00 74.31           O\\nANISOU 2354  O   TRP A1138    11960   8813   7461  -1395   1022   2377       O\\nATOM   2355  CB  TRP A1138      28.387 -17.069  43.541  1.00 81.72           C\\nANISOU 2355  CB  TRP A1138    13205   8653   9191   -970    885   2291       C\\nATOM   2356  CG  TRP A1138      28.200 -15.675  43.038  1.00 80.37           C\\nANISOU 2356  CG  TRP A1138    12659   8893   8984   -845    952   1971       C\\nATOM   2357  CD1 TRP A1138      29.008 -14.601  43.270  1.00 79.75           C\\nANISOU 2357  CD1 TRP A1138    12375   9046   8880   -571    866   1931       C\\nATOM   2358  CD2 TRP A1138      27.151 -15.209  42.179  1.00 79.40           C\\nANISOU 2358  CD2 TRP A1138    12339   8950   8882   -990   1065   1659       C\\nATOM   2359  NE1 TRP A1138      28.520 -13.492  42.620  1.00 74.10           N\\nANISOU 2359  NE1 TRP A1138    11385   8600   8171   -543    925   1634       N\\nATOM   2360  CE2 TRP A1138      27.381 -13.840  41.944  1.00 77.74           C\\nANISOU 2360  CE2 TRP A1138    11841   9040   8657   -775   1031   1470       C\\nATOM   2361  CE3 TRP A1138      26.036 -15.814  41.592  1.00 70.14           C\\nANISOU 2361  CE3 TRP A1138    11201   7697   7754  -1292   1152   1527       C\\nATOM   2362  CZ2 TRP A1138      26.539 -13.069  41.149  1.00 75.61           C\\nANISOU 2362  CZ2 TRP A1138    11345   8968   8416   -815   1054   1185       C\\nATOM   2363  CZ3 TRP A1138      25.201 -15.044  40.801  1.00 72.99           C\\nANISOU 2363  CZ3 TRP A1138    11290   8307   8136  -1332   1174   1217       C\\nATOM   2364  CH2 TRP A1138      25.457 -13.689  40.588  1.00 72.54           C\\nANISOU 2364  CH2 TRP A1138    10974   8524   8064  -1078   1113   1063       C\\nATOM   2365  N   TYR A1139      25.867 -16.790  45.424  1.00 82.65           N\\nANISOU 2365  N   TYR A1139    13198   9549   8658  -1927   1233   2375       N\\nATOM   2366  CA  TYR A1139      24.743 -16.053  45.987  1.00 86.12           C\\nANISOU 2366  CA  TYR A1139    13337  10541   8845  -2219   1452   2182       C\\nATOM   2367  C   TYR A1139      24.771 -16.040  47.509  1.00 83.42           C\\nANISOU 2367  C   TYR A1139    13129  10492   8073  -2444   1516   2445       C\\nATOM   2368  O   TYR A1139      24.214 -15.122  48.120  1.00 85.20           O\\nANISOU 2368  O   TYR A1139    13075  11244   8055  -2528   1680   2223       O\\nATOM   2369  CB  TYR A1139      23.424 -16.647  45.483  1.00 93.06           C\\nANISOU 2369  CB  TYR A1139    14126  11418   9815  -2639   1632   2048       C\\nATOM   2370  CG  TYR A1139      22.187 -15.947  45.998  1.00 97.27           C\\nANISOU 2370  CG  TYR A1139    14256  12545  10156  -2931   1887   1793       C\\nATOM   2371  CD1 TYR A1139      21.714 -14.791  45.393  1.00 97.09           C\\nANISOU 2371  CD1 TYR A1139    13784  12829  10275  -2703   1891   1360       C\\nATOM   2372  CD2 TYR A1139      21.487 -16.449  47.086  1.00101.31           C\\nANISOU 2372  CD2 TYR A1139    14831  13310  10352  -3435   2125   1984       C\\nATOM   2373  CE1 TYR A1139      20.582 -14.152  45.862  1.00 98.45           C\\nANISOU 2373  CE1 TYR A1139    13534  13534  10340  -2906   2113   1072       C\\nATOM   2374  CE2 TYR A1139      20.357 -15.817  47.560  1.00102.23           C\\nANISOU 2374  CE2 TYR A1139    14515  14020  10307  -3689   2412   1691       C\\nATOM   2375  CZ  TYR A1139      19.909 -14.671  46.946  1.00 98.03           C\\nANISOU 2375  CZ  TYR A1139    13492  13774   9981  -3392   2400   1210       C\\nATOM   2376  OH  TYR A1139      18.781 -14.044  47.424  1.00 96.25           O\\nANISOU 2376  OH  TYR A1139    12784  14130   9656  -3586   2677    868       O\\nATOM   2377  N   ASN A1140      25.410 -17.028  48.134  1.00 84.98           N\\nANISOU 2377  N   ASN A1140    13766  10358   8165  -2531   1372   2902       N\\nATOM   2378  CA  ASN A1140      25.511 -17.069  49.585  1.00 81.09           C\\nANISOU 2378  CA  ASN A1140    13485  10139   7189  -2767   1384   3212       C\\nATOM   2379  C   ASN A1140      26.720 -16.316  50.123  1.00 81.14           C\\nANISOU 2379  C   ASN A1140    13495  10255   7081  -2354   1121   3259       C\\nATOM   2380  O   ASN A1140      26.732 -15.963  51.308  1.00 91.34           O\\nANISOU 2380  O   ASN A1140    14868  11933   7905  -2514   1139   3371       O\\nATOM   2381  CB  ASN A1140      25.564 -18.521  50.073  1.00 83.93           C\\nANISOU 2381  CB  ASN A1140    14351  10066   7474  -3090   1289   3738       C\\nATOM   2382  CG  ASN A1140      24.263 -19.268  49.834  1.00 88.69           C\\nANISOU 2382  CG  ASN A1140    14898  10646   8154  -3583   1553   3682       C\\nATOM   2383  OD1 ASN A1140      23.328 -19.182  50.631  1.00 94.13           O\\nANISOU 2383  OD1 ASN A1140    15427  11795   8542  -3964   1814   3633       O\\nATOM   2384  ND2 ASN A1140      24.203 -20.015  48.739  1.00 88.26           N\\nANISOU 2384  ND2 ASN A1140    14971  10056   8508  -3583   1485   3663       N\\nATOM   2385  N   GLN A1141      27.731 -16.058  49.292  1.00 79.05           N\\nANISOU 2385  N   GLN A1141    13135   9692   7209  -1861    889   3159       N\\nATOM   2386  CA  GLN A1141      28.944 -15.389  49.751  1.00 83.34           C\\nANISOU 2386  CA  GLN A1141    13640  10316   7710  -1493    612   3207       C\\nATOM   2387  C   GLN A1141      28.857 -13.872  49.622  1.00 86.83           C\\nANISOU 2387  C   GLN A1141    13669  11193   8130  -1321    691   2761       C\\nATOM   2388  O   GLN A1141      29.270 -13.148  50.534  1.00 90.33           O\\nANISOU 2388  O   GLN A1141    14085  11948   8290  -1274    578   2742       O\\nATOM   2389  CB  GLN A1141      30.158 -15.908  48.974  1.00 81.76           C\\nANISOU 2389  CB  GLN A1141    13505   9595   7966  -1066    339   3330       C\\nATOM   2390  N   THR A1142      28.341 -13.378  48.497  1.00 81.15           N\\nANISOU 2390  N   THR A1142    12660  10468   7708  -1228    841   2404       N\\nATOM   2391  CA  THR A1142      28.099 -11.952  48.276  1.00 75.62           C\\nANISOU 2391  CA  THR A1142    11594  10099   7040  -1081    896   1987       C\\nATOM   2392  C   THR A1142      26.654 -11.815  47.825  1.00 80.15           C\\nANISOU 2392  C   THR A1142    11953  10861   7638  -1313   1170   1698       C\\nATOM   2393  O   THR A1142      26.373 -11.645  46.629  1.00 76.21           O\\nANISOU 2393  O   THR A1142    11292  10208   7456  -1195   1180   1504       O\\nATOM   2394  CB  THR A1142      29.064 -11.368  47.245  1.00 71.01           C\\nANISOU 2394  CB  THR A1142    10854   9291   6836   -689    721   1873       C\\nATOM   2395  OG1 THR A1142      28.852 -12.004  45.979  1.00 61.90           O\\nANISOU 2395  OG1 THR A1142     9720   7819   5981   -656    792   1847       O\\nATOM   2396  CG2 THR A1142      30.507 -11.581  47.678  1.00 64.20           C\\nANISOU 2396  CG2 THR A1142    10120   8261   6011   -463    447   2144       C\\nATOM   2397  N   PRO A1143      25.702 -11.890  48.760  1.00 78.66           N\\nANISOU 2397  N   PRO A1143    11743  11039   7106  -1659   1396   1658       N\\nATOM   2398  CA  PRO A1143      24.288 -11.947  48.355  1.00 77.44           C\\nANISOU 2398  CA  PRO A1143    11332  11073   7019  -1917   1663   1400       C\\nATOM   2399  C   PRO A1143      23.754 -10.645  47.786  1.00 81.38           C\\nANISOU 2399  C   PRO A1143    11396  11793   7731  -1681   1672    913       C\\nATOM   2400  O   PRO A1143      22.964 -10.679  46.836  1.00 67.23           O\\nANISOU 2400  O   PRO A1143     9390   9947   6208  -1709   1715    723       O\\nATOM   2401  CB  PRO A1143      23.575 -12.337  49.655  1.00 74.02           C\\nANISOU 2401  CB  PRO A1143    10976  11033   6115  -2363   1931   1502       C\\nATOM   2402  CG  PRO A1143      24.484 -11.856  50.733  1.00 74.95           C\\nANISOU 2402  CG  PRO A1143    11275  11318   5883  -2235   1792   1614       C\\nATOM   2403  CD  PRO A1143      25.873 -12.037  50.213  1.00 80.85           C\\nANISOU 2403  CD  PRO A1143    12236  11590   6893  -1870   1423   1866       C\\nATOM   2404  N   ASN A1144      24.148  -9.498  48.346  1.00 79.84           N\\nANISOU 2404  N   ASN A1144    11080  11820   7435  -1453   1593    702       N\\nATOM   2405  CA  ASN A1144      23.656  -8.219  47.839  1.00 82.18           C\\nANISOU 2405  CA  ASN A1144    11000  12248   7977  -1203   1550    249       C\\nATOM   2406  C   ASN A1144      24.024  -8.031  46.372  1.00 83.32           C\\nANISOU 2406  C   ASN A1144    11122  12002   8536   -947   1323    262       C\\nATOM   2407  O   ASN A1144      23.168  -7.712  45.538  1.00 77.89           O\\nANISOU 2407  O   ASN A1144    10184  11322   8089   -907   1317     25       O\\nATOM   2408  CB  ASN A1144      24.209  -7.072  48.683  1.00 86.17           C\\nANISOU 2408  CB  ASN A1144    11466  12947   8328   -999   1448     44       C\\nATOM   2409  CG  ASN A1144      23.399  -6.831  49.942  1.00 91.58           C\\nANISOU 2409  CG  ASN A1144    12020  14149   8626  -1210   1730   -220       C\\nATOM   2410  OD1 ASN A1144      22.445  -6.054  49.938  1.00 89.43           O\\nANISOU 2410  OD1 ASN A1144    11378  14135   8467  -1137   1861   -680       O\\nATOM   2411  ND2 ASN A1144      23.778  -7.496  51.028  1.00 95.06           N\\nANISOU 2411  ND2 ASN A1144    12763  14756   8600  -1466   1818     62       N\\nATOM   2412  N   ARG A1145      25.302  -8.228  46.040  1.00 83.54           N\\nANISOU 2412  N   ARG A1145    11397  11711   8633   -780   1132    536       N\\nATOM   2413  CA  ARG A1145      25.740  -8.103  44.655  1.00 77.75           C\\nANISOU 2413  CA  ARG A1145    10673  10652   8215   -579    973    561       C\\nATOM   2414  C   ARG A1145      25.101  -9.167  43.774  1.00 76.82           C\\nANISOU 2414  C   ARG A1145    10624  10365   8200   -753   1062    630       C\\nATOM   2415  O   ARG A1145      24.721  -8.887  42.631  1.00 82.58           O\\nANISOU 2415  O   ARG A1145    11252  10993   9130   -675    981    488       O\\nATOM   2416  CB  ARG A1145      27.264  -8.189  44.587  1.00 73.67           C\\nANISOU 2416  CB  ARG A1145    10353   9896   7744   -393    814    816       C\\nATOM   2417  CG  ARG A1145      27.829  -8.227  43.179  1.00 69.75           C\\nANISOU 2417  CG  ARG A1145     9893   9104   7505   -234    729    865       C\\nATOM   2418  CD  ARG A1145      29.352  -8.232  43.189  1.00 73.59           C\\nANISOU 2418  CD  ARG A1145    10468   9428   8064    -50    612   1067       C\\nATOM   2419  NE  ARG A1145      29.897  -8.135  41.837  1.00 80.75           N\\nANISOU 2419  NE  ARG A1145    11375  10131   9175     79    594   1070       N\\nATOM   2420  CZ  ARG A1145      31.175  -7.901  41.556  1.00 82.83           C\\nANISOU 2420  CZ  ARG A1145    11612  10298   9561    237    528   1175       C\\nATOM   2421  NH1 ARG A1145      32.054  -7.734  42.535  1.00 82.57           N\\nANISOU 2421  NH1 ARG A1145    11535  10328   9508    307    415   1287       N\\nATOM   2422  NH2 ARG A1145      31.574  -7.829  40.293  1.00 85.74           N\\nANISOU 2422  NH2 ARG A1145    11982  10541  10053    302    578   1158       N\\nATOM   2423  N   ALA A1146      24.974 -10.393  44.287  1.00 78.38           N\\nANISOU 2423  N   ALA A1146    11025  10507   8249  -1011   1196    857       N\\nATOM   2424  CA  ALA A1146      24.412 -11.480  43.491  1.00 77.28           C\\nANISOU 2424  CA  ALA A1146    10992  10148   8224  -1212   1259    913       C\\nATOM   2425  C   ALA A1146      22.965 -11.191  43.114  1.00 83.69           C\\nANISOU 2425  C   ALA A1146    11482  11202   9113  -1389   1341    610       C\\nATOM   2426  O   ALA A1146      22.575 -11.340  41.951  1.00 81.20           O\\nANISOU 2426  O   ALA A1146    11127  10738   8988  -1380   1252    495       O\\nATOM   2427  CB  ALA A1146      24.519 -12.800  44.253  1.00 75.31           C\\nANISOU 2427  CB  ALA A1146    11049   9751   7813  -1491   1359   1239       C\\nATOM   2428  N   LYS A1147      22.154 -10.771  44.090  1.00 81.29           N\\nANISOU 2428  N   LYS A1147    10927  11303   8657  -1547   1506    451       N\\nATOM   2429  CA  LYS A1147      20.760 -10.442  43.804  1.00 80.52           C\\nANISOU 2429  CA  LYS A1147    10420  11486   8686  -1680   1585    116       C\\nATOM   2430  C   LYS A1147      20.649  -9.302  42.799  1.00 83.83           C\\nANISOU 2430  C   LYS A1147    10611  11866   9377  -1325   1329   -152       C\\nATOM   2431  O   LYS A1147      19.710  -9.273  41.995  1.00 68.30           O\\nANISOU 2431  O   LYS A1147     8403   9940   7609  -1375   1246   -350       O\\nATOM   2432  CB  LYS A1147      20.023 -10.088  45.098  1.00 67.35           C\\nANISOU 2432  CB  LYS A1147     8483  10311   6797  -1863   1853    -63       C\\nATOM   2433  N   ARG A1148      21.599  -8.365  42.815  1.00 85.54           N\\nANISOU 2433  N   ARG A1148    10910  11984   9606   -988   1167   -140       N\\nATOM   2434  CA  ARG A1148      21.574  -7.277  41.842  1.00 79.68           C\\nANISOU 2434  CA  ARG A1148    10031  11139   9107   -685    892   -317       C\\nATOM   2435  C   ARG A1148      21.891  -7.783  40.437  1.00 82.33           C\\nANISOU 2435  C   ARG A1148    10589  11152   9539   -673    733   -165       C\\nATOM   2436  O   ARG A1148      21.289  -7.330  39.457  1.00 90.33           O\\nANISOU 2436  O   ARG A1148    11469  12136  10717   -591    526   -312       O\\nATOM   2437  CB  ARG A1148      22.555  -6.182  42.261  1.00 70.66           C\\nANISOU 2437  CB  ARG A1148     8952   9944   7952   -403    768   -316       C\\nATOM   2438  CG  ARG A1148      21.892  -4.860  42.620  1.00 71.12           C\\nANISOU 2438  CG  ARG A1148     8676  10192   8155   -198    669   -688       C\\nATOM   2439  CD  ARG A1148      22.475  -4.260  43.892  1.00 73.19           C\\nANISOU 2439  CD  ARG A1148     8962  10601   8247   -122    743   -769       C\\nATOM   2440  NE  ARG A1148      23.934  -4.303  43.899  1.00 73.07           N\\nANISOU 2440  NE  ARG A1148     9271  10346   8145    -63    641   -461       N\\nATOM   2441  CZ  ARG A1148      24.686  -4.003  44.953  1.00 72.04           C\\nANISOU 2441  CZ  ARG A1148     9236  10306   7829    -40    656   -444       C\\nATOM   2442  NH1 ARG A1148      24.121  -3.632  46.093  1.00 77.77           N\\nANISOU 2442  NH1 ARG A1148     9809  11363   8378    -79    795   -729       N\\nATOM   2443  NH2 ARG A1148      26.005  -4.075  44.867  1.00 70.75           N\\nANISOU 2443  NH2 ARG A1148     9301   9933   7647     15    532   -167       N\\nATOM   2444  N   VAL A1149      22.824  -8.727  40.321  1.00 86.59           N\\nANISOU 2444  N   VAL A1149    11473  11454   9974   -742    812    112       N\\nATOM   2445  CA  VAL A1149      23.201  -9.252  39.011  1.00 82.53           C\\nANISOU 2445  CA  VAL A1149    11189  10655   9513   -723    713    200       C\\nATOM   2446  C   VAL A1149      22.160 -10.240  38.500  1.00 89.46           C\\nANISOU 2446  C   VAL A1149    12052  11515  10424  -1007    747    112       C\\nATOM   2447  O   VAL A1149      21.841 -10.260  37.304  1.00 88.71           O\\nANISOU 2447  O   VAL A1149    11995  11326  10387  -1003    583     17       O\\nATOM   2448  CB  VAL A1149      24.603  -9.881  39.089  1.00 69.15           C\\nANISOU 2448  CB  VAL A1149     9812   8710   7751   -638    790    459       C\\nATOM   2449  CG1 VAL A1149      24.961 -10.583  37.793  1.00 62.41           C\\nANISOU 2449  CG1 VAL A1149     9197   7590   6927   -632    765    483       C\\nATOM   2450  CG2 VAL A1149      25.636  -8.812  39.423  1.00 65.57           C\\nANISOU 2450  CG2 VAL A1149     9323   8286   7303   -385    710    522       C\\nATOM   2451  N   ILE A1150      21.606 -11.063  39.394  1.00 84.73           N\\nANISOU 2451  N   ILE A1150    11413  11014   9767  -1295    945    151       N\\nATOM   2452  CA  ILE A1150      20.566 -12.008  38.997  1.00 83.24           C\\nANISOU 2452  CA  ILE A1150    11179  10809   9639  -1639    980     64       C\\nATOM   2453  C   ILE A1150      19.315 -11.263  38.545  1.00 84.16           C\\nANISOU 2453  C   ILE A1150    10861  11211   9905  -1651    831   -246       C\\nATOM   2454  O   ILE A1150      18.622 -11.692  37.612  1.00 93.69           O\\nANISOU 2454  O   ILE A1150    12028  12360  11209  -1807    688   -369       O\\nATOM   2455  CB  ILE A1150      20.272 -12.986  40.152  1.00 84.83           C\\nANISOU 2455  CB  ILE A1150    11442  11060   9730  -2003   1240    225       C\\nATOM   2456  CG1 ILE A1150      21.486 -13.878  40.414  1.00 82.12           C\\nANISOU 2456  CG1 ILE A1150    11568  10333   9299  -1964   1285    553       C\\nATOM   2457  CG2 ILE A1150      19.059 -13.839  39.844  1.00 86.81           C\\nANISOU 2457  CG2 ILE A1150    11564  11344  10076  -2432   1287    113       C\\nATOM   2458  CD1 ILE A1150      21.367 -14.717  41.663  1.00 70.60           C\\nANISOU 2458  CD1 ILE A1150    10253   8891   7682  -2294   1484    806       C\\nATOM   2459  N   THR A1151      19.009 -10.131  39.188  1.00 79.62           N\\nANISOU 2459  N   THR A1151     9946  10934   9371  -1467    829   -404       N\\nATOM   2460  CA  THR A1151      17.920  -9.283  38.713  1.00 85.27           C\\nANISOU 2460  CA  THR A1151    10223  11875  10301  -1363    618   -716       C\\nATOM   2461  C   THR A1151      18.194  -8.785  37.302  1.00 88.73           C\\nANISOU 2461  C   THR A1151    10820  12078  10815  -1128    245   -709       C\\nATOM   2462  O   THR A1151      17.290  -8.744  36.460  1.00 89.80           O\\nANISOU 2462  O   THR A1151    10761  12268  11090  -1177     -2   -876       O\\nATOM   2463  CB  THR A1151      17.713  -8.098  39.655  1.00 85.11           C\\nANISOU 2463  CB  THR A1151     9861  12141  10338  -1127    668   -919       C\\nATOM   2464  OG1 THR A1151      17.364  -8.577  40.957  1.00 90.34           O\\nANISOU 2464  OG1 THR A1151    10377  13098  10849  -1398   1046   -947       O\\nATOM   2465  CG2 THR A1151      16.602  -7.194  39.144  1.00 80.06           C\\nANISOU 2465  CG2 THR A1151     8743  11680   9998   -942    398  -1262       C\\nATOM   2466  N   THR A1152      19.440  -8.402  37.023  1.00 89.05           N\\nANISOU 2466  N   THR A1152    11208  11880  10745   -898    191   -508       N\\nATOM   2467  CA  THR A1152      19.772  -7.948  35.679  1.00 88.03           C\\nANISOU 2467  CA  THR A1152    11283  11556  10607   -736   -114   -459       C\\nATOM   2468  C   THR A1152      19.666  -9.080  34.665  1.00 84.57           C\\nANISOU 2468  C   THR A1152    11105  10963  10066   -967   -143   -432       C\\nATOM   2469  O   THR A1152      19.276  -8.846  33.516  1.00 88.93           O\\nANISOU 2469  O   THR A1152    11704  11483  10603   -948   -442   -501       O\\nATOM   2470  CB  THR A1152      21.170  -7.335  35.670  1.00 84.93           C\\nANISOU 2470  CB  THR A1152    11169  10986  10115   -508    -96   -248       C\\nATOM   2471  OG1 THR A1152      21.238  -6.314  36.674  1.00 87.26           O\\nANISOU 2471  OG1 THR A1152    11240  11404  10511   -322    -88   -315       O\\nATOM   2472  CG2 THR A1152      21.473  -6.721  34.321  1.00 75.79           C\\nANISOU 2472  CG2 THR A1152    10215   9677   8903   -385   -386   -175       C\\nATOM   2473  N   PHE A1153      19.988 -10.311  35.069  1.00 80.31           N\\nANISOU 2473  N   PHE A1153    10763  10305   9447  -1189    130   -341       N\\nATOM   2474  CA  PHE A1153      19.838 -11.445  34.163  1.00 86.85           C\\nANISOU 2474  CA  PHE A1153    11850  10938  10209  -1417    102   -378       C\\nATOM   2475  C   PHE A1153      18.375 -11.753  33.876  1.00 94.28           C\\nANISOU 2475  C   PHE A1153    12493  12048  11280  -1692    -61   -605       C\\nATOM   2476  O   PHE A1153      18.051 -12.271  32.802  1.00 97.03           O\\nANISOU 2476  O   PHE A1153    13001  12289  11578  -1834   -250   -712       O\\nATOM   2477  CB  PHE A1153      20.524 -12.681  34.744  1.00 85.98           C\\nANISOU 2477  CB  PHE A1153    12033  10584  10052  -1564    394   -224       C\\nATOM   2478  CG  PHE A1153      21.973 -12.790  34.388  1.00 82.81           C\\nANISOU 2478  CG  PHE A1153    11993   9932   9541  -1323    479    -73       C\\nATOM   2479  CD1 PHE A1153      22.400 -12.549  33.096  1.00 87.89           C\\nANISOU 2479  CD1 PHE A1153    12840  10494  10062  -1196    348   -140       C\\nATOM   2480  CD2 PHE A1153      22.908 -13.132  35.345  1.00 77.41           C\\nANISOU 2480  CD2 PHE A1153    11425   9126   8862  -1234    685    132       C\\nATOM   2481  CE1 PHE A1153      23.735 -12.650  32.764  1.00 85.44           C\\nANISOU 2481  CE1 PHE A1153    12792  10012   9660   -991    485    -39       C\\nATOM   2482  CE2 PHE A1153      24.244 -13.233  35.021  1.00 77.07           C\\nANISOU 2482  CE2 PHE A1153    11625   8883   8776   -993    759    238       C\\nATOM   2483  CZ  PHE A1153      24.658 -12.992  33.729  1.00 80.39           C\\nANISOU 2483  CZ  PHE A1153    12194   9251   9099   -874    690    135       C\\nATOM   2484  N   ARG A1154      17.484 -11.446  34.817  1.00 88.53           N\\nANISOU 2484  N   ARG A1154    11311  11612  10713  -1783     15   -710       N\\nATOM   2485  CA  ARG A1154      16.070 -11.771  34.679  1.00 90.56           C\\nANISOU 2485  CA  ARG A1154    11175  12087  11146  -2076    -96   -944       C\\nATOM   2486  C   ARG A1154      15.287 -10.657  33.990  1.00 94.08           C\\nANISOU 2486  C   ARG A1154    11255  12736  11753  -1845   -507  -1151       C\\nATOM   2487  O   ARG A1154      14.589 -10.908  33.004  1.00 98.43           O\\nANISOU 2487  O   ARG A1154    11752  13292  12353  -1977   -823  -1290       O\\nATOM   2488  CB  ARG A1154      15.471 -12.072  36.056  1.00 91.66           C\\nANISOU 2488  CB  ARG A1154    10967  12492  11368  -2333    250   -973       C\\nATOM   2489  CG  ARG A1154      13.953 -12.110  36.087  1.00 98.75           C\\nANISOU 2489  CG  ARG A1154    11273  13741  12505  -2600    179  -1261       C\\nATOM   2490  CD  ARG A1154      13.450 -12.527  37.460  1.00 98.15           C\\nANISOU 2490  CD  ARG A1154    10903  13957  12432  -2937    616  -1264       C\\nATOM   2491  NE  ARG A1154      14.141 -11.809  38.526  1.00 96.23           N\\nANISOU 2491  NE  ARG A1154    10691  13830  12042  -2666    855  -1169       N\\nATOM   2492  CZ  ARG A1154      13.729 -10.656  39.043  1.00 99.35           C\\nANISOU 2492  CZ  ARG A1154    10627  14571  12550  -2384    862  -1413       C\\nATOM   2493  NH1 ARG A1154      12.618 -10.085  38.594  1.00102.81           N\\nANISOU 2493  NH1 ARG A1154    10503  15271  13290  -2299    634  -1752       N\\nATOM   2494  NH2 ARG A1154      14.426 -10.074  40.011  1.00 97.58           N\\nANISOU 2494  NH2 ARG A1154    10500  14418  12157  -2171   1067  -1343       N\\nATOM   2495  N   THR A1155      15.394  -9.425  34.492  1.00 91.70           N\\nANISOU 2495  N   THR A1155    10720  12575  11545  -1493   -553  -1180       N\\nATOM   2496  CA  THR A1155      14.626  -8.327  33.913  1.00 95.66           C\\nANISOU 2496  CA  THR A1155    10869  13211  12265  -1227   -991  -1368       C\\nATOM   2497  C   THR A1155      15.189  -7.887  32.570  1.00 97.84           C\\nANISOU 2497  C   THR A1155    11567  13229  12380  -1038  -1391  -1215       C\\nATOM   2498  O   THR A1155      14.426  -7.500  31.678  1.00103.63           O\\nANISOU 2498  O   THR A1155    12148  14011  13216   -975  -1852  -1325       O\\nATOM   2499  CB  THR A1155      14.590  -7.135  34.871  1.00 96.53           C\\nANISOU 2499  CB  THR A1155    10639  13482  12554   -890   -932  -1480       C\\nATOM   2500  OG1 THR A1155      15.865  -6.481  34.875  1.00 89.26           O\\nANISOU 2500  OG1 THR A1155    10139  12306  11469   -624   -926  -1243       O\\nATOM   2501  CG2 THR A1155      14.254  -7.597  36.282  1.00102.13           C\\nANISOU 2501  CG2 THR A1155    11038  14480  13285  -1108   -443  -1599       C\\nATOM   2502  N   GLY A1156      16.506  -7.938  32.402  1.00 98.59           N\\nANISOU 2502  N   GLY A1156    12176  13074  12209   -961  -1232   -958       N\\nATOM   2503  CA  GLY A1156      17.109  -7.426  31.192  1.00 97.17           C\\nANISOU 2503  CA  GLY A1156    12393  12702  11824   -813  -1538   -796       C\\nATOM   2504  C   GLY A1156      17.208  -5.922  31.139  1.00 94.99           C\\nANISOU 2504  C   GLY A1156    12028  12391  11674   -459  -1843   -727       C\\nATOM   2505  O   GLY A1156      17.414  -5.364  30.057  1.00 94.83           O\\nANISOU 2505  O   GLY A1156    12287  12241  11502   -370  -2199   -582       O\\nATOM   2506  N   THR A1157      17.055  -5.243  32.275  1.00 98.59           N\\nANISOU 2506  N   THR A1157    12130  12944  12386   -269  -1724   -831       N\\nATOM   2507  CA  THR A1157      17.188  -3.793  32.334  1.00 99.99           C\\nANISOU 2507  CA  THR A1157    12241  13012  12740     83  -2014   -798       C\\nATOM   2508  C   THR A1157      18.117  -3.396  33.475  1.00 95.58           C\\nANISOU 2508  C   THR A1157    11722  12408  12187    197  -1666   -741       C\\nATOM   2509  O   THR A1157      18.739  -4.258  34.103  1.00 99.83           O\\nANISOU 2509  O   THR A1157    12385  12993  12552     13  -1238   -673       O\\nATOM   2510  CB  THR A1157      15.819  -3.130  32.503  1.00100.53           C\\nANISOU 2510  CB  THR A1157    11744  13243  13210    283  -2359  -1106       C\\nATOM   2511  N   TRP A1158      18.225  -2.094  33.747  1.00 93.22           N\\nANISOU 2511  N   TRP A1158    11337  11987  12095    500  -1890   -770       N\\nATOM   2512  CA  TRP A1158      19.077  -1.577  34.810  1.00 93.29           C\\nANISOU 2512  CA  TRP A1158    11380  11944  12121    611  -1638   -757       C\\nATOM   2513  C   TRP A1158      18.284  -1.180  36.050  1.00100.83           C\\nANISOU 2513  C   TRP A1158    11839  13130  13343    767  -1520  -1143       C\\nATOM   2514  O   TRP A1158      18.687  -0.262  36.773  1.00104.41           O\\nANISOU 2514  O   TRP A1158    12262  13494  13913    976  -1523  -1234       O\\nATOM   2515  CB  TRP A1158      19.888  -0.380  34.315  1.00 93.24           C\\nANISOU 2515  CB  TRP A1158    11675  11603  12148    796  -1939   -534       C\\nATOM   2516  CG  TRP A1158      20.831  -0.689  33.202  1.00 90.86           C\\nANISOU 2516  CG  TRP A1158    11861  11134  11527    615  -1955   -159       C\\nATOM   2517  CD1 TRP A1158      20.661  -0.401  31.878  1.00 92.31           C\\nANISOU 2517  CD1 TRP A1158    12294  11175  11605    591  -2335     30       C\\nATOM   2518  CD2 TRP A1158      22.100  -1.341  33.312  1.00 84.64           C\\nANISOU 2518  CD2 TRP A1158    11359  10335  10467    435  -1569     52       C\\nATOM   2519  NE1 TRP A1158      21.746  -0.835  31.158  1.00 87.61           N\\nANISOU 2519  NE1 TRP A1158    12125  10516  10649    382  -2146    322       N\\nATOM   2520  CE2 TRP A1158      22.643  -1.417  32.015  1.00 81.33           C\\nANISOU 2520  CE2 TRP A1158    11324   9793   9787    307  -1675    322       C\\nATOM   2521  CE3 TRP A1158      22.829  -1.871  34.381  1.00 79.01           C\\nANISOU 2521  CE3 TRP A1158    10605   9715   9699    377  -1161     35       C\\nATOM   2522  CZ2 TRP A1158      23.881  -2.001  31.759  1.00 77.25           C\\nANISOU 2522  CZ2 TRP A1158    11088   9260   9004    149  -1343    521       C\\nATOM   2523  CZ3 TRP A1158      24.059  -2.452  34.124  1.00 69.87           C\\nANISOU 2523  CZ3 TRP A1158     9733   8502   8314    244   -903    268       C\\nATOM   2524  CH2 TRP A1158      24.572  -2.511  32.824  1.00 69.73           C\\nANISOU 2524  CH2 TRP A1158    10033   8375   8085    144   -972    482       C\\nATOM   2525  N   ASP A1159      17.156  -1.850  36.306  1.00 98.45           N\\nANISOU 2525  N   ASP A1159    11135  13138  13133    646  -1402  -1399       N\\nATOM   2526  CA  ASP A1159      16.331  -1.497  37.457  1.00 97.23           C\\nANISOU 2526  CA  ASP A1159    10456  13283  13205    769  -1227  -1814       C\\nATOM   2527  C   ASP A1159      17.098  -1.638  38.765  1.00 90.66           C\\nANISOU 2527  C   ASP A1159     9725  12569  12151    685   -774  -1819       C\\nATOM   2528  O   ASP A1159      16.820  -0.916  39.727  1.00 92.33           O\\nANISOU 2528  O   ASP A1159     9651  12933  12497    879   -679  -2146       O\\nATOM   2529  CB  ASP A1159      15.076  -2.368  37.498  1.00105.69           C\\nANISOU 2529  CB  ASP A1159    11073  14718  14366    540  -1095  -2046       C\\nATOM   2530  CG  ASP A1159      14.329  -2.379  36.182  1.00109.35           C\\nANISOU 2530  CG  ASP A1159    11447  15092  15007    573  -1581  -2031       C\\nATOM   2531  OD1 ASP A1159      14.839  -2.991  35.220  1.00106.95           O\\nANISOU 2531  OD1 ASP A1159    11588  14593  14457    378  -1693  -1714       O\\nATOM   2532  OD2 ASP A1159      13.231  -1.786  36.115  1.00113.68           O\\nANISOU 2532  OD2 ASP A1159    11472  15783  15940    804  -1860  -2361       O\\nATOM   2533  N   ALA A1160      18.061  -2.558  38.822  1.00 90.75           N\\nANISOU 2533  N   ALA A1160    10142  12514  11824    416   -516  -1483       N\\nATOM   2534  CA  ALA A1160      18.793  -2.777  40.062  1.00 83.07           C\\nANISOU 2534  CA  ALA A1160     9285  11661  10616    322   -147  -1445       C\\nATOM   2535  C   ALA A1160      19.805  -1.671  40.330  1.00 83.07           C\\nANISOU 2535  C   ALA A1160     9492  11427  10644    577   -301  -1398       C\\nATOM   2536  O   ALA A1160      20.159  -1.427  41.488  1.00 80.26           O\\nANISOU 2536  O   ALA A1160     9111  11213  10170    595    -98  -1520       O\\nATOM   2537  CB  ALA A1160      19.490  -4.133  40.023  1.00 69.19           C\\nANISOU 2537  CB  ALA A1160     7878   9858   8554     -5    110  -1098       C\\nATOM   2538  N   TYR A1161      20.270  -0.989  39.289  1.00 85.89           N\\nANISOU 2538  N   TYR A1161    10067  11436  11131    737   -663  -1221       N\\nATOM   2539  CA  TYR A1161      21.312   0.021  39.439  1.00 81.29           C\\nANISOU 2539  CA  TYR A1161     9712  10587  10590    902   -820  -1122       C\\nATOM   2540  C   TYR A1161      20.830   1.413  39.031  1.00 86.56           C\\nANISOU 2540  C   TYR A1161    10259  11009  11620   1221  -1257  -1309       C\\nATOM   2541  O   TYR A1161      19.780   1.882  39.473  1.00 90.75           O\\nANISOU 2541  O   TYR A1161    10405  11678  12398   1423  -1325  -1710       O\\nATOM   2542  CB  TYR A1161      22.541  -0.357  38.608  1.00 78.82           C\\nANISOU 2542  CB  TYR A1161     9822  10037  10089    757   -833   -681       C\\nATOM   2543  CG  TYR A1161      23.144  -1.708  38.932  1.00 79.07           C\\nANISOU 2543  CG  TYR A1161    10004  10209   9831    508   -467   -486       C\\nATOM   2544  CD1 TYR A1161      22.612  -2.876  38.400  1.00 78.87           C\\nANISOU 2544  CD1 TYR A1161     9993  10274   9701    320   -342   -427       C\\nATOM   2545  CD2 TYR A1161      24.263  -1.813  39.748  1.00 75.01           C\\nANISOU 2545  CD2 TYR A1161     9629   9697   9174    468   -297   -359       C\\nATOM   2546  CE1 TYR A1161      23.166  -4.110  38.683  1.00 74.50           C\\nANISOU 2546  CE1 TYR A1161     9613   9760   8934    118    -53   -248       C\\nATOM   2547  CE2 TYR A1161      24.824  -3.042  40.039  1.00 67.83           C\\nANISOU 2547  CE2 TYR A1161     8865   8860   8048    288    -30   -162       C\\nATOM   2548  CZ  TYR A1161      24.272  -4.189  39.504  1.00 71.43           C\\nANISOU 2548  CZ  TYR A1161     9359   9354   8428    123     94   -104       C\\nATOM   2549  OH  TYR A1161      24.829  -5.416  39.787  1.00 69.66           O\\nANISOU 2549  OH  TYR A1161     9313   9118   8037    -32    319     91       O\\nATOM   2550  N   SER A 364      17.508   3.047  36.367  1.00104.00           N\\nATOM   2551  CA  SER A 364      18.568   3.670  35.585  1.00104.92           C\\nATOM   2552  C   SER A 364      18.623   3.097  34.167  1.00111.72           C\\nATOM   2553  O   SER A 364      19.675   3.111  33.526  1.00111.66           O\\nATOM   2554  CB  SER A 364      19.919   3.488  36.282  1.00 97.65           C\\nATOM   2555  N   GLN A 365      17.486   2.600  33.682  1.00122.15           N\\nATOM   2556  CA  GLN A 365      17.397   1.937  32.386  1.00115.38           C\\nATOM   2557  C   GLN A 365      16.553   2.767  31.428  1.00110.61           C\\nATOM   2558  O   GLN A 365      15.419   3.137  31.753  1.00 98.43           O\\nATOM   2559  CB  GLN A 365      16.796   0.536  32.527  1.00106.22           C\\nATOM   2560  N   GLN A 366      17.101   3.039  30.246  1.00120.06           N\\nATOM   2561  CA  GLN A 366      16.385   3.791  29.223  1.00115.06           C\\nATOM   2562  C   GLN A 366      15.363   2.887  28.544  1.00110.82           C\\nATOM   2563  O   GLN A 366      15.719   1.836  27.999  1.00106.83           O\\nATOM   2564  CB  GLN A 366      17.364   4.363  28.199  1.00114.61           C\\nATOM   2565  N   LYS A 367      14.097   3.295  28.574  1.00106.95           N\\nATOM   2566  CA  LYS A 367      13.014   2.529  27.974  1.00112.85           C\\nATOM   2567  C   LYS A 367      12.771   2.895  26.516  1.00109.20           C\\nATOM   2568  O   LYS A 367      11.803   2.410  25.921  1.00103.35           O\\nATOM   2569  CB  LYS A 367      11.727   2.721  28.781  1.00115.42           C\\nATOM   2570  N   GLU A 368      13.626   3.733  25.930  1.00114.20           N\\nATOM   2571  CA  GLU A 368      13.436   4.206  24.566  1.00 99.97           C\\nATOM   2572  C   GLU A 368      14.152   3.361  23.525  1.00100.67           C\\nATOM   2573  O   GLU A 368      13.805   3.444  22.342  1.00 97.34           O\\nATOM   2574  CB  GLU A 368      13.920   5.655  24.437  1.00 81.44           C\\nATOM   2575  CG  GLU A 368      13.087   6.681  25.188  1.00 79.48           C\\nATOM   2576  CD  GLU A 368      11.923   7.216  24.368  1.00 87.69           C\\nATOM   2577  OE1 GLU A 368      11.484   6.529  23.419  1.00 87.57           O\\nATOM   2578  OE2 GLU A 368      11.451   8.332  24.674  1.00 90.78           O\\nATOM   2579  N   LYS A 369      15.139   2.557  23.932  1.00101.97           N\\nATOM   2580  CA  LYS A 369      15.965   1.842  22.963  1.00 93.96           C\\nATOM   2581  C   LYS A 369      15.123   0.959  22.051  1.00 87.89           C\\nATOM   2582  O   LYS A 369      15.377   0.886  20.844  1.00 84.82           O\\nATOM   2583  CB  LYS A 369      17.025   1.012  23.689  1.00 94.15           C\\nATOM   2584  N   LYS A 370      14.107   0.291  22.605  1.00 95.07           N\\nATOM   2585  CA  LYS A 370      13.254  -0.567  21.787  1.00 92.51           C\\nATOM   2586  C   LYS A 370      12.587   0.220  20.665  1.00 85.60           C\\nATOM   2587  O   LYS A 370      12.454  -0.280  19.541  1.00 77.93           O\\nATOM   2588  CB  LYS A 370      12.203  -1.254  22.662  1.00 85.65           C\\nATOM   2589  N   ALA A 371      12.167   1.454  20.944  1.00 85.70           N\\nATOM   2590  CA  ALA A 371      11.556   2.271  19.901  1.00 78.85           C\\nATOM   2591  C   ALA A 371      12.589   2.776  18.902  1.00 73.40           C\\nATOM   2592  O   ALA A 371      12.274   2.940  17.718  1.00 67.94           O\\nATOM   2593  CB  ALA A 371      10.805   3.440  20.520  1.00 20.00           C\\nATOM   2594  N   THR A 372      13.820   3.030  19.357  1.00 75.36           N\\nATOM   2595  CA  THR A 372      14.875   3.470  18.451  1.00 64.07           C\\nATOM   2596  C   THR A 372      15.326   2.343  17.535  1.00 71.79           C\\nATOM   2597  O   THR A 372      15.714   2.593  16.389  1.00 80.74           O\\nATOM   2598  CB  THR A 372      16.066   4.010  19.246  1.00 69.33           C\\nATOM   2599  OG1 THR A 372      15.634   5.071  20.104  1.00 74.68           O\\nATOM   2600  CG2 THR A 372      17.138   4.544  18.316  1.00 68.04           C\\nATOM   2601  N   GLN A 373      15.283   1.100  18.019  1.00 68.72           N\\nATOM   2602  CA  GLN A 373      15.663  -0.031  17.180  1.00 79.96           C\\nATOM   2603  C   GLN A 373      14.624  -0.283  16.095  1.00 79.40           C\\nATOM   2604  O   GLN A 373      14.972  -0.633  14.961  1.00 75.09           O\\nATOM   2605  CB  GLN A 373      15.857  -1.276  18.043  1.00 95.27           C\\nATOM   2606  CG  GLN A 373      17.006  -1.162  19.028  1.00107.01           C\\nATOM   2607  CD  GLN A 373      16.835  -2.074  20.228  1.00113.19           C\\nATOM   2608  OE1 GLN A 373      15.768  -2.652  20.438  1.00109.22           O\\nATOM   2609  NE2 GLN A 373      17.889  -2.204  21.025  1.00117.08           N\\nATOM   2610  N   MET A 374      13.345  -0.105  16.421  1.00 79.17           N\\nATOM   2611  CA  MET A 374      12.307  -0.277  15.413  1.00 76.40           C\\nATOM   2612  C   MET A 374      12.384   0.814  14.350  1.00 70.69           C\\nATOM   2613  O   MET A 374      12.182   0.543  13.160  1.00 68.25           O\\nATOM   2614  CB  MET A 374      10.934  -0.292  16.079  1.00 77.49           C\\nATOM   2615  CG  MET A 374       9.801  -0.689  15.153  1.00 81.14           C\\nATOM   2616  SD  MET A 374       8.219  -0.741  16.009  1.00 84.97           S\\nATOM   2617  CE  MET A 374       8.086   0.958  16.565  1.00103.28           C\\nATOM   2618  N   ALA A 375      12.684   2.052  14.756  1.00 72.85           N\\nATOM   2619  CA  ALA A 375      12.789   3.144  13.793  1.00 69.01           C\\nATOM   2620  C   ALA A 375      13.899   2.887  12.783  1.00 71.99           C\\nATOM   2621  O   ALA A 375      13.756   3.203  11.596  1.00 68.65           O\\nATOM   2622  CB  ALA A 375      13.021   4.464  14.513  1.00 20.00           C\\nATOM   2623  N   ALA A 376      15.014   2.312  13.234  1.00 72.30           N\\nATOM   2624  CA  ALA A 376      16.110   2.018  12.320  1.00 74.21           C\\nATOM   2625  C   ALA A 376      15.790   0.830  11.427  1.00 77.19           C\\nATOM   2626  O   ALA A 376      16.261   0.771  10.285  1.00 87.02           O\\nATOM   2627  CB  ALA A 376      17.398   1.765  13.104  1.00 74.32           C\\nATOM   2628  N   ILE A 377      15.001  -0.125  11.921  1.00 87.67           N\\nATOM   2629  CA  ILE A 377      14.633  -1.265  11.089  1.00 95.90           C\\nATOM   2630  C   ILE A 377      13.706  -0.839   9.957  1.00101.03           C\\nATOM   2631  O   ILE A 377      13.826  -1.331   8.830  1.00 92.85           O\\nATOM   2632  CB  ILE A 377      13.963  -2.361  11.939  1.00 20.00           C\\nATOM   2633  CG1 ILE A 377      14.964  -2.954  12.932  1.00 20.00           C\\nATOM   2634  CG2 ILE A 377      13.385  -3.448  11.046  1.00 20.00           C\\nATOM   2635  CD1 ILE A 377      14.332  -3.844  13.978  1.00 20.00           C\\nATOM   2636  N   VAL A 378      12.786   0.088  10.234  1.00 89.06           N\\nATOM   2637  CA  VAL A 378      11.896   0.596   9.192  1.00 75.68           C\\nATOM   2638  C   VAL A 378      12.683   1.387   8.156  1.00 75.18           C\\nATOM   2639  O   VAL A 378      12.445   1.268   6.948  1.00 76.19           O\\nATOM   2640  CB  VAL A 378      10.775   1.445   9.820  1.00 64.00           C\\nATOM   2641  CG1 VAL A 378       9.960   2.132   8.740  1.00 62.64           C\\nATOM   2642  CG2 VAL A 378       9.887   0.580  10.701  1.00 69.48           C\\nATOM   2643  N   ALA A 379      13.629   2.210   8.612  1.00 84.87           N\\nATOM   2644  CA  ALA A 379      14.470   2.963   7.688  1.00 87.10           C\\nATOM   2645  C   ALA A 379      15.330   2.035   6.842  1.00 88.96           C\\nATOM   2646  O   ALA A 379      15.578   2.310   5.662  1.00 81.40           O\\nATOM   2647  CB  ALA A 379      15.348   3.945   8.463  1.00 44.79           C\\nATOM   2648  N   GLY A 380      15.802   0.935   7.428  1.00 77.23           N\\nATOM   2649  CA  GLY A 380      16.620   0.001   6.670  1.00 80.45           C\\nATOM   2650  C   GLY A 380      15.818  -0.749   5.624  1.00 77.59           C\\nATOM   2651  O   GLY A 380      16.246  -0.884   4.475  1.00 69.34           O\\nATOM   2652  N   VAL A 381      14.642  -1.252   6.012  1.00 81.99           N\\nATOM   2653  CA  VAL A 381      13.758  -1.918   5.057  1.00 83.38           C\\nATOM   2654  C   VAL A 381      13.412  -0.978   3.910  1.00 77.79           C\\nATOM   2655  O   VAL A 381      13.311  -1.397   2.751  1.00 66.26           O\\nATOM   2656  CB  VAL A 381      12.494  -2.434   5.772  1.00 76.89           C\\nATOM   2657  CG1 VAL A 381      11.472  -2.937   4.769  1.00 69.18           C\\nATOM   2658  CG2 VAL A 381      12.858  -3.534   6.752  1.00 75.31           C\\nATOM   2659  N   PHE A 382      13.231   0.308   4.214  1.00 79.75           N\\nATOM   2660  CA  PHE A 382      13.014   1.298   3.166  1.00 68.40           C\\nATOM   2661  C   PHE A 382      14.165   1.294   2.171  1.00 73.80           C\\nATOM   2662  O   PHE A 382      13.953   1.186   0.958  1.00 78.38           O\\nATOM   2663  CB  PHE A 382      12.844   2.679   3.796  1.00 62.89           C\\nATOM   2664  CG  PHE A 382      12.514   3.767   2.815  1.00 69.81           C\\nATOM   2665  CD1 PHE A 382      11.203   4.013   2.452  1.00 78.17           C\\nATOM   2666  CD2 PHE A 382      13.513   4.560   2.276  1.00 67.00           C\\nATOM   2667  CE1 PHE A 382      10.895   5.021   1.557  1.00 75.89           C\\nATOM   2668  CE2 PHE A 382      13.211   5.566   1.380  1.00 62.38           C\\nATOM   2669  CZ  PHE A 382      11.900   5.797   1.021  1.00 65.04           C\\nATOM   2670  N   ILE A 383      15.399   1.395   2.672  1.00 79.94           N\\nATOM   2671  CA  ILE A 383      16.564   1.405   1.792  1.00 76.66           C\\nATOM   2672  C   ILE A 383      16.668   0.093   1.027  1.00 74.25           C\\nATOM   2673  O   ILE A 383      17.053   0.072  -0.148  1.00 81.52           O\\nATOM   2674  CB  ILE A 383      17.840   1.702   2.601  1.00 71.78           C\\nATOM   2675  CG1 ILE A 383      17.851   3.163   3.035  1.00 63.66           C\\nATOM   2676  CG2 ILE A 383      19.084   1.400   1.789  1.00 79.30           C\\nATOM   2677  CD1 ILE A 383      17.701   4.126   1.880  1.00 64.10           C\\nATOM   2678  N   ILE A 384      16.309  -1.019   1.668  1.00 77.47           N\\nANISOU 2678  N   ILE A 384    10269   8636  10532   1676   -785   -446       N\\nATOM   2679  CA  ILE A 384      16.346  -2.312   0.990  1.00 77.09           C\\nANISOU 2679  CA  ILE A 384    10626   8415  10249   1786   -743   -487       C\\nATOM   2680  C   ILE A 384      15.395  -2.323  -0.203  1.00 79.25           C\\nANISOU 2680  C   ILE A 384    11068   8660  10381   1476   -652   -397       C\\nATOM   2681  O   ILE A 384      15.699  -2.905  -1.252  1.00 79.85           O\\nANISOU 2681  O   ILE A 384    11325   8712  10302   1540   -544   -477       O\\nATOM   2682  CB  ILE A 384      16.026  -3.439   1.989  1.00 74.75           C\\nANISOU 2682  CB  ILE A 384    10740   7870   9793   1895   -906   -471       C\\nATOM   2683  CG1 ILE A 384      17.200  -3.648   2.941  1.00 77.41           C\\nANISOU 2683  CG1 ILE A 384    10961   8240  10210   2294  -1026   -570       C\\nATOM   2684  CG2 ILE A 384      15.704  -4.737   1.267  1.00 71.60           C\\nANISOU 2684  CG2 ILE A 384    10844   7191   9169   1898   -891   -497       C\\nATOM   2685  CD1 ILE A 384      18.443  -4.186   2.256  1.00 79.90           C\\nANISOU 2685  CD1 ILE A 384    11224   8571  10564   2673   -951   -738       C\\nATOM   2686  N   CYS A 385      14.245  -1.657  -0.076  1.00 75.66           N\\nANISOU 2686  N   CYS A 385    10540   8236   9971   1156   -704   -252       N\\nATOM   2687  CA  CYS A 385      13.214  -1.744  -1.106  1.00 79.40           C\\nANISOU 2687  CA  CYS A 385    11178   8693  10298    856   -690   -152       C\\nATOM   2688  C   CYS A 385      13.483  -0.807  -2.281  1.00 77.99           C\\nANISOU 2688  C   CYS A 385    10754   8710  10168    769   -575    -84       C\\nATOM   2689  O   CYS A 385      13.199  -1.160  -3.432  1.00 80.47           O\\nANISOU 2689  O   CYS A 385    11270   9043  10261    646   -531    -66       O\\nATOM   2690  CB  CYS A 385      11.842  -1.449  -0.500  1.00 80.67           C\\nANISOU 2690  CB  CYS A 385    11312   8841  10500    576   -801    -23       C\\nATOM   2691  SG  CYS A 385      11.235  -2.722   0.645  1.00 83.19           S\\nANISOU 2691  SG  CYS A 385    12017   8939  10653    532   -901    -25       S\\nATOM   2692  N   TRP A 386      14.018   0.384  -2.024  1.00 68.60           N\\nANISOU 2692  N   TRP A 386     9160   7658   9246    804   -535    -37       N\\nATOM   2693  CA  TRP A 386      14.213   1.350  -3.095  1.00 71.32           C\\nANISOU 2693  CA  TRP A 386     9293   8158   9646    667   -432     98       C\\nATOM   2694  C   TRP A 386      15.618   1.346  -3.677  1.00 73.91           C\\nANISOU 2694  C   TRP A 386     9483   8642   9959    842   -227     12       C\\nATOM   2695  O   TRP A 386      15.812   1.874  -4.776  1.00 77.41           O\\nANISOU 2695  O   TRP A 386     9849   9237  10328    705    -92    139       O\\nATOM   2696  CB  TRP A 386      13.885   2.767  -2.612  1.00 68.85           C\\nANISOU 2696  CB  TRP A 386     8631   7857   9670    543   -510    230       C\\nATOM   2697  CG  TRP A 386      12.415   3.071  -2.565  1.00 72.68           C\\nANISOU 2697  CG  TRP A 386     9161   8279  10174    338   -661    365       C\\nATOM   2698  CD1 TRP A 386      11.648   3.236  -1.448  1.00 67.00           C\\nANISOU 2698  CD1 TRP A 386     8370   7494   9594    332   -777    320       C\\nATOM   2699  CD2 TRP A 386      11.534   3.244  -3.684  1.00 78.89           C\\nANISOU 2699  CD2 TRP A 386    10042   9108  10823    121   -715    558       C\\nATOM   2700  NE1 TRP A 386      10.348   3.502  -1.801  1.00 70.95           N\\nANISOU 2700  NE1 TRP A 386     8865   8000  10093    139   -882    461       N\\nATOM   2701  CE2 TRP A 386      10.251   3.512  -3.168  1.00 76.55           C\\nANISOU 2701  CE2 TRP A 386     9677   8767  10641      9   -876    617       C\\nATOM   2702  CE3 TRP A 386      11.706   3.200  -5.072  1.00 78.88           C\\nANISOU 2702  CE3 TRP A 386    10168   9215  10586     17   -646    682       C\\nATOM   2703  CZ2 TRP A 386       9.146   3.736  -3.988  1.00 75.36           C\\nANISOU 2703  CZ2 TRP A 386     9547   8666  10419   -188  -1008    800       C\\nATOM   2704  CZ3 TRP A 386      10.606   3.421  -5.885  1.00 78.84           C\\nANISOU 2704  CZ3 TRP A 386    10240   9252  10462   -196   -791    875       C\\nATOM   2705  CH2 TRP A 386       9.343   3.684  -5.340  1.00 78.30           C\\nANISOU 2705  CH2 TRP A 386    10069   9128  10555   -289   -989    935       C\\nATOM   2706  N   LEU A 387      16.599   0.779  -2.986  1.00 71.16           N\\nANISOU 2706  N   LEU A 387     9082   8289   9666   1138   -199   -185       N\\nATOM   2707  CA  LEU A 387      17.963   0.908  -3.486  1.00 77.39           C\\nANISOU 2707  CA  LEU A 387     9613   9290  10501   1307     10   -275       C\\nATOM   2708  C   LEU A 387      18.178   0.130  -4.783  1.00 81.59           C\\nANISOU 2708  C   LEU A 387    10394   9919  10687   1358    212   -346       C\\nATOM   2709  O   LEU A 387      18.816   0.661  -5.701  1.00 86.35           O\\nANISOU 2709  O   LEU A 387    10786  10774  11250   1288    442   -288       O\\nATOM   2710  CB  LEU A 387      18.985   0.473  -2.436  1.00 76.08           C\\nANISOU 2710  CB  LEU A 387     9284   9129  10492   1656    -47   -481       C\\nATOM   2711  CG  LEU A 387      20.393   0.933  -2.792  1.00 73.95           C\\nANISOU 2711  CG  LEU A 387     8566   9145  10385   1779    152   -557       C\\nATOM   2712  CD1 LEU A 387      20.380   2.425  -3.067  1.00 70.62           C\\nANISOU 2712  CD1 LEU A 387     7792   8838  10202   1432    210   -352       C\\nATOM   2713  CD2 LEU A 387      21.363   0.599  -1.677  1.00 74.27           C\\nANISOU 2713  CD2 LEU A 387     8384   9220  10617   2125     25   -752       C\\nATOM   2714  N   PRO A 388      17.692  -1.112  -4.913  1.00 79.42           N\\nANISOU 2714  N   PRO A 388    10576   9454  10144   1463    148   -479       N\\nATOM   2715  CA  PRO A 388      17.785  -1.780  -6.223  1.00 83.37           C\\nANISOU 2715  CA  PRO A 388    11355  10040  10283   1481    328   -585       C\\nATOM   2716  C   PRO A 388      17.190  -0.967  -7.356  1.00 88.60           C\\nANISOU 2716  C   PRO A 388    12005  10889  10771   1117    400   -357       C\\nATOM   2717  O   PRO A 388      17.670  -1.054  -8.493  1.00 89.35           O\\nANISOU 2717  O   PRO A 388    12143  11216  10591   1123    637   -407       O\\nATOM   2718  CB  PRO A 388      17.015  -3.085  -5.998  1.00 78.09           C\\nANISOU 2718  CB  PRO A 388    11219   9031   9418   1534    148   -722       C\\nATOM   2719  CG  PRO A 388      17.214  -3.371  -4.563  1.00 73.10           C\\nANISOU 2719  CG  PRO A 388    10537   8200   9037   1742    -22   -758       C\\nATOM   2720  CD  PRO A 388      17.196  -2.039  -3.878  1.00 74.29           C\\nANISOU 2720  CD  PRO A 388    10229   8503   9495   1588    -73   -564       C\\nATOM   2721  N   PHE A 389      16.157  -0.168  -7.077  1.00 87.86           N\\nANISOU 2721  N   PHE A 389    11851  10717  10815    821    202   -105       N\\nATOM   2722  CA  PHE A 389      15.588   0.699  -8.103  1.00 88.83           C\\nANISOU 2722  CA  PHE A 389    11946  10997  10808    504    215    164       C\\nATOM   2723  C   PHE A 389      16.581   1.776  -8.524  1.00 87.11           C\\nANISOU 2723  C   PHE A 389    11342  11030  10726    460    445    317       C\\nATOM   2724  O   PHE A 389      16.791   2.009  -9.719  1.00 91.58           O\\nANISOU 2724  O   PHE A 389    11960  11831  11005    327    627    435       O\\nATOM   2725  CB  PHE A 389      14.287   1.323  -7.592  1.00 81.78           C\\nANISOU 2725  CB  PHE A 389    11019   9946  10106    271    -69    378       C\\nATOM   2726  CG  PHE A 389      13.670   2.319  -8.536  1.00 78.75           C\\nANISOU 2726  CG  PHE A 389    10580   9686   9656    -11   -125    698       C\\nATOM   2727  CD1 PHE A 389      12.947   1.897  -9.638  1.00 72.20           C\\nANISOU 2727  CD1 PHE A 389    10065   8946   8421   -182   -197    758       C\\nATOM   2728  CD2 PHE A 389      13.795   3.677  -8.309  1.00 74.32           C\\nANISOU 2728  CD2 PHE A 389     9675   9124   9438   -104   -142    940       C\\nATOM   2729  CE1 PHE A 389      12.374   2.812 -10.501  1.00 66.21           C\\nANISOU 2729  CE1 PHE A 389     9270   8308   7580   -418   -296   1089       C\\nATOM   2730  CE2 PHE A 389      13.221   4.593  -9.169  1.00 73.66           C\\nANISOU 2730  CE2 PHE A 389     9576   9102   9309   -336   -229   1275       C\\nATOM   2731  CZ  PHE A 389      12.508   4.160 -10.263  1.00 67.96           C\\nANISOU 2731  CZ  PHE A 389     9160   8501   8161   -483   -313   1367       C\\nATOM   2732  N   PHE A 390      17.211   2.438  -7.553  1.00 78.28           N\\nANISOU 2732  N   PHE A 390     9842   9876  10022    542    440    319       N\\nATOM   2733  CA  PHE A 390      18.154   3.503  -7.865  1.00 77.80           C\\nANISOU 2733  CA  PHE A 390     9387  10020  10154    435    640    473       C\\nATOM   2734  C   PHE A 390      19.520   2.977  -8.285  1.00 85.50           C\\nANISOU 2734  C   PHE A 390    10201  11281  11003    650    968    266       C\\nATOM   2735  O   PHE A 390      20.266   3.699  -8.955  1.00 80.65           O\\nANISOU 2735  O   PHE A 390     9313  10928  10401    495   1220    418       O\\nATOM   2736  CB  PHE A 390      18.290   4.441  -6.666  1.00 72.78           C\\nANISOU 2736  CB  PHE A 390     8403   9227  10023    409    479    515       C\\nATOM   2737  CG  PHE A 390      17.046   5.229  -6.384  1.00 71.97           C\\nANISOU 2737  CG  PHE A 390     8367   8891  10086    201    217    731       C\\nATOM   2738  CD1 PHE A 390      16.770   6.384  -7.095  1.00 73.92           C\\nANISOU 2738  CD1 PHE A 390     8531   9132  10422    -77    215   1066       C\\nATOM   2739  CD2 PHE A 390      16.146   4.810  -5.423  1.00 69.40           C\\nANISOU 2739  CD2 PHE A 390     8185   8358   9824    295    -21    611       C\\nATOM   2740  CE1 PHE A 390      15.624   7.110  -6.848  1.00 69.85           C\\nANISOU 2740  CE1 PHE A 390     8056   8392  10093   -202    -42   1247       C\\nATOM   2741  CE2 PHE A 390      14.995   5.533  -5.171  1.00 69.17           C\\nANISOU 2741  CE2 PHE A 390     8161   8162   9960    142   -234    777       C\\nATOM   2742  CZ  PHE A 390      14.735   6.685  -5.884  1.00 63.89           C\\nANISOU 2742  CZ  PHE A 390     7389   7471   9415    -78   -256   1080       C\\nATOM   2743  N   ILE A 391      19.865   1.744  -7.905  1.00 83.05           N\\nANISOU 2743  N   ILE A 391    10043  10926  10586   1005    976    -67       N\\nATOM   2744  CA  ILE A 391      21.044   1.100  -8.477  1.00 88.93           C\\nANISOU 2744  CA  ILE A 391    10677  11954  11158   1273   1299   -305       C\\nATOM   2745  C   ILE A 391      20.854   0.907  -9.975  1.00 91.28           C\\nANISOU 2745  C   ILE A 391    11243  12480  10960   1127   1541   -254       C\\nATOM   2746  O   ILE A 391      21.789   1.084 -10.766  1.00 94.74           O\\nANISOU 2746  O   ILE A 391    11451  13294  11253   1139   1904   -276       O\\nATOM   2747  CB  ILE A 391      21.321  -0.238  -7.761  1.00 85.00           C\\nANISOU 2747  CB  ILE A 391    10370  11271  10655   1728   1197   -664       C\\nATOM   2748  CG1 ILE A 391      21.803   0.004  -6.329  1.00 81.99           C\\nANISOU 2748  CG1 ILE A 391     9657  10782  10715   1901    995   -715       C\\nATOM   2749  CG2 ILE A 391      22.336  -1.068  -8.534  1.00 85.18           C\\nANISOU 2749  CG2 ILE A 391    10376  11551  10438   2063   1525   -960       C\\nATOM   2750  CD1 ILE A 391      22.006  -1.268  -5.531  1.00 79.71           C\\nANISOU 2750  CD1 ILE A 391     9598  10266  10423   2344    833   -991       C\\nATOM   2751  N   THR A 392      19.633   0.564 -10.388  1.00 91.03           N\\nANISOU 2751  N   THR A 392    11682  12262  10642    965   1345   -183       N\\nATOM   2752  CA  THR A 392      19.347   0.341 -11.801  1.00 92.03           C\\nANISOU 2752  CA  THR A 392    12124  12607  10236    813   1511   -151       C\\nATOM   2753  C   THR A 392      19.510   1.622 -12.611  1.00 96.64           C\\nANISOU 2753  C   THR A 392    12473  13487  10758    456   1684    247       C\\nATOM   2754  O   THR A 392      19.972   1.585 -13.759  1.00 99.51           O\\nANISOU 2754  O   THR A 392    12896  14212  10701    394   2002    256       O\\nATOM   2755  CB  THR A 392      17.934  -0.222 -11.949  1.00 85.65           C\\nANISOU 2755  CB  THR A 392    11821  11527   9195    670   1183   -144       C\\nATOM   2756  OG1 THR A 392      17.843  -1.462 -11.238  1.00 86.36           O\\nANISOU 2756  OG1 THR A 392    12169  11313   9330    965   1047   -489       O\\nATOM   2757  CG2 THR A 392      17.589  -0.458 -13.404  1.00 82.50           C\\nANISOU 2757  CG2 THR A 392    11776  11367   8203    498   1292   -131       C\\nATOM   2758  N   HIS A 393      19.187   2.742 -12.031  1.00 88.71           N\\nANISOU 2758  N   HIS A 393    11226  12324  10155    219   1485    579       N\\nATOM   2759  CA  HIS A 393      19.363   3.957 -12.738  1.00 88.98           C\\nANISOU 2759  CA  HIS A 393    11056  12550  10202   -130   1618   1001       C\\nATOM   2760  C   HIS A 393      20.809   4.181 -13.033  1.00 88.31           C\\nANISOU 2760  C   HIS A 393    10554  12829  10172   -105   2051    965       C\\nATOM   2761  O   HIS A 393      21.145   4.651 -14.071  1.00 90.40           O\\nANISOU 2761  O   HIS A 393    10759  13392  10197   -381   2313   1255       O\\nATOM   2762  CB  HIS A 393      18.863   5.074 -11.893  1.00 92.81           C\\nANISOU 2762  CB  HIS A 393    11357  12712  11192   -324   1304   1294       C\\nATOM   2763  CG  HIS A 393      17.412   5.334 -12.064  1.00 96.38           C\\nANISOU 2763  CG  HIS A 393    12141  12922  11557   -443    932   1454       C\\nATOM   2764  ND1 HIS A 393      16.815   5.355 -13.296  1.00101.35           N\\nANISOU 2764  ND1 HIS A 393    12985  13642  11882   -712    860   1815       N\\nATOM   2765  CD2 HIS A 393      16.440   5.591 -11.168  1.00 93.09           C\\nANISOU 2765  CD2 HIS A 393    11851  12212  11307   -333    611   1312       C\\nATOM   2766  CE1 HIS A 393      15.536   5.622 -13.155  1.00 98.51           C\\nANISOU 2766  CE1 HIS A 393    12830  13059  11540   -744    489   1868       C\\nATOM   2767  NE2 HIS A 393      15.282   5.762 -11.872  1.00 93.35           N\\nANISOU 2767  NE2 HIS A 393    12117  12180  11171   -533    357   1563       N\\nATOM   2768  N   ILE A 394      21.675   3.869 -12.094  1.00 95.53           N\\nANISOU 2768  N   ILE A 394    11157  13746  11395    209   2124    635       N\\nATOM   2769  CA  ILE A 394      23.103   4.065 -12.304  1.00100.46           C\\nANISOU 2769  CA  ILE A 394    11300  14765  12104    258   2532    556       C\\nATOM   2770  C   ILE A 394      23.590   3.234 -13.480  1.00110.00           C\\nANISOU 2770  C   ILE A 394    12669  16389  12736    410   2939    349       C\\nATOM   2771  O   ILE A 394      24.530   3.628 -14.181  1.00116.65           O\\nANISOU 2771  O   ILE A 394    13187  17679  13455    283   3367    434       O\\nATOM   2772  CB  ILE A 394      23.876   3.735 -11.014  1.00 95.87           C\\nANISOU 2772  CB  ILE A 394    10335  14092  12001    599   2436    239       C\\nATOM   2773  N   LEU A 395      22.959   2.084 -13.726  1.00109.05           N\\nANISOU 2773  N   LEU A 395    13051  16136  12246    661   2828     65       N\\nATOM   2774  CA  LEU A 395      23.384   1.213 -14.816  1.00115.80           C\\nANISOU 2774  CA  LEU A 395    14119  17349  12533    853   3195   -221       C\\nATOM   2775  C   LEU A 395      22.911   1.731 -16.169  1.00123.98           C\\nANISOU 2775  C   LEU A 395    15434  18666  13007    451   3352    106       C\\nATOM   2776  O   LEU A 395      23.622   1.591 -17.170  1.00132.70           O\\nANISOU 2776  O   LEU A 395    16488  20259  13673    459   3812     22       O\\nATOM   2777  CB  LEU A 395      22.873  -0.208 -14.578  1.00113.04           C\\nANISOU 2777  CB  LEU A 395    14254  16684  12011   1243   2983   -662       C\\nATOM   2778  CG  LEU A 395      23.285  -0.827 -13.242  1.00107.58           C\\nANISOU 2778  CG  LEU A 395    13379  15684  11813   1666   2788   -952       C\\nATOM   2779  CD1 LEU A 395      22.874  -2.287 -13.174  1.00109.94           C\\nANISOU 2779  CD1 LEU A 395    14213  15663  11896   2035   2631  -1369       C\\nATOM   2780  CD2 LEU A 395      24.782  -0.681 -13.009  1.00102.89           C\\nANISOU 2780  CD2 LEU A 395    12151  15454  11490   1927   3132  -1110       C\\nATOM   2781  N   ASN A 396      21.713   2.324 -16.219  1.00120.69           N\\nANISOU 2781  N   ASN A 396    15306  17974  12576    116   2975    478       N\\nATOM   2782  CA  ASN A 396      21.242   2.943 -17.454  1.00120.58           C\\nANISOU 2782  CA  ASN A 396    15547  18214  12053   -278   3052    871       C\\nATOM   2783  C   ASN A 396      22.194   4.031 -17.930  1.00122.42           C\\nANISOU 2783  C   ASN A 396    15355  18837  12322   -573   3455   1241       C\\nATOM   2784  O   ASN A 396      22.387   4.205 -19.139  1.00125.81           O\\nANISOU 2784  O   ASN A 396    15933  19697  12171   -784   3770   1420       O\\nATOM   2785  CB  ASN A 396      19.841   3.523 -17.251  1.00116.75           C\\nANISOU 2785  CB  ASN A 396    15328  17340  11693   -546   2527   1239       C\\nATOM   2786  CG  ASN A 396      18.760   2.676 -17.888  1.00117.94           C\\nANISOU 2786  CG  ASN A 396    16062  17433  11316   -534   2274   1087       C\\nATOM   2787  OD1 ASN A 396      18.987   1.516 -18.228  1.00121.59           O\\nANISOU 2787  OD1 ASN A 396    16780  18007  11413   -276   2424    626       O\\nATOM   2788  ND2 ASN A 396      17.576   3.253 -18.057  1.00116.24           N\\nANISOU 2788  ND2 ASN A 396    16052  17032  11079   -807   1870   1457       N\\nATOM   2789  N   ILE A 397      22.806   4.760 -16.997  1.00128.30           N\\nANISOU 2789  N   ILE A 397    15581  19448  13721   -619   3450   1356       N\\nATOM   2790  CA  ILE A 397      23.706   5.849 -17.357  1.00131.63           C\\nANISOU 2790  CA  ILE A 397    15568  20182  14265   -972   3805   1730       C\\nATOM   2791  C   ILE A 397      25.103   5.322 -17.667  1.00137.13           C\\nANISOU 2791  C   ILE A 397    15858  21427  14818   -764   4380   1392       C\\nATOM   2792  O   ILE A 397      25.789   5.839 -18.556  1.00140.52           O\\nANISOU 2792  O   ILE A 397    16093  22338  14959  -1056   4838   1642       O\\nATOM   2793  CB  ILE A 397      23.731   6.896 -16.228  1.00123.72           C\\nANISOU 2793  CB  ILE A 397    14191  18774  14042  -1149   3517   1971       C\\nATOM   2794  CG1 ILE A 397      22.331   7.473 -16.007  1.00113.56           C\\nANISOU 2794  CG1 ILE A 397    13280  16985  12883  -1327   2987   2301       C\\nATOM   2795  CG2 ILE A 397      24.735   8.002 -16.530  1.00125.40           C\\nANISOU 2795  CG2 ILE A 397    13930  19262  14453  -1557   3873   2337       C\\nATOM   2796  CD1 ILE A 397      22.251   8.459 -14.860  1.00102.21           C\\nANISOU 2796  CD1 ILE A 397    11537  15104  12195  -1449   2680   2462       C\\nATOM   2797  N   HIS A 398      25.537   4.278 -16.959  1.00136.75           N\\nANISOU 2797  N   HIS A 398    15674  21329  14958   -248   4372    832       N\\nATOM   2798  CA  HIS A 398      26.930   3.846 -17.033  1.00140.25           C\\nANISOU 2798  CA  HIS A 398    15599  22260  15431     23   4867    485       C\\nATOM   2799  C   HIS A 398      27.250   3.199 -18.376  1.00154.68           C\\nANISOU 2799  C   HIS A 398    17644  24638  16490    117   5371    293       C\\nATOM   2800  O   HIS A 398      28.121   3.674 -19.114  1.00162.37           O\\nANISOU 2800  O   HIS A 398    18256  26184  17254   -111   5901    448       O\\nATOM   2801  CB  HIS A 398      27.240   2.881 -15.886  1.00132.50           C\\nANISOU 2801  CB  HIS A 398    14462  21019  14861    602   4649    -39       C\\nATOM   2802  N   CYS A 399      26.570   2.103 -18.707  1.00157.99           N\\nANISOU 2802  N   CYS A 399    18652  24908  16468    436   5229    -65       N\\nATOM   2803  CA  CYS A 399      26.929   1.309 -19.875  1.00171.19           C\\nANISOU 2803  CA  CYS A 399    20554  27077  17414    635   5693   -403       C\\nATOM   2804  C   CYS A 399      25.915   1.388 -21.006  1.00172.38           C\\nANISOU 2804  C   CYS A 399    21379  27292  16826    306   5614   -163       C\\nATOM   2805  O   CYS A 399      26.152   0.799 -22.069  1.00171.94           O\\nANISOU 2805  O   CYS A 399    21574  27683  16070    417   5999   -433       O\\nATOM   2806  CB  CYS A 399      27.145  -0.157 -19.472  1.00177.68           C\\nANISOU 2806  CB  CYS A 399    21527  27720  18264   1324   5648  -1118       C\\nATOM   2807  SG  CYS A 399      25.689  -1.129 -18.956  1.00177.65           S\\nANISOU 2807  SG  CYS A 399    22318  26935  18245   1520   4957  -1341       S\\nATOM   2808  N   ASP A 400      24.802   2.093 -20.815  1.00169.42           N\\nANISOU 2808  N   ASP A 400    21292  26506  16572    -73   5118    313       N\\nATOM   2809  CA  ASP A 400      23.708   2.176 -21.779  1.00172.19           C\\nANISOU 2809  CA  ASP A 400    22278  26866  16282   -369   4909    565       C\\nATOM   2810  C   ASP A 400      23.130   0.810 -22.126  1.00178.49           C\\nANISOU 2810  C   ASP A 400    23661  27552  16606    -24   4760      1       C\\nATOM   2811  O   ASP A 400      22.354   0.694 -23.084  1.00180.90           O\\nANISOU 2811  O   ASP A 400    24500  27979  16254   -230   4642     91       O\\nATOM   2812  CB  ASP A 400      24.139   2.903 -23.061  1.00174.58           C\\nANISOU 2812  CB  ASP A 400    22570  27804  15958   -772   5382    965       C\\nATOM   2813  N   CYS A 401      23.494  -0.229 -21.377  1.00180.63           N\\nANISOU 2813  N   CYS A 401    23862  27575  17194    489   4738   -576       N\\nATOM   2814  CA  CYS A 401      22.923  -1.551 -21.583  1.00179.00           C\\nANISOU 2814  CA  CYS A 401    24242  27130  16641    806   4543  -1120       C\\nATOM   2815  C   CYS A 401      21.440  -1.519 -21.252  1.00170.63           C\\nANISOU 2815  C   CYS A 401    23622  25538  15671    556   3881   -897       C\\nATOM   2816  O   CYS A 401      21.063  -1.243 -20.109  1.00166.40           O\\nANISOU 2816  O   CYS A 401    22893  24541  15789    548   3513   -729       O\\nATOM   2817  CB  CYS A 401      23.624  -2.583 -20.701  1.00179.14           C\\nANISOU 2817  CB  CYS A 401    24079  26891  17096   1410   4598  -1700       C\\nATOM   2818  SG  CYS A 401      25.421  -2.457 -20.478  1.00183.37           S\\nANISOU 2818  SG  CYS A 401    23801  27930  17940   1774   5237  -1908       S\\nATOM   2819  N   ASN A 402      20.597  -1.793 -22.244  1.00163.09           N\\nANISOU 2819  N   ASN A 402    23235  24683  14049    348   3727   -908       N\\nATOM   2820  CA  ASN A 402      19.171  -1.877 -21.964  1.00152.09           C\\nANISOU 2820  CA  ASN A 402    22222  22828  12736    126   3092   -755       C\\nATOM   2821  C   ASN A 402      18.914  -3.031 -21.004  1.00144.87           C\\nANISOU 2821  C   ASN A 402    21476  21352  12215    479   2819  -1242       C\\nATOM   2822  O   ASN A 402      19.334  -4.167 -21.242  1.00148.09           O\\nANISOU 2822  O   ASN A 402    22151  21737  12380    836   2997  -1823       O\\nATOM   2823  CB  ASN A 402      18.364  -2.039 -23.255  1.00153.00           C\\nANISOU 2823  CB  ASN A 402    22907  23202  12025   -153   2955   -727       C\\nATOM   2824  CG  ASN A 402      18.644  -3.344 -23.970  1.00154.48           C\\nANISOU 2824  CG  ASN A 402    23550  23525  11619    142   3169  -1424       C\\nATOM   2825  OD1 ASN A 402      18.048  -4.376 -23.657  1.00152.23           O\\nANISOU 2825  OD1 ASN A 402    23645  22801  11394    294   2842  -1846       O\\nATOM   2826  ND2 ASN A 402      19.540  -3.303 -24.949  1.00156.47           N\\nANISOU 2826  ND2 ASN A 402    23784  24383  11285    209   3730  -1554       N\\nATOM   2827  N   ILE A 403      18.259  -2.719 -19.893  1.00137.95           N\\nANISOU 2827  N   ILE A 403    20445  20015  11956    389   2403   -999       N\\nATOM   2828  CA  ILE A 403      18.056  -3.664 -18.801  1.00126.08           C\\nANISOU 2828  CA  ILE A 403    19041  17968  10897    679   2150  -1342       C\\nATOM   2829  C   ILE A 403      16.725  -4.370 -19.025  1.00123.67           C\\nANISOU 2829  C   ILE A 403    19300  17348  10341    476   1691  -1463       C\\nATOM   2830  O   ILE A 403      15.774  -3.737 -19.506  1.00123.23           O\\nANISOU 2830  O   ILE A 403    19345  17396  10082     73   1419  -1099       O\\nATOM   2831  CB  ILE A 403      18.121  -2.936 -17.448  1.00116.57           C\\nANISOU 2831  CB  ILE A 403    17344  16498  10450    680   1990  -1029       C\\nATOM   2832  CG1 ILE A 403      19.571  -2.545 -17.154  1.00117.76           C\\nANISOU 2832  CG1 ILE A 403    16950  16923  10871    944   2430  -1064       C\\nATOM   2833  CG2 ILE A 403      17.524  -3.771 -16.324  1.00111.83           C\\nANISOU 2833  CG2 ILE A 403    16927  15326  10238    834   1619  -1235       C\\nATOM   2834  CD1 ILE A 403      19.744  -1.682 -15.938  1.00115.05           C\\nANISOU 2834  CD1 ILE A 403    16103  16396  11214    903   2293   -760       C\\nATOM   2835  N   PRO A 404      16.628  -5.671 -18.745  1.00118.90           N\\nANISOU 2835  N   PRO A 404    19074  16363   9738    731   1581  -1960       N\\nATOM   2836  CA  PRO A 404      15.360  -6.387 -18.918  1.00118.90           C\\nANISOU 2836  CA  PRO A 404    19598  16036   9542    479   1130  -2089       C\\nATOM   2837  C   PRO A 404      14.199  -5.600 -18.342  1.00114.46           C\\nANISOU 2837  C   PRO A 404    18849  15327   9312     80    700  -1589       C\\nATOM   2838  O   PRO A 404      14.149  -5.345 -17.130  1.00111.06           O\\nANISOU 2838  O   PRO A 404    18106  14611   9479    144    589  -1414       O\\nATOM   2839  CB  PRO A 404      15.590  -7.690 -18.142  1.00118.42           C\\nANISOU 2839  CB  PRO A 404    19799  15435   9759    841   1069  -2563       C\\nATOM   2840  CG  PRO A 404      17.050  -7.938 -18.305  1.00121.83           C\\nANISOU 2840  CG  PRO A 404    20054  16085  10152   1347   1569  -2883       C\\nATOM   2841  CD  PRO A 404      17.718  -6.580 -18.344  1.00119.79           C\\nANISOU 2841  CD  PRO A 404    19169  16331  10014   1271   1867  -2444       C\\nATOM   2842  N   PRO A 405      13.257  -5.175 -19.187  1.00111.48           N\\nANISOU 2842  N   PRO A 405    18639  15168   8549   -316    448  -1354       N\\nATOM   2843  CA  PRO A 405      12.126  -4.381 -18.686  1.00109.02           C\\nANISOU 2843  CA  PRO A 405    18100  14751   8571   -653     36   -886       C\\nATOM   2844  C   PRO A 405      11.320  -5.093 -17.621  1.00107.40           C\\nANISOU 2844  C   PRO A 405    17974  14039   8792   -700   -301  -1012       C\\nATOM   2845  O   PRO A 405      10.656  -4.425 -16.820  1.00106.74           O\\nANISOU 2845  O   PRO A 405    17562  13840   9155   -851   -528   -666       O\\nATOM   2846  CB  PRO A 405      11.292  -4.119 -19.948  1.00110.35           C\\nANISOU 2846  CB  PRO A 405    18539  15248   8141  -1009   -207   -731       C\\nATOM   2847  CG  PRO A 405      11.691  -5.197 -20.899  1.00113.76           C\\nANISOU 2847  CG  PRO A 405    19491  15789   7942   -900    -38  -1264       C\\nATOM   2848  CD  PRO A 405      13.141  -5.456 -20.627  1.00117.16           C\\nANISOU 2848  CD  PRO A 405    19780  16246   8490   -452    496  -1536       C\\nATOM   2849  N   VAL A 406      11.356  -6.428 -17.580  1.00111.87           N\\nANISOU 2849  N   VAL A 406    18978  14290   9236   -579   -329  -1496       N\\nATOM   2850  CA  VAL A 406      10.738  -7.139 -16.469  1.00102.56           C\\nANISOU 2850  CA  VAL A 406    17881  12600   8486   -624   -592  -1581       C\\nATOM   2851  C   VAL A 406      11.508  -6.882 -15.181  1.00104.10           C\\nANISOU 2851  C   VAL A 406    17697  12610   9246   -300   -398  -1479       C\\nATOM   2852  O   VAL A 406      10.926  -6.894 -14.090  1.00102.17           O\\nANISOU 2852  O   VAL A 406    17313  12081   9424   -395   -602  -1324       O\\nATOM   2853  CB  VAL A 406      10.640  -8.644 -16.776  1.00 94.49           C\\nANISOU 2853  CB  VAL A 406    17480  11217   7203   -584   -680  -2114       C\\nATOM   2854  N   LEU A 407      12.818  -6.639 -15.277  1.00103.82           N\\nANISOU 2854  N   LEU A 407    17468  12769   9209     74     -3  -1567       N\\nATOM   2855  CA  LEU A 407      13.592  -6.296 -14.089  1.00100.38           C\\nANISOU 2855  CA  LEU A 407    16623  12220   9296    369    146  -1462       C\\nATOM   2856  C   LEU A 407      13.390  -4.838 -13.698  1.00 94.26           C\\nANISOU 2856  C   LEU A 407    15315  11675   8824    182    114   -975       C\\nATOM   2857  O   LEU A 407      13.200  -4.533 -12.516  1.00 88.29           O\\nANISOU 2857  O   LEU A 407    14299  10718   8529    200     -8   -812       O\\nATOM   2858  CB  LEU A 407      15.077  -6.584 -14.317  1.00101.90           C\\nANISOU 2858  CB  LEU A 407    16737  12562   9418    837    561  -1755       C\\nATOM   2859  N   TYR A 408      13.370  -3.956 -14.650  1.00 94.06           N\\nANISOU 2859  N   TYR A 408    15152  12055   8531      5    218   -738       N\\nATOM   2860  CA  TYR A 408      13.143  -2.599 -14.299  1.00 92.67           C\\nANISOU 2860  CA  TYR A 408    14536  12021   8655   -189    141   -264       C\\nATOM   2861  C   TYR A 408      11.764  -2.493 -13.713  1.00 95.64           C\\nANISOU 2861  C   TYR A 408    14901  12179   9258   -462   -278    -65       C\\nATOM   2862  O   TYR A 408      11.578  -1.795 -12.766  1.00 92.85           O\\nANISOU 2862  O   TYR A 408    14175  11751   9352   -489   -366    194       O\\nATOM   2863  CB  TYR A 408      13.263  -1.746 -15.521  1.00 92.66           C\\nANISOU 2863  CB  TYR A 408    14496  12449   8263   -369    283     -7       C\\nATOM   2864  CG  TYR A 408      13.909  -0.444 -15.274  1.00 92.93           C\\nANISOU 2864  CG  TYR A 408    14043  12651   8617   -377    472    359       C\\nATOM   2865  CD1 TYR A 408      13.694   0.227 -14.129  1.00 88.51           C\\nANISOU 2865  CD1 TYR A 408    13122  11858   8651   -379    316    564       C\\nATOM   2866  CD2 TYR A 408      14.725   0.122 -16.199  1.00 98.66           C\\nANISOU 2866  CD2 TYR A 408    14681  13767   9040   -406    819    487       C\\nATOM   2867  CE1 TYR A 408      14.287   1.434 -13.904  1.00 87.26           C\\nANISOU 2867  CE1 TYR A 408    12549  11797   8809   -413    462    866       C\\nATOM   2868  CE2 TYR A 408      15.323   1.331 -15.973  1.00 98.99           C\\nANISOU 2868  CE2 TYR A 408    14288  13921   9401   -474    985    837       C\\nATOM   2869  CZ  TYR A 408      15.086   1.974 -14.814  1.00 95.40           C\\nANISOU 2869  CZ  TYR A 408    13502  13174   9570   -479    786   1014       C\\nATOM   2870  OH  TYR A 408      15.640   3.178 -14.533  1.00 98.94           O\\nANISOU 2870  OH  TYR A 408    13550  13681  10361   -572    923   1329       O\\nATOM   2871  N   SER A 409      10.781  -3.173 -14.278  1.00105.38           N\\nANISOU 2871  N   SER A 409    16521  13320  10198   -667   -536   -211       N\\nATOM   2872  CA  SER A 409       9.431  -3.119 -13.727  1.00100.18           C\\nANISOU 2872  CA  SER A 409    15802  12496   9765   -940   -916    -53       C\\nATOM   2873  C   SER A 409       9.363  -3.750 -12.341  1.00 91.59           C\\nANISOU 2873  C   SER A 409    14684  11035   9081   -825   -948   -193       C\\nATOM   2874  O   SER A 409       8.543  -3.336 -11.513  1.00 85.61           O\\nANISOU 2874  O   SER A 409    13671  10195   8661   -967  -1137      4       O\\nATOM   2875  CB  SER A 409       8.447  -3.811 -14.672  1.00102.06           C\\nANISOU 2875  CB  SER A 409    16434  12778   9567  -1245  -1202   -175       C\\nATOM   2876  OG  SER A 409       8.493  -3.239 -15.967  1.00105.65           O\\nANISOU 2876  OG  SER A 409    16956  13611   9576  -1354  -1197    -26       O\\nATOM   2877  N   ALA A 410      10.216  -4.740 -12.069  1.00 90.76           N\\nANISOU 2877  N   ALA A 410    14837  10715   8935   -552   -765   -524       N\\nATOM   2878  CA  ALA A 410      10.196  -5.405 -10.769  1.00 84.55           C\\nANISOU 2878  CA  ALA A 410    14089   9558   8478   -436   -813   -622       C\\nATOM   2879  C   ALA A 410      10.716  -4.488  -9.669  1.00 85.46           C\\nANISOU 2879  C   ALA A 410    13726   9716   9028   -244   -702   -420       C\\nATOM   2880  O   ALA A 410      10.097  -4.365  -8.607  1.00 76.26           O\\nANISOU 2880  O   ALA A 410    12411   8410   8155   -337   -841   -294       O\\nATOM   2881  CB  ALA A 410      11.018  -6.693 -10.829  1.00 79.54           C\\nANISOU 2881  CB  ALA A 410    13883   8649   7690   -141   -680  -1016       C\\nATOM   2882  N   PHE A 411      11.858  -3.837  -9.904  1.00 82.88           N\\nANISOU 2882  N   PHE A 411    13149   9606   8736      5   -442   -403       N\\nATOM   2883  CA  PHE A 411      12.446  -2.977  -8.883  1.00 81.51           C\\nANISOU 2883  CA  PHE A 411    12529   9464   8975    175   -355   -259       C\\nATOM   2884  C   PHE A 411      11.593  -1.745  -8.614  1.00 76.95           C\\nANISOU 2884  C   PHE A 411    11608   8991   8637    -75   -511     73       C\\nATOM   2885  O   PHE A 411      11.658  -1.179  -7.516  1.00 76.38           O\\nANISOU 2885  O   PHE A 411    11240   8854   8929      0   -536    155       O\\nATOM   2886  CB  PHE A 411      13.859  -2.567  -9.293  1.00 88.89           C\\nANISOU 2886  CB  PHE A 411    13244  10633   9898    438    -44   -321       C\\nATOM   2887  CG  PHE A 411      14.856  -3.688  -9.233  1.00 94.35           C\\nANISOU 2887  CG  PHE A 411    14147  11212  10488    811    121   -674       C\\nATOM   2888  CD1 PHE A 411      14.562  -4.860  -8.555  1.00 93.62           C\\nANISOU 2888  CD1 PHE A 411    14407  10746  10418    926    -36   -865       C\\nATOM   2889  CD2 PHE A 411      16.092  -3.568  -9.846  1.00 94.90           C\\nANISOU 2889  CD2 PHE A 411    14052  11548  10457   1055    438   -805       C\\nATOM   2890  CE1 PHE A 411      15.480  -5.891  -8.497  1.00 91.66           C\\nANISOU 2890  CE1 PHE A 411    14375  10339  10112   1324     82  -1184       C\\nATOM   2891  CE2 PHE A 411      17.013  -4.595  -9.790  1.00 91.21           C\\nANISOU 2891  CE2 PHE A 411    13738  10988   9931   1464    585  -1156       C\\nATOM   2892  CZ  PHE A 411      16.707  -5.757  -9.115  1.00 90.35           C\\nANISOU 2892  CZ  PHE A 411    14011  10453   9865   1623    389  -1349       C\\nATOM   2893  N   THR A 412      10.799  -1.310  -9.596  1.00 86.37           N\\nANISOU 2893  N   THR A 412    12841  10347   9628   -346   -634    251       N\\nATOM   2894  CA  THR A 412       9.854  -0.225  -9.353  1.00 83.78           C\\nANISOU 2894  CA  THR A 412    12208  10075   9551   -541   -831    553       C\\nATOM   2895  C   THR A 412       8.712  -0.693  -8.459  1.00 78.58           C\\nANISOU 2895  C   THR A 412    11565   9242   9050   -678  -1053    522       C\\nATOM   2896  O   THR A 412       8.335  -0.005  -7.503  1.00 75.36           O\\nANISOU 2896  O   THR A 412    10841   8797   8997   -662  -1111    634       O\\nATOM   2897  CB  THR A 412       9.310   0.315 -10.677  1.00 83.99           C\\nANISOU 2897  CB  THR A 412    12287  10328   9297   -765   -948    775       C\\nATOM   2898  OG1 THR A 412      10.397   0.624 -11.557  1.00 88.79           O\\nANISOU 2898  OG1 THR A 412    12926  11134   9675   -676   -690    805       O\\nATOM   2899  CG2 THR A 412       8.491   1.578 -10.436  1.00 76.49           C\\nANISOU 2899  CG2 THR A 412    10981   9411   8671   -879  -1149   1106       C\\nATOM   2900  N   TRP A 413       8.148  -1.866  -8.758  1.00 79.97           N\\nANISOU 2900  N   TRP A 413    12110   9314   8961   -831  -1168    357       N\\nATOM   2901  CA  TRP A 413       7.078  -2.406  -7.927  1.00 79.43           C\\nANISOU 2901  CA  TRP A 413    12060   9094   9024  -1024  -1347    342       C\\nATOM   2902  C   TRP A 413       7.576  -2.703  -6.520  1.00 73.46           C\\nANISOU 2902  C   TRP A 413    11258   8138   8517   -819  -1224    254       C\\nATOM   2903  O   TRP A 413       6.853  -2.491  -5.539  1.00 70.81           O\\nANISOU 2903  O   TRP A 413    10714   7782   8407   -915  -1295    340       O\\nATOM   2904  CB  TRP A 413       6.498  -3.667  -8.569  1.00 85.80           C\\nANISOU 2904  CB  TRP A 413    13317   9783   9501  -1268  -1494    166       C\\nATOM   2905  CG  TRP A 413       5.728  -3.398  -9.828  1.00 91.51           C\\nANISOU 2905  CG  TRP A 413    14070  10739   9962  -1534  -1703    261       C\\nATOM   2906  CD1 TRP A 413       5.242  -2.195 -10.250  1.00 85.59           C\\nANISOU 2906  CD1 TRP A 413    12966  10256   9299  -1598  -1823    542       C\\nATOM   2907  CD2 TRP A 413       5.358  -4.354 -10.833  1.00 96.72           C\\nANISOU 2907  CD2 TRP A 413    15160  11373  10216  -1760  -1855     72       C\\nATOM   2908  NE1 TRP A 413       4.589  -2.343 -11.449  1.00 88.41           N\\nANISOU 2908  NE1 TRP A 413    13492  10790   9309  -1846  -2056    571       N\\nATOM   2909  CE2 TRP A 413       4.646  -3.658 -11.829  1.00 95.02           C\\nANISOU 2909  CE2 TRP A 413    14808  11468   9826  -1963  -2077    265       C\\nATOM   2910  CE3 TRP A 413       5.558  -5.731 -10.985  1.00100.43           C\\nANISOU 2910  CE3 TRP A 413    16143  11559  10456  -1802  -1850   -252       C\\nATOM   2911  CZ2 TRP A 413       4.135  -4.290 -12.963  1.00 98.69           C\\nANISOU 2911  CZ2 TRP A 413    15618  12022   9858  -2226  -2299    130       C\\nATOM   2912  CZ3 TRP A 413       5.049  -6.356 -12.111  1.00103.40           C\\nANISOU 2912  CZ3 TRP A 413    16876  11980  10432  -2067  -2053   -417       C\\nATOM   2913  CH2 TRP A 413       4.347  -5.636 -13.085  1.00102.66           C\\nANISOU 2913  CH2 TRP A 413    16621  12251  10133  -2286  -2277   -233       C\\nATOM   2914  N   LEU A 414       8.817  -3.184  -6.402  1.00 75.32           N\\nANISOU 2914  N   LEU A 414    11667   8256   8695   -521  -1041     79       N\\nATOM   2915  CA  LEU A 414       9.384  -3.467  -5.087  1.00 69.21           C\\nANISOU 2915  CA  LEU A 414    10863   7310   8123   -291   -967     10       C\\nATOM   2916  C   LEU A 414       9.434  -2.210  -4.226  1.00 77.59           C\\nANISOU 2916  C   LEU A 414    11447   8517   9516   -215   -939    159       C\\nATOM   2917  O   LEU A 414       9.179  -2.265  -3.016  1.00 79.71           O\\nANISOU 2917  O   LEU A 414    11637   8710   9938   -194   -969    169       O\\nATOM   2918  CB  LEU A 414      10.778  -4.078  -5.238  1.00 67.92           C\\nANISOU 2918  CB  LEU A 414    10893   7049   7867     71   -800   -201       C\\nATOM   2919  CG  LEU A 414      11.552  -4.368  -3.947  1.00 71.97           C\\nANISOU 2919  CG  LEU A 414    11370   7408   8567    375   -760   -268       C\\nATOM   2920  CD1 LEU A 414      10.756  -5.279  -3.035  1.00 56.68           C\\nANISOU 2920  CD1 LEU A 414     9726   5197   6611    226   -906   -242       C\\nATOM   2921  CD2 LEU A 414      12.904  -4.980  -4.260  1.00 76.87           C\\nANISOU 2921  CD2 LEU A 414    12133   7966   9108    768   -617   -490       C\\nATOM   2922  N   GLY A 415       9.747  -1.065  -4.832  1.00 76.07           N\\nANISOU 2922  N   GLY A 415    10960   8524   9421   -187   -885    275       N\\nATOM   2923  CA  GLY A 415       9.745   0.179  -4.081  1.00 72.96           C\\nANISOU 2923  CA  GLY A 415    10144   8207   9369   -132   -886    390       C\\nATOM   2924  C   GLY A 415       8.357   0.581  -3.618  1.00 74.19           C\\nANISOU 2924  C   GLY A 415    10131   8394   9665   -339  -1044    507       C\\nATOM   2925  O   GLY A 415       8.180   1.043  -2.488  1.00 75.00           O\\nANISOU 2925  O   GLY A 415    10010   8487   9999   -269  -1044    489       O\\nATOM   2926  N   TYR A 416       7.355   0.423  -4.485  1.00 71.29           N\\nANISOU 2926  N   TYR A 416     9841   8097   9148   -588  -1184    609       N\\nATOM   2927  CA  TYR A 416       5.978   0.695  -4.089  1.00 65.72           C\\nANISOU 2927  CA  TYR A 416     8925   7466   8580   -782  -1337    704       C\\nATOM   2928  C   TYR A 416       5.494  -0.288  -3.030  1.00 74.23           C\\nANISOU 2928  C   TYR A 416    10136   8452   9617   -880  -1320    595       C\\nATOM   2929  O   TYR A 416       4.629   0.058  -2.215  1.00 72.94           O\\nANISOU 2929  O   TYR A 416     9706   8378   9627   -957  -1345    631       O\\nATOM   2930  CB  TYR A 416       5.065   0.646  -5.312  1.00 62.97           C\\nANISOU 2930  CB  TYR A 416     8626   7243   8059  -1034  -1533    831       C\\nATOM   2931  CG  TYR A 416       5.257   1.800  -6.266  1.00 72.57           C\\nANISOU 2931  CG  TYR A 416     9671   8573   9328   -975  -1592   1030       C\\nATOM   2932  CD1 TYR A 416       5.334   3.107  -5.802  1.00 77.77           C\\nANISOU 2932  CD1 TYR A 416     9966   9229  10353   -816  -1582   1149       C\\nATOM   2933  CD2 TYR A 416       5.362   1.584  -7.633  1.00 70.98           C\\nANISOU 2933  CD2 TYR A 416     9709   8467   8795  -1089  -1663   1103       C\\nATOM   2934  CE1 TYR A 416       5.505   4.166  -6.675  1.00 81.18           C\\nANISOU 2934  CE1 TYR A 416    10288   9707  10852   -788  -1652   1381       C\\nATOM   2935  CE2 TYR A 416       5.537   2.637  -8.513  1.00 78.84           C\\nANISOU 2935  CE2 TYR A 416    10587   9572   9796  -1063  -1716   1345       C\\nATOM   2936  CZ  TYR A 416       5.608   3.925  -8.030  1.00 78.01           C\\nANISOU 2936  CZ  TYR A 416    10131   9419  10091   -919  -1715   1507       C\\nATOM   2937  OH  TYR A 416       5.781   4.974  -8.906  1.00 66.59           O\\nANISOU 2937  OH  TYR A 416     8612   8022   8665   -917  -1783   1795       O\\nATOM   2938  N   VAL A 417       6.036  -1.510  -3.031  1.00 75.00           N\\nANISOU 2938  N   VAL A 417    10650   8367   9481   -873  -1268    468       N\\nATOM   2939  CA  VAL A 417       5.682  -2.503  -2.019  1.00 75.22           C\\nANISOU 2939  CA  VAL A 417    10882   8250   9450   -979  -1253    416       C\\nATOM   2940  C   VAL A 417       6.049  -2.017  -0.621  1.00 75.65           C\\nANISOU 2940  C   VAL A 417    10726   8332   9686   -769  -1144    400       C\\nATOM   2941  O   VAL A 417       5.383  -2.367   0.363  1.00 73.28           O\\nANISOU 2941  O   VAL A 417    10419   8044   9381   -909  -1125    429       O\\nATOM   2942  CB  VAL A 417       6.357  -3.847  -2.359  1.00 69.42           C\\nANISOU 2942  CB  VAL A 417    10679   7234   8461   -938  -1241    282       C\\nATOM   2943  CG1 VAL A 417       6.474  -4.740  -1.133  1.00 66.88           C\\nANISOU 2943  CG1 VAL A 417    10605   6693   8112   -911  -1204    262       C\\nATOM   2944  CG2 VAL A 417       5.575  -4.550  -3.446  1.00 68.97           C\\nANISOU 2944  CG2 VAL A 417    10878   7133   8193  -1268  -1387    262       C\\nATOM   2945  N   ASN A 418       7.086  -1.184  -0.510  1.00 69.14           N\\nANISOU 2945  N   ASN A 418     9719   7544   9007   -464  -1071    354       N\\nATOM   2946  CA  ASN A 418       7.506  -0.674   0.790  1.00 59.69           C\\nANISOU 2946  CA  ASN A 418     8331   6385   7962   -263  -1004    296       C\\nATOM   2947  C   ASN A 418       6.365   0.000   1.544  1.00 72.46           C\\nANISOU 2947  C   ASN A 418     9629   8176   9728   -397  -1007    338       C\\nATOM   2948  O   ASN A 418       6.372   0.033   2.780  1.00 78.40           O\\nANISOU 2948  O   ASN A 418    10330   8974  10483   -321   -946    277       O\\nATOM   2949  CB  ASN A 418       8.666   0.302   0.607  1.00 65.48           C\\nANISOU 2949  CB  ASN A 418     8842   7154   8882      6   -958    240       C\\nATOM   2950  CG  ASN A 418       9.105   0.938   1.907  1.00 70.06           C\\nANISOU 2950  CG  ASN A 418     9208   7784   9627    195   -932    141       C\\nATOM   2951  OD1 ASN A 418       9.915   0.373   2.644  1.00 72.31           O\\nANISOU 2951  OD1 ASN A 418     9648   8008   9820    376   -923     50       O\\nATOM   2952  ND2 ASN A 418       8.575   2.123   2.197  1.00 73.88           N\\nANISOU 2952  ND2 ASN A 418     9344   8372  10354    175   -946    143       N\\nATOM   2953  N   SER A 419       5.371   0.528   0.828  1.00 73.71           N\\nANISOU 2953  N   SER A 419     9563   8456   9988   -577  -1081    433       N\\nATOM   2954  CA  SER A 419       4.257   1.208   1.479  1.00 74.87           C\\nANISOU 2954  CA  SER A 419     9342   8795  10311   -653  -1075    444       C\\nATOM   2955  C   SER A 419       3.387   0.269   2.304  1.00 71.13           C\\nANISOU 2955  C   SER A 419     8963   8398   9665   -899  -1010    455       C\\nATOM   2956  O   SER A 419       2.578   0.748   3.105  1.00 79.35           O\\nANISOU 2956  O   SER A 419     9691   9646  10814   -930   -935    423       O\\nATOM   2957  CB  SER A 419       3.402   1.927   0.433  1.00 76.98           C\\nANISOU 2957  CB  SER A 419     9339   9174  10737   -757  -1215    564       C\\nATOM   2958  OG  SER A 419       4.102   3.028  -0.124  1.00 76.00           O\\nANISOU 2958  OG  SER A 419     9078   8985  10813   -542  -1256    597       O\\nATOM   2959  N   ALA A 420       3.532  -1.043   2.146  1.00 64.52           N\\nANISOU 2959  N   ALA A 420     8553   7392   8567  -1076  -1023    494       N\\nATOM   2960  CA  ALA A 420       2.711  -1.998   2.873  1.00 70.62           C\\nANISOU 2960  CA  ALA A 420     9465   8194   9173  -1382   -964    556       C\\nATOM   2961  C   ALA A 420       3.486  -2.802   3.908  1.00 76.87           C\\nANISOU 2961  C   ALA A 420    10638   8808   9762  -1279   -878    546       C\\nATOM   2962  O   ALA A 420       2.886  -3.634   4.598  1.00 79.00           O\\nANISOU 2962  O   ALA A 420    11085   9071   9862  -1550   -815    643       O\\nATOM   2963  CB  ALA A 420       2.026  -2.954   1.892  1.00 69.09           C\\nANISOU 2963  CB  ALA A 420     9496   7901   8853  -1760  -1092    637       C\\nATOM   2964  N   VAL A 421       4.793  -2.590   4.035  1.00 77.91           N\\nANISOU 2964  N   VAL A 421    10893   8806   9904   -910   -888    455       N\\nATOM   2965  CA  VAL A 421       5.579  -3.412   4.946  1.00 79.27           C\\nANISOU 2965  CA  VAL A 421    11443   8799   9879   -770   -869    464       C\\nATOM   2966  C   VAL A 421       5.680  -2.792   6.335  1.00 78.59           C\\nANISOU 2966  C   VAL A 421    11159   8929   9775   -616   -776    415       C\\nATOM   2967  O   VAL A 421       5.844  -3.521   7.319  1.00 80.37           O\\nANISOU 2967  O   VAL A 421    11677   9096   9766   -626   -753    490       O\\nATOM   2968  CB  VAL A 421       6.980  -3.686   4.367  1.00 73.59           C\\nANISOU 2968  CB  VAL A 421    10961   7841   9160   -437   -947    375       C\\nATOM   2969  CG1 VAL A 421       6.871  -4.312   2.991  1.00 71.39           C\\nANISOU 2969  CG1 VAL A 421    10910   7375   8838   -578  -1015    377       C\\nATOM   2970  CG2 VAL A 421       7.810  -2.409   4.324  1.00 65.73           C\\nANISOU 2970  CG2 VAL A 421     9584   7002   8387   -121   -934    246       C\\nATOM   2971  N   ASN A 422       5.581  -1.466   6.440  1.00 74.03           N\\nANISOU 2971  N   ASN A 422    10123   8582   9422   -475   -738    288       N\\nATOM   2972  CA  ASN A 422       5.742  -0.820   7.742  1.00 73.83           C\\nANISOU 2972  CA  ASN A 422     9929   8759   9366   -304   -662    170       C\\nATOM   2973  C   ASN A 422       4.697  -1.265   8.756  1.00 74.68           C\\nANISOU 2973  C   ASN A 422    10063   9076   9236   -564   -510    254       C\\nATOM   2974  O   ASN A 422       5.081  -1.611   9.887  1.00 76.59           O\\nANISOU 2974  O   ASN A 422    10516   9367   9218   -484   -475    261       O\\nATOM   2975  CB  ASN A 422       5.757   0.700   7.560  1.00 72.41           C\\nANISOU 2975  CB  ASN A 422     9279   8717   9517   -120   -663     -7       C\\nATOM   2976  CG  ASN A 422       7.075   1.199   7.026  1.00 70.46           C\\nANISOU 2976  CG  ASN A 422     9018   8305   9448    152   -777    -94       C\\nATOM   2977  OD1 ASN A 422       8.006   0.419   6.829  1.00 69.93           O\\nANISOU 2977  OD1 ASN A 422     9248   8068   9254    251   -842    -54       O\\nATOM   2978  ND2 ASN A 422       7.166   2.500   6.780  1.00 74.23           N\\nANISOU 2978  ND2 ASN A 422     9142   8823  10239    275   -798   -213       N\\nATOM   2979  N   PRO A 423       3.396  -1.299   8.444  1.00 74.98           N\\nANISOU 2979  N   PRO A 423     9889   9275   9326   -884   -418    332       N\\nATOM   2980  CA  PRO A 423       2.439  -1.829   9.431  1.00 79.39           C\\nANISOU 2980  CA  PRO A 423    10466  10068   9629  -1180   -229    435       C\\nATOM   2981  C   PRO A 423       2.722  -3.267   9.832  1.00 83.90           C\\nANISOU 2981  C   PRO A 423    11615  10404   9861  -1378   -249    663       C\\nATOM   2982  O   PRO A 423       2.406  -3.662  10.961  1.00 90.16           O\\nANISOU 2982  O   PRO A 423    12538  11363  10356  -1521    -99    763       O\\nATOM   2983  CB  PRO A 423       1.089  -1.697   8.713  1.00 72.48           C\\nANISOU 2983  CB  PRO A 423     9227   9375   8937  -1503   -180    488       C\\nATOM   2984  CG  PRO A 423       1.299  -0.620   7.719  1.00 68.97           C\\nANISOU 2984  CG  PRO A 423     8463   8890   8854  -1250   -321    353       C\\nATOM   2985  CD  PRO A 423       2.703  -0.792   7.246  1.00 69.67           C\\nANISOU 2985  CD  PRO A 423     8902   8634   8934   -993   -481    335       C\\nATOM   2986  N   ILE A 424       3.313  -4.062   8.939  1.00 83.26           N\\nANISOU 2986  N   ILE A 424    11907   9927   9801  -1380   -427    747       N\\nATOM   2987  CA  ILE A 424       3.682  -5.430   9.285  1.00 83.10           C\\nANISOU 2987  CA  ILE A 424    12489   9580   9504  -1500   -487    952       C\\nATOM   2988  C   ILE A 424       4.819  -5.441  10.300  1.00 81.27           C\\nANISOU 2988  C   ILE A 424    12492   9304   9083  -1119   -542    931       C\\nATOM   2989  O   ILE A 424       4.919  -6.359  11.125  1.00 80.08           O\\nANISOU 2989  O   ILE A 424    12773   9025   8629  -1213   -546   1138       O\\nATOM   2990  CB  ILE A 424       4.040  -6.206   8.002  1.00 78.55           C\\nANISOU 2990  CB  ILE A 424    12237   8582   9027  -1536   -666    971       C\\nATOM   2991  CG1 ILE A 424       2.825  -6.276   7.073  1.00 73.56           C\\nANISOU 2991  CG1 ILE A 424    11398   8028   8524  -1971   -654   1003       C\\nATOM   2992  CG2 ILE A 424       4.560  -7.600   8.325  1.00 80.22           C\\nANISOU 2992  CG2 ILE A 424    13116   8357   9008  -1567   -766   1149       C\\nATOM   2993  CD1 ILE A 424       3.095  -6.975   5.758  1.00 71.89           C\\nANISOU 2993  CD1 ILE A 424    11502   7446   8367  -2028   -834    970       C\\nATOM   2994  N   ILE A 425       5.680  -4.422  10.275  1.00 72.91           N\\nANISOU 2994  N   ILE A 425    11155   8352   8197   -705   -607    699       N\\nATOM   2995  CA  ILE A 425       6.795  -4.363  11.215  1.00 77.19           C\\nANISOU 2995  CA  ILE A 425    11857   8894   8577   -341   -708    646       C\\nATOM   2996  C   ILE A 425       6.320  -3.961  12.608  1.00 86.64           C\\nANISOU 2996  C   ILE A 425    12947  10469   9504   -403   -561    636       C\\nATOM   2997  O   ILE A 425       6.863  -4.432  13.615  1.00 84.58           O\\nANISOU 2997  O   ILE A 425    13008  10207   8921   -280   -633    733       O\\nATOM   2998  CB  ILE A 425       7.877  -3.406  10.689  1.00 71.65           C\\nANISOU 2998  CB  ILE A 425    10863   8188   8172     58   -830    392       C\\nATOM   2999  CG1 ILE A 425       8.343  -3.850   9.303  1.00 71.05           C\\nANISOU 2999  CG1 ILE A 425    10906   7796   8294    111   -926    402       C\\nATOM   3000  CG2 ILE A 425       9.062  -3.360  11.634  1.00 68.37           C\\nANISOU 3000  CG2 ILE A 425    10565   7798   7613    422   -980    318       C\\nATOM   3001  CD1 ILE A 425       9.377  -2.939   8.685  1.00 69.86           C\\nANISOU 3001  CD1 ILE A 425    10448   7667   8427    435  -1000    194       C\\nATOM   3002  N   TYR A 426       5.302  -3.102  12.695  1.00 80.85           N\\nANISOU 3002  N   TYR A 426    11769  10077   8874   -571   -359    514       N\\nATOM   3003  CA  TYR A 426       4.811  -2.668  13.999  1.00 87.40           C\\nANISOU 3003  CA  TYR A 426    12467  11316   9424   -609   -172    444       C\\nATOM   3004  C   TYR A 426       4.159  -3.813  14.767  1.00 95.75           C\\nANISOU 3004  C   TYR A 426    13906  12427  10045   -980    -30    771       C\\nATOM   3005  O   TYR A 426       4.175  -3.815  16.004  1.00 99.16           O\\nANISOU 3005  O   TYR A 426    14463  13130  10085   -961     67    794       O\\nATOM   3006  CB  TYR A 426       3.826  -1.511  13.828  1.00 86.99           C\\nANISOU 3006  CB  TYR A 426    11825  11596   9630   -664     22    214       C\\nATOM   3007  CG  TYR A 426       4.370  -0.345  13.027  1.00 85.70           C\\nANISOU 3007  CG  TYR A 426    11311  11332   9920   -350   -120    -55       C\\nATOM   3008  CD1 TYR A 426       5.706   0.027  13.118  1.00 83.30           C\\nANISOU 3008  CD1 TYR A 426    11097  10869   9684      2   -327   -201       C\\nATOM   3009  CD2 TYR A 426       3.547   0.381  12.176  1.00 83.93           C\\nANISOU 3009  CD2 TYR A 426    10656  11172  10061   -422    -61   -137       C\\nATOM   3010  CE1 TYR A 426       6.206   1.093  12.385  1.00 79.72           C\\nANISOU 3010  CE1 TYR A 426    10330  10311   9648    224   -438   -408       C\\nATOM   3011  CE2 TYR A 426       4.037   1.447  11.441  1.00 82.37           C\\nANISOU 3011  CE2 TYR A 426    10186  10845  10265   -163   -196   -323       C\\nATOM   3012  CZ  TYR A 426       5.368   1.799  11.548  1.00 77.29           C\\nANISOU 3012  CZ  TYR A 426     9656  10030   9679    135   -368   -452       C\\nATOM   3013  OH  TYR A 426       5.859   2.858  10.815  1.00 65.48           O\\nANISOU 3013  OH  TYR A 426     7898   8395   8588    330   -485   -601       O\\nATOM   3014  N   THR A 427       3.583  -4.790  14.059  1.00 94.12           N\\nANISOU 3014  N   THR A 427    13912  11967   9880  -1346    -21   1029       N\\nATOM   3015  CA  THR A 427       2.981  -5.936  14.735  1.00 94.73           C\\nANISOU 3015  CA  THR A 427    14395  12024   9574  -1766    104   1385       C\\nATOM   3016  C   THR A 427       4.036  -6.873  15.301  1.00 93.77           C\\nANISOU 3016  C   THR A 427    14923  11553   9151  -1581   -115   1608       C\\nATOM   3017  O   THR A 427       3.779  -7.565  16.293  1.00107.23           O\\nANISOU 3017  O   THR A 427    16989  13325  10429  -1808    -22   1896       O\\nATOM   3018  CB  THR A 427       2.076  -6.711  13.777  1.00 92.02           C\\nANISOU 3018  CB  THR A 427    14101  11462   9402  -2246    135   1572       C\\nATOM   3019  OG1 THR A 427       2.869  -7.267  12.722  1.00 87.69           O\\nANISOU 3019  OG1 THR A 427    13873  10378   9067  -2083   -148   1577       O\\nATOM   3020  CG2 THR A 427       1.028  -5.801  13.182  1.00 92.49           C\\nANISOU 3020  CG2 THR A 427    13488  11881   9771  -2397    298   1371       C\\nATOM   3021  N   THR A 428       5.216  -6.918  14.687  1.00 86.78           N\\nANISOU 3021  N   THR A 428    14188  10309   8477  -1167   -404   1497       N\\nATOM   3022  CA  THR A 428       6.250  -7.850  15.112  1.00 80.90           C\\nANISOU 3022  CA  THR A 428    14030   9197   7512   -924   -656   1699       C\\nATOM   3023  C   THR A 428       7.087  -7.298  16.260  1.00 88.26           C\\nANISOU 3023  C   THR A 428    14945  10410   8178   -536   -758   1595       C\\nATOM   3024  O   THR A 428       7.228  -7.954  17.297  1.00 98.04           O\\nANISOU 3024  O   THR A 428    16618  11653   8981   -567   -810   1867       O\\nATOM   3025  CB  THR A 428       7.162  -8.200  13.934  1.00 75.14           C\\nANISOU 3025  CB  THR A 428    13433   7992   7124   -626   -905   1599       C\\nATOM   3026  OG1 THR A 428       6.369  -8.438  12.764  1.00 66.95           O\\nANISOU 3026  OG1 THR A 428    12310   6784   6344   -965   -819   1592       O\\nATOM   3027  CG2 THR A 428       7.977  -9.450  14.258  1.00 74.10           C\\nANISOU 3027  CG2 THR A 428    13971   7385   6798   -439  -1156   1861       C\\nATOM   3028  N   PHE A 429       7.642  -6.097  16.092  1.00 82.80           N\\nANISOU 3028  N   PHE A 429    13778   9948   7733   -194   -807   1216       N\\nATOM   3029  CA  PHE A 429       8.628  -5.569  17.024  1.00 85.65           C\\nANISOU 3029  CA  PHE A 429    14115  10520   7909    205   -988   1057       C\\nATOM   3030  C   PHE A 429       8.031  -4.731  18.145  1.00 88.27           C\\nANISOU 3030  C   PHE A 429    14208  11398   7933    109   -780    904       C\\nATOM   3031  O   PHE A 429       8.759  -4.373  19.077  1.00 94.52           O\\nANISOU 3031  O   PHE A 429    15046  12401   8467    386   -940    780       O\\nATOM   3032  CB  PHE A 429       9.666  -4.731  16.274  1.00 81.51           C\\nANISOU 3032  CB  PHE A 429    13220   9923   7826    606  -1176    717       C\\nATOM   3033  CG  PHE A 429      10.610  -5.545  15.451  1.00 86.84           C\\nANISOU 3033  CG  PHE A 429    14151  10141   8702    848  -1415    814       C\\nATOM   3034  CD1 PHE A 429      11.723  -6.132  16.031  1.00 95.71           C\\nANISOU 3034  CD1 PHE A 429    15590  11131   9647   1208  -1714    909       C\\nATOM   3035  CD2 PHE A 429      10.383  -5.736  14.099  1.00 90.50           C\\nANISOU 3035  CD2 PHE A 429    14539  10330   9515    740  -1348    797       C\\nATOM   3036  CE1 PHE A 429      12.597  -6.891  15.275  1.00100.77           C\\nANISOU 3036  CE1 PHE A 429    16434  11359  10493   1488  -1918    962       C\\nATOM   3037  CE2 PHE A 429      11.253  -6.492  13.334  1.00 94.15           C\\nANISOU 3037  CE2 PHE A 429    15239  10395  10137    990  -1533    835       C\\nATOM   3038  CZ  PHE A 429      12.362  -7.070  13.923  1.00 99.97           C\\nANISOU 3038  CZ  PHE A 429    16261  10992  10733   1381  -1805    907       C\\nATOM   3039  N   ASN A 430       6.743  -4.409  18.090  1.00 83.72           N\\nANISOU 3039  N   ASN A 430    13363  11080   7368   -257   -438    882       N\\nATOM   3040  CA  ASN A 430       6.116  -3.571  19.103  1.00 88.98           C\\nANISOU 3040  CA  ASN A 430    13756  12293   7759   -315   -190    673       C\\nATOM   3041  C   ASN A 430       4.910  -4.295  19.678  1.00 94.26           C\\nANISOU 3041  C   ASN A 430    14603  13185   8026   -804    139    994       C\\nATOM   3042  O   ASN A 430       3.949  -4.578  18.954  1.00 90.37           O\\nANISOU 3042  O   ASN A 430    13952  12628   7755  -1162    332   1116       O\\nATOM   3043  CB  ASN A 430       5.708  -2.218  18.523  1.00 82.34           C\\nANISOU 3043  CB  ASN A 430    12274  11632   7378   -219    -60    251       C\\nATOM   3044  CG  ASN A 430       5.177  -1.278  19.577  1.00 86.94           C\\nANISOU 3044  CG  ASN A 430    12575  12746   7711   -183    175    -57       C\\nATOM   3045  OD1 ASN A 430       3.978  -1.247  19.844  1.00 86.57           O\\nANISOU 3045  OD1 ASN A 430    12339  13023   7531   -474    525    -28       O\\nATOM   3046  ND2 ASN A 430       6.069  -0.510  20.193  1.00 93.49           N\\nANISOU 3046  ND2 ASN A 430    13362  13689   8473    174    -14   -380       N\\nATOM   3047  N   ILE A 431       4.963  -4.590  20.979  1.00 96.66           N\\nANISOU 3047  N   ILE A 431    15226  13779   7721   -842    197   1137       N\\nATOM   3048  CA  ILE A 431       3.848  -5.262  21.638  1.00 92.58           C\\nANISOU 3048  CA  ILE A 431    14883  13536   6757  -1346    552   1472       C\\nATOM   3049  C   ILE A 431       2.630  -4.348  21.695  1.00 98.55           C\\nANISOU 3049  C   ILE A 431    15013  14819   7614  -1537    984   1175       C\\nATOM   3050  O   ILE A 431       1.488  -4.806  21.569  1.00 98.81           O\\nANISOU 3050  O   ILE A 431    14936  14997   7611  -2018   1303   1397       O\\nATOM   3051  CB  ILE A 431       4.263  -5.738  23.042  1.00 91.00           C\\nANISOU 3051  CB  ILE A 431    15200  13558   5818  -1318    503   1710       C\\nATOM   3052  N   GLU A 432       2.851  -3.043  21.881  1.00 96.20           N\\nANISOU 3052  N   GLU A 432    14279  14803   7470  -1163    992    657       N\\nATOM   3053  CA  GLU A 432       1.733  -2.109  21.979  1.00 93.30           C\\nANISOU 3053  CA  GLU A 432    13305  14920   7225  -1248   1385    325       C\\nATOM   3054  C   GLU A 432       1.005  -1.971  20.646  1.00 90.82           C\\nANISOU 3054  C   GLU A 432    12560  14400   7549  -1408   1437    316       C\\nATOM   3055  O   GLU A 432      -0.230  -1.927  20.610  1.00 84.30           O\\nANISOU 3055  O   GLU A 432    11363  13912   6757  -1725   1791    333       O\\nATOM   3056  CB  GLU A 432       2.229  -0.750  22.471  1.00 88.42           C\\nANISOU 3056  CB  GLU A 432    12394  14544   6659   -774   1324   -250       C\\nATOM   3057  N   PHE A 433       1.747  -1.901  19.538  1.00 90.26           N\\nANISOU 3057  N   PHE A 433    12509  13817   7970  -1197   1087    288       N\\nATOM   3058  CA  PHE A 433       1.098  -1.850  18.232  1.00 93.03           C\\nANISOU 3058  CA  PHE A 433    12520  13969   8860  -1363   1090    317       C\\nATOM   3059  C   PHE A 433       0.366  -3.155  17.929  1.00 92.59           C\\nANISOU 3059  C   PHE A 433    12717  13789   8674  -1909   1194    776       C\\nATOM   3060  O   PHE A 433      -0.768  -3.136  17.438  1.00 86.48           O\\nANISOU 3060  O   PHE A 433    11554  13195   8111  -2229   1396    805       O\\nATOM   3061  CB  PHE A 433       2.125  -1.540  17.137  1.00 94.23           C\\nANISOU 3061  CB  PHE A 433    12696  13628   9479  -1036    712    208       C\\nATOM   3062  CG  PHE A 433       2.253  -0.070  16.807  1.00 90.02           C\\nANISOU 3062  CG  PHE A 433    11657  13176   9371   -672    669   -233       C\\nATOM   3063  CD1 PHE A 433       1.220   0.604  16.178  1.00 82.18           C\\nANISOU 3063  CD1 PHE A 433    10137  12335   8753   -746    821   -367       C\\nATOM   3064  CD2 PHE A 433       3.413   0.630  17.106  1.00 88.82           C\\nANISOU 3064  CD2 PHE A 433    11559  12920   9269   -265    446   -498       C\\nATOM   3065  CE1 PHE A 433       1.331   1.949  15.867  1.00 78.56           C\\nANISOU 3065  CE1 PHE A 433     9265  11877   8709   -401    756   -738       C\\nATOM   3066  CE2 PHE A 433       3.531   1.976  16.796  1.00 82.75           C\\nANISOU 3066  CE2 PHE A 433    10368  12155   8919     24    394   -882       C\\nATOM   3067  CZ  PHE A 433       2.487   2.635  16.177  1.00 81.74           C\\nANISOU 3067  CZ  PHE A 433     9768  12128   9161    -34    550   -991       C\\nATOM   3068  N   ARG A 434       0.991  -4.296  18.232  1.00 96.08           N\\nANISOU 3068  N   ARG A 434    13805  13913   8786  -2025   1037   1134       N\\nATOM   3069  CA  ARG A 434       0.385  -5.588  17.918  1.00 91.88           C\\nANISOU 3069  CA  ARG A 434    13600  13146   8164  -2562   1089   1576       C\\nATOM   3070  C   ARG A 434      -0.930  -5.778  18.663  1.00 88.38           C\\nANISOU 3070  C   ARG A 434    12942  13229   7411  -3068   1532   1730       C\\nATOM   3071  O   ARG A 434      -1.944  -6.162  18.068  1.00 89.59           O\\nANISOU 3071  O   ARG A 434    12864  13413   7764  -3530   1674   1870       O\\nATOM   3072  CB  ARG A 434       1.360  -6.718  18.249  1.00 91.99           C\\nANISOU 3072  CB  ARG A 434    14390  12689   7871  -2520    823   1923       C\\nATOM   3073  N   LYS A 435      -0.934  -5.515  19.973  1.00 92.30           N\\nANISOU 3073  N   LYS A 435    13491  14183   7397  -3005   1759   1697       N\\nATOM   3074  CA  LYS A 435      -2.157  -5.679  20.753  1.00 95.80           C\\nANISOU 3074  CA  LYS A 435    13709  15207   7485  -3485   2243   1837       C\\nATOM   3075  C   LYS A 435      -3.199  -4.633  20.385  1.00 95.39           C\\nANISOU 3075  C   LYS A 435    12798  15636   7810  -3466   2525   1447       C\\nATOM   3076  O   LYS A 435      -4.399  -4.865  20.566  1.00100.11           O\\nANISOU 3076  O   LYS A 435    13054  16654   8329  -3942   2904   1572       O\\nATOM   3077  CB  LYS A 435      -1.843  -5.617  22.249  1.00100.45           C\\nANISOU 3077  CB  LYS A 435    14594  16206   7366  -3383   2418   1871       C\\nATOM   3078  N   ALA A 436      -2.763  -3.482  19.869  1.00 97.48           N\\nANISOU 3078  N   ALA A 436    12695  15840   8503  -2926   2339    989       N\\nATOM   3079  CA  ALA A 436      -3.711  -2.457  19.446  1.00 99.12           C\\nANISOU 3079  CA  ALA A 436    12109  16422   9131  -2835   2542    627       C\\nATOM   3080  C   ALA A 436      -4.463  -2.884  18.193  1.00 98.71           C\\nANISOU 3080  C   ALA A 436    11791  16164   9549  -3194   2456    809       C\\nATOM   3081  O   ALA A 436      -5.682  -2.702  18.103  1.00 98.79           O\\nANISOU 3081  O   ALA A 436    11222  16613   9701  -3464   2744    764       O\\nATOM   3082  CB  ALA A 436      -2.984  -1.133  19.210  1.00 94.08           C\\nANISOU 3082  CB  ALA A 436    11230  15675   8839  -2179   2321    134       C\\nATOM   3083  N   PHE A 437      -3.753  -3.456  17.217  1.00 90.64           N\\nANISOU 3083  N   PHE A 437    11168  14510   8763  -3193   2056    991       N\\nATOM   3084  CA  PHE A 437      -4.405  -3.888  15.985  1.00 89.75           C\\nANISOU 3084  CA  PHE A 437    10864  14185   9052  -3536   1925   1136       C\\nATOM   3085  C   PHE A 437      -5.403  -5.004  16.256  1.00 98.61           C\\nANISOU 3085  C   PHE A 437    12055  15479   9935  -4263   2173   1518       C\\nATOM   3086  O   PHE A 437      -6.491  -5.031  15.669  1.00 97.68           O\\nANISOU 3086  O   PHE A 437    11436  15585  10092  -4617   2265   1534       O\\nATOM   3087  CB  PHE A 437      -3.365  -4.353  14.965  1.00 85.17           C\\nANISOU 3087  CB  PHE A 437    10775  12904   8681  -3381   1477   1231       C\\nATOM   3088  CG  PHE A 437      -2.480  -3.255  14.437  1.00 86.40           C\\nANISOU 3088  CG  PHE A 437    10779  12886   9165  -2763   1230    890       C\\nATOM   3089  CD1 PHE A 437      -2.661  -1.937  14.822  1.00 90.40           C\\nANISOU 3089  CD1 PHE A 437    10767  13767   9814  -2388   1365    522       C\\nATOM   3090  CD2 PHE A 437      -1.469  -3.548  13.540  1.00 80.59           C\\nANISOU 3090  CD2 PHE A 437    10422  11598   8603  -2569    873    931       C\\nATOM   3091  CE1 PHE A 437      -1.838  -0.938  14.328  1.00 85.90           C\\nANISOU 3091  CE1 PHE A 437    10090  12981   9568  -1879   1127    241       C\\nATOM   3092  CE2 PHE A 437      -0.645  -2.555  13.044  1.00 80.08           C\\nANISOU 3092  CE2 PHE A 437    10206  11388   8833  -2065    672    655       C\\nATOM   3093  CZ  PHE A 437      -0.831  -1.248  13.438  1.00 81.28           C\\nANISOU 3093  CZ  PHE A 437     9867  11875   9140  -1744    789    329       C\\nATOM   3094  N   LEU A 438      -5.047  -5.938  17.144  1.00 97.43           N\\nANISOU 3094  N   LEU A 438    12520  15222   9276  -4511   2262   1848       N\\nATOM   3095  CA  LEU A 438      -5.930  -7.059  17.446  1.00 99.16           C\\nANISOU 3095  CA  LEU A 438    12887  15540   9250  -5265   2497   2270       C\\nATOM   3096  C   LEU A 438      -7.187  -6.605  18.176  1.00104.88           C\\nANISOU 3096  C   LEU A 438    12926  17091   9832  -5548   3020   2189       C\\nATOM   3097  O   LEU A 438      -8.233  -7.257  18.066  1.00112.28           O\\nANISOU 3097  O   LEU A 438    13646  18228  10786  -6211   3228   2440       O\\nATOM   3098  CB  LEU A 438      -5.179  -8.106  18.269  1.00101.79           C\\nANISOU 3098  CB  LEU A 438    14093  15526   9057  -5410   2445   2676       C\\nATOM   3099  N   LYS A 439      -7.108  -5.501  18.923  1.00104.77           N\\nANISOU 3099  N   LYS A 439    12553  17573   9684  -5064   3242   1817       N\\nATOM   3100  CA  LYS A 439      -8.295  -4.960  19.574  1.00111.86           C\\nANISOU 3100  CA  LYS A 439    12728  19296  10480  -5232   3763   1648       C\\nATOM   3101  C   LYS A 439      -9.200  -4.234  18.588  1.00113.57           C\\nANISOU 3101  C   LYS A 439    12089  19730  11334  -5165   3740   1359       C\\nATOM   3102  O   LYS A 439     -10.419  -4.192  18.788  1.00116.22           O\\nANISOU 3102  O   LYS A 439    11788  20658  11710  -5514   4113   1349       O\\nATOM   3103  CB  LYS A 439      -7.894  -4.019  20.711  1.00111.35           C\\nANISOU 3103  CB  LYS A 439    12602  19665  10042  -4703   3997   1288       C\\nATOM   3104  N   ILE A 440      -8.629  -3.664  17.526  1.00111.11           N\\nANISOU 3104  N   ILE A 440    11741  18958  11519  -4713   3295   1139       N\\nATOM   3105  CA  ILE A 440      -9.451  -3.036  16.502  1.00110.51           C\\nANISOU 3105  CA  ILE A 440    10923  19028  12037  -4650   3192    931       C\\nATOM   3106  C   ILE A 440     -10.182  -4.088  15.675  1.00112.85           C\\nANISOU 3106  C   ILE A 440    11191  19185  12503  -5352   3077   1285       C\\nATOM   3107  O   ILE A 440     -11.326  -3.874  15.259  1.00112.91           O\\nANISOU 3107  O   ILE A 440    10465  19613  12823  -5584   3184   1219       O\\nATOM   3108  CB  ILE A 440      -8.581  -2.115  15.629  1.00104.69           C\\nANISOU 3108  CB  ILE A 440    10219  17834  11725  -3988   2753    640       C\\nATOM   3109  CG1 ILE A 440      -7.927  -1.040  16.500  1.00107.61           C\\nANISOU 3109  CG1 ILE A 440    10580  18352  11953  -3351   2868    257       C\\nATOM   3110  CG2 ILE A 440      -9.411  -1.469  14.537  1.00101.39           C\\nANISOU 3110  CG2 ILE A 440     9088  17539  11896  -3905   2594    477       C\\nATOM   3111  CD1 ILE A 440      -7.131  -0.015  15.728  1.00100.57           C\\nANISOU 3111  CD1 ILE A 440     9658  17052  11502  -2734   2483    -35       C\\nATOM   3112  N   LEU A 441      -9.554  -5.245  15.440  1.00112.02           N\\nANISOU 3112  N   LEU A 441    11866  18490  12207  -5698   2844   1648       N\\nATOM   3113  CA  LEU A 441     -10.167  -6.342  14.697  1.00113.38           C\\nANISOU 3113  CA  LEU A 441    12136  18432  12510  -6402   2704   1969       C\\nATOM   3114  C   LEU A 441     -10.959  -7.287  15.593  1.00125.26           C\\nANISOU 3114  C   LEU A 441    13779  20090  13724  -6864   2989   2236       C\\nATOM   3115  O   LEU A 441     -11.000  -8.499  15.335  1.00130.59           O\\nANISOU 3115  O   LEU A 441    14979  20276  14364  -7284   2800   2536       O\\nATOM   3116  CB  LEU A 441      -9.096  -7.115  13.924  1.00105.56           C\\nANISOU 3116  CB  LEU A 441    11981  16582  11546  -6372   2234   2137       C\\nATOM   3117  CG  LEU A 441      -8.272  -6.304  12.915  1.00100.01           C\\nANISOU 3117  CG  LEU A 441    11276  15521  11203  -5710   1825   1833       C\\nATOM   3118  CD1 LEU A 441      -7.049  -7.083  12.435  1.00 92.92           C\\nANISOU 3118  CD1 LEU A 441    11249  13839  10218  -5600   1460   1975       C\\nATOM   3119  CD2 LEU A 441      -9.133  -5.880  11.735  1.00101.27           C\\nANISOU 3119  CD2 LEU A 441    10791  15843  11843  -5803   1635   1687       C\\nATOM   3120  N   HIS A 442     -11.587  -6.766  16.640  1.00118.20           N\\nANISOU 3120  N   HIS A 442    12431  19851  12628  -6779   3439   2114       N\\nATOM   3121  CA  HIS A 442     -12.365  -7.591  17.554  1.00126.48           C\\nANISOU 3121  CA  HIS A 442    13562  21110  13385  -7224   3754   2376       C\\nATOM   3122  C   HIS A 442     -13.375  -6.752  18.337  1.00131.96           C\\nANISOU 3122  C   HIS A 442    13462  22622  14057  -7071   4227   2114       C\\nATOM   3123  O   HIS A 442     -14.028  -5.864  17.785  1.00131.46           O\\nANISOU 3123  O   HIS A 442    12638  22887  14424  -6809   4221   1787       O\\nATOM   3124  CB  HIS A 442     -11.436  -8.335  18.515  1.00127.27           C\\nANISOU 3124  CB  HIS A 442    14545  20900  12913  -7295   3807   2692       C\\nCONECT    1    2\\nCONECT    2    1    5    3\\nCONECT    3    2    4    6\\nCONECT    4    3\\nCONECT    5    2\\nCONECT    6    7    3\\nCONECT    7    6   10    8\\nCONECT    8    7    9   11\\nCONECT    9    8\\nCONECT   10    7\\nCONECT   58   59   53\\nCONECT   59   58   62   60\\nCONECT   60   59   61   63\\nCONECT   61   60\\nCONECT   62   59\\nCONECT  194  195  185\\nCONECT  195  194  198  196\\nCONECT  196  195  197  199\\nCONECT  197  196\\nCONECT  198  195\\nCONECT  199  200  196\\nCONECT  200  199  203  201\\nCONECT  201  200  202  204\\nCONECT  202  201\\nCONECT  203  200\\nCONECT  451  452  444\\nCONECT  452  451  455  453\\nCONECT  453  452  454  456\\nCONECT  454  453\\nCONECT  455  452\\nCONECT  467  468  465\\nCONECT  468  467  471  469\\nCONECT  469  468  470  472\\nCONECT  470  469\\nCONECT  471  468\\nCONECT  486  487  474\\nCONECT  487  486  490  488\\nCONECT  488  487  489  491\\nCONECT  489  488\\nCONECT  490  487\\nCONECT  542 1057  541\\nCONECT  772  778  773  766\\nCONECT  773  772  776  774\\nCONECT  774  773  775\\nCONECT  775  774\\nCONECT  776  773  777\\nCONECT  777  776  778\\nCONECT  778  772  777\\nCONECT  779  780\\nCONECT  780  779  783  781\\nCONECT  781  780  782  784\\nCONECT  782  781\\nCONECT  783  780\\nCONECT  784  785  781\\nCONECT  785  784  788  786\\nCONECT  786  785  787  789\\nCONECT  787  786\\nCONECT  788  785\\nCONECT  801  802  791\\nCONECT  802  801  805  803\\nCONECT  803  802  804  806\\nCONECT  804  803\\nCONECT  805  802\\nCONECT  812  813  808\\nCONECT  813  812  816  814\\nCONECT  814  813  815  817\\nCONECT  815  814\\nCONECT  816  813\\nCONECT  817  818  814\\nCONECT  818  817  821  819\\nCONECT  819  818  820  822\\nCONECT  820  819\\nCONECT  821  818\\nCONECT 1018 1019 1012\\nCONECT 1019 1018 1022 1020\\nCONECT 1020 1019 1021 1023\\nCONECT 1021 1020\\nCONECT 1022 1019\\nCONECT 1028 1029 1025\\nCONECT 1029 1028 1032 1030\\nCONECT 1030 1029 1031 1033\\nCONECT 1031 1030\\nCONECT 1032 1029\\nCONECT 1033 1034 1030\\nCONECT 1034 1033 1037 1035\\nCONECT 1035 1034 1036 1038\\nCONECT 1036 1035\\nCONECT 1037 1034\\nCONECT 1038 1039 1035\\nCONECT 1039 1038 1042 1040\\nCONECT 1040 1039 1041 1043\\nCONECT 1041 1040\\nCONECT 1042 1039\\nCONECT 1057  542 1056\\nCONECT 1282 1283 1276\\nCONECT 1283 1282 1286 1284\\nCONECT 1284 1283 1285 1289\\nCONECT 1285 1284\\nCONECT 1286 1283 1287\\nCONECT 1287 1286 1288\\nCONECT 1288 1287\\nCONECT 1332 1333 1326\\nCONECT 1333 1332 1336 1334\\nCONECT 1334 1333 1335 1337\\nCONECT 1335 1334\\nCONECT 1336 1333\\nCONECT 1337 1338 1334\\nCONECT 1338 1337 1341 1339\\nCONECT 1339 1338 1340 1342\\nCONECT 1340 1339\\nCONECT 1341 1338\\nCONECT 1364 1365 1355\\nCONECT 1365 1364 1368 1366\\nCONECT 1366 1365 1367 1369\\nCONECT 1367 1366\\nCONECT 1368 1365\\nCONECT 1369 1370 1366\\nCONECT 1370 1369 1373 1371\\nCONECT 1371 1370 1372 1374\\nCONECT 1372 1371\\nCONECT 1373 1370\\nCONECT 1493 1494 1487\\nCONECT 1494 1493 1497 1495\\nCONECT 1495 1494 1496 1498\\nCONECT 1496 1495\\nCONECT 1497 1494\\nCONECT 1518 1519 1508\\nCONECT 1519 1518 1522 1520\\nCONECT 1520 1519 1521 1523\\nCONECT 1521 1520\\nCONECT 1522 1519\\nCONECT 1538 1539 1533\\nCONECT 1539 1538 1542 1540\\nCONECT 1540 1539 1541 1543\\nCONECT 1541 1540\\nCONECT 1542 1539\\nCONECT 1612 1613 1604\\nCONECT 1613 1612 1616 1614\\nCONECT 1614 1613 1615 1617\\nCONECT 1615 1614\\nCONECT 1616 1613\\nCONECT 1617 1618 1614\\nCONECT 1618 1617 1621 1619\\nCONECT 1619 1618 1620 1622\\nCONECT 1620 1619\\nCONECT 1621 1618\\nCONECT 1629 1630 1624\\nCONECT 1630 1629 1633 1631\\nCONECT 1631 1630 1632 1634\\nCONECT 1632 1631\\nCONECT 1633 1630\\nCONECT 1634 1635 1631\\nCONECT 1635 1634 1638 1636\\nCONECT 1636 1635 1637 1639\\nCONECT 1637 1636\\nCONECT 1638 1635\\nCONECT 1646 1647 1641\\nCONECT 1647 1646 1650 1648\\nCONECT 1648 1647 1649 1651\\nCONECT 1649 1648\\nCONECT 1650 1647\\nCONECT 1659 1660 1653\\nCONECT 1660 1659 1663 1661\\nCONECT 1661 1660 1662 1664\\nCONECT 1662 1661\\nCONECT 1663 1660\\nCONECT 1683 1684 1676\\nCONECT 1684 1683 1687 1685\\nCONECT 1685 1684 1686 1688\\nCONECT 1686 1685\\nCONECT 1687 1684\\nCONECT 1688 1689 1685\\nCONECT 1689 1688 1692 1690\\nCONECT 1690 1689 1691 1693\\nCONECT 1691 1690\\nCONECT 1692 1689\\nCONECT 1709 1710 1703\\nCONECT 1710 1709 1713 1711\\nCONECT 1711 1710 1712 1714\\nCONECT 1712 1711\\nCONECT 1713 1710\\nCONECT 1719 1720 1716\\nCONECT 1720 1719 1723 1721\\nCONECT 1721 1720 1722 1724\\nCONECT 1722 1721\\nCONECT 1723 1720\\nCONECT 1739 1740 1730\\nCONECT 1740 1739 1743 1741\\nCONECT 1741 1740 1742 1744\\nCONECT 1742 1741\\nCONECT 1743 1740\\nCONECT 1744 1745 1741\\nCONECT 1745 1744 1748 1746\\nCONECT 1746 1745 1747 1749\\nCONECT 1747 1746\\nCONECT 1748 1745\\nCONECT 1749 1750 1746\\nCONECT 1750 1749 1753 1751\\nCONECT 1751 1750 1752 1754\\nCONECT 1752 1751\\nCONECT 1753 1750\\nCONECT 1758 1759 1756\\nCONECT 1759 1758 1762 1760\\nCONECT 1760 1759 1761 1763\\nCONECT 1761 1760\\nCONECT 1762 1759\\nCONECT 1778 1779 1773\\nCONECT 1779 1778 1782 1780\\nCONECT 1780 1779 1781 1783\\nCONECT 1781 1780\\nCONECT 1782 1779\\nCONECT 1814 1815 1807\\nCONECT 1815 1814 1818 1816\\nCONECT 1816 1815 1817 1819\\nCONECT 1817 1816\\nCONECT 1818 1815\\nCONECT 1926 1927 1920\\nCONECT 1927 1926 1930 1928\\nCONECT 1928 1927 1929 1931\\nCONECT 1929 1928\\nCONECT 1930 1927\\nCONECT 1944 1945 1941\\nCONECT 1945 1944 1948 1946\\nCONECT 1946 1945 1947 1949\\nCONECT 1947 1946\\nCONECT 1948 1945\\nCONECT 1957 1958 1951\\nCONECT 1958 1957 1961 1959\\nCONECT 1959 1958 1960 1962\\nCONECT 1960 1959\\nCONECT 1961 1958\\nCONECT 2187 2188 2182\\nCONECT 2188 2187 2191 2189\\nCONECT 2189 2188 2190 2192\\nCONECT 2190 2189\\nCONECT 2191 2188\\nCONECT 2285 2286 2273\\nCONECT 2286 2285 2289 2287\\nCONECT 2287 2286 2288 2290\\nCONECT 2288 2287\\nCONECT 2289 2286\\nCONECT 2309 2310 2306\\nCONECT 2310 2309 2313 2311\\nCONECT 2311 2310 2312 2314\\nCONECT 2312 2311\\nCONECT 2313 2310\\nCONECT 2335 2336 2332\\nCONECT 2336 2335 2339 2337\\nCONECT 2337 2336 2338 2340\\nCONECT 2338 2337\\nCONECT 2339 2336\\nCONECT 2346 2347 2342\\nCONECT 2347 2346 2350 2348\\nCONECT 2348 2347 2349 2351\\nCONECT 2349 2348\\nCONECT 2350 2347\\nCONECT 2385 2386 2379\\nCONECT 2386 2385 2389 2387\\nCONECT 2387 2386 2388 2390\\nCONECT 2388 2387\\nCONECT 2389 2386\\nCONECT 2428 2429 2425\\nCONECT 2429 2428 2432 2430\\nCONECT 2430 2429 2431 2433\\nCONECT 2431 2430\\nCONECT 2432 2429\\nCONECT 2506 2507 2504\\nCONECT 2507 2506 2510 2508\\nCONECT 2508 2507 2509 2511\\nCONECT 2509 2508\\nCONECT 2510 2507\\nCONECT 2538 2539 2535\\nCONECT 2539 2538 2542 2540\\nCONECT 2540 2539 2541\\nCONECT 2541 2540\\nCONECT 2542 2539 2543\\nCONECT 2543 2542 2544 2545\\nCONECT 2544 2543 2546\\nCONECT 2545 2543 2547\\nCONECT 2546 2544 2548\\nCONECT 2547 2545 2548\\nCONECT 2548 2546 2547 2549\\nCONECT 2549 2548\\nCONECT 2550 2551\\nCONECT 2551 2550 2554 2552\\nCONECT 2552 2551 2553 2555\\nCONECT 2553 2552\\nCONECT 2554 2551\\nCONECT 2555 2556 2552\\nCONECT 2556 2555 2559 2557\\nCONECT 2557 2556 2558 2560\\nCONECT 2558 2557\\nCONECT 2559 2556\\nCONECT 2560 2561 2557\\nCONECT 2561 2560 2564 2562\\nCONECT 2562 2561 2563 2565\\nCONECT 2563 2562\\nCONECT 2564 2561\\nCONECT 2565 2566 2562\\nCONECT 2566 2565 2569 2567\\nCONECT 2567 2566 2568 2570\\nCONECT 2568 2567\\nCONECT 2569 2566\\nCONECT 2579 2580 2572\\nCONECT 2580 2579 2583 2581\\nCONECT 2581 2580 2582 2584\\nCONECT 2582 2581\\nCONECT 2583 2580\\nCONECT 2584 2585 2581\\nCONECT 2585 2584 2588 2586\\nCONECT 2586 2585 2587 2589\\nCONECT 2587 2586\\nCONECT 2588 2585\\nCONECT 2768 2769 2760\\nCONECT 2769 2768 2772 2770\\nCONECT 2770 2769 2771 2773\\nCONECT 2771 2770\\nCONECT 2772 2769\\nCONECT 2797 2798 2791\\nCONECT 2798 2797 2801 2799\\nCONECT 2799 2798 2800 2802\\nCONECT 2800 2799\\nCONECT 2801 2798\\nCONECT 2807 2818 2806\\nCONECT 2808 2809 2804\\nCONECT 2809 2808 2812 2810\\nCONECT 2810 2809 2811 2813\\nCONECT 2811 2810\\nCONECT 2812 2809\\nCONECT 2818 2807 2817\\nCONECT 2849 2850 2844\\nCONECT 2850 2849 2853 2851\\nCONECT 2851 2850 2852 2854\\nCONECT 2852 2851\\nCONECT 2853 2850\\nCONECT 2854 2855 2851\\nCONECT 2855 2854 2858 2856\\nCONECT 2856 2855 2857 2859\\nCONECT 2857 2856\\nCONECT 2858 2855\\nCONECT 3047 3048 3041\\nCONECT 3048 3047 3051 3049\\nCONECT 3049 3048 3050 3052\\nCONECT 3050 3049\\nCONECT 3051 3048\\nCONECT 3052 3053 3049\\nCONECT 3053 3052 3056 3054\\nCONECT 3054 3053 3055 3057\\nCONECT 3055 3054\\nCONECT 3056 3053\\nCONECT 3068 3069 3059\\nCONECT 3069 3068 3072 3070\\nCONECT 3070 3069 3071 3073\\nCONECT 3071 3070\\nCONECT 3072 3069\\nCONECT 3073 3074 3070\\nCONECT 3074 3073 3077 3075\\nCONECT 3075 3074 3076 3078\\nCONECT 3076 3075\\nCONECT 3077 3074\\nCONECT 3094 3095 3085\\nCONECT 3095 3094 3098 3096\\nCONECT 3096 3095 3097 3099\\nCONECT 3097 3096\\nCONECT 3098 3095\\nCONECT 3099 3100 3096\\nCONECT 3100 3099 3103 3101\\nCONECT 3101 3100 3102 3104\\nCONECT 3102 3101\\nCONECT 3103 3100\\nCONECT 3120 3121 3114\\nCONECT 3121 3120 3124 3122\\nCONECT 3122 3121 3123\\nCONECT 3123 3122\\nCONECT 3124 3121\\nEND\\n\",\"pdb\");\n\tviewer_1716807258080235.setStyle({\"model\": 0},{\"cartoon\": {}});\n\tviewer_1716807258080235.addSurface(null,{\"opacity\": 1, \"color\": \"lightgray\"});\n\tviewer_1716807258080235.addModels(\"HETATM    1 C72  UNL   1       10.837   5.700 -13.643  1.00  0.00           C  \\nHETATM    2 C73  UNL   1        9.571   4.916 -13.045  1.00  0.00           C  \\nHETATM    3 C74  UNL   1        8.776   4.163 -14.133  1.00  0.00           C  \\nHETATM    4 C75  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10.677   5.749 -15.050  1.00  0.00           O  \\nHETATM   17 C84  UNL   1       11.020   7.124 -12.977  1.00  0.00           C  \\nHETATM   18 C85  UNL   1       11.942   7.219 -11.725  1.00  0.00           C  \\nHETATM   19 C86  UNL   1       11.148   7.523 -10.423  1.00  0.00           C  \\nHETATM   20 C87  UNL   1       11.734   8.670  -9.566  1.00  0.00           C  \\nHETATM   21 O8   UNL   1       12.901   8.219  -8.867  1.00  0.00           O  \\nHETATM   22 C88  UNL   1       10.752   9.202  -8.473  1.00  0.00           C  \\nHETATM   23 N12  UNL   1       10.483   8.065  -7.514  1.00  0.00           N1+\\nHETATM   24 C89  UNL   1       10.638   8.197  -6.032  1.00  0.00           C  \\nHETATM   25 C90  UNL   1       11.400   7.030  -5.411  1.00  0.00           C  \\nHETATM   26 C91  UNL   1       11.356   7.156  -3.879  1.00  0.00           C  \\nHETATM   27 C92  UNL   1       11.652   8.560  -3.317  1.00  0.00           C  \\nHETATM   28 O9   UNL   1       11.218   9.629  -4.145  1.00  0.00           O  \\nHETATM   29 C93  UNL   1       11.327   9.481  -5.563  1.00  0.00           C  \\nHETATM   30 N13  UNL   1       13.054   8.692  -2.912  1.00  0.00           N1+\\nCONECT    1    2   14   16   17\\nCONECT    2    1    3   11\\nCONECT   14    1\\nCONECT   16    1   15\\nCONECT   17    1   18\\nCONECT    3    2    4\\nCONECT   11    2   10   12\\nCONECT    4    3    5    5    9\\nCONECT    5    4    4    6\\nCONECT    9    4    8    8   10\\nCONECT    6    5    7    7\\nCONECT    7    6    6    8\\nCONECT    8    7    9    9\\nCONECT   10    9   11   13\\nCONECT   13   10\\nCONECT   12   11\\nCONECT   15   16\\nCONECT   18   17   19\\nCONECT   19   18   20\\nCONECT   20   19   21   22\\nCONECT   21   20\\nCONECT   22   20   23\\nCONECT   23   22   24\\nCONECT   24   23   25   29\\nCONECT   25   24   26\\nCONECT   29   24   28\\nCONECT   26   25   27\\nCONECT   27   26   28   30\\nCONECT   28   27   29\\nCONECT   30   27\\nEND\",\"pdb\");\n\tviewer_1716807258080235.setStyle({\"model\": 1},{\"stick\": {\"color\": \"cyan\"}});\n\tviewer_1716807258080235.zoomTo();\nviewer_1716807258080235.render();\n});\n</script>",
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       "        <tt>jupyter labextension install jupyterlab_3dmol</tt></p>\n",
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       "\tviewer_1716807258080235.addModels(\"HEADER    MEMBRANE PROTEIN                        02-MAR-18   6CM4              \\nTITLE     STRUCTURE OF THE D2 DOPAMINE RECEPTOR BOUND TO THE ATYPICAL           \\nTITLE    2 ANTIPSYCHOTIC DRUG RISPERIDONE                                       \\nCOMPND    MOL_ID: 1;                                                            \\nCOMPND   2 MOLECULE: D(2) DOPAMINE RECEPTOR, ENDOLYSIN CHIMERA;                 \\nCOMPND   3 CHAIN: A;                                                            \\nCOMPND   4 SYNONYM: DOPAMINE D2 RECEPTOR, LYSIS PROTEIN, LYSOZYME, MURAMIDASE,  \\nCOMPND   5 DOPAMINE D2 RECEPTOR;                                                \\nCOMPND   6 EC: 3.2.1.17;                                                        \\nCOMPND   7 ENGINEERED: YES                                                      \\nSOURCE    MOL_ID: 1;                                                            \\nSOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, ENTEROBACTERIA PHAGE T4;          \\nSOURCE   3 ORGANISM_COMMON: HUMAN, BACTERIOPHAGE T4;                            \\nSOURCE   4 ORGANISM_TAXID: 9606, 10665;                                         \\nSOURCE   5 GENE: DRD2, E, T4TP126;                                              \\nSOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            \\nSOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             \\nSOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;                                       \\nSOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          \\nSOURCE  10 EXPRESSION_SYSTEM_PLASMID: PFASTBAC1-HM                              \\nKEYWDS    GPCR, D2, DOPAMINE RECEPTOR, ANTIPSYCHOTIC, RISPERIDONE, MEMBRANE     \\nKEYWDS   2 PROTEIN                                                              \\nEXPDTA    X-RAY DIFFRACTION                                                     \\nAUTHOR    S.WANG,T.CHE,A.LEVIT,B.K.SHOICHET,D.WACKER,B.L.ROTH                   \\nREVDAT   6   04-OCT-23 6CM4    1       REMARK                                   \\nREVDAT   5   27-NOV-19 6CM4    1       REMARK                                   \\nREVDAT   4   20-FEB-19 6CM4    1       REMARK                                   \\nREVDAT   3   11-APR-18 6CM4    1       DBREF                                    \\nREVDAT   2   21-MAR-18 6CM4    1       JRNL                                     \\nREVDAT   1   14-MAR-18 6CM4    0                                                \\nSPRSDE     14-MAR-18 6CM4      6C38                                             \\nJRNL        AUTH   S.WANG,T.CHE,A.LEVIT,B.K.SHOICHET,D.WACKER,B.L.ROTH          \\nJRNL        TITL   STRUCTURE OF THE D2 DOPAMINE RECEPTOR BOUND TO THE ATYPICAL  \\nJRNL        TITL 2 ANTIPSYCHOTIC DRUG RISPERIDONE.                              \\nJRNL        REF    NATURE                        V. 555   269 2018              \\nJRNL        REFN                   ESSN 1476-4687                               \\nJRNL        PMID   29466326                                                     \\nJRNL        DOI    10.1038/NATURE25758                                          \\nREMARK   2                                                                      \\nREMARK   2 RESOLUTION.    2.87 ANGSTROMS.                                       \\nREMARK   3                                                                      \\nREMARK   3 REFINEMENT.                                                          \\nREMARK   3   PROGRAM     : PHENIX (1.12_2829: ???)                              \\nREMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            \\nREMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           \\nREMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            \\nREMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              \\nREMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               \\nREMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           \\nREMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  \\nREMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  \\nREMARK   3                                                                      \\nREMARK   3    REFINEMENT TARGET : ML                                            \\nREMARK   3                                                                      \\nREMARK   3  DATA USED IN REFINEMENT.                                            \\nREMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.87                           \\nREMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.55                          \\nREMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.360                          \\nREMARK   3   COMPLETENESS FOR RANGE        (%) : 95.2                           \\nREMARK   3   NUMBER OF REFLECTIONS             : 12814                          \\nREMARK   3                                                                      \\nREMARK   3  FIT TO DATA USED IN REFINEMENT.                                     \\nREMARK   3   R VALUE     (WORKING + TEST SET) : 0.227                           \\nREMARK   3   R VALUE            (WORKING SET) : 0.226                           \\nREMARK   3   FREE R VALUE                     : 0.249                           \\nREMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.850                           \\nREMARK   3   FREE R VALUE TEST SET COUNT      : 622                             \\nREMARK   3                                                                      \\nREMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           \\nREMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        \\nREMARK   3     1 29.5504 -  4.5475    0.98     3287   157  0.2103 0.2188        \\nREMARK   3     2  4.5475 -  3.6116    0.99     3151   170  0.2090 0.2511        \\nREMARK   3     3  3.6116 -  3.1556    0.99     3111   162  0.2730 0.3034        \\nREMARK   3     4  3.1556 -  2.8674    0.84     2643   133  0.3166 0.3214        \\nREMARK   3                                                                      \\nREMARK   3  BULK SOLVENT MODELLING.                                             \\nREMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       \\nREMARK   3   SOLVENT RADIUS     : 1.11                                          \\nREMARK   3   SHRINKAGE RADIUS   : 0.90                                          \\nREMARK   3   K_SOL              : NULL                                          \\nREMARK   3   B_SOL              : NULL                                          \\nREMARK   3                                                                      \\nREMARK   3  ERROR ESTIMATES.                                                    \\nREMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.390            \\nREMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.640           \\nREMARK   3                                                                      \\nREMARK   3  B VALUES.                                                           \\nREMARK   3   FROM WILSON PLOT           (A**2) : NULL                           \\nREMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           \\nREMARK   3   OVERALL ANISOTROPIC B VALUE.                                       \\nREMARK   3    B11 (A**2) : NULL                                                 \\nREMARK   3    B22 (A**2) : NULL                                                 \\nREMARK   3    B33 (A**2) : NULL                                                 \\nREMARK   3    B12 (A**2) : NULL                                                 \\nREMARK   3    B13 (A**2) : NULL                                                 \\nREMARK   3    B23 (A**2) : NULL                                                 \\nREMARK   3                                                                      \\nREMARK   3  TWINNING INFORMATION.                                               \\nREMARK   3   FRACTION: NULL                                                     \\nREMARK   3   OPERATOR: NULL                                                     \\nREMARK   3                                                                      \\nREMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       \\nREMARK   3                 RMSD          COUNT                                  \\nREMARK   3   BOND      :  0.003           3283                                  \\nREMARK   3   ANGLE     :  0.516           4483                                  \\nREMARK   3   CHIRALITY :  0.037            544                                  \\nREMARK   3   PLANARITY :  0.003            549                                  \\nREMARK   3   DIHEDRAL  : 10.862           1928                                  \\nREMARK   3                                                                      \\nREMARK   3  TLS DETAILS                                                         \\nREMARK   3   NUMBER OF TLS GROUPS  : 3                                          \\nREMARK   3   TLS GROUP : 1                                                      \\nREMARK   3    SELECTION: CHAIN 'A' AND (RESID 36 THROUGH 222 )                  \\nREMARK   3    ORIGIN FOR THE GROUP (A):   7.6595   9.9883   1.8227              \\nREMARK   3    T TENSOR                                                          \\nREMARK   3      T11:   0.3906 T22:   0.3948                                     \\nREMARK   3      T33:   0.4097 T12:  -0.0409                                     \\nREMARK   3      T13:   0.0298 T23:   0.0323                                     \\nREMARK   3    L TENSOR                                                          \\nREMARK   3      L11:   4.8704 L22:   2.9655                                     \\nREMARK   3      L33:   4.7317 L12:   0.7811                                     \\nREMARK   3      L13:   2.8181 L23:   1.4507                                     \\nREMARK   3    S TENSOR                                                          \\nREMARK   3      S11:   0.0593 S12:  -0.1051 S13:   0.0093                       \\nREMARK   3      S21:   0.1418 S22:  -0.1464 S23:   0.1356                       \\nREMARK   3      S31:   0.4299 S32:  -0.3974 S33:  -0.0137                       \\nREMARK   3   TLS GROUP : 2                                                      \\nREMARK   3    SELECTION: CHAIN 'A' AND (RESID 1002 THROUGH 1161 )               \\nREMARK   3    ORIGIN FOR THE GROUP (A):  32.7700  -7.7446  36.3658              \\nREMARK   3    T TENSOR                                                          \\nREMARK   3      T11:   0.6968 T22:   0.5198                                     \\nREMARK   3      T33:   0.5000 T12:   0.0363                                     \\nREMARK   3      T13:   0.0872 T23:   0.1084                                     \\nREMARK   3    L TENSOR                                                          \\nREMARK   3      L11:   6.6697 L22:   6.8821                                     \\nREMARK   3      L33:   6.4568 L12:   1.6541                                     \\nREMARK   3      L13:   1.9941 L23:   1.4205                                     \\nREMARK   3    S TENSOR                                                          \\nREMARK   3      S11:  -0.2551 S12:   0.1211 S13:  -0.2547                       \\nREMARK   3      S21:  -0.3908 S22:  -0.0566 S23:  -0.4642                       \\nREMARK   3      S31:   0.4711 S32:   0.2364 S33:   0.3147                       \\nREMARK   3   TLS GROUP : 3                                                      \\nREMARK   3    SELECTION: CHAIN 'A' AND (RESID 384 THROUGH 460 )                 \\nREMARK   3    ORIGIN FOR THE GROUP (A):   9.8885  -1.6530  -1.3224              \\nREMARK   3    T TENSOR                                                          \\nREMARK   3      T11:   0.6392 T22:   0.3770                                     \\nREMARK   3      T33:   0.5276 T12:   0.0087                                     \\nREMARK   3      T13:  -0.0908 T23:   0.0140                                     \\nREMARK   3    L TENSOR                                                          \\nREMARK   3      L11:   6.0244 L22:   5.3813                                     \\nREMARK   3      L33:   6.7255 L12:   0.3578                                     \\nREMARK   3      L13:   1.1698 L23:   0.5209                                     \\nREMARK   3    S TENSOR                                                          \\nREMARK   3      S11:  -0.0948 S12:   0.3307 S13:   0.0832                       \\nREMARK   3      S21:  -0.4022 S22:   0.2772 S23:  -0.0581                       \\nREMARK   3      S31:   1.2902 S32:  -0.0417 S33:  -0.2847                       \\nREMARK   3                                                                      \\nREMARK   3  NCS DETAILS                                                         \\nREMARK   3   NUMBER OF NCS GROUPS : NULL                                        \\nREMARK   3                                                                      \\nREMARK   3  OTHER REFINEMENT REMARKS: NULL                                      \\nREMARK   4                                                                      \\nREMARK   4 6CM4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         \\nREMARK 100                                                                      \\nREMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-MAR-18.                  \\nREMARK 100 THE DEPOSITION ID IS D_1000232947.                                   \\nREMARK 200                                                                      \\nREMARK 200 EXPERIMENTAL DETAILS                                                 \\nREMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  \\nREMARK 200  DATE OF DATA COLLECTION        : 13-AUG-17                          \\nREMARK 200  TEMPERATURE           (KELVIN) : 100                                \\nREMARK 200  PH                             : NULL                               \\nREMARK 200  NUMBER OF CRYSTALS USED        : 1                                  \\nREMARK 200                                                                      \\nREMARK 200  SYNCHROTRON              (Y/N) : Y                                  \\nREMARK 200  RADIATION SOURCE               : APS                                \\nREMARK 200  BEAMLINE                       : 23-ID-B                            \\nREMARK 200  X-RAY GENERATOR MODEL          : NULL                               \\nREMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  \\nREMARK 200  WAVELENGTH OR RANGE        (A) : 1.033                              \\nREMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL CRYO-COOLED         \\nREMARK 200                                   SI(111)                            \\nREMARK 200  OPTICS                         : NULL                               \\nREMARK 200                                                                      \\nREMARK 200  DETECTOR TYPE                  : PIXEL                              \\nREMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER X 16M                \\nREMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000                           \\nREMARK 200  DATA SCALING SOFTWARE          : HKL-3000                           \\nREMARK 200                                                                      \\nREMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 12826                              \\nREMARK 200  RESOLUTION RANGE HIGH      (A) : 2.867                              \\nREMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             \\nREMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               \\nREMARK 200                                                                      \\nREMARK 200 OVERALL.                                                             \\nREMARK 200  COMPLETENESS FOR RANGE     (%) : 97.3                               \\nREMARK 200  DATA REDUNDANCY                : 5.500                              \\nREMARK 200  R MERGE                    (I) : 0.13400                            \\nREMARK 200  R SYM                      (I) : NULL                               \\nREMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.2000                            \\nREMARK 200                                                                      \\nREMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     \\nREMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90                     \\nREMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.99                     \\nREMARK 200  COMPLETENESS FOR SHELL     (%) : 86.9                               \\nREMARK 200  DATA REDUNDANCY IN SHELL       : 2.50                               \\nREMARK 200  R MERGE FOR SHELL          (I) : 0.73800                            \\nREMARK 200  R SYM FOR SHELL            (I) : NULL                               \\nREMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.000                              \\nREMARK 200                                                                      \\nREMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              \\nREMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        \\nREMARK 200 SOFTWARE USED: PHASER                                                \\nREMARK 200 STARTING MODEL: PDB ENTRIES 5WIU & 2RH1                              \\nREMARK 200                                                                      \\nREMARK 200 REMARK: NULL                                                         \\nREMARK 280                                                                      \\nREMARK 280 CRYSTAL                                                              \\nREMARK 280 SOLVENT CONTENT, VS   (%): 57.13                                     \\nREMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.87                     \\nREMARK 280                                                                      \\nREMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM TRIS-HCL, PH 7.8, 230 MM          \\nREMARK 280  LITHIUM NITRATE, 25% PEG400, 4% 1,3-BUTANEDIOL, LIPIDIC CUBIC       \\nREMARK 280  PHASE, TEMPERATURE 293K                                             \\nREMARK 290                                                                      \\nREMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            \\nREMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       \\nREMARK 290                                                                      \\nREMARK 290      SYMOP   SYMMETRY                                                \\nREMARK 290     NNNMMM   OPERATOR                                                \\nREMARK 290       1555   X,Y,Z                                                   \\nREMARK 290       2555   -X+1/2,-Y,Z+1/2                                         \\nREMARK 290       3555   -X,Y+1/2,-Z+1/2                                         \\nREMARK 290       4555   X+1/2,-Y+1/2,-Z                                         \\nREMARK 290                                                                      \\nREMARK 290     WHERE NNN -> OPERATOR NUMBER                                     \\nREMARK 290           MMM -> TRANSLATION VECTOR                                  \\nREMARK 290                                                                      \\nREMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            \\nREMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             \\nREMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                \\nREMARK 290 RELATED MOLECULES.                                                   \\nREMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            \\nREMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            \\nREMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            \\nREMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       25.48950            \\nREMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            \\nREMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       75.65350            \\nREMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            \\nREMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       36.26150            \\nREMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       75.65350            \\nREMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       25.48950            \\nREMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       36.26150            \\nREMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            \\nREMARK 290                                                                      \\nREMARK 290 REMARK: NULL                                                         \\nREMARK 300                                                                      \\nREMARK 300 BIOMOLECULE: 1                                                       \\nREMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                \\nREMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  \\nREMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               \\nREMARK 300 BURIED SURFACE AREA.                                                 \\nREMARK 350                                                                      \\nREMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           \\nREMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                \\nREMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          \\nREMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          \\nREMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               \\nREMARK 350                                                                      \\nREMARK 350 BIOMOLECULE: 1                                                       \\nREMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         \\nREMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  \\nREMARK 350 SOFTWARE USED: PISA                                                  \\nREMARK 350 TOTAL BURIED SURFACE AREA: 1850 ANGSTROM**2                          \\nREMARK 350 SURFACE AREA OF THE COMPLEX: 20460 ANGSTROM**2                       \\nREMARK 350 CHANGE IN SOLVENT FREE ENERGY: 12.0 KCAL/MOL                         \\nREMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     \\nREMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            \\nREMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            \\nREMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            \\nREMARK 465                                                                      \\nREMARK 465 MISSING RESIDUES                                                     \\nREMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       \\nREMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               \\nREMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                \\nREMARK 465                                                                      \\nREMARK 465   M RES C SSSEQI                                                     \\nREMARK 465     MET A   140                                                      \\nREMARK 465     LEU A   141                                                      \\nREMARK 465     TYR A   142                                                      \\nREMARK 465     ASN A   143                                                      \\nREMARK 465     LYS A   362                                                      \\nREMARK 465     LEU A   363                                                      \\nREMARK 465     CYS A   443                                                      \\nREMARK 470                                                                      \\nREMARK 470 MISSING ATOM                                                         \\nREMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           \\nREMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          \\nREMARK 470 I=INSERTION CODE):                                                   \\nREMARK 470   M RES CSSEQI  ATOMS                                                \\nREMARK 470     ASN A  35    CG   OD1  ND2                                       \\nREMARK 470     TYR A  36    CG   CD1  CD2  CE1  CE2  CZ   OH                    \\nREMARK 470     LEU A  43    CG   CD1  CD2                                       \\nREMARK 470     GLU A  62    CG   CD   OE1  OE2                                  \\nREMARK 470     LYS A  63    CG   CD   CE   NZ                                   \\nREMARK 470     VAL A  96    CG1  CG2                                            \\nREMARK 470     GLU A  99    CG   CD   OE1  OE2                                  \\nREMARK 470     LYS A 101    CG   CD   CE   NZ                                   \\nREMARK 470     THR A 144    OG1  CG2                                            \\nREMARK 470     ARG A 145    CG   CD   NE   CZ   NH1  NH2                        \\nREMARK 470     SER A 147    OG                                                  \\nREMARK 470     LYS A 149    CG   CD   CE   NZ                                   \\nREMARK 470     ARG A 150    CG   CD   NE   CZ   NH1  NH2                        \\nREMARK 470     ASN A 176    CG   OD1  ND2                                       \\nREMARK 470     ASP A 178    CG   OD1  OD2                                       \\nREMARK 470     GLN A 179    CG   CD   OE1  NE2                                  \\nREMARK 470     ASN A 180    CG   OD1  ND2                                       \\nREMARK 470     LYS A 211    CE   NZ                                             \\nREMARK 470     ARG A 217    CG   CD   NE   CZ   NH1  NH2                        \\nREMARK 470     ARG A 218    CG   CD   NE   CZ   NH1  NH2                        \\nREMARK 470     LYS A 221    CG   CD   CE   NZ                                   \\nREMARK 470     ARG A 222    CG   CD   NE   CZ   NH1  NH2                        \\nREMARK 470     LYS A1016    CG   CD   CE   NZ                                   \\nREMARK 470     LYS A1019    CG   CD   CE   NZ                                   \\nREMARK 470     GLU A1022    CG   CD   OE1  OE2                                  \\nREMARK 470     LEU A1032    CG   CD1  CD2                                       \\nREMARK 470     LEU A1033    CG   CD1  CD2                                       \\nREMARK 470     LYS A1035    CG   CD   CE   NZ                                   \\nREMARK 470     SER A1036    OG                                                  \\nREMARK 470     SER A1038    OG                                                  \\nREMARK 470     ASN A1040    CG   OD1  ND2                                       \\nREMARK 470     SER A1044    OG                                                  \\nREMARK 470     GLU A1045    CG   CD   OE1  OE2                                  \\nREMARK 470     LYS A1048    CG   CD   CE   NZ                                   \\nREMARK 470     ILE A1050    CG1  CG2  CD1                                       \\nREMARK 470     ASN A1053    CG   OD1  ND2                                       \\nREMARK 470     THR A1054    OG1  CG2                                            \\nREMARK 470     ASN A1055    CG   OD1  ND2                                       \\nREMARK 470     VAL A1057    CG1  CG2                                            \\nREMARK 470     LYS A1060    CG   CD   CE   NZ                                   \\nREMARK 470     LYS A1065    CG   CD   CE   NZ                                   \\nREMARK 470     ARG A1080    CG   CD   NE   CZ   NH1  NH2                        \\nREMARK 470     LYS A1083    CG   CD   CE   NZ                                   \\nREMARK 470     LYS A1085    CG   CD   CE   NZ                                   \\nREMARK 470     ASN A1116    CG   OD1  ND2                                       \\nREMARK 470     ASP A1127    CG   OD1  OD2                                       \\nREMARK 470     VAL A1131    CG1  CG2                                            \\nREMARK 470     LYS A1135    CG   CD   CE   NZ                                   \\nREMARK 470     ARG A1137    CG   CD   NE   CZ   NH1  NH2                        \\nREMARK 470     GLN A1141    CG   CD   OE1  NE2                                  \\nREMARK 470     LYS A1147    CG   CD   CE   NZ                                   \\nREMARK 470     THR A1157    OG1  CG2                                            \\nREMARK 470     SER A 364    OG                                                  \\nREMARK 470     GLN A 365    CG   CD   OE1  NE2                                  \\nREMARK 470     GLN A 366    CG   CD   OE1  NE2                                  \\nREMARK 470     LYS A 367    CG   CD   CE   NZ                                   \\nREMARK 470     LYS A 369    CG   CD   CE   NZ                                   \\nREMARK 470     LYS A 370    CG   CD   CE   NZ                                   \\nREMARK 470     ILE A 394    CG1  CG2  CD1                                       \\nREMARK 470     HIS A 398    CG   ND1  CD2  CE1  NE2                             \\nREMARK 470     ASP A 400    CG   OD1  OD2                                       \\nREMARK 470     VAL A 406    CG1  CG2                                            \\nREMARK 470     LEU A 407    CG   CD1  CD2                                       \\nREMARK 470     ILE A 431    CG1  CG2  CD1                                       \\nREMARK 470     GLU A 432    CG   CD   OE1  OE2                                  \\nREMARK 470     ARG A 434    CG   CD   NE   CZ   NH1  NH2                        \\nREMARK 470     LYS A 435    CG   CD   CE   NZ                                   \\nREMARK 470     LEU A 438    CG   CD1  CD2                                       \\nREMARK 470     LYS A 439    CG   CD   CE   NZ                                   \\nREMARK 470     HIS A 442    CG   ND1  CD2  CE1  NE2                             \\nREMARK 500                                                                      \\nREMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         \\nREMARK 500 SUBTOPIC: TORSION ANGLES                                             \\nREMARK 500                                                                      \\nREMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            \\nREMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               \\nREMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             \\nREMARK 500                                                                      \\nREMARK 500 STANDARD TABLE:                                                      \\nREMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    \\nREMARK 500                                                                      \\nREMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           \\nREMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            \\nREMARK 500                                                                      \\nREMARK 500  M RES CSSEQI        PSI       PHI                                   \\nREMARK 500    GLN A  66       70.23   -104.22                                   \\nREMARK 500    VAL A  87      -52.46   -121.67                                   \\nREMARK 500    PHE A 198      -60.72   -124.56                                   \\nREMARK 500    ASN A1055       17.81     58.75                                   \\nREMARK 500    PHE A1114       49.44    -89.78                                   \\nREMARK 500    ASP A 400       11.47     57.92                                   \\nREMARK 500    LEU A 441       33.98    -88.55                                   \\nREMARK 500                                                                      \\nREMARK 500 REMARK: NULL                                                         \\nREMARK 610                                                                      \\nREMARK 610 MISSING HETEROATOM                                                   \\nREMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           \\nREMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          \\nREMARK 610 I=INSERTION CODE):                                                   \\nREMARK 610   M RES C SSEQI                                                      \\nREMARK 610     OLA A 2005                                                       \\nREMARK 610     OLA A 2006                                                       \\nDBREF  6CM4 A   35   222  UNP    P14416   DRD2_HUMAN      35    222             \\nDBREF  6CM4 A 1002  1161  UNP    D9IEF7   D9IEF7_BPT4      2    161             \\nDBREF  6CM4 A  362   443  UNP    P14416   DRD2_HUMAN     362    443             \\nSEQADV 6CM4 ALA A  122  UNP  P14416    ILE   122 CONFLICT                       \\nSEQADV 6CM4 THR A 1054  UNP  D9IEF7    CYS    54 CONFLICT                       \\nSEQADV 6CM4 ALA A 1097  UNP  D9IEF7    CYS    97 CONFLICT                       \\nSEQADV 6CM4 ALA A  375  UNP  P14416    LEU   375 CONFLICT                       \\nSEQADV 6CM4 ALA A  379  UNP  P14416    LEU   379 CONFLICT                       \\nSEQRES   1 A  430  ASN TYR TYR ALA THR LEU LEU THR LEU LEU ILE ALA VAL\\nSEQRES   2 A  430  ILE VAL PHE GLY ASN VAL LEU VAL CYS MET ALA VAL SER\\nSEQRES   3 A  430  ARG GLU LYS ALA LEU GLN THR THR THR ASN TYR LEU ILE\\nSEQRES   4 A  430  VAL SER LEU ALA VAL ALA ASP LEU LEU VAL ALA THR LEU\\nSEQRES   5 A  430  VAL MET PRO TRP VAL VAL TYR LEU GLU VAL VAL GLY GLU\\nSEQRES   6 A  430  TRP LYS PHE SER ARG ILE HIS CYS ASP ILE PHE VAL THR\\nSEQRES   7 A  430  LEU ASP VAL MET MET CYS THR ALA SER ALA LEU ASN LEU\\nSEQRES   8 A  430  CYS ALA ILE SER ILE ASP ARG TYR THR ALA VAL ALA MET\\nSEQRES   9 A  430  PRO MET LEU TYR ASN THR ARG TYR SER SER LYS ARG ARG\\nSEQRES  10 A  430  VAL THR VAL MET ILE SER ILE VAL TRP VAL LEU SER PHE\\nSEQRES  11 A  430  THR ILE SER CYS PRO LEU LEU PHE GLY LEU ASN ASN ALA\\nSEQRES  12 A  430  ASP GLN ASN GLU CYS ILE ILE ALA ASN PRO ALA PHE VAL\\nSEQRES  13 A  430  VAL TYR SER SER ILE VAL SER PHE TYR VAL PRO PHE ILE\\nSEQRES  14 A  430  VAL THR LEU LEU VAL TYR ILE LYS ILE TYR ILE VAL LEU\\nSEQRES  15 A  430  ARG ARG ARG ARG LYS ARG ASN ILE PHE GLU MET LEU ARG\\nSEQRES  16 A  430  ILE ASP GLU GLY LEU ARG LEU LYS ILE TYR LYS ASP THR\\nSEQRES  17 A  430  GLU GLY TYR TYR THR ILE GLY ILE GLY HIS LEU LEU THR\\nSEQRES  18 A  430  LYS SER PRO SER LEU ASN ALA ALA LYS SER GLU LEU ASP\\nSEQRES  19 A  430  LYS ALA ILE GLY ARG ASN THR ASN GLY VAL ILE THR LYS\\nSEQRES  20 A  430  ASP GLU ALA GLU LYS LEU PHE ASN GLN ASP VAL ASP ALA\\nSEQRES  21 A  430  ALA VAL ARG GLY ILE LEU ARG ASN ALA LYS LEU LYS PRO\\nSEQRES  22 A  430  VAL TYR ASP SER LEU ASP ALA VAL ARG ARG ALA ALA LEU\\nSEQRES  23 A  430  ILE ASN MET VAL PHE GLN MET GLY GLU THR GLY VAL ALA\\nSEQRES  24 A  430  GLY PHE THR ASN SER LEU ARG MET LEU GLN GLN LYS ARG\\nSEQRES  25 A  430  TRP ASP GLU ALA ALA VAL ASN LEU ALA LYS SER ARG TRP\\nSEQRES  26 A  430  TYR ASN GLN THR PRO ASN ARG ALA LYS ARG VAL ILE THR\\nSEQRES  27 A  430  THR PHE ARG THR GLY THR TRP ASP ALA TYR LYS LEU SER\\nSEQRES  28 A  430  GLN GLN LYS GLU LYS LYS ALA THR GLN MET ALA ALA ILE\\nSEQRES  29 A  430  VAL ALA GLY VAL PHE ILE ILE CYS TRP LEU PRO PHE PHE\\nSEQRES  30 A  430  ILE THR HIS ILE LEU ASN ILE HIS CYS ASP CYS ASN ILE\\nSEQRES  31 A  430  PRO PRO VAL LEU TYR SER ALA PHE THR TRP LEU GLY TYR\\nSEQRES  32 A  430  VAL ASN SER ALA VAL ASN PRO ILE ILE TYR THR THR PHE\\nSEQRES  33 A  430  ASN ILE GLU PHE ARG LYS ALA PHE LEU LYS ILE LEU HIS\\nSEQRES  34 A  430  CYS\\nHET    8NU  A2001      30                                                       \\nHET    PEG  A2002       7                                                       \\nHET    PEG  A2003       7                                                       \\nHET    PEG  A2004       7                                                       \\nHET    OLA  A2005      13                                                       \\nHET    OLA  A2006      12                                                       \\nHET    OLA  A2007      20                                                       \\nHETNAM     8NU 3-[2-[4-(6-FLUORANYL-1,2-BENZOXAZOL-3-YL)PIPERIDIN-1-            \\nHETNAM   2 8NU  YL]ETHYL]-2-METHYL-6,7,8,9-TETRAHYDROPYRIDO[1,2-                \\nHETNAM   3 8NU  A]PYRIMIDIN-4-ONE                                               \\nHETNAM     PEG DI(HYDROXYETHYL)ETHER                                            \\nHETNAM     OLA OLEIC ACID                                                       \\nFORMUL   2  8NU    C23 H27 F N4 O2                                              \\nFORMUL   3  PEG    3(C4 H10 O3)                                                 \\nFORMUL   6  OLA    3(C18 H34 O2)                                                \\nFORMUL   9  HOH   *16(H2 O)                                                     \\nHELIX    1   1 ASN A   35  GLU A   62  1                                  28\\nHELIX    2   2 LYS A   63  GLN A   66  1                                   4\\nHELIX    3   3 THR A   67  LEU A   86  1                                  20\\nHELIX    4   4 VAL A   87  GLY A   98  1                                  12\\nHELIX    5   5 SER A  103  MET A  138  1                                  36\\nHELIX    6   6 TYR A  146  CYS A  168  1                                  23\\nHELIX    7   7 PRO A  169  ASN A  176  1                                   8\\nHELIX    8   8 CYS A  182  ASN A  186  1                                   5\\nHELIX    9   9 ALA A  188  VAL A  196  1                                   9\\nHELIX   10  10 PHE A  198  GLU A 1011  1                                  35\\nHELIX   11  11 SER A 1038  GLY A 1051  1                                  14\\nHELIX   12  12 THR A 1059  ASN A 1081  1                                  23\\nHELIX   13  13 LEU A 1084  LEU A 1091  1                                   8\\nHELIX   14  14 ASP A 1092  ALA A 1112  1                                  21\\nHELIX   15  15 PHE A 1114  GLN A 1123  1                                  10\\nHELIX   16  16 ARG A 1125  ALA A 1134  1                                  10\\nHELIX   17  17 SER A 1136  GLN A 1141  1                                   6\\nHELIX   18  18 THR A 1142  GLY A 1156  1                                  15\\nHELIX   19  19 GLU A  368  CYS A  399  1                                  32\\nHELIX   20  20 PRO A  404  ASN A  418  1                                  15\\nHELIX   21  21 VAL A  421  PHE A  429  1                                   9\\nHELIX   22  22 ASN A  430  LEU A  441  1                                  12\\nSHEET    1   1 1 ARG A1014  LYS A1019  0\\nSHEET    2   2 1 TYR A1025  GLY A1028  0\\nSHEET    3   3 1 HIS A1031  THR A1034  0\\nSSBOND   1 CYS A  107    CYS A  182                          1555   1555  2.03\\nSSBOND   2 CYS A  399    CYS A  401                          1555   1555  2.04\\nCRYST1   50.979   72.523  151.307  90.00  90.00  90.00 P 21 21 21    4          \\nORIGX1      1.000000  0.000000  0.000000        0.00000                         \\nORIGX2      0.000000  1.000000  0.000000        0.00000                         \\nORIGX3      0.000000  0.000000  1.000000        0.00000                         \\nSCALE1      0.019616  0.000000  0.000000        0.00000                         \\nSCALE2      0.000000  0.013789  0.000000        0.00000                         \\nSCALE3      0.000000  0.000000  0.006609        0.00000                         \\nATOM      1  N   ASN A  35      -5.317  -8.666 -16.658  1.00108.95           N\\nATOM      2  CA  ASN A  35      -3.999  -9.279 -16.550  1.00112.41           C\\nATOM      3  C   ASN A  35      -3.770  -9.829 -15.148  1.00103.98           C\\nATOM      4  O   ASN A  35      -4.596  -9.642 -14.253  1.00111.14           O\\nATOM      5  CB  ASN A  35      -2.903  -8.271 -16.904  1.00115.88           C\\nATOM      6  N   TYR A  36      -2.640 -10.512 -14.962  1.00122.79           N\\nANISOU    6  N   TYR A  36    17290  13079  16284  -1997  -3163  -3043       N\\nATOM      7  CA  TYR A  36      -2.284 -11.046 -13.653  1.00105.49           C\\nANISOU    7  CA  TYR A  36    15314  10451  14315  -2168  -3210  -2776       C\\nATOM      8  C   TYR A  36      -1.522 -10.036 -12.804  1.00100.38           C\\nANISOU    8  C   TYR A  36    14564  10022  13555  -2013  -2870  -2480       C\\nATOM      9  O   TYR A  36      -1.767  -9.933 -11.597  1.00 95.60           O\\nANISOU    9  O   TYR A  36    13979   9308  13038  -2297  -2774  -2120       O\\nATOM     10  CB  TYR A  36      -1.455 -12.323 -13.811  1.00 98.01           C\\nANISOU   10  CB  TYR A  36    14721   8957  13564  -1967  -3571  -3071       C\\nATOM     11  N   TYR A  37      -0.606  -9.280 -13.416  1.00105.86           N\\nANISOU   11  N   TYR A  37    15140  11047  14036  -1589  -2687  -2627       N\\nATOM     12  CA  TYR A  37       0.202  -8.334 -12.652  1.00101.50           C\\nANISOU   12  CA  TYR A  37    14496  10678  13392  -1434  -2394  -2372       C\\nATOM     13  C   TYR A  37      -0.596  -7.105 -12.233  1.00 97.18           C\\nANISOU   13  C   TYR A  37    13669  10521  12732  -1638  -2109  -2055       C\\nATOM     14  O   TYR A  37      -0.269  -6.474 -11.221  1.00 92.55           O\\nANISOU   14  O   TYR A  37    13035   9983  12145  -1663  -1908  -1774       O\\nATOM     15  CB  TYR A  37       1.435  -7.931 -13.459  1.00105.43           C\\nANISOU   15  CB  TYR A  37    14938  11423  13698   -962  -2294  -2627       C\\nATOM     16  CG  TYR A  37       2.442  -9.052 -13.603  1.00112.39           C\\nANISOU   16  CG  TYR A  37    16060  11928  14715   -688  -2547  -2949       C\\nATOM     17  CD1 TYR A  37       2.745  -9.880 -12.528  1.00116.25           C\\nANISOU   17  CD1 TYR A  37    16804  11893  15472   -778  -2740  -2820       C\\nATOM     18  CD2 TYR A  37       3.084  -9.291 -14.814  1.00112.70           C\\nANISOU   18  CD2 TYR A  37    16070  12145  14606   -332  -2615  -3395       C\\nATOM     19  CE1 TYR A  37       3.662 -10.907 -12.650  1.00117.63           C\\nANISOU   19  CE1 TYR A  37    17203  11682  15808   -489  -3027  -3136       C\\nATOM     20  CE2 TYR A  37       4.002 -10.320 -14.944  1.00114.52           C\\nANISOU   20  CE2 TYR A  37    16488  12042  14980    -35  -2866  -3754       C\\nATOM     21  CZ  TYR A  37       4.287 -11.123 -13.860  1.00116.82           C\\nANISOU   21  CZ  TYR A  37    17037  11766  15584    -99  -3089  -3627       C\\nATOM     22  OH  TYR A  37       5.200 -12.147 -13.987  1.00116.76           O\\nANISOU   22  OH  TYR A  37    17222  11387  15756    236  -3393  -4004       O\\nATOM     23  N   ALA A  38      -1.639  -6.750 -12.985  1.00 96.22           N\\nANISOU   23  N   ALA A  38    13359  10676  12525  -1764  -2113  -2120       N\\nATOM     24  CA  ALA A  38      -2.506  -5.655 -12.566  1.00 90.24           C\\nANISOU   24  CA  ALA A  38    12324  10255  11709  -1946  -1899  -1864       C\\nATOM     25  C   ALA A  38      -3.348  -6.039 -11.356  1.00 93.14           C\\nANISOU   25  C   ALA A  38    12686  10447  12255  -2375  -1898  -1620       C\\nATOM     26  O   ALA A  38      -3.625  -5.191 -10.500  1.00 89.27           O\\nANISOU   26  O   ALA A  38    12015  10164  11737  -2476  -1673  -1375       O\\nATOM     27  CB  ALA A  38      -3.409  -5.222 -13.721  1.00 92.04           C\\nANISOU   27  CB  ALA A  38    12349  10812  11811  -1948  -1956  -2018       C\\nATOM     28  N   THR A  39      -3.759  -7.307 -11.265  1.00101.53           N\\nANISOU   28  N   THR A  39    13946  11141  13491  -2646  -2152  -1687       N\\nATOM     29  CA  THR A  39      -4.521  -7.761 -10.105  1.00 98.62           C\\nANISOU   29  CA  THR A  39    13594  10616  13261  -3121  -2155  -1423       C\\nATOM     30  C   THR A  39      -3.673  -7.706  -8.839  1.00 94.46           C\\nANISOU   30  C   THR A  39    13228   9915  12749  -3111  -2033  -1154       C\\nATOM     31  O   THR A  39      -4.127  -7.220  -7.795  1.00 90.19           O\\nANISOU   31  O   THR A  39    12545   9551  12174  -3363  -1831   -884       O\\nATOM     32  CB  THR A  39      -5.041  -9.178 -10.345  1.00 96.91           C\\nANISOU   32  CB  THR A  39    13602   9983  13235  -3430  -2502  -1538       C\\nATOM     33  OG1 THR A  39      -5.673  -9.242 -11.631  1.00 99.65           O\\nANISOU   33  OG1 THR A  39    13821  10489  13554  -3372  -2644  -1841       O\\nATOM     34  CG2 THR A  39      -6.044  -9.566  -9.272  1.00 85.14           C\\nANISOU   34  CG2 THR A  39    12068   8436  11847  -4016  -2487  -1245       C\\nATOM     35  N   LEU A  40      -2.434  -8.202  -8.915  1.00 91.92           N\\nANISOU   35  N   LEU A  40    13187   9271  12469  -2807  -2162  -1251       N\\nATOM     36  CA  LEU A  40      -1.537  -8.138  -7.766  1.00 89.55           C\\nANISOU   36  CA  LEU A  40    13043   8803  12179  -2751  -2081  -1015       C\\nATOM     37  C   LEU A  40      -1.335  -6.702  -7.304  1.00 83.76           C\\nANISOU   37  C   LEU A  40    12038   8512  11276  -2605  -1722   -856       C\\nATOM     38  O   LEU A  40      -1.301  -6.429  -6.098  1.00 87.36           O\\nANISOU   38  O   LEU A  40    12497   8987  11709  -2775  -1584   -580       O\\nATOM     39  CB  LEU A  40      -0.191  -8.777  -8.104  1.00 87.94           C\\nANISOU   39  CB  LEU A  40    13114   8249  12051  -2357  -2285  -1222       C\\nATOM     40  CG  LEU A  40      -0.166 -10.273  -8.417  1.00 86.57           C\\nANISOU   40  CG  LEU A  40    13274   7524  12094  -2433  -2707  -1405       C\\nATOM     41  CD1 LEU A  40       1.260 -10.798  -8.334  1.00 81.27           C\\nANISOU   41  CD1 LEU A  40    12855   6507  11518  -2029  -2890  -1557       C\\nATOM     42  CD2 LEU A  40      -1.085 -11.041  -7.480  1.00 87.43           C\\nANISOU   42  CD2 LEU A  40    13549   7331  12340  -3007  -2857  -1101       C\\nATOM     43  N   LEU A  41      -1.202  -5.770  -8.248  1.00 77.53           N\\nANISOU   43  N   LEU A  41    11027   8075  10356  -2302  -1588  -1023       N\\nATOM     44  CA  LEU A  41      -1.025  -4.372  -7.871  1.00 83.20           C\\nANISOU   44  CA  LEU A  41    11504   9166  10941  -2162  -1296   -879       C\\nATOM     45  C   LEU A  41      -2.242  -3.847  -7.120  1.00 91.88           C\\nANISOU   45  C   LEU A  41    12365  10511  12032  -2501  -1145   -694       C\\nATOM     46  O   LEU A  41      -2.101  -3.145  -6.111  1.00 94.79           O\\nANISOU   46  O   LEU A  41    12646  11017  12354  -2528   -951   -503       O\\nATOM     47  CB  LEU A  41      -0.739  -3.520  -9.108  1.00 84.35           C\\nANISOU   47  CB  LEU A  41    11487   9616  10946  -1830  -1231  -1064       C\\nATOM     48  CG  LEU A  41       0.684  -3.615  -9.668  1.00 84.82           C\\nANISOU   48  CG  LEU A  41    11682   9604  10941  -1449  -1257  -1222       C\\nATOM     49  CD1 LEU A  41       0.863  -2.686 -10.856  1.00 82.66           C\\nANISOU   49  CD1 LEU A  41    11233   9703  10473  -1206  -1167  -1345       C\\nATOM     50  CD2 LEU A  41       1.708  -3.304  -8.588  1.00 84.95           C\\nANISOU   50  CD2 LEU A  41    11768   9527  10981  -1340  -1134  -1042       C\\nATOM     51  N   THR A  42      -3.447  -4.187  -7.587  1.00 91.95           N\\nANISOU   51  N   THR A  42    12247  10603  12085  -2760  -1237   -778       N\\nATOM     52  CA  THR A  42      -4.651  -3.758  -6.883  1.00 87.42           C\\nANISOU   52  CA  THR A  42    11395  10312  11509  -3092  -1095   -650       C\\nATOM     53  C   THR A  42      -4.741  -4.405  -5.507  1.00 89.21           C\\nANISOU   53  C   THR A  42    11759  10370  11767  -3467  -1059   -402       C\\nATOM     54  O   THR A  42      -5.141  -3.757  -4.533  1.00 90.48           O\\nANISOU   54  O   THR A  42    11720  10805  11853  -3617   -841   -252       O\\nATOM     55  CB  THR A  42      -5.894  -4.085  -7.708  1.00 81.63           C\\nANISOU   55  CB  THR A  42    10483   9703  10829  -3302  -1229   -812       C\\nATOM     56  OG1 THR A  42      -5.719  -3.600  -9.045  1.00 80.89           O\\nANISOU   56  OG1 THR A  42    10326   9737  10673  -2956  -1306  -1030       O\\nATOM     57  CG2 THR A  42      -7.122  -3.427  -7.095  1.00 73.78           C\\nANISOU   57  CG2 THR A  42     9102   9107   9822  -3566  -1057   -743       C\\nATOM     58  N   LEU A  43      -4.372  -5.685  -5.408  1.00 89.32           N\\nANISOU   58  N   LEU A  43    12123   9933  11882  -3624  -1291   -363       N\\nATOM     59  CA  LEU A  43      -4.291  -6.324  -4.100  1.00 89.41           C\\nANISOU   59  CA  LEU A  43    12339   9733  11900  -3975  -1300    -78       C\\nATOM     60  C   LEU A  43      -3.297  -5.599  -3.203  1.00 85.76           C\\nANISOU   60  C   LEU A  43    11923   9332  11330  -3737  -1117     75       C\\nATOM     61  O   LEU A  43      -3.540  -5.429  -2.003  1.00 86.73           O\\nANISOU   61  O   LEU A  43    12007   9591  11355  -4009   -965    311       O\\nATOM     62  CB  LEU A  43      -3.907  -7.795  -4.254  1.00 92.73           C\\nANISOU   62  CB  LEU A  43    13182   9571  12480  -4106  -1657    -74       C\\nATOM     63  N   LEU A  44      -2.173  -5.155  -3.773  1.00 83.60           N\\nANISOU   63  N   LEU A  44    11715   8995  11055  -3246  -1124    -66       N\\nATOM     64  CA  LEU A  44      -1.214  -4.375  -3.000  1.00 85.11           C\\nANISOU   64  CA  LEU A  44    11914   9267  11155  -3006   -957     53       C\\nATOM     65  C   LEU A  44      -1.839  -3.078  -2.502  1.00 85.13           C\\nANISOU   65  C   LEU A  44    11557   9754  11035  -3039   -660    109       C\\nATOM     66  O   LEU A  44      -1.633  -2.688  -1.347  1.00 86.93           O\\nANISOU   66  O   LEU A  44    11776  10082  11172  -3118   -515    286       O\\nATOM     67  CB  LEU A  44       0.031  -4.082  -3.838  1.00 87.56           C\\nANISOU   67  CB  LEU A  44    12295   9491  11483  -2502  -1005   -135       C\\nATOM     68  CG  LEU A  44       1.048  -3.125  -3.207  1.00 86.61           C\\nANISOU   68  CG  LEU A  44    12129   9496  11281  -2230   -831    -46       C\\nATOM     69  CD1 LEU A  44       1.618  -3.719  -1.930  1.00 87.91           C\\nANISOU   69  CD1 LEU A  44    12554   9391  11458  -2363   -905    175       C\\nATOM     70  CD2 LEU A  44       2.164  -2.764  -4.177  1.00 83.34           C\\nANISOU   70  CD2 LEU A  44    11712   9091  10864  -1783   -849   -246       C\\nATOM     71  N   ILE A  45      -2.611  -2.400  -3.356  1.00 82.86           N\\nANISOU   71  N   ILE A  45    10974   9766  10745  -2965   -594    -59       N\\nATOM     72  CA  ILE A  45      -3.287  -1.172  -2.940  1.00 83.78           C\\nANISOU   72  CA  ILE A  45    10732  10317  10784  -2961   -364    -56       C\\nATOM     73  C   ILE A  45      -4.154  -1.429  -1.715  1.00 85.75           C\\nANISOU   73  C   ILE A  45    10876  10734  10969  -3402   -243     98       C\\nATOM     74  O   ILE A  45      -4.169  -0.633  -0.767  1.00 85.46           O\\nANISOU   74  O   ILE A  45    10685  10954  10832  -3395    -44    165       O\\nATOM     75  CB  ILE A  45      -4.118  -0.594  -4.101  1.00 80.09           C\\nANISOU   75  CB  ILE A  45     9986  10096  10350  -2847   -391   -260       C\\nATOM     76  CG1 ILE A  45      -3.232  -0.296  -5.309  1.00 82.72           C\\nANISOU   76  CG1 ILE A  45    10426  10322  10681  -2446   -492   -386       C\\nATOM     77  CG2 ILE A  45      -4.845   0.666  -3.657  1.00 71.03           C\\nANISOU   77  CG2 ILE A  45     8464   9363   9163  -2807   -205   -292       C\\nATOM     78  CD1 ILE A  45      -3.998   0.221  -6.511  1.00 85.25           C\\nANISOU   78  CD1 ILE A  45    10525  10865  11002  -2340   -563   -559       C\\nATOM     79  N   ALA A  46      -4.887  -2.544  -1.711  1.00 89.24           N\\nANISOU   79  N   ALA A  46    11398  11053  11455  -3812   -363    150       N\\nATOM     80  CA  ALA A  46      -5.719  -2.875  -0.560  1.00 84.99           C\\nANISOU   80  CA  ALA A  46    10762  10712  10819  -4309   -240    325       C\\nATOM     81  C   ALA A  46      -4.868  -3.120   0.678  1.00 86.02           C\\nANISOU   81  C   ALA A  46    11172  10680  10833  -4395   -199    583       C\\nATOM     82  O   ALA A  46      -5.201  -2.653   1.773  1.00 82.61           O\\nANISOU   82  O   ALA A  46    10575  10580  10232  -4584     19    688       O\\nATOM     83  CB  ALA A  46      -6.581  -4.096  -0.869  1.00 77.37           C\\nANISOU   83  CB  ALA A  46     9868   9590   9938  -4771   -418    360       C\\nATOM     84  N   VAL A  47      -3.758  -3.841   0.522  1.00 84.11           N\\nANISOU   84  N   VAL A  47    11343   9946  10669  -4238   -419    662       N\\nATOM     85  CA  VAL A  47      -2.894  -4.117   1.664  1.00 83.65           C\\nANISOU   85  CA  VAL A  47    11575   9696  10512  -4292   -436    908       C\\nATOM     86  C   VAL A  47      -2.272  -2.829   2.191  1.00 82.63           C\\nANISOU   86  C   VAL A  47    11279   9847  10269  -3948   -212    871       C\\nATOM     87  O   VAL A  47      -2.139  -2.644   3.406  1.00 89.41           O\\nANISOU   87  O   VAL A  47    12171  10845  10957  -4107    -91   1051       O\\nATOM     88  CB  VAL A  47      -1.826  -5.156   1.281  1.00 85.45           C\\nANISOU   88  CB  VAL A  47    12252   9322  10892  -4129   -768    941       C\\nATOM     89  CG1 VAL A  47      -0.873  -5.397   2.438  1.00 84.04           C\\nANISOU   89  CG1 VAL A  47    12375   8931  10627  -4135   -829   1190       C\\nATOM     90  CG2 VAL A  47      -2.490  -6.457   0.863  1.00 89.97           C\\nANISOU   90  CG2 VAL A  47    13015   9574  11594  -4506  -1029    979       C\\nATOM     91  N   ILE A  48      -1.893  -1.915   1.294  1.00 78.76           N\\nANISOU   91  N   ILE A  48    10618   9450   9859  -3495   -165    645       N\\nATOM     92  CA  ILE A  48      -1.320  -0.643   1.730  1.00 77.79           C\\nANISOU   92  CA  ILE A  48    10338   9559   9659  -3180     16    603       C\\nATOM     93  C   ILE A  48      -2.344   0.158   2.522  1.00 82.81           C\\nANISOU   93  C   ILE A  48    10623  10681  10158  -3375    261    582       C\\nATOM     94  O   ILE A  48      -2.025   0.749   3.560  1.00 85.46           O\\nANISOU   94  O   ILE A  48    10924  11187  10359  -3347    400    647       O\\nATOM     95  CB  ILE A  48      -0.797   0.158   0.525  1.00 76.69           C\\nANISOU   95  CB  ILE A  48    10090   9420   9628  -2722     -7    395       C\\nATOM     96  CG1 ILE A  48       0.350  -0.582  -0.162  1.00 81.09           C\\nANISOU   96  CG1 ILE A  48    10957   9571  10283  -2498   -216    373       C\\nATOM     97  CG2 ILE A  48      -0.339   1.535   0.969  1.00 73.83           C\\nANISOU   97  CG2 ILE A  48     9552   9290   9212  -2449    157    360       C\\nATOM     98  CD1 ILE A  48       0.859   0.105  -1.411  1.00 83.26           C\\nANISOU   98  CD1 ILE A  48    11128   9896  10613  -2110   -227    183       C\\nATOM     99  N   VAL A  49      -3.590   0.189   2.047  1.00 85.62           N\\nANISOU   99  N   VAL A  49    10696  11290  10545  -3560    309    458       N\\nATOM    100  CA  VAL A  49      -4.628   0.950   2.736  1.00 86.41           C\\nANISOU  100  CA  VAL A  49    10399  11901  10530  -3713    539    369       C\\nATOM    101  C   VAL A  49      -5.028   0.256   4.033  1.00 86.76           C\\nANISOU  101  C   VAL A  49    10505  12094  10367  -4215    646    582       C\\nATOM    102  O   VAL A  49      -5.154   0.896   5.083  1.00 84.97           O\\nANISOU  102  O   VAL A  49    10110  12216   9958  -4262    848    578       O\\nATOM    103  CB  VAL A  49      -5.837   1.166   1.811  1.00 85.12           C\\nANISOU  103  CB  VAL A  49     9887  11980  10477  -3747    531    151       C\\nATOM    104  CG1 VAL A  49      -7.004   1.745   2.592  1.00 88.42           C\\nANISOU  104  CG1 VAL A  49     9863  12953  10781  -3956    756     30       C\\nATOM    105  CG2 VAL A  49      -5.456   2.084   0.662  1.00 80.88           C\\nANISOU  105  CG2 VAL A  49     9274  11370  10087  -3251    439    -34       C\\nATOM    106  N   PHE A  50      -5.229  -1.063   3.980  1.00 87.95           N\\nANISOU  106  N   PHE A  50    10908  11980  10529  -4611    497    773       N\\nATOM    107  CA  PHE A  50      -5.635  -1.794   5.177  1.00 89.88           C\\nANISOU  107  CA  PHE A  50    11255  12333  10561  -5041    554   1009       C\\nATOM    108  C   PHE A  50      -4.604  -1.654   6.289  1.00 92.06           C\\nANISOU  108  C   PHE A  50    11792  12524  10663  -4962    580   1197       C\\nATOM    109  O   PHE A  50      -4.957  -1.394   7.445  1.00 93.62           O\\nANISOU  109  O   PHE A  50    11871  13085  10613  -5087    752   1242       O\\nATOM    110  CB  PHE A  50      -5.857  -3.269   4.846  1.00 88.37           C\\nANISOU  110  CB  PHE A  50    11370  11743  10463  -5313    300   1176       C\\nATOM    111  CG  PHE A  50      -6.166  -4.119   6.048  1.00 91.54           C\\nANISOU  111  CG  PHE A  50    11945  12184  10651  -5658    293   1438       C\\nATOM    112  CD1 PHE A  50      -7.465  -4.232   6.518  1.00 92.88           C\\nANISOU  112  CD1 PHE A  50    11823  12793  10672  -5976    452   1419       C\\nATOM    113  CD2 PHE A  50      -5.157  -4.805   6.708  1.00 90.81           C\\nANISOU  113  CD2 PHE A  50    12302  11702  10500  -5665    108   1698       C\\nATOM    114  CE1 PHE A  50      -7.752  -5.011   7.623  1.00 96.10           C\\nANISOU  114  CE1 PHE A  50    12394  13265  10853  -6335    441   1672       C\\nATOM    115  CE2 PHE A  50      -5.439  -5.583   7.816  1.00 94.85           C\\nANISOU  115  CE2 PHE A  50    12982  12260  10797  -6003     73   1952       C\\nATOM    116  CZ  PHE A  50      -6.737  -5.688   8.272  1.00 98.38           C\\nANISOU  116  CZ  PHE A  50    13146  13159  11074  -6358    245   1949       C\\nATOM    117  N   GLY A  51      -3.324  -1.822   5.959  1.00 89.17           N\\nANISOU  117  N   GLY A  51    11775  11692  10415  -4731    395   1283       N\\nATOM    118  CA  GLY A  51      -2.301  -1.796   6.988  1.00 84.51           C\\nANISOU  118  CA  GLY A  51    11458  10976   9676  -4664    370   1475       C\\nATOM    119  C   GLY A  51      -2.075  -0.415   7.573  1.00 79.23           C\\nANISOU  119  C   GLY A  51    10517  10705   8881  -4366    607   1313       C\\nATOM    120  O   GLY A  51      -1.800  -0.278   8.767  1.00 79.21           O\\nANISOU  120  O   GLY A  51    10593  10866   8639  -4497    694   1454       O\\nATOM    121  N   ASN A  52      -2.183   0.626   6.746  1.00 74.87           N\\nANISOU  121  N   ASN A  52     9661  10300   8487  -3969    686   1017       N\\nATOM    122  CA  ASN A  52      -1.869   1.971   7.213  1.00 72.04           C\\nANISOU  122  CA  ASN A  52     9081  10223   8066  -3641    847    847       C\\nATOM    123  C   ASN A  52      -3.057   2.680   7.841  1.00 76.56           C\\nANISOU  123  C   ASN A  52     9223  11393   8475  -3813   1107    674       C\\nATOM    124  O   ASN A  52      -2.860   3.566   8.681  1.00 76.05           O\\nANISOU  124  O   ASN A  52     9026  11599   8272  -3672   1243    574       O\\nATOM    125  CB  ASN A  52      -1.305   2.809   6.069  1.00 68.61           C\\nANISOU  125  CB  ASN A  52     8565   9624   7879  -3132    768    642       C\\nATOM    126  CG  ASN A  52       0.113   2.416   5.715  1.00 79.96           C\\nANISOU  126  CG  ASN A  52    10362  10592   9427  -2882    569    754       C\\nATOM    127  OD1 ASN A  52       1.065   2.835   6.370  1.00 77.35           O\\nANISOU  127  OD1 ASN A  52    10144  10206   9041  -2704    566    802       O\\nATOM    128  ND2 ASN A  52       0.261   1.600   4.681  1.00 80.13           N\\nANISOU  128  ND2 ASN A  52    10547  10294   9604  -2861    393    767       N\\nATOM    129  N   VAL A  53      -4.286   2.318   7.468  1.00 82.38           N\\nANISOU  129  N   VAL A  53     9715  12360   9224  -4106   1170    606       N\\nATOM    130  CA  VAL A  53      -5.441   2.817   8.209  1.00 86.81           C\\nANISOU  130  CA  VAL A  53     9853  13535   9597  -4309   1419    435       C\\nATOM    131  C   VAL A  53      -5.398   2.300   9.643  1.00 91.28           C\\nANISOU  131  C   VAL A  53    10607  14230   9845  -4566   1474    633       C\\nATOM    132  O   VAL A  53      -5.768   3.009  10.588  1.00 98.44           O\\nANISOU  132  O   VAL A  53    11273  15582  10548  -4528   1653    471       O\\nATOM    133  CB  VAL A  53      -6.751   2.433   7.494  1.00 83.17           C\\nANISOU  133  CB  VAL A  53     9126  13231   9243  -4473   1406    307       C\\nATOM    134  CG1 VAL A  53      -7.949   2.691   8.387  1.00 78.74           C\\nANISOU  134  CG1 VAL A  53     8217  13227   8475  -4616   1596    143       C\\nATOM    135  CG2 VAL A  53      -6.893   3.217   6.198  1.00 79.84           C\\nANISOU  135  CG2 VAL A  53     8453  12777   9107  -4129   1341     45       C\\nATOM    136  N   LEU A  54      -4.923   1.065   9.827  1.00 86.53           N\\nANISOU  136  N   LEU A  54    10442  13233   9201  -4813   1292    968       N\\nATOM    137  CA  LEU A  54      -4.726   0.529  11.172  1.00 88.26           C\\nANISOU  137  CA  LEU A  54    10891  13520   9123  -5054   1288   1196       C\\nATOM    138  C   LEU A  54      -3.747   1.383  11.968  1.00 86.94           C\\nANISOU  138  C   LEU A  54    10787  13428   8817  -4810   1356   1171       C\\nATOM    139  O   LEU A  54      -4.002   1.722  13.130  1.00 94.33           O\\nANISOU  139  O   LEU A  54    11611  14759   9469  -4901   1496   1127       O\\nATOM    140  CB  LEU A  54      -4.224  -0.914  11.097  1.00 90.28           C\\nANISOU  140  CB  LEU A  54    11637  13240   9427  -5281   1006   1548       C\\nATOM    141  CG  LEU A  54      -5.198  -2.030  10.729  1.00 92.89           C\\nANISOU  141  CG  LEU A  54    11990  13500   9806  -5638    909   1650       C\\nATOM    142  CD1 LEU A  54      -4.459  -3.354  10.614  1.00 97.20           C\\nANISOU  142  CD1 LEU A  54    13055  13428  10449  -5757    575   1961       C\\nATOM    143  CD2 LEU A  54      -6.301  -2.128  11.763  1.00 96.43           C\\nANISOU  143  CD2 LEU A  54    12213  14478   9948  -5990   1090   1654       C\\nATOM    144  N   VAL A  55      -2.613   1.737  11.356  1.00 84.36           N\\nANISOU  144  N   VAL A  55    10638  12737   8678  -4508   1252   1188       N\\nATOM    145  CA  VAL A  55      -1.593   2.518  12.053  1.00 89.47           C\\nANISOU  145  CA  VAL A  55    11371  13417   9208  -4276   1291   1178       C\\nATOM    146  C   VAL A  55      -2.164   3.838  12.551  1.00 92.31           C\\nANISOU  146  C   VAL A  55    11279  14347   9446  -4112   1550    831       C\\nATOM    147  O   VAL A  55      -1.801   4.314  13.634  1.00 95.44           O\\nANISOU  147  O   VAL A  55    11689  14966   9606  -4066   1624    802       O\\nATOM    148  CB  VAL A  55      -0.374   2.741  11.133  1.00 85.96           C\\nANISOU  148  CB  VAL A  55    11134  12447   9082  -3803   1074   1151       C\\nATOM    149  CG1 VAL A  55       0.679   3.587  11.829  1.00 76.85           C\\nANISOU  149  CG1 VAL A  55    10045  11292   7864  -3476   1063   1092       C\\nATOM    150  CG2 VAL A  55       0.217   1.408  10.697  1.00 86.37           C\\nANISOU  150  CG2 VAL A  55    11619  11948   9251  -3934    799   1439       C\\nATOM    151  N   CYS A  56      -3.075   4.442  11.786  1.00 85.56           N\\nANISOU  151  N   CYS A  56    10018  13731   8759  -3998   1660    538       N\\nATOM    152  CA  CYS A  56      -3.627   5.737  12.175  1.00 80.56           C\\nANISOU  152  CA  CYS A  56     8941  13592   8075  -3762   1850    148       C\\nATOM    153  C   CYS A  56      -4.603   5.598  13.334  1.00 86.48           C\\nANISOU  153  C   CYS A  56     9514  14821   8522  -4005   1984     66       C\\nATOM    154  O   CYS A  56      -4.495   6.313  14.337  1.00 84.77           O\\nANISOU  154  O   CYS A  56     9186  14923   8102  -3899   2089   -102       O\\nATOM    155  CB  CYS A  56      -4.301   6.398  10.975  1.00 67.26           C\\nANISOU  155  CB  CYS A  56     6920  11917   6720  -3468   1818   -150       C\\nATOM    156  SG  CYS A  56      -3.139   6.859   9.688  1.00 71.11           S\\nANISOU  156  SG  CYS A  56     7652  11761   7605  -2939   1540   -134       S\\nATOM    157  N   MET A  57      -5.565   4.680  13.217  1.00 89.30           N\\nANISOU  157  N   MET A  57     9839  15250   8838  -4343   1978    170       N\\nATOM    158  CA  MET A  57      -6.547   4.508  14.283  1.00 99.11           C\\nANISOU  158  CA  MET A  57    10893  16987   9777  -4621   2115     99       C\\nATOM    159  C   MET A  57      -5.891   4.028  15.570  1.00100.31           C\\nANISOU  159  C   MET A  57    11370  17145   9601  -4843   2094    365       C\\nATOM    160  O   MET A  57      -6.282   4.448  16.665  1.00109.98           O\\nANISOU  160  O   MET A  57    12410  18838  10541  -4909   2235    210       O\\nATOM    161  CB  MET A  57      -7.633   3.529  13.845  1.00106.16           C\\nANISOU  161  CB  MET A  57    11719  17920  10695  -4975   2095    198       C\\nATOM    162  CG  MET A  57      -8.458   4.012  12.672  1.00104.93           C\\nANISOU  162  CG  MET A  57    11195  17843  10830  -4777   2113    -94       C\\nATOM    163  SD  MET A  57      -9.729   2.811  12.239  1.00106.23           S\\nANISOU  163  SD  MET A  57    11291  18073  11000  -5226   2085     28       S\\nATOM    164  CE  MET A  57      -8.718   1.360  11.965  1.00104.77           C\\nANISOU  164  CE  MET A  57    11736  17203  10870  -5491   1838    545       C\\nATOM    165  N   ALA A  58      -4.891   3.151  15.458  1.00 91.70           N\\nANISOU  165  N   ALA A  58    10761  15535   8547  -4945   1896    749       N\\nATOM    166  CA  ALA A  58      -4.253   2.590  16.647  1.00 94.86           C\\nANISOU  166  CA  ALA A  58    11502  15887   8653  -5159   1819   1033       C\\nATOM    167  C   ALA A  58      -3.578   3.673  17.478  1.00 93.98           C\\nANISOU  167  C   ALA A  58    11323  16005   8380  -4887   1912    851       C\\nATOM    168  O   ALA A  58      -3.795   3.769  18.691  1.00 97.13           O\\nANISOU  168  O   ALA A  58    11671  16787   8447  -5049   2002    828       O\\nATOM    169  CB  ALA A  58      -3.240   1.521  16.244  1.00 92.30           C\\nANISOU  169  CB  ALA A  58    11700  14899   8471  -5223   1532   1429       C\\nATOM    170  N   VAL A  59      -2.740   4.492  16.841  1.00 96.30           N\\nANISOU  170  N   VAL A  59    11619  16077   8895  -4483   1883    717       N\\nATOM    171  CA  VAL A  59      -2.102   5.595  17.551  1.00 91.92           C\\nANISOU  171  CA  VAL A  59    10983  15733   8211  -4197   1959    504       C\\nATOM    172  C   VAL A  59      -3.144   6.585  18.045  1.00 91.74           C\\nANISOU  172  C   VAL A  59    10460  16322   8077  -4097   2177     56       C\\nATOM    173  O   VAL A  59      -2.990   7.184  19.117  1.00 99.07           O\\nANISOU  173  O   VAL A  59    11313  17573   8756  -4030   2251   -105       O\\nATOM    174  CB  VAL A  59      -1.062   6.271  16.638  1.00 84.96           C\\nANISOU  174  CB  VAL A  59    10179  14491   7608  -3805   1881    441       C\\nATOM    175  CG1 VAL A  59      -0.446   7.484  17.318  1.00 88.37           C\\nANISOU  175  CG1 VAL A  59    10505  15150   7923  -3491   1949    173       C\\nATOM    176  CG2 VAL A  59       0.009   5.267  16.235  1.00 77.23           C\\nANISOU  176  CG2 VAL A  59     9704  12913   6729  -3889   1637    864       C\\nATOM    177  N   SER A  60      -4.229   6.759  17.291  1.00 95.26           N\\nANISOU  177  N   SER A  60    10557  16933   8706  -4072   2257   -169       N\\nATOM    178  CA  SER A  60      -5.247   7.733  17.658  1.00 98.05           C\\nANISOU  178  CA  SER A  60    10416  17831   9007  -3917   2417   -638       C\\nATOM    179  C   SER A  60      -6.057   7.307  18.875  1.00104.36           C\\nANISOU  179  C   SER A  60    11113  19121   9420  -4286   2535   -633       C\\nATOM    180  O   SER A  60      -6.732   8.148  19.479  1.00107.43           O\\nANISOU  180  O   SER A  60    11125  20003   9691  -4157   2661  -1033       O\\nATOM    181  CB  SER A  60      -6.183   7.974  16.473  1.00 97.14           C\\nANISOU  181  CB  SER A  60     9973  17730   9205  -3784   2427   -864       C\\nATOM    182  OG  SER A  60      -7.148   8.967  16.770  1.00 99.99           O\\nANISOU  182  OG  SER A  60     9859  18573   9559  -3574   2531  -1349       O\\nATOM    183  N   ARG A  61      -6.003   6.030  19.255  1.00 98.78           N\\nANISOU  183  N   ARG A  61    10729  18286   8518  -4738   2478   -202       N\\nATOM    184  CA  ARG A  61      -6.880   5.512  20.291  1.00103.46           C\\nANISOU  184  CA  ARG A  61    11212  19353   8745  -5156   2589   -162       C\\nATOM    185  C   ARG A  61      -6.159   4.772  21.410  1.00107.55           C\\nANISOU  185  C   ARG A  61    12131  19803   8928  -5464   2513    219       C\\nATOM    186  O   ARG A  61      -6.808   4.395  22.392  1.00117.52           O\\nANISOU  186  O   ARG A  61    13311  21498   9842  -5828   2609    262       O\\nATOM    187  CB  ARG A  61      -7.937   4.590  19.664  1.00104.53           C\\nANISOU  187  CB  ARG A  61    11265  19502   8951  -5497   2593    -37       C\\nATOM    188  CG  ARG A  61      -8.730   5.267  18.557  1.00 96.67           C\\nANISOU  188  CG  ARG A  61     9865  18588   8277  -5209   2647   -407       C\\nATOM    189  CD  ARG A  61     -10.016   4.534  18.248  1.00108.57           C\\nANISOU  189  CD  ARG A  61    11174  20320   9758  -5564   2702   -387       C\\nATOM    190  NE  ARG A  61      -9.801   3.362  17.409  1.00109.71           N\\nANISOU  190  NE  ARG A  61    11662  19943  10079  -5797   2536     11       N\\nATOM    191  CZ  ARG A  61     -10.778   2.566  16.987  1.00115.93           C\\nANISOU  191  CZ  ARG A  61    12357  20800  10890  -6123   2537     93       C\\nATOM    192  NH1 ARG A  61     -12.034   2.820  17.330  1.00116.46           N\\nANISOU  192  NH1 ARG A  61    11988  21459  10801  -6264   2710   -185       N\\nATOM    193  NH2 ARG A  61     -10.501   1.519  16.223  1.00119.11           N\\nANISOU  193  NH2 ARG A  61    13096  20686  11475  -6303   2354    434       N\\nATOM    194  N   GLU A  62      -4.853   4.558  21.301  1.00 96.97           N\\nANISOU  194  N   GLU A  62    11215  17953   7675  -5333   2333    491       N\\nATOM    195  CA  GLU A  62      -4.083   3.859  22.320  1.00101.43           C\\nANISOU  195  CA  GLU A  62    12192  18393   7956  -5580   2207    858       C\\nATOM    196  C   GLU A  62      -3.184   4.851  23.046  1.00102.22           C\\nANISOU  196  C   GLU A  62    12307  18603   7928  -5257   2227    678       C\\nATOM    197  O   GLU A  62      -2.426   5.591  22.409  1.00 92.57           O\\nANISOU  197  O   GLU A  62    11100  17116   6955  -4842   2178    531       O\\nATOM    198  CB  GLU A  62      -3.246   2.737  21.703  1.00100.84           C\\nANISOU  198  CB  GLU A  62    12621  17618   8074  -5678   1928   1315       C\\nATOM    199  N   LYS A  63      -3.269   4.854  24.378  1.00108.00           N\\nANISOU  199  N   LYS A  63    13040  19738   8259  -5463   2293    691       N\\nATOM    200  CA  LYS A  63      -2.467   5.770  25.183  1.00106.16           C\\nANISOU  200  CA  LYS A  63    12820  19652   7864  -5180   2305    504       C\\nATOM    201  C   LYS A  63      -0.976   5.535  24.970  1.00 98.83           C\\nANISOU  201  C   LYS A  63    12367  18125   7059  -4996   2054    800       C\\nATOM    202  O   LYS A  63      -0.243   6.439  24.552  1.00 90.24           O\\nANISOU  202  O   LYS A  63    11250  16879   6157  -4571   2024    584       O\\nATOM    203  CB  LYS A  63      -2.833   5.616  26.660  1.00114.28           C\\nANISOU  203  CB  LYS A  63    13807  21206   8408  -5502   2401    526       C\\nATOM    204  N   ALA A  64      -0.510   4.312  25.239  1.00108.15           N\\nANISOU  204  N   ALA A  64    13988  18956   8148  -5308   1844   1286       N\\nATOM    205  CA  ALA A  64       0.917   4.011  25.200  1.00103.75           C\\nANISOU  205  CA  ALA A  64    13892  17853   7678  -5142   1563   1569       C\\nATOM    206  C   ALA A  64       1.513   4.169  23.805  1.00 99.33           C\\nANISOU  206  C   ALA A  64    13405  16779   7558  -4812   1452   1552       C\\nATOM    207  O   ALA A  64       2.735   4.041  23.649  1.00 84.58           O\\nANISOU  207  O   ALA A  64    11875  14464   5799  -4615   1215   1732       O\\nATOM    208  CB  ALA A  64       1.164   2.590  25.719  1.00103.60           C\\nANISOU  208  CB  ALA A  64    14310  17538   7516  -5540   1320   2073       C\\nATOM    209  N   LEU A  65       0.685   4.450  22.798  1.00 91.85           N\\nANISOU  209  N   LEU A  65    12140  15902   6858  -4745   1606   1334       N\\nATOM    210  CA  LEU A  65       1.126   4.676  21.429  1.00 92.45           C\\nANISOU  210  CA  LEU A  65    12233  15560   7334  -4450   1535   1288       C\\nATOM    211  C   LEU A  65       1.071   6.143  21.021  1.00 91.55           C\\nANISOU  211  C   LEU A  65    11741  15700   7344  -4047   1715    824       C\\nATOM    212  O   LEU A  65       1.216   6.447  19.835  1.00 98.95           O\\nANISOU  212  O   LEU A  65    12606  16387   8603  -3825   1705    736       O\\nATOM    213  CB  LEU A  65       0.282   3.842  20.465  1.00 91.67           C\\nANISOU  213  CB  LEU A  65    12087  15284   7459  -4662   1529   1402       C\\nATOM    214  CG  LEU A  65       0.533   2.337  20.472  1.00 96.52           C\\nANISOU  214  CG  LEU A  65    13133  15448   8091  -4973   1266   1854       C\\nATOM    215  CD1 LEU A  65      -0.389   1.627  19.490  1.00101.66           C\\nANISOU  215  CD1 LEU A  65    13694  15972   8962  -5162   1269   1895       C\\nATOM    216  CD2 LEU A  65       1.987   2.059  20.143  1.00 88.49           C\\nANISOU  216  CD2 LEU A  65    12531  13837   7256  -4733    974   2071       C\\nATOM    217  N   GLN A  66       0.870   7.056  21.966  1.00 97.64           N\\nANISOU  217  N   GLN A  66    12271  16951   7878  -3940   1858    509       N\\nATOM    218  CA  GLN A  66       0.729   8.476  21.643  1.00 91.59           C\\nANISOU  218  CA  GLN A  66    11125  16421   7256  -3531   1991      9       C\\nATOM    219  C   GLN A  66       2.014   9.220  22.003  1.00 88.27           C\\nANISOU  219  C   GLN A  66    10883  15873   6783  -3219   1872    -76       C\\nATOM    220  O   GLN A  66       2.081  10.015  22.940  1.00 95.43           O\\nANISOU  220  O   GLN A  66    11654  17116   7488  -3077   1921   -364       O\\nATOM    221  CB  GLN A  66      -0.488   9.060  22.354  1.00 94.21           C\\nANISOU  221  CB  GLN A  66    11011  17366   7418  -3569   2200   -377       C\\nATOM    222  CG  GLN A  66      -1.806   8.615  21.747  1.00 90.38           C\\nANISOU  222  CG  GLN A  66    10255  17032   7053  -3778   2313   -412       C\\nATOM    223  CD  GLN A  66      -3.010   9.067  22.544  1.00 98.45           C\\nANISOU  223  CD  GLN A  66    10853  18690   7865  -3861   2497   -767       C\\nATOM    224  OE1 GLN A  66      -2.887   9.506  23.689  1.00102.35           O\\nANISOU  224  OE1 GLN A  66    11295  19524   8070  -3847   2548   -921       O\\nATOM    225  NE2 GLN A  66      -4.187   8.960  21.941  1.00101.41           N\\nANISOU  225  NE2 GLN A  66    10914  19243   8376  -3945   2588   -913       N\\nATOM    226  N   THR A  67       3.049   8.942  21.221  1.00 81.40           N\\nANISOU  226  N   THR A  67    10313  14420   6193  -3058   1648    159       N\\nATOM    227  CA  THR A  67       4.366   9.523  21.416  1.00 80.16           C\\nANISOU  227  CA  THR A  67    10341  13928   6189  -2690   1412    112       C\\nATOM    228  C   THR A  67       4.724  10.396  20.219  1.00 81.81           C\\nANISOU  228  C   THR A  67    10385  13739   6959  -2223   1303   -122       C\\nATOM    229  O   THR A  67       4.047  10.388  19.187  1.00 83.11           O\\nANISOU  229  O   THR A  67    10366  13821   7392  -2189   1372   -182       O\\nATOM    230  CB  THR A  67       5.424   8.430  21.618  1.00 74.28           C\\nANISOU  230  CB  THR A  67    10089  12752   5384  -2838   1150    588       C\\nATOM    231  OG1 THR A  67       5.732   7.823  20.359  1.00 77.15           O\\nANISOU  231  OG1 THR A  67    10579  12565   6169  -2749   1000    784       O\\nATOM    232  CG2 THR A  67       4.909   7.358  22.566  1.00 76.90           C\\nANISOU  232  CG2 THR A  67    10631  13398   5190  -3391   1228    928       C\\nATOM    233  N   THR A  68       5.803  11.165  20.370  1.00 86.60           N\\nANISOU  233  N   THR A  68    11062  14111   7731  -1884   1119   -244       N\\nATOM    234  CA  THR A  68       6.274  11.984  19.259  1.00 81.90           C\\nANISOU  234  CA  THR A  68    10353  13120   7646  -1492    990   -405       C\\nATOM    235  C   THR A  68       6.614  11.116  18.055  1.00 76.38           C\\nANISOU  235  C   THR A  68     9828  11956   7236  -1519    883    -94       C\\nATOM    236  O   THR A  68       6.157  11.379  16.939  1.00 74.99           O\\nANISOU  236  O   THR A  68     9479  11652   7360  -1401    915   -182       O\\nATOM    237  CB  THR A  68       7.490  12.816  19.681  1.00 80.77           C\\nANISOU  237  CB  THR A  68    10291  12786   7611  -1198    788   -526       C\\nATOM    238  OG1 THR A  68       8.582  11.948  20.014  1.00 75.97           O\\nANISOU  238  OG1 THR A  68    10037  11917   6911  -1290    604   -182       O\\nATOM    239  CG2 THR A  68       7.155  13.692  20.878  1.00 83.25           C\\nANISOU  239  CG2 THR A  68    10436  13561   7636  -1147    872   -884       C\\nATOM    240  N   THR A  69       7.412  10.066  18.270  1.00 78.37           N\\nANISOU  240  N   THR A  69    10426  11955   7395  -1662    733    255       N\\nATOM    241  CA  THR A  69       7.811   9.195  17.168  1.00 78.88           C\\nANISOU  241  CA  THR A  69    10662  11578   7732  -1656    605    503       C\\nATOM    242  C   THR A  69       6.596   8.584  16.482  1.00 78.27           C\\nANISOU  242  C   THR A  69    10482  11594   7664  -1890    759    558       C\\nATOM    243  O   THR A  69       6.522   8.550  15.247  1.00 73.15           O\\nANISOU  243  O   THR A  69     9763  10702   7330  -1761    732    539       O\\nATOM    244  CB  THR A  69       8.748   8.097  17.676  1.00 76.37           C\\nANISOU  244  CB  THR A  69    10733  11000   7285  -1777    388    839       C\\nATOM    245  OG1 THR A  69       9.982   8.680  18.112  1.00 72.19           O\\nANISOU  245  OG1 THR A  69    10268  10338   6821  -1513    212    771       O\\nATOM    246  CG2 THR A  69       9.035   7.083  16.582  1.00 74.02           C\\nANISOU  246  CG2 THR A  69    10604  10273   7247  -1776    252   1050       C\\nATOM    247  N   ASN A  70       5.625   8.114  17.269  1.00 82.86           N\\nANISOU  247  N   ASN A  70    11039  12561   7884  -2256    925    618       N\\nATOM    248  CA  ASN A  70       4.436   7.496  16.698  1.00 81.91           C\\nANISOU  248  CA  ASN A  70    10800  12565   7757  -2530   1069    672       C\\nATOM    249  C   ASN A  70       3.562   8.494  15.947  1.00 81.00           C\\nANISOU  249  C   ASN A  70    10269  12649   7860  -2327   1221    314       C\\nATOM    250  O   ASN A  70       2.805   8.084  15.063  1.00 74.10           O\\nANISOU  250  O   ASN A  70     9290  11736   7128  -2431   1271    335       O\\nATOM    251  CB  ASN A  70       3.629   6.801  17.798  1.00 79.20           C\\nANISOU  251  CB  ASN A  70    10505  12647   6942  -3020   1221    832       C\\nATOM    252  CG  ASN A  70       4.333   5.581  18.348  1.00 78.28           C\\nANISOU  252  CG  ASN A  70    10856  12250   6638  -3286   1014   1268       C\\nATOM    253  OD1 ASN A  70       5.224   5.030  17.706  1.00 74.09           O\\nANISOU  253  OD1 ASN A  70    10588  11183   6379  -3127    762   1443       O\\nATOM    254  ND2 ASN A  70       3.941   5.152  19.542  1.00 73.15           N\\nANISOU  254  ND2 ASN A  70    10308  11972   5512  -3692   1103   1439       N\\nATOM    255  N   TYR A  71       3.640   9.786  16.274  1.00 84.07           N\\nANISOU  255  N   TYR A  71    10427  13227   8291  -2033   1261    -20       N\\nATOM    256  CA  TYR A  71       2.933  10.782  15.475  1.00 77.80           C\\nANISOU  256  CA  TYR A  71     9275  12516   7768  -1780   1321   -352       C\\nATOM    257  C   TYR A  71       3.632  11.001  14.143  1.00 70.85           C\\nANISOU  257  C   TYR A  71     8477  11134   7310  -1497   1135   -290       C\\nATOM    258  O   TYR A  71       2.978  11.216  13.117  1.00 65.56           O\\nANISOU  258  O   TYR A  71     7626  10422   6864  -1416   1148   -386       O\\nATOM    259  CB  TYR A  71       2.809  12.094  16.246  1.00 74.68           C\\nANISOU  259  CB  TYR A  71     8632  12431   7314  -1540   1370   -746       C\\nATOM    260  CG  TYR A  71       1.783  12.035  17.350  1.00 80.29           C\\nANISOU  260  CG  TYR A  71     9123  13772   7611  -1796   1612   -924       C\\nATOM    261  CD1 TYR A  71       0.690  11.189  17.253  1.00 82.22           C\\nANISOU  261  CD1 TYR A  71     9248  14311   7681  -2164   1796   -825       C\\nATOM    262  CD2 TYR A  71       1.912  12.814  18.492  1.00 84.10           C\\nANISOU  262  CD2 TYR A  71     9504  14589   7861  -1688   1658  -1202       C\\nATOM    263  CE1 TYR A  71      -0.250  11.123  18.258  1.00 91.89           C\\nANISOU  263  CE1 TYR A  71    10236  16183   8495  -2441   2045   -986       C\\nATOM    264  CE2 TYR A  71       0.976  12.756  19.503  1.00 85.39           C\\nANISOU  264  CE2 TYR A  71     9439  15406   7599  -1932   1905  -1392       C\\nATOM    265  CZ  TYR A  71      -0.103  11.907  19.381  1.00 94.33           C\\nANISOU  265  CZ  TYR A  71    10434  16859   8548  -2320   2110  -1275       C\\nATOM    266  OH  TYR A  71      -1.045  11.839  20.381  1.00 99.85           O\\nANISOU  266  OH  TYR A  71    10911  18103   8926  -2541   2275  -1429       O\\nATOM    267  N   LEU A  72       4.963  10.950  14.139  1.00 66.28           N\\nANISOU  267  N   LEU A  72     8155  10205   6825  -1355    960   -134       N\\nATOM    268  CA  LEU A  72       5.688  10.938  12.880  1.00 65.47           C\\nANISOU  268  CA  LEU A  72     8142   9678   7057  -1158    810    -34       C\\nATOM    269  C   LEU A  72       5.520   9.612  12.156  1.00 66.26           C\\nANISOU  269  C   LEU A  72     8411   9590   7173  -1363    790    218       C\\nATOM    270  O   LEU A  72       5.755   9.545  10.947  1.00 70.26           O\\nANISOU  270  O   LEU A  72     8925   9843   7928  -1232    713    248       O\\nATOM    271  CB  LEU A  72       7.166  11.237  13.129  1.00 68.98           C\\nANISOU  271  CB  LEU A  72     8763   9860   7585   -964    640     32       C\\nATOM    272  CG  LEU A  72       7.464  12.668  13.586  1.00 71.02           C\\nANISOU  272  CG  LEU A  72     8861  10200   7924   -721    600   -231       C\\nATOM    273  CD1 LEU A  72       8.795  12.745  14.308  1.00 68.45           C\\nANISOU  273  CD1 LEU A  72     8719   9732   7557   -638    454   -157       C\\nATOM    274  CD2 LEU A  72       7.449  13.618  12.399  1.00 69.98           C\\nANISOU  274  CD2 LEU A  72     8565   9884   8138   -488    531   -351       C\\nATOM    275  N   ILE A  73       5.112   8.562  12.866  1.00 69.01           N\\nANISOU  275  N   ILE A  73     8906  10062   7254  -1697    844    397       N\\nATOM    276  CA  ILE A  73       4.844   7.288  12.214  1.00 67.68           C\\nANISOU  276  CA  ILE A  73     8907   9691   7118  -1917    795    618       C\\nATOM    277  C   ILE A  73       3.522   7.340  11.460  1.00 71.94           C\\nANISOU  277  C   ILE A  73     9183  10422   7728  -2023    929    489       C\\nATOM    278  O   ILE A  73       3.411   6.809  10.350  1.00 75.02           O\\nANISOU  278  O   ILE A  73     9617  10582   8307  -2015    856    546       O\\nATOM    279  CB  ILE A  73       4.880   6.148  13.249  1.00 69.17           C\\nANISOU  279  CB  ILE A  73     9379   9898   7006  -2275    759    894       C\\nATOM    280  CG1 ILE A  73       6.327   5.743  13.542  1.00 66.13           C\\nANISOU  280  CG1 ILE A  73     9319   9150   6659  -2128    522   1069       C\\nATOM    281  CG2 ILE A  73       4.072   4.944  12.777  1.00 68.47           C\\nANISOU  281  CG2 ILE A  73     9386   9730   6900  -2615    755   1076       C\\nATOM    282  CD1 ILE A  73       6.453   4.548  14.461  1.00 67.07           C\\nANISOU  282  CD1 ILE A  73     9782   9188   6514  -2462    402   1387       C\\nATOM    283  N   VAL A  74       2.507   7.996  12.029  1.00 70.79           N\\nANISOU  283  N   VAL A  74     8739  10720   7436  -2102   1115    280       N\\nATOM    284  CA  VAL A  74       1.244   8.128  11.308  1.00 74.58           C\\nANISOU  284  CA  VAL A  74     8921  11407   8009  -2166   1221    118       C\\nATOM    285  C   VAL A  74       1.392   9.116  10.161  1.00 73.54           C\\nANISOU  285  C   VAL A  74     8633  11099   8211  -1776   1127    -73       C\\nATOM    286  O   VAL A  74       0.708   8.995   9.137  1.00 75.63           O\\nANISOU  286  O   VAL A  74     8769  11334   8631  -1776   1112   -121       O\\nATOM    287  CB  VAL A  74       0.095   8.527  12.256  1.00 73.62           C\\nANISOU  287  CB  VAL A  74     8477  11862   7633  -2350   1446    -95       C\\nATOM    288  CG1 VAL A  74       0.133   7.692  13.523  1.00 69.23           C\\nANISOU  288  CG1 VAL A  74     8110  11512   6684  -2747   1535    127       C\\nATOM    289  CG2 VAL A  74       0.126  10.011  12.581  1.00 69.08           C\\nANISOU  289  CG2 VAL A  74     7641  11478   7130  -1988   1471   -451       C\\nATOM    290  N   SER A  75       2.276  10.106  10.306  1.00 69.43           N\\nANISOU  290  N   SER A  75     8129  10455   7797  -1464   1043   -169       N\\nATOM    291  CA  SER A  75       2.644  10.933   9.164  1.00 66.75           C\\nANISOU  291  CA  SER A  75     7729   9871   7764  -1146    912   -253       C\\nATOM    292  C   SER A  75       3.278  10.082   8.075  1.00 68.29           C\\nANISOU  292  C   SER A  75     8151   9714   8082  -1158    801    -30       C\\nATOM    293  O   SER A  75       3.025  10.291   6.882  1.00 67.91           O\\nANISOU  293  O   SER A  75     8025   9564   8214  -1048    739    -65       O\\nATOM    294  CB  SER A  75       3.595  12.044   9.605  1.00 65.59           C\\nANISOU  294  CB  SER A  75     7599   9627   7697   -876    823   -350       C\\nATOM    295  OG  SER A  75       4.148  12.722   8.492  1.00 65.64           O\\nANISOU  295  OG  SER A  75     7609   9355   7975   -636    678   -344       O\\nATOM    296  N   LEU A  76       4.099   9.107   8.470  1.00 69.61           N\\nANISOU  296  N   LEU A  76     8600   9702   8145  -1281    755    185       N\\nATOM    297  CA  LEU A  76       4.653   8.169   7.503  1.00 70.39           C\\nANISOU  297  CA  LEU A  76     8904   9490   8352  -1284    641    344       C\\nATOM    298  C   LEU A  76       3.555   7.304   6.898  1.00 71.56           C\\nANISOU  298  C   LEU A  76     9015   9685   8488  -1514    675    369       C\\nATOM    299  O   LEU A  76       3.587   6.994   5.700  1.00 67.72           O\\nANISOU  299  O   LEU A  76     8556   9030   8146  -1442    597    372       O\\nATOM    300  CB  LEU A  76       5.725   7.307   8.170  1.00 71.65           C\\nANISOU  300  CB  LEU A  76     9365   9437   8421  -1339    541    534       C\\nATOM    301  CG  LEU A  76       6.488   6.311   7.296  1.00 73.93           C\\nANISOU  301  CG  LEU A  76     9872   9386   8833  -1283    387    648       C\\nATOM    302  CD1 LEU A  76       7.050   6.993   6.057  1.00 66.82           C\\nANISOU  302  CD1 LEU A  76     8859   8395   8135  -1003    352    542       C\\nATOM    303  CD2 LEU A  76       7.598   5.643   8.104  1.00 66.32           C\\nANISOU  303  CD2 LEU A  76     9178   8218   7804  -1274    247    796       C\\nATOM    304  N   ALA A  77       2.567   6.918   7.708  1.00 76.17           N\\nANISOU  304  N   ALA A  77     9525  10531   8886  -1810    794    379       N\\nATOM    305  CA  ALA A  77       1.468   6.103   7.203  1.00 75.85           C\\nANISOU  305  CA  ALA A  77     9422  10562   8836  -2078    825    401       C\\nATOM    306  C   ALA A  77       0.603   6.875   6.217  1.00 76.40           C\\nANISOU  306  C   ALA A  77     9182  10781   9066  -1929    853    183       C\\nATOM    307  O   ALA A  77       0.034   6.277   5.295  1.00 74.94           O\\nANISOU  307  O   ALA A  77     8980  10529   8965  -2027    802    189       O\\nATOM    308  CB  ALA A  77       0.618   5.589   8.364  1.00 77.54           C\\nANISOU  308  CB  ALA A  77     9590  11086   8784  -2476    967    470       C\\nATOM    309  N   VAL A  78       0.484   8.192   6.395  1.00 72.57           N\\nANISOU  309  N   VAL A  78     8462  10479   8634  -1687    898    -17       N\\nATOM    310  CA  VAL A  78      -0.263   9.001   5.438  1.00 73.72           C\\nANISOU  310  CA  VAL A  78     8340  10714   8956  -1502    861   -213       C\\nATOM    311  C   VAL A  78       0.492   9.092   4.118  1.00 73.77           C\\nANISOU  311  C   VAL A  78     8495  10392   9143  -1286    699   -137       C\\nATOM    312  O   VAL A  78      -0.108   9.025   3.037  1.00 75.36           O\\nANISOU  312  O   VAL A  78     8606  10583   9444  -1265    631   -185       O\\nATOM    313  CB  VAL A  78      -0.556  10.391   6.030  1.00 69.67           C\\nANISOU  313  CB  VAL A  78     7563  10433   8477  -1281    899   -460       C\\nATOM    314  CG1 VAL A  78      -1.042  11.346   4.951  1.00 67.83           C\\nANISOU  314  CG1 VAL A  78     7129  10169   8475  -1016    769   -625       C\\nATOM    315  CG2 VAL A  78      -1.591  10.281   7.138  1.00 54.88           C\\nANISOU  315  CG2 VAL A  78     5447   9002   6402  -1505   1086   -609       C\\nATOM    316  N   ALA A  79       1.819   9.239   4.180  1.00 71.40           N\\nANISOU  316  N   ALA A  79     8408   9854   8865  -1136    637    -25       N\\nATOM    317  CA  ALA A  79       2.617   9.243   2.959  1.00 72.25           C\\nANISOU  317  CA  ALA A  79     8642   9715   9095   -969    515     48       C\\nATOM    318  C   ALA A  79       2.382   7.976   2.148  1.00 78.12           C\\nANISOU  318  C   ALA A  79     9512  10348   9824  -1122    472    118       C\\nATOM    319  O   ALA A  79       2.254   8.030   0.919  1.00 82.23           O\\nANISOU  319  O   ALA A  79    10005  10818  10420  -1035    394     87       O\\nATOM    320  CB  ALA A  79       4.097   9.398   3.301  1.00 67.24           C\\nANISOU  320  CB  ALA A  79     8191   8894   8464   -836    476    149       C\\nATOM    321  N   ASP A  80       2.306   6.826   2.820  1.00 70.96           N\\nANISOU  321  N   ASP A  80     8756   9392   8812  -1362    499    214       N\\nATOM    322  CA  ASP A  80       2.041   5.580   2.113  1.00 74.85           C\\nANISOU  322  CA  ASP A  80     9387   9736   9318  -1522    420    263       C\\nATOM    323  C   ASP A  80       0.578   5.468   1.707  1.00 70.40           C\\nANISOU  323  C   ASP A  80     8610   9377   8763  -1703    452    165       C\\nATOM    324  O   ASP A  80       0.275   4.919   0.641  1.00 75.04           O\\nANISOU  324  O   ASP A  80     9225   9874   9413  -1725    358    129       O\\nATOM    325  CB  ASP A  80       2.453   4.386   2.975  1.00 85.13           C\\nANISOU  325  CB  ASP A  80    10957  10859  10529  -1735    379    424       C\\nATOM    326  CG  ASP A  80       3.955   4.316   3.193  1.00 91.73           C\\nANISOU  326  CG  ASP A  80    12008  11459  11389  -1526    293    497       C\\nATOM    327  OD1 ASP A  80       4.707   4.814   2.326  1.00 90.12           O\\nANISOU  327  OD1 ASP A  80    11774  11187  11279  -1257    253    424       O\\nATOM    328  OD2 ASP A  80       4.383   3.762   4.231  1.00 93.76           O\\nANISOU  328  OD2 ASP A  80    12452  11616  11555  -1644    259    631       O\\nATOM    329  N   LEU A  81      -0.340   5.974   2.535  1.00 74.65           N\\nANISOU  329  N   LEU A  81     8912  10218   9233  -1827    580     91       N\\nATOM    330  CA  LEU A  81      -1.751   5.961   2.159  1.00 71.55           C\\nANISOU  330  CA  LEU A  81     8249  10074   8865  -1978    612    -40       C\\nATOM    331  C   LEU A  81      -2.001   6.765   0.893  1.00 74.65           C\\nANISOU  331  C   LEU A  81     8488  10471   9406  -1709    505   -178       C\\nATOM    332  O   LEU A  81      -2.886   6.418   0.105  1.00 69.21           O\\nANISOU  332  O   LEU A  81     7680   9851   8766  -1803    444   -254       O\\nATOM    333  CB  LEU A  81      -2.611   6.504   3.297  1.00 69.87           C\\nANISOU  333  CB  LEU A  81     7752  10250   8545  -2106    782   -153       C\\nATOM    334  CG  LEU A  81      -3.075   5.485   4.331  1.00 74.99           C\\nANISOU  334  CG  LEU A  81     8452  11043   8999  -2544    901    -27       C\\nATOM    335  CD1 LEU A  81      -3.852   6.179   5.437  1.00 74.69           C\\nANISOU  335  CD1 LEU A  81     8087  11477   8814  -2632   1099   -186       C\\nATOM    336  CD2 LEU A  81      -3.924   4.409   3.669  1.00 73.03           C\\nANISOU  336  CD2 LEU A  81     8197  10767   8785  -2854    842     14       C\\nATOM    337  N   LEU A  82      -1.237   7.838   0.678  1.00 69.87           N\\nANISOU  337  N   LEU A  82     7892   9789   8867  -1397    460   -196       N\\nATOM    338  CA  LEU A  82      -1.409   8.637  -0.529  1.00 65.99           C\\nANISOU  338  CA  LEU A  82     7299   9280   8492  -1167    327   -272       C\\nATOM    339  C   LEU A  82      -0.757   7.982  -1.740  1.00 70.21           C\\nANISOU  339  C   LEU A  82     8057   9596   9025  -1131    218   -180       C\\nATOM    340  O   LEU A  82      -1.178   8.231  -2.875  1.00 71.57           O\\nANISOU  340  O   LEU A  82     8160   9794   9239  -1047    101   -233       O\\nATOM    341  CB  LEU A  82      -0.848  10.040  -0.313  1.00 59.37           C\\nANISOU  341  CB  LEU A  82     6407   8421   7728   -892    291   -300       C\\nATOM    342  CG  LEU A  82      -1.644  10.851   0.706  1.00 62.33           C\\nANISOU  342  CG  LEU A  82     6510   9044   8130   -856    360   -482       C\\nATOM    343  CD1 LEU A  82      -1.091  12.261   0.855  1.00 55.10           C\\nANISOU  343  CD1 LEU A  82     5564   8044   7327   -570    267   -530       C\\nATOM    344  CD2 LEU A  82      -3.114  10.883   0.314  1.00 64.42           C\\nANISOU  344  CD2 LEU A  82     6475   9550   8451   -907    325   -667       C\\nATOM    345  N   VAL A  83       0.261   7.147  -1.524  1.00 71.76           N\\nANISOU  345  N   VAL A  83     8510   9592   9162  -1179    238    -64       N\\nATOM    346  CA  VAL A  83       0.813   6.355  -2.620  1.00 69.53           C\\nANISOU  346  CA  VAL A  83     8414   9139   8867  -1147    140    -43       C\\nATOM    347  C   VAL A  83      -0.238   5.394  -3.158  1.00 73.89           C\\nANISOU  347  C   VAL A  83     8937   9715   9422  -1353     76   -116       C\\nATOM    348  O   VAL A  83      -0.404   5.247  -4.375  1.00 79.13           O\\nANISOU  348  O   VAL A  83     9606  10373  10087  -1289    -32   -185       O\\nATOM    349  CB  VAL A  83       2.078   5.608  -2.159  1.00 61.51           C\\nANISOU  349  CB  VAL A  83     7653   7900   7818  -1130    147     49       C\\nATOM    350  CG1 VAL A  83       2.537   4.623  -3.222  1.00 56.33           C\\nANISOU  350  CG1 VAL A  83     7164   7084   7153  -1094     37      1       C\\nATOM    351  CG2 VAL A  83       3.187   6.592  -1.827  1.00 55.01           C\\nANISOU  351  CG2 VAL A  83     6836   7065   7001   -921    189    106       C\\nATOM    352  N   ALA A  84      -0.973   4.732  -2.264  1.00 63.07           N\\nANISOU  352  N   ALA A  84     7532   8393   8036  -1628    136   -100       N\\nATOM    353  CA  ALA A  84      -1.979   3.777  -2.713  1.00 68.51           C\\nANISOU  353  CA  ALA A  84     8190   9097   8744  -1877     65   -159       C\\nATOM    354  C   ALA A  84      -3.109   4.458  -3.475  1.00 67.78           C\\nANISOU  354  C   ALA A  84     7803   9251   8701  -1831     21   -306       C\\nATOM    355  O   ALA A  84      -3.668   3.871  -4.408  1.00 63.21           O\\nANISOU  355  O   ALA A  84     7217   8653   8146  -1911   -101   -386       O\\nATOM    356  CB  ALA A  84      -2.540   3.003  -1.520  1.00 70.03           C\\nANISOU  356  CB  ALA A  84     8393   9327   8888  -2241    149    -72       C\\nATOM    357  N   THR A  85      -3.449   5.692  -3.108  1.00 59.88           N\\nANISOU  357  N   THR A  85     6561   8463   7726  -1685     85   -362       N\\nATOM    358  CA  THR A  85      -4.630   6.368  -3.632  1.00 70.05           C\\nANISOU  358  CA  THR A  85     7536   9994   9087  -1632     16   -521       C\\nATOM    359  C   THR A  85      -4.329   7.352  -4.758  1.00 73.23           C\\nANISOU  359  C   THR A  85     7938  10354   9531  -1316   -140   -540       C\\nATOM    360  O   THR A  85      -5.144   7.493  -5.674  1.00 73.60           O\\nANISOU  360  O   THR A  85     7844  10501   9619  -1283   -285   -640       O\\nATOM    361  CB  THR A  85      -5.355   7.103  -2.501  1.00 66.86           C\\nANISOU  361  CB  THR A  85     6829   9873   8704  -1660    148   -625       C\\nATOM    362  OG1 THR A  85      -4.432   7.958  -1.812  1.00 68.22           O\\nANISOU  362  OG1 THR A  85     7080   9977   8864  -1454    215   -567       O\\nATOM    363  CG2 THR A  85      -5.948   6.109  -1.519  1.00 61.69           C\\nANISOU  363  CG2 THR A  85     6117   9358   7964  -2054    299   -604       C\\nATOM    364  N   LEU A  86      -3.186   8.043  -4.718  1.00 62.95           N\\nANISOU  364  N   LEU A  86     6792   8914   8211  -1106   -129   -431       N\\nATOM    365  CA  LEU A  86      -2.875   9.074  -5.699  1.00 69.96           C\\nANISOU  365  CA  LEU A  86     7691   9770   9119   -857   -279   -398       C\\nATOM    366  C   LEU A  86      -1.823   8.663  -6.718  1.00 73.74           C\\nANISOU  366  C   LEU A  86     8430  10102   9484   -805   -327   -290       C\\nATOM    367  O   LEU A  86      -1.627   9.386  -7.700  1.00 78.44           O\\nANISOU  367  O   LEU A  86     9050  10709  10044   -662   -458   -237       O\\nATOM    368  CB  LEU A  86      -2.400  10.356  -5.000  1.00 71.90           C\\nANISOU  368  CB  LEU A  86     7888   9995   9438   -669   -260   -361       C\\nATOM    369  CG  LEU A  86      -3.358  11.015  -4.012  1.00 70.39           C\\nANISOU  369  CG  LEU A  86     7407   9983   9357   -640   -226   -527       C\\nATOM    370  CD1 LEU A  86      -2.805  12.358  -3.572  1.00 66.08           C\\nANISOU  370  CD1 LEU A  86     6851   9355   8902   -408   -280   -511       C\\nATOM    371  CD2 LEU A  86      -4.735  11.169  -4.633  1.00 73.10           C\\nANISOU  371  CD2 LEU A  86     7488  10505   9781   -625   -371   -694       C\\nATOM    372  N   VAL A  87      -1.137   7.538  -6.512  1.00 71.08           N\\nANISOU  372  N   VAL A  87     8285   9640   9081   -916   -240   -262       N\\nATOM    373  CA  VAL A  87      -0.068   7.087  -7.395  1.00 73.29           C\\nANISOU  373  CA  VAL A  87     8777   9820   9251   -840   -268   -222       C\\nATOM    374  C   VAL A  87      -0.364   5.702  -7.963  1.00 77.64           C\\nANISOU  374  C   VAL A  87     9430  10309   9760   -973   -330   -334       C\\nATOM    375  O   VAL A  87      -0.313   5.497  -9.179  1.00 73.98           O\\nANISOU  375  O   VAL A  87     9018   9892   9199   -916   -433   -399       O\\nATOM    376  CB  VAL A  87       1.295   7.094  -6.673  1.00 71.74           C\\nANISOU  376  CB  VAL A  87     8723   9494   9039   -769   -152   -126       C\\nATOM    377  CG1 VAL A  87       2.408   6.688  -7.635  1.00 74.66           C\\nANISOU  377  CG1 VAL A  87     9249   9829   9290   -667   -171   -133       C\\nATOM    378  CG2 VAL A  87       1.561   8.458  -6.054  1.00 66.12           C\\nANISOU  378  CG2 VAL A  87     7914   8818   8388   -656   -114    -33       C\\nATOM    379  N   MET A  88      -0.666   4.743  -7.091  1.00 80.11           N\\nANISOU  379  N   MET A  88     9788  10515  10136  -1166   -284   -354       N\\nATOM    380  CA  MET A  88      -0.910   3.374  -7.543  1.00 77.27           C\\nANISOU  380  CA  MET A  88     9560  10025   9773  -1313   -382   -456       C\\nATOM    381  C   MET A  88      -2.014   3.257  -8.587  1.00 74.77           C\\nANISOU  381  C   MET A  88     9120   9842   9447  -1377   -521   -585       C\\nATOM    382  O   MET A  88      -1.856   2.434  -9.508  1.00 75.54           O\\nANISOU  382  O   MET A  88     9351   9858   9492  -1370   -641   -704       O\\nATOM    383  CB  MET A  88      -1.213   2.478  -6.335  1.00 80.86           C\\nANISOU  383  CB  MET A  88    10082  10339  10303  -1575   -337   -400       C\\nATOM    384  CG  MET A  88      -0.060   2.322  -5.349  1.00 81.25           C\\nANISOU  384  CG  MET A  88    10311  10211  10350  -1521   -256   -278       C\\nATOM    385  SD  MET A  88       1.427   1.569  -6.040  1.00 83.45           S\\nANISOU  385  SD  MET A  88    10860  10245  10603  -1297   -355   -350       S\\nATOM    386  CE  MET A  88       0.780   0.002  -6.622  1.00 86.55           C\\nANISOU  386  CE  MET A  88    11408  10421  11056  -1493   -560   -493       C\\nATOM    387  N   PRO A  89      -3.134   3.998  -8.521  1.00 73.85           N\\nANISOU  387  N   PRO A  89     8745   9932   9382  -1424   -534   -603       N\\nATOM    388  CA  PRO A  89      -4.103   3.930  -9.629  1.00 74.48           C\\nANISOU  388  CA  PRO A  89     8707  10146   9448  -1448   -704   -735       C\\nATOM    389  C   PRO A  89      -3.480   4.213 -10.985  1.00 73.67           C\\nANISOU  389  C   PRO A  89     8725  10074   9192  -1237   -816   -758       C\\nATOM    390  O   PRO A  89      -3.834   3.559 -11.972  1.00 74.04           O\\nANISOU  390  O   PRO A  89     8817  10141   9174  -1277   -962   -893       O\\nATOM    391  CB  PRO A  89      -5.142   4.990  -9.248  1.00 73.14           C\\nANISOU  391  CB  PRO A  89     8221  10200   9368  -1431   -703   -747       C\\nATOM    392  CG  PRO A  89      -5.085   5.041  -7.779  1.00 71.74           C\\nANISOU  392  CG  PRO A  89     7982  10016   9258  -1543   -514   -680       C\\nATOM    393  CD  PRO A  89      -3.645   4.834  -7.418  1.00 67.98           C\\nANISOU  393  CD  PRO A  89     7787   9325   8719  -1455   -417   -550       C\\nATOM    394  N   TRP A  90      -2.552   5.170 -11.056  1.00 69.93           N\\nANISOU  394  N   TRP A  90     8302   9624   8643  -1037   -753   -630       N\\nATOM    395  CA  TRP A  90      -1.831   5.402 -12.301  1.00 70.06           C\\nANISOU  395  CA  TRP A  90     8440   9716   8463   -885   -824   -623       C\\nATOM    396  C   TRP A  90      -0.927   4.229 -12.652  1.00 73.43           C\\nANISOU  396  C   TRP A  90     9074  10033   8794   -879   -795   -740       C\\nATOM    397  O   TRP A  90      -0.713   3.948 -13.836  1.00 80.52           O\\nANISOU  397  O   TRP A  90    10046  11036   9511   -815   -885   -849       O\\nATOM    398  CB  TRP A  90      -0.996   6.677 -12.206  1.00 72.68           C\\nANISOU  398  CB  TRP A  90     8778  10094   8744   -730   -758   -431       C\\nATOM    399  CG  TRP A  90      -1.743   7.924 -11.827  1.00 78.23           C\\nANISOU  399  CG  TRP A  90     9301  10853   9571   -681   -825   -337       C\\nATOM    400  CD1 TRP A  90      -2.061   8.338 -10.567  1.00 78.70           C\\nANISOU  400  CD1 TRP A  90     9229  10858   9814   -696   -738   -319       C\\nATOM    401  CD2 TRP A  90      -2.229   8.939 -12.716  1.00 88.37           C\\nANISOU  401  CD2 TRP A  90    10523  12253  10801   -588  -1022   -264       C\\nATOM    402  NE1 TRP A  90      -2.729   9.539 -10.616  1.00 79.87           N\\nANISOU  402  NE1 TRP A  90     9218  11075  10052   -589   -872   -284       N\\nATOM    403  CE2 TRP A  90      -2.844   9.929 -11.925  1.00 85.91           C\\nANISOU  403  CE2 TRP A  90    10036  11918  10690   -521  -1067   -232       C\\nATOM    404  CE3 TRP A  90      -2.213   9.101 -14.106  1.00 93.09           C\\nANISOU  404  CE3 TRP A  90    11205  12978  11187   -553  -1185   -228       C\\nATOM    405  CZ2 TRP A  90      -3.436  11.064 -12.476  1.00 91.05           C\\nANISOU  405  CZ2 TRP A  90    10603  12614  11379   -398  -1303   -166       C\\nATOM    406  CZ3 TRP A  90      -2.801  10.229 -14.651  1.00 88.71           C\\nANISOU  406  CZ3 TRP A  90    10584  12483  10637   -467  -1412   -117       C\\nATOM    407  CH2 TRP A  90      -3.404  11.195 -13.838  1.00 91.05           C\\nANISOU  407  CH2 TRP A  90    10716  12700  11179   -380  -1486    -87       C\\nATOM    408  N   VAL A  91      -0.382   3.540 -11.646  1.00 69.25           N\\nANISOU  408  N   VAL A  91     8640   9297   8374   -930   -690   -736       N\\nATOM    409  CA  VAL A  91       0.555   2.453 -11.912  1.00 71.26           C\\nANISOU  409  CA  VAL A  91     9090   9406   8578   -872   -701   -873       C\\nATOM    410  C   VAL A  91      -0.181   1.188 -12.341  1.00 81.86           C\\nANISOU  410  C   VAL A  91    10506  10626   9969  -1010   -867  -1076       C\\nATOM    411  O   VAL A  91       0.272   0.468 -13.239  1.00 84.97           O\\nANISOU  411  O   VAL A  91    11020  11005  10261   -913   -961  -1279       O\\nATOM    412  CB  VAL A  91       1.447   2.203 -10.683  1.00 66.23           C\\nANISOU  412  CB  VAL A  91     8549   8562   8051   -856   -583   -782       C\\nATOM    413  CG1 VAL A  91       2.331   0.984 -10.905  1.00 66.75           C\\nANISOU  413  CG1 VAL A  91     8812   8434   8116   -769   -652   -961       C\\nATOM    414  CG2 VAL A  91       2.295   3.427 -10.395  1.00 71.66           C\\nANISOU  414  CG2 VAL A  91     9171   9373   8685   -712   -442   -614       C\\nATOM    415  N   VAL A  92      -1.320   0.890 -11.713  1.00 76.99           N\\nANISOU  415  N   VAL A  92     9808   9938   9507  -1247   -911  -1047       N\\nATOM    416  CA  VAL A  92      -2.100  -0.267 -12.139  1.00 83.11           C\\nANISOU  416  CA  VAL A  92    10641  10591  10346  -1426  -1092  -1225       C\\nATOM    417  C   VAL A  92      -2.714  -0.014 -13.513  1.00 85.39           C\\nANISOU  417  C   VAL A  92    10837  11112  10496  -1365  -1232  -1373       C\\nATOM    418  O   VAL A  92      -2.760  -0.914 -14.362  1.00 87.20           O\\nANISOU  418  O   VAL A  92    11179  11274  10677  -1366  -1396  -1596       O\\nATOM    419  CB  VAL A  92      -3.160  -0.626 -11.077  1.00 86.97           C\\nANISOU  419  CB  VAL A  92    11035  10994  11015  -1752  -1083  -1133       C\\nATOM    420  CG1 VAL A  92      -4.059   0.557 -10.774  1.00 88.40           C\\nANISOU  420  CG1 VAL A  92    10916  11464  11208  -1788   -990  -1030       C\\nATOM    421  CG2 VAL A  92      -3.984  -1.823 -11.526  1.00 90.14           C\\nANISOU  421  CG2 VAL A  92    11495  11253  11500  -1988  -1291  -1301       C\\nATOM    422  N   TYR A  93      -3.173   1.217 -13.762  1.00 86.77           N\\nANISOU  422  N   TYR A  93    10817  11548  10602  -1298  -1201  -1261       N\\nATOM    423  CA  TYR A  93      -3.600   1.598 -15.106  1.00 83.84           C\\nANISOU  423  CA  TYR A  93    10389  11409  10056  -1209  -1354  -1357       C\\nATOM    424  C   TYR A  93      -2.477   1.379 -16.111  1.00 80.40           C\\nANISOU  424  C   TYR A  93    10133  11042   9375  -1017  -1359  -1466       C\\nATOM    425  O   TYR A  93      -2.706   0.878 -17.219  1.00 74.40           O\\nANISOU  425  O   TYR A  93     9423  10381   8465   -997  -1517  -1669       O\\nATOM    426  CB  TYR A  93      -4.062   3.059 -15.102  1.00 86.78           C\\nANISOU  426  CB  TYR A  93    10567  11993  10412  -1130  -1345  -1178       C\\nATOM    427  CG  TYR A  93      -4.289   3.683 -16.465  1.00 96.56           C\\nANISOU  427  CG  TYR A  93    11788  13469  11430  -1012  -1516  -1193       C\\nATOM    428  CD1 TYR A  93      -5.528   3.603 -17.096  1.00 94.66           C\\nANISOU  428  CD1 TYR A  93    11412  13349  11207  -1088  -1737  -1310       C\\nATOM    429  CD2 TYR A  93      -3.274   4.383 -17.106  1.00 98.40           C\\nANISOU  429  CD2 TYR A  93    12135  13829  11423   -849  -1468  -1073       C\\nATOM    430  CE1 TYR A  93      -5.739   4.185 -18.334  1.00 95.59           C\\nANISOU  430  CE1 TYR A  93    11537  13682  11100   -983  -1926  -1302       C\\nATOM    431  CE2 TYR A  93      -3.475   4.965 -18.343  1.00 97.04           C\\nANISOU  431  CE2 TYR A  93    11974  13889  11007   -780  -1636  -1042       C\\nATOM    432  CZ  TYR A  93      -4.707   4.864 -18.952  1.00 96.39           C\\nANISOU  432  CZ  TYR A  93    11785  13900  10937   -837  -1876  -1153       C\\nATOM    433  OH  TYR A  93      -4.903   5.446 -20.182  1.00 95.53           O\\nANISOU  433  OH  TYR A  93    11712  14022  10562   -771  -2074  -1102       O\\nATOM    434  N   LEU A  94      -1.250   1.724 -15.722  1.00 88.56           N\\nANISOU  434  N   LEU A  94    11244  12051  10355   -879  -1185  -1358       N\\nATOM    435  CA  LEU A  94      -0.090   1.590 -16.592  1.00 90.25           C\\nANISOU  435  CA  LEU A  94    11571  12398  10320   -698  -1144  -1470       C\\nATOM    436  C   LEU A  94       0.187   0.143 -16.984  1.00 86.74           C\\nANISOU  436  C   LEU A  94    11276  11802   9879   -668  -1251  -1798       C\\nATOM    437  O   LEU A  94       0.806  -0.096 -18.027  1.00 79.60           O\\nANISOU  437  O   LEU A  94    10426  11091   8726   -524  -1274  -1999       O\\nATOM    438  CB  LEU A  94       1.131   2.192 -15.893  1.00 91.19           C\\nANISOU  438  CB  LEU A  94    11704  12504  10440   -587   -935  -1297       C\\nATOM    439  CG  LEU A  94       2.362   2.481 -16.745  1.00 96.59           C\\nANISOU  439  CG  LEU A  94    12420  13445  10836   -422   -839  -1342       C\\nATOM    440  CD1 LEU A  94       1.952   3.241 -17.987  1.00 95.48           C\\nANISOU  440  CD1 LEU A  94    12233  13639  10407   -435   -921  -1281       C\\nATOM    441  CD2 LEU A  94       3.366   3.277 -15.931  1.00 94.01           C\\nANISOU  441  CD2 LEU A  94    12057  13105  10556   -364   -648  -1120       C\\nATOM    442  N   GLU A  95      -0.244  -0.827 -16.175  1.00 91.64           N\\nANISOU  442  N   GLU A  95    11967  12086  10767   -809  -1328  -1863       N\\nATOM    443  CA  GLU A  95      -0.007  -2.228 -16.505  1.00 89.73           C\\nANISOU  443  CA  GLU A  95    11897  11617  10578   -779  -1491  -2179       C\\nATOM    444  C   GLU A  95      -1.104  -2.803 -17.392  1.00 87.68           C\\nANISOU  444  C   GLU A  95    11631  11388  10293   -904  -1724  -2391       C\\nATOM    445  O   GLU A  95      -0.812  -3.568 -18.317  1.00 89.77           O\\nANISOU  445  O   GLU A  95    12002  11667  10441   -784  -1865  -2717       O\\nATOM    446  CB  GLU A  95       0.121  -3.065 -15.229  1.00 87.59           C\\nANISOU  446  CB  GLU A  95    11758  10917  10607   -899  -1515  -2120       C\\nATOM    447  CG  GLU A  95       0.439  -4.539 -15.480  1.00 93.67           C\\nANISOU  447  CG  GLU A  95    12747  11357  11487   -851  -1741  -2438       C\\nATOM    448  CD  GLU A  95       1.851  -4.758 -16.002  1.00102.62           C\\nANISOU  448  CD  GLU A  95    13952  12557  12482   -504  -1707  -2681       C\\nATOM    449  OE1 GLU A  95       2.722  -3.902 -15.740  1.00104.20           O\\nANISOU  449  OE1 GLU A  95    14062  12957  12571   -357  -1484  -2527       O\\nATOM    450  OE2 GLU A  95       2.093  -5.788 -16.670  1.00107.64           O\\nANISOU  450  OE2 GLU A  95    14717  13056  13125   -376  -1910  -3051       O\\nATOM    451  N   VAL A  96      -2.362  -2.449 -17.129  1.00 78.94           N\\nANISOU  451  N   VAL A  96    10382  10316   9297  -1131  -1774  -2245       N\\nATOM    452  CA  VAL A  96      -3.462  -2.952 -17.947  1.00 80.52           C\\nANISOU  452  CA  VAL A  96    10543  10563   9488  -1267  -2011  -2444       C\\nATOM    453  C   VAL A  96      -3.331  -2.439 -19.375  1.00 85.05           C\\nANISOU  453  C   VAL A  96    11087  11511   9717  -1081  -2072  -2578       C\\nATOM    454  O   VAL A  96      -3.404  -3.209 -20.340  1.00 82.90           O\\nANISOU  454  O   VAL A  96    10906  11266   9327  -1037  -2258  -2893       O\\nATOM    455  CB  VAL A  96      -4.816  -2.561 -17.328  1.00 77.18           C\\nANISOU  455  CB  VAL A  96     9907  10166   9251  -1538  -2032  -2265       C\\nATOM    456  N   VAL A  97      -3.117  -1.130 -19.528  1.00 87.40           N\\nANISOU  456  N   VAL A  97    11271  12099   9836   -979  -1932  -2336       N\\nATOM    457  CA  VAL A  97      -2.995  -0.529 -20.854  1.00 88.86           C\\nANISOU  457  CA  VAL A  97    11446  12664   9653   -847  -1994  -2384       C\\nATOM    458  C   VAL A  97      -1.719  -0.983 -21.554  1.00 90.16           C\\nANISOU  458  C   VAL A  97    11752  12956   9548   -647  -1919  -2608       C\\nATOM    459  O   VAL A  97      -1.694  -1.122 -22.783  1.00 92.93           O\\nANISOU  459  O   VAL A  97    12140  13588   9583   -572  -2028  -2817       O\\nATOM    460  CB  VAL A  97      -3.061   1.005 -20.740  1.00 86.80           C\\nANISOU  460  CB  VAL A  97    11060  12617   9305   -817  -1897  -2025       C\\nATOM    461  CG1 VAL A  97      -2.893   1.659 -22.106  1.00 88.76           C\\nANISOU  461  CG1 VAL A  97    11335  13252   9139   -721  -1981  -2009       C\\nATOM    462  CG2 VAL A  97      -4.372   1.434 -20.086  1.00 86.16           C\\nANISOU  462  CG2 VAL A  97    10792  12448   9495   -970  -1990  -1884       C\\nATOM    463  N   GLY A  98      -0.650  -1.230 -20.800  1.00 88.15           N\\nANISOU  463  N   GLY A  98    11562  12531   9400   -550  -1740  -2596       N\\nATOM    464  CA  GLY A  98       0.613  -1.604 -21.402  1.00 89.34           C\\nANISOU  464  CA  GLY A  98    11789  12846   9310   -334  -1652  -2837       C\\nATOM    465  C   GLY A  98       1.360  -0.469 -22.059  1.00 91.48           C\\nANISOU  465  C   GLY A  98    11987  13570   9202   -247  -1473  -2660       C\\nATOM    466  O   GLY A  98       2.307  -0.717 -22.810  1.00 93.59           O\\nANISOU  466  O   GLY A  98    12270  14114   9177    -92  -1395  -2892       O\\nATOM    467  N   GLU A  99       0.962   0.772 -21.797  1.00 93.52           N\\nANISOU  467  N   GLU A  99    12159  13918   9455   -352  -1418  -2264       N\\nATOM    468  CA  GLU A  99       1.609   1.938 -22.378  1.00 95.54           C\\nANISOU  468  CA  GLU A  99    12373  14557   9372   -328  -1286  -2022       C\\nATOM    469  C   GLU A  99       1.259   3.151 -21.529  1.00 92.97           C\\nANISOU  469  C   GLU A  99    11976  14105   9244   -422  -1241  -1593       C\\nATOM    470  O   GLU A  99       0.253   3.163 -20.815  1.00 85.82           O\\nANISOU  470  O   GLU A  99    11021  12937   8648   -506  -1345  -1519       O\\nATOM    471  CB  GLU A  99       1.181   2.153 -23.835  1.00 94.86           C\\nANISOU  471  CB  GLU A  99    12308  14866   8868   -355  -1437  -2092       C\\nATOM    472  N   TRP A 100       2.110   4.174 -21.614  1.00 89.68           N\\nANISOU  472  N   TRP A 100    11539  13894   8642   -414  -1089  -1330       N\\nATOM    473  CA  TRP A 100       1.871   5.446 -20.932  1.00 88.27           C\\nANISOU  473  CA  TRP A 100    11308  13606   8625   -483  -1080   -935       C\\nATOM    474  C   TRP A 100       0.892   6.302 -21.742  1.00 91.37           C\\nANISOU  474  C   TRP A 100    11702  14149   8867   -556  -1315   -744       C\\nATOM    475  O   TRP A 100       1.217   7.382 -22.236  1.00 95.09           O\\nANISOU  475  O   TRP A 100    12204  14809   9115   -605  -1334   -453       O\\nATOM    476  CB  TRP A 100       3.188   6.177 -20.702  1.00 86.77           C\\nANISOU  476  CB  TRP A 100    11107  13540   8322   -471   -861   -729       C\\nATOM    477  CG  TRP A 100       4.148   5.471 -19.784  1.00 92.86           C\\nANISOU  477  CG  TRP A 100    11859  14140   9283   -376   -663   -888       C\\nATOM    478  CD1 TRP A 100       4.731   4.252 -19.983  1.00 99.53           C\\nANISOU  478  CD1 TRP A 100    12726  15011  10078   -261   -605  -1253       C\\nATOM    479  CD2 TRP A 100       4.655   5.958 -18.534  1.00 93.04           C\\nANISOU  479  CD2 TRP A 100    11841  13932   9577   -369   -533   -700       C\\nATOM    480  NE1 TRP A 100       5.558   3.944 -18.928  1.00 99.78           N\\nANISOU  480  NE1 TRP A 100    12740  14828  10345   -179   -465  -1286       N\\nATOM    481  CE2 TRP A 100       5.530   4.975 -18.027  1.00 94.10           C\\nANISOU  481  CE2 TRP A 100    11981  13965   9809   -254   -408   -944       C\\nATOM    482  CE3 TRP A 100       4.449   7.125 -17.792  1.00 92.42           C\\nANISOU  482  CE3 TRP A 100    11726  13714   9675   -431   -538   -373       C\\nATOM    483  CZ2 TRP A 100       6.198   5.125 -16.811  1.00 92.35           C\\nANISOU  483  CZ2 TRP A 100    11733  13525   9830   -217   -285   -845       C\\nATOM    484  CZ3 TRP A 100       5.114   7.273 -16.583  1.00 87.83           C\\nANISOU  484  CZ3 TRP A 100    11114  12928   9330   -397   -398   -300       C\\nATOM    485  CH2 TRP A 100       5.977   6.279 -16.107  1.00 90.94           C\\nANISOU  485  CH2 TRP A 100    11517  13244   9792   -299   -271   -522       C\\nATOM    486  N   LYS A 101      -0.329   5.791 -21.877  1.00 95.15           N\\nANISOU  486  N   LYS A 101    12148  14527   9477   -577  -1521   -906       N\\nATOM    487  CA  LYS A 101      -1.365   6.446 -22.678  1.00 96.45           C\\nANISOU  487  CA  LYS A 101    12300  14824   9522   -619  -1798   -787       C\\nATOM    488  C   LYS A 101      -2.121   7.498 -21.869  1.00 98.53           C\\nANISOU  488  C   LYS A 101    12457  14876  10104   -621  -1907   -529       C\\nATOM    489  O   LYS A 101      -3.351   7.502 -21.813  1.00100.15           O\\nANISOU  489  O   LYS A 101    12553  15004  10495   -628  -2120   -595       O\\nATOM    490  CB  LYS A 101      -2.319   5.405 -23.251  1.00 91.01           C\\nANISOU  490  CB  LYS A 101    11597  14158   8826   -638  -1991  -1116       C\\nATOM    491  N   PHE A 102      -1.377   8.397 -21.223  1.00 92.76           N\\nANISOU  491  N   PHE A 102    11736  14060   9449   -605  -1768   -264       N\\nATOM    492  CA  PHE A 102      -1.943   9.593 -20.620  1.00 93.22           C\\nANISOU  492  CA  PHE A 102    11716  13947   9756   -575  -1904    -18       C\\nATOM    493  C   PHE A 102      -1.857  10.735 -21.628  1.00 91.71           C\\nANISOU  493  C   PHE A 102    11641  13918   9287   -599  -2119    289       C\\nATOM    494  O   PHE A 102      -1.422  10.558 -22.768  1.00103.07           O\\nANISOU  494  O   PHE A 102    13204  15642  10313   -665  -2138    313       O\\nATOM    495  CB  PHE A 102      -1.202   9.983 -19.340  1.00 94.22           C\\nANISOU  495  CB  PHE A 102    11808  13862  10129   -551  -1677     95       C\\nATOM    496  CG  PHE A 102      -0.815   8.827 -18.469  1.00 91.97           C\\nANISOU  496  CG  PHE A 102    11490  13455  10000   -556  -1432   -141       C\\nATOM    497  CD1 PHE A 102      -1.737   8.243 -17.618  1.00 88.34           C\\nANISOU  497  CD1 PHE A 102    10903  12822   9841   -574  -1444   -314       C\\nATOM    498  CD2 PHE A 102       0.483   8.344 -18.477  1.00 88.17           C\\nANISOU  498  CD2 PHE A 102    11097  13037   9364   -553  -1204   -181       C\\nATOM    499  CE1 PHE A 102      -1.375   7.184 -16.805  1.00 84.23           C\\nANISOU  499  CE1 PHE A 102    10394  12156   9452   -611  -1257   -481       C\\nATOM    500  CE2 PHE A 102       0.849   7.286 -17.667  1.00 83.36           C\\nANISOU  500  CE2 PHE A 102    10485  12270   8917   -538  -1037   -386       C\\nATOM    501  CZ  PHE A 102      -0.082   6.706 -16.830  1.00 81.83           C\\nANISOU  501  CZ  PHE A 102    10213  11865   9014   -578  -1075   -513       C\\nATOM    502  N   SER A 103      -2.265  11.924 -21.210  1.00 88.70           N\\nANISOU  502  N   SER A 103    11226  13356   9120   -550  -2299    526       N\\nATOM    503  CA  SER A 103      -1.855  13.135 -21.896  1.00 82.43           C\\nANISOU  503  CA  SER A 103    10589  12620   8110   -603  -2476    904       C\\nATOM    504  C   SER A 103      -0.586  13.661 -21.237  1.00 83.13           C\\nANISOU  504  C   SER A 103    10732  12623   8230   -660  -2230   1106       C\\nATOM    505  O   SER A 103      -0.135  13.148 -20.210  1.00 83.31           O\\nANISOU  505  O   SER A 103    10661  12526   8466   -622  -1957    945       O\\nATOM    506  CB  SER A 103      -2.969  14.182 -21.869  1.00 79.20           C\\nANISOU  506  CB  SER A 103    10137  12018   7939   -498  -2879   1043       C\\nATOM    507  OG  SER A 103      -3.335  14.521 -20.542  1.00 76.16           O\\nANISOU  507  OG  SER A 103     9579  11344   8016   -372  -2840    955       O\\nATOM    508  N   ARG A 104       0.009  14.689 -21.845  1.00 84.27           N\\nANISOU  508  N   ARG A 104    11037  12833   8148   -776  -2344   1478       N\\nATOM    509  CA  ARG A 104       1.252  15.212 -21.290  1.00 80.60           C\\nANISOU  509  CA  ARG A 104    10612  12312   7701   -868  -2123   1679       C\\nATOM    510  C   ARG A 104       1.025  15.830 -19.921  1.00 77.44           C\\nANISOU  510  C   ARG A 104    10113  11518   7794   -740  -2150   1682       C\\nATOM    511  O   ARG A 104       1.913  15.783 -19.064  1.00 78.86           O\\nANISOU  511  O   ARG A 104    10250  11620   8096   -755  -1890   1666       O\\nATOM    512  CB  ARG A 104       1.881  16.231 -22.235  1.00 80.66           C\\nANISOU  512  CB  ARG A 104    10815  12469   7362  -1078  -2266   2114       C\\nATOM    513  CG  ARG A 104       3.382  16.383 -22.031  1.00 90.20           C\\nANISOU  513  CG  ARG A 104    12038  13815   8417  -1248  -1948   2260       C\\nATOM    514  CD  ARG A 104       3.766  17.736 -21.446  1.00101.17           C\\nANISOU  514  CD  ARG A 104    13504  14894  10041  -1329  -2089   2624       C\\nATOM    515  NE  ARG A 104       3.451  18.831 -22.359  1.00106.68           N\\nANISOU  515  NE  ARG A 104    14414  15562  10556  -1484  -2476   3046       N\\nATOM    516  CZ  ARG A 104       2.650  19.849 -22.059  1.00108.76           C\\nANISOU  516  CZ  ARG A 104    14758  15416  11150  -1381  -2885   3220       C\\nATOM    517  NH1 ARG A 104       2.092  19.927 -20.857  1.00104.63           N\\nANISOU  517  NH1 ARG A 104    14088  14533  11136  -1126  -2918   2984       N\\nATOM    518  NH2 ARG A 104       2.417  20.795 -22.961  1.00112.28           N\\nANISOU  518  NH2 ARG A 104    15433  15822  11408  -1532  -3275   3626       N\\nATOM    519  N   ILE A 105      -0.160  16.392 -19.688  1.00 79.98           N\\nANISOU  519  N   ILE A 105    10379  11613   8397   -597  -2469   1666       N\\nATOM    520  CA  ILE A 105      -0.435  17.000 -18.394  1.00 78.38           C\\nANISOU  520  CA  ILE A 105    10057  11079   8646   -452  -2502   1613       C\\nATOM    521  C   ILE A 105      -0.797  15.939 -17.359  1.00 74.85           C\\nANISOU  521  C   ILE A 105     9401  10617   8423   -355  -2239   1232       C\\nATOM    522  O   ILE A 105      -0.422  16.063 -16.189  1.00 73.96           O\\nANISOU  522  O   ILE A 105     9211  10343   8549   -307  -2066   1171       O\\nATOM    523  CB  ILE A 105      -1.528  18.076 -18.534  1.00 77.26           C\\nANISOU  523  CB  ILE A 105     9910  10715   8730   -308  -2966   1710       C\\nATOM    524  CG1 ILE A 105      -1.691  18.858 -17.227  1.00 76.93           C\\nANISOU  524  CG1 ILE A 105     9750  10345   9133   -142  -3017   1643       C\\nATOM    525  CG2 ILE A 105      -2.847  17.465 -18.989  1.00 71.80           C\\nANISOU  525  CG2 ILE A 105     9083  10142   8055   -199  -3143   1458       C\\nATOM    526  CD1 ILE A 105      -0.522  19.761 -16.903  1.00 63.79           C\\nANISOU  526  CD1 ILE A 105     8244   8504   7489   -248  -2982   1938       C\\nATOM    527  N   HIS A 106      -1.425  14.862 -17.789  1.00 78.10           N\\nANISOU  527  N   HIS A 106     9732  11194   8747   -350  -2214    984       N\\nATOM    528  CA  HIS A 106      -1.751  13.780 -16.889  1.00 72.04           C\\nANISOU  528  CA  HIS A 106     8805  10412   8157   -326  -1967    668       C\\nATOM    529  C   HIS A 106      -0.480  13.081 -16.470  1.00 75.28           C\\nANISOU  529  C   HIS A 106     9289  10863   8451   -409  -1617    644       C\\nATOM    530  O   HIS A 106      -0.345  12.663 -15.351  1.00 70.37           O\\nANISOU  530  O   HIS A 106     8580  10125   8032   -389  -1418    503       O\\nATOM    531  CB  HIS A 106      -2.690  12.806 -17.558  1.00 69.03           C\\nANISOU  531  CB  HIS A 106     8344  10182   7701   -344  -2050    426       C\\nATOM    532  CG  HIS A 106      -4.109  13.257 -17.558  1.00 86.66           C\\nANISOU  532  CG  HIS A 106    10420  12382  10122   -239  -2375    359       C\\nATOM    533  ND1 HIS A 106      -4.497  14.469 -17.043  1.00 93.53           N\\nANISOU  533  ND1 HIS A 106    11265  13098  11175   -109  -2634    518       N\\nATOM    534  CD2 HIS A 106      -5.234  12.662 -18.003  1.00 92.54           C\\nANISOU  534  CD2 HIS A 106    11011  13228  10921   -235  -2507    125       C\\nATOM    535  CE1 HIS A 106      -5.801  14.602 -17.170  1.00 95.16           C\\nANISOU  535  CE1 HIS A 106    11292  13325  11539     -1  -2912    369       C\\nATOM    536  NE2 HIS A 106      -6.273  13.520 -17.751  1.00 94.46           N\\nANISOU  536  NE2 HIS A 106    11111  13409  11371    -89  -2829    134       N\\nATOM    537  N   CYS A 107       0.459  12.953 -17.384  1.00 74.40           N\\nANISOU  537  N   CYS A 107     9326  10942   8001   -501  -1547    768       N\\nATOM    538  CA  CYS A 107       1.750  12.355 -17.073  1.00 74.41           C\\nANISOU  538  CA  CYS A 107     9366  11008   7898   -548  -1239    725       C\\nATOM    539  C   CYS A 107       2.520  13.220 -16.082  1.00 69.26           C\\nANISOU  539  C   CYS A 107     8705  10174   7436   -541  -1146    902       C\\nATOM    540  O   CYS A 107       3.036  12.718 -15.076  1.00 62.15           O\\nANISOU  540  O   CYS A 107     7754   9173   6688   -508   -936    780       O\\nATOM    541  CB  CYS A 107       2.542  12.149 -18.368  1.00 77.98           C\\nANISOU  541  CB  CYS A 107     9930  11782   7918   -646  -1190    790       C\\nATOM    542  SG  CYS A 107       4.200  11.445 -18.193  1.00 79.49           S\\nANISOU  542  SG  CYS A 107    10119  12137   7945   -673   -832    689       S\\nATOM    543  N   ASP A 108       2.590  14.530 -16.341  1.00 68.64           N\\nANISOU  543  N   ASP A 108     8692  10029   7359   -576  -1335   1195       N\\nATOM    544  CA  ASP A 108       3.289  15.433 -15.430  1.00 67.61           C\\nANISOU  544  CA  ASP A 108     8561   9699   7427   -578  -1293   1358       C\\nATOM    545  C   ASP A 108       2.673  15.405 -14.037  1.00 65.65           C\\nANISOU  545  C   ASP A 108     8180   9208   7557   -435  -1270   1167       C\\nATOM    546  O   ASP A 108       3.393  15.362 -13.033  1.00 66.27           O\\nANISOU  546  O   ASP A 108     8226   9190   7765   -423  -1086   1133       O\\nATOM    547  CB  ASP A 108       3.280  16.856 -15.990  1.00 70.02           C\\nANISOU  547  CB  ASP A 108     8985   9912   7707   -648  -1582   1705       C\\nATOM    548  CG  ASP A 108       4.274  17.047 -17.124  1.00 81.41           C\\nANISOU  548  CG  ASP A 108    10562  11623   8747   -867  -1532   1967       C\\nATOM    549  OD1 ASP A 108       5.293  16.329 -17.150  1.00 84.41           O\\nANISOU  549  OD1 ASP A 108    10904  12225   8943   -940  -1226   1879       O\\nATOM    550  OD2 ASP A 108       4.043  17.922 -17.986  1.00 86.93           O\\nANISOU  550  OD2 ASP A 108    11397  12326   9305   -971  -1808   2260       O\\nATOM    551  N   ILE A 109       1.341  15.424 -13.956  1.00 63.48           N\\nANISOU  551  N   ILE A 109     7808   8870   7442   -332  -1455   1030       N\\nATOM    552  CA  ILE A 109       0.665  15.365 -12.662  1.00 61.96           C\\nANISOU  552  CA  ILE A 109     7449   8532   7562   -218  -1412    821       C\\nATOM    553  C   ILE A 109       1.015  14.072 -11.937  1.00 63.72           C\\nANISOU  553  C   ILE A 109     7629   8811   7771   -268  -1106    623       C\\nATOM    554  O   ILE A 109       1.341  14.076 -10.743  1.00 59.23           O\\nANISOU  554  O   ILE A 109     7010   8137   7359   -241   -960    564       O\\nATOM    555  CB  ILE A 109      -0.856  15.511 -12.845  1.00 58.03           C\\nANISOU  555  CB  ILE A 109     6805   8039   7204   -115  -1656    674       C\\nATOM    556  CG1 ILE A 109      -1.212  16.937 -13.262  1.00 58.42           C\\nANISOU  556  CG1 ILE A 109     6896   7940   7362    -12  -2018    855       C\\nATOM    557  CG2 ILE A 109      -1.588  15.133 -11.573  1.00 56.04           C\\nANISOU  557  CG2 ILE A 109     6336   7761   7197    -50  -1535    405       C\\nATOM    558  CD1 ILE A 109      -2.681  17.131 -13.524  1.00 59.89           C\\nANISOU  558  CD1 ILE A 109     6917   8142   7695    126  -2302    693       C\\nATOM    559  N   PHE A 110       0.949  12.945 -12.648  1.00 61.78           N\\nANISOU  559  N   PHE A 110     7422   8717   7335   -338  -1034    516       N\\nATOM    560  CA  PHE A 110       1.250  11.658 -12.031  1.00 58.79           C\\nANISOU  560  CA  PHE A 110     7039   8336   6961   -385   -808    335       C\\nATOM    561  C   PHE A 110       2.679  11.622 -11.510  1.00 63.91           C\\nANISOU  561  C   PHE A 110     7771   8939   7574   -390   -613    414       C\\nATOM    562  O   PHE A 110       2.921  11.236 -10.361  1.00 59.44           O\\nANISOU  562  O   PHE A 110     7180   8260   7146   -384   -476    340       O\\nATOM    563  CB  PHE A 110       0.997  10.530 -13.034  1.00 61.38           C\\nANISOU  563  CB  PHE A 110     7419   8803   7098   -442   -823    194       C\\nATOM    564  CG  PHE A 110       1.692   9.234 -12.700  1.00 68.94           C\\nANISOU  564  CG  PHE A 110     8447   9728   8016   -477   -636     42       C\\nATOM    565  CD1 PHE A 110       1.579   8.662 -11.444  1.00 75.18           C\\nANISOU  565  CD1 PHE A 110     9204  10361   8999   -508   -525    -42       C\\nATOM    566  CD2 PHE A 110       2.437   8.573 -13.660  1.00 71.59           C\\nANISOU  566  CD2 PHE A 110     8887  10201   8115   -474   -595    -28       C\\nATOM    567  CE1 PHE A 110       2.216   7.472 -11.150  1.00 77.40           C\\nANISOU  567  CE1 PHE A 110     9585  10560   9264   -531   -416   -161       C\\nATOM    568  CE2 PHE A 110       3.070   7.383 -13.372  1.00 74.90           C\\nANISOU  568  CE2 PHE A 110     9372  10553   8534   -462   -477   -203       C\\nATOM    569  CZ  PHE A 110       2.960   6.833 -12.116  1.00 77.70           C\\nANISOU  569  CZ  PHE A 110     9724  10690   9110   -489   -407   -255       C\\nATOM    570  N   VAL A 111       3.641  12.034 -12.340  1.00 65.60           N\\nANISOU  570  N   VAL A 111     8072   9264   7587   -416   -603    568       N\\nATOM    571  CA  VAL A 111       5.043  11.987 -11.930  1.00 66.54           C\\nANISOU  571  CA  VAL A 111     8228   9388   7667   -424   -420    620       C\\nATOM    572  C   VAL A 111       5.288  12.924 -10.757  1.00 60.65           C\\nANISOU  572  C   VAL A 111     7442   8452   7150   -393   -417    727       C\\nATOM    573  O   VAL A 111       6.026  12.590  -9.822  1.00 56.21           O\\nANISOU  573  O   VAL A 111     6872   7814   6670   -370   -270    674       O\\nATOM    574  CB  VAL A 111       5.960  12.317 -13.119  1.00 69.81           C\\nANISOU  574  CB  VAL A 111     8700  10035   7791   -499   -401    765       C\\nATOM    575  CG1 VAL A 111       7.405  12.336 -12.671  1.00 60.98           C\\nANISOU  575  CG1 VAL A 111     7563   8955   6651   -512   -214    801       C\\nATOM    576  CG2 VAL A 111       5.758  11.308 -14.235  1.00 72.95           C\\nANISOU  576  CG2 VAL A 111     9130  10652   7937   -508   -394    597       C\\nATOM    577  N   THR A 112       4.669  14.106 -10.784  1.00 59.23           N\\nANISOU  577  N   THR A 112     7242   8180   7083   -374   -610    861       N\\nATOM    578  CA  THR A 112       4.789  15.036  -9.664  1.00 65.31           C\\nANISOU  578  CA  THR A 112     7970   8754   8090   -319   -646    910       C\\nATOM    579  C   THR A 112       4.286  14.407  -8.371  1.00 66.52           C\\nANISOU  579  C   THR A 112     8031   8833   8410   -256   -532    693       C\\nATOM    580  O   THR A 112       4.970  14.440  -7.343  1.00 76.31           O\\nANISOU  580  O   THR A 112     9268   9991   9734   -241   -417    676       O\\nATOM    581  CB  THR A 112       4.019  16.321  -9.963  1.00 64.71           C\\nANISOU  581  CB  THR A 112     7889   8561   8139   -269   -933   1031       C\\nATOM    582  OG1 THR A 112       4.645  17.010 -11.052  1.00 63.73           O\\nANISOU  582  OG1 THR A 112     7888   8484   7843   -379  -1048   1304       O\\nATOM    583  CG2 THR A 112       3.995  17.223  -8.744  1.00 62.38           C\\nANISOU  583  CG2 THR A 112     7534   8052   8116   -171   -994    998       C\\nATOM    584  N   LEU A 113       3.086  13.825  -8.407  1.00 61.29           N\\nANISOU  584  N   LEU A 113     7289   8219   7778   -245   -569    534       N\\nATOM    585  CA  LEU A 113       2.533  13.195  -7.214  1.00 68.29           C\\nANISOU  585  CA  LEU A 113     8081   9085   8780   -248   -453    353       C\\nATOM    586  C   LEU A 113       3.348  11.975  -6.799  1.00 67.53           C\\nANISOU  586  C   LEU A 113     8081   8983   8595   -321   -257    312       C\\nATOM    587  O   LEU A 113       3.573  11.752  -5.604  1.00 68.67           O\\nANISOU  587  O   LEU A 113     8216   9064   8811   -332   -149    267       O\\nATOM    588  CB  LEU A 113       1.075  12.808  -7.454  1.00 70.65           C\\nANISOU  588  CB  LEU A 113     8249   9477   9119   -266   -536    201       C\\nATOM    589  CG  LEU A 113       0.073  13.960  -7.517  1.00 65.91           C\\nANISOU  589  CG  LEU A 113     7497   8872   8673   -146   -751    162       C\\nATOM    590  CD1 LEU A 113      -1.287  13.451  -7.958  1.00 61.41           C\\nANISOU  590  CD1 LEU A 113     6776   8439   8118   -174   -840      2       C\\nATOM    591  CD2 LEU A 113      -0.016  14.648  -6.165  1.00 61.76           C\\nANISOU  591  CD2 LEU A 113     6853   8287   8324    -59   -710     69       C\\nATOM    592  N   ASP A 114       3.794  11.174  -7.768  1.00 63.91           N\\nANISOU  592  N   ASP A 114     7718   8590   7975   -359   -233    311       N\\nATOM    593  CA  ASP A 114       4.598   9.999  -7.445  1.00 66.05           C\\nANISOU  593  CA  ASP A 114     8086   8820   8191   -384   -102    240       C\\nATOM    594  C   ASP A 114       5.885  10.392  -6.734  1.00 66.08           C\\nANISOU  594  C   ASP A 114     8124   8760   8225   -333    -12    324       C\\nATOM    595  O   ASP A 114       6.262   9.778  -5.730  1.00 69.96           O\\nANISOU  595  O   ASP A 114     8658   9151   8773   -337     64    278       O\\nATOM    596  CB  ASP A 114       4.901   9.208  -8.720  1.00 75.01           C\\nANISOU  596  CB  ASP A 114     9296  10059   9148   -388   -118    174       C\\nATOM    597  CG  ASP A 114       5.951   8.133  -8.509  1.00 75.49           C\\nANISOU  597  CG  ASP A 114     9451  10063   9168   -352    -25     76       C\\nATOM    598  OD1 ASP A 114       5.746   7.255  -7.648  1.00 74.37           O\\nANISOU  598  OD1 ASP A 114     9364   9766   9125   -388     -9     -2       O\\nATOM    599  OD2 ASP A 114       6.981   8.161  -9.214  1.00 76.15           O\\nANISOU  599  OD2 ASP A 114     9549  10268   9116   -291     20     74       O\\nATOM    600  N   VAL A 115       6.568  11.421  -7.235  1.00 71.45           N\\nANISOU  600  N   VAL A 115     8790   9494   8864   -306    -41    464       N\\nATOM    601  CA  VAL A 115       7.809  11.865  -6.610  1.00 70.24           C\\nANISOU  601  CA  VAL A 115     8641   9297   8749   -279     30    542       C\\nATOM    602  C   VAL A 115       7.535  12.461  -5.234  1.00 69.24           C\\nANISOU  602  C   VAL A 115     8477   9030   8802   -253     19    542       C\\nATOM    603  O   VAL A 115       8.282  12.220  -4.279  1.00 70.91           O\\nANISOU  603  O   VAL A 115     8710   9175   9059   -230     93    521       O\\nATOM    604  CB  VAL A 115       8.536  12.862  -7.531  1.00 65.07           C\\nANISOU  604  CB  VAL A 115     7975   8750   7999   -319     -9    719       C\\nATOM    605  CG1 VAL A 115       9.683  13.529  -6.804  1.00 60.52           C\\nANISOU  605  CG1 VAL A 115     7374   8118   7505   -321     36    809       C\\nATOM    606  CG2 VAL A 115       9.043  12.156  -8.778  1.00 62.56           C\\nANISOU  606  CG2 VAL A 115     7676   8649   7446   -346     53    680       C\\nATOM    607  N   MET A 116       6.454  13.232  -5.103  1.00 72.12           N\\nANISOU  607  N   MET A 116     8773   9364   9266   -239    -88    539       N\\nATOM    608  CA  MET A 116       6.164  13.889  -3.832  1.00 68.31           C\\nANISOU  608  CA  MET A 116     8226   8792   8936   -191   -103    487       C\\nATOM    609  C   MET A 116       5.814  12.877  -2.746  1.00 67.37           C\\nANISOU  609  C   MET A 116     8106   8685   8808   -232     19    357       C\\nATOM    610  O   MET A 116       6.435  12.860  -1.677  1.00 67.14           O\\nANISOU  610  O   MET A 116     8105   8604   8802   -221     83    349       O\\nATOM    611  CB  MET A 116       5.031  14.896  -4.005  1.00 66.63           C\\nANISOU  611  CB  MET A 116     7912   8564   8843   -129   -269    455       C\\nATOM    612  CG  MET A 116       4.669  15.602  -2.718  1.00 65.54           C\\nANISOU  612  CG  MET A 116     7676   8370   8856    -46   -291    332       C\\nATOM    613  SD  MET A 116       3.209  16.636  -2.880  1.00 73.08           S\\nANISOU  613  SD  MET A 116     8464   9323   9980     85   -509    199       S\\nATOM    614  CE  MET A 116       3.000  17.178  -1.184  1.00 75.15           C\\nANISOU  614  CE  MET A 116     8597   9592  10365    186   -462    -23       C\\nATOM    615  N   MET A 117       4.820  12.023  -3.000  1.00 57.68           N\\nANISOU  615  N   MET A 117     6854   7527   7535   -303     36    271       N\\nATOM    616  CA  MET A 117       4.373  11.084  -1.977  1.00 63.01           C\\nANISOU  616  CA  MET A 117     7536   8218   8187   -406    135    188       C\\nATOM    617  C   MET A 117       5.457  10.093  -1.578  1.00 71.53           C\\nANISOU  617  C   MET A 117     8783   9196   9201   -439    202    236       C\\nATOM    618  O   MET A 117       5.388   9.526  -0.482  1.00 77.20           O\\nANISOU  618  O   MET A 117     9549   9888   9894   -524    260    225       O\\nATOM    619  CB  MET A 117       3.132  10.337  -2.457  1.00 61.50           C\\nANISOU  619  CB  MET A 117     7283   8115   7968   -518    120    103       C\\nATOM    620  CG  MET A 117       1.975  11.258  -2.770  1.00 64.85           C\\nANISOU  620  CG  MET A 117     7509   8654   8476   -463     28     19       C\\nATOM    621  SD  MET A 117       1.790  12.509  -1.489  1.00 62.59           S\\nANISOU  621  SD  MET A 117     7071   8409   8301   -354     37    -66       S\\nATOM    622  CE  MET A 117       0.518  13.548  -2.206  1.00 56.74           C\\nANISOU  622  CE  MET A 117     6109   7754   7697   -221   -153   -189       C\\nATOM    623  N   CYS A 118       6.449   9.867  -2.434  1.00 70.60           N\\nANISOU  623  N   CYS A 118     8747   9036   9042   -373    183    282       N\\nATOM    624  CA  CYS A 118       7.576   9.023  -2.062  1.00 70.67           C\\nANISOU  624  CA  CYS A 118     8885   8946   9021   -346    211    289       C\\nATOM    625  C   CYS A 118       8.689   9.813  -1.387  1.00 68.27           C\\nANISOU  625  C   CYS A 118     8564   8615   8761   -260    228    351       C\\nATOM    626  O   CYS A 118       9.435   9.249  -0.578  1.00 62.32           O\\nANISOU  626  O   CYS A 118     7898   7774   8009   -239    233    351       O\\nATOM    627  CB  CYS A 118       8.121   8.295  -3.295  1.00 71.86           C\\nANISOU  627  CB  CYS A 118     9091   9112   9101   -295    188    239       C\\nATOM    628  SG  CYS A 118       6.974   7.093  -4.021  1.00 68.74           S\\nANISOU  628  SG  CYS A 118     8755   8698   8664   -398    132    131       S\\nATOM    629  N   THR A 119       8.819  11.105  -1.703  1.00 71.90           N\\nANISOU  629  N   THR A 119     8925   9128   9267   -218    203    409       N\\nATOM    630  CA  THR A 119       9.769  11.947  -0.985  1.00 68.93           C\\nANISOU  630  CA  THR A 119     8523   8711   8956   -165    196    461       C\\nATOM    631  C   THR A 119       9.300  12.212   0.440  1.00 62.52           C\\nANISOU  631  C   THR A 119     7704   7861   8191   -175    201    411       C\\nATOM    632  O   THR A 119      10.125  12.295   1.357  1.00 61.89           O\\nANISOU  632  O   THR A 119     7656   7732   8127   -144    202    417       O\\nATOM    633  CB  THR A 119       9.981  13.271  -1.728  1.00 67.89           C\\nANISOU  633  CB  THR A 119     8314   8606   8874   -156    129    558       C\\nATOM    634  OG1 THR A 119      10.268  13.009  -3.105  1.00 63.88           O\\nANISOU  634  OG1 THR A 119     7808   8202   8260   -182    139    610       O\\nATOM    635  CG2 THR A 119      11.148  14.045  -1.129  1.00 64.40           C\\nANISOU  635  CG2 THR A 119     7848   8113   8507   -132    108    616       C\\nATOM    636  N   ALA A 120       7.987  12.343   0.642  1.00 61.79           N\\nANISOU  636  N   ALA A 120     7547   7824   8105   -218    203    341       N\\nATOM    637  CA  ALA A 120       7.457  12.486   1.992  1.00 59.49           C\\nANISOU  637  CA  ALA A 120     7220   7579   7805   -246    240    258       C\\nATOM    638  C   ALA A 120       7.815  11.283   2.852  1.00 61.28           C\\nANISOU  638  C   ALA A 120     7585   7779   7919   -337    300    286       C\\nATOM    639  O   ALA A 120       8.114  11.433   4.041  1.00 62.06           O\\nANISOU  639  O   ALA A 120     7711   7891   7976   -343    316    271       O\\nATOM    640  CB  ALA A 120       5.943  12.676   1.947  1.00 60.06           C\\nANISOU  640  CB  ALA A 120     7153   7780   7886   -287    251    145       C\\nATOM    641  N   SER A 121       7.784  10.080   2.268  1.00 59.91           N\\nANISOU  641  N   SER A 121     7518   7552   7694   -409    305    325       N\\nATOM    642  CA  SER A 121       8.208   8.889   2.998  1.00 65.17           C\\nANISOU  642  CA  SER A 121     8361   8120   8282   -489    296    378       C\\nATOM    643  C   SER A 121       9.662   9.003   3.431  1.00 68.85           C\\nANISOU  643  C   SER A 121     8900   8486   8775   -361    241    416       C\\nATOM    644  O   SER A 121      10.014   8.643   4.561  1.00 69.48           O\\nANISOU  644  O   SER A 121     9088   8521   8792   -399    214    457       O\\nATOM    645  CB  SER A 121       8.013   7.640   2.137  1.00 61.09           C\\nANISOU  645  CB  SER A 121     7954   7505   7753   -550    254    383       C\\nATOM    646  OG  SER A 121       6.661   7.485   1.747  1.00 71.73           O\\nANISOU  646  OG  SER A 121     9221   8952   9081   -688    290    343       O\\nATOM    647  N   ALA A 122      10.522   9.500   2.544  1.00 66.20           N\\nANISOU  647  N   ALA A 122     8498   8140   8516   -228    219    409       N\\nATOM    648  CA  ALA A 122      11.932   9.632   2.882  1.00 64.09           C\\nANISOU  648  CA  ALA A 122     8247   7817   8288   -115    169    424       C\\nATOM    649  C   ALA A 122      12.144  10.731   3.911  1.00 67.35           C\\nANISOU  649  C   ALA A 122     8599   8264   8729    -99    162    428       C\\nATOM    650  O   ALA A 122      12.870  10.544   4.893  1.00 67.60           O\\nANISOU  650  O   ALA A 122     8699   8245   8739    -68    109    438       O\\nATOM    651  CB  ALA A 122      12.746   9.905   1.621  1.00 62.95           C\\nANISOU  651  CB  ALA A 122     8005   7723   8189    -24    175    411       C\\nATOM    652  N   LEU A 123      11.511  11.886   3.707  1.00 62.65           N\\nANISOU  652  N   LEU A 123     7879   7737   8186   -107    182    403       N\\nATOM    653  CA  LEU A 123      11.661  12.982   4.654  1.00 64.73           C\\nANISOU  653  CA  LEU A 123     8084   8013   8499    -71    145    360       C\\nATOM    654  C   LEU A 123      11.002  12.677   5.993  1.00 68.58           C\\nANISOU  654  C   LEU A 123     8623   8569   8865   -134    179    297       C\\nATOM    655  O   LEU A 123      11.397  13.259   7.008  1.00 65.26           O\\nANISOU  655  O   LEU A 123     8197   8165   8435    -96    140    244       O\\nATOM    656  CB  LEU A 123      11.095  14.271   4.056  1.00 60.03           C\\nANISOU  656  CB  LEU A 123     7361   7429   8020    -42    106    331       C\\nATOM    657  CG  LEU A 123      12.060  15.137   3.236  1.00 62.40           C\\nANISOU  657  CG  LEU A 123     7610   7663   8437    -13     31    421       C\\nATOM    658  CD1 LEU A 123      12.857  14.325   2.223  1.00 59.85           C\\nANISOU  658  CD1 LEU A 123     7308   7374   8057    -33     81    508       C\\nATOM    659  CD2 LEU A 123      11.293  16.248   2.540  1.00 58.42           C\\nANISOU  659  CD2 LEU A 123     7032   7125   8039     -7    -54    431       C\\nATOM    660  N   ASN A 124      10.015  11.778   6.022  1.00 64.20           N\\nANISOU  660  N   ASN A 124     8115   8078   8200   -253    250    303       N\\nATOM    661  CA  ASN A 124       9.452  11.343   7.295  1.00 68.55           C\\nANISOU  661  CA  ASN A 124     8724   8742   8580   -376    301    282       C\\nATOM    662  C   ASN A 124      10.430  10.450   8.047  1.00 72.49           C\\nANISOU  662  C   ASN A 124     9424   9133   8985   -402    229    393       C\\nATOM    663  O   ASN A 124      10.617  10.600   9.260  1.00 78.80           O\\nANISOU  663  O   ASN A 124    10273  10006   9661   -433    215    382       O\\nATOM    664  CB  ASN A 124       8.129  10.616   7.067  1.00 63.03           C\\nANISOU  664  CB  ASN A 124     8004   8152   7791   -549    391    281       C\\nATOM    665  CG  ASN A 124       6.940  11.540   7.141  1.00 59.12           C\\nANISOU  665  CG  ASN A 124     7283   7866   7312   -543    463    113       C\\nATOM    666  OD1 ASN A 124       6.864  12.399   8.016  1.00 58.74           O\\nANISOU  666  OD1 ASN A 124     7141   7941   7236   -481    474    -16       O\\nATOM    667  ND2 ASN A 124       6.000  11.373   6.218  1.00 59.97           N\\nANISOU  667  ND2 ASN A 124     7292   8020   7473   -588    490     83       N\\nATOM    668  N   LEU A 125      11.062   9.508   7.343  1.00 66.29           N\\nANISOU  668  N   LEU A 125     8756   8179   8253   -373    162    480       N\\nATOM    669  CA  LEU A 125      12.084   8.682   7.972  1.00 65.46           C\\nANISOU  669  CA  LEU A 125     8836   7929   8106   -343     35    565       C\\nATOM    670  C   LEU A 125      13.243   9.524   8.477  1.00 65.97           C\\nANISOU  670  C   LEU A 125     8840   7991   8234   -191    -37    522       C\\nATOM    671  O   LEU A 125      13.922   9.139   9.436  1.00 61.15           O\\nANISOU  671  O   LEU A 125     8360   7325   7547   -177   -149    572       O\\nATOM    672  CB  LEU A 125      12.583   7.629   6.988  1.00 62.70           C\\nANISOU  672  CB  LEU A 125     8578   7397   7847   -276    -48    593       C\\nATOM    673  CG  LEU A 125      11.555   6.553   6.663  1.00 64.43           C\\nANISOU  673  CG  LEU A 125     8919   7557   8006   -451    -38    646       C\\nATOM    674  CD1 LEU A 125      12.089   5.633   5.597  1.00 62.96           C\\nANISOU  674  CD1 LEU A 125     8802   7188   7932   -337   -140    608       C\\nATOM    675  CD2 LEU A 125      11.214   5.779   7.920  1.00 61.82           C\\nANISOU  675  CD2 LEU A 125     8799   7183   7505   -650   -100    783       C\\nATOM    676  N   CYS A 126      13.482  10.673   7.849  1.00 67.22           N\\nANISOU  676  N   CYS A 126     8812   8199   8530    -94      0    444       N\\nATOM    677  CA  CYS A 126      14.522  11.568   8.333  1.00 68.85           C\\nANISOU  677  CA  CYS A 126     8945   8402   8814     11    -78    401       C\\nATOM    678  C   CYS A 126      14.084  12.257   9.617  1.00 71.84           C\\nANISOU  678  C   CYS A 126     9323   8885   9086    -30    -78    330       C\\nATOM    679  O   CYS A 126      14.848  12.331  10.588  1.00 74.42           O\\nANISOU  679  O   CYS A 126     9709   9205   9362      8   -177    320       O\\nATOM    680  CB  CYS A 126      14.866  12.592   7.257  1.00 64.79           C\\nANISOU  680  CB  CYS A 126     8252   7891   8474     72    -60    375       C\\nATOM    681  SG  CYS A 126      16.409  13.441   7.561  1.00 69.06           S\\nANISOU  681  SG  CYS A 126     8693   8402   9146    160   -175    353       S\\nATOM    682  N   ALA A 127      12.849  12.762   9.642  1.00 60.58           N\\nANISOU  682  N   ALA A 127     7817   7582   7618    -95     24    250       N\\nATOM    683  CA  ALA A 127      12.322  13.375  10.854  1.00 61.10           C\\nANISOU  683  CA  ALA A 127     7852   7809   7555   -121     44    122       C\\nATOM    684  C   ALA A 127      12.220  12.369  11.990  1.00 65.12           C\\nANISOU  684  C   ALA A 127     8538   8411   7794   -256     52    201       C\\nATOM    685  O   ALA A 127      12.407  12.729  13.158  1.00 65.71           O\\nANISOU  685  O   ALA A 127     8640   8603   7724   -258     16    127       O\\nATOM    686  CB  ALA A 127      10.957  13.996  10.570  1.00 60.25           C\\nANISOU  686  CB  ALA A 127     7585   7843   7462   -141    147    -17       C\\nATOM    687  N   ILE A 128      11.925  11.108  11.673  1.00 64.09           N\\nANISOU  687  N   ILE A 128     8546   8221   7582   -384     77    357       N\\nATOM    688  CA  ILE A 128      11.829  10.083  12.705  1.00 61.38           C\\nANISOU  688  CA  ILE A 128     8417   7924   6982   -558     46    492       C\\nATOM    689  C   ILE A 128      13.184   9.868  13.370  1.00 64.99           C\\nANISOU  689  C   ILE A 128     9025   8241   7426   -455   -148    563       C\\nATOM    690  O   ILE A 128      13.286   9.807  14.600  1.00 69.74           O\\nANISOU  690  O   ILE A 128     9740   8959   7800   -534   -198    591       O\\nATOM    691  CB  ILE A 128      11.271   8.779  12.108  1.00 62.32           C\\nANISOU  691  CB  ILE A 128     8673   7934   7072   -722     61    653       C\\nATOM    692  CG1 ILE A 128       9.772   8.923  11.836  1.00 63.83           C\\nANISOU  692  CG1 ILE A 128     8711   8345   7195   -888    252    582       C\\nATOM    693  CG2 ILE A 128      11.548   7.604  13.028  1.00 64.88           C\\nANISOU  693  CG2 ILE A 128     9290   8172   7190   -886    -69    860       C\\nATOM    694  CD1 ILE A 128       9.120   7.668  11.294  1.00 68.59           C\\nANISOU  694  CD1 ILE A 128     9440   8852   7770  -1092    259    730       C\\nATOM    695  N   SER A 129      14.244   9.756  12.565  1.00 66.20           N\\nANISOU  695  N   SER A 129     9164   8178   7810   -278   -262    578       N\\nATOM    696  CA  SER A 129      15.586   9.611  13.121  1.00 63.02           C\\nANISOU  696  CA  SER A 129     8848   7658   7438   -147   -463    607       C\\nATOM    697  C   SER A 129      15.949  10.799  13.998  1.00 65.47           C\\nANISOU  697  C   SER A 129     9055   8109   7713    -86   -487    474       C\\nATOM    698  O   SER A 129      16.527  10.629  15.078  1.00 65.88           O\\nANISOU  698  O   SER A 129     9234   8177   7619    -82   -631    506       O\\nATOM    699  CB  SER A 129      16.603   9.467  11.995  1.00 65.36           C\\nANISOU  699  CB  SER A 129     9050   7784   7998     39   -538    582       C\\nATOM    700  OG  SER A 129      16.749  10.693  11.302  1.00 65.87           O\\nANISOU  700  OG  SER A 129     8871   7922   8235    114   -445    460       O\\nATOM    701  N   ILE A 130      15.624  12.011  13.546  1.00 64.82           N\\nANISOU  701  N   ILE A 130     8755   8106   7766    -35   -383    319       N\\nATOM    702  CA  ILE A 130      15.959  13.208  14.313  1.00 68.76           C\\nANISOU  702  CA  ILE A 130     9156   8695   8276     36   -439    156       C\\nATOM    703  C   ILE A 130      15.205  13.216  15.636  1.00 70.22           C\\nANISOU  703  C   ILE A 130     9425   9110   8144    -76   -395     92       C\\nATOM    704  O   ILE A 130      15.775  13.502  16.695  1.00 76.17           O\\nANISOU  704  O   ILE A 130    10235   9933   8773    -45   -514     30       O\\nATOM    705  CB  ILE A 130      15.668  14.473  13.488  1.00 69.26           C\\nANISOU  705  CB  ILE A 130     9002   8739   8574    105   -379     19       C\\nATOM    706  CG1 ILE A 130      16.553  14.504  12.241  1.00 65.51           C\\nANISOU  706  CG1 ILE A 130     8440   8094   8355    174   -420    103       C\\nATOM    707  CG2 ILE A 130      15.878  15.716  14.329  1.00 65.28           C\\nANISOU  707  CG2 ILE A 130     8415   8293   8097    175   -469   -180       C\\nATOM    708  CD1 ILE A 130      16.380  15.745  11.402  1.00 62.56           C\\nANISOU  708  CD1 ILE A 130     7895   7673   8203    202   -405     32       C\\nATOM    709  N   ASP A 131      13.909  12.904  15.595  1.00 70.28           N\\nANISOU  709  N   ASP A 131     9426   9280   7998   -221   -219     94       N\\nATOM    710  CA  ASP A 131      13.155  12.749  16.833  1.00 71.28           C\\nANISOU  710  CA  ASP A 131     9617   9702   7763   -378   -141     50       C\\nATOM    711  C   ASP A 131      13.708  11.611  17.677  1.00 75.20           C\\nANISOU  711  C   ASP A 131    10397  10170   8008   -506   -269    283       C\\nATOM    712  O   ASP A 131      13.639  11.660  18.910  1.00 73.14           O\\nANISOU  712  O   ASP A 131    10222  10134   7432   -599   -289    255       O\\nATOM    713  CB  ASP A 131      11.678  12.515  16.525  1.00 70.71           C\\nANISOU  713  CB  ASP A 131     9449   9834   7586   -540     79     22       C\\nATOM    714  CG  ASP A 131      10.820  12.477  17.775  1.00 76.68           C\\nANISOU  714  CG  ASP A 131    10201  10991   7942   -727    206    -66       C\\nATOM    715  OD1 ASP A 131      10.819  13.472  18.528  1.00 78.05           O\\nANISOU  715  OD1 ASP A 131    10254  11363   8039   -619    204   -327       O\\nATOM    716  OD2 ASP A 131      10.140  11.455  18.001  1.00 79.31           O\\nANISOU  716  OD2 ASP A 131    10647  11456   8030   -996    304    118       O\\nATOM    717  N   ARG A 132      14.264  10.581  17.036  1.00 72.55           N\\nANISOU  717  N   ARG A 132    10215   9556   7796   -504   -380    502       N\\nATOM    718  CA  ARG A 132      14.921   9.521  17.791  1.00 74.39           C\\nANISOU  718  CA  ARG A 132    10739   9679   7847   -579   -584    726       C\\nATOM    719  C   ARG A 132      16.221  10.003  18.417  1.00 74.84           C\\nANISOU  719  C   ARG A 132    10811   9673   7954   -388   -804    656       C\\nATOM    720  O   ARG A 132      16.614   9.507  19.479  1.00 74.70           O\\nANISOU  720  O   ARG A 132    11012   9686   7686   -458   -973    778       O\\nATOM    721  CB  ARG A 132      15.175   8.307  16.894  1.00 71.71           C\\nANISOU  721  CB  ARG A 132    10547   9024   7674   -578   -687    923       C\\nATOM    722  CG  ARG A 132      13.976   7.378  16.715  1.00 69.10           C\\nANISOU  722  CG  ARG A 132    10338   8727   7188   -858   -567   1086       C\\nATOM    723  CD  ARG A 132      13.493   6.832  18.055  1.00 75.91           C\\nANISOU  723  CD  ARG A 132    11433   9782   7627  -1155   -591   1269       C\\nATOM    724  NE  ARG A 132      12.518   7.717  18.686  1.00 77.94           N\\nANISOU  724  NE  ARG A 132    11497  10480   7636  -1291   -337   1099       N\\nATOM    725  CZ  ARG A 132      12.271   7.756  19.990  1.00 77.58           C\\nANISOU  725  CZ  ARG A 132    11552  10740   7186  -1484   -317   1141       C\\nATOM    726  NH1 ARG A 132      12.931   6.960  20.822  1.00 76.41           N\\nANISOU  726  NH1 ARG A 132    11728  10477   6827  -1585   -559   1394       N\\nATOM    727  NH2 ARG A 132      11.366   8.602  20.464  1.00 79.78           N\\nANISOU  727  NH2 ARG A 132    11599  11452   7261  -1565    -71    912       N\\nATOM    728  N   TYR A 133      16.902  10.960  17.786  1.00 73.32           N\\nANISOU  728  N   TYR A 133    10393   9395   8070   -171   -822    476       N\\nATOM    729  CA  TYR A 133      18.124  11.492  18.379  1.00 72.55           C\\nANISOU  729  CA  TYR A 133    10271   9257   8037    -13  -1032    389       C\\nATOM    730  C   TYR A 133      17.813  12.311  19.624  1.00 76.41           C\\nANISOU  730  C   TYR A 133    10753  10016   8263    -65  -1020    228       C\\nATOM    731  O   TYR A 133      18.475  12.161  20.658  1.00 82.66           O\\nANISOU  731  O   TYR A 133    11685  10852   8869    -54  -1214    255       O\\nATOM    732  CB  TYR A 133      18.894  12.340  17.365  1.00 65.57           C\\nANISOU  732  CB  TYR A 133     9133   8238   7542    169  -1045    254       C\\nATOM    733  CG  TYR A 133      20.160  12.957  17.931  1.00 69.03           C\\nANISOU  733  CG  TYR A 133     9504   8648   8079    305  -1262    149       C\\nATOM    734  CD1 TYR A 133      21.367  12.268  17.901  1.00 73.59           C\\nANISOU  734  CD1 TYR A 133    10124   9075   8760    424  -1482    232       C\\nATOM    735  CD2 TYR A 133      20.148  14.224  18.502  1.00 67.30           C\\nANISOU  735  CD2 TYR A 133     9162   8546   7862    326  -1271    -61       C\\nATOM    736  CE1 TYR A 133      22.526  12.825  18.419  1.00 73.44           C\\nANISOU  736  CE1 TYR A 133    10011   9052   8839    539  -1690    123       C\\nATOM    737  CE2 TYR A 133      21.303  14.789  19.022  1.00 69.25           C\\nANISOU  737  CE2 TYR A 133     9341   8760   8209    429  -1488   -164       C\\nATOM    738  CZ  TYR A 133      22.488  14.084  18.977  1.00 74.54           C\\nANISOU  738  CZ  TYR A 133    10039   9309   8975    524  -1689    -64       C\\nATOM    739  OH  TYR A 133      23.637  14.640  19.490  1.00 78.51           O\\nANISOU  739  OH  TYR A 133    10443   9800   9586    618  -1914   -178       O\\nATOM    740  N   THR A 134      16.813  13.190  19.544  1.00 70.79           N\\nANISOU  740  N   THR A 134     9871   9496   7530   -102   -814     34       N\\nATOM    741  CA  THR A 134      16.526  14.064  20.674  1.00 74.84           C\\nANISOU  741  CA  THR A 134    10337  10284   7814   -106   -805   -201       C\\nATOM    742  C   THR A 134      16.021  13.276  21.876  1.00 73.81           C\\nANISOU  742  C   THR A 134    10425  10433   7188   -319   -780    -82       C\\nATOM    743  O   THR A 134      16.266  13.672  23.021  1.00 83.45           O\\nANISOU  743  O   THR A 134    11696  11863   8150   -318   -870   -208       O\\nATOM    744  CB  THR A 134      15.517  15.137  20.270  1.00 81.04           C\\nANISOU  744  CB  THR A 134    10877  11199   8715    -61   -617   -471       C\\nATOM    745  OG1 THR A 134      14.231  14.541  20.084  1.00 85.24           O\\nANISOU  745  OG1 THR A 134    11407  11920   9060   -236   -387   -405       O\\nATOM    746  CG2 THR A 134      15.945  15.803  18.969  1.00 80.96           C\\nANISOU  746  CG2 THR A 134    10697  10893   9169     91   -653   -505       C\\nATOM    747  N   ALA A 135      15.341  12.151  21.642  1.00 74.49           N\\nANISOU  747  N   ALA A 135    10655  10530   7120   -527   -674    172       N\\nATOM    748  CA  ALA A 135      14.858  11.340  22.756  1.00 76.81           C\\nANISOU  748  CA  ALA A 135    11182  11087   6918   -800   -658    350       C\\nATOM    749  C   ALA A 135      16.008  10.654  23.480  1.00 76.81           C\\nANISOU  749  C   ALA A 135    11471  10921   6791   -787   -978    571       C\\nATOM    750  O   ALA A 135      15.979  10.505  24.707  1.00 82.26           O\\nANISOU  750  O   ALA A 135    12330  11871   7053   -935  -1044    623       O\\nATOM    751  CB  ALA A 135      13.849  10.307  22.259  1.00 69.76           C\\nANISOU  751  CB  ALA A 135    10373  10203   5930  -1063   -492    588       C\\nATOM    752  N   VAL A 136      17.029  10.233  22.739  1.00 76.95           N\\nANISOU  752  N   VAL A 136    11539  10534   7164   -603  -1189    688       N\\nATOM    753  CA  VAL A 136      18.154   9.535  23.350  1.00 82.31           C\\nANISOU  753  CA  VAL A 136    12472  11024   7777   -545  -1537    878       C\\nATOM    754  C   VAL A 136      19.136  10.524  23.967  1.00 82.04           C\\nANISOU  754  C   VAL A 136    12325  11053   7795   -336  -1708    644       C\\nATOM    755  O   VAL A 136      19.554  10.367  25.120  1.00 81.48           O\\nANISOU  755  O   VAL A 136    12446  11103   7411   -382  -1911    704       O\\nATOM    756  CB  VAL A 136      18.839   8.630  22.309  1.00 77.31           C\\nANISOU  756  CB  VAL A 136    11904   9961   7508   -406  -1706   1045       C\\nATOM    757  CG1 VAL A 136      20.246   8.278  22.755  1.00 77.43           C\\nANISOU  757  CG1 VAL A 136    12049   9764   7606   -210  -2095   1106       C\\nATOM    758  CG2 VAL A 136      18.017   7.366  22.083  1.00 72.64           C\\nANISOU  758  CG2 VAL A 136    11557   9266   6777   -655  -1667   1340       C\\nATOM    759  N   ALA A 137      19.501  11.568  23.224  1.00 77.79           N\\nANISOU  759  N   ALA A 137    11484  10437   7637   -128  -1644    384       N\\nATOM    760  CA  ALA A 137      20.609  12.434  23.603  1.00 80.22           C\\nANISOU  760  CA  ALA A 137    11669  10715   8097     69  -1852    182       C\\nATOM    761  C   ALA A 137      20.209  13.605  24.491  1.00 87.12           C\\nANISOU  761  C   ALA A 137    12440  11898   8765     54  -1780   -115       C\\nATOM    762  O   ALA A 137      21.094  14.243  25.073  1.00 87.55           O\\nANISOU  762  O   ALA A 137    12447  11955   8861    179  -1994   -277       O\\nATOM    763  CB  ALA A 137      21.304  12.975  22.349  1.00 74.40           C\\nANISOU  763  CB  ALA A 137    10663   9730   7877    260  -1849     74       C\\nATOM    764  N   MET A 138      18.922  13.910  24.616  1.00 85.65           N\\nANISOU  764  N   MET A 138    12198  11978   8368    -81  -1504   -224       N\\nATOM    765  CA  MET A 138      18.517  15.099  25.348  1.00 91.36           C\\nANISOU  765  CA  MET A 138    12776  12989   8948    -40  -1439   -587       C\\nATOM    766  C   MET A 138      17.450  14.760  26.377  1.00 93.65           C\\nANISOU  766  C   MET A 138    13184  13730   8670   -264  -1268   -595       C\\nATOM    767  O   MET A 138      16.648  13.844  26.169  1.00 90.32           O\\nANISOU  767  O   MET A 138    12865  13389   8064   -478  -1095   -353       O\\nATOM    768  CB  MET A 138      18.001  16.181  24.387  1.00 94.18           C\\nANISOU  768  CB  MET A 138    12839  13259   9687     83  -1276   -847       C\\nATOM    769  CG  MET A 138      19.095  16.769  23.500  1.00 98.65           C\\nANISOU  769  CG  MET A 138    13264  13452  10767    263  -1446   -874       C\\nATOM    770  SD  MET A 138      18.521  18.077  22.402  1.00105.80           S\\nANISOU  770  SD  MET A 138    13881  14215  12101    371  -1319  -1121       S\\nATOM    771  CE  MET A 138      20.031  18.481  21.533  1.00105.56           C\\nANISOU  771  CE  MET A 138    13744  13805  12559    477  -1542  -1039       C\\nATOM    772  N   PRO A 139      17.425  15.482  27.515  1.00104.46           N\\nANISOU  772  N   PRO A 139    14532  15425   9735   -241  -1315   -880       N\\nATOM    773  CA  PRO A 139      16.509  15.224  28.635  1.00105.59           C\\nANISOU  773  CA  PRO A 139    14765  16095   9259   -469  -1152   -923       C\\nATOM    774  C   PRO A 139      15.042  15.103  28.221  1.00104.65           C\\nANISOU  774  C   PRO A 139    14492  16238   9033   -630   -782   -969       C\\nATOM    775  O   PRO A 139      14.317  16.097  28.261  1.00106.02           O\\nANISOU  775  O   PRO A 139    14394  16653   9234   -519   -617  -1385       O\\nATOM    776  CB  PRO A 139      16.714  16.446  29.535  1.00103.32           C\\nANISOU  776  CB  PRO A 139    14347  16058   8852   -301  -1242  -1390       C\\nATOM    777  CG  PRO A 139      18.112  16.868  29.263  1.00100.62           C\\nANISOU  777  CG  PRO A 139    14009  15289   8934    -72  -1575  -1406       C\\nATOM    778  CD  PRO A 139      18.340  16.603  27.805  1.00 97.12           C\\nANISOU  778  CD  PRO A 139    13483  14389   9030     -4  -1545  -1193       C\\nATOM    779  N   THR A 144       8.716  17.350  27.929  1.00103.31           N\\nANISOU  779  N   THR A 144    12885  17966   8400   -718    631  -2535       N\\nATOM    780  CA  THR A 144       7.590  18.233  28.208  1.00111.55           C\\nANISOU  780  CA  THR A 144    13533  19499   9351   -578    832  -3111       C\\nATOM    781  C   THR A 144       6.396  17.895  27.318  1.00111.78           C\\nANISOU  781  C   THR A 144    13322  19627   9521   -685   1084  -3075       C\\nATOM    782  O   THR A 144       6.556  17.666  26.122  1.00115.16           O\\nANISOU  782  O   THR A 144    13802  19541  10411   -631   1006  -2812       O\\nATOM    783  CB  THR A 144       7.971  19.712  28.006  1.00112.47           C\\nANISOU  783  CB  THR A 144    13477  19327   9931   -104    597  -3618       C\\nATOM    784  N   ARG A 145       5.198  17.868  27.907  1.00112.87           N\\nANISOU  784  N   ARG A 145    13181  20279   9425   -824   1334  -3251       N\\nATOM    785  CA  ARG A 145       4.002  17.509  27.151  1.00114.09           C\\nANISOU  785  CA  ARG A 145    13078  20551   9719   -950   1551  -3212       C\\nATOM    786  C   ARG A 145       3.581  18.596  26.170  1.00118.73           C\\nANISOU  786  C   ARG A 145    13352  20930  10830   -531   1477  -3651       C\\nATOM    787  O   ARG A 145       2.846  18.305  25.221  1.00119.01           O\\nANISOU  787  O   ARG A 145    13234  20913  11072   -582   1585  -3578       O\\nATOM    788  CB  ARG A 145       2.846  17.198  28.104  1.00118.50           C\\nANISOU  788  CB  ARG A 145    13396  21689   9937  -1221   1786  -3270       C\\nATOM    789  N   TYR A 146       4.024  19.834  26.375  1.00121.59           N\\nANISOU  789  N   TYR A 146    13630  21133  11434   -123   1259  -4089       N\\nATOM    790  CA  TYR A 146       3.700  20.948  25.491  1.00117.64           C\\nANISOU  790  CA  TYR A 146    12880  20335  11482    295   1102  -4485       C\\nATOM    791  C   TYR A 146       4.829  21.280  24.526  1.00108.31           C\\nANISOU  791  C   TYR A 146    11951  18428  10772    498    805  -4303       C\\nATOM    792  O   TYR A 146       4.573  21.530  23.344  1.00100.71           O\\nANISOU  792  O   TYR A 146    10911  17078  10275    638    718  -4241       O\\nATOM    793  CB  TYR A 146       3.345  22.185  26.325  1.00124.08           C\\nANISOU  793  CB  TYR A 146    13429  21323  12394    606    974  -5030       C\\nATOM    794  CG  TYR A 146       3.156  23.462  25.533  1.00125.41           C\\nANISOU  794  CG  TYR A 146    13400  21084  13165   1062    702  -5422       C\\nATOM    795  CD1 TYR A 146       1.920  23.794  24.993  1.00128.22           C\\nANISOU  795  CD1 TYR A 146    13405  21556  13758   1181    740  -5641       C\\nATOM    796  CD2 TYR A 146       4.211  24.347  25.345  1.00125.84           C\\nANISOU  796  CD2 TYR A 146    13634  20614  13563   1355    362  -5554       C\\nATOM    797  CE1 TYR A 146       1.746  24.966  24.276  1.00131.82           C\\nANISOU  797  CE1 TYR A 146    13721  21595  14769   1588    432  -5955       C\\nATOM    798  CE2 TYR A 146       4.047  25.515  24.631  1.00128.03           C\\nANISOU  798  CE2 TYR A 146    13776  20456  14413   1732     64  -5846       C\\nATOM    799  CZ  TYR A 146       2.815  25.821  24.099  1.00132.64           C\\nANISOU  799  CZ  TYR A 146    14037  21147  15214   1852     92  -6034       C\\nATOM    800  OH  TYR A 146       2.656  26.988  23.388  1.00136.93           O\\nANISOU  800  OH  TYR A 146    14484  21222  16320   2213   -261  -6277       O\\nATOM    801  N   SER A 147       6.076  21.287  25.005  1.00108.97           N\\nANISOU  801  N   SER A 147    12336  18257  10810    490    611  -4125       N\\nATOM    802  CA  SER A 147       7.206  21.602  24.138  1.00104.01           C\\nANISOU  802  CA  SER A 147    11926  16901  10691    633    308  -3860       C\\nATOM    803  C   SER A 147       7.407  20.541  23.065  1.00103.85           C\\nANISOU  803  C   SER A 147    12083  16559  10818    407    370  -3277       C\\nATOM    804  O   SER A 147       7.842  20.861  21.953  1.00 99.45           O\\nANISOU  804  O   SER A 147    11570  15480  10738    539    199  -3123       O\\nATOM    805  CB  SER A 147       8.481  21.758  24.972  1.00101.67           C\\nANISOU  805  CB  SER A 147    11877  16479  10273    647     99  -3814       C\\nATOM    806  N   SER A 148       7.103  19.279  23.375  1.00100.58           N\\nANISOU  806  N   SER A 148    11778  16447   9991     56    598  -2950       N\\nATOM    807  CA  SER A 148       7.325  18.214  22.404  1.00 97.98           C\\nANISOU  807  CA  SER A 148    11636  15794   9798   -147    625  -2427       C\\nATOM    808  C   SER A 148       6.273  18.239  21.303  1.00 88.88           C\\nANISOU  808  C   SER A 148    10254  14611   8905   -117    745  -2472       C\\nATOM    809  O   SER A 148       6.602  18.071  20.125  1.00 80.56           O\\nANISOU  809  O   SER A 148     9283  13109   8218    -74    646  -2217       O\\nATOM    810  CB  SER A 148       7.339  16.858  23.106  1.00103.00           C\\nANISOU  810  CB  SER A 148    12497  16702   9935   -541    771  -2055       C\\nATOM    811  OG  SER A 148       6.089  16.599  23.719  1.00106.17           O\\nANISOU  811  OG  SER A 148    12692  17721   9926   -754   1057  -2228       O\\nATOM    812  N   LYS A 149       5.003  18.446  21.667  1.00 92.05           N\\nANISOU  812  N   LYS A 149    10349  15519   9108   -139    955  -2812       N\\nATOM    813  CA  LYS A 149       3.946  18.506  20.661  1.00 84.26           C\\nANISOU  813  CA  LYS A 149     9110  14536   8369    -93   1046  -2895       C\\nATOM    814  C   LYS A 149       4.192  19.638  19.673  1.00 88.93           C\\nANISOU  814  C   LYS A 149     9627  14634   9529    289    781  -3067       C\\nATOM    815  O   LYS A 149       3.943  19.488  18.470  1.00 93.01           O\\nANISOU  815  O   LYS A 149    10125  14862  10350    308    742  -2887       O\\nATOM    816  CB  LYS A 149       2.585  18.670  21.333  1.00 79.97           C\\nANISOU  816  CB  LYS A 149     8188  14678   7518   -142   1299  -3315       C\\nATOM    817  N   ARG A 150       4.688  20.778  20.160  1.00 87.49           N\\nANISOU  817  N   ARG A 150     9416  14340   9487    578    575  -3405       N\\nATOM    818  CA  ARG A 150       5.060  21.865  19.261  1.00 81.69           C\\nANISOU  818  CA  ARG A 150     8671  13071   9295    893    273  -3505       C\\nATOM    819  C   ARG A 150       6.223  21.474  18.359  1.00 80.21           C\\nANISOU  819  C   ARG A 150     8786  12341   9349    799    130  -2998       C\\nATOM    820  O   ARG A 150       6.317  21.964  17.230  1.00 82.46           O\\nANISOU  820  O   ARG A 150     9071  12222  10039    928    -38  -2909       O\\nATOM    821  CB  ARG A 150       5.411  23.117  20.063  1.00 80.33           C\\nANISOU  821  CB  ARG A 150     8437  12868   9215   1187     52  -3965       C\\nATOM    822  N   ARG A 151       7.111  20.595  18.831  1.00 78.36           N\\nANISOU  822  N   ARG A 151     8802  12110   8862    578    185  -2672       N\\nATOM    823  CA  ARG A 151       8.234  20.166  18.003  1.00 72.71           C\\nANISOU  823  CA  ARG A 151     8328  10937   8361    507     62  -2239       C\\nATOM    824  C   ARG A 151       7.780  19.202  16.916  1.00 79.91           C\\nANISOU  824  C   ARG A 151     9266  11777   9319    342    198  -1915       C\\nATOM    825  O   ARG A 151       8.310  19.226  15.799  1.00 80.42           O\\nANISOU  825  O   ARG A 151     9410  11464   9683    376     87  -1687       O\\nATOM    826  CB  ARG A 151       9.319  19.528  18.870  1.00 74.01           C\\nANISOU  826  CB  ARG A 151     8732  11123   8264    367     34  -2034       C\\nATOM    827  CG  ARG A 151      10.576  19.134  18.110  1.00 82.30           C\\nANISOU  827  CG  ARG A 151     9986  11745   9540    333   -108  -1658       C\\nATOM    828  CD  ARG A 151      11.637  18.577  19.045  1.00 87.06           C\\nANISOU  828  CD  ARG A 151    10798  12374   9905    242   -184  -1509       C\\nATOM    829  NE  ARG A 151      11.097  17.537  19.917  1.00 91.56           N\\nANISOU  829  NE  ARG A 151    11463  13317  10010     18     -7  -1413       N\\nATOM    830  CZ  ARG A 151      11.047  16.249  19.600  1.00 88.57           C\\nANISOU  830  CZ  ARG A 151    11241  12910   9500   -194     83  -1059       C\\nATOM    831  NH1 ARG A 151      10.538  15.370  20.453  1.00 83.32           N\\nANISOU  831  NH1 ARG A 151    10680  12574   8402   -440    216   -953       N\\nATOM    832  NH2 ARG A 151      11.506  15.837  18.428  1.00 87.56           N\\nANISOU  832  NH2 ARG A 151    11174  12429   9667   -175     27   -816       N\\nATOM    833  N   VAL A 152       6.797  18.350  17.218  1.00 81.56           N\\nANISOU  833  N   VAL A 152     9402  12365   9221    140    437  -1897       N\\nATOM    834  CA  VAL A 152       6.288  17.429  16.204  1.00 81.36           C\\nANISOU  834  CA  VAL A 152     9394  12272   9245    -25    549  -1623       C\\nATOM    835  C   VAL A 152       5.564  18.196  15.104  1.00 80.65           C\\nANISOU  835  C   VAL A 152     9093  12045   9504    168    481  -1785       C\\nATOM    836  O   VAL A 152       5.709  17.888  13.915  1.00 78.73           O\\nANISOU  836  O   VAL A 152     8921  11517   9474    149    431  -1543       O\\nATOM    837  CB  VAL A 152       5.377  16.364  16.843  1.00 80.98           C\\nANISOU  837  CB  VAL A 152     9312  12669   8787   -333    803  -1562       C\\nATOM    838  CG1 VAL A 152       5.106  15.241  15.863  1.00 82.24           C\\nANISOU  838  CG1 VAL A 152     9570  12682   8997   -541    871  -1224       C\\nATOM    839  CG2 VAL A 152       6.004  15.810  18.104  1.00 83.35           C\\nANISOU  839  CG2 VAL A 152     9819  13145   8703   -511    831  -1443       C\\nATOM    840  N   THR A 153       4.781  19.211  15.482  1.00 84.22           N\\nANISOU  840  N   THR A 153     9285  12700  10015    371    455  -2213       N\\nATOM    841  CA  THR A 153       4.057  20.004  14.492  1.00 78.54           C\\nANISOU  841  CA  THR A 153     8369  11830   9642    587    332  -2387       C\\nATOM    842  C   THR A 153       5.011  20.696  13.525  1.00 75.61           C\\nANISOU  842  C   THR A 153     8160  10910   9657    737     57  -2208       C\\nATOM    843  O   THR A 153       4.738  20.779  12.322  1.00 76.21           O\\nANISOU  843  O   THR A 153     8221  10766   9967    773    -25  -2073       O\\nATOM    844  CB  THR A 153       3.168  21.031  15.195  1.00 80.46           C\\nANISOU  844  CB  THR A 153     8306  12365   9901    832    300  -2933       C\\nATOM    845  OG1 THR A 153       2.144  20.354  15.937  1.00 82.11           O\\nANISOU  845  OG1 THR A 153     8305  13162   9733    652    595  -3096       O\\nATOM    846  CG2 THR A 153       2.527  21.976  14.186  1.00 77.79           C\\nANISOU  846  CG2 THR A 153     7796  11785   9977   1109     80  -3121       C\\nATOM    847  N   VAL A 154       6.141  21.193  14.030  1.00 73.65           N\\nANISOU  847  N   VAL A 154     8065  10459   9460    799    -90  -2194       N\\nATOM    848  CA  VAL A 154       7.112  21.843  13.156  1.00 71.40           C\\nANISOU  848  CA  VAL A 154     7922   9692   9516    880   -337  -2000       C\\nATOM    849  C   VAL A 154       7.787  20.821  12.246  1.00 67.73           C\\nANISOU  849  C   VAL A 154     7638   9069   9028    675   -255  -1548       C\\nATOM    850  O   VAL A 154       8.007  21.079  11.057  1.00 61.81           O\\nANISOU  850  O   VAL A 154     6927   8041   8515    690   -370  -1361       O\\nATOM    851  CB  VAL A 154       8.137  22.627  13.993  1.00 65.37           C\\nANISOU  851  CB  VAL A 154     7244   8781   8811    974   -518  -2127       C\\nATOM    852  CG1 VAL A 154       9.256  23.154  13.108  1.00 56.93           C\\nANISOU  852  CG1 VAL A 154     6321   7254   8055    968   -742  -1864       C\\nATOM    853  CG2 VAL A 154       7.453  23.767  14.722  1.00 60.75           C\\nANISOU  853  CG2 VAL A 154     6475   8294   8312   1228   -654  -2627       C\\nATOM    854  N   MET A 155       8.122  19.645  12.784  1.00 69.04           N\\nANISOU  854  N   MET A 155     7921   9413   8899    483    -75  -1374       N\\nATOM    855  CA  MET A 155       8.784  18.630  11.972  1.00 68.64           C\\nANISOU  855  CA  MET A 155     8035   9207   8837    329    -24  -1003       C\\nATOM    856  C   MET A 155       7.875  18.134  10.856  1.00 64.55           C\\nANISOU  856  C   MET A 155     7452   8706   8368    269     63   -905       C\\nATOM    857  O   MET A 155       8.316  17.979   9.712  1.00 59.62           O\\nANISOU  857  O   MET A 155     6898   7863   7894    252      8   -690       O\\nATOM    858  CB  MET A 155       9.241  17.467  12.851  1.00 72.37           C\\nANISOU  858  CB  MET A 155     8663   9833   9001    158     94   -859       C\\nATOM    859  CG  MET A 155      10.407  17.803  13.768  1.00 80.64           C\\nANISOU  859  CG  MET A 155     9815  10814  10011    208    -29   -884       C\\nATOM    860  SD  MET A 155      11.031  16.373  14.674  1.00 89.65           S\\nANISOU  860  SD  MET A 155    11184  12069  10810     19     37   -657       S\\nATOM    861  CE  MET A 155      12.405  17.110  15.553  1.00 99.07           C\\nANISOU  861  CE  MET A 155    12443  13153  12047    140   -171   -742       C\\nATOM    862  N   ILE A 156       6.602  17.886  11.166  1.00 67.34           N\\nANISOU  862  N   ILE A 156     7652   9352   8582    227    200  -1075       N\\nATOM    863  CA  ILE A 156       5.685  17.372  10.156  1.00 68.91           C\\nANISOU  863  CA  ILE A 156     7773   9590   8821    157    271  -1001       C\\nATOM    864  C   ILE A 156       5.469  18.403   9.059  1.00 69.08           C\\nANISOU  864  C   ILE A 156     7705   9384   9158    345     81  -1053       C\\nATOM    865  O   ILE A 156       5.484  18.072   7.867  1.00 70.31           O\\nANISOU  865  O   ILE A 156     7916   9392   9407    300     52   -852       O\\nATOM    866  CB  ILE A 156       4.357  16.945  10.806  1.00 70.36           C\\nANISOU  866  CB  ILE A 156     7765  10184   8786     48    458  -1197       C\\nATOM    867  CG1 ILE A 156       4.590  15.773  11.761  1.00 67.02           C\\nANISOU  867  CG1 ILE A 156     7488   9956   8020   -215    628  -1044       C\\nATOM    868  CG2 ILE A 156       3.332  16.571   9.742  1.00 64.85           C\\nANISOU  868  CG2 ILE A 156     6940   9528   8171     -3    496  -1169       C\\nATOM    869  CD1 ILE A 156       3.333  15.249  12.401  1.00 60.59           C\\nANISOU  869  CD1 ILE A 156     6493   9587   6942   -411    838  -1180       C\\nATOM    870  N   SER A 157       5.271  19.668   9.439  1.00 67.59           N\\nANISOU  870  N   SER A 157     7393   9155   9133    558    -76  -1325       N\\nATOM    871  CA  SER A 157       5.081  20.719   8.446  1.00 66.91           C\\nANISOU  871  CA  SER A 157     7261   8799   9364    734   -321  -1352       C\\nATOM    872  C   SER A 157       6.261  20.789   7.488  1.00 65.20           C\\nANISOU  872  C   SER A 157     7252   8247   9275    664   -437  -1006       C\\nATOM    873  O   SER A 157       6.079  20.905   6.271  1.00 70.97           O\\nANISOU  873  O   SER A 157     8005   8831  10130    658   -531   -845       O\\nATOM    874  CB  SER A 157       4.876  22.064   9.138  1.00 53.19           C\\nANISOU  874  CB  SER A 157     5403   7001   7805    983   -525  -1706       C\\nATOM    875  OG  SER A 157       3.770  22.013  10.019  1.00 59.25           O\\nANISOU  875  OG  SER A 157     5930   8154   8428   1059   -395  -2076       O\\nATOM    876  N   ILE A 158       7.481  20.701   8.019  1.00 63.38           N\\nANISOU  876  N   ILE A 158     7159   7930   8993    600   -428   -895       N\\nATOM    877  CA  ILE A 158       8.662  20.757   7.168  1.00 62.29           C\\nANISOU  877  CA  ILE A 158     7167   7544   8955    516   -512   -595       C\\nATOM    878  C   ILE A 158       8.684  19.577   6.207  1.00 66.42           C\\nANISOU  878  C   ILE A 158     7754   8134   9350    369   -356   -352       C\\nATOM    879  O   ILE A 158       9.069  19.717   5.042  1.00 76.92           O\\nANISOU  879  O   ILE A 158     9134   9324  10767    323   -426   -148       O\\nATOM    880  CB  ILE A 158       9.935  20.815   8.030  1.00 62.52           C\\nANISOU  880  CB  ILE A 158     7286   7519   8948    483   -529   -568       C\\nATOM    881  CG1 ILE A 158       9.969  22.114   8.833  1.00 61.54           C\\nANISOU  881  CG1 ILE A 158     7112   7280   8990    635   -734   -823       C\\nATOM    882  CG2 ILE A 158      11.177  20.683   7.165  1.00 56.51           C\\nANISOU  882  CG2 ILE A 158     6625   6594   8253    369   -564   -273       C\\nATOM    883  CD1 ILE A 158      11.102  22.178   9.819  1.00 68.44           C\\nANISOU  883  CD1 ILE A 158     8055   8136   9811    610   -764   -846       C\\nATOM    884  N   VAL A 159       8.260  18.399   6.670  1.00 61.58           N\\nANISOU  884  N   VAL A 159     7145   7737   8515    280   -157   -371       N\\nATOM    885  CA  VAL A 159       8.270  17.217   5.808  1.00 61.95           C\\nANISOU  885  CA  VAL A 159     7267   7816   8456    152    -40   -177       C\\nATOM    886  C   VAL A 159       7.403  17.448   4.578  1.00 58.47           C\\nANISOU  886  C   VAL A 159     6754   7353   8111    173    -97   -152       C\\nATOM    887  O   VAL A 159       7.847  17.270   3.437  1.00 64.62           O\\nANISOU  887  O   VAL A 159     7599   8038   8915    129   -128     32       O\\nATOM    888  CB  VAL A 159       7.811  15.973   6.589  1.00 61.71           C\\nANISOU  888  CB  VAL A 159     7270   7984   8194     28    136   -202       C\\nATOM    889  CG1 VAL A 159       7.571  14.812   5.641  1.00 58.85           C\\nANISOU  889  CG1 VAL A 159     6974   7622   7763    -90    212    -53       C\\nATOM    890  CG2 VAL A 159       8.840  15.593   7.634  1.00 64.69           C\\nANISOU  890  CG2 VAL A 159     7772   8351   8457     -6    154   -157       C\\nATOM    891  N   TRP A 160       6.156  17.865   4.792  1.00 55.67           N\\nANISOU  891  N   TRP A 160     6244   7112   7797    249   -122   -357       N\\nATOM    892  CA  TRP A 160       5.209  17.964   3.688  1.00 61.87           C\\nANISOU  892  CA  TRP A 160     6946   7902   8658    275   -191   -352       C\\nATOM    893  C   TRP A 160       5.414  19.222   2.854  1.00 68.14           C\\nANISOU  893  C   TRP A 160     7758   8458   9675    394   -447   -287       C\\nATOM    894  O   TRP A 160       5.155  19.201   1.645  1.00 72.46           O\\nANISOU  894  O   TRP A 160     8331   8951  10250    369   -527   -148       O\\nATOM    895  CB  TRP A 160       3.778  17.893   4.226  1.00 54.20           C\\nANISOU  895  CB  TRP A 160     5762   7176   7654    313   -130   -618       C\\nATOM    896  CG  TRP A 160       3.447  16.528   4.729  1.00 59.47           C\\nANISOU  896  CG  TRP A 160     6436   8074   8087    111    106   -599       C\\nATOM    897  CD1 TRP A 160       3.428  16.111   6.027  1.00 64.43           C\\nANISOU  897  CD1 TRP A 160     7047   8894   8538     21    258   -694       C\\nATOM    898  CD2 TRP A 160       3.129  15.380   3.933  1.00 65.48           C\\nANISOU  898  CD2 TRP A 160     7253   8873   8755    -53    190   -456       C\\nATOM    899  NE1 TRP A 160       3.105  14.776   6.089  1.00 64.83           N\\nANISOU  899  NE1 TRP A 160     7153   9080   8400   -211    420   -586       N\\nATOM    900  CE2 TRP A 160       2.917  14.305   4.817  1.00 67.13           C\\nANISOU  900  CE2 TRP A 160     7487   9263   8758   -251    374   -455       C\\nATOM    901  CE3 TRP A 160       2.997  15.161   2.558  1.00 66.76           C\\nANISOU  901  CE3 TRP A 160     7455   8935   8975    -62    110   -331       C\\nATOM    902  CZ2 TRP A 160       2.575  13.030   4.371  1.00 70.04           C\\nANISOU  902  CZ2 TRP A 160     7926   9666   9019   -454    457   -337       C\\nATOM    903  CZ3 TRP A 160       2.659  13.895   2.117  1.00 69.12           C\\nANISOU  903  CZ3 TRP A 160     7807   9302   9154   -239    209   -252       C\\nATOM    904  CH2 TRP A 160       2.451  12.846   3.021  1.00 68.25           C\\nANISOU  904  CH2 TRP A 160     7727   9325   8880   -431    370   -257       C\\nATOM    905  N   VAL A 161       5.874  20.317   3.463  1.00 67.95           N\\nANISOU  905  N   VAL A 161     7737   8280   9802    507   -599   -373       N\\nATOM    906  CA  VAL A 161       6.140  21.520   2.680  1.00 69.19           C\\nANISOU  906  CA  VAL A 161     7952   8155  10182    576   -883   -262       C\\nATOM    907  C   VAL A 161       7.379  21.323   1.823  1.00 65.64           C\\nANISOU  907  C   VAL A 161     7665   7597   9678    402   -867     76       C\\nATOM    908  O   VAL A 161       7.447  21.799   0.684  1.00 71.00           O\\nANISOU  908  O   VAL A 161     8411   8144  10420    354  -1023    278       O\\nATOM    909  CB  VAL A 161       6.273  22.747   3.599  1.00 68.92           C\\nANISOU  909  CB  VAL A 161     7883   7953  10351    740  -1087   -473       C\\nATOM    910  CG1 VAL A 161       6.754  23.958   2.810  1.00 55.10           C\\nANISOU  910  CG1 VAL A 161     6251   5845   8841    751  -1414   -291       C\\nATOM    911  CG2 VAL A 161       4.941  23.041   4.271  1.00 68.37           C\\nANISOU  911  CG2 VAL A 161     7604   8033  10340    947  -1123   -858       C\\nATOM    912  N   LEU A 162       8.370  20.607   2.346  1.00 57.34           N\\nANISOU  912  N   LEU A 162     6669   6627   8492    302   -683    137       N\\nATOM    913  CA  LEU A 162       9.567  20.343   1.562  1.00 62.34           C\\nANISOU  913  CA  LEU A 162     7399   7226   9060    152   -640    403       C\\nATOM    914  C   LEU A 162       9.274  19.375   0.424  1.00 64.44           C\\nANISOU  914  C   LEU A 162     7686   7633   9165     68   -521    527       C\\nATOM    915  O   LEU A 162       9.756  19.565  -0.698  1.00 73.70           O\\nANISOU  915  O   LEU A 162     8910   8787  10307    -32   -568    735       O\\nATOM    916  CB  LEU A 162      10.668  19.803   2.467  1.00 66.33           C\\nANISOU  916  CB  LEU A 162     7929   7786   9485    111   -507    389       C\\nATOM    917  CG  LEU A 162      12.083  19.741   1.909  1.00 71.44           C\\nANISOU  917  CG  LEU A 162     8616   8419  10108    -16   -484    596       C\\nATOM    918  CD1 LEU A 162      12.409  21.020   1.165  1.00 63.78           C\\nANISOU  918  CD1 LEU A 162     7665   7275   9293    -96   -691    765       C\\nATOM    919  CD2 LEU A 162      13.044  19.530   3.061  1.00 75.47           C\\nANISOU  919  CD2 LEU A 162     9125   8941  10610      0   -439    519       C\\nATOM    920  N   SER A 163       8.481  18.334   0.691  1.00 62.39           N\\nANISOU  920  N   SER A 163     7390   7531   8786     86   -371    399       N\\nATOM    921  CA  SER A 163       8.099  17.410  -0.371  1.00 64.81           C\\nANISOU  921  CA  SER A 163     7718   7951   8957     15   -289    475       C\\nATOM    922  C   SER A 163       7.384  18.143  -1.499  1.00 65.90           C\\nANISOU  922  C   SER A 163     7840   8039   9160     33   -467    552       C\\nATOM    923  O   SER A 163       7.634  17.874  -2.680  1.00 71.94           O\\nANISOU  923  O   SER A 163     8662   8855   9817    -51   -466    710       O\\nATOM    924  CB  SER A 163       7.213  16.302   0.193  1.00 64.78           C\\nANISOU  924  CB  SER A 163     7674   8087   8852      4   -146    321       C\\nATOM    925  OG  SER A 163       7.785  15.740   1.357  1.00 61.15           O\\nANISOU  925  OG  SER A 163     7254   7650   8329    -18    -31    269       O\\nATOM    926  N   PHE A 164       6.497  19.078  -1.153  1.00 60.59           N\\nANISOU  926  N   PHE A 164     7089   7277   8655    156   -639    427       N\\nATOM    927  CA  PHE A 164       5.825  19.887  -2.164  1.00 61.72           C\\nANISOU  927  CA  PHE A 164     7234   7322   8893    201   -880    505       C\\nATOM    928  C   PHE A 164       6.833  20.691  -2.972  1.00 65.16           C\\nANISOU  928  C   PHE A 164     7806   7601   9350     94  -1027    793       C\\nATOM    929  O   PHE A 164       6.879  20.597  -4.203  1.00 65.92           O\\nANISOU  929  O   PHE A 164     7974   7746   9327    -10  -1074    992       O\\nATOM    930  CB  PHE A 164       4.803  20.813  -1.496  1.00 57.42           C\\nANISOU  930  CB  PHE A 164     6564   6683   8568    400  -1076    267       C\\nATOM    931  CG  PHE A 164       4.135  21.779  -2.443  1.00 61.42           C\\nANISOU  931  CG  PHE A 164     7089   7023   9226    488  -1405    340       C\\nATOM    932  CD1 PHE A 164       3.067  21.374  -3.232  1.00 63.79           C\\nANISOU  932  CD1 PHE A 164     7317   7446   9476    519  -1453    302       C\\nATOM    933  CD2 PHE A 164       4.563  23.097  -2.528  1.00 60.79           C\\nANISOU  933  CD2 PHE A 164     7109   6640   9350    534  -1703    451       C\\nATOM    934  CE1 PHE A 164       2.450  22.259  -4.099  1.00 64.22           C\\nANISOU  934  CE1 PHE A 164     7400   7336   9667    615  -1799    378       C\\nATOM    935  CE2 PHE A 164       3.946  23.988  -3.393  1.00 65.28           C\\nANISOU  935  CE2 PHE A 164     7729   7008  10065    614  -2062    545       C\\nATOM    936  CZ  PHE A 164       2.889  23.566  -4.178  1.00 64.54           C\\nANISOU  936  CZ  PHE A 164     7564   7051   9906    666  -2113    510       C\\nATOM    937  N   THR A 165       7.667  21.477  -2.285  1.00 60.91           N\\nANISOU  937  N   THR A 165     7302   6899   8944     90  -1100    820       N\\nATOM    938  CA  THR A 165       8.590  22.366  -2.984  1.00 68.08           C\\nANISOU  938  CA  THR A 165     8326   7648   9893    -59  -1264   1109       C\\nATOM    939  C   THR A 165       9.585  21.592  -3.836  1.00 67.06           C\\nANISOU  939  C   THR A 165     8237   7731   9511   -266  -1055   1321       C\\nATOM    940  O   THR A 165      10.068  22.114  -4.846  1.00 74.56           O\\nANISOU  940  O   THR A 165     9269   8666  10395   -439  -1158   1596       O\\nATOM    941  CB  THR A 165       9.335  23.256  -1.988  1.00 72.21           C\\nANISOU  941  CB  THR A 165     8862   7963  10613    -43  -1373   1067       C\\nATOM    942  OG1 THR A 165      10.064  22.439  -1.068  1.00 84.36           O\\nANISOU  942  OG1 THR A 165    10343   9656  12055    -52  -1111    946       O\\nATOM    943  CG2 THR A 165       8.362  24.133  -1.215  1.00 69.54           C\\nANISOU  943  CG2 THR A 165     8475   7415  10531    191  -1616    813       C\\nATOM    944  N   ILE A 166       9.898  20.352  -3.455  1.00 69.64           N\\nANISOU  944  N   ILE A 166     8506   8267   9687   -255   -775   1193       N\\nATOM    945  CA  ILE A 166      10.825  19.548  -4.247  1.00 72.15           C\\nANISOU  945  CA  ILE A 166     8831   8805   9778   -397   -585   1317       C\\nATOM    946  C   ILE A 166      10.150  19.043  -5.520  1.00 72.60           C\\nANISOU  946  C   ILE A 166     8918   9016   9653   -435   -578   1379       C\\nATOM    947  O   ILE A 166      10.751  19.045  -6.601  1.00 74.34           O\\nANISOU  947  O   ILE A 166     9167   9388   9690   -588   -548   1564       O\\nATOM    948  CB  ILE A 166      11.383  18.389  -3.402  1.00 64.44           C\\nANISOU  948  CB  ILE A 166     7804   7945   8737   -337   -355   1141       C\\nATOM    949  CG1 ILE A 166      12.401  18.911  -2.386  1.00 65.09           C\\nANISOU  949  CG1 ILE A 166     7859   7927   8946   -345   -368   1133       C\\nATOM    950  CG2 ILE A 166      12.008  17.326  -4.294  1.00 61.90           C\\nANISOU  950  CG2 ILE A 166     7469   7861   8189   -405   -177   1168       C\\nATOM    951  CD1 ILE A 166      12.979  17.825  -1.505  1.00 55.41           C\\nANISOU  951  CD1 ILE A 166     6604   6788   7663   -276   -195    979       C\\nATOM    952  N   SER A 167       8.896  18.605  -5.414  1.00 66.08           N\\nANISOU  952  N   SER A 167     8070   8185   8852   -311   -603   1216       N\\nATOM    953  CA  SER A 167       8.168  18.066  -6.554  1.00 69.77           C\\nANISOU  953  CA  SER A 167     8557   8794   9156   -335   -616   1237       C\\nATOM    954  C   SER A 167       7.500  19.138  -7.404  1.00 70.97           C\\nANISOU  954  C   SER A 167     8769   8841   9355   -354   -900   1407       C\\nATOM    955  O   SER A 167       7.132  18.860  -8.553  1.00 69.63           O\\nANISOU  955  O   SER A 167     8642   8809   9005   -415   -942   1493       O\\nATOM    956  CB  SER A 167       7.104  17.078  -6.070  1.00 67.68           C\\nANISOU  956  CB  SER A 167     8226   8582   8907   -228   -531    989       C\\nATOM    957  OG  SER A 167       6.153  17.737  -5.251  1.00 68.82           O\\nANISOU  957  OG  SER A 167     8295   8591   9261   -104   -663    859       O\\nATOM    958  N   CYS A 168       7.324  20.345  -6.871  1.00 72.75           N\\nANISOU  958  N   CYS A 168     9009   8812   9819   -293  -1126   1446       N\\nATOM    959  CA  CYS A 168       6.648  21.393  -7.631  1.00 73.51           C\\nANISOU  959  CA  CYS A 168     9186   8743  10001   -284  -1466   1607       C\\nATOM    960  C   CYS A 168       7.347  21.747  -8.942  1.00 77.62           C\\nANISOU  960  C   CYS A 168     9848   9341  10301   -524  -1540   1966       C\\nATOM    961  O   CYS A 168       6.638  22.045  -9.918  1.00 81.68           O\\nANISOU  961  O   CYS A 168    10442   9849  10744   -540  -1760   2098       O\\nATOM    962  CB  CYS A 168       6.478  22.640  -6.754  1.00 74.94           C\\nANISOU  962  CB  CYS A 168     9371   8593  10510   -158  -1727   1556       C\\nATOM    963  SG  CYS A 168       5.411  23.906  -7.472  1.00 83.98           S\\nANISOU  963  SG  CYS A 168    10608   9450  11852    -51  -2231   1669       S\\nATOM    964  N   PRO A 169       8.683  21.755  -9.044  1.00 78.38           N\\nANISOU  964  N   PRO A 169     9970   9541  10269   -727  -1380   2136       N\\nATOM    965  CA  PRO A 169       9.296  22.005 -10.360  1.00 83.73           C\\nANISOU  965  CA  PRO A 169    10752  10394  10669   -996  -1410   2471       C\\nATOM    966  C   PRO A 169       8.894  21.001 -11.428  1.00 84.95           C\\nANISOU  966  C   PRO A 169    10900  10878  10501  -1015  -1280   2429       C\\nATOM    967  O   PRO A 169       8.857  21.362 -12.611  1.00 84.19           O\\nANISOU  967  O   PRO A 169    10915  10894  10178  -1189  -1413   2692       O\\nATOM    968  CB  PRO A 169      10.799  21.935 -10.063  1.00 82.55           C\\nANISOU  968  CB  PRO A 169    10540  10383  10443  -1178  -1179   2547       C\\nATOM    969  CG  PRO A 169      10.912  22.332  -8.645  1.00 76.42           C\\nANISOU  969  CG  PRO A 169     9712   9325   9998  -1032  -1220   2380       C\\nATOM    970  CD  PRO A 169       9.698  21.762  -7.973  1.00 74.69           C\\nANISOU  970  CD  PRO A 169     9435   9030   9916   -740  -1219   2057       C\\nATOM    971  N   LEU A 170       8.584  19.755 -11.051  1.00 79.08           N\\nANISOU  971  N   LEU A 170    10044  10281   9723   -856  -1047   2113       N\\nATOM    972  CA  LEU A 170       8.270  18.731 -12.044  1.00 73.43           C\\nANISOU  972  CA  LEU A 170     9322   9863   8714   -871   -932   2033       C\\nATOM    973  C   LEU A 170       7.035  19.090 -12.860  1.00 76.56           C\\nANISOU  973  C   LEU A 170     9801  10208   9081   -835  -1215   2109       C\\nATOM    974  O   LEU A 170       6.917  18.677 -14.020  1.00 77.86           O\\nANISOU  974  O   LEU A 170    10015  10626   8942   -927  -1211   2171       O\\nATOM    975  CB  LEU A 170       8.080  17.380 -11.356  1.00 67.28           C\\nANISOU  975  CB  LEU A 170     8435   9155   7972   -710   -697   1684       C\\nATOM    976  CG  LEU A 170       9.176  16.975 -10.366  1.00 66.79           C\\nANISOU  976  CG  LEU A 170     8297   9091   7988   -692   -470   1577       C\\nATOM    977  CD1 LEU A 170       8.737  15.773  -9.563  1.00 66.74           C\\nANISOU  977  CD1 LEU A 170     8235   9057   8068   -536   -332   1276       C\\nATOM    978  CD2 LEU A 170      10.488  16.689 -11.074  1.00 61.58           C\\nANISOU  978  CD2 LEU A 170     7607   8724   7065   -840   -287   1659       C\\nATOM    979  N   LEU A 171       6.108  19.856 -12.280  1.00 72.91           N\\nANISOU  979  N   LEU A 171     9340   9439   8925   -685  -1477   2076       N\\nATOM    980  CA  LEU A 171       4.945  20.322 -13.024  1.00 75.80           C\\nANISOU  980  CA  LEU A 171     9768   9727   9306   -622  -1806   2146       C\\nATOM    981  C   LEU A 171       5.311  21.339 -14.094  1.00 79.71           C\\nANISOU  981  C   LEU A 171    10460  10190   9637   -830  -2066   2561       C\\nATOM    982  O   LEU A 171       4.541  21.531 -15.041  1.00 84.88           O\\nANISOU  982  O   LEU A 171    11203  10874  10173   -833  -2320   2673       O\\nATOM    983  CB  LEU A 171       3.917  20.942 -12.075  1.00 74.05           C\\nANISOU  983  CB  LEU A 171     9460   9199   9478   -376  -2034   1961       C\\nATOM    984  CG  LEU A 171       2.918  20.015 -11.385  1.00 69.74           C\\nANISOU  984  CG  LEU A 171     8717   8733   9050   -185  -1900   1574       C\\nATOM    985  CD1 LEU A 171       2.056  20.807 -10.416  1.00 68.86           C\\nANISOU  985  CD1 LEU A 171     8486   8373   9305     44  -2112   1385       C\\nATOM    986  CD2 LEU A 171       2.059  19.311 -12.420  1.00 65.45           C\\nANISOU  986  CD2 LEU A 171     8160   8395   8313   -188  -1959   1520       C\\nATOM    987  N   PHE A 172       6.460  21.995 -13.967  1.00 68.04           N\\nANISOU  987  N   PHE A 172     9054   8656   8140  -1028  -2027   2807       N\\nATOM    988  CA  PHE A 172       6.795  23.074 -14.882  1.00 78.77           C\\nANISOU  988  CA  PHE A 172    10620   9942   9366  -1280  -2310   3252       C\\nATOM    989  C   PHE A 172       8.096  22.777 -15.619  1.00 85.91           C\\nANISOU  989  C   PHE A 172    11542  11237   9862  -1615  -2028   3473       C\\nATOM    990  O   PHE A 172       9.011  23.607 -15.641  1.00 88.20           O\\nANISOU  990  O   PHE A 172    11911  11460  10141  -1873  -2078   3779       O\\nATOM    991  CB  PHE A 172       6.876  24.399 -14.118  1.00 84.73           C\\nANISOU  991  CB  PHE A 172    11461  10224  10509  -1254  -2621   3391       C\\nATOM    992  CG  PHE A 172       5.617  24.738 -13.360  1.00 85.93           C\\nANISOU  992  CG  PHE A 172    11551  10035  11063   -893  -2895   3113       C\\nATOM    993  CD1 PHE A 172       4.602  25.461 -13.964  1.00 86.94           C\\nANISOU  993  CD1 PHE A 172    11803   9937  11293   -793  -3356   3232       C\\nATOM    994  CD2 PHE A 172       5.447  24.323 -12.046  1.00 83.56           C\\nANISOU  994  CD2 PHE A 172    11054   9673  11022   -654  -2699   2721       C\\nATOM    995  CE1 PHE A 172       3.443  25.769 -13.275  1.00 83.30           C\\nANISOU  995  CE1 PHE A 172    11232   9212  11208   -436  -3605   2923       C\\nATOM    996  CE2 PHE A 172       4.288  24.629 -11.350  1.00 82.96           C\\nANISOU  996  CE2 PHE A 172    10876   9366  11280   -334  -2919   2431       C\\nATOM    997  CZ  PHE A 172       3.286  25.353 -11.967  1.00 83.10           C\\nANISOU  997  CZ  PHE A 172    10978   9179  11417   -212  -3367   2511       C\\nATOM    998  N   GLY A 173       8.179  21.592 -16.224  1.00 92.00           N\\nANISOU  998  N   GLY A 173    12224  12431  10302  -1618  -1741   3296       N\\nATOM    999  CA  GLY A 173       9.333  21.223 -17.023  1.00 99.29           C\\nANISOU  999  CA  GLY A 173    13120  13810  10797  -1900  -1463   3431       C\\nATOM   1000  C   GLY A 173      10.629  21.114 -16.255  1.00105.40           C\\nANISOU 1000  C   GLY A 173    13746  14661  11642  -1983  -1167   3370       C\\nATOM   1001  O   GLY A 173      11.703  21.225 -16.853  1.00109.34           O\\nANISOU 1001  O   GLY A 173    14209  15498  11836  -2275   -998   3563       O\\nATOM   1002  N   LEU A 174      10.558  20.899 -14.940  1.00100.46           N\\nANISOU 1002  N   LEU A 174    13015  13761  11393  -1742  -1102   3100       N\\nATOM   1003  CA  LEU A 174      11.734  20.873 -14.068  1.00103.35           C\\nANISOU 1003  CA  LEU A 174    13246  14141  11880  -1788   -879   3034       C\\nATOM   1004  C   LEU A 174      12.539  22.163 -14.183  1.00110.64           C\\nANISOU 1004  C   LEU A 174    14250  14960  12828  -2107  -1028   3434       C\\nATOM   1005  O   LEU A 174      13.746  22.179 -13.930  1.00113.38           O\\nANISOU 1005  O   LEU A 174    14470  15481  13128  -2273   -823   3467       O\\nATOM   1006  CB  LEU A 174      12.615  19.654 -14.361  1.00 97.67           C\\nANISOU 1006  CB  LEU A 174    12350  13885  10875  -1796   -492   2806       C\\nATOM   1007  CG  LEU A 174      13.534  19.118 -13.264  1.00 92.37           C\\nANISOU 1007  CG  LEU A 174    11502  13215  10381  -1682   -254   2560       C\\nATOM   1008  CD1 LEU A 174      12.928  19.339 -11.890  1.00 88.80           C\\nANISOU 1008  CD1 LEU A 174    11078  12307  10354  -1450   -387   2419       C\\nATOM   1009  CD2 LEU A 174      13.792  17.638 -13.505  1.00 90.06           C\\nANISOU 1009  CD2 LEU A 174    11076  13252   9891  -1525     22   2210       C\\nATOM   1010  N   ASN A 175      11.863  23.254 -14.556  1.00127.08           N\\nANISOU 1010  N   ASN A 175    16542  16739  15004  -2196  -1417   3738       N\\nATOM   1011  CA  ASN A 175      12.511  24.539 -14.814  1.00131.09           C\\nANISOU 1011  CA  ASN A 175    17185  17092  15530  -2547  -1637   4178       C\\nATOM   1012  C   ASN A 175      13.737  24.358 -15.706  1.00135.52           C\\nANISOU 1012  C   ASN A 175    17627  18169  15696  -2875  -1339   4267       C\\nATOM   1013  O   ASN A 175      14.777  24.991 -15.516  1.00141.49           O\\nANISOU 1013  O   ASN A 175    18317  18930  16514  -3096  -1295   4368       O\\nATOM   1014  CB  ASN A 175      12.876  25.244 -13.504  1.00127.19           C\\nANISOU 1014  CB  ASN A 175    16665  16177  15484  -2475  -1748   4122       C\\nATOM   1015  CG  ASN A 175      11.656  25.790 -12.774  1.00121.37           C\\nANISOU 1015  CG  ASN A 175    16035  14913  15169  -2144  -2109   3974       C\\nATOM   1016  OD1 ASN A 175      10.689  26.228 -13.400  1.00120.30           O\\nANISOU 1016  OD1 ASN A 175    16064  14605  15041  -2092  -2430   4105       O\\nATOM   1017  ND2 ASN A 175      11.697  25.764 -11.445  1.00115.08           N\\nANISOU 1017  ND2 ASN A 175    15127  13886  14713  -1906  -2061   3672       N\\nATOM   1018  N   ASN A 176      13.611  23.469 -16.686  1.00138.51           N\\nANISOU 1018  N   ASN A 176    17960  19005  15662  -2893  -1141   4194       N\\nATOM   1019  CA  ASN A 176      14.702  23.139 -17.593  1.00128.90           C\\nANISOU 1019  CA  ASN A 176    16590  18346  14041  -3148   -837   4194       C\\nATOM   1020  C   ASN A 176      14.143  23.135 -19.012  1.00130.29           C\\nANISOU 1020  C   ASN A 176    16893  18756  13854  -3256   -934   4312       C\\nATOM   1021  O   ASN A 176      13.054  23.656 -19.280  1.00128.25           O\\nANISOU 1021  O   ASN A 176    16856  18174  13701  -3186  -1280   4456       O\\nATOM   1022  CB  ASN A 176      15.347  21.804 -17.188  1.00114.40           C\\nANISOU 1022  CB  ASN A 176    14490  16909  12066  -3004   -416   3849       C\\nATOM   1023  N   ALA A 177      14.888  22.541 -19.940  1.00131.35           N\\nANISOU 1023  N   ALA A 177    16876  19466  13564  -3410   -639   4223       N\\nATOM   1024  CA  ALA A 177      14.518  22.512 -21.354  1.00133.06           C\\nANISOU 1024  CA  ALA A 177    17193  19978  13388  -3547   -695   4324       C\\nATOM   1025  C   ALA A 177      13.850  21.175 -21.665  1.00139.43           C\\nANISOU 1025  C   ALA A 177    17953  21060  13966  -3279   -543   3999       C\\nATOM   1026  O   ALA A 177      14.499  20.218 -22.087  1.00134.42           O\\nANISOU 1026  O   ALA A 177    17113  20932  13028  -3260   -210   3722       O\\nATOM   1027  CB  ALA A 177      15.744  22.740 -22.230  1.00132.82           C\\nANISOU 1027  CB  ALA A 177    17018  20431  13018  -3895   -487   4415       C\\nATOM   1028  N   ASP A 178      12.535  21.113 -21.456  1.00139.56           N\\nANISOU 1028  N   ASP A 178    18147  20737  14141  -3057   -814   4002       N\\nATOM   1029  CA  ASP A 178      11.738  19.985 -21.927  1.00140.00           C\\nANISOU 1029  CA  ASP A 178    18203  21034  13957  -2843   -761   3735       C\\nATOM   1030  C   ASP A 178      10.328  20.465 -22.235  1.00139.46           C\\nANISOU 1030  C   ASP A 178    18375  20618  13994  -2746  -1185   3897       C\\nATOM   1031  O   ASP A 178       9.372  20.082 -21.554  1.00142.64           O\\nANISOU 1031  O   ASP A 178    18808  20766  14622  -2479  -1336   3761       O\\nATOM   1032  CB  ASP A 178      11.711  18.857 -20.894  1.00137.06           C\\nANISOU 1032  CB  ASP A 178    17675  20675  13728  -2556   -547   3368       C\\nATOM   1033  N   GLN A 179      10.191  21.295 -23.270  1.00143.02           N\\nANISOU 1033  N   GLN A 179    18983  21074  14284  -2960  -1392   4178       N\\nATOM   1034  CA  GLN A 179       8.987  22.105 -23.424  1.00133.33           C\\nANISOU 1034  CA  GLN A 179    17987  19403  13269  -2879  -1859   4383       C\\nATOM   1035  C   GLN A 179       7.753  21.243 -23.675  1.00128.51           C\\nANISOU 1035  C   GLN A 179    17406  18844  12578  -2605  -1987   4153       C\\nATOM   1036  O   GLN A 179       6.787  21.279 -22.902  1.00124.40           O\\nANISOU 1036  O   GLN A 179    16911  17946  12410  -2345  -2237   4071       O\\nATOM   1037  CB  GLN A 179       9.188  23.117 -24.553  1.00132.56           C\\nANISOU 1037  CB  GLN A 179    18056  19342  12970  -3191  -2041   4737       C\\nATOM   1038  N   ASN A 180       7.766  20.455 -24.749  1.00126.77           N\\nANISOU 1038  N   ASN A 180    17160  19104  11903  -2656  -1831   4014       N\\nATOM   1039  CA  ASN A 180       6.565  19.780 -25.230  1.00115.92           C\\nANISOU 1039  CA  ASN A 180    15839  17790  10414  -2448  -2017   3825       C\\nATOM   1040  C   ASN A 180       6.535  18.292 -24.886  1.00111.57           C\\nANISOU 1040  C   ASN A 180    15109  17542   9741  -2253  -1745   3379       C\\nATOM   1041  O   ASN A 180       5.949  17.498 -25.625  1.00103.18           O\\nANISOU 1041  O   ASN A 180    14050  16740   8415  -2166  -1771   3154       O\\nATOM   1042  CB  ASN A 180       6.419  19.972 -26.739  1.00115.56           C\\nANISOU 1042  CB  ASN A 180    15926  18028   9952  -2620  -2110   3964       C\\nATOM   1043  N   GLU A 181       7.135  17.896 -23.764  1.00104.62           N\\nANISOU 1043  N   GLU A 181    14065  16578   9107  -2156  -1490   3195       N\\nATOM   1044  CA  GLU A 181       7.136  16.494 -23.369  1.00106.80           C\\nANISOU 1044  CA  GLU A 181    14149  16965   9465  -1902  -1204   2656       C\\nATOM   1045  C   GLU A 181       6.948  16.366 -21.867  1.00100.72           C\\nANISOU 1045  C   GLU A 181    13266  15721   9281  -1661  -1157   2456       C\\nATOM   1046  O   GLU A 181       7.211  17.295 -21.099  1.00102.83           O\\nANISOU 1046  O   GLU A 181    13557  15677   9838  -1708  -1233   2688       O\\nATOM   1047  CB  GLU A 181       8.426  15.780 -23.782  1.00111.20           C\\nANISOU 1047  CB  GLU A 181    14562  18052   9639  -2014   -799   2478       C\\nATOM   1048  CG  GLU A 181       8.455  15.363 -25.237  1.00118.18           C\\nANISOU 1048  CG  GLU A 181    15491  19499   9912  -2150   -768   2439       C\\nATOM   1049  CD  GLU A 181       9.558  14.373 -25.529  1.00125.80           C\\nANISOU 1049  CD  GLU A 181    16244  20936  10620  -2119   -359   2054       C\\nATOM   1050  OE1 GLU A 181       9.649  13.356 -24.809  1.00127.00           O\\nANISOU 1050  OE1 GLU A 181    16258  20997  10999  -1858   -200   1630       O\\nATOM   1051  OE2 GLU A 181      10.339  14.618 -26.473  1.00132.18           O\\nANISOU 1051  OE2 GLU A 181    16999  22090  11133  -2311   -210   2123       O\\nATOM   1052  N   CYS A 182       6.490  15.185 -21.461  1.00 85.77           N\\nANISOU 1052  N   CYS A 182    11262  13784   7544  -1421  -1042   2020       N\\nATOM   1053  CA  CYS A 182       6.326  14.886 -20.051  1.00 85.01           C\\nANISOU 1053  CA  CYS A 182    11057  13309   7934  -1219   -963   1809       C\\nATOM   1054  C   CYS A 182       7.659  15.034 -19.325  1.00 85.25           C\\nANISOU 1054  C   CYS A 182    10998  13354   8038  -1280   -699   1848       C\\nATOM   1055  O   CYS A 182       8.737  14.991 -19.927  1.00 87.66           O\\nANISOU 1055  O   CYS A 182    11266  14030   8011  -1441   -506   1910       O\\nATOM   1056  CB  CYS A 182       5.770  13.473 -19.864  1.00 85.07           C\\nANISOU 1056  CB  CYS A 182    10980  13320   8021  -1022   -869   1364       C\\nATOM   1057  SG  CYS A 182       5.430  13.056 -18.147  1.00 88.55           S\\nANISOU 1057  SG  CYS A 182    11313  13325   9006   -826   -793   1143       S\\nATOM   1058  N   ILE A 183       7.575  15.222 -18.009  1.00 86.69           N\\nANISOU 1058  N   ILE A 183    11127  13162   8650  -1153   -694   1796       N\\nATOM   1059  CA  ILE A 183       8.782  15.505 -17.243  1.00 88.06           C\\nANISOU 1059  CA  ILE A 183    11221  13307   8931  -1209   -498   1856       C\\nATOM   1060  C   ILE A 183       9.631  14.253 -17.070  1.00 90.76           C\\nANISOU 1060  C   ILE A 183    11430  13873   9183  -1113   -193   1518       C\\nATOM   1061  O   ILE A 183      10.856  14.349 -16.944  1.00 89.70           O\\nANISOU 1061  O   ILE A 183    11199  13916   8966  -1199     -1   1550       O\\nATOM   1062  CB  ILE A 183       8.428  16.141 -15.888  1.00 82.65           C\\nANISOU 1062  CB  ILE A 183    10529  12169   8706  -1098   -610   1893       C\\nATOM   1063  CG1 ILE A 183       9.689  16.703 -15.236  1.00 81.90           C\\nANISOU 1063  CG1 ILE A 183    10377  12044   8696  -1203   -475   2026       C\\nATOM   1064  CG2 ILE A 183       7.755  15.134 -14.972  1.00 80.02           C\\nANISOU 1064  CG2 ILE A 183    10121  11657   8626   -869   -543   1542       C\\nATOM   1065  CD1 ILE A 183      10.562  17.486 -16.201  1.00 77.13           C\\nANISOU 1065  CD1 ILE A 183     9815  11711   7778  -1501   -472   2363       C\\nATOM   1066  N   ILE A 184       9.020  13.066 -17.078  1.00 86.05           N\\nANISOU 1066  N   ILE A 184    10817  13266   8612   -938   -167   1182       N\\nATOM   1067  CA  ILE A 184       9.808  11.848 -16.945  1.00 81.50           C\\nANISOU 1067  CA  ILE A 184    10141  12849   7978   -818     61    843       C\\nATOM   1068  C   ILE A 184      10.649  11.603 -18.187  1.00 77.44           C\\nANISOU 1068  C   ILE A 184     9566  12848   7010   -918    205    786       C\\nATOM   1069  O   ILE A 184      11.589  10.802 -18.148  1.00 77.18           O\\nANISOU 1069  O   ILE A 184     9408  13014   6904   -822    403    514       O\\nATOM   1070  CB  ILE A 184       8.907  10.636 -16.645  1.00 80.64           C\\nANISOU 1070  CB  ILE A 184    10060  12549   8030   -635      7    515       C\\nATOM   1071  CG1 ILE A 184       9.694   9.574 -15.876  1.00 78.25           C\\nANISOU 1071  CG1 ILE A 184     9688  12171   7873   -478    168    222       C\\nATOM   1072  CG2 ILE A 184       8.346  10.052 -17.932  1.00 83.92           C\\nANISOU 1072  CG2 ILE A 184    10523  13226   8137   -643    -67    367       C\\nATOM   1073  CD1 ILE A 184       8.861   8.383 -15.456  1.00 80.33           C\\nANISOU 1073  CD1 ILE A 184    10011  12185   8326   -346     90    -54       C\\nATOM   1074  N   ALA A 185      10.335  12.279 -19.291  1.00 80.23           N\\nANISOU 1074  N   ALA A 185     9999  13442   7044  -1105     98   1028       N\\nATOM   1075  CA  ALA A 185      11.162  12.234 -20.487  1.00 83.51           C\\nANISOU 1075  CA  ALA A 185    10349  14420   6960  -1262    251   1031       C\\nATOM   1076  C   ALA A 185      12.352  13.177 -20.411  1.00 83.75           C\\nANISOU 1076  C   ALA A 185    10288  14647   6887  -1499    393   1327       C\\nATOM   1077  O   ALA A 185      13.207  13.143 -21.301  1.00 89.61           O\\nANISOU 1077  O   ALA A 185    10921  15924   7202  -1661    576   1320       O\\nATOM   1078  CB  ALA A 185      10.320  12.565 -21.723  1.00 73.89           C\\nANISOU 1078  CB  ALA A 185     9279  13403   5395  -1401     57   1201       C\\nATOM   1079  N   ASN A 186      12.425  14.011 -19.384  1.00 87.95           N\\nANISOU 1079  N   ASN A 186    10846  14788   7782  -1536    315   1567       N\\nATOM   1080  CA  ASN A 186      13.545  14.931 -19.235  1.00 90.37           C\\nANISOU 1080  CA  ASN A 186    11066  15232   8039  -1784    421   1852       C\\nATOM   1081  C   ASN A 186      14.781  14.156 -18.795  1.00 93.04           C\\nANISOU 1081  C   ASN A 186    11153  15806   8392  -1671    718   1526       C\\nATOM   1082  O   ASN A 186      14.734  13.472 -17.765  1.00 90.82           O\\nANISOU 1082  O   ASN A 186    10830  15214   8462  -1399    737   1252       O\\nATOM   1083  CB  ASN A 186      13.200  16.017 -18.220  1.00 86.22           C\\nANISOU 1083  CB  ASN A 186    10651  14175   7934  -1820    209   2150       C\\nATOM   1084  CG  ASN A 186      14.162  17.185 -18.259  1.00 89.29           C\\nANISOU 1084  CG  ASN A 186    11013  14659   8255  -2152    225   2537       C\\nATOM   1085  OD1 ASN A 186      15.380  17.008 -18.241  1.00 95.97           O\\nANISOU 1085  OD1 ASN A 186    11655  15837   8971  -2255    479   2464       O\\nATOM   1086  ND2 ASN A 186      13.616  18.393 -18.314  1.00 87.60           N\\nANISOU 1086  ND2 ASN A 186    10997  14142   8145  -2325    -71   2943       N\\nATOM   1087  N   PRO A 187      15.895  14.232 -19.527  1.00 95.07           N\\nANISOU 1087  N   PRO A 187    11229  16621   8273  -1873    941   1541       N\\nATOM   1088  CA  PRO A 187      17.095  13.486 -19.110  1.00 94.27           C\\nANISOU 1088  CA  PRO A 187    10845  16765   8209  -1726   1203   1183       C\\nATOM   1089  C   PRO A 187      17.587  13.857 -17.721  1.00 93.98           C\\nANISOU 1089  C   PRO A 187    10749  16330   8627  -1662   1185   1242       C\\nATOM   1090  O   PRO A 187      18.317  13.067 -17.109  1.00 94.56           O\\nANISOU 1090  O   PRO A 187    10638  16436   8855  -1433   1319    896       O\\nATOM   1091  CB  PRO A 187      18.127  13.845 -20.190  1.00 87.30           C\\nANISOU 1091  CB  PRO A 187     9769  16534   6867  -2026   1406   1271       C\\nATOM   1092  CG  PRO A 187      17.630  15.128 -20.784  1.00 81.91           C\\nANISOU 1092  CG  PRO A 187     9311  15710   6102  -2368   1189   1793       C\\nATOM   1093  CD  PRO A 187      16.135  15.035 -20.737  1.00 89.48           C\\nANISOU 1093  CD  PRO A 187    10552  16349   7098  -2256    952   1890       C\\nATOM   1094  N   ALA A 188      17.198  15.020 -17.198  1.00 89.90           N\\nANISOU 1094  N   ALA A 188    10393  15427   8337  -1837    994   1648       N\\nATOM   1095  CA  ALA A 188      17.621  15.462 -15.877  1.00 87.20           C\\nANISOU 1095  CA  ALA A 188    10012  14708   8411  -1788    952   1704       C\\nATOM   1096  C   ALA A 188      16.681  15.017 -14.764  1.00 83.84           C\\nANISOU 1096  C   ALA A 188     9732  13727   8396  -1473    795   1536       C\\nATOM   1097  O   ALA A 188      16.983  15.253 -13.591  1.00 75.80           O\\nANISOU 1097  O   ALA A 188     8687  12406   7707  -1395    761   1530       O\\nATOM   1098  CB  ALA A 188      17.750  16.987 -15.848  1.00 80.85           C\\nANISOU 1098  CB  ALA A 188     9302  13764   7654  -2142    804   2201       C\\nATOM   1099  N   PHE A 189      15.554  14.386 -15.094  1.00 80.92           N\\nANISOU 1099  N   PHE A 189     9504  13244   7997  -1314    698   1400       N\\nATOM   1100  CA  PHE A 189      14.640  13.936 -14.051  1.00 78.27           C\\nANISOU 1100  CA  PHE A 189     9281  12440   8018  -1065    570   1248       C\\nATOM   1101  C   PHE A 189      15.276  12.851 -13.193  1.00 80.35           C\\nANISOU 1101  C   PHE A 189     9430  12648   8450   -824    697    901       C\\nATOM   1102  O   PHE A 189      15.128  12.856 -11.964  1.00 75.11           O\\nANISOU 1102  O   PHE A 189     8806  11626   8105   -710    633    876       O\\nATOM   1103  CB  PHE A 189      13.335  13.437 -14.671  1.00 80.58           C\\nANISOU 1103  CB  PHE A 189     9715  12675   8225   -983    445   1165       C\\nATOM   1104  CG  PHE A 189      12.426  12.754 -13.693  1.00 85.91           C\\nANISOU 1104  CG  PHE A 189    10465  12965   9214   -760    358    965       C\\nATOM   1105  CD1 PHE A 189      11.690  13.490 -12.780  1.00 86.83           C\\nANISOU 1105  CD1 PHE A 189    10658  12708   9625   -749    203   1115       C\\nATOM   1106  CD2 PHE A 189      12.306  11.375 -13.683  1.00 84.50           C\\nANISOU 1106  CD2 PHE A 189    10274  12804   9028   -575    421    619       C\\nATOM   1107  CE1 PHE A 189      10.853  12.861 -11.873  1.00 82.22           C\\nANISOU 1107  CE1 PHE A 189    10115  11841   9283   -588    152    936       C\\nATOM   1108  CE2 PHE A 189      11.471  10.742 -12.779  1.00 79.97           C\\nANISOU 1108  CE2 PHE A 189     9777  11887   8720   -435    339    479       C\\nATOM   1109  CZ  PHE A 189      10.745  11.486 -11.874  1.00 75.49           C\\nANISOU 1109  CZ  PHE A 189     9262  11015   8404   -457    224    645       C\\nATOM   1110  N   VAL A 190      15.990  11.913 -13.820  1.00 82.64           N\\nANISOU 1110  N   VAL A 190     9581  13296   8524   -736    857    620       N\\nATOM   1111  CA  VAL A 190      16.608  10.825 -13.066  1.00 79.80           C\\nANISOU 1111  CA  VAL A 190     9129  12855   8338   -476    921    274       C\\nATOM   1112  C   VAL A 190      17.619  11.375 -12.070  1.00 73.96           C\\nANISOU 1112  C   VAL A 190     8263  12038   7801   -501    965    362       C\\nATOM   1113  O   VAL A 190      17.647  10.963 -10.905  1.00 69.81           O\\nANISOU 1113  O   VAL A 190     7780  11184   7561   -328    899    257       O\\nATOM   1114  CB  VAL A 190      17.246   9.799 -14.024  1.00 76.29           C\\nANISOU 1114  CB  VAL A 190     8531  12834   7621   -350   1058    -85       C\\nATOM   1115  CG1 VAL A 190      18.329   8.997 -13.321  1.00 73.98           C\\nANISOU 1115  CG1 VAL A 190     8071  12543   7496   -111   1121   -401       C\\nATOM   1116  CG2 VAL A 190      16.181   8.863 -14.570  1.00 70.22           C\\nANISOU 1116  CG2 VAL A 190     7922  11973   6787   -219    957   -292       C\\nATOM   1117  N   VAL A 191      18.449  12.327 -12.502  1.00 74.89           N\\nANISOU 1117  N   VAL A 191     8232  12459   7764   -745   1062    574       N\\nATOM   1118  CA  VAL A 191      19.440  12.910 -11.603  1.00 69.99           C\\nANISOU 1118  CA  VAL A 191     7472  11783   7337   -800   1089    659       C\\nATOM   1119  C   VAL A 191      18.756  13.666 -10.472  1.00 71.73           C\\nANISOU 1119  C   VAL A 191     7882  11494   7879   -818    904    880       C\\nATOM   1120  O   VAL A 191      19.167  13.580  -9.308  1.00 74.22           O\\nANISOU 1120  O   VAL A 191     8168  11584   8449   -696    866    802       O\\nATOM   1121  CB  VAL A 191      20.401  13.820 -12.387  1.00 69.86           C\\nANISOU 1121  CB  VAL A 191     7256  12216   7071  -1128   1224    873       C\\nATOM   1122  CG1 VAL A 191      21.588  14.210 -11.518  1.00 61.69           C\\nANISOU 1122  CG1 VAL A 191     6014  11194   6229  -1167   1269    875       C\\nATOM   1123  CG2 VAL A 191      20.860  13.135 -13.669  1.00 71.25           C\\nANISOU 1123  CG2 VAL A 191     7250  12975   6848  -1136   1419    651       C\\nATOM   1124  N   TYR A 192      17.698  14.409 -10.792  1.00 73.30           N\\nANISOU 1124  N   TYR A 192     8269  11519   8064   -952    769   1133       N\\nATOM   1125  CA  TYR A 192      17.008  15.209  -9.786  1.00 69.49           C\\nANISOU 1125  CA  TYR A 192     7937  10591   7877   -952    585   1300       C\\nATOM   1126  C   TYR A 192      16.386  14.323  -8.714  1.00 69.05           C\\nANISOU 1126  C   TYR A 192     7966  10230   8040   -683    540   1063       C\\nATOM   1127  O   TYR A 192      16.743  14.407  -7.534  1.00 70.50           O\\nANISOU 1127  O   TYR A 192     8135  10210   8443   -602    510   1018       O\\nATOM   1128  CB  TYR A 192      15.946  16.079 -10.460  1.00 70.53           C\\nANISOU 1128  CB  TYR A 192     8235  10616   7948  -1102    419   1566       C\\nATOM   1129  CG  TYR A 192      15.223  17.022  -9.524  1.00 71.79           C\\nANISOU 1129  CG  TYR A 192     8522  10343   8412  -1083    204   1704       C\\nATOM   1130  CD1 TYR A 192      15.814  18.212  -9.114  1.00 72.52           C\\nANISOU 1130  CD1 TYR A 192     8604  10305   8647  -1251    105   1926       C\\nATOM   1131  CD2 TYR A 192      13.943  16.733  -9.066  1.00 75.40           C\\nANISOU 1131  CD2 TYR A 192     9093  10543   9014   -904     92   1589       C\\nATOM   1132  CE1 TYR A 192      15.157  19.082  -8.265  1.00 72.60           C\\nANISOU 1132  CE1 TYR A 192     8724   9917   8942  -1200   -114   1996       C\\nATOM   1133  CE2 TYR A 192      13.275  17.600  -8.217  1.00 78.40           C\\nANISOU 1133  CE2 TYR A 192     9549  10580   9658   -860    -96   1656       C\\nATOM   1134  CZ  TYR A 192      13.887  18.772  -7.820  1.00 72.16           C\\nANISOU 1134  CZ  TYR A 192     8758   9648   9013   -988   -206   1843       C\\nATOM   1135  OH  TYR A 192      13.226  19.632  -6.973  1.00 63.34           O\\nANISOU 1135  OH  TYR A 192     7711   8188   8168   -909   -415   1853       O\\nATOM   1136  N   SER A 193      15.457  13.449  -9.114  1.00 72.61           N\\nANISOU 1136  N   SER A 193     8511  10659   8417   -566    526    916       N\\nATOM   1137  CA  SER A 193      14.715  12.654  -8.139  1.00 77.34           C\\nANISOU 1137  CA  SER A 193     9213  10968   9205   -382    469    746       C\\nATOM   1138  C   SER A 193      15.615  11.681  -7.386  1.00 75.22           C\\nANISOU 1138  C   SER A 193     8884  10678   9019   -217    535    524       C\\nATOM   1139  O   SER A 193      15.294  11.286  -6.260  1.00 76.80           O\\nANISOU 1139  O   SER A 193     9170  10614   9397   -116    473    460       O\\nATOM   1140  CB  SER A 193      13.580  11.897  -8.830  1.00 79.11           C\\nANISOU 1140  CB  SER A 193     9536  11195   9327   -336    430    640       C\\nATOM   1141  OG  SER A 193      14.075  10.934  -9.741  1.00 69.99           O\\nANISOU 1141  OG  SER A 193     8324  10300   7968   -274    524    442       O\\nATOM   1142  N   SER A 194      16.739  11.283  -7.980  1.00 71.25           N\\nANISOU 1142  N   SER A 194     8226  10467   8381   -186    646    398       N\\nATOM   1143  CA  SER A 194      17.664  10.407  -7.271  1.00 72.26           C\\nANISOU 1143  CA  SER A 194     8279  10561   8614      6    663    171       C\\nATOM   1144  C   SER A 194      18.401  11.166  -6.177  1.00 76.18           C\\nANISOU 1144  C   SER A 194     8709  10947   9290    -29    635    286       C\\nATOM   1145  O   SER A 194      18.423  10.741  -5.014  1.00 72.02           O\\nANISOU 1145  O   SER A 194     8263  10164   8939     99    550    218       O\\nATOM   1146  CB  SER A 194      18.661   9.784  -8.246  1.00 72.31           C\\nANISOU 1146  CB  SER A 194     8087  10955   8432     84    784    -57       C\\nATOM   1147  OG  SER A 194      17.998   9.092  -9.286  1.00 80.43           O\\nANISOU 1147  OG  SER A 194     9180  12101   9277    122    797   -194       O\\nATOM   1148  N   ILE A 195      19.005  12.300  -6.530  1.00 77.08           N\\nANISOU 1148  N   ILE A 195     8687  11249   9349   -226    688    474       N\\nATOM   1149  CA  ILE A 195      19.847  13.021  -5.580  1.00 70.51           C\\nANISOU 1149  CA  ILE A 195     7763  10342   8685   -272    652    555       C\\nATOM   1150  C   ILE A 195      18.988  13.748  -4.552  1.00 66.52           C\\nANISOU 1150  C   ILE A 195     7438   9466   8370   -304    511    708       C\\nATOM   1151  O   ILE A 195      19.129  13.541  -3.341  1.00 74.63           O\\nANISOU 1151  O   ILE A 195     8511  10286   9557   -186    438    633       O\\nATOM   1152  CB  ILE A 195      20.787  13.987  -6.321  1.00 68.49           C\\nANISOU 1152  CB  ILE A 195     7299  10412   8313   -520    744    715       C\\nATOM   1153  CG1 ILE A 195      21.784  13.200  -7.177  1.00 66.22           C\\nANISOU 1153  CG1 ILE A 195     6764  10568   7828   -459    911    488       C\\nATOM   1154  CG2 ILE A 195      21.510  14.892  -5.337  1.00 63.89           C\\nANISOU 1154  CG2 ILE A 195     6643   9700   7932   -613    668    829       C\\nATOM   1155  CD1 ILE A 195      22.738  14.064  -7.971  1.00 56.97           C\\nANISOU 1155  CD1 ILE A 195     5348   9813   6484   -752   1041    642       C\\nATOM   1156  N   VAL A 196      18.073  14.597  -5.019  1.00 62.66           N\\nANISOU 1156  N   VAL A 196     7052   8902   7854   -450    454    905       N\\nATOM   1157  CA  VAL A 196      17.332  15.463  -4.105  1.00 67.97           C\\nANISOU 1157  CA  VAL A 196     7847   9264   8715   -469    309   1012       C\\nATOM   1158  C   VAL A 196      16.343  14.656  -3.269  1.00 67.07           C\\nANISOU 1158  C   VAL A 196     7868   8944   8670   -296    275    861       C\\nATOM   1159  O   VAL A 196      16.268  14.814  -2.046  1.00 61.49           O\\nANISOU 1159  O   VAL A 196     7206   8054   8102   -231    210    818       O\\nATOM   1160  CB  VAL A 196      16.626  16.582  -4.888  1.00 64.23           C\\nANISOU 1160  CB  VAL A 196     7440   8750   8216   -643    212   1244       C\\nATOM   1161  CG1 VAL A 196      15.849  17.474  -3.945  1.00 52.97           C\\nANISOU 1161  CG1 VAL A 196     6116   7001   7009   -610     37   1287       C\\nATOM   1162  CG2 VAL A 196      17.638  17.392  -5.674  1.00 71.96           C\\nANISOU 1162  CG2 VAL A 196     8304   9935   9102   -883    238   1445       C\\nATOM   1163  N   SER A 197      15.571  13.778  -3.911  1.00 68.31           N\\nANISOU 1163  N   SER A 197     8091   9151   8712   -244    315    780       N\\nATOM   1164  CA  SER A 197      14.505  13.073  -3.211  1.00 64.29           C\\nANISOU 1164  CA  SER A 197     7706   8466   8256   -150    280    676       C\\nATOM   1165  C   SER A 197      14.986  11.839  -2.460  1.00 64.86           C\\nANISOU 1165  C   SER A 197     7819   8478   8346    -22    301    516       C\\nATOM   1166  O   SER A 197      14.304  11.401  -1.528  1.00 71.84           O\\nANISOU 1166  O   SER A 197     8812   9202   9284      7    262    476       O\\nATOM   1167  CB  SER A 197      13.401  12.668  -4.191  1.00 64.34           C\\nANISOU 1167  CB  SER A 197     7768   8525   8155   -175    281    661       C\\nATOM   1168  OG  SER A 197      12.416  13.677  -4.297  1.00 65.40           O\\nANISOU 1168  OG  SER A 197     7921   8583   8345   -241    188    775       O\\nATOM   1169  N   PHE A 198      16.134  11.265  -2.824  1.00 56.65           N\\nANISOU 1169  N   PHE A 198     6693   7571   7259     50    348    422       N\\nATOM   1170  CA  PHE A 198      16.563  10.006  -2.225  1.00 61.84           C\\nANISOU 1170  CA  PHE A 198     7413   8131   7953    205    308    258       C\\nATOM   1171  C   PHE A 198      17.951  10.080  -1.597  1.00 66.94           C\\nANISOU 1171  C   PHE A 198     7945   8814   8677    293    283    207       C\\nATOM   1172  O   PHE A 198      18.076   9.853  -0.391  1.00 63.30           O\\nANISOU 1172  O   PHE A 198     7574   8170   8306    352    191    202       O\\nATOM   1173  CB  PHE A 198      16.518   8.887  -3.269  1.00 62.27           C\\nANISOU 1173  CB  PHE A 198     7477   8279   7904    290    331     91       C\\nATOM   1174  CG  PHE A 198      16.836   7.525  -2.714  1.00 71.87           C\\nANISOU 1174  CG  PHE A 198     8800   9318   9188    461    226    -82       C\\nATOM   1175  CD1 PHE A 198      15.889   6.822  -1.986  1.00 73.26           C\\nANISOU 1175  CD1 PHE A 198     9194   9229   9414    432    130    -54       C\\nATOM   1176  CD2 PHE A 198      18.074   6.944  -2.927  1.00 66.14           C\\nANISOU 1176  CD2 PHE A 198     7955   8695   8481    641    204   -273       C\\nATOM   1177  CE1 PHE A 198      16.173   5.566  -1.481  1.00 70.07           C\\nANISOU 1177  CE1 PHE A 198     8932   8611   9079    560    -15   -171       C\\nATOM   1178  CE2 PHE A 198      18.365   5.687  -2.423  1.00 70.55           C\\nANISOU 1178  CE2 PHE A 198     8637   9036   9134    826     45   -436       C\\nATOM   1179  CZ  PHE A 198      17.412   4.997  -1.700  1.00 69.64           C\\nANISOU 1179  CZ  PHE A 198     8787   8602   9070    775    -79   -363       C\\nATOM   1180  N   TYR A 199      18.996  10.380  -2.373  1.00 67.17           N\\nANISOU 1180  N   TYR A 199     7766   9103   8654    290    360    166       N\\nATOM   1181  CA  TYR A 199      20.356  10.230  -1.861  1.00 67.05           C\\nANISOU 1181  CA  TYR A 199     7598   9159   8719    402    329     58       C\\nATOM   1182  C   TYR A 199      20.656  11.224  -0.746  1.00 67.17           C\\nANISOU 1182  C   TYR A 199     7604   9058   8859    323    261    193       C\\nATOM   1183  O   TYR A 199      21.379  10.897   0.202  1.00 60.26           O\\nANISOU 1183  O   TYR A 199     6716   8098   8082    445    161    112       O\\nATOM   1184  CB  TYR A 199      21.367  10.375  -2.997  1.00 71.88           C\\nANISOU 1184  CB  TYR A 199     7935  10155   9221    380    457    -32       C\\nATOM   1185  CG  TYR A 199      21.372   9.197  -3.942  1.00 81.30           C\\nANISOU 1185  CG  TYR A 199     9102  11489  10299    540    498   -275       C\\nATOM   1186  CD1 TYR A 199      21.185   7.907  -3.469  1.00 86.13           C\\nANISOU 1186  CD1 TYR A 199     9871  11856  10998    769    359   -463       C\\nATOM   1187  CD2 TYR A 199      21.545   9.374  -5.307  1.00 83.10           C\\nANISOU 1187  CD2 TYR A 199     9165  12088  10320    449    652   -315       C\\nATOM   1188  CE1 TYR A 199      21.177   6.825  -4.325  1.00 85.63           C\\nANISOU 1188  CE1 TYR A 199     9799  11878  10859    933    355   -719       C\\nATOM   1189  CE2 TYR A 199      21.538   8.297  -6.171  1.00 80.51           C\\nANISOU 1189  CE2 TYR A 199     8809  11905   9875    615    680   -585       C\\nATOM   1190  CZ  TYR A 199      21.352   7.026  -5.674  1.00 76.43           C\\nANISOU 1190  CZ  TYR A 199     8448  11104   9487    871    522   -803       C\\nATOM   1191  OH  TYR A 199      21.344   5.950  -6.531  1.00 69.70           O\\nANISOU 1191  OH  TYR A 199     7579  10355   8547   1053    510  -1106       O\\nATOM   1192  N   VAL A 200      20.116  12.435  -0.831  1.00 65.74           N\\nANISOU 1192  N   VAL A 200     7439   8856   8685    133    281    383       N\\nATOM   1193  CA  VAL A 200      20.375  13.434   0.206  1.00 71.58           C\\nANISOU 1193  CA  VAL A 200     8173   9468   9555     66    193    476       C\\nATOM   1194  C   VAL A 200      19.616  13.076   1.483  1.00 70.25           C\\nANISOU 1194  C   VAL A 200     8210   9046   9435    156     95    445       C\\nATOM   1195  O   VAL A 200      20.203  13.156   2.571  1.00 66.48           O\\nANISOU 1195  O   VAL A 200     7736   8490   9035    213      0    407       O\\nATOM   1196  CB  VAL A 200      20.038  14.854  -0.281  1.00 71.46           C\\nANISOU 1196  CB  VAL A 200     8129   9461   9562   -148    192    671       C\\nATOM   1197  CG1 VAL A 200      20.109  15.848   0.873  1.00 70.31           C\\nANISOU 1197  CG1 VAL A 200     8017   9123   9575   -187     60    720       C\\nATOM   1198  CG2 VAL A 200      20.992  15.264  -1.393  1.00 67.72           C\\nANISOU 1198  CG2 VAL A 200     7444   9277   9011   -300    285    742       C\\nATOM   1199  N   PRO A 201      18.333  12.691   1.432  1.00 68.63           N\\nANISOU 1199  N   PRO A 201     8167   8739   9171    150    111    459       N\\nATOM   1200  CA  PRO A 201      17.717  12.147   2.655  1.00 67.01           C\\nANISOU 1200  CA  PRO A 201     8135   8363   8962    204     43    424       C\\nATOM   1201  C   PRO A 201      18.416  10.898   3.166  1.00 63.12           C\\nANISOU 1201  C   PRO A 201     7712   7811   8461    342    -32    331       C\\nATOM   1202  O   PRO A 201      18.541  10.711   4.383  1.00 64.72           O\\nANISOU 1202  O   PRO A 201     8019   7903   8669    376   -131    332       O\\nATOM   1203  CB  PRO A 201      16.275  11.860   2.217  1.00 66.92           C\\nANISOU 1203  CB  PRO A 201     8227   8319   8879    142     97    446       C\\nATOM   1204  CG  PRO A 201      16.022  12.833   1.137  1.00 66.63           C\\nANISOU 1204  CG  PRO A 201     8086   8379   8852     55    144    523       C\\nATOM   1205  CD  PRO A 201      17.319  12.916   0.383  1.00 66.70           C\\nANISOU 1205  CD  PRO A 201     7946   8542   8857     61    178    525       C\\nATOM   1206  N   PHE A 202      18.884  10.041   2.258  1.00 56.10           N\\nANISOU 1206  N   PHE A 202     6771   6992   7551    435    -11    238       N\\nATOM   1207  CA  PHE A 202      19.593   8.829   2.655  1.00 63.87           C\\nANISOU 1207  CA  PHE A 202     7821   7882   8566    610   -137    119       C\\nATOM   1208  C   PHE A 202      20.816   9.156   3.509  1.00 70.36           C\\nANISOU 1208  C   PHE A 202     8539   8718   9475    697   -242     86       C\\nATOM   1209  O   PHE A 202      20.977   8.621   4.613  1.00 72.54           O\\nANISOU 1209  O   PHE A 202     8969   8826   9768    771   -400     91       O\\nATOM   1210  CB  PHE A 202      19.992   8.047   1.402  1.00 62.85           C\\nANISOU 1210  CB  PHE A 202     7591   7872   8416    726    -97    -41       C\\nATOM   1211  CG  PHE A 202      20.499   6.659   1.671  1.00 70.17           C\\nANISOU 1211  CG  PHE A 202     8620   8639   9403    941   -273   -200       C\\nATOM   1212  CD1 PHE A 202      20.468   6.114   2.942  1.00 73.47           C\\nANISOU 1212  CD1 PHE A 202     9254   8795   9864    982   -462   -139       C\\nATOM   1213  CD2 PHE A 202      21.014   5.899   0.638  1.00 76.10           C\\nANISOU 1213  CD2 PHE A 202     9257   9501  10156   1108   -271   -423       C\\nATOM   1214  CE1 PHE A 202      20.939   4.847   3.177  1.00 78.88           C\\nANISOU 1214  CE1 PHE A 202    10067   9279  10625   1182   -682   -264       C\\nATOM   1215  CE2 PHE A 202      21.485   4.628   0.866  1.00 75.62           C\\nANISOU 1215  CE2 PHE A 202     9296   9248  10187   1343   -483   -603       C\\nATOM   1216  CZ  PHE A 202      21.447   4.100   2.137  1.00 79.28           C\\nANISOU 1216  CZ  PHE A 202    10003   9395  10724   1380   -707   -507       C\\nATOM   1217  N   ILE A 203      21.692  10.031   3.011  1.00 69.89           N\\nANISOU 1217  N   ILE A 203     8223   8871   9462    667   -169     66       N\\nATOM   1218  CA  ILE A 203      22.931  10.333   3.726  1.00 70.07           C\\nANISOU 1218  CA  ILE A 203     8101   8940   9583    743   -275      9       C\\nATOM   1219  C   ILE A 203      22.628  10.977   5.074  1.00 68.51           C\\nANISOU 1219  C   ILE A 203     8043   8585   9403    671   -375    114       C\\nATOM   1220  O   ILE A 203      23.185  10.584   6.106  1.00 61.96           O\\nANISOU 1220  O   ILE A 203     7279   7659   8605    783   -545     72       O\\nATOM   1221  CB  ILE A 203      23.843  11.227   2.870  1.00 67.00           C\\nANISOU 1221  CB  ILE A 203     7390   8840   9226    648   -158     -7       C\\nATOM   1222  CG1 ILE A 203      24.189  10.534   1.555  1.00 68.52           C\\nANISOU 1222  CG1 ILE A 203     7420   9264   9349    728    -43   -152       C\\nATOM   1223  CG2 ILE A 203      25.111  11.566   3.623  1.00 62.39           C\\nANISOU 1223  CG2 ILE A 203     6625   8319   8761    704   -276    -75       C\\nATOM   1224  CD1 ILE A 203      24.882  11.438   0.566  1.00 75.16           C\\nANISOU 1224  CD1 ILE A 203     7956  10453  10148    555    118   -121       C\\nATOM   1225  N   VAL A 204      21.738  11.974   5.082  1.00 68.09           N\\nANISOU 1225  N   VAL A 204     8035   8512   9324    499   -292    232       N\\nATOM   1226  CA  VAL A 204      21.439  12.706   6.313  1.00 64.98           C\\nANISOU 1226  CA  VAL A 204     7739   8013   8938    443   -378    276       C\\nATOM   1227  C   VAL A 204      20.881  11.767   7.375  1.00 65.55           C\\nANISOU 1227  C   VAL A 204     8061   7945   8902    504   -469    277       C\\nATOM   1228  O   VAL A 204      21.332  11.764   8.527  1.00 66.60           O\\nANISOU 1228  O   VAL A 204     8259   8027   9017    550   -610    260       O\\nATOM   1229  CB  VAL A 204      20.471  13.865   6.027  1.00 56.49           C\\nANISOU 1229  CB  VAL A 204     6664   6928   7872    291   -296    354       C\\nATOM   1230  CG1 VAL A 204      19.900  14.399   7.325  1.00 59.98           C\\nANISOU 1230  CG1 VAL A 204     7227   7276   8289    274   -375    333       C\\nATOM   1231  CG2 VAL A 204      21.185  14.972   5.267  1.00 55.27           C\\nANISOU 1231  CG2 VAL A 204     6299   6869   7831    182   -275    403       C\\nATOM   1232  N   THR A 205      19.886  10.960   7.005  1.00 66.29           N\\nANISOU 1232  N   THR A 205     8302   7982   8903    478   -403    312       N\\nATOM   1233  CA  THR A 205      19.340   9.991   7.947  1.00 66.07           C\\nANISOU 1233  CA  THR A 205     8524   7824   8753    475   -492    356       C\\nATOM   1234  C   THR A 205      20.407   9.003   8.395  1.00 73.22           C\\nANISOU 1234  C   THR A 205     9501   8627   9694    637   -693    319       C\\nATOM   1235  O   THR A 205      20.450   8.611   9.567  1.00 73.97           O\\nANISOU 1235  O   THR A 205     9780   8626   9698    635   -843    376       O\\nATOM   1236  CB  THR A 205      18.162   9.258   7.313  1.00 64.13           C\\nANISOU 1236  CB  THR A 205     8398   7536   8434    391   -397    399       C\\nATOM   1237  OG1 THR A 205      17.159  10.210   6.937  1.00 70.05           O\\nANISOU 1237  OG1 THR A 205     9065   8385   9167    268   -244    415       O\\nATOM   1238  CG2 THR A 205      17.567   8.265   8.291  1.00 59.18           C\\nANISOU 1238  CG2 THR A 205     8038   6780   7668    317   -492    485       C\\nATOM   1239  N   LEU A 206      21.282   8.594   7.476  1.00 71.22           N\\nANISOU 1239  N   LEU A 206     9095   8407   9557    784   -714    211       N\\nATOM   1240  CA  LEU A 206      22.343   7.663   7.839  1.00 69.37           C\\nANISOU 1240  CA  LEU A 206     8891   8070   9395    992   -940    126       C\\nATOM   1241  C   LEU A 206      23.325   8.302   8.810  1.00 67.69           C\\nANISOU 1241  C   LEU A 206     8584   7907   9228   1046  -1074    104       C\\nATOM   1242  O   LEU A 206      23.847   7.629   9.705  1.00 63.83           O\\nANISOU 1242  O   LEU A 206     8237   7281   8736   1166  -1318    106       O\\nATOM   1243  CB  LEU A 206      23.069   7.177   6.586  1.00 68.74           C\\nANISOU 1243  CB  LEU A 206     8603   8086   9429   1162   -911    -54       C\\nATOM   1244  CG  LEU A 206      24.254   6.253   6.864  1.00 66.60           C\\nANISOU 1244  CG  LEU A 206     8300   7728   9276   1438  -1170   -212       C\\nATOM   1245  CD1 LEU A 206      23.779   4.999   7.577  1.00 68.61           C\\nANISOU 1245  CD1 LEU A 206     8929   7645   9495   1492  -1416   -131       C\\nATOM   1246  CD2 LEU A 206      24.981   5.908   5.578  1.00 65.91           C\\nANISOU 1246  CD2 LEU A 206     7933   7826   9284   1614  -1102   -453       C\\nATOM   1247  N   LEU A 207      23.592   9.597   8.647  1.00 71.05           N\\nANISOU 1247  N   LEU A 207     8784   8507   9703    951   -950     91       N\\nATOM   1248  CA  LEU A 207      24.489  10.279   9.572  1.00 68.27           C\\nANISOU 1248  CA  LEU A 207     8336   8199   9405    979  -1088     58       C\\nATOM   1249  C   LEU A 207      23.856  10.418  10.949  1.00 68.21           C\\nANISOU 1249  C   LEU A 207     8586   8088   9244    897  -1186    154       C\\nATOM   1250  O   LEU A 207      24.552  10.352  11.967  1.00 66.32           O\\nANISOU 1250  O   LEU A 207     8392   7815   8989    976  -1395    132       O\\nATOM   1251  CB  LEU A 207      24.875  11.645   9.012  1.00 63.44           C\\nANISOU 1251  CB  LEU A 207     7441   7765   8897    855   -953     35       C\\nATOM   1252  CG  LEU A 207      25.757  11.605   7.765  1.00 58.28           C\\nANISOU 1252  CG  LEU A 207     6481   7306   8356    900   -859    -62       C\\nATOM   1253  CD1 LEU A 207      25.869  12.987   7.135  1.00 58.28           C\\nANISOU 1253  CD1 LEU A 207     6266   7458   8418    685   -713     -2       C\\nATOM   1254  CD2 LEU A 207      27.133  11.057   8.115  1.00 60.06           C\\nANISOU 1254  CD2 LEU A 207     6537   7593   8688   1106  -1049   -219       C\\nATOM   1255  N   VAL A 208      22.536  10.604  11.000  1.00 65.76           N\\nANISOU 1255  N   VAL A 208     8427   7760   8800    740  -1039    244       N\\nATOM   1256  CA  VAL A 208      21.850  10.728  12.283  1.00 70.01           C\\nANISOU 1256  CA  VAL A 208     9179   8279   9143    643  -1090    309       C\\nATOM   1257  C   VAL A 208      21.897   9.408  13.042  1.00 72.90           C\\nANISOU 1257  C   VAL A 208     9821   8505   9370    686  -1284    405       C\\nATOM   1258  O   VAL A 208      22.211   9.371  14.237  1.00 72.29           O\\nANISOU 1258  O   VAL A 208     9878   8422   9167    690  -1459    437       O\\nATOM   1259  CB  VAL A 208      20.403  11.205  12.072  1.00 62.31           C\\nANISOU 1259  CB  VAL A 208     8243   7366   8066    475   -875    344       C\\nATOM   1260  CG1 VAL A 208      19.616  11.100  13.361  1.00 57.35           C\\nANISOU 1260  CG1 VAL A 208     7821   6784   7185    363   -898    391       C\\nATOM   1261  CG2 VAL A 208      20.388  12.634  11.560  1.00 55.34           C\\nANISOU 1261  CG2 VAL A 208     7134   6567   7324    438   -769    263       C\\nATOM   1262  N   TYR A 209      21.584   8.304  12.360  1.00 67.17           N\\nANISOU 1262  N   TYR A 209     9206   7651   8663    711  -1285    458       N\\nATOM   1263  CA  TYR A 209      21.578   7.010  13.032  1.00 62.85           C\\nANISOU 1263  CA  TYR A 209     8966   6907   8008    728  -1515    581       C\\nATOM   1264  C   TYR A 209      22.975   6.598  13.468  1.00 67.38           C\\nANISOU 1264  C   TYR A 209     9528   7379   8695    962  -1822    518       C\\nATOM   1265  O   TYR A 209      23.130   5.942  14.504  1.00 76.08           O\\nANISOU 1265  O   TYR A 209    10894   8346   9666    963  -2077    640       O\\nATOM   1266  CB  TYR A 209      20.960   5.946  12.126  1.00 60.49           C\\nANISOU 1266  CB  TYR A 209     8784   6452   7749    710  -1483    623       C\\nATOM   1267  CG  TYR A 209      19.452   5.927  12.179  1.00 66.56           C\\nANISOU 1267  CG  TYR A 209     9685   7270   8334    437  -1286    750       C\\nATOM   1268  CD1 TYR A 209      18.788   5.544  13.335  1.00 66.30           C\\nANISOU 1268  CD1 TYR A 209     9921   7223   8047    229  -1351    931       C\\nATOM   1269  CD2 TYR A 209      18.693   6.292  11.078  1.00 67.85           C\\nANISOU 1269  CD2 TYR A 209     9692   7530   8559    372  -1040    687       C\\nATOM   1270  CE1 TYR A 209      17.408   5.526  13.397  1.00 71.51           C\\nANISOU 1270  CE1 TYR A 209    10651   7990   8531    -39  -1153   1024       C\\nATOM   1271  CE2 TYR A 209      17.312   6.271  11.129  1.00 67.87           C\\nANISOU 1271  CE2 TYR A 209     9776   7601   8410    135   -874    776       C\\nATOM   1272  CZ  TYR A 209      16.675   5.892  12.292  1.00 73.98           C\\nANISOU 1272  CZ  TYR A 209    10778   8387   8944    -71   -920    933       C\\nATOM   1273  OH  TYR A 209      15.301   5.875  12.350  1.00 78.65           O\\nANISOU 1273  OH  TYR A 209    11400   9107   9378   -325   -736    998       O\\nATOM   1274  N   ILE A 210      24.002   6.972  12.702  1.00 65.59           N\\nANISOU 1274  N   ILE A 210     8989   7235   8698   1151  -1815    332       N\\nATOM   1275  CA  ILE A 210      25.373   6.731  13.144  1.00 66.53           C\\nANISOU 1275  CA  ILE A 210     9020   7316   8943   1384  -2102    228       C\\nATOM   1276  C   ILE A 210      25.669   7.536  14.402  1.00 68.90           C\\nANISOU 1276  C   ILE A 210     9347   7706   9128   1318  -2205    265       C\\nATOM   1277  O   ILE A 210      26.296   7.036  15.343  1.00 66.82           O\\nANISOU 1277  O   ILE A 210     9234   7337   8820   1429  -2518    299       O\\nATOM   1278  CB  ILE A 210      26.368   7.053  12.015  1.00 68.77           C\\nANISOU 1278  CB  ILE A 210     8898   7760   9473   1556  -2020      2       C\\nATOM   1279  CG1 ILE A 210      26.237   6.043  10.879  1.00 66.91           C\\nANISOU 1279  CG1 ILE A 210     8656   7435   9331   1685  -1991    -87       C\\nATOM   1280  CG2 ILE A 210      27.792   7.062  12.545  1.00 69.56           C\\nANISOU 1280  CG2 ILE A 210     8822   7898   9711   1774  -2291   -139       C\\nATOM   1281  CD1 ILE A 210      27.237   6.254   9.771  1.00 66.26           C\\nANISOU 1281  CD1 ILE A 210     8158   7579   9440   1852  -1900   -335       C\\nATOM   1282  N   LYS A 211      25.221   8.797  14.439  1.00 68.09           N\\nANISOU 1282  N   LYS A 211     9108   7786   8977   1147  -1974    247       N\\nATOM   1283  CA  LYS A 211      25.368   9.607  15.645  1.00 72.77           C\\nANISOU 1283  CA  LYS A 211     9739   8468   9442   1077  -2066    245       C\\nATOM   1284  C   LYS A 211      24.551   9.044  16.798  1.00 75.75           C\\nANISOU 1284  C   LYS A 211    10492   8790   9501    949  -2158    418       C\\nATOM   1285  O   LYS A 211      24.918   9.225  17.965  1.00 75.16           O\\nANISOU 1285  O   LYS A 211    10526   8758   9275    949  -2353    430       O\\nATOM   1286  CB  LYS A 211      24.956  11.053  15.367  1.00 72.52           C\\nANISOU 1286  CB  LYS A 211     9503   8598   9455    934  -1825    165       C\\nATOM   1287  CG  LYS A 211      26.059  11.921  14.784  1.00 76.74           C\\nANISOU 1287  CG  LYS A 211     9682   9223  10251    997  -1830     21       C\\nATOM   1288  CD  LYS A 211      27.081  12.304  15.845  1.00 80.50           C\\nANISOU 1288  CD  LYS A 211    10106   9734  10746   1072  -2092    -66       C\\nATOM   1289  N   ILE A 212      23.444   8.363  16.492  1.00 76.82           N\\nANISOU 1289  N   ILE A 212    10821   8858   9510    813  -2022    555       N\\nATOM   1290  CA  ILE A 212      22.634   7.738  17.534  1.00 75.49           C\\nANISOU 1290  CA  ILE A 212    11004   8670   9009    629  -2092    753       C\\nATOM   1291  C   ILE A 212      23.351   6.523  18.110  1.00 78.85           C\\nANISOU 1291  C   ILE A 212    11697   8862   9401    741  -2475    889       C\\nATOM   1292  O   ILE A 212      23.426   6.348  19.332  1.00 81.23           O\\nANISOU 1292  O   ILE A 212    12234   9186   9445    664  -2673   1015       O\\nATOM   1293  CB  ILE A 212      21.244   7.368  16.983  1.00 72.94           C\\nANISOU 1293  CB  ILE A 212    10775   8353   8584    420  -1838    858       C\\nATOM   1294  CG1 ILE A 212      20.367   8.618  16.858  1.00 72.24           C\\nANISOU 1294  CG1 ILE A 212    10488   8519   8442    291  -1522    738       C\\nATOM   1295  CG2 ILE A 212      20.575   6.319  17.861  1.00 71.22           C\\nANISOU 1295  CG2 ILE A 212    10941   8062   8058    211  -1961   1112       C\\nATOM   1296  CD1 ILE A 212      18.962   8.339  16.351  1.00 65.08           C\\nANISOU 1296  CD1 ILE A 212     9627   7664   7437     90  -1276    811       C\\nATOM   1297  N   TYR A 213      23.890   5.666  17.237  1.00 80.40           N\\nANISOU 1297  N   TYR A 213    11866   8833   9849    936  -2607    855       N\\nATOM   1298  CA  TYR A 213      24.609   4.484  17.706  1.00 74.91           C\\nANISOU 1298  CA  TYR A 213    11423   7857   9182   1095  -3032    956       C\\nATOM   1299  C   TYR A 213      25.796   4.871  18.580  1.00 76.60           C\\nANISOU 1299  C   TYR A 213    11566   8127   9414   1272  -3314    873       C\\nATOM   1300  O   TYR A 213      26.091   4.197  19.574  1.00 75.58           O\\nANISOU 1300  O   TYR A 213    11741   7846   9129   1288  -3670   1037       O\\nATOM   1301  CB  TYR A 213      25.070   3.642  16.515  1.00 69.47           C\\nANISOU 1301  CB  TYR A 213    10637   6949   8811   1339  -3122    828       C\\nATOM   1302  CG  TYR A 213      25.850   2.401  16.899  1.00 82.87           C\\nANISOU 1302  CG  TYR A 213    12578   8305  10605   1567  -3612    881       C\\nATOM   1303  CD1 TYR A 213      25.198   1.248  17.317  1.00 88.00           C\\nANISOU 1303  CD1 TYR A 213    13681   8643  11110   1422  -3838   1153       C\\nATOM   1304  CD2 TYR A 213      27.237   2.376  16.828  1.00 83.04           C\\nANISOU 1304  CD2 TYR A 213    12370   8305  10877   1924  -3876    656       C\\nATOM   1305  CE1 TYR A 213      25.906   0.107  17.664  1.00 88.45           C\\nANISOU 1305  CE1 TYR A 213    13945   8382  11281   1597  -4262   1171       C\\nATOM   1306  CE2 TYR A 213      27.955   1.241  17.174  1.00 84.14           C\\nANISOU 1306  CE2 TYR A 213    12701   8139  11130   2144  -4318    655       C\\nATOM   1307  CZ  TYR A 213      27.286   0.109  17.589  1.00 88.74           C\\nANISOU 1307  CZ  TYR A 213    13713   8432  11572   1950  -4461    892       C\\nATOM   1308  OH  TYR A 213      27.998  -1.023  17.933  1.00 93.97           O\\nANISOU 1308  OH  TYR A 213    14524   8828  12351   2091  -4813    843       O\\nATOM   1309  N   ILE A 214      26.491   5.955  18.226  1.00 79.22           N\\nANISOU 1309  N   ILE A 214    11503   8668   9929   1388  -3184    634       N\\nATOM   1310  CA  ILE A 214      27.667   6.368  18.988  1.00 79.71           C\\nANISOU 1310  CA  ILE A 214    11448   8796  10043   1553  -3456    525       C\\nATOM   1311  C   ILE A 214      27.278   6.769  20.407  1.00 82.99           C\\nANISOU 1311  C   ILE A 214    12112   9325  10094   1359  -3536    663       C\\nATOM   1312  O   ILE A 214      27.993   6.468  21.373  1.00 77.18           O\\nANISOU 1312  O   ILE A 214    11526   8534   9267   1459  -3903    709       O\\nATOM   1313  CB  ILE A 214      28.405   7.505  18.256  1.00 74.49           C\\nANISOU 1313  CB  ILE A 214    10301   8350   9651   1642  -3272    259       C\\nATOM   1314  CG1 ILE A 214      28.993   6.995  16.944  1.00 73.37           C\\nANISOU 1314  CG1 ILE A 214     9897   8156   9825   1855  -3239    102       C\\nATOM   1315  CG2 ILE A 214      29.508   8.085  19.125  1.00 79.54           C\\nANISOU 1315  CG2 ILE A 214    10802   9091  10328   1753  -3532    141       C\\nATOM   1316  CD1 ILE A 214      29.840   8.022  16.221  1.00 79.87           C\\nANISOU 1316  CD1 ILE A 214    10233   9224  10891   1906  -3079   -130       C\\nATOM   1317  N   VAL A 215      26.138   7.447  20.558  1.00 80.48           N\\nANISOU 1317  N   VAL A 215    11834   9193   9553   1092  -3207    710       N\\nATOM   1318  CA  VAL A 215      25.693   7.866  21.883  1.00 80.01           C\\nANISOU 1318  CA  VAL A 215    11978   9313   9108    905  -3241    790       C\\nATOM   1319  C   VAL A 215      25.303   6.658  22.722  1.00 86.31           C\\nANISOU 1319  C   VAL A 215    13235   9978   9582    774  -3480   1098       C\\nATOM   1320  O   VAL A 215      25.668   6.557  23.900  1.00 89.76           O\\nANISOU 1320  O   VAL A 215    13882  10466   9758    750  -3755   1189       O\\nATOM   1321  CB  VAL A 215      24.532   8.868  21.764  1.00 69.82           C\\nANISOU 1321  CB  VAL A 215    10575   8272   7681    685  -2829    710       C\\nATOM   1322  CG1 VAL A 215      23.873   9.073  23.115  1.00 70.46           C\\nANISOU 1322  CG1 VAL A 215    10891   8582   7299    474  -2833    787       C\\nATOM   1323  CG2 VAL A 215      25.035  10.188  21.201  1.00 70.96           C\\nANISOU 1323  CG2 VAL A 215    10323   8520   8117    791  -2692    435       C\\nATOM   1324  N   LEU A 216      24.556   5.722  22.131  1.00 88.27           N\\nANISOU 1324  N   LEU A 216    13660  10047   9830    664  -3400   1278       N\\nATOM   1325  CA  LEU A 216      24.129   4.539  22.870  1.00 81.42           C\\nANISOU 1325  CA  LEU A 216    13257   9014   8666    480  -3641   1616       C\\nATOM   1326  C   LEU A 216      25.314   3.682  23.294  1.00 84.21           C\\nANISOU 1326  C   LEU A 216    13802   9063   9129    728  -4180   1700       C\\nATOM   1327  O   LEU A 216      25.268   3.046  24.353  1.00 81.69           O\\nANISOU 1327  O   LEU A 216    13836   8687   8514    577  -4427   1947       O\\nATOM   1328  CB  LEU A 216      23.148   3.725  22.025  1.00 83.40           C\\nANISOU 1328  CB  LEU A 216    13629   9094   8967    318  -3470   1765       C\\nATOM   1329  CG  LEU A 216      21.846   4.440  21.657  1.00 89.34           C\\nANISOU 1329  CG  LEU A 216    14218  10142   9584     56  -2973   1707       C\\nATOM   1330  CD1 LEU A 216      21.017   3.625  20.676  1.00 88.79           C\\nANISOU 1330  CD1 LEU A 216    14221   9881   9633    -62  -2839   1814       C\\nATOM   1331  CD2 LEU A 216      21.046   4.736  22.911  1.00 97.88           C\\nANISOU 1331  CD2 LEU A 216    15482  11550  10159   -274  -2870   1850       C\\nATOM   1332  N   ARG A 217      26.382   3.651  22.492  1.00 81.94           N\\nANISOU 1332  N   ARG A 217    13237   8618   9279   1094  -4322   1464       N\\nATOM   1333  CA  ARG A 217      27.561   2.877  22.871  1.00 83.41           C\\nANISOU 1333  CA  ARG A 217    13486   8566   9641   1348  -4750   1435       C\\nATOM   1334  C   ARG A 217      28.345   3.556  23.985  1.00 85.61           C\\nANISOU 1334  C   ARG A 217    13711   9042   9775   1403  -4934   1364       C\\nATOM   1335  O   ARG A 217      28.952   2.873  24.816  1.00 80.30           O\\nANISOU 1335  O   ARG A 217    13221   8234   9057   1442  -5229   1443       O\\nATOM   1336  CB  ARG A 217      28.460   2.641  21.658  1.00 74.00           C\\nANISOU 1336  CB  ARG A 217    11946   7228   8942   1710  -4789   1141       C\\nATOM   1337  N   ARG A 218      28.347   4.891  24.021  1.00 77.47           N\\nANISOU 1337  N   ARG A 218    12427   8320   8687   1399  -4771   1198       N\\nATOM   1338  CA  ARG A 218      28.948   5.589  25.152  1.00 79.95           C\\nANISOU 1338  CA  ARG A 218    12725   8839   8812   1411  -4955   1127       C\\nATOM   1339  C   ARG A 218      28.170   5.328  26.435  1.00 82.04           C\\nANISOU 1339  C   ARG A 218    13403   9226   8543   1087  -4970   1402       C\\nATOM   1340  O   ARG A 218      28.765   5.243  27.517  1.00 84.60           O\\nANISOU 1340  O   ARG A 218    13838   9600   8707   1097  -5207   1432       O\\nATOM   1341  CB  ARG A 218      29.022   7.089  24.868  1.00 75.14           C\\nANISOU 1341  CB  ARG A 218    11692   8536   8320   1397  -4623    823       C\\nATOM   1342  N   ARG A 219      26.847   5.179  26.326  1.00 85.99           N\\nANISOU 1342  N   ARG A 219    14111   9803   8758    785  -4704   1599       N\\nATOM   1343  CA  ARG A 219      26.016   4.885  27.490  1.00 84.46           C\\nANISOU 1343  CA  ARG A 219    14260   9795   8035    425  -4645   1858       C\\nATOM   1344  C   ARG A 219      26.340   3.511  28.066  1.00 86.08           C\\nANISOU 1344  C   ARG A 219    14765   9710   8230    380  -4920   2118       C\\nATOM   1345  O   ARG A 219      26.501   3.361  29.283  1.00 90.06           O\\nANISOU 1345  O   ARG A 219    15467  10337   8414    256  -5076   2247       O\\nATOM   1346  CB  ARG A 219      24.539   4.978  27.102  1.00 85.75           C\\nANISOU 1346  CB  ARG A 219    14494  10127   7961    100  -4243   1970       C\\nATOM   1347  CG  ARG A 219      23.566   4.985  28.270  1.00 97.90           C\\nANISOU 1347  CG  ARG A 219    16277  12019   8900   -302  -4086   2160       C\\nATOM   1348  CD  ARG A 219      22.137   5.191  27.780  1.00103.51           C\\nANISOU 1348  CD  ARG A 219    16923  12951   9455   -597  -3619   2177       C\\nATOM   1349  NE  ARG A 219      22.015   6.380  26.940  1.00103.98           N\\nANISOU 1349  NE  ARG A 219    16513  13152   9842   -422  -3259   1780       N\\nATOM   1350  CZ  ARG A 219      21.746   7.599  27.400  1.00102.81           C\\nANISOU 1350  CZ  ARG A 219    16138  13388   9536   -439  -3032   1497       C\\nATOM   1351  NH1 ARG A 219      21.567   7.793  28.700  1.00112.25           N\\nANISOU 1351  NH1 ARG A 219    17509  14920  10223   -616  -3093   1534       N\\nATOM   1352  NH2 ARG A 219      21.656   8.624  26.563  1.00 90.07           N\\nANISOU 1352  NH2 ARG A 219    14137  11821   8266   -282  -2765   1173       N\\nATOM   1353  N   ARG A 220      26.443   2.493  27.205  1.00 85.93           N\\nANISOU 1353  N   ARG A 220    14788   9305   8558    483  -5002   2177       N\\nATOM   1354  CA  ARG A 220      26.753   1.145  27.680  1.00 92.53           C\\nANISOU 1354  CA  ARG A 220    15922   9808   9426    451  -5313   2391       C\\nATOM   1355  C   ARG A 220      28.118   1.092  28.355  1.00 98.18           C\\nANISOU 1355  C   ARG A 220    16600  10438  10265    730  -5700   2278       C\\nATOM   1356  O   ARG A 220      28.296   0.384  29.353  1.00 99.06           O\\nANISOU 1356  O   ARG A 220    17008  10452  10178    616  -5960   2492       O\\nATOM   1357  CB  ARG A 220      26.686   0.149  26.522  1.00 94.83           C\\nANISOU 1357  CB  ARG A 220    16221   9701  10109    561  -5350   2378       C\\nATOM   1358  CG  ARG A 220      25.281  -0.055  25.969  1.00100.75           C\\nANISOU 1358  CG  ARG A 220    17071  10487  10720    234  -5015   2543       C\\nATOM   1359  CD  ARG A 220      25.299  -0.715  24.596  1.00102.73           C\\nANISOU 1359  CD  ARG A 220    17220  10409  11403    417  -5011   2417       C\\nATOM   1360  NE  ARG A 220      23.971  -0.712  23.986  1.00105.76           N\\nANISOU 1360  NE  ARG A 220    17640  10872  11673    124  -4663   2533       N\\nATOM   1361  CZ  ARG A 220      23.743  -0.876  22.687  1.00111.13           C\\nANISOU 1361  CZ  ARG A 220    18166  11401  12658    249  -4533   2393       C\\nATOM   1362  NH1 ARG A 220      24.756  -1.052  21.850  1.00115.91           N\\nANISOU 1362  NH1 ARG A 220    18552  11801  13687    664  -4699   2115       N\\nATOM   1363  NH2 ARG A 220      22.500  -0.857  22.220  1.00109.07           N\\nANISOU 1363  NH2 ARG A 220    17943  11230  12267    -44  -4223   2509       N\\nATOM   1364  N   LYS A 221      29.096   1.832  27.826  1.00 87.90           N\\nANISOU 1364  N   LYS A 221    14922   9183   9293   1081  -5746   1943       N\\nATOM   1365  CA  LYS A 221      30.396   1.903  28.485  1.00 91.01           C\\nANISOU 1365  CA  LYS A 221    15227   9552   9800   1332  -6088   1803       C\\nATOM   1366  C   LYS A 221      30.311   2.643  29.815  1.00 92.81           C\\nANISOU 1366  C   LYS A 221    15563  10123   9576   1152  -6111   1881       C\\nATOM   1367  O   LYS A 221      31.080   2.348  30.738  1.00 97.14           O\\nANISOU 1367  O   LYS A 221    16229  10626  10054   1227  -6434   1922       O\\nATOM   1368  CB  LYS A 221      31.420   2.575  27.569  1.00 88.24           C\\nANISOU 1368  CB  LYS A 221    14391   9229   9907   1702  -6082   1409       C\\nATOM   1369  N   ARG A 222      29.386   3.599  29.935  1.00 89.90           N\\nANISOU 1369  N   ARG A 222    15156  10111   8890    923  -5782   1877       N\\nATOM   1370  CA  ARG A 222      29.220   4.328  31.190  1.00 91.86           C\\nANISOU 1370  CA  ARG A 222    15494  10740   8669    746  -5774   1897       C\\nATOM   1371  C   ARG A 222      28.375   3.544  32.190  1.00 96.10           C\\nANISOU 1371  C   ARG A 222    16450  11352   8712    379  -5763   2271       C\\nATOM   1372  O   ARG A 222      28.677   3.536  33.390  1.00100.34           O\\nANISOU 1372  O   ARG A 222    17145  12050   8928    306  -5948   2359       O\\nATOM   1373  CB  ARG A 222      28.596   5.698  30.923  1.00 87.62           C\\nANISOU 1373  CB  ARG A 222    14726  10572   7995    668  -5443   1670       C\\nATOM   1374  N   ASN A1002      27.322   2.874  31.712  1.00 85.72           N\\nANISOU 1374  N   ASN A1002    12716   9421  10431    154  -1889   1403       N\\nATOM   1375  CA  ASN A1002      26.456   2.104  32.601  1.00 78.54           C\\nANISOU 1375  CA  ASN A1002    11488   8720   9636    336  -1772   1042       C\\nATOM   1376  C   ASN A1002      27.206   0.951  33.259  1.00 74.17           C\\nANISOU 1376  C   ASN A1002    10829   8409   8943    253  -1283    980       C\\nATOM   1377  O   ASN A1002      26.974   0.646  34.435  1.00 77.99           O\\nANISOU 1377  O   ASN A1002    11066   9013   9552    361  -1151    748       O\\nATOM   1378  CB  ASN A1002      25.242   1.584  31.828  1.00 72.27           C\\nANISOU 1378  CB  ASN A1002    10694   8018   8747    370  -1959    956       C\\nATOM   1379  CG  ASN A1002      24.296   2.693  31.414  1.00 85.39           C\\nANISOU 1379  CG  ASN A1002    12363   9440  10641    548  -2522    954       C\\nATOM   1380  OD1 ASN A1002      24.569   3.871  31.643  1.00 91.93           O\\nANISOU 1380  OD1 ASN A1002    13249   9977  11701    641  -2774   1033       O\\nATOM   1381  ND2 ASN A1002      23.179   2.324  30.796  1.00 95.12           N\\nANISOU 1381  ND2 ASN A1002    13533  10764  11844    599  -2763    857       N\\nATOM   1382  N   ILE A1003      28.104   0.295  32.520  1.00 69.88           N\\nANISOU 1382  N   ILE A1003    10476   7942   8134     67  -1017   1180       N\\nATOM   1383  CA  ILE A1003      28.844  -0.824  33.094  1.00 75.25           C\\nANISOU 1383  CA  ILE A1003    11058   8796   8739     40   -607   1126       C\\nATOM   1384  C   ILE A1003      29.846  -0.336  34.137  1.00 79.70           C\\nANISOU 1384  C   ILE A1003    11473   9334   9474     69   -527   1154       C\\nATOM   1385  O   ILE A1003      30.117  -1.035  35.121  1.00 81.90           O\\nANISOU 1385  O   ILE A1003    11597   9734   9788    131   -334   1048       O\\nATOM   1386  CB  ILE A1003      29.526  -1.644  31.981  1.00 76.66           C\\nANISOU 1386  CB  ILE A1003    11445   9056   8624   -116   -342   1259       C\\nATOM   1387  CG1 ILE A1003      30.131  -2.927  32.553  1.00 83.23           C\\nANISOU 1387  CG1 ILE A1003    12171  10007   9446    -76     25   1164       C\\nATOM   1388  CG2 ILE A1003      30.599  -0.830  31.276  1.00 75.86           C\\nANISOU 1388  CG2 ILE A1003    11492   8897   8434   -279   -312   1524       C\\nATOM   1389  CD1 ILE A1003      30.765  -3.812  31.509  1.00 89.05           C\\nANISOU 1389  CD1 ILE A1003    13083  10813   9939   -170    311   1194       C\\nATOM   1390  N   PHE A1004      30.403   0.862  33.954  1.00 72.73           N\\nANISOU 1390  N   PHE A1004    10657   8281   8697      0   -708   1309       N\\nATOM   1391  CA  PHE A1004      31.300   1.419  34.961  1.00 72.86           C\\nANISOU 1391  CA  PHE A1004    10523   8260   8901      1   -698   1302       C\\nATOM   1392  C   PHE A1004      30.561   1.658  36.271  1.00 75.78           C\\nANISOU 1392  C   PHE A1004    10709   8641   9442    194   -837   1009       C\\nATOM   1393  O   PHE A1004      31.045   1.293  37.349  1.00 75.51           O\\nANISOU 1393  O   PHE A1004    10525   8740   9424    231   -703    911       O\\nATOM   1394  CB  PHE A1004      31.920   2.718  34.446  1.00 74.85           C\\nANISOU 1394  CB  PHE A1004    10908   8273   9256   -164   -904   1525       C\\nATOM   1395  CG  PHE A1004      32.831   3.387  35.431  1.00 80.49           C\\nANISOU 1395  CG  PHE A1004    11471   8921  10192   -205   -951   1497       C\\nATOM   1396  CD1 PHE A1004      34.093   2.876  35.685  1.00 79.31           C\\nANISOU 1396  CD1 PHE A1004    11166   8951  10018   -317   -675   1584       C\\nATOM   1397  CD2 PHE A1004      32.429   4.533  36.100  1.00 83.97           C\\nANISOU 1397  CD2 PHE A1004    11907   9110  10888   -118  -1297   1351       C\\nATOM   1398  CE1 PHE A1004      34.938   3.492  36.589  1.00 82.95           C\\nANISOU 1398  CE1 PHE A1004    11465   9368  10684   -377   -769   1550       C\\nATOM   1399  CE2 PHE A1004      33.269   5.154  37.007  1.00 85.07           C\\nANISOU 1399  CE2 PHE A1004    11928   9181  11215   -183  -1370   1289       C\\nATOM   1400  CZ  PHE A1004      34.525   4.633  37.251  1.00 84.25           C\\nANISOU 1400  CZ  PHE A1004    11666   9282  11062   -331  -1119   1402       C\\nATOM   1401  N   GLU A1005      29.376   2.270  36.194  1.00 75.34           N\\nANISOU 1401  N   GLU A1005    10654   8467   9503    325  -1114    852       N\\nATOM   1402  CA  GLU A1005      28.576   2.488  37.395  1.00 80.23           C\\nANISOU 1402  CA  GLU A1005    11062   9155  10266    516  -1188    504       C\\nATOM   1403  C   GLU A1005      28.115   1.169  38.000  1.00 86.02           C\\nANISOU 1403  C   GLU A1005    11656  10202  10825    527   -889    366       C\\nATOM   1404  O   GLU A1005      28.046   1.030  39.227  1.00 90.45           O\\nANISOU 1404  O   GLU A1005    12070  10923  11372    580   -788    167       O\\nATOM   1405  CB  GLU A1005      27.375   3.375  37.076  1.00 77.92           C\\nANISOU 1405  CB  GLU A1005    10741   8676  10189    694  -1544    334       C\\nATOM   1406  CG  GLU A1005      27.742   4.831  36.890  1.00 84.80           C\\nANISOU 1406  CG  GLU A1005    11751   9159  11311    720  -1903    409       C\\nATOM   1407  CD  GLU A1005      28.491   5.393  38.081  1.00 89.89           C\\nANISOU 1407  CD  GLU A1005    12315   9761  12076    724  -1883    248       C\\nATOM   1408  OE1 GLU A1005      27.991   5.262  39.219  1.00 89.61           O\\nANISOU 1408  OE1 GLU A1005    12069   9916  12064    880  -1796   -120       O\\nATOM   1409  OE2 GLU A1005      29.591   5.949  37.880  1.00 88.50           O\\nANISOU 1409  OE2 GLU A1005    12285   9394  11947    539  -1944    483       O\\nATOM   1410  N   MET A1006      27.798   0.187  37.153  1.00 78.13           N\\nANISOU 1410  N   MET A1006    10736   9284   9667    448   -755    474       N\\nATOM   1411  CA  MET A1006      27.337  -1.104  37.657  1.00 72.09           C\\nANISOU 1411  CA  MET A1006     9881   8748   8762    410   -494    376       C\\nATOM   1412  C   MET A1006      28.381  -1.755  38.553  1.00 75.65           C\\nANISOU 1412  C   MET A1006    10336   9295   9114    362   -262    468       C\\nATOM   1413  O   MET A1006      28.038  -2.402  39.549  1.00 76.42           O\\nANISOU 1413  O   MET A1006    10345   9565   9126    348   -119    363       O\\nATOM   1414  CB  MET A1006      26.994  -2.033  36.497  1.00 63.48           C\\nANISOU 1414  CB  MET A1006     8926   7661   7531    307   -419    476       C\\nATOM   1415  CG  MET A1006      26.279  -3.292  36.913  1.00 70.23           C\\nANISOU 1415  CG  MET A1006     9703   8684   8298    231   -215    360       C\\nATOM   1416  SD  MET A1006      26.609  -4.663  35.798  1.00 70.93           S\\nANISOU 1416  SD  MET A1006    10037   8714   8198     86    -29    502       S\\nATOM   1417  CE  MET A1006      25.235  -5.747  36.183  1.00 79.60           C\\nANISOU 1417  CE  MET A1006    11010   9948   9288    -46     55    311       C\\nATOM   1418  N   LEU A1007      29.660  -1.591  38.223  1.00 74.32           N\\nANISOU 1418  N   LEU A1007    10257   9030   8951    321   -234    678       N\\nATOM   1419  CA  LEU A1007      30.716  -2.231  38.992  1.00 72.19           C\\nANISOU 1419  CA  LEU A1007     9955   8841   8633    310    -74    777       C\\nATOM   1420  C   LEU A1007      31.310  -1.346  40.078  1.00 77.91           C\\nANISOU 1420  C   LEU A1007    10574   9585   9442    343   -217    715       C\\nATOM   1421  O   LEU A1007      31.846  -1.881  41.054  1.00 81.18           O\\nANISOU 1421  O   LEU A1007    10944  10120   9781    352   -154    740       O\\nATOM   1422  CB  LEU A1007      31.835  -2.718  38.066  1.00 71.02           C\\nANISOU 1422  CB  LEU A1007     9882   8633   8470    261     76    992       C\\nATOM   1423  CG  LEU A1007      31.556  -4.102  37.475  1.00 67.80           C\\nANISOU 1423  CG  LEU A1007     9585   8237   7941    251    288   1010       C\\nATOM   1424  CD1 LEU A1007      30.727  -4.015  36.198  1.00 65.13           C\\nANISOU 1424  CD1 LEU A1007     9386   7844   7514    183    249    974       C\\nATOM   1425  CD2 LEU A1007      32.848  -4.848  37.236  1.00 68.79           C\\nANISOU 1425  CD2 LEU A1007     9698   8348   8090    287    481   1140       C\\nATOM   1426  N   ARG A1008      31.232  -0.018  39.954  1.00 81.15           N\\nANISOU 1426  N   ARG A1008    10972   9855  10007    355   -447    635       N\\nATOM   1427  CA  ARG A1008      31.610   0.793  41.106  1.00 79.83           C\\nANISOU 1427  CA  ARG A1008    10721   9701   9912    383   -602    485       C\\nATOM   1428  C   ARG A1008      30.583   0.693  42.224  1.00 79.95           C\\nANISOU 1428  C   ARG A1008    10660   9903   9815    473   -581    181       C\\nATOM   1429  O   ARG A1008      30.878   1.089  43.357  1.00 82.62           O\\nANISOU 1429  O   ARG A1008    10953  10337  10104    486   -655     22       O\\nATOM   1430  CB  ARG A1008      31.814   2.257  40.711  1.00 75.25           C\\nANISOU 1430  CB  ARG A1008    10178   8848   9565    361   -878    461       C\\nATOM   1431  CG  ARG A1008      30.548   3.009  40.384  1.00 84.73           C\\nANISOU 1431  CG  ARG A1008    11405   9893  10893    488  -1070    258       C\\nATOM   1432  CD  ARG A1008      30.759   4.502  40.562  1.00 91.79           C\\nANISOU 1432  CD  ARG A1008    12342  10481  12053    509  -1399    147       C\\nATOM   1433  NE  ARG A1008      30.802   4.870  41.973  1.00 97.78           N\\nANISOU 1433  NE  ARG A1008    12996  11338  12815    587  -1451   -187       N\\nATOM   1434  CZ  ARG A1008      29.731   5.209  42.684  1.00100.58           C\\nANISOU 1434  CZ  ARG A1008    13254  11756  13206    785  -1504   -595       C\\nATOM   1435  NH1 ARG A1008      28.534   5.231  42.111  1.00 94.43           N\\nANISOU 1435  NH1 ARG A1008    12420  10935  12522    941  -1541   -707       N\\nATOM   1436  NH2 ARG A1008      29.857   5.526  43.966  1.00105.64           N\\nANISOU 1436  NH2 ARG A1008    13834  12529  13777    825  -1520   -917       N\\nATOM   1437  N   ILE A1009      29.394   0.171  41.926  1.00 74.25           N\\nANISOU 1437  N   ILE A1009     9910   9267   9034    507   -473     81       N\\nATOM   1438  CA  ILE A1009      28.416  -0.151  42.956  1.00 75.30           C\\nANISOU 1438  CA  ILE A1009     9929   9661   9019    531   -350   -186       C\\nATOM   1439  C   ILE A1009      28.680  -1.535  43.536  1.00 78.79           C\\nANISOU 1439  C   ILE A1009    10438  10305   9194    403   -107     -8       C\\nATOM   1440  O   ILE A1009      28.534  -1.752  44.743  1.00 85.17           O\\nANISOU 1440  O   ILE A1009    11227  11348   9787    355    -20   -120       O\\nATOM   1441  CB  ILE A1009      26.996  -0.039  42.373  1.00 72.07           C\\nANISOU 1441  CB  ILE A1009     9394   9267   8722    603   -364   -387       C\\nATOM   1442  CG1 ILE A1009      26.670   1.415  42.030  1.00 73.75           C\\nANISOU 1442  CG1 ILE A1009     9547   9243   9230    783   -675   -591       C\\nATOM   1443  CG2 ILE A1009      25.968  -0.620  43.332  1.00 70.49           C\\nANISOU 1443  CG2 ILE A1009     9027   9408   8349    556   -136   -634       C\\nATOM   1444  CD1 ILE A1009      25.423   1.572  41.190  1.00 76.17           C\\nANISOU 1444  CD1 ILE A1009     9730   9499   9713    890   -796   -718       C\\nATOM   1445  N   ASP A1010      29.079  -2.490  42.694  1.00 72.06           N\\nANISOU 1445  N   ASP A1010     9694   9350   8336    343     -7    269       N\\nATOM   1446  CA  ASP A1010      29.286  -3.870  43.127  1.00 72.56           C\\nANISOU 1446  CA  ASP A1010     9858   9501   8210    243    179    457       C\\nATOM   1447  C   ASP A1010      30.708  -4.106  43.629  1.00 75.95           C\\nANISOU 1447  C   ASP A1010    10352   9894   8612    272    117    675       C\\nATOM   1448  O   ASP A1010      30.908  -4.550  44.763  1.00 79.91           O\\nANISOU 1448  O   ASP A1010    10905  10541   8916    226    124    730       O\\nATOM   1449  CB  ASP A1010      28.966  -4.834  41.979  1.00 68.87           C\\nANISOU 1449  CB  ASP A1010     9481   8902   7784    190    300    582       C\\nATOM   1450  CG  ASP A1010      27.482  -4.951  41.709  1.00 73.05           C\\nANISOU 1450  CG  ASP A1010     9921   9528   8308    113    358    385       C\\nATOM   1451  OD1 ASP A1010      26.693  -4.307  42.432  1.00 67.48           O\\nANISOU 1451  OD1 ASP A1010     9046   9009   7582    124    341    140       O\\nATOM   1452  OD2 ASP A1010      27.105  -5.691  40.773  1.00 78.54           O\\nANISOU 1452  OD2 ASP A1010    10691  10123   9026     43    418    440       O\\nATOM   1453  N   GLU A1011      31.702  -3.824  42.788  1.00 76.16           N\\nANISOU 1453  N   GLU A1011    10363   9749   8825    334     50    808       N\\nATOM   1454  CA  GLU A1011      33.088  -4.089  43.149  1.00 80.16           C\\nANISOU 1454  CA  GLU A1011    10842  10236   9377    379    -14    997       C\\nATOM   1455  C   GLU A1011      33.663  -2.965  44.003  1.00 86.62           C\\nANISOU 1455  C   GLU A1011    11560  11131  10222    377   -238    897       C\\nATOM   1456  O   GLU A1011      34.212  -3.213  45.081  1.00 98.58           O\\nANISOU 1456  O   GLU A1011    13076  12768  11614    380   -345    952       O\\nATOM   1457  CB  GLU A1011      33.926  -4.284  41.885  1.00 82.54           C\\nANISOU 1457  CB  GLU A1011    11111  10383   9867    418     68   1140       C\\nATOM   1458  CG  GLU A1011      35.344  -4.765  42.134  1.00 89.74           C\\nANISOU 1458  CG  GLU A1011    11913  11291  10894    502     40   1313       C\\nATOM   1459  CD  GLU A1011      35.393  -6.223  42.539  1.00 95.34           C\\nANISOU 1459  CD  GLU A1011    12731  11959  11534    586    111   1445       C\\nATOM   1460  OE1 GLU A1011      35.895  -6.518  43.646  1.00 99.56           O\\nANISOU 1460  OE1 GLU A1011    13255  12559  12013    632    -51   1549       O\\nATOM   1461  OE2 GLU A1011      34.920  -7.072  41.751  1.00 94.59           O\\nANISOU 1461  OE2 GLU A1011    12763  11742  11436    596    295   1450       O\\nATOM   1462  N   GLY A1012      33.549  -1.725  43.534  1.00 83.15           N\\nANISOU 1462  N   GLY A1012    11062  10592   9938    362   -351    758       N\\nATOM   1463  CA  GLY A1012      34.064  -0.590  44.272  1.00 80.42           C\\nANISOU 1463  CA  GLY A1012    10644  10253   9660    339   -589    621       C\\nATOM   1464  C   GLY A1012      35.145   0.176  43.536  1.00 76.41           C\\nANISOU 1464  C   GLY A1012    10041   9573   9418    270   -701    745       C\\nATOM   1465  O   GLY A1012      36.026  -0.422  42.909  1.00 75.35           O\\nANISOU 1465  O   GLY A1012     9829   9430   9369    254   -588    972       O\\nATOM   1466  N   LEU A1013      35.090   1.505  43.610  1.00 72.47           N\\nANISOU 1466  N   LEU A1013     9539   8928   9066    216   -914    581       N\\nATOM   1467  CA  LEU A1013      36.059   2.381  42.960  1.00 75.06           C\\nANISOU 1467  CA  LEU A1013     9799   9069   9653     69  -1037    711       C\\nATOM   1468  C   LEU A1013      37.076   2.842  43.998  1.00 85.43           C\\nANISOU 1468  C   LEU A1013    10980  10447  11031    -12  -1266    645       C\\nATOM   1469  O   LEU A1013      36.730   3.569  44.935  1.00 92.30           O\\nANISOU 1469  O   LEU A1013    11906  11301  11864      3  -1478    364       O\\nATOM   1470  CB  LEU A1013      35.362   3.575  42.309  1.00 76.93           C\\nANISOU 1470  CB  LEU A1013    10164   9014  10053     35  -1188    614       C\\nATOM   1471  CG  LEU A1013      36.264   4.677  41.743  1.00 81.85           C\\nANISOU 1471  CG  LEU A1013    10778   9382  10939   -188  -1361    759       C\\nATOM   1472  CD1 LEU A1013      37.119   4.145  40.607  1.00 83.65           C\\nANISOU 1472  CD1 LEU A1013    10936   9672  11176   -345  -1119   1104       C\\nATOM   1473  CD2 LEU A1013      35.444   5.879  41.290  1.00 79.42           C\\nANISOU 1473  CD2 LEU A1013    10661   8711  10803   -183  -1600    657       C\\nATOM   1474  N   ARG A1014      38.324   2.416  43.830  1.00 82.30           N\\nANISOU 1474  N   ARG A1014    10388  10143  10740    -92  -1229    865       N\\nATOM   1475  CA  ARG A1014      39.431   2.846  44.673  1.00 87.70           C\\nANISOU 1475  CA  ARG A1014    10885  10900  11537   -200  -1487    834       C\\nATOM   1476  C   ARG A1014      40.374   3.720  43.858  1.00 91.11           C\\nANISOU 1476  C   ARG A1014    11154  11170  12293   -454  -1533    970       C\\nATOM   1477  O   ARG A1014      40.854   3.301  42.800  1.00 93.58           O\\nANISOU 1477  O   ARG A1014    11348  11510  12699   -513  -1278   1201       O\\nATOM   1478  CB  ARG A1014      40.189   1.647  45.242  1.00 89.70           C\\nANISOU 1478  CB  ARG A1014    10969  11409  11702    -83  -1465    977       C\\nATOM   1479  CG  ARG A1014      39.445   0.867  46.311  1.00 95.14           C\\nANISOU 1479  CG  ARG A1014    11845  12266  12037     80  -1493    888       C\\nATOM   1480  CD  ARG A1014      40.338   0.658  47.527  1.00103.70           C\\nANISOU 1480  CD  ARG A1014    12817  13547  13039     82  -1799    903       C\\nATOM   1481  NE  ARG A1014      39.801  -0.327  48.462  1.00107.67           N\\nANISOU 1481  NE  ARG A1014    13522  14230  13160    204  -1802    939       N\\nATOM   1482  CZ  ARG A1014      40.399  -0.677  49.597  1.00111.85           C\\nANISOU 1482  CZ  ARG A1014    14048  14948  13504    219  -2094    997       C\\nATOM   1483  NH1 ARG A1014      41.553  -0.119  49.939  1.00113.46           N\\nANISOU 1483  NH1 ARG A1014    14008  15196  13905    140  -2424    984       N\\nATOM   1484  NH2 ARG A1014      39.844  -1.584  50.391  1.00112.62           N\\nANISOU 1484  NH2 ARG A1014    14392  15192  13208    282  -2078   1085       N\\nATOM   1485  N   LEU A1015      40.648   4.926  44.357  1.00 92.65           N\\nANISOU 1485  N   LEU A1015    11353  11202  12646   -633  -1845    811       N\\nATOM   1486  CA  LEU A1015      41.453   5.897  43.627  1.00 98.42           C\\nANISOU 1486  CA  LEU A1015    11974  11728  13694   -955  -1914    952       C\\nATOM   1487  C   LEU A1015      42.928   5.886  44.013  1.00100.85           C\\nANISOU 1487  C   LEU A1015    11893  12218  14209  -1148  -2036   1034       C\\nATOM   1488  O   LEU A1015      43.750   6.434  43.268  1.00 98.40           O\\nANISOU 1488  O   LEU A1015    11399  11829  14161  -1460  -1984   1214       O\\nATOM   1489  CB  LEU A1015      40.885   7.309  43.827  1.00 99.65           C\\nANISOU 1489  CB  LEU A1015    12381  11497  13985  -1071  -2220    736       C\\nATOM   1490  CG  LEU A1015      39.471   7.567  43.292  1.00 99.54           C\\nANISOU 1490  CG  LEU A1015    12694  11242  13885   -893  -2166    655       C\\nATOM   1491  CD1 LEU A1015      39.000   8.964  43.667  1.00 99.18           C\\nANISOU 1491  CD1 LEU A1015    12859  10780  14044   -939  -2532    377       C\\nATOM   1492  CD2 LEU A1015      39.410   7.369  41.782  1.00 97.70           C\\nANISOU 1492  CD2 LEU A1015    12526  10927  13670   -996  -1904   1008       C\\nATOM   1493  N   LYS A1016      43.285   5.285  45.145  1.00105.59           N\\nANISOU 1493  N   LYS A1016    12353  13074  14693   -995  -2209    921       N\\nATOM   1494  CA  LYS A1016      44.673   5.127  45.549  1.00101.07           C\\nANISOU 1494  CA  LYS A1016    11354  12717  14330  -1119  -2373    997       C\\nATOM   1495  C   LYS A1016      45.057   3.654  45.506  1.00 97.42           C\\nANISOU 1495  C   LYS A1016    10673  12549  13792   -837  -2171   1168       C\\nATOM   1496  O   LYS A1016      44.204   2.765  45.581  1.00 93.98           O\\nANISOU 1496  O   LYS A1016    10480  12152  13076   -558  -2006   1179       O\\nATOM   1497  CB  LYS A1016      44.913   5.693  46.953  1.00 96.36           C\\nANISOU 1497  CB  LYS A1016    10775  12159  13680  -1180  -2856    730       C\\nATOM   1498  N   ILE A1017      46.361   3.401  45.382  1.00 93.92           N\\nANISOU 1498  N   ILE A1017     9745  12296  13643   -915  -2196   1291       N\\nATOM   1499  CA  ILE A1017      46.835   2.030  45.257  1.00 95.27           C\\nANISOU 1499  CA  ILE A1017     9663  12692  13845   -609  -2025   1434       C\\nATOM   1500  C   ILE A1017      46.498   1.247  46.517  1.00 93.58           C\\nANISOU 1500  C   ILE A1017     9634  12578  13344   -317  -2322   1390       C\\nATOM   1501  O   ILE A1017      46.630   1.745  47.643  1.00 98.49           O\\nANISOU 1501  O   ILE A1017    10306  13255  13861   -400  -2751   1258       O\\nATOM   1502  CB  ILE A1017      48.346   2.013  44.968  1.00 99.88           C\\nANISOU 1502  CB  ILE A1017     9604  13484  14862   -733  -2035   1517       C\\nATOM   1503  CG1 ILE A1017      48.641   2.776  43.677  1.00 99.15           C\\nANISOU 1503  CG1 ILE A1017     9368  13325  14980  -1097  -1674   1598       C\\nATOM   1504  CG2 ILE A1017      48.859   0.586  44.863  1.00102.32           C\\nANISOU 1504  CG2 ILE A1017     9624  13983  15272   -342  -1894   1617       C\\nATOM   1505  CD1 ILE A1017      50.072   2.657  43.214  1.00100.19           C\\nANISOU 1505  CD1 ILE A1017     8808  13728  15530  -1237  -1535   1668       C\\nATOM   1506  N   TYR A1018      46.040   0.013  46.328  1.00 96.96           N\\nANISOU 1506  N   TYR A1018    10204  13021  13613     -4  -2100   1503       N\\nATOM   1507  CA  TYR A1018      45.693  -0.867  47.432  1.00100.96           C\\nANISOU 1507  CA  TYR A1018    10937  13603  13821    241  -2341   1544       C\\nATOM   1508  C   TYR A1018      45.961  -2.303  47.006  1.00113.96           C\\nANISOU 1508  C   TYR A1018    12472  15250  15576    569  -2149   1734       C\\nATOM   1509  O   TYR A1018      46.224  -2.587  45.835  1.00121.07           O\\nANISOU 1509  O   TYR A1018    13172  16106  16722    616  -1774   1767       O\\nATOM   1510  CB  TYR A1018      44.232  -0.693  47.850  1.00 93.06           C\\nANISOU 1510  CB  TYR A1018    10474  12514  12372    220  -2278   1421       C\\nATOM   1511  CG  TYR A1018      43.253  -1.208  46.822  1.00 94.64           C\\nANISOU 1511  CG  TYR A1018    10901  12566  12493    308  -1824   1465       C\\nATOM   1512  CD1 TYR A1018      43.069  -0.541  45.617  1.00 98.44           C\\nANISOU 1512  CD1 TYR A1018    11346  12911  13146    160  -1544   1428       C\\nATOM   1513  CD2 TYR A1018      42.513  -2.358  47.053  1.00 92.36           C\\nANISOU 1513  CD2 TYR A1018    10884  12266  11944    505  -1704   1563       C\\nATOM   1514  CE1 TYR A1018      42.179  -1.007  44.669  1.00 97.08           C\\nANISOU 1514  CE1 TYR A1018    11389  12624  12873    230  -1183   1460       C\\nATOM   1515  CE2 TYR A1018      41.614  -2.831  46.111  1.00 95.41           C\\nANISOU 1515  CE2 TYR A1018    11463  12519  12271    556  -1325   1577       C\\nATOM   1516  CZ  TYR A1018      41.450  -2.147  44.923  1.00 96.24           C\\nANISOU 1516  CZ  TYR A1018    11515  12518  12534    430  -1079   1511       C\\nATOM   1517  OH  TYR A1018      40.562  -2.611  43.980  1.00 94.30           O\\nANISOU 1517  OH  TYR A1018    11469  12159  12201    471   -755   1517       O\\nATOM   1518  N   LYS A1019      45.882  -3.212  47.972  1.00112.29           N\\nANISOU 1518  N   LYS A1019    12428  15075  15161    787  -2416   1854       N\\nATOM   1519  CA  LYS A1019      46.124  -4.629  47.736  1.00114.49           C\\nANISOU 1519  CA  LYS A1019    12662  15272  15567   1129  -2330   2040       C\\nATOM   1520  C   LYS A1019      44.796  -5.365  47.616  1.00112.47           C\\nANISOU 1520  C   LYS A1019    12933  14846  14954   1191  -2067   2094       C\\nATOM   1521  O   LYS A1019      43.893  -5.162  48.435  1.00114.99           O\\nANISOU 1521  O   LYS A1019    13645  15200  14846   1061  -2176   2073       O\\nATOM   1522  CB  LYS A1019      46.964  -5.233  48.863  1.00116.93           C\\nANISOU 1522  CB  LYS A1019    12829  15675  15923   1330  -2866   2206       C\\nATOM   1523  N   ASP A1020      44.677  -6.212  46.597  1.00112.39           N\\nANISOU 1523  N   ASP A1020    12914  14672  15118   1369  -1707   2129       N\\nATOM   1524  CA  ASP A1020      43.491  -7.038  46.453  1.00108.38           C\\nANISOU 1524  CA  ASP A1020    12868  13981  14329   1415  -1485   2186       C\\nATOM   1525  C   ASP A1020      43.556  -8.206  47.436  1.00111.34           C\\nANISOU 1525  C   ASP A1020    13459  14255  14590   1619  -1796   2432       C\\nATOM   1526  O   ASP A1020      44.475  -8.316  48.253  1.00111.64           O\\nANISOU 1526  O   ASP A1020    13307  14376  14734   1741  -2219   2559       O\\nATOM   1527  CB  ASP A1020      43.344  -7.520  45.010  1.00103.84           C\\nANISOU 1527  CB  ASP A1020    12244  13254  13957   1507  -1026   2105       C\\nATOM   1528  CG  ASP A1020      44.444  -8.477  44.594  1.00108.01           C\\nANISOU 1528  CG  ASP A1020    12440  13694  14903   1844  -1010   2150       C\\nATOM   1529  OD1 ASP A1020      45.525  -8.453  45.217  1.00113.64           O\\nANISOU 1529  OD1 ASP A1020    12802  14515  15861   1981  -1346   2220       O\\nATOM   1530  OD2 ASP A1020      44.228  -9.253  43.639  1.00105.75           O\\nANISOU 1530  OD2 ASP A1020    12227  13235  14718   1987   -677   2082       O\\nATOM   1531  N   THR A1021      42.571  -9.101  47.357  1.00111.86           N\\nANISOU 1531  N   THR A1021    13936  14124  14441   1634  -1618   2524       N\\nATOM   1532  CA  THR A1021      42.498 -10.201  48.311  1.00111.37           C\\nANISOU 1532  CA  THR A1021    14180  13918  14216   1754  -1913   2816       C\\nATOM   1533  C   THR A1021      43.592 -11.242  48.108  1.00113.87           C\\nANISOU 1533  C   THR A1021    14272  14000  14994   2154  -2104   2966       C\\nATOM   1534  O   THR A1021      43.713 -12.150  48.936  1.00122.97           O\\nANISOU 1534  O   THR A1021    15669  14982  16073   2291  -2453   3261       O\\nATOM   1535  CB  THR A1021      41.130 -10.879  48.236  1.00106.11           C\\nANISOU 1535  CB  THR A1021    14000  13085  13230   1600  -1650   2877       C\\nATOM   1536  OG1 THR A1021      40.997 -11.555  46.980  1.00101.52           O\\nANISOU 1536  OG1 THR A1021    13390  12234  12949   1746  -1308   2783       O\\nATOM   1537  CG2 THR A1021      40.020  -9.844  48.372  1.00105.59           C\\nANISOU 1537  CG2 THR A1021    14074  13265  12778   1259  -1443   2671       C\\nATOM   1538  N   GLU A1022      44.388 -11.136  47.045  1.00109.65           N\\nANISOU 1538  N   GLU A1022    13282  13452  14927   2346  -1889   2772       N\\nATOM   1539  CA  GLU A1022      45.477 -12.070  46.790  1.00109.91           C\\nANISOU 1539  CA  GLU A1022    13002  13289  15472   2780  -2033   2824       C\\nATOM   1540  C   GLU A1022      46.850 -11.447  47.014  1.00110.30           C\\nANISOU 1540  C   GLU A1022    12423  13602  15882   2906  -2315   2766       C\\nATOM   1541  O   GLU A1022      47.866 -12.107  46.769  1.00114.91           O\\nANISOU 1541  O   GLU A1022    12609  14084  16969   3299  -2431   2752       O\\nATOM   1542  CB  GLU A1022      45.376 -12.625  45.367  1.00110.94           C\\nANISOU 1542  CB  GLU A1022    13056  13217  15878   2939  -1526   2594       C\\nATOM   1543  N   GLY A1023      46.907 -10.195  47.471  1.00108.89           N\\nANISOU 1543  N   GLY A1023    12123  13753  15498   2586  -2436   2704       N\\nATOM   1544  CA  GLY A1023      48.156  -9.536  47.793  1.00110.44           C\\nANISOU 1544  CA  GLY A1023    11736  14212  16013   2619  -2755   2653       C\\nATOM   1545  C   GLY A1023      48.709  -8.632  46.710  1.00113.05           C\\nANISOU 1545  C   GLY A1023    11548  14751  16654   2465  -2360   2382       C\\nATOM   1546  O   GLY A1023      49.639  -7.862  46.986  1.00112.39           O\\nANISOU 1546  O   GLY A1023    10982  14921  16798   2361  -2597   2323       O\\nATOM   1547  N   TYR A1024      48.174  -8.700  45.495  1.00108.30           N\\nANISOU 1547  N   TYR A1024    11043  14058  16046   2411  -1784   2230       N\\nATOM   1548  CA  TYR A1024      48.663  -7.880  44.398  1.00113.34           C\\nANISOU 1548  CA  TYR A1024    11259  14900  16907   2217  -1372   2019       C\\nATOM   1549  C   TYR A1024      48.186  -6.439  44.545  1.00111.52           C\\nANISOU 1549  C   TYR A1024    11170  14816  16386   1738  -1381   1979       C\\nATOM   1550  O   TYR A1024      47.084  -6.173  45.033  1.00110.91           O\\nANISOU 1550  O   TYR A1024    11615  14645  15882   1574  -1459   2021       O\\nATOM   1551  CB  TYR A1024      48.188  -8.447  43.060  1.00116.94           C\\nANISOU 1551  CB  TYR A1024    11856  15216  17360   2297   -787   1879       C\\nATOM   1552  CG  TYR A1024      48.578  -9.890  42.820  1.00122.30           C\\nANISOU 1552  CG  TYR A1024    12446  15674  18349   2790   -744   1850       C\\nATOM   1553  CD1 TYR A1024      49.830 -10.364  43.189  1.00128.61           C\\nANISOU 1553  CD1 TYR A1024    12689  16530  19645   3150  -1024   1848       C\\nATOM   1554  CD2 TYR A1024      47.689 -10.779  42.227  1.00118.01           C\\nANISOU 1554  CD2 TYR A1024    12364  14836  17638   2906   -460   1804       C\\nATOM   1555  CE1 TYR A1024      50.188 -11.681  42.970  1.00131.77           C\\nANISOU 1555  CE1 TYR A1024    13011  16664  20391   3655  -1019   1793       C\\nATOM   1556  CE2 TYR A1024      48.037 -12.096  42.004  1.00120.38           C\\nANISOU 1556  CE2 TYR A1024    12621  14859  18257   3363   -444   1744       C\\nATOM   1557  CZ  TYR A1024      49.287 -12.542  42.377  1.00129.11           C\\nANISOU 1557  CZ  TYR A1024    13187  15991  19879   3758   -723   1736       C\\nATOM   1558  OH  TYR A1024      49.639 -13.855  42.158  1.00133.04           O\\nANISOU 1558  OH  TYR A1024    13642  16152  20756   4269   -742   1651       O\\nATOM   1559  N   TYR A1025      49.029  -5.504  44.113  1.00117.71           N\\nANISOU 1559  N   TYR A1025    11469  15821  17433   1507  -1294   1881       N\\nATOM   1560  CA  TYR A1025      48.682  -4.087  44.152  1.00110.35           C\\nANISOU 1560  CA  TYR A1025    10659  14955  16314   1049  -1319   1834       C\\nATOM   1561  C   TYR A1025      47.758  -3.760  42.985  1.00104.43           C\\nANISOU 1561  C   TYR A1025    10246  14092  15339    855   -821   1781       C\\nATOM   1562  O   TYR A1025      48.115  -3.979  41.822  1.00101.17           O\\nANISOU 1562  O   TYR A1025     9617  13740  15082    859   -384   1729       O\\nATOM   1563  CB  TYR A1025      49.939  -3.221  44.101  1.00111.84           C\\nANISOU 1563  CB  TYR A1025    10220  15385  16890    814  -1427   1782       C\\nATOM   1564  CG  TYR A1025      50.892  -3.432  45.257  1.00115.51           C\\nANISOU 1564  CG  TYR A1025    10303  15992  17595    978  -1998   1822       C\\nATOM   1565  CD1 TYR A1025      50.776  -2.688  46.423  1.00114.38           C\\nANISOU 1565  CD1 TYR A1025    10332  15875  17252    775  -2517   1825       C\\nATOM   1566  CD2 TYR A1025      51.915  -4.369  45.177  1.00120.42           C\\nANISOU 1566  CD2 TYR A1025    10384  16722  18646   1352  -2046   1830       C\\nATOM   1567  CE1 TYR A1025      51.647  -2.875  47.481  1.00116.89           C\\nANISOU 1567  CE1 TYR A1025    10328  16345  17742    906  -3095   1869       C\\nATOM   1568  CE2 TYR A1025      52.791  -4.563  46.228  1.00124.27           C\\nANISOU 1568  CE2 TYR A1025    10509  17338  19372   1522  -2643   1887       C\\nATOM   1569  CZ  TYR A1025      52.653  -3.813  47.377  1.00124.31           C\\nANISOU 1569  CZ  TYR A1025    10724  17386  19121   1279  -3180   1923       C\\nATOM   1570  OH  TYR A1025      53.523  -4.004  48.428  1.00131.17           O\\nANISOU 1570  OH  TYR A1025    11258  18402  20177   1430  -3829   1986       O\\nATOM   1571  N   THR A1026      46.569  -3.247  43.288  1.00104.70           N\\nANISOU 1571  N   THR A1026    10799  13985  14997    692   -893   1776       N\\nATOM   1572  CA  THR A1026      45.596  -2.892  42.268  1.00105.81           C\\nANISOU 1572  CA  THR A1026    11282  14002  14919    524   -528   1739       C\\nATOM   1573  C   THR A1026      45.108  -1.467  42.499  1.00102.55           C\\nANISOU 1573  C   THR A1026    11058  13525  14382    179   -701   1694       C\\nATOM   1574  O   THR A1026      45.449  -0.819  43.493  1.00 98.86           O\\nANISOU 1574  O   THR A1026    10500  13102  13962     75  -1083   1653       O\\nATOM   1575  CB  THR A1026      44.400  -3.858  42.255  1.00102.47           C\\nANISOU 1575  CB  THR A1026    11323  13413  14198    735   -413   1745       C\\nATOM   1576  OG1 THR A1026      43.497  -3.517  43.312  1.00 98.43           O\\nANISOU 1576  OG1 THR A1026    11152  12846  13400    677   -704   1728       O\\nATOM   1577  CG2 THR A1026      44.861  -5.301  42.437  1.00103.30           C\\nANISOU 1577  CG2 THR A1026    11315  13487  14447   1108   -410   1798       C\\nATOM   1578  N   ILE A1027      44.296  -0.982  41.560  1.00 99.57           N\\nANISOU 1578  N   ILE A1027    10963  13018  13850     15   -450   1686       N\\nATOM   1579  CA  ILE A1027      43.734   0.361  41.638  1.00 94.27           C\\nANISOU 1579  CA  ILE A1027    10513  12198  13107   -265   -621   1637       C\\nATOM   1580  C   ILE A1027      42.483   0.419  40.770  1.00 89.78           C\\nANISOU 1580  C   ILE A1027    10350  11463  12301   -276   -407   1635       C\\nATOM   1581  O   ILE A1027      42.233  -0.483  39.962  1.00 86.52           O\\nANISOU 1581  O   ILE A1027    10008  11080  11787   -145    -97   1677       O\\nATOM   1582  CB  ILE A1027      44.771   1.417  41.213  1.00 89.65           C\\nANISOU 1582  CB  ILE A1027     9615  11643  12803   -620   -639   1700       C\\nATOM   1583  CG1 ILE A1027      44.397   2.796  41.761  1.00 84.69           C\\nANISOU 1583  CG1 ILE A1027     9187  10803  12189   -869   -988   1614       C\\nATOM   1584  CG2 ILE A1027      44.914   1.453  39.698  1.00 80.58           C\\nANISOU 1584  CG2 ILE A1027     8450  10512  11654   -794   -204   1829       C\\nATOM   1585  CD1 ILE A1027      45.403   3.866  41.434  1.00 82.74           C\\nANISOU 1585  CD1 ILE A1027     8667  10528  12241  -1282  -1056   1694       C\\nATOM   1586  N   GLY A1028      41.681   1.469  40.938  1.00 90.15           N\\nANISOU 1586  N   GLY A1028    10659  11318  12274   -414   -605   1560       N\\nATOM   1587  CA  GLY A1028      40.491   1.617  40.118  1.00 84.64           C\\nANISOU 1587  CA  GLY A1028    10306  10458  11396   -412   -482   1559       C\\nATOM   1588  C   GLY A1028      39.429   0.607  40.504  1.00 83.32           C\\nANISOU 1588  C   GLY A1028    10333  10329  10994   -142   -422   1455       C\\nATOM   1589  O   GLY A1028      39.140   0.390  41.685  1.00 81.04           O\\nANISOU 1589  O   GLY A1028    10066  10102  10624    -17   -599   1333       O\\nATOM   1590  N   ILE A1029      38.832  -0.021  39.494  1.00 90.61           N\\nANISOU 1590  N   ILE A1029    11415  11232  11782    -90   -168   1506       N\\nATOM   1591  CA  ILE A1029      37.857  -1.077  39.728  1.00 88.98           C\\nANISOU 1591  CA  ILE A1029    11375  11052  11381    109    -82   1426       C\\nATOM   1592  C   ILE A1029      38.467  -2.405  39.306  1.00 96.86           C\\nANISOU 1592  C   ILE A1029    12278  12138  12386    239    180   1504       C\\nATOM   1593  O   ILE A1029      38.305  -2.841  38.160  1.00 98.47           O\\nANISOU 1593  O   ILE A1029    12577  12322  12515    224    426   1527       O\\nATOM   1594  CB  ILE A1029      36.538  -0.812  38.980  1.00 75.33           C\\nANISOU 1594  CB  ILE A1029     9908   9202   9511     82    -63   1368       C\\nATOM   1595  CG1 ILE A1029      35.978   0.560  39.350  1.00 71.56           C\\nANISOU 1595  CG1 ILE A1029     9501   8581   9108     11   -352   1261       C\\nATOM   1596  CG2 ILE A1029      35.522  -1.900  39.298  1.00 63.88           C\\nANISOU 1596  CG2 ILE A1029     8583   7799   7889    229     23   1272       C\\nATOM   1597  CD1 ILE A1029      34.589   0.806  38.813  1.00 68.30           C\\nANISOU 1597  CD1 ILE A1029     9287   8054   8610     55   -413   1168       C\\nATOM   1598  N   GLY A1030      39.179  -3.050  40.226  1.00 99.15           N\\nANISOU 1598  N   GLY A1030    12396  12511  12765    380    101   1529       N\\nATOM   1599  CA  GLY A1030      39.787  -4.335  39.947  1.00 98.18           C\\nANISOU 1599  CA  GLY A1030    12171  12410  12722    571    291   1577       C\\nATOM   1600  C   GLY A1030      40.760  -4.288  38.789  1.00 94.57           C\\nANISOU 1600  C   GLY A1030    11485  12025  12421    523    562   1598       C\\nATOM   1601  O   GLY A1030      40.506  -4.869  37.728  1.00 95.69           O\\nANISOU 1601  O   GLY A1030    11749  12138  12469    550    849   1553       O\\nATOM   1602  N   HIS A1031      41.878  -3.592  38.977  1.00 87.03           N\\nANISOU 1602  N   HIS A1031    10189  11192  11687    421    486   1644       N\\nATOM   1603  CA  HIS A1031      42.893  -3.436  37.938  1.00 89.86           C\\nANISOU 1603  CA  HIS A1031    10256  11692  12196    312    785   1660       C\\nATOM   1604  C   HIS A1031      44.259  -3.687  38.565  1.00 92.16           C\\nANISOU 1604  C   HIS A1031    10046  12138  12831    439    693   1664       C\\nATOM   1605  O   HIS A1031      44.848  -2.781  39.162  1.00 95.75           O\\nANISOU 1605  O   HIS A1031    10270  12666  13443    260    450   1711       O\\nATOM   1606  CB  HIS A1031      42.821  -2.053  37.308  1.00 89.34           C\\nANISOU 1606  CB  HIS A1031    10256  11621  12066    -69    797   1742       C\\nATOM   1607  CG  HIS A1031      43.762  -1.865  36.161  1.00 92.70           C\\nANISOU 1607  CG  HIS A1031    10434  12232  12556   -271   1167   1789       C\\nATOM   1608  ND1 HIS A1031      43.332  -1.784  34.855  1.00 93.45           N\\nANISOU 1608  ND1 HIS A1031    10789  12339  12379   -440   1471   1824       N\\nATOM   1609  CD2 HIS A1031      45.109  -1.748  36.123  1.00 96.67           C\\nANISOU 1609  CD2 HIS A1031    10434  12956  13341   -356   1297   1798       C\\nATOM   1610  CE1 HIS A1031      44.375  -1.621  34.061  1.00 97.80           C\\nANISOU 1610  CE1 HIS A1031    11037  13125  12996   -641   1814   1858       C\\nATOM   1611  NE2 HIS A1031      45.465  -1.597  34.805  1.00100.11           N\\nANISOU 1611  NE2 HIS A1031    10830  13554  13654   -592   1731   1833       N\\nATOM   1612  N   LEU A1032      44.761  -4.912  38.422  1.00 91.24           N\\nANISOU 1612  N   LEU A1032     9754  12051  12863    756    853   1596       N\\nATOM   1613  CA  LEU A1032      46.058  -5.267  38.982  1.00 95.11           C\\nANISOU 1613  CA  LEU A1032     9720  12682  13737    952    730   1587       C\\nATOM   1614  C   LEU A1032      47.161  -4.499  38.265  1.00 99.71           C\\nANISOU 1614  C   LEU A1032     9815  13531  14540    697    975   1562       C\\nATOM   1615  O   LEU A1032      47.347  -4.649  37.054  1.00 96.96           O\\nANISOU 1615  O   LEU A1032     9403  13297  14140    624   1442   1479       O\\nATOM   1616  CB  LEU A1032      46.290  -6.772  38.868  1.00 93.50           C\\nANISOU 1616  CB  LEU A1032     9457  12381  13686   1392    849   1495       C\\nATOM   1617  N   LEU A1033      47.887  -3.667  39.013  1.00 97.35           N\\nANISOU 1617  N   LEU A1033     9181  13349  14459    521    666   1628       N\\nATOM   1618  CA  LEU A1033      49.025  -2.964  38.434  1.00104.31           C\\nANISOU 1618  CA  LEU A1033     9528  14502  15604    230    883   1619       C\\nATOM   1619  C   LEU A1033      50.158  -3.934  38.121  1.00112.65           C\\nANISOU 1619  C   LEU A1033     9983  15786  17034    550   1131   1473       C\\nATOM   1620  O   LEU A1033      50.737  -3.897  37.029  1.00115.99           O\\nANISOU 1620  O   LEU A1033    10102  16446  17521    410   1635   1381       O\\nATOM   1621  CB  LEU A1033      49.494  -1.861  39.381  1.00103.46           C\\nANISOU 1621  CB  LEU A1033     9213  14430  15668    -55    434   1699       C\\nATOM   1622  N   THR A1034      50.477  -4.818  39.064  1.00114.71           N\\nANISOU 1622  N   THR A1034    10071  15980  17534    990    782   1443       N\\nATOM   1623  CA  THR A1034      51.514  -5.822  38.866  1.00119.05           C\\nANISOU 1623  CA  THR A1034    10043  16677  18514   1403    933   1278       C\\nATOM   1624  C   THR A1034      51.333  -6.919  39.904  1.00116.13           C\\nANISOU 1624  C   THR A1034     9831  16045  18250   1915    470   1326       C\\nATOM   1625  O   THR A1034      50.615  -6.756  40.893  1.00112.94           O\\nANISOU 1625  O   THR A1034     9869  15449  17593   1873     24   1499       O\\nATOM   1626  CB  THR A1034      52.919  -5.218  38.968  1.00123.11           C\\nANISOU 1626  CB  THR A1034     9729  17558  19489   1237    901   1232       C\\nATOM   1627  OG1 THR A1034      53.898  -6.241  38.746  1.00127.31           O\\nANISOU 1627  OG1 THR A1034     9644  18240  20490   1707   1059   1022       O\\nATOM   1628  CG2 THR A1034      53.135  -4.617  40.344  1.00124.58           C\\nANISOU 1628  CG2 THR A1034     9836  17714  19783   1140    210   1384       C\\nATOM   1629  N   LYS A1035      51.998  -8.046  39.660  1.00124.24           N\\nANISOU 1629  N   LYS A1035    10499  17061  19647   2398    588   1165       N\\nATOM   1630  CA  LYS A1035      52.071  -9.132  40.624  1.00115.60           C\\nANISOU 1630  CA  LYS A1035     9471  15694  18757   2910    100   1245       C\\nATOM   1631  C   LYS A1035      53.350  -9.089  41.448  1.00124.45           C\\nANISOU 1631  C   LYS A1035     9878  17011  20395   3112   -361   1270       C\\nATOM   1632  O   LYS A1035      53.591 -10.004  42.241  1.00126.86           O\\nANISOU 1632  O   LYS A1035    10167  17100  20932   3572   -826   1360       O\\nATOM   1633  CB  LYS A1035      51.953 -10.483  39.911  1.00108.04           C\\nANISOU 1633  CB  LYS A1035     8621  14489  17940   3381    417   1046       C\\nATOM   1634  N   SER A1036      54.169  -8.044  41.282  1.00124.75           N\\nANISOU 1634  N   SER A1036     9333  17441  20626   2756   -279   1212       N\\nATOM   1635  CA  SER A1036      55.429  -7.892  41.994  1.00130.16           C\\nANISOU 1635  CA  SER A1036     9248  18374  21834   2880   -717   1205       C\\nATOM   1636  C   SER A1036      55.191  -7.369  43.411  1.00127.51           C\\nANISOU 1636  C   SER A1036     9199  17961  21290   2719  -1470   1465       C\\nATOM   1637  O   SER A1036      54.249  -6.611  43.652  1.00124.62           O\\nANISOU 1637  O   SER A1036     9437  17497  20415   2316  -1507   1585       O\\nATOM   1638  CB  SER A1036      56.351  -6.937  41.243  1.00133.68           C\\nANISOU 1638  CB  SER A1036     8966  19280  22547   2465   -307   1043       C\\nATOM   1639  N   PRO A1037      56.041  -7.758  44.369  1.00132.59           N\\nANISOU 1639  N   PRO A1037     9408  18656  22314   3043  -2094   1531       N\\nATOM   1640  CA  PRO A1037      55.818  -7.332  45.758  1.00131.46           C\\nANISOU 1640  CA  PRO A1037     9590  18465  21895   2895  -2836   1763       C\\nATOM   1641  C   PRO A1037      56.251  -5.907  46.050  1.00131.07           C\\nANISOU 1641  C   PRO A1037     9233  18724  21845   2324  -3004   1723       C\\nATOM   1642  O   PRO A1037      55.767  -5.327  47.031  1.00128.15           O\\nANISOU 1642  O   PRO A1037     9314  18300  21079   2075  -3470   1849       O\\nATOM   1643  CB  PRO A1037      56.658  -8.330  46.564  1.00137.89           C\\nANISOU 1643  CB  PRO A1037    10022  19225  23144   3474  -3467   1855       C\\nATOM   1644  CG  PRO A1037      57.788  -8.659  45.647  1.00141.32           C\\nANISOU 1644  CG  PRO A1037     9525  19887  24282   3748  -3098   1581       C\\nATOM   1645  CD  PRO A1037      57.205  -8.654  44.250  1.00138.32           C\\nANISOU 1645  CD  PRO A1037     9352  19476  23728   3597  -2186   1384       C\\nATOM   1646  N   SER A1038      57.142  -5.329  45.249  1.00134.97           N\\nANISOU 1646  N   SER A1038     8987  19535  22758   2087  -2636   1539       N\\nATOM   1647  CA  SER A1038      57.615  -3.977  45.512  1.00138.82           C\\nANISOU 1647  CA  SER A1038     9165  20272  23307   1497  -2818   1510       C\\nATOM   1648  C   SER A1038      56.508  -2.965  45.234  1.00142.03           C\\nANISOU 1648  C   SER A1038    10304  20506  23157    966  -2548   1556       C\\nATOM   1649  O   SER A1038      55.905  -2.966  44.156  1.00142.81           O\\nANISOU 1649  O   SER A1038    10685  20515  23061    864  -1905   1526       O\\nATOM   1650  CB  SER A1038      58.845  -3.669  44.659  1.00137.97           C\\nANISOU 1650  CB  SER A1038     8060  20560  23801   1331  -2429   1322       C\\nATOM   1651  N   LEU A1039      56.235  -2.105  46.219  1.00148.93           N\\nANISOU 1651  N   LEU A1039    11491  21326  23772    647  -3071   1607       N\\nATOM   1652  CA  LEU A1039      55.237  -1.059  46.027  1.00137.41           C\\nANISOU 1652  CA  LEU A1039    10670  19674  21866    176  -2887   1609       C\\nATOM   1653  C   LEU A1039      55.728  -0.005  45.042  1.00134.86           C\\nANISOU 1653  C   LEU A1039     9968  19484  21790   -372  -2464   1547       C\\nATOM   1654  O   LEU A1039      54.942   0.522  44.246  1.00128.51           O\\nANISOU 1654  O   LEU A1039     9617  18504  20707   -648  -2029   1577       O\\nATOM   1655  CB  LEU A1039      54.882  -0.422  47.371  1.00133.76           C\\nANISOU 1655  CB  LEU A1039    10606  19126  21088      8  -3557   1606       C\\nATOM   1656  CG  LEU A1039      53.969   0.807  47.351  1.00123.44           C\\nANISOU 1656  CG  LEU A1039     9880  17606  19417   -461  -3487   1537       C\\nATOM   1657  CD1 LEU A1039      52.634   0.486  46.697  1.00115.73           C\\nANISOU 1657  CD1 LEU A1039     9575  16373  18024   -334  -3002   1586       C\\nATOM   1658  CD2 LEU A1039      53.766   1.349  48.759  1.00121.51           C\\nANISOU 1658  CD2 LEU A1039     9948  17332  18887   -575  -4163   1451       C\\nATOM   1659  N   ASN A1040      57.027   0.309  45.078  1.00140.78           N\\nANISOU 1659  N   ASN A1040     9881  20545  23065   -557  -2602   1481       N\\nATOM   1660  CA  ASN A1040      57.584   1.273  44.135  1.00137.59           C\\nANISOU 1660  CA  ASN A1040     9069  20297  22910  -1145  -2171   1458       C\\nATOM   1661  C   ASN A1040      57.424   0.803  42.695  1.00142.78           C\\nANISOU 1661  C   ASN A1040     9696  21027  23528  -1086  -1335   1468       C\\nATOM   1662  O   ASN A1040      57.214   1.623  41.793  1.00129.49           O\\nANISOU 1662  O   ASN A1040     8176  19309  21715  -1595   -895   1536       O\\nATOM   1663  CB  ASN A1040      59.058   1.528  44.452  1.00137.97           C\\nANISOU 1663  CB  ASN A1040     8117  20728  23578  -1326  -2453   1368       C\\nATOM   1664  N   ALA A1041      57.513  -0.508  42.459  1.00141.43           N\\nANISOU 1664  N   ALA A1041     9359  20933  23447   -478  -1132   1401       N\\nATOM   1665  CA  ALA A1041      57.326  -1.032  41.111  1.00146.42           C\\nANISOU 1665  CA  ALA A1041    10009  21635  23988   -388   -344   1347       C\\nATOM   1666  C   ALA A1041      55.865  -0.980  40.683  1.00137.93           C\\nANISOU 1666  C   ALA A1041     9919  20195  22294   -425   -117   1454       C\\nATOM   1667  O   ALA A1041      55.576  -0.783  39.497  1.00137.36           O\\nANISOU 1667  O   ALA A1041    10016  20159  22015   -671    490   1467       O\\nATOM   1668  CB  ALA A1041      57.852  -2.465  41.023  1.00155.04           C\\nANISOU 1668  CB  ALA A1041    10644  22857  25406    310   -239   1186       C\\nATOM   1669  N   ALA A1042      54.935  -1.157  41.626  1.00140.82           N\\nANISOU 1669  N   ALA A1042    10925  20238  22341   -200   -595   1527       N\\nATOM   1670  CA  ALA A1042      53.519  -1.060  41.288  1.00132.90           C\\nANISOU 1670  CA  ALA A1042    10790  18913  20795   -244   -420   1604       C\\nATOM   1671  C   ALA A1042      53.142   0.352  40.863  1.00133.14           C\\nANISOU 1671  C   ALA A1042    11109  18838  20640   -869   -326   1693       C\\nATOM   1672  O   ALA A1042      52.205   0.531  40.075  1.00130.01           O\\nANISOU 1672  O   ALA A1042    11253  18260  19885   -986      1   1755       O\\nATOM   1673  CB  ALA A1042      52.662  -1.505  42.472  1.00126.18           C\\nANISOU 1673  CB  ALA A1042    10481  17801  19659     81   -937   1646       C\\nATOM   1674  N   LYS A1043      53.853   1.361  41.370  1.00137.98           N\\nANISOU 1674  N   LYS A1043    11384  19531  21510  -1275   -652   1703       N\\nATOM   1675  CA  LYS A1043      53.613   2.736  40.950  1.00131.35           C\\nANISOU 1675  CA  LYS A1043    10799  18530  20579  -1894   -598   1802       C\\nATOM   1676  C   LYS A1043      54.204   3.022  39.577  1.00133.43           C\\nANISOU 1676  C   LYS A1043    10730  19015  20952  -2291     34   1891       C\\nATOM   1677  O   LYS A1043      53.705   3.899  38.864  1.00133.13           O\\nANISOU 1677  O   LYS A1043    11108  18782  20694  -2733    227   2044       O\\nATOM   1678  CB  LYS A1043      54.192   3.713  41.976  1.00128.92           C\\nANISOU 1678  CB  LYS A1043    10263  18193  20526  -2230  -1186   1758       C\\nATOM   1679  CG  LYS A1043      53.569   3.618  43.359  1.00124.36           C\\nANISOU 1679  CG  LYS A1043    10090  17422  19739  -1936  -1811   1654       C\\nATOM   1680  CD  LYS A1043      54.054   4.744  44.258  1.00124.45           C\\nANISOU 1680  CD  LYS A1043     9973  17371  19941  -2345  -2374   1565       C\\nATOM   1681  CE  LYS A1043      53.301   4.761  45.577  1.00122.13           C\\nANISOU 1681  CE  LYS A1043    10189  16897  19319  -2105  -2935   1426       C\\nATOM   1682  NZ  LYS A1043      53.698   5.919  46.425  1.00124.65           N\\nANISOU 1682  NZ  LYS A1043    10461  17121  19779  -2520  -3485   1275       N\\nATOM   1683  N   SER A1044      55.263   2.305  39.194  1.00130.51           N\\nANISOU 1683  N   SER A1044     9619  19057  20914  -2142    357   1795       N\\nATOM   1684  CA  SER A1044      55.858   2.511  37.879  1.00137.15           C\\nANISOU 1684  CA  SER A1044    10108  20197  21806  -2533   1041   1845       C\\nATOM   1685  C   SER A1044      54.904   2.086  36.770  1.00136.57           C\\nANISOU 1685  C   SER A1044    10643  20016  21232  -2427   1563   1899       C\\nATOM   1686  O   SER A1044      54.789   2.771  35.747  1.00141.22           O\\nANISOU 1686  O   SER A1044    11441  20628  21589  -2937   1967   2067       O\\nATOM   1687  CB  SER A1044      57.179   1.749  37.775  1.00143.25           C\\nANISOU 1687  CB  SER A1044     9888  21468  23072  -2311   1285   1648       C\\nATOM   1688  N   GLU A1045      54.211   0.960  36.954  1.00136.81           N\\nANISOU 1688  N   GLU A1045    10988  19917  21076  -1800   1534   1777       N\\nATOM   1689  CA  GLU A1045      53.243   0.521  35.955  1.00129.18           C\\nANISOU 1689  CA  GLU A1045    10619  18832  19631  -1695   1960   1797       C\\nATOM   1690  C   GLU A1045      52.010   1.415  35.939  1.00128.34           C\\nANISOU 1690  C   GLU A1045    11333  18313  19118  -1974   1718   2002       C\\nATOM   1691  O   GLU A1045      51.383   1.582  34.887  1.00126.75           O\\nANISOU 1691  O   GLU A1045    11575  18053  18531  -2171   2069   2109       O\\nATOM   1692  CB  GLU A1045      52.847  -0.934  36.210  1.00121.20           C\\nANISOU 1692  CB  GLU A1045     9714  17751  18586   -982   1950   1604       C\\nATOM   1693  N   LEU A1046      51.650   1.998  37.088  1.00131.91           N\\nANISOU 1693  N   LEU A1046    11988  18485  19645  -1980   1106   2037       N\\nATOM   1694  CA  LEU A1046      50.490   2.885  37.146  1.00126.43           C\\nANISOU 1694  CA  LEU A1046    12012  17383  18643  -2189    846   2169       C\\nATOM   1695  C   LEU A1046      50.730   4.156  36.342  1.00134.52           C\\nANISOU 1695  C   LEU A1046    13116  18345  19652  -2860    993   2395       C\\nATOM   1696  O   LEU A1046      49.873   4.579  35.558  1.00138.35           O\\nANISOU 1696  O   LEU A1046    14165  18604  19797  -3036   1114   2555       O\\nATOM   1697  CB  LEU A1046      50.156   3.227  38.600  1.00114.87           C\\nANISOU 1697  CB  LEU A1046    10689  15684  17273  -2043    195   2081       C\\nATOM   1698  CG  LEU A1046      49.189   4.395  38.827  1.00103.62           C\\nANISOU 1698  CG  LEU A1046     9857  13838  15674  -2297   -138   2146       C\\nATOM   1699  CD1 LEU A1046      47.828   4.107  38.217  1.00 96.31           C\\nANISOU 1699  CD1 LEU A1046     9556  12698  14341  -2097     22   2183       C\\nATOM   1700  CD2 LEU A1046      49.056   4.722  40.308  1.00 99.47           C\\nANISOU 1700  CD2 LEU A1046     9379  13170  15245  -2171   -734   1980       C\\nATOM   1701  N   ASP A1047      51.893   4.784  36.529  1.00127.49           N\\nANISOU 1701  N   ASP A1047    11667  17635  19137  -3262    951   2433       N\\nATOM   1702  CA  ASP A1047      52.188   6.012  35.801  1.00131.96           C\\nANISOU 1702  CA  ASP A1047    12311  18112  19714  -3978   1078   2692       C\\nATOM   1703  C   ASP A1047      52.444   5.742  34.324  1.00130.92           C\\nANISOU 1703  C   ASP A1047    12130  18291  19323  -4228   1792   2837       C\\nATOM   1704  O   ASP A1047      52.172   6.607  33.483  1.00133.98           O\\nANISOU 1704  O   ASP A1047    12921  18510  19475  -4745   1927   3128       O\\nATOM   1705  CB  ASP A1047      53.382   6.723  36.435  1.00141.47           C\\nANISOU 1705  CB  ASP A1047    12895  19442  21416  -4390    835   2678       C\\nATOM   1706  CG  ASP A1047      53.050   7.320  37.791  1.00139.91           C\\nANISOU 1706  CG  ASP A1047    12900  18874  21385  -4305     95   2555       C\\nATOM   1707  OD1 ASP A1047      51.910   7.125  38.263  1.00133.93           O\\nANISOU 1707  OD1 ASP A1047    12719  17809  20359  -3898   -178   2466       O\\nATOM   1708  OD2 ASP A1047      53.925   7.988  38.382  1.00142.42           O\\nANISOU 1708  OD2 ASP A1047    12791  19231  22093  -4666   -203   2522       O\\nATOM   1709  N   LYS A1048      52.958   4.557  33.986  1.00136.15           N\\nANISOU 1709  N   LYS A1048    12332  19393  20008  -3866   2239   2634       N\\nATOM   1710  CA  LYS A1048      53.156   4.211  32.584  1.00137.23           C\\nANISOU 1710  CA  LYS A1048    12447  19868  19828  -4059   2961   2691       C\\nATOM   1711  C   LYS A1048      51.836   3.990  31.855  1.00136.24           C\\nANISOU 1711  C   LYS A1048    13159  19483  19123  -3907   3045   2785       C\\nATOM   1712  O   LYS A1048      51.813   4.012  30.619  1.00135.03           O\\nANISOU 1712  O   LYS A1048    13198  19529  18579  -4209   3556   2913       O\\nATOM   1713  CB  LYS A1048      54.036   2.964  32.467  1.00137.25           C\\nANISOU 1713  CB  LYS A1048    11720  20374  20055  -3634   3395   2361       C\\nATOM   1714  N   ALA A1049      50.743   3.782  32.587  1.00134.09           N\\nANISOU 1714  N   ALA A1049    13374  18806  18767  -3471   2557   2719       N\\nATOM   1715  CA  ALA A1049      49.423   3.607  31.993  1.00136.97           C\\nANISOU 1715  CA  ALA A1049    14488  18911  18642  -3319   2551   2790       C\\nATOM   1716  C   ALA A1049      48.555   4.853  32.093  1.00139.86           C\\nANISOU 1716  C   ALA A1049    15461  18785  18895  -3629   2088   3059       C\\nATOM   1717  O   ALA A1049      47.775   5.130  31.178  1.00144.34           O\\nANISOU 1717  O   ALA A1049    16587  19202  19054  -3792   2166   3254       O\\nATOM   1718  CB  ALA A1049      48.697   2.429  32.649  1.00134.83           C\\nANISOU 1718  CB  ALA A1049    14339  18543  18349  -2619   2376   2514       C\\nATOM   1719  N   ILE A1050      48.667   5.615  33.186  1.00147.00           N\\nANISOU 1719  N   ILE A1050    16279  19419  20157  -3696   1573   3052       N\\nATOM   1720  CA  ILE A1050      47.884   6.843  33.320  1.00137.76           C\\nANISOU 1720  CA  ILE A1050    15661  17727  18955  -3954   1109   3250       C\\nATOM   1721  C   ILE A1050      48.527   8.029  32.621  1.00135.31           C\\nANISOU 1721  C   ILE A1050    15376  17334  18700  -4696   1193   3602       C\\nATOM   1722  O   ILE A1050      47.861   9.054  32.425  1.00132.09           O\\nANISOU 1722  O   ILE A1050    15513  16449  18227  -4950    855   3834       O\\nATOM   1723  CB  ILE A1050      47.649   7.192  34.802  1.00112.75           C\\nANISOU 1723  CB  ILE A1050    12459  14272  16111  -3710    512   3036       C\\nATOM   1724  N   GLY A1051      49.800   7.923  32.236  1.00128.26           N\\nANISOU 1724  N   GLY A1051    13902  16884  17947  -5058   1630   3652       N\\nATOM   1725  CA  GLY A1051      50.479   8.964  31.501  1.00126.01           C\\nANISOU 1725  CA  GLY A1051    13606  16592  17681  -5844   1802   4017       C\\nATOM   1726  C   GLY A1051      51.114  10.046  32.350  1.00125.68           C\\nANISOU 1726  C   GLY A1051    13328  16279  18144  -6255   1362   4067       C\\nATOM   1727  O   GLY A1051      52.053  10.703  31.888  1.00131.62           O\\nANISOU 1727  O   GLY A1051    13814  17166  19028  -6906   1590   4283       O\\nATOM   1728  N   ARG A1052      50.638  10.250  33.572  1.00125.39           N\\nANISOU 1728  N   ARG A1052    13398  15875  18368  -5892    754   3830       N\\nATOM   1729  CA  ARG A1052      51.137  11.295  34.452  1.00130.48           C\\nANISOU 1729  CA  ARG A1052    13895  16207  19473  -6249    261   3810       C\\nATOM   1730  C   ARG A1052      51.879  10.681  35.633  1.00133.64           C\\nANISOU 1730  C   ARG A1052    13610  16936  20230  -5922     98   3432       C\\nATOM   1731  O   ARG A1052      51.880   9.465  35.836  1.00139.15           O\\nANISOU 1731  O   ARG A1052    14025  18014  20831  -5363    306   3204       O\\nATOM   1732  CB  ARG A1052      49.986  12.174  34.954  1.00127.22           C\\nANISOU 1732  CB  ARG A1052    14202  15072  19066  -6123   -369   3798       C\\nATOM   1733  CG  ARG A1052      49.063  11.466  35.933  1.00118.27           C\\nANISOU 1733  CG  ARG A1052    13210  13879  17849  -5343   -664   3404       C\\nATOM   1734  CD  ARG A1052      47.922  12.363  36.372  1.00115.96           C\\nANISOU 1734  CD  ARG A1052    13565  12916  17579  -5212  -1224   3339       C\\nATOM   1735  NE  ARG A1052      47.116  11.751  37.424  1.00114.03           N\\nANISOU 1735  NE  ARG A1052    13390  12676  17262  -4541  -1477   2931       N\\nATOM   1736  CZ  ARG A1052      47.303  11.960  38.723  1.00115.93           C\\nANISOU 1736  CZ  ARG A1052    13460  12852  17737  -4403  -1881   2594       C\\nATOM   1737  NH1 ARG A1052      48.271  12.768  39.132  1.00119.81           N\\nANISOU 1737  NH1 ARG A1052    13686  13244  18594  -4875  -2117   2592       N\\nATOM   1738  NH2 ARG A1052      46.523  11.364  39.613  1.00113.10           N\\nANISOU 1738  NH2 ARG A1052    13205  12544  17222  -3834  -2048   2259       N\\nATOM   1739  N   ASN A1053      52.517  11.551  36.419  1.00125.16           N\\nANISOU 1739  N   ASN A1053    12297  15678  19580  -6291   -324   3375       N\\nATOM   1740  CA  ASN A1053      53.118  11.156  37.692  1.00123.03           C\\nANISOU 1740  CA  ASN A1053    11481  15629  19636  -6002   -663   3022       C\\nATOM   1741  C   ASN A1053      52.002  11.117  38.731  1.00122.77           C\\nANISOU 1741  C   ASN A1053    11968  15217  19462  -5447  -1194   2750       C\\nATOM   1742  O   ASN A1053      51.786  12.056  39.502  1.00122.02           O\\nANISOU 1742  O   ASN A1053    12131  14690  19541  -5602  -1734   2626       O\\nATOM   1743  CB  ASN A1053      54.234  12.115  38.089  1.00126.67           C\\nANISOU 1743  CB  ASN A1053    11485  16063  20583  -6663   -923   3047       C\\nATOM   1744  N   THR A1054      51.272   9.995  38.739  1.00124.33           N\\nANISOU 1744  N   THR A1054    12319  15587  19333  -4804  -1013   2632       N\\nATOM   1745  CA  THR A1054      50.060   9.901  39.547  1.00119.55           C\\nANISOU 1745  CA  THR A1054    12244  14668  18513  -4306  -1394   2406       C\\nATOM   1746  C   THR A1054      50.366   9.947  41.037  1.00119.71           C\\nANISOU 1746  C   THR A1054    12048  14716  18720  -4133  -1918   2083       C\\nATOM   1747  O   THR A1054      49.504  10.334  41.835  1.00120.96           O\\nANISOU 1747  O   THR A1054    12645  14548  18764  -3922  -2315   1863       O\\nATOM   1748  CB  THR A1054      49.295   8.620  39.212  1.00115.03           C\\nANISOU 1748  CB  THR A1054    11827  14310  17568  -3728  -1059   2370       C\\nATOM   1749  N   ASN A1055      51.577   9.556  41.433  1.00118.97           N\\nANISOU 1749  N   ASN A1055    11271  15030  18901  -4213  -1934   2029       N\\nATOM   1750  CA  ASN A1055      52.004   9.557  42.830  1.00116.22           C\\nANISOU 1750  CA  ASN A1055    10681  14771  18707  -4084  -2473   1748       C\\nATOM   1751  C   ASN A1055      51.115   8.687  43.711  1.00119.38           C\\nANISOU 1751  C   ASN A1055    11395  15214  18750  -3437  -2650   1539       C\\nATOM   1752  O   ASN A1055      51.131   8.822  44.935  1.00121.96           O\\nANISOU 1752  O   ASN A1055    11754  15533  19052  -3324  -3143   1293       O\\nATOM   1753  CB  ASN A1055      52.071  10.984  43.391  1.00109.11           C\\nANISOU 1753  CB  ASN A1055     9992  13444  18023  -4552  -2980   1627       C\\nATOM   1754  N   GLY A1056      50.340   7.783  43.111  1.00115.78           N\\nANISOU 1754  N   GLY A1056    11183  14819  17987  -3045  -2253   1632       N\\nATOM   1755  CA  GLY A1056      49.518   6.838  43.832  1.00115.99           C\\nANISOU 1755  CA  GLY A1056    11480  14915  17677  -2485  -2341   1489       C\\nATOM   1756  C   GLY A1056      48.027   7.076  43.671  1.00112.88           C\\nANISOU 1756  C   GLY A1056    11762  14182  16944  -2317  -2293   1431       C\\nATOM   1757  O   GLY A1056      47.247   6.120  43.742  1.00109.86           O\\nANISOU 1757  O   GLY A1056    11592  13885  16264  -1902  -2132   1408       O\\nATOM   1758  N   VAL A1057      47.618   8.323  43.454  1.00113.85           N\\nANISOU 1758  N   VAL A1057    12208  13906  17145  -2632  -2448   1405       N\\nATOM   1759  CA  VAL A1057      46.211   8.699  43.361  1.00103.36           C\\nANISOU 1759  CA  VAL A1057    11467  12226  15579  -2456  -2483   1304       C\\nATOM   1760  C   VAL A1057      45.881   9.003  41.907  1.00105.21           C\\nANISOU 1760  C   VAL A1057    11904  12256  15814  -2653  -2149   1598       C\\nATOM   1761  O   VAL A1057      46.708   9.560  41.176  1.00111.08           O\\nANISOU 1761  O   VAL A1057    12459  12960  16785  -3103  -2041   1831       O\\nATOM   1762  CB  VAL A1057      45.900   9.912  44.260  1.00 96.42           C\\nANISOU 1762  CB  VAL A1057    10853  10979  14804  -2591  -2980   1005       C\\nATOM   1763  N   ILE A1058      44.667   8.639  41.488  1.00104.59           N\\nANISOU 1763  N   ILE A1058    12209  12071  15459  -2350  -1994   1597       N\\nATOM   1764  CA  ILE A1058      44.203   8.889  40.131  1.00100.91           C\\nANISOU 1764  CA  ILE A1058    12012  11414  14916  -2498  -1744   1872       C\\nATOM   1765  C   ILE A1058      42.794   9.466  40.170  1.00 98.60           C\\nANISOU 1765  C   ILE A1058    12224  10714  14524  -2295  -1978   1737       C\\nATOM   1766  O   ILE A1058      42.091   9.405  41.182  1.00 92.24           O\\nANISOU 1766  O   ILE A1058    11523   9875  13648  -1976  -2199   1403       O\\nATOM   1767  CB  ILE A1058      44.229   7.619  39.253  1.00 94.08           C\\nANISOU 1767  CB  ILE A1058    11024  10914  13808  -2321  -1243   2041       C\\nATOM   1768  CG1 ILE A1058      43.313   6.543  39.831  1.00 82.54           C\\nANISOU 1768  CG1 ILE A1058     9675   9599  12089  -1804  -1208   1830       C\\nATOM   1769  CG2 ILE A1058      45.650   7.101  39.083  1.00 91.55           C\\nANISOU 1769  CG2 ILE A1058    10149  10986  13649  -2498   -980   2147       C\\nATOM   1770  CD1 ILE A1058      43.175   5.325  38.950  1.00 80.94           C\\nANISOU 1770  CD1 ILE A1058     9440   9653  11661  -1618   -764   1951       C\\nATOM   1771  N   THR A1059      42.391  10.038  39.038  1.00100.27           N\\nANISOU 1771  N   THR A1059    12740  10636  14723  -2488  -1928   2000       N\\nATOM   1772  CA  THR A1059      41.046  10.571  38.887  1.00100.12           C\\nANISOU 1772  CA  THR A1059    13164  10218  14658  -2267  -2166   1907       C\\nATOM   1773  C   THR A1059      40.043   9.431  38.714  1.00 93.93           C\\nANISOU 1773  C   THR A1059    12445   9697  13549  -1832  -1928   1816       C\\nATOM   1774  O   THR A1059      40.390   8.322  38.302  1.00 93.12           O\\nANISOU 1774  O   THR A1059    12152   9988  13239  -1781  -1546   1935       O\\nATOM   1775  CB  THR A1059      40.982  11.515  37.681  1.00103.74           C\\nANISOU 1775  CB  THR A1059    13952  10269  15193  -2630  -2248   2286       C\\nATOM   1776  OG1 THR A1059      42.175  12.306  37.630  1.00105.14           O\\nANISOU 1776  OG1 THR A1059    13991  10320  15636  -3159  -2321   2476       O\\nATOM   1777  CG2 THR A1059      39.778  12.440  37.771  1.00108.32           C\\nANISOU 1777  CG2 THR A1059    14955  10292  15912  -2422  -2687   2144       C\\nATOM   1778  N   LYS A1060      38.780   9.709  39.047  1.00 98.18           N\\nANISOU 1778  N   LYS A1060    13229  10001  14072  -1515  -2161   1570       N\\nATOM   1779  CA  LYS A1060      37.721   8.768  38.697  1.00 98.24           C\\nANISOU 1779  CA  LYS A1060    13319  10201  13806  -1182  -1964   1522       C\\nATOM   1780  C   LYS A1060      37.594   8.635  37.188  1.00 99.60           C\\nANISOU 1780  C   LYS A1060    13688  10335  13819  -1346  -1790   1903       C\\nATOM   1781  O   LYS A1060      37.139   7.599  36.688  1.00 95.67           O\\nANISOU 1781  O   LYS A1060    13192  10106  13053  -1183  -1519   1935       O\\nATOM   1782  CB  LYS A1060      36.389   9.207  39.307  1.00 93.38           C\\nANISOU 1782  CB  LYS A1060    12863   9359  13257   -838  -2249   1162       C\\nATOM   1783  N   ASP A1061      37.997   9.671  36.449  1.00103.09           N\\nANISOU 1783  N   ASP A1061    14329  10441  14400  -1703  -1952   2200       N\\nATOM   1784  CA  ASP A1061      38.006   9.603  34.993  1.00101.97           C\\nANISOU 1784  CA  ASP A1061    14414  10301  14028  -1942  -1780   2607       C\\nATOM   1785  C   ASP A1061      39.176   8.768  34.485  1.00100.34           C\\nANISOU 1785  C   ASP A1061    13939  10555  13629  -2196  -1275   2797       C\\nATOM   1786  O   ASP A1061      39.012   7.961  33.563  1.00 99.43           O\\nANISOU 1786  O   ASP A1061    13894  10699  13185  -2180   -958   2926       O\\nATOM   1787  CB  ASP A1061      38.055  11.015  34.413  1.00102.76           C\\nANISOU 1787  CB  ASP A1061    14862   9863  14320  -2281  -2142   2907       C\\nATOM   1788  CG  ASP A1061      37.962  11.029  32.903  1.00102.52           C\\nANISOU 1788  CG  ASP A1061    15156   9822  13974  -2555  -2021   3367       C\\nATOM   1789  OD1 ASP A1061      36.881  10.700  32.371  1.00 98.49           O\\nANISOU 1789  OD1 ASP A1061    14872   9291  13258  -2289  -2114   3362       O\\nATOM   1790  OD2 ASP A1061      38.970  11.374  32.248  1.00105.90           O\\nANISOU 1790  OD2 ASP A1061    15607  10290  14339  -3064  -1832   3728       O\\nATOM   1791  N   GLU A1062      40.362   8.948  35.075  1.00102.50           N\\nANISOU 1791  N   GLU A1062    13880  10945  14119  -2420  -1205   2776       N\\nATOM   1792  CA  GLU A1062      41.504   8.118  34.707  1.00 96.62           C\\nANISOU 1792  CA  GLU A1062    12770  10671  13271  -2592   -725   2880       C\\nATOM   1793  C   GLU A1062      41.237   6.651  35.014  1.00 88.82           C\\nANISOU 1793  C   GLU A1062    11588  10061  12098  -2156   -455   2641       C\\nATOM   1794  O   GLU A1062      41.657   5.764  34.262  1.00 83.40           O\\nANISOU 1794  O   GLU A1062    10776   9705  11208  -2174    -28   2718       O\\nATOM   1795  CB  GLU A1062      42.761   8.595  35.435  1.00 87.02           C\\nANISOU 1795  CB  GLU A1062    11163   9509  12392  -2870   -785   2852       C\\nATOM   1796  CG  GLU A1062      43.240   9.972  35.025  1.00 95.42           C\\nANISOU 1796  CG  GLU A1062    12385  10212  13658  -3416   -988   3136       C\\nATOM   1797  CD  GLU A1062      44.494  10.395  35.768  1.00 99.73           C\\nANISOU 1797  CD  GLU A1062    12491  10838  14563  -3723  -1061   3077       C\\nATOM   1798  OE1 GLU A1062      44.628  10.042  36.959  1.00 95.17           O\\nANISOU 1798  OE1 GLU A1062    11645  10382  14135  -3431  -1231   2743       O\\nATOM   1799  OE2 GLU A1062      45.347  11.075  35.159  1.00104.48           O\\nANISOU 1799  OE2 GLU A1062    13018  11399  15279  -4288   -958   3375       O\\nATOM   1800  N   ALA A1063      40.542   6.377  36.121  1.00 85.45           N\\nANISOU 1800  N   ALA A1063    11151   9581  11735  -1777   -689   2337       N\\nATOM   1801  CA  ALA A1063      40.186   5.003  36.456  1.00 86.64           C\\nANISOU 1801  CA  ALA A1063    11186  10021  11712  -1400   -477   2151       C\\nATOM   1802  C   ALA A1063      39.112   4.459  35.526  1.00 88.99           C\\nANISOU 1802  C   ALA A1063    11790  10309  11715  -1259   -345   2190       C\\nATOM   1803  O   ALA A1063      39.030   3.242  35.325  1.00 88.77           O\\nANISOU 1803  O   ALA A1063    11692  10524  11512  -1068    -60   2120       O\\nATOM   1804  CB  ALA A1063      39.719   4.914  37.909  1.00 84.46           C\\nANISOU 1804  CB  ALA A1063    10850   9716  11524  -1112   -751   1850       C\\nATOM   1805  N   GLU A1064      38.283   5.337  34.957  1.00 91.39           N\\nANISOU 1805  N   GLU A1064    12438  10307  11980  -1346   -590   2294       N\\nATOM   1806  CA  GLU A1064      37.273   4.882  34.009  1.00 91.30           C\\nANISOU 1806  CA  GLU A1064    12709  10296  11686  -1243   -529   2345       C\\nATOM   1807  C   GLU A1064      37.898   4.478  32.678  1.00 95.38           C\\nANISOU 1807  C   GLU A1064    13297  11022  11922  -1504   -156   2596       C\\nATOM   1808  O   GLU A1064      37.402   3.560  32.016  1.00 93.85           O\\nANISOU 1808  O   GLU A1064    13219  10996  11445  -1384     47   2550       O\\nATOM   1809  CB  GLU A1064      36.216   5.969  33.805  1.00 88.36           C\\nANISOU 1809  CB  GLU A1064    12660   9522  11391  -1222   -972   2387       C\\nATOM   1810  CG  GLU A1064      34.995   5.506  33.022  1.00 85.95           C\\nANISOU 1810  CG  GLU A1064    12598   9220  10839  -1054  -1023   2379       C\\nATOM   1811  CD  GLU A1064      33.877   6.532  33.012  1.00 92.64           C\\nANISOU 1811  CD  GLU A1064    13676   9668  11857   -926  -1527   2353       C\\nATOM   1812  OE1 GLU A1064      32.798   6.224  32.460  1.00 92.14           O\\nANISOU 1812  OE1 GLU A1064    13758   9602  11649   -763  -1648   2318       O\\nATOM   1813  OE2 GLU A1064      34.072   7.641  33.555  1.00 96.90           O\\nANISOU 1813  OE2 GLU A1064    14234   9879  12704   -975  -1826   2343       O\\nATOM   1814  N   LYS A1065      38.982   5.144  32.270  1.00 96.04           N\\nANISOU 1814  N   LYS A1065    13309  11119  12064  -1890    -43   2837       N\\nATOM   1815  CA  LYS A1065      39.706   4.695  31.086  1.00 95.76           C\\nANISOU 1815  CA  LYS A1065    13269  11382  11732  -2158    412   3024       C\\nATOM   1816  C   LYS A1065      40.338   3.328  31.321  1.00 92.50           C\\nANISOU 1816  C   LYS A1065    12480  11360  11306  -1927    838   2784       C\\nATOM   1817  O   LYS A1065      40.296   2.460  30.442  1.00 93.15           O\\nANISOU 1817  O   LYS A1065    12640  11673  11077  -1892   1185   2745       O\\nATOM   1818  CB  LYS A1065      40.767   5.724  30.695  1.00 97.00           C\\nANISOU 1818  CB  LYS A1065    13372  11502  11982  -2673    474   3332       C\\nATOM   1819  N   LEU A1066      40.918   3.114  32.505  1.00 86.38           N\\nANISOU 1819  N   LEU A1066    11317  10638  10865  -1755    781   2609       N\\nATOM   1820  CA  LEU A1066      41.504   1.814  32.815  1.00 89.95           C\\nANISOU 1820  CA  LEU A1066    11422  11389  11367  -1482   1095   2400       C\\nATOM   1821  C   LEU A1066      40.439   0.729  32.871  1.00 88.33           C\\nANISOU 1821  C   LEU A1066    11426  11159  10977  -1113   1097   2208       C\\nATOM   1822  O   LEU A1066      40.672  -0.401  32.428  1.00 91.55           O\\nANISOU 1822  O   LEU A1066    11755  11759  11269   -957   1433   2085       O\\nATOM   1823  CB  LEU A1066      42.265   1.875  34.139  1.00 96.43           C\\nANISOU 1823  CB  LEU A1066    11833  12240  12567  -1373    917   2292       C\\nATOM   1824  CG  LEU A1066      43.442   2.845  34.220  1.00110.23           C\\nANISOU 1824  CG  LEU A1066    13274  14038  14572  -1754    899   2439       C\\nATOM   1825  CD1 LEU A1066      44.173   2.679  35.543  1.00109.37           C\\nANISOU 1825  CD1 LEU A1066    12741  14009  14807  -1592    693   2287       C\\nATOM   1826  CD2 LEU A1066      44.392   2.653  33.043  1.00117.21           C\\nANISOU 1826  CD2 LEU A1066    13951  15231  15353  -2035   1407   2560       C\\nATOM   1827  N   PHE A1067      39.266   1.055  33.417  1.00 88.20           N\\nANISOU 1827  N   PHE A1067    11656  10901  10956   -977    731   2152       N\\nATOM   1828  CA  PHE A1067      38.202   0.064  33.527  1.00 86.10           C\\nANISOU 1828  CA  PHE A1067    11554  10620  10539   -687    725   1975       C\\nATOM   1829  C   PHE A1067      37.743  -0.409  32.155  1.00 85.87           C\\nANISOU 1829  C   PHE A1067    11803  10657  10168   -762    941   2008       C\\nATOM   1830  O   PHE A1067      37.513  -1.606  31.949  1.00 84.89           O\\nANISOU 1830  O   PHE A1067    11703  10627   9925   -580   1146   1847       O\\nATOM   1831  CB  PHE A1067      37.028   0.640  34.316  1.00 89.23           C\\nANISOU 1831  CB  PHE A1067    12101  10796  11006   -569    323   1888       C\\nATOM   1832  CG  PHE A1067      35.849  -0.282  34.400  1.00 87.05           C\\nANISOU 1832  CG  PHE A1067    11964  10525  10586   -347    317   1719       C\\nATOM   1833  CD1 PHE A1067      35.865  -1.372  35.252  1.00 83.17           C\\nANISOU 1833  CD1 PHE A1067    11332  10130  10137   -136    418   1574       C\\nATOM   1834  CD2 PHE A1067      34.724  -0.058  33.627  1.00 86.11           C\\nANISOU 1834  CD2 PHE A1067    12115  10304  10299   -373    179   1726       C\\nATOM   1835  CE1 PHE A1067      34.781  -2.221  35.329  1.00 78.20           C\\nANISOU 1835  CE1 PHE A1067    10832   9493   9387     -3    424   1440       C\\nATOM   1836  CE2 PHE A1067      33.638  -0.903  33.702  1.00 81.95           C\\nANISOU 1836  CE2 PHE A1067    11664   9800   9671   -214    168   1558       C\\nATOM   1837  CZ  PHE A1067      33.666  -1.985  34.553  1.00 78.15           C\\nANISOU 1837  CZ  PHE A1067    11043   9414   9235    -52    312   1415       C\\nATOM   1838  N   ASN A1068      37.604   0.516  31.201  1.00 90.24           N\\nANISOU 1838  N   ASN A1068    12604  11140  10543  -1046    869   2222       N\\nATOM   1839  CA  ASN A1068      37.203   0.127  29.853  1.00 83.46           C\\nANISOU 1839  CA  ASN A1068    12053  10378   9278  -1159   1045   2269       C\\nATOM   1840  C   ASN A1068      38.222  -0.816  29.228  1.00 82.78           C\\nANISOU 1840  C   ASN A1068    11803  10602   9046  -1191   1575   2173       C\\nATOM   1841  O   ASN A1068      37.856  -1.728  28.479  1.00 84.94           O\\nANISOU 1841  O   ASN A1068    12255  10985   9033  -1118   1777   2024       O\\nATOM   1842  CB  ASN A1068      37.008   1.367  28.984  1.00 87.76           C\\nANISOU 1842  CB  ASN A1068    12920  10786   9638  -1498    837   2587       C\\nATOM   1843  CG  ASN A1068      35.631   1.982  29.145  1.00 95.27           C\\nANISOU 1843  CG  ASN A1068    14135  11430  10632  -1379    315   2609       C\\nATOM   1844  OD1 ASN A1068      34.845   2.027  28.198  1.00102.99           O\\nANISOU 1844  OD1 ASN A1068    15454  12372  11305  -1446    169   2702       O\\nATOM   1845  ND2 ASN A1068      35.327   2.448  30.350  1.00 94.72           N\\nANISOU 1845  ND2 ASN A1068    13890  11159  10939  -1190     20   2495       N\\nATOM   1846  N   GLN A1069      39.507  -0.618  29.532  1.00 82.90           N\\nANISOU 1846  N   GLN A1069    11450  10766   9281  -1289   1799   2217       N\\nATOM   1847  CA  GLN A1069      40.533  -1.532  29.041  1.00 93.96           C\\nANISOU 1847  CA  GLN A1069    12588  12479  10633  -1250   2317   2059       C\\nATOM   1848  C   GLN A1069      40.355  -2.926  29.631  1.00 96.67           C\\nANISOU 1848  C   GLN A1069    12801  12800  11129   -811   2383   1749       C\\nATOM   1849  O   GLN A1069      40.472  -3.931  28.918  1.00 96.30           O\\nANISOU 1849  O   GLN A1069    12800  12887  10901   -697   2721   1539       O\\nATOM   1850  CB  GLN A1069      41.922  -0.978  29.364  1.00104.31           C\\nANISOU 1850  CB  GLN A1069    13439  13961  12234  -1436   2488   2158       C\\nATOM   1851  CG  GLN A1069      42.191   0.399  28.770  1.00112.15           C\\nANISOU 1851  CG  GLN A1069    14573  14942  13096  -1947   2442   2503       C\\nATOM   1852  CD  GLN A1069      43.505   1.002  29.237  1.00116.78           C\\nANISOU 1852  CD  GLN A1069    14664  15667  14039  -2175   2548   2595       C\\nATOM   1853  OE1 GLN A1069      44.350   0.314  29.812  1.00124.86           O\\nANISOU 1853  OE1 GLN A1069    15191  16882  15370  -1946   2730   2385       O\\nATOM   1854  NE2 GLN A1069      43.681   2.297  28.993  1.00109.98           N\\nANISOU 1854  NE2 GLN A1069    13937  14684  13167  -2636   2395   2919       N\\nATOM   1855  N   ASP A1070      40.068  -3.007  30.934  1.00 93.20           N\\nANISOU 1855  N   ASP A1070    12231  12176  11004   -577   2056   1715       N\\nATOM   1856  CA  ASP A1070      39.831  -4.304  31.560  1.00 92.78           C\\nANISOU 1856  CA  ASP A1070    12121  12049  11083   -206   2064   1494       C\\nATOM   1857  C   ASP A1070      38.580  -4.968  31.000  1.00 84.10           C\\nANISOU 1857  C   ASP A1070    11427  10832   9697   -148   2030   1376       C\\nATOM   1858  O   ASP A1070      38.532  -6.195  30.858  1.00 74.28           O\\nANISOU 1858  O   ASP A1070    10218   9558   8448     64   2204   1167       O\\nATOM   1859  CB  ASP A1070      39.714  -4.145  33.076  1.00 97.16           C\\nANISOU 1859  CB  ASP A1070    12517  12464  11936    -46   1705   1529       C\\nATOM   1860  CG  ASP A1070      40.993  -3.637  33.711  1.00101.50           C\\nANISOU 1860  CG  ASP A1070    12635  13134  12794    -83   1688   1606       C\\nATOM   1861  OD1 ASP A1070      42.082  -3.940  33.181  1.00105.37           O\\nANISOU 1861  OD1 ASP A1070    12832  13826  13379    -89   2015   1558       O\\nATOM   1862  OD2 ASP A1070      40.905  -2.936  34.743  1.00 98.07           O\\nANISOU 1862  OD2 ASP A1070    12136  12614  12514   -110   1349   1680       O\\nATOM   1863  N   VAL A1071      37.557  -4.174  30.679  1.00 85.78           N\\nANISOU 1863  N   VAL A1071    11939  10950   9704   -328   1771   1495       N\\nATOM   1864  CA  VAL A1071      36.322  -4.733  30.136  1.00 82.23           C\\nANISOU 1864  CA  VAL A1071    11829  10413   9002   -301   1681   1379       C\\nATOM   1865  C   VAL A1071      36.565  -5.310  28.749  1.00 86.97           C\\nANISOU 1865  C   VAL A1071    12623  11169   9251   -401   2023   1266       C\\nATOM   1866  O   VAL A1071      36.169  -6.443  28.455  1.00 91.66           O\\nANISOU 1866  O   VAL A1071    13352  11723   9752   -267   2137   1029       O\\nATOM   1867  CB  VAL A1071      35.214  -3.667  30.113  1.00 77.64           C\\nANISOU 1867  CB  VAL A1071    11459   9702   8338   -435   1276   1525       C\\nATOM   1868  CG1 VAL A1071      34.018  -4.169  29.323  1.00 68.20           C\\nANISOU 1868  CG1 VAL A1071    10579   8473   6862   -455   1173   1415       C\\nATOM   1869  CG2 VAL A1071      34.807  -3.308  31.524  1.00 79.71           C\\nANISOU 1869  CG2 VAL A1071    11544   9829   8913   -289    982   1517       C\\nATOM   1870  N   ASP A1072      37.208  -4.533  27.872  1.00 86.89           N\\nANISOU 1870  N   ASP A1072    12656  11340   9019   -672   2197   1425       N\\nATOM   1871  CA  ASP A1072      37.548  -5.045  26.549  1.00 93.69           C\\nANISOU 1871  CA  ASP A1072    13699  12426   9474   -799   2587   1294       C\\nATOM   1872  C   ASP A1072      38.419  -6.289  26.649  1.00 93.29           C\\nANISOU 1872  C   ASP A1072    13380  12470   9598   -530   3002    969       C\\nATOM   1873  O   ASP A1072      38.186  -7.273  25.940  1.00100.45           O\\nANISOU 1873  O   ASP A1072    14485  13404  10277   -445   3208    683       O\\nATOM   1874  CB  ASP A1072      38.246  -3.964  25.724  1.00101.72           C\\nANISOU 1874  CB  ASP A1072    14764  13660  10224  -1186   2755   1563       C\\nATOM   1875  CG  ASP A1072      37.274  -2.951  25.152  1.00105.64           C\\nANISOU 1875  CG  ASP A1072    15691  14039  10407  -1457   2355   1858       C\\nATOM   1876  OD1 ASP A1072      36.104  -3.321  24.911  1.00105.43           O\\nANISOU 1876  OD1 ASP A1072    15959  13888  10212  -1367   2080   1761       O\\nATOM   1877  OD2 ASP A1072      37.677  -1.787  24.942  1.00108.66           O\\nANISOU 1877  OD2 ASP A1072    16112  14434  10740  -1764   2286   2192       O\\nATOM   1878  N   ALA A1073      39.417  -6.269  27.537  1.00 84.98           N\\nANISOU 1878  N   ALA A1073    11874  11440   8973   -376   3089    988       N\\nATOM   1879  CA  ALA A1073      40.250  -7.451  27.738  1.00 87.42           C\\nANISOU 1879  CA  ALA A1073    11887  11783   9546    -46   3401    685       C\\nATOM   1880  C   ALA A1073      39.418  -8.640  28.199  1.00 88.42           C\\nANISOU 1880  C   ALA A1073    12207  11603   9787    254   3220    480       C\\nATOM   1881  O   ALA A1073      39.645  -9.774  27.760  1.00 91.45           O\\nANISOU 1881  O   ALA A1073    12623  11947  10175    465   3482    159       O\\nATOM   1882  CB  ALA A1073      41.357  -7.149  28.747  1.00 88.38           C\\nANISOU 1882  CB  ALA A1073    11477  11958  10146     77   3385    785       C\\nATOM   1883  N   ALA A1074      38.441  -8.397  29.079  1.00 83.01           N\\nANISOU 1883  N   ALA A1074    11651  10689   9199    259   2785    645       N\\nATOM   1884  CA  ALA A1074      37.590  -9.476  29.567  1.00 85.44           C\\nANISOU 1884  CA  ALA A1074    12143  10714   9605    456   2615    500       C\\nATOM   1885  C   ALA A1074      36.749 -10.084  28.454  1.00 93.89           C\\nANISOU 1885  C   ALA A1074    13614  11749  10313    356   2695    279       C\\nATOM   1886  O   ALA A1074      36.388 -11.263  28.528  1.00 97.64           O\\nANISOU 1886  O   ALA A1074    14228  11998  10874    520   2705     57       O\\nATOM   1887  CB  ALA A1074      36.686  -8.968  30.689  1.00 78.28           C\\nANISOU 1887  CB  ALA A1074    11263   9662   8819    417   2191    709       C\\nATOM   1888  N   VAL A1075      36.430  -9.305  27.419  1.00 95.22           N\\nANISOU 1888  N   VAL A1075    13998  12114  10069     70   2718    348       N\\nATOM   1889  CA  VAL A1075      35.614  -9.821  26.325  1.00 92.66           C\\nANISOU 1889  CA  VAL A1075    14075  11790   9341    -54   2737    139       C\\nATOM   1890  C   VAL A1075      36.457 -10.646  25.357  1.00100.97           C\\nANISOU 1890  C   VAL A1075    15170  12983  10213     22   3217   -207       C\\nATOM   1891  O   VAL A1075      35.987 -11.658  24.824  1.00101.40           O\\nANISOU 1891  O   VAL A1075    15489  12912  10125     79   3272   -531       O\\nATOM   1892  CB  VAL A1075      34.888  -8.661  25.617  1.00 82.73           C\\nANISOU 1892  CB  VAL A1075    13071  10672   7689   -380   2491    377       C\\nATOM   1893  CG1 VAL A1075      34.069  -9.171  24.446  1.00 75.94           C\\nANISOU 1893  CG1 VAL A1075    12635   9852   6368   -528   2457    166       C\\nATOM   1894  CG2 VAL A1075      33.993  -7.930  26.604  1.00 76.88           C\\nANISOU 1894  CG2 VAL A1075    12256   9765   7192   -384   2023    620       C\\nATOM   1895  N   ARG A1076      37.712 -10.240  25.115  1.00100.09           N\\nANISOU 1895  N   ARG A1076    14776  13139  10116     17   3583   -182       N\\nATOM   1896  CA  ARG A1076      38.592 -11.049  24.273  1.00106.02           C\\nANISOU 1896  CA  ARG A1076    15475  14062  10744    139   4103   -579       C\\nATOM   1897  C   ARG A1076      38.740 -12.458  24.828  1.00110.21           C\\nANISOU 1897  C   ARG A1076    15911  14258  11706    564   4141   -922       C\\nATOM   1898  O   ARG A1076      38.867 -13.421  24.062  1.00118.72           O\\nANISOU 1898  O   ARG A1076    17153  15310  12647    690   4425  -1359       O\\nATOM   1899  CB  ARG A1076      39.980 -10.411  24.143  1.00109.75           C\\nANISOU 1899  CB  ARG A1076    15519  14893  11289     84   4503   -500       C\\nATOM   1900  CG  ARG A1076      40.027  -8.904  24.227  1.00109.02           C\\nANISOU 1900  CG  ARG A1076    15378  14979  11066   -286   4338    -22       C\\nATOM   1901  CD  ARG A1076      39.706  -8.229  22.910  1.00113.54           C\\nANISOU 1901  CD  ARG A1076    16360  15831  10947   -724   4457     91       C\\nATOM   1902  NE  ARG A1076      39.657  -6.778  23.063  1.00113.48           N\\nANISOU 1902  NE  ARG A1076    16365  15872  10879  -1069   4203    591       N\\nATOM   1903  CZ  ARG A1076      39.507  -5.923  22.058  1.00114.12           C\\nANISOU 1903  CZ  ARG A1076    16787  16166  10409  -1503   4233    842       C\\nATOM   1904  NH1 ARG A1076      39.395  -6.367  20.812  1.00118.70           N\\nANISOU 1904  NH1 ARG A1076    17722  16997  10383  -1663   4528    629       N\\nATOM   1905  NH2 ARG A1076      39.471  -4.619  22.301  1.00110.17           N\\nANISOU 1905  NH2 ARG A1076    16305  15605   9949  -1786   3945   1307       N\\nATOM   1906  N   GLY A1077      38.727 -12.597  26.152  1.00104.33           N\\nANISOU 1906  N   GLY A1077    14938  13235  11468    780   3843   -732       N\\nATOM   1907  CA  GLY A1077      38.862 -13.893  26.781  1.00103.24           C\\nANISOU 1907  CA  GLY A1077    14749  12715  11761   1164   3801   -960       C\\nATOM   1908  C   GLY A1077      37.555 -14.652  26.832  1.00100.52           C\\nANISOU 1908  C   GLY A1077    14844  12012  11338   1106   3509  -1046       C\\nATOM   1909  O   GLY A1077      37.538 -15.875  26.663  1.00104.59           O\\nANISOU 1909  O   GLY A1077    15516  12220  12003   1321   3586  -1382       O\\nATOM   1910  N   ILE A1078      36.453 -13.936  27.070  1.00 99.32           N\\nANISOU 1910  N   ILE A1078    14869  11880  10988    814   3165   -762       N\\nATOM   1911  CA  ILE A1078      35.138 -14.573  27.087  1.00 95.36           C\\nANISOU 1911  CA  ILE A1078    14721  11103  10410    692   2887   -841       C\\nATOM   1912  C   ILE A1078      34.872 -15.266  25.758  1.00 94.23           C\\nANISOU 1912  C   ILE A1078    14931  10962   9909    611   3076  -1259       C\\nATOM   1913  O   ILE A1078      34.461 -16.432  25.713  1.00 91.07           O\\nANISOU 1913  O   ILE A1078    14757  10213   9633    693   3032  -1537       O\\nATOM   1914  CB  ILE A1078      34.042 -13.542  27.412  1.00 93.90           C\\nANISOU 1914  CB  ILE A1078    14585  11030  10063    404   2522   -518       C\\nATOM   1915  CG1 ILE A1078      33.993 -13.263  28.917  1.00 93.60           C\\nANISOU 1915  CG1 ILE A1078    14291  10873  10400    497   2289   -213       C\\nATOM   1916  CG2 ILE A1078      32.692 -14.024  26.911  1.00 91.88           C\\nANISOU 1916  CG2 ILE A1078    14674  10646   9590    192   2300   -673       C\\nATOM   1917  CD1 ILE A1078      33.002 -12.183  29.313  1.00 86.14           C\\nANISOU 1917  CD1 ILE A1078    13326  10053   9351    273   1966     41       C\\nATOM   1918  N   LEU A1079      35.121 -14.560  24.654  1.00 96.21           N\\nANISOU 1918  N   LEU A1079    15266  11598   9690    421   3283  -1311       N\\nATOM   1919  CA  LEU A1079      34.910 -15.148  23.339  1.00 99.06           C\\nANISOU 1919  CA  LEU A1079    15997  12035   9608    315   3475  -1730       C\\nATOM   1920  C   LEU A1079      35.911 -16.261  23.058  1.00104.43           C\\nANISOU 1920  C   LEU A1079    16609  12586  10483    653   3898  -2204       C\\nATOM   1921  O   LEU A1079      35.576 -17.237  22.375  1.00107.18           O\\nANISOU 1921  O   LEU A1079    17287  12752  10686    675   3966  -2650       O\\nATOM   1922  CB  LEU A1079      34.990 -14.061  22.271  1.00 97.08           C\\nANISOU 1922  CB  LEU A1079    15879  12261   8747     -2   3592  -1606       C\\nATOM   1923  CG  LEU A1079      34.022 -12.896  22.494  1.00 92.62           C\\nANISOU 1923  CG  LEU A1079    15381  11775   8035   -286   3126  -1146       C\\nATOM   1924  CD1 LEU A1079      34.208 -11.832  21.427  1.00 87.85           C\\nANISOU 1924  CD1 LEU A1079    14956  11583   6838   -599   3216   -967       C\\nATOM   1925  CD2 LEU A1079      32.586 -13.395  22.521  1.00 89.61           C\\nANISOU 1925  CD2 LEU A1079    15271  11148   7628   -399   2691  -1233       C\\nATOM   1926  N   ARG A1080      37.134 -16.141  23.574  1.00102.78           N\\nANISOU 1926  N   ARG A1080    15961  12455  10635    932   4161  -2150       N\\nATOM   1927  CA  ARG A1080      38.113 -17.215  23.463  1.00106.42           C\\nANISOU 1927  CA  ARG A1080    16265  12749  11422   1346   4516  -2607       C\\nATOM   1928  C   ARG A1080      37.864 -18.345  24.454  1.00114.00           C\\nANISOU 1928  C   ARG A1080    17260  13084  12971   1658   4225  -2653       C\\nATOM   1929  O   ARG A1080      38.585 -19.348  24.417  1.00121.35           O\\nANISOU 1929  O   ARG A1080    18104  13749  14255   2055   4430  -3041       O\\nATOM   1930  CB  ARG A1080      39.528 -16.662  23.652  1.00 95.46           C\\nANISOU 1930  CB  ARG A1080    14320  11699  10249   1534   4874  -2535       C\\nATOM   1931  N   ASN A1081      36.877 -18.203  25.339  1.00113.30           N\\nANISOU 1931  N   ASN A1081    17292  12754  13003   1487   3760  -2268       N\\nATOM   1932  CA  ASN A1081      36.488 -19.263  26.264  1.00110.82           C\\nANISOU 1932  CA  ASN A1081    17098  11850  13160   1666   3466  -2242       C\\nATOM   1933  C   ASN A1081      35.348 -20.052  25.630  1.00107.85           C\\nANISOU 1933  C   ASN A1081    17225  11189  12565   1437   3324  -2533       C\\nATOM   1934  O   ASN A1081      34.255 -19.516  25.418  1.00 96.74           O\\nANISOU 1934  O   ASN A1081    16004   9943  10809   1044   3098  -2372       O\\nATOM   1935  CB  ASN A1081      36.075 -18.682  27.614  1.00104.89           C\\nANISOU 1935  CB  ASN A1081    16179  11052  12621   1564   3094  -1681       C\\nATOM   1936  CG  ASN A1081      35.935 -19.745  28.696  1.00100.82           C\\nANISOU 1936  CG  ASN A1081    15751   9964  12593   1757   2830  -1573       C\\nATOM   1937  OD1 ASN A1081      35.536 -20.881  28.430  1.00 96.54           O\\nANISOU 1937  OD1 ASN A1081    15540   8975  12166   1793   2783  -1851       O\\nATOM   1938  ND2 ASN A1081      36.265 -19.375  29.927  1.00 99.41           N\\nANISOU 1938  ND2 ASN A1081    15308   9782  12683   1855   2634  -1158       N\\nATOM   1939  N   ALA A1082      35.603 -21.330  25.335  1.00104.72           N\\nANISOU 1939  N   ALA A1082    17030  10346  12412   1693   3425  -2982       N\\nATOM   1940  CA  ALA A1082      34.620 -22.148  24.633  1.00104.56           C\\nANISOU 1940  CA  ALA A1082    17500  10033  12195   1466   3305  -3342       C\\nATOM   1941  C   ALA A1082      33.348 -22.360  25.442  1.00101.54           C\\nANISOU 1941  C   ALA A1082    17302   9334  11945   1142   2845  -3001       C\\nATOM   1942  O   ALA A1082      32.300 -22.654  24.856  1.00101.98           O\\nANISOU 1942  O   ALA A1082    17693   9314  11739    801   2679  -3190       O\\nATOM   1943  CB  ALA A1082      35.231 -23.499  24.264  1.00107.82           C\\nANISOU 1943  CB  ALA A1082    18086   9944  12935   1850   3489  -3914       C\\nATOM   1944  N   LYS A1083      33.409 -22.219  26.764  1.00105.02           N\\nANISOU 1944  N   LYS A1083    17519   9623  12760   1215   2642  -2520       N\\nATOM   1945  CA  LYS A1083      32.243 -22.435  27.607  1.00 99.72           C\\nANISOU 1945  CA  LYS A1083    16986   8701  12202    885   2273  -2194       C\\nATOM   1946  C   LYS A1083      31.446 -21.163  27.871  1.00 97.98           C\\nANISOU 1946  C   LYS A1083    16574   8985  11668    541   2119  -1821       C\\nATOM   1947  O   LYS A1083      30.317 -21.253  28.366  1.00 96.09           O\\nANISOU 1947  O   LYS A1083    16414   8652  11442    209   1857  -1636       O\\nATOM   1948  CB  LYS A1083      32.666 -23.061  28.941  1.00 98.15           C\\nANISOU 1948  CB  LYS A1083    16717   8046  12528   1114   2120  -1873       C\\nATOM   1949  N   LEU A1084      31.992 -19.986  27.551  1.00 99.46           N\\nANISOU 1949  N   LEU A1084    16502   9689  11600    605   2275  -1719       N\\nATOM   1950  CA  LEU A1084      31.288 -18.729  27.771  1.00 97.55           C\\nANISOU 1950  CA  LEU A1084    16090   9867  11109    333   2100  -1390       C\\nATOM   1951  C   LEU A1084      30.919 -17.993  26.491  1.00101.44           C\\nANISOU 1951  C   LEU A1084    16699  10753  11090    121   2131  -1554       C\\nATOM   1952  O   LEU A1084      30.009 -17.161  26.521  1.00102.09           O\\nANISOU 1952  O   LEU A1084    16730  11072  10987   -136   1884  -1351       O\\nATOM   1953  CB  LEU A1084      32.124 -17.790  28.654  1.00 93.67           C\\nANISOU 1953  CB  LEU A1084    15216   9609  10766    522   2147  -1024       C\\nATOM   1954  CG  LEU A1084      32.376 -18.250  30.092  1.00 99.39           C\\nANISOU 1954  CG  LEU A1084    15814  10040  11911    678   2020   -744       C\\nATOM   1955  CD1 LEU A1084      33.068 -17.160  30.896  1.00100.96           C\\nANISOU 1955  CD1 LEU A1084    15645  10540  12174    797   2010   -411       C\\nATOM   1956  CD2 LEU A1084      31.075 -18.668  30.757  1.00 98.30           C\\nANISOU 1956  CD2 LEU A1084    15830   9700  11820    371   1756   -602       C\\nATOM   1957  N   LYS A1085      31.598 -18.269  25.378  1.00102.45           N\\nANISOU 1957  N   LYS A1085    16983  10965  10978    227   2417  -1917       N\\nATOM   1958  CA  LYS A1085      31.262 -17.597  24.126  1.00 99.55           C\\nANISOU 1958  CA  LYS A1085    16799  10990  10037    -13   2431  -2041       C\\nATOM   1959  C   LYS A1085      29.850 -17.899  23.627  1.00 99.81           C\\nANISOU 1959  C   LYS A1085    17128  10950   9847   -354   2083  -2182       C\\nATOM   1960  O   LYS A1085      29.193 -16.966  23.138  1.00 92.79           O\\nANISOU 1960  O   LYS A1085    16268  10388   8598   -594   1861  -2023       O\\nATOM   1961  CB  LYS A1085      32.301 -17.947  23.053  1.00 96.22           C\\nANISOU 1961  CB  LYS A1085    16501  10703   9355    149   2870  -2453       C\\nATOM   1962  N   PRO A1086      29.335 -19.137  23.693  1.00105.32           N\\nANISOU 1962  N   PRO A1086    18044  11220  10751   -402   1987  -2468       N\\nATOM   1963  CA  PRO A1086      27.961 -19.366  23.201  1.00106.72           C\\nANISOU 1963  CA  PRO A1086    18449  11373  10729   -778   1625  -2606       C\\nATOM   1964  C   PRO A1086      26.904 -18.527  23.902  1.00101.72           C\\nANISOU 1964  C   PRO A1086    17551  10915  10184  -1000   1260  -2201       C\\nATOM   1965  O   PRO A1086      26.130 -17.830  23.232  1.00 97.88           O\\nANISOU 1965  O   PRO A1086    17104  10733   9353  -1226    992  -2175       O\\nATOM   1966  CB  PRO A1086      27.759 -20.868  23.445  1.00108.18           C\\nANISOU 1966  CB  PRO A1086    18857  10979  11267   -780   1611  -2917       C\\nATOM   1967  CG  PRO A1086      29.125 -21.438  23.364  1.00108.60           C\\nANISOU 1967  CG  PRO A1086    18951  10834  11479   -369   2012  -3150       C\\nATOM   1968  CD  PRO A1086      30.018 -20.411  23.991  1.00103.81           C\\nANISOU 1968  CD  PRO A1086    17951  10542  10950   -127   2192  -2744       C\\nATOM   1969  N   VAL A1087      26.844 -18.575  25.235  1.00 98.45           N\\nANISOU 1969  N   VAL A1087    16867  10324  10214   -932   1231  -1899       N\\nATOM   1970  CA  VAL A1087      25.825 -17.817  25.956  1.00 96.16           C\\nANISOU 1970  CA  VAL A1087    16290  10223  10024  -1125    937  -1588       C\\nATOM   1971  C   VAL A1087      26.024 -16.321  25.749  1.00 94.05           C\\nANISOU 1971  C   VAL A1087    15830  10386   9517  -1049    881  -1337       C\\nATOM   1972  O   VAL A1087      25.055 -15.564  25.617  1.00 93.16           O\\nANISOU 1972  O   VAL A1087    15592  10501   9302  -1221    565  -1236       O\\nATOM   1973  CB  VAL A1087      25.834 -18.196  27.449  1.00 97.74           C\\nANISOU 1973  CB  VAL A1087    16281  10182  10673  -1078    978  -1328       C\\nATOM   1974  CG1 VAL A1087      27.238 -18.088  28.024  1.00102.40           C\\nANISOU 1974  CG1 VAL A1087    16780  10706  11420   -706   1259  -1166       C\\nATOM   1975  CG2 VAL A1087      24.863 -17.323  28.230  1.00 89.97           C\\nANISOU 1975  CG2 VAL A1087    14954   9465   9765  -1245    754  -1058       C\\nATOM   1976  N   TYR A1088      27.284 -15.876  25.692  1.00 89.69           N\\nANISOU 1976  N   TYR A1088    15242   9934   8902   -793   1168  -1242       N\\nATOM   1977  CA  TYR A1088      27.580 -14.457  25.515  1.00 90.57           C\\nANISOU 1977  CA  TYR A1088    15204  10393   8813   -755   1125   -975       C\\nATOM   1978  C   TYR A1088      26.959 -13.916  24.234  1.00 95.61           C\\nANISOU 1978  C   TYR A1088    16073  11277   8976   -968    892  -1053       C\\nATOM   1979  O   TYR A1088      26.470 -12.781  24.202  1.00 93.98           O\\nANISOU 1979  O   TYR A1088    15753  11275   8682  -1035    611   -805       O\\nATOM   1980  CB  TYR A1088      29.095 -14.250  25.512  1.00 93.94           C\\nANISOU 1980  CB  TYR A1088    15566  10885   9242   -509   1510   -919       C\\nATOM   1981  CG  TYR A1088      29.544 -12.810  25.574  1.00 98.44           C\\nANISOU 1981  CG  TYR A1088    15953  11742   9710   -493   1488   -591       C\\nATOM   1982  CD1 TYR A1088      29.740 -12.178  26.794  1.00 98.86           C\\nANISOU 1982  CD1 TYR A1088    15682  11781  10099   -378   1424   -304       C\\nATOM   1983  CD2 TYR A1088      29.792 -12.088  24.415  1.00103.73           C\\nANISOU 1983  CD2 TYR A1088    16808  12681   9923   -622   1523   -565       C\\nATOM   1984  CE1 TYR A1088      30.162 -10.863  26.860  1.00 99.84           C\\nANISOU 1984  CE1 TYR A1088    15661  12107  10167   -380   1378    -29       C\\nATOM   1985  CE2 TYR A1088      30.213 -10.771  24.470  1.00106.12           C\\nANISOU 1985  CE2 TYR A1088    16981  13181  10158   -650   1482   -232       C\\nATOM   1986  CZ  TYR A1088      30.395 -10.164  25.696  1.00103.83           C\\nANISOU 1986  CZ  TYR A1088    16357  12826  10268   -522   1402     20       C\\nATOM   1987  OH  TYR A1088      30.810  -8.854  25.759  1.00103.35           O\\nANISOU 1987  OH  TYR A1088    16189  12904  10176   -568   1333    326       O\\nATOM   1988  N   ASP A1089      26.969 -14.714  23.164  1.00102.12           N\\nANISOU 1988  N   ASP A1089    17248  12069   9485  -1067    973  -1406       N\\nATOM   1989  CA  ASP A1089      26.320 -14.293  21.927  1.00102.51           C\\nANISOU 1989  CA  ASP A1089    17573  12361   9018  -1301    696  -1486       C\\nATOM   1990  C   ASP A1089      24.810 -14.185  22.110  1.00 97.68           C\\nANISOU 1990  C   ASP A1089    16847  11734   8531  -1503    175  -1453       C\\nATOM   1991  O   ASP A1089      24.193 -13.208  21.669  1.00 94.27           O\\nANISOU 1991  O   ASP A1089    16405  11528   7886  -1603   -198  -1266       O\\nATOM   1992  CB  ASP A1089      26.658 -15.270  20.798  1.00107.75           C\\nANISOU 1992  CB  ASP A1089    18652  12996   9292  -1371    911  -1943       C\\nATOM   1993  CG  ASP A1089      28.153 -15.360  20.522  1.00109.36           C\\nANISOU 1993  CG  ASP A1089    18906  13282   9365  -1158   1468  -2039       C\\nATOM   1994  OD1 ASP A1089      28.859 -14.349  20.724  1.00107.83           O\\nANISOU 1994  OD1 ASP A1089    18522  13306   9142  -1077   1610  -1702       O\\nATOM   1995  OD2 ASP A1089      28.623 -16.442  20.104  1.00108.54           O\\nANISOU 1995  OD2 ASP A1089    19006  13016   9217  -1074   1762  -2478       O\\nATOM   1996  N   SER A1090      24.200 -15.124  22.768  1.00 95.52           N\\nANISOU 1996  N   SER A1090    16469  11190   8635  -1571    131  -1622       N\\nATOM   1997  CA  SER A1090      22.775 -15.087  22.914  1.00100.79           C\\nANISOU 1997  CA  SER A1090    16964  11869   9463  -1805   -311  -1652       C\\nATOM   1998  C   SER A1090      22.220 -13.982  23.739  1.00102.57           C\\nANISOU 1998  C   SER A1090    16755  12269   9949  -1733   -541  -1311       C\\nATOM   1999  O   SER A1090      21.034 -13.763  23.747  1.00106.04           O\\nANISOU 1999  O   SER A1090    16983  12810  10497  -1894   -938  -1340       O\\nATOM   2000  CB  SER A1090      22.377 -16.406  23.588  1.00 99.01           C\\nANISOU 2000  CB  SER A1090    16709  11296   9615  -1937   -227  -1860       C\\nATOM   2001  OG  SER A1090      21.208 -16.357  24.395  1.00 95.53           O\\nANISOU 2001  OG  SER A1090    15874  10901   9522  -2092   -478  -1730       O\\nATOM   2002  N   LEU A1091      23.062 -13.325  24.481  1.00 99.87           N\\nANISOU 2002  N   LEU A1091    16250  11965   9730  -1492   -315  -1031       N\\nATOM   2003  CA  LEU A1091      22.607 -12.416  25.517  1.00 95.87           C\\nANISOU 2003  CA  LEU A1091    15324  11551   9550  -1398   -463   -783       C\\nATOM   2004  C   LEU A1091      22.327 -11.026  24.968  1.00 97.76           C\\nANISOU 2004  C   LEU A1091    15525  12007   9612  -1342   -816   -587       C\\nATOM   2005  O   LEU A1091      23.032 -10.535  24.083  1.00 95.64           O\\nANISOU 2005  O   LEU A1091    15549  11818   8971  -1317   -786   -485       O\\nATOM   2006  CB  LEU A1091      23.641 -12.333  26.638  1.00 87.84           C\\nANISOU 2006  CB  LEU A1091    14159  10436   8780  -1181    -92   -597       C\\nATOM   2007  CG  LEU A1091      23.680 -13.560  27.542  1.00 82.06           C\\nANISOU 2007  CG  LEU A1091    13386   9458   8336  -1224    143   -690       C\\nATOM   2008  CD1 LEU A1091      24.786 -13.425  28.573  1.00 80.82           C\\nANISOU 2008  CD1 LEU A1091    13114   9224   8371   -989    440   -482       C\\nATOM   2009  CD2 LEU A1091      22.327 -13.769  28.206  1.00 80.36           C\\nANISOU 2009  CD2 LEU A1091    12890   9277   8367  -1435    -70   -736       C\\nATOM   2010  N   ASP A1092      21.376 -10.343  25.562  1.00 96.05           N\\nANISOU 2010  N   ASP A1092    14944  11880   9672  -1329  -1151   -538       N\\nATOM   2011  CA  ASP A1092      21.052  -8.988  25.248  1.00 94.58           C\\nANISOU 2011  CA  ASP A1092    14656  11809   9469  -1194  -1512   -321       C\\nATOM   2012  C   ASP A1092      22.222  -8.197  25.771  1.00 90.97           C\\nANISOU 2012  C   ASP A1092    14182  11304   9080   -989  -1249    -61       C\\nATOM   2013  O   ASP A1092      22.961  -8.670  26.567  1.00 94.84           O\\nANISOU 2013  O   ASP A1092    14566  11715   9754   -916   -857    -59       O\\nATOM   2014  CB  ASP A1092      19.780  -8.669  26.007  1.00101.30           C\\nANISOU 2014  CB  ASP A1092    15029  12751  10711  -1166  -1868   -406       C\\nATOM   2015  CG  ASP A1092      19.607  -7.210  26.318  1.00111.33           C\\nANISOU 2015  CG  ASP A1092    16080  14045  12176   -914  -2131   -205       C\\nATOM   2016  OD1 ASP A1092      20.277  -6.361  25.708  1.00117.45           O\\nANISOU 2016  OD1 ASP A1092    17125  14798  12702   -861  -2417     -1       O\\nATOM   2017  OD2 ASP A1092      18.756  -6.904  27.171  1.00112.11           O\\nANISOU 2017  OD2 ASP A1092    15757  14174  12666   -784  -2057   -258       O\\nATOM   2018  N   ALA A1093      22.381  -6.966  25.331  1.00 96.88           N\\nANISOU 2018  N   ALA A1093    15054  12081   9674   -916  -1505    178       N\\nATOM   2019  CA  ALA A1093      23.488  -6.122  25.778  1.00 91.46           C\\nANISOU 2019  CA  ALA A1093    14374  11336   9042   -782  -1292    431       C\\nATOM   2020  C   ALA A1093      23.421  -5.832  27.272  1.00 93.10           C\\nANISOU 2020  C   ALA A1093    14165  11492   9718   -603  -1188    414       C\\nATOM   2021  O   ALA A1093      24.464  -5.712  27.927  1.00 87.73           O\\nANISOU 2021  O   ALA A1093    13451  10765   9118   -524   -866    519       O\\nATOM   2022  CB  ALA A1093      23.503  -4.814  24.988  1.00 88.70           C\\nANISOU 2022  CB  ALA A1093    14227  10970   8505   -779  -1676    717       C\\nATOM   2023  N   VAL A1094      22.214  -5.720  27.829  1.00 97.94           N\\nANISOU 2023  N   VAL A1094    14439  12147  10627   -546  -1450    262       N\\nATOM   2024  CA  VAL A1094      22.076  -5.445  29.257  1.00 93.00           C\\nANISOU 2024  CA  VAL A1094    13427  11531  10378   -399  -1324    200       C\\nATOM   2025  C   VAL A1094      22.441  -6.680  30.072  1.00 88.59           C\\nANISOU 2025  C   VAL A1094    12819  10982   9860   -491   -879     98       C\\nATOM   2026  O   VAL A1094      23.204  -6.601  31.041  1.00 83.02           O\\nANISOU 2026  O   VAL A1094    12036  10247   9261   -400   -616    175       O\\nATOM   2027  CB  VAL A1094      20.652  -4.956  29.576  1.00 91.34           C\\nANISOU 2027  CB  VAL A1094    12822  11413  10469   -310  -1694     21       C\\nATOM   2028  CG1 VAL A1094      20.546  -4.549  31.038  1.00 87.18           C\\nANISOU 2028  CG1 VAL A1094    11914  10940  10271   -155  -1529    -81       C\\nATOM   2029  CG2 VAL A1094      20.261  -3.802  28.656  1.00 92.19           C\\nANISOU 2029  CG2 VAL A1094    13027  11445  10557   -192  -2230    148       C\\nATOM   2030  N   ARG A1095      21.898  -7.840  29.694  1.00 90.63           N\\nANISOU 2030  N   ARG A1095    13144  11253  10038   -685   -833    -66       N\\nATOM   2031  CA  ARG A1095      22.284  -9.087  30.344  1.00 90.96           C\\nANISOU 2031  CA  ARG A1095    13231  11214  10116   -790   -456   -122       C\\nATOM   2032  C   ARG A1095      23.746  -9.427  30.091  1.00 87.34           C\\nANISOU 2032  C   ARG A1095    13078  10619   9487   -715   -154      0       C\\nATOM   2033  O   ARG A1095      24.354 -10.144  30.893  1.00 79.42           O\\nANISOU 2033  O   ARG A1095    12074   9515   8587   -689    132     31       O\\nATOM   2034  CB  ARG A1095      21.389 -10.229  29.864  1.00 87.99           C\\nANISOU 2034  CB  ARG A1095    12907  10817   9709  -1046   -517   -333       C\\nATOM   2035  CG  ARG A1095      19.913  -9.890  29.887  1.00 88.08           C\\nANISOU 2035  CG  ARG A1095    12562  11010   9896  -1139   -853   -486       C\\nATOM   2036  CD  ARG A1095      19.099 -10.979  29.236  1.00 93.06           C\\nANISOU 2036  CD  ARG A1095    13265  11616  10479  -1439   -963   -697       C\\nATOM   2037  NE  ARG A1095      17.793 -10.502  28.791  1.00103.22           N\\nANISOU 2037  NE  ARG A1095    14244  13099  11877  -1501  -1404   -846       N\\nATOM   2038  CZ  ARG A1095      16.679 -10.583  29.511  1.00102.98           C\\nANISOU 2038  CZ  ARG A1095    13724  13246  12157  -1620  -1455   -997       C\\nATOM   2039  NH1 ARG A1095      16.705 -11.126  30.720  1.00101.20           N\\nANISOU 2039  NH1 ARG A1095    13324  13034  12095  -1735  -1072   -988       N\\nATOM   2040  NH2 ARG A1095      15.535 -10.122  29.020  1.00102.93           N\\nANISOU 2040  NH2 ARG A1095    13394  13427  12289  -1634  -1897  -1154       N\\nATOM   2041  N   ARG A1096      24.321  -8.920  29.001  1.00 90.45           N\\nANISOU 2041  N   ARG A1096    13718  11024   9623   -685   -218     78       N\\nATOM   2042  CA  ARG A1096      25.730  -9.168  28.728  1.00 86.04           C\\nANISOU 2042  CA  ARG A1096    13368  10402   8921   -614    110    159       C\\nATOM   2043  C   ARG A1096      26.623  -8.481  29.750  1.00 81.52           C\\nANISOU 2043  C   ARG A1096    12598   9829   8548   -445    250    350       C\\nATOM   2044  O   ARG A1096      27.697  -8.997  30.076  1.00 76.37           O\\nANISOU 2044  O   ARG A1096    11967   9110   7940   -359    548    380       O\\nATOM   2045  CB  ARG A1096      26.072  -8.706  27.313  1.00 85.80           C\\nANISOU 2045  CB  ARG A1096    13637  10453   8510   -686     38    205       C\\nATOM   2046  CG  ARG A1096      26.974  -9.657  26.568  1.00 82.89           C\\nANISOU 2046  CG  ARG A1096    13541  10054   7898   -716    389     63       C\\nATOM   2047  CD  ARG A1096      27.247  -9.180  25.159  1.00 85.44           C\\nANISOU 2047  CD  ARG A1096    14183  10531   7750   -844    350    102       C\\nATOM   2048  NE  ARG A1096      26.098  -9.355  24.282  1.00 94.36           N\\nANISOU 2048  NE  ARG A1096    15514  11710   8629  -1018     -6    -32       N\\nATOM   2049  CZ  ARG A1096      26.167  -9.297  22.957  1.00 97.59           C\\nANISOU 2049  CZ  ARG A1096    16291  12257   8531  -1179    -60    -72       C\\nATOM   2050  NH1 ARG A1096      27.333  -9.075  22.369  1.00 93.17           N\\nANISOU 2050  NH1 ARG A1096    15919  11820   7663  -1201    286      6       N\\nATOM   2051  NH2 ARG A1096      25.078  -9.465  22.222  1.00102.27           N\\nANISOU 2051  NH2 ARG A1096    17053  12899   8906  -1338   -456   -197       N\\nATOM   2052  N   ALA A1097      26.196  -7.325  30.270  1.00 83.15           N\\nANISOU 2052  N   ALA A1097    12599  10095   8899   -381     10    450       N\\nATOM   2053  CA  ALA A1097      26.963  -6.656  31.316  1.00 74.83           C\\nANISOU 2053  CA  ALA A1097    11361   9035   8036   -245    100    585       C\\nATOM   2054  C   ALA A1097      26.946  -7.446  32.617  1.00 73.67           C\\nANISOU 2054  C   ALA A1097    11047   8874   8072   -207    277    525       C\\nATOM   2055  O   ALA A1097      27.942  -7.452  33.348  1.00 74.45           O\\nANISOU 2055  O   ALA A1097    11087   8949   8253   -111    442    628       O\\nATOM   2056  CB  ALA A1097      26.423  -5.246  31.550  1.00 63.51           C\\nANISOU 2056  CB  ALA A1097     9778   7621   6732   -175   -226    643       C\\nATOM   2057  N   ALA A1098      25.832  -8.117  32.923  1.00 71.99           N\\nANISOU 2057  N   ALA A1098    10755   8685   7912   -311    230    379       N\\nATOM   2058  CA  ALA A1098      25.774  -8.940  34.125  1.00 74.69           C\\nANISOU 2058  CA  ALA A1098    11001   9011   8365   -346    407    373       C\\nATOM   2059  C   ALA A1098      26.760 -10.098  34.047  1.00 83.58           C\\nANISOU 2059  C   ALA A1098    12344   9949   9462   -326    646    434       C\\nATOM   2060  O   ALA A1098      27.358 -10.485  35.059  1.00 82.43           O\\nANISOU 2060  O   ALA A1098    12168   9750   9403   -262    768    547       O\\nATOM   2061  CB  ALA A1098      24.351  -9.450  34.338  1.00 76.99           C\\nANISOU 2061  CB  ALA A1098    11160   9381   8710   -537    335    213       C\\nATOM   2062  N   LEU A1099      26.946 -10.665  32.852  1.00 86.05           N\\nANISOU 2062  N   LEU A1099    12886  10156   9651   -363    693    343       N\\nATOM   2063  CA  LEU A1099      27.950 -11.710  32.691  1.00 84.37           C\\nANISOU 2063  CA  LEU A1099    12858   9742   9457   -276    922    336       C\\nATOM   2064  C   LEU A1099      29.360 -11.153  32.838  1.00 75.62           C\\nANISOU 2064  C   LEU A1099    11669   8675   8388    -65   1050    473       C\\nATOM   2065  O   LEU A1099      30.242 -11.829  33.380  1.00 59.72           O\\nANISOU 2065  O   LEU A1099     9651   6525   6517     79   1192    528       O\\nATOM   2066  CB  LEU A1099      27.785 -12.397  31.335  1.00 88.81           C\\nANISOU 2066  CB  LEU A1099    13687  10211   9847   -362    961    126       C\\nATOM   2067  CG  LEU A1099      28.635 -13.647  31.091  1.00 89.13           C\\nANISOU 2067  CG  LEU A1099    13929   9988   9947   -253   1195     11       C\\nATOM   2068  CD1 LEU A1099      28.246 -14.750  32.060  1.00 88.78           C\\nANISOU 2068  CD1 LEU A1099    13929   9678  10126   -318   1188     43       C\\nATOM   2069  CD2 LEU A1099      28.496 -14.118  29.655  1.00 91.08           C\\nANISOU 2069  CD2 LEU A1099    14451  10201   9955   -337   1240   -262       C\\nATOM   2070  N   ILE A1100      29.591  -9.928  32.363  1.00 70.27           N\\nANISOU 2070  N   ILE A1100    10921   8168   7612    -56    974    541       N\\nATOM   2071  CA  ILE A1100      30.888  -9.294  32.557  1.00 70.30           C\\nANISOU 2071  CA  ILE A1100    10796   8234   7680     77   1083    680       C\\nATOM   2072  C   ILE A1100      31.120  -9.006  34.034  1.00 76.98           C\\nANISOU 2072  C   ILE A1100    11428   9092   8729    165   1006    808       C\\nATOM   2073  O   ILE A1100      32.244  -9.120  34.537  1.00 80.54           O\\nANISOU 2073  O   ILE A1100    11764   9529   9310    301   1104    897       O\\nATOM   2074  CB  ILE A1100      30.983  -8.022  31.697  1.00 68.88           C\\nANISOU 2074  CB  ILE A1100    10638   8193   7340    -10    989    761       C\\nATOM   2075  CG1 ILE A1100      30.869  -8.386  30.212  1.00 75.73           C\\nANISOU 2075  CG1 ILE A1100    11771   9090   7912   -120   1082    646       C\\nATOM   2076  CG2 ILE A1100      32.279  -7.281  31.978  1.00 63.94           C\\nANISOU 2076  CG2 ILE A1100     9841   7638   6817     56   1090    917       C\\nATOM   2077  CD1 ILE A1100      30.869  -7.196  29.275  1.00 65.67           C\\nANISOU 2077  CD1 ILE A1100    10607   7938   6405   -260    954    784       C\\nATOM   2078  N   ASN A1101      30.057  -8.645  34.757  1.00 76.26           N\\nANISOU 2078  N   ASN A1101    11262   9055   8656     88    828    795       N\\nATOM   2079  CA  ASN A1101      30.161  -8.449  36.200  1.00 71.74           C\\nANISOU 2079  CA  ASN A1101    10532   8535   8191    138    773    876       C\\nATOM   2080  C   ASN A1101      30.619  -9.725  36.896  1.00 69.64           C\\nANISOU 2080  C   ASN A1101    10339   8134   7987    190    891    949       C\\nATOM   2081  O   ASN A1101      31.439  -9.679  37.821  1.00 64.42           O\\nANISOU 2081  O   ASN A1101     9588   7486   7403    297    869   1078       O\\nATOM   2082  CB  ASN A1101      28.811  -7.981  36.750  1.00 72.99           C\\nANISOU 2082  CB  ASN A1101    10589   8814   8330     34    629    774       C\\nATOM   2083  CG  ASN A1101      28.882  -7.542  38.204  1.00 79.76           C\\nANISOU 2083  CG  ASN A1101    11293   9793   9219     68    586    807       C\\nATOM   2084  OD1 ASN A1101      29.385  -8.264  39.065  1.00 88.11           O\\nANISOU 2084  OD1 ASN A1101    12391  10824  10262     80    664    919       O\\nATOM   2085  ND2 ASN A1101      28.363  -6.353  38.484  1.00 77.04           N\\nANISOU 2085  ND2 ASN A1101    10794   9569   8909     92    434    696       N\\nATOM   2086  N   MET A1102      30.111 -10.877  36.452  1.00 67.47           N\\nANISOU 2086  N   MET A1102    10246   7696   7691    110    973    875       N\\nATOM   2087  CA  MET A1102      30.457 -12.137  37.100  1.00 68.00           C\\nANISOU 2087  CA  MET A1102    10442   7546   7851    150   1035    971       C\\nATOM   2088  C   MET A1102      31.900 -12.539  36.815  1.00 75.21           C\\nANISOU 2088  C   MET A1102    11354   8314   8910    407   1126   1011       C\\nATOM   2089  O   MET A1102      32.611 -12.984  37.723  1.00 77.63           O\\nANISOU 2089  O   MET A1102    11635   8519   9341    543   1075   1172       O\\nATOM   2090  CB  MET A1102      29.492 -13.233  36.655  1.00 70.40           C\\nANISOU 2090  CB  MET A1102    10958   7659   8132    -38   1075    861       C\\nATOM   2091  CG  MET A1102      28.072 -13.024  37.150  1.00 76.57           C\\nANISOU 2091  CG  MET A1102    11663   8605   8824   -310   1005    826       C\\nATOM   2092  SD  MET A1102      27.010 -14.445  36.822  1.00 81.97           S\\nANISOU 2092  SD  MET A1102    12572   9042   9532   -608   1039    733       S\\nATOM   2093  CE  MET A1102      27.916 -15.743  37.652  1.00 80.68           C\\nANISOU 2093  CE  MET A1102    12664   8490   9502   -523   1086    972       C\\nATOM   2094  N   VAL A1103      32.352 -12.395  35.565  1.00 79.58           N\\nANISOU 2094  N   VAL A1103    11918   8879   9439    475   1257    861       N\\nATOM   2095  CA  VAL A1103      33.743 -12.721  35.251  1.00 82.54           C\\nANISOU 2095  CA  VAL A1103    12205   9184   9974    728   1400    840       C\\nATOM   2096  C   VAL A1103      34.689 -11.726  35.912  1.00 80.24           C\\nANISOU 2096  C   VAL A1103    11618   9095   9774    826   1331   1000       C\\nATOM   2097  O   VAL A1103      35.848 -12.053  36.198  1.00 82.23           O\\nANISOU 2097  O   VAL A1103    11705   9299  10238   1051   1366   1045       O\\nATOM   2098  CB  VAL A1103      33.969 -12.782  33.727  1.00 84.75           C\\nANISOU 2098  CB  VAL A1103    12570   9500  10133    729   1619    609       C\\nATOM   2099  CG1 VAL A1103      32.942 -13.689  33.066  1.00 85.19           C\\nANISOU 2099  CG1 VAL A1103    12933   9364  10070    590   1631    415       C\\nATOM   2100  CG2 VAL A1103      33.931 -11.394  33.115  1.00 83.71           C\\nANISOU 2100  CG2 VAL A1103    12339   9665   9801    582   1615    646       C\\nATOM   2101  N   PHE A1104      34.222 -10.502  36.163  1.00 72.46           N\\nANISOU 2101  N   PHE A1104    10543   8321   8669    670   1206   1064       N\\nATOM   2102  CA  PHE A1104      35.025  -9.556  36.927  1.00 74.27           C\\nANISOU 2102  CA  PHE A1104    10521   8703   8994    721   1090   1196       C\\nATOM   2103  C   PHE A1104      35.203 -10.013  38.369  1.00 79.15           C\\nANISOU 2103  C   PHE A1104    11108   9268   9696    808    920   1340       C\\nATOM   2104  O   PHE A1104      36.258  -9.779  38.969  1.00 81.90           O\\nANISOU 2104  O   PHE A1104    11250   9676  10191    937    827   1439       O\\nATOM   2105  CB  PHE A1104      34.382  -8.171  36.883  1.00 67.54           C\\nANISOU 2105  CB  PHE A1104     9633   8010   8019    545    959   1195       C\\nATOM   2106  CG  PHE A1104      35.032  -7.234  35.911  1.00 71.68           C\\nANISOU 2106  CG  PHE A1104    10068   8632   8534    483   1036   1205       C\\nATOM   2107  CD1 PHE A1104      34.785  -7.340  34.554  1.00 74.18           C\\nANISOU 2107  CD1 PHE A1104    10546   8950   8690    396   1191   1126       C\\nATOM   2108  CD2 PHE A1104      35.892  -6.243  36.356  1.00 80.86           C\\nANISOU 2108  CD2 PHE A1104    11011   9893   9821    465    944   1303       C\\nATOM   2109  CE1 PHE A1104      35.384  -6.477  33.659  1.00 78.16           C\\nANISOU 2109  CE1 PHE A1104    11011   9565   9121    278   1280   1183       C\\nATOM   2110  CE2 PHE A1104      36.492  -5.376  35.467  1.00 85.63           C\\nANISOU 2110  CE2 PHE A1104    11550  10576  10412    335   1028   1354       C\\nATOM   2111  CZ  PHE A1104      36.238  -5.493  34.115  1.00 81.25           C\\nANISOU 2111  CZ  PHE A1104    11176  10035   9661    234   1209   1314       C\\nATOM   2112  N   GLN A1105      34.192 -10.669  38.935  1.00 80.45           N\\nANISOU 2112  N   GLN A1105    11475   9341   9754    708    866   1365       N\\nATOM   2113  CA  GLN A1105      34.237 -11.118  40.319  1.00 76.17           C\\nANISOU 2113  CA  GLN A1105    10978   8769   9193    723    706   1544       C\\nATOM   2114  C   GLN A1105      34.839 -12.508  40.465  1.00 79.87           C\\nANISOU 2114  C   GLN A1105    11579   8938   9829    899    695   1660       C\\nATOM   2115  O   GLN A1105      35.670 -12.731  41.352  1.00 77.78           O\\nANISOU 2115  O   GLN A1105    11252   8640   9660   1051    517   1841       O\\nATOM   2116  CB  GLN A1105      32.830 -11.107  40.918  1.00 71.88           C\\nANISOU 2116  CB  GLN A1105    10574   8313   8426    472    687   1531       C\\nATOM   2117  CG  GLN A1105      32.752 -11.692  42.313  1.00 71.95           C\\nANISOU 2117  CG  GLN A1105    10707   8315   8315    408    569   1741       C\\nATOM   2118  CD  GLN A1105      31.379 -11.534  42.928  1.00 72.70           C\\nANISOU 2118  CD  GLN A1105    10864   8598   8159    121    622   1689       C\\nATOM   2119  OE1 GLN A1105      30.414 -11.193  42.241  1.00 76.06           O\\nANISOU 2119  OE1 GLN A1105    11232   9099   8567     -1    727   1488       O\\nATOM   2120  NE2 GLN A1105      31.282 -11.777  44.230  1.00 68.30           N\\nANISOU 2120  NE2 GLN A1105    10410   8146   7396      7    545   1865       N\\nATOM   2121  N   MET A1106      34.433 -13.446  39.607  1.00 80.28           N\\nANISOU 2121  N   MET A1106    11826   8743   9934    892    842   1548       N\\nATOM   2122  CA  MET A1106      34.803 -14.847  39.734  1.00 82.95           C\\nANISOU 2122  CA  MET A1106    12358   8697  10463   1051    807   1630       C\\nATOM   2123  C   MET A1106      35.843 -15.311  38.725  1.00 89.43           C\\nANISOU 2123  C   MET A1106    13075   9350  11554   1362    949   1444       C\\nATOM   2124  O   MET A1106      36.305 -16.452  38.830  1.00 92.75           O\\nANISOU 2124  O   MET A1106    13623   9404  12215   1580    890   1476       O\\nATOM   2125  CB  MET A1106      33.551 -15.727  39.604  1.00 79.57           C\\nANISOU 2125  CB  MET A1106    12259   8043   9930    793    855   1607       C\\nATOM   2126  CG  MET A1106      32.706 -15.755  40.856  1.00 84.73           C\\nANISOU 2126  CG  MET A1106    13038   8785  10370    512    733   1843       C\\nATOM   2127  SD  MET A1106      30.984 -16.135  40.503  1.00 86.03           S\\nANISOU 2127  SD  MET A1106    13388   8937  10364     82    862   1721       S\\nATOM   2128  CE  MET A1106      30.421 -14.540  39.929  1.00 88.27           C\\nANISOU 2128  CE  MET A1106    13356   9694  10490     13    937   1471       C\\nATOM   2129  N   GLY A1107      36.219 -14.477  37.763  1.00 83.47           N\\nANISOU 2129  N   GLY A1107    12104   8844  10768   1383   1136   1249       N\\nATOM   2130  CA  GLY A1107      37.045 -14.923  36.668  1.00 86.98           C\\nANISOU 2130  CA  GLY A1107    12460   9202  11389   1617   1365   1006       C\\nATOM   2131  C   GLY A1107      36.292 -15.824  35.707  1.00 88.79           C\\nANISOU 2131  C   GLY A1107    13014   9179  11544   1543   1521    764       C\\nATOM   2132  O   GLY A1107      35.264 -16.426  36.027  1.00 86.13           O\\nANISOU 2132  O   GLY A1107    12973   8625  11128   1354   1409    824       O\\nATOM   2133  N   GLU A1108      36.843 -15.917  34.497  1.00 89.49           N\\nANISOU 2133  N   GLU A1108    13038   9319  11644   1667   1796    468       N\\nATOM   2134  CA  GLU A1108      36.262 -16.761  33.464  1.00 87.52           C\\nANISOU 2134  CA  GLU A1108    13103   8850  11300   1613   1951    163       C\\nATOM   2135  C   GLU A1108      36.230 -18.231  33.861  1.00 85.64           C\\nANISOU 2135  C   GLU A1108    13113   8070  11356   1798   1837    124       C\\nATOM   2136  O   GLU A1108      35.365 -18.973  33.377  1.00 84.49           O\\nANISOU 2136  O   GLU A1108    13313   7661  11130   1634   1842    -46       O\\nATOM   2137  CB  GLU A1108      37.029 -16.590  32.160  1.00 95.88           C\\nANISOU 2137  CB  GLU A1108    14037  10114  12279   1733   2303   -169       C\\nATOM   2138  CG  GLU A1108      36.931 -15.181  31.598  1.00102.62           C\\nANISOU 2138  CG  GLU A1108    14756  11443  12792   1470   2402   -100       C\\nATOM   2139  CD  GLU A1108      37.375 -15.104  30.157  1.00109.37           C\\nANISOU 2139  CD  GLU A1108    15629  12514  13413   1456   2771   -421       C\\nATOM   2140  OE1 GLU A1108      37.716 -16.168  29.591  1.00113.53           O\\nANISOU 2140  OE1 GLU A1108    16260  12832  14044   1672   2970   -764       O\\nATOM   2141  OE2 GLU A1108      37.380 -13.985  29.593  1.00105.41           O\\nANISOU 2141  OE2 GLU A1108    15063  12377  12612   1221   2859   -335       O\\nATOM   2142  N   THR A1109      37.155 -18.669  34.719  1.00 90.70           N\\nANISOU 2142  N   THR A1109    13597   8510  12353   2124   1695    286       N\\nATOM   2143  CA  THR A1109      37.120 -20.042  35.207  1.00 95.84           C\\nANISOU 2143  CA  THR A1109    14532   8571  13311   2298   1506    331       C\\nATOM   2144  C   THR A1109      35.855 -20.297  36.012  1.00 92.70           C\\nANISOU 2144  C   THR A1109    14477   8003  12741   1906   1273    629       C\\nATOM   2145  O   THR A1109      35.133 -21.269  35.766  1.00 95.09           O\\nANISOU 2145  O   THR A1109    15151   7895  13084   1765   1241    533       O\\nATOM   2146  CB  THR A1109      38.349 -20.335  36.066  1.00 97.86           C\\nANISOU 2146  CB  THR A1109    14535   8674  13974   2728   1309    517       C\\nATOM   2147  OG1 THR A1109      39.538 -19.920  35.381  1.00102.45           O\\nANISOU 2147  OG1 THR A1109    14672   9535  14718   3048   1561    242       O\\nATOM   2148  CG2 THR A1109      38.427 -21.828  36.376  1.00 97.85           C\\nANISOU 2148  CG2 THR A1109    14861   7969  14349   2976   1099    531       C\\nATOM   2149  N   GLY A1110      35.567 -19.420  36.975  1.00 95.75           N\\nANISOU 2149  N   GLY A1110    14731   8720  12931   1701   1128    965       N\\nATOM   2150  CA  GLY A1110      34.456 -19.660  37.880  1.00 94.88           C\\nANISOU 2150  CA  GLY A1110    14887   8513  12649   1331    949   1253       C\\nATOM   2151  C   GLY A1110      33.103 -19.552  37.204  1.00 88.67           C\\nANISOU 2151  C   GLY A1110    14261   7826  11602    922   1075   1072       C\\nATOM   2152  O   GLY A1110      32.191 -20.329  37.497  1.00 82.42           O\\nANISOU 2152  O   GLY A1110    13765   6760  10793    635    997   1160       O\\nATOM   2153  N   VAL A1111      32.952 -18.588  36.296  1.00 85.36           N\\nANISOU 2153  N   VAL A1111    13649   7799  10986    866   1244    836       N\\nATOM   2154  CA  VAL A1111      31.676 -18.422  35.606  1.00 83.59           C\\nANISOU 2154  CA  VAL A1111    13541   7694  10525    508   1297    660       C\\nATOM   2155  C   VAL A1111      31.371 -19.646  34.751  1.00 86.94           C\\nANISOU 2155  C   VAL A1111    14292   7686  11055    469   1346    385       C\\nATOM   2156  O   VAL A1111      30.217 -20.080  34.649  1.00 84.62           O\\nANISOU 2156  O   VAL A1111    14188   7281  10681    116   1284    338       O\\nATOM   2157  CB  VAL A1111      31.689 -17.125  34.776  1.00 78.72           C\\nANISOU 2157  CB  VAL A1111    12692   7539   9679    492   1403    508       C\\nATOM   2158  CG1 VAL A1111      30.403 -16.979  33.994  1.00 82.94           C\\nANISOU 2158  CG1 VAL A1111    13340   8183   9992    166   1385    324       C\\nATOM   2159  CG2 VAL A1111      31.894 -15.925  35.684  1.00 68.67           C\\nANISOU 2159  CG2 VAL A1111    11133   6621   8339    498   1317    755       C\\nATOM   2160  N   ALA A1112      32.402 -20.242  34.147  1.00 83.83           N\\nANISOU 2160  N   ALA A1112    13946   7039  10867    828   1457    166       N\\nATOM   2161  CA  ALA A1112      32.208 -21.434  33.331  1.00 86.95           C\\nANISOU 2161  CA  ALA A1112    14676   6976  11386    838   1502   -166       C\\nATOM   2162  C   ALA A1112      31.727 -22.636  34.137  1.00 97.68           C\\nANISOU 2162  C   ALA A1112    16361   7762  12989    696   1293     31       C\\nATOM   2163  O   ALA A1112      31.408 -23.672  33.541  1.00107.07           O\\nANISOU 2163  O   ALA A1112    17878   8495  14308    634   1283   -236       O\\nATOM   2164  CB  ALA A1112      33.504 -21.784  32.597  1.00 82.87           C\\nANISOU 2164  CB  ALA A1112    14088   6331  11068   1312   1699   -487       C\\nATOM   2165  N   GLY A1113      31.670 -22.528  35.467  1.00 94.08           N\\nANISOU 2165  N   GLY A1113    15859   7311  12576    613   1121    490       N\\nATOM   2166  CA  GLY A1113      31.127 -23.580  36.301  1.00 91.96           C\\nANISOU 2166  CA  GLY A1113    15934   6547  12461    374    924    767       C\\nATOM   2167  C   GLY A1113      29.632 -23.536  36.499  1.00 88.01           C\\nANISOU 2167  C   GLY A1113    15526   6189  11726   -228    907    854       C\\nATOM   2168  O   GLY A1113      29.067 -24.463  37.088  1.00 90.55           O\\nANISOU 2168  O   GLY A1113    16155   6098  12153   -532    780   1074       O\\nATOM   2169  N   PHE A1114      28.975 -22.477  36.030  1.00 89.32           N\\nANISOU 2169  N   PHE A1114    15419   6923  11597   -417   1020    697       N\\nATOM   2170  CA  PHE A1114      27.518 -22.347  36.101  1.00 93.06           C\\nANISOU 2170  CA  PHE A1114    15868   7604  11887   -955   1007    701       C\\nATOM   2171  C   PHE A1114      26.844 -22.935  34.867  1.00 97.68           C\\nANISOU 2171  C   PHE A1114    16640   7982  12490  -1154   1008    293       C\\nATOM   2172  O   PHE A1114      25.996 -22.294  34.250  1.00100.46           O\\nANISOU 2172  O   PHE A1114    16812   8720  12638  -1379   1016     94       O\\nATOM   2173  CB  PHE A1114      27.127 -20.883  36.266  1.00 94.49           C\\nANISOU 2173  CB  PHE A1114    15638   8468  11794  -1010   1062    728       C\\nATOM   2174  CG  PHE A1114      27.602 -20.258  37.542  1.00 95.33           C\\nANISOU 2174  CG  PHE A1114    15570   8818  11834   -900   1044   1086       C\\nATOM   2175  CD1 PHE A1114      26.863 -20.382  38.706  1.00 96.26           C\\nANISOU 2175  CD1 PHE A1114    15694   9032  11847  -1255   1023   1375       C\\nATOM   2176  CD2 PHE A1114      28.773 -19.521  37.572  1.00 93.76           C\\nANISOU 2176  CD2 PHE A1114    15190   8788  11647   -478   1057   1113       C\\nATOM   2177  CE1 PHE A1114      27.293 -19.799  39.881  1.00 93.49           C\\nANISOU 2177  CE1 PHE A1114    15219   8937  11366  -1170    999   1669       C\\nATOM   2178  CE2 PHE A1114      29.209 -18.933  38.743  1.00 90.99           C\\nANISOU 2178  CE2 PHE A1114    14688   8664  11219   -396    999   1410       C\\nATOM   2179  CZ  PHE A1114      28.468 -19.072  39.900  1.00 89.90           C\\nANISOU 2179  CZ  PHE A1114    14603   8619  10937   -731    961   1678       C\\nATOM   2180  N   THR A1115      27.213 -24.163  34.496  1.00 93.63           N\\nANISOU 2180  N   THR A1115    16502   6840  12234  -1062    963    146       N\\nATOM   2181  CA  THR A1115      26.755 -24.715  33.225  1.00 97.80           C\\nANISOU 2181  CA  THR A1115    17241   7160  12760  -1192    960   -325       C\\nATOM   2182  C   THR A1115      25.237 -24.821  33.175  1.00101.53           C\\nANISOU 2182  C   THR A1115    17699   7752  13126  -1809    862   -353       C\\nATOM   2183  O   THR A1115      24.618 -24.467  32.164  1.00100.69           O\\nANISOU 2183  O   THR A1115    17515   7914  12829  -1958    838   -694       O\\nATOM   2184  CB  THR A1115      27.395 -26.081  32.984  1.00104.56           C\\nANISOU 2184  CB  THR A1115    18523   7240  13966   -980    909   -494       C\\nATOM   2185  OG1 THR A1115      26.936 -27.010  33.974  1.00111.74           O\\nANISOU 2185  OG1 THR A1115    19700   7650  15106  -1304    745   -134       O\\nATOM   2186  CG2 THR A1115      28.912 -25.975  33.059  1.00103.25           C\\nANISOU 2186  CG2 THR A1115    18273   6991  13964   -334   1002   -493       C\\nATOM   2187  N   ASN A1116      24.617 -25.292  34.259  1.00109.01           N\\nANISOU 2187  N   ASN A1116    18703   8536  14180  -2193    797     12       N\\nATOM   2188  CA  ASN A1116      23.168 -25.450  34.256  1.00114.25           C\\nANISOU 2188  CA  ASN A1116    19286   9335  14790  -2821    734    -24       C\\nATOM   2189  C   ASN A1116      22.464 -24.103  34.180  1.00108.33           C\\nANISOU 2189  C   ASN A1116    18027   9368  13766  -2910    776    -69       C\\nATOM   2190  O   ASN A1116      21.401 -23.993  33.560  1.00112.39           O\\nANISOU 2190  O   ASN A1116    18389  10096  14219  -3257    688   -317       O\\nATOM   2191  CB  ASN A1116      22.716 -26.227  35.496  1.00119.12           C\\nANISOU 2191  CB  ASN A1116    20066   9646  15546  -3254    712    417       C\\nATOM   2192  N   SER A1117      23.040 -23.071  34.794  1.00107.10           N\\nANISOU 2192  N   SER A1117    17599   9621  13474  -2592    871    149       N\\nATOM   2193  CA  SER A1117      22.434 -21.748  34.719  1.00102.31           C\\nANISOU 2193  CA  SER A1117    16531   9686  12658  -2613    880     85       C\\nATOM   2194  C   SER A1117      22.674 -21.101  33.361  1.00102.29           C\\nANISOU 2194  C   SER A1117    16484   9870  12513  -2343    814   -265       C\\nATOM   2195  O   SER A1117      21.756 -20.507  32.785  1.00100.23           O\\nANISOU 2195  O   SER A1117    15984   9960  12139  -2521    696   -453       O\\nATOM   2196  CB  SER A1117      22.981 -20.857  35.835  1.00 98.47           C\\nANISOU 2196  CB  SER A1117    15811   9527  12076  -2381    982    404       C\\nATOM   2197  OG  SER A1117      22.892 -21.504  37.092  1.00 97.73           O\\nANISOU 2197  OG  SER A1117    15842   9258  12035  -2624   1039    761       O\\nATOM   2198  N   LEU A1118      23.897 -21.215  32.836  1.00104.26           N\\nANISOU 2198  N   LEU A1118    16951   9904  12761  -1923    883   -351       N\\nATOM   2199  CA  LEU A1118      24.243 -20.548  31.585  1.00100.23           C\\nANISOU 2199  CA  LEU A1118    16425   9622  12038  -1690    875   -637       C\\nATOM   2200  C   LEU A1118      23.389 -21.046  30.427  1.00107.73           C\\nANISOU 2200  C   LEU A1118    17547  10492  12892  -1976    724  -1011       C\\nATOM   2201  O   LEU A1118      23.041 -20.274  29.525  1.00110.02           O\\nANISOU 2201  O   LEU A1118    17736  11135  12931  -1982    613  -1185       O\\nATOM   2202  CB  LEU A1118      25.722 -20.757  31.279  1.00 92.05           C\\nANISOU 2202  CB  LEU A1118    15569   8366  11040  -1233   1041   -692       C\\nATOM   2203  CG  LEU A1118      26.695 -19.998  32.171  1.00 86.98           C\\nANISOU 2203  CG  LEU A1118    14695   7910  10443   -907   1144   -375       C\\nATOM   2204  CD1 LEU A1118      28.100 -20.549  32.003  1.00 86.56           C\\nANISOU 2204  CD1 LEU A1118    14792   7548  10551   -488   1291   -444       C\\nATOM   2205  CD2 LEU A1118      26.654 -18.516  31.846  1.00 86.67           C\\nANISOU 2205  CD2 LEU A1118    14359   8413  10159   -835   1133   -349       C\\nATOM   2206  N   ARG A1119      23.046 -22.333  30.429  1.00104.44           N\\nANISOU 2206  N   ARG A1119    17422   9590  12668  -2232    680  -1129       N\\nATOM   2207  CA  ARG A1119      22.191 -22.858  29.372  1.00103.70           C\\nANISOU 2207  CA  ARG A1119    17500   9406  12496  -2554    498  -1514       C\\nATOM   2208  C   ARG A1119      20.795 -22.250  29.433  1.00102.63           C\\nANISOU 2208  C   ARG A1119    16991   9707  12297  -2952    292  -1490       C\\nATOM   2209  O   ARG A1119      20.133 -22.113  28.398  1.00102.11           O\\nANISOU 2209  O   ARG A1119    16930   9811  12055  -3119     75  -1792       O\\nATOM   2210  CB  ARG A1119      22.123 -24.383  29.466  1.00105.66           C\\nANISOU 2210  CB  ARG A1119    18150   8971  13026  -2774    474  -1635       C\\nATOM   2211  CG  ARG A1119      21.461 -25.066  28.282  1.00110.68           C\\nANISOU 2211  CG  ARG A1119    19053   9414  13586  -3068    283  -2116       C\\nATOM   2212  CD  ARG A1119      21.400 -26.576  28.478  1.00119.37           C\\nANISOU 2212  CD  ARG A1119    20574   9750  15030  -3303    239  -2220       C\\nATOM   2213  NE  ARG A1119      20.881 -26.936  29.795  1.00121.59           N\\nANISOU 2213  NE  ARG A1119    20741   9865  15590  -3652    240  -1772       N\\nATOM   2214  CZ  ARG A1119      21.609 -27.484  30.763  1.00120.23           C\\nANISOU 2214  CZ  ARG A1119    20757   9256  15669  -3483    350  -1432       C\\nATOM   2215  NH1 ARG A1119      22.893 -27.748  30.561  1.00119.50           N\\nANISOU 2215  NH1 ARG A1119    20917   8831  15658  -2927    455  -1524       N\\nATOM   2216  NH2 ARG A1119      21.053 -27.772  31.933  1.00120.62           N\\nANISOU 2216  NH2 ARG A1119    20732   9219  15878  -3878    351  -1000       N\\nATOM   2217  N   MET A1120      20.338 -21.863  30.627  1.00100.48           N\\nANISOU 2217  N   MET A1120    16375   9649  12155  -3093    347  -1158       N\\nATOM   2218  CA  MET A1120      19.012 -21.263  30.756  1.00103.10           C\\nANISOU 2218  CA  MET A1120    16260  10430  12486  -3427    184  -1176       C\\nATOM   2219  C   MET A1120      19.000 -19.818  30.272  1.00100.31           C\\nANISOU 2219  C   MET A1120    15604  10594  11915  -3129     66  -1209       C\\nATOM   2220  O   MET A1120      18.009 -19.365  29.686  1.00100.24           O\\nANISOU 2220  O   MET A1120    15342  10888  11857  -3303   -198  -1388       O\\nATOM   2221  CB  MET A1120      18.535 -21.349  32.203  1.00106.18           C\\nANISOU 2221  CB  MET A1120    16380  10910  13054  -3686    341   -856       C\\nATOM   2222  CG  MET A1120      18.420 -22.776  32.714  1.00117.71           C\\nANISOU 2222  CG  MET A1120    18166  11832  14725  -4073    415   -750       C\\nATOM   2223  SD  MET A1120      17.789 -22.885  34.401  1.00123.98           S\\nANISOU 2223  SD  MET A1120    18683  12804  15620  -4485    629   -335       S\\nATOM   2224  CE  MET A1120      17.761 -24.663  34.625  1.00131.09           C\\nANISOU 2224  CE  MET A1120    20134  12916  16760  -4951    624   -214       C\\nATOM   2225  N   LEU A1121      20.082 -19.075  30.519  1.00100.35           N\\nANISOU 2225  N   LEU A1121    15626  10687  11815  -2692    222  -1026       N\\nATOM   2226  CA  LEU A1121      20.236 -17.769  29.884  1.00100.41           C\\nANISOU 2226  CA  LEU A1121    15473  11071  11608  -2415     91  -1049       C\\nATOM   2227  C   LEU A1121      20.299 -17.911  28.369  1.00105.95           C\\nANISOU 2227  C   LEU A1121    16480  11732  12045  -2411    -85  -1340       C\\nATOM   2228  O   LEU A1121      19.794 -17.057  27.629  1.00108.90           O\\nANISOU 2228  O   LEU A1121    16728  12416  12235  -2399   -355  -1411       O\\nATOM   2229  CB  LEU A1121      21.498 -17.077  30.396  1.00 89.96           C\\nANISOU 2229  CB  LEU A1121    14156   9787  10238  -2005    306   -807       C\\nATOM   2230  CG  LEU A1121      21.578 -16.711  31.874  1.00 82.79           C\\nANISOU 2230  CG  LEU A1121    12972   8988   9494  -1956    454   -522       C\\nATOM   2231  CD1 LEU A1121      22.975 -16.220  32.204  1.00 72.92           C\\nANISOU 2231  CD1 LEU A1121    11799   7708   8200  -1566    625   -331       C\\nATOM   2232  CD2 LEU A1121      20.549 -15.649  32.207  1.00 85.66           C\\nANISOU 2232  CD2 LEU A1121    12882   9776   9890  -2027    296   -524       C\\nATOM   2233  N   GLN A1122      20.920 -18.991  27.892  1.00 98.13           N\\nANISOU 2233  N   GLN A1122    15913  10351  11023  -2411     46  -1520       N\\nATOM   2234  CA  GLN A1122      21.020 -19.232  26.459  1.00 98.26           C\\nANISOU 2234  CA  GLN A1122    16271  10336  10727  -2427    -75  -1857       C\\nATOM   2235  C   GLN A1122      19.667 -19.584  25.852  1.00 96.39           C\\nANISOU 2235  C   GLN A1122    15998  10161  10466  -2846   -440  -2111       C\\nATOM   2236  O   GLN A1122      19.425 -19.301  24.674  1.00 98.68           O\\nANISOU 2236  O   GLN A1122    16445  10634  10417  -2889   -682  -2330       O\\nATOM   2237  CB  GLN A1122      22.036 -20.346  26.201  1.00103.05           C\\nANISOU 2237  CB  GLN A1122    17309  10483  11362  -2283    189  -2053       C\\nATOM   2238  CG  GLN A1122      22.347 -20.616  24.747  1.00107.55           C\\nANISOU 2238  CG  GLN A1122    18269  11042  11552  -2252    165  -2458       C\\nATOM   2239  CD  GLN A1122      23.447 -21.645  24.581  1.00111.75           C\\nANISOU 2239  CD  GLN A1122    19160  11128  12172  -2017    475  -2696       C\\nATOM   2240  OE1 GLN A1122      24.039 -22.100  25.559  1.00115.12           O\\nANISOU 2240  OE1 GLN A1122    19540  11237  12962  -1840    666  -2506       O\\nATOM   2241  NE2 GLN A1122      23.726 -22.017  23.338  1.00113.25           N\\nANISOU 2241  NE2 GLN A1122    19714  11294  12023  -1998    511  -3131       N\\nATOM   2242  N   GLN A1123      18.773 -20.184  26.639  1.00102.08           N\\nANISOU 2242  N   GLN A1123    16506  10761  11521  -3189   -495  -2073       N\\nATOM   2243  CA  GLN A1123      17.459 -20.603  26.168  1.00103.74           C\\nANISOU 2243  CA  GLN A1123    16604  11025  11786  -3643   -839  -2321       C\\nATOM   2244  C   GLN A1123      16.362 -19.590  26.496  1.00108.72           C\\nANISOU 2244  C   GLN A1123    16638  12153  12517  -3742  -1093  -2203       C\\nATOM   2245  O   GLN A1123      15.179 -19.947  26.486  1.00110.87           O\\nANISOU 2245  O   GLN A1123    16643  12510  12973  -4152  -1332  -2352       O\\nATOM   2246  CB  GLN A1123      17.101 -21.971  26.754  1.00101.84           C\\nANISOU 2246  CB  GLN A1123    16492  10326  11878  -4039   -744  -2378       C\\nATOM   2247  CG  GLN A1123      17.964 -23.119  26.251  1.00 99.00           C\\nANISOU 2247  CG  GLN A1123    16739   9389  11487  -3971   -604  -2613       C\\nATOM   2248  CD  GLN A1123      17.609 -24.442  26.905  1.00109.60           C\\nANISOU 2248  CD  GLN A1123    18244  10191  13208  -4372   -553  -2607       C\\nATOM   2249  OE1 GLN A1123      17.694 -24.589  28.124  1.00109.83           O\\nANISOU 2249  OE1 GLN A1123    18131  10108  13491  -4423   -352  -2243       O\\nATOM   2250  NE2 GLN A1123      17.200 -25.410  26.095  1.00111.61           N\\nANISOU 2250  NE2 GLN A1123    18833  10095  13478  -4692   -754  -3005       N\\nATOM   2251  N   LYS A1124      16.728 -18.344  26.794  1.00101.10           N\\nANISOU 2251  N   LYS A1124    15436  11503  11475  -3376  -1053  -1965       N\\nATOM   2252  CA  LYS A1124      15.801 -17.264  27.128  1.00102.00           C\\nANISOU 2252  CA  LYS A1124    14979  12055  11722  -3354  -1290  -1880       C\\nATOM   2253  C   LYS A1124      14.956 -17.560  28.362  1.00106.14           C\\nANISOU 2253  C   LYS A1124    15026  12671  12629  -3642  -1145  -1813       C\\nATOM   2254  O   LYS A1124      13.969 -16.858  28.613  1.00108.27           O\\nANISOU 2254  O   LYS A1124    14746  13316  13075  -3688  -1344  -1851       O\\nATOM   2255  CB  LYS A1124      14.875 -16.927  25.950  1.00104.85           C\\nANISOU 2255  CB  LYS A1124    15253  12649  11937  -3482  -1823  -2115       C\\nATOM   2256  CG  LYS A1124      15.585 -16.569  24.655  1.00106.34           C\\nANISOU 2256  CG  LYS A1124    15931  12827  11648  -3267  -1994  -2170       C\\nATOM   2257  CD  LYS A1124      16.318 -15.246  24.762  1.00102.53           C\\nANISOU 2257  CD  LYS A1124    15411  12521  11026  -2834  -1939  -1876       C\\nATOM   2258  CE  LYS A1124      16.710 -14.725  23.392  1.00104.63           C\\nANISOU 2258  CE  LYS A1124    16088  12882  10786  -2721  -2205  -1897       C\\nATOM   2259  NZ  LYS A1124      15.510 -14.429  22.560  1.00109.17           N\\nANISOU 2259  NZ  LYS A1124    16517  13684  11279  -2897  -2828  -2043       N\\nATOM   2260  N   ARG A1125      15.311 -18.583  29.142  1.00109.81           N\\nANISOU 2260  N   ARG A1125    15685  12809  13228  -3839   -806  -1713       N\\nATOM   2261  CA  ARG A1125      14.563 -18.937  30.349  1.00105.46           C\\nANISOU 2261  CA  ARG A1125    14749  12354  12966  -4188   -611  -1603       C\\nATOM   2262  C   ARG A1125      15.011 -18.038  31.502  1.00105.15           C\\nANISOU 2262  C   ARG A1125    14454  12555  12943  -3878   -338  -1327       C\\nATOM   2263  O   ARG A1125      15.645 -18.469  32.467  1.00102.11           O\\nANISOU 2263  O   ARG A1125    14245  11977  12576  -3884    -12  -1083       O\\nATOM   2264  CB  ARG A1125      14.757 -20.408  30.687  1.00100.56           C\\nANISOU 2264  CB  ARG A1125    14519  11232  12456  -4562   -413  -1558       C\\nATOM   2265  CG  ARG A1125      14.118 -21.370  29.702  1.00104.76           C\\nANISOU 2265  CG  ARG A1125    15255  11516  13034  -4972   -689  -1879       C\\nATOM   2266  CD  ARG A1125      14.117 -22.790  30.251  1.00109.68           C\\nANISOU 2266  CD  ARG A1125    16197  11614  13861  -5418   -505  -1800       C\\nATOM   2267  NE  ARG A1125      15.435 -23.419  30.187  1.00111.71           N\\nANISOU 2267  NE  ARG A1125    17086  11317  14042  -5114   -333  -1714       N\\nATOM   2268  CZ  ARG A1125      15.756 -24.551  30.807  1.00114.79           C\\nANISOU 2268  CZ  ARG A1125    17840  11156  14619  -5338   -166  -1549       C\\nATOM   2269  NH1 ARG A1125      14.859 -25.182  31.553  1.00117.33           N\\nANISOU 2269  NH1 ARG A1125    17995  11419  15168  -5934   -115  -1411       N\\nATOM   2270  NH2 ARG A1125      16.978 -25.051  30.689  1.00114.27           N\\nANISOU 2270  NH2 ARG A1125    18294  10594  14529  -4971    -54  -1512       N\\nATOM   2271  N   TRP A1126      14.657 -16.753  31.387  1.00102.43           N\\nANISOU 2271  N   TRP A1126    13702  12620  12595  -3599   -520  -1377       N\\nATOM   2272  CA  TRP A1126      15.103 -15.775  32.375  1.00 99.11           C\\nANISOU 2272  CA  TRP A1126    13061  12418  12179  -3267   -310  -1183       C\\nATOM   2273  C   TRP A1126      14.567 -16.088  33.763  1.00100.00           C\\nANISOU 2273  C   TRP A1126    12842  12708  12447  -3564     17  -1092       C\\nATOM   2274  O   TRP A1126      15.235 -15.807  34.763  1.00 95.88           O\\nANISOU 2274  O   TRP A1126    12367  12211  11852  -3395    296   -877       O\\nATOM   2275  CB  TRP A1126      14.683 -14.363  31.959  1.00 98.18           C\\nANISOU 2275  CB  TRP A1126    12566  12644  12092  -2934   -622  -1293       C\\nATOM   2276  CG  TRP A1126      15.001 -14.027  30.537  1.00 99.97           C\\nANISOU 2276  CG  TRP A1126    13108  12760  12116  -2737   -990  -1360       C\\nATOM   2277  CD1 TRP A1126      14.127 -13.586  29.588  1.00102.49           C\\nANISOU 2277  CD1 TRP A1126    13224  13259  12460  -2750  -1458  -1549       C\\nATOM   2278  CD2 TRP A1126      16.280 -14.113  29.895  1.00100.88           C\\nANISOU 2278  CD2 TRP A1126    13796  12592  11940  -2519   -920  -1236       C\\nATOM   2279  NE1 TRP A1126      14.782 -13.387  28.397  1.00102.69           N\\nANISOU 2279  NE1 TRP A1126    13720  13132  12164  -2582  -1684  -1520       N\\nATOM   2280  CE2 TRP A1126      16.105 -13.705  28.559  1.00102.48           C\\nANISOU 2280  CE2 TRP A1126    14155  12841  11942  -2447  -1322  -1348       C\\nATOM   2281  CE3 TRP A1126      17.558 -14.494  30.321  1.00101.84           C\\nANISOU 2281  CE3 TRP A1126    14288  12451  11954  -2377   -563  -1048       C\\nATOM   2282  CZ2 TRP A1126      17.157 -13.666  27.646  1.00107.44           C\\nANISOU 2282  CZ2 TRP A1126    15302  13297  12222  -2277  -1308  -1288       C\\nATOM   2283  CZ3 TRP A1126      18.601 -14.457  29.411  1.00101.67           C\\nANISOU 2283  CZ3 TRP A1126    14713  12253  11664  -2171   -560  -1020       C\\nATOM   2284  CH2 TRP A1126      18.393 -14.051  28.088  1.00104.96           C\\nANISOU 2284  CH2 TRP A1126    15284  12756  11842  -2142   -895  -1146       C\\nATOM   2285  N   ASP A1127      13.370 -16.667  33.848  1.00105.05           N\\nANISOU 2285  N   ASP A1127    13142  13500  13273  -4040    -10  -1251       N\\nATOM   2286  CA  ASP A1127      12.801 -16.985  35.152  1.00105.65           C\\nANISOU 2286  CA  ASP A1127    12891  13805  13446  -4403    350  -1159       C\\nATOM   2287  C   ASP A1127      13.638 -18.034  35.873  1.00102.58           C\\nANISOU 2287  C   ASP A1127    13044  13002  12929  -4604    661   -828       C\\nATOM   2288  O   ASP A1127      14.085 -17.819  37.005  1.00 97.10           O\\nANISOU 2288  O   ASP A1127    12362  12413  12117  -4531    958   -598       O\\nATOM   2289  CB  ASP A1127      11.355 -17.458  34.988  1.00113.14           C\\nANISOU 2289  CB  ASP A1127    13346  15002  14642  -4937    260  -1403       C\\nATOM   2290  N   GLU A1128      13.877 -19.175  35.221  1.00105.05           N\\nANISOU 2290  N   GLU A1128    13834  12818  13263  -4840    560   -812       N\\nATOM   2291  CA  GLU A1128      14.589 -20.266  35.881  1.00101.37           C\\nANISOU 2291  CA  GLU A1128    13890  11878  12749  -5036    788   -497       C\\nATOM   2292  C   GLU A1128      16.064 -19.940  36.072  1.00 98.59           C\\nANISOU 2292  C   GLU A1128    13939  11292  12227  -4482    856   -278       C\\nATOM   2293  O   GLU A1128      16.652 -20.294  37.101  1.00 98.75           O\\nANISOU 2293  O   GLU A1128    14183  11164  12175  -4507   1075     48       O\\nATOM   2294  CB  GLU A1128      14.433 -21.557  35.083  1.00102.72           C\\nANISOU 2294  CB  GLU A1128    14465  11516  13047  -5400    625   -601       C\\nATOM   2295  CG  GLU A1128      13.004 -22.014  34.909  1.00109.16           C\\nANISOU 2295  CG  GLU A1128    14894  12518  14063  -6031    538   -807       C\\nATOM   2296  CD  GLU A1128      12.920 -23.465  34.496  1.00117.05           C\\nANISOU 2296  CD  GLU A1128    16374  12895  15205  -6501    444   -827       C\\nATOM   2297  OE1 GLU A1128      13.445 -24.324  35.236  1.00119.18           O\\nANISOU 2297  OE1 GLU A1128    17078  12716  15487  -6681    639   -499       O\\nATOM   2298  OE2 GLU A1128      12.343 -23.744  33.426  1.00122.20           O\\nANISOU 2298  OE2 GLU A1128    16997  13477  15956  -6685    137  -1171       O\\nATOM   2299  N   ALA A1129      16.686 -19.280  35.090  1.00106.39           N\\nANISOU 2299  N   ALA A1129    15026  12259  13140  -4007    658   -438       N\\nATOM   2300  CA  ALA A1129      18.089 -18.904  35.232  1.00 98.44           C\\nANISOU 2300  CA  ALA A1129    14315  11087  12002  -3503    734   -256       C\\nATOM   2301  C   ALA A1129      18.313 -18.065  36.481  1.00 99.96           C\\nANISOU 2301  C   ALA A1129    14247  11624  12110  -3345    925    -40       C\\nATOM   2302  O   ALA A1129      19.394 -18.111  37.080  1.00 91.71           O\\nANISOU 2302  O   ALA A1129    13458  10403  10986  -3100   1037    208       O\\nATOM   2303  CB  ALA A1129      18.562 -18.146  33.991  1.00 90.27           C\\nANISOU 2303  CB  ALA A1129    13335  10100  10864  -3097    524   -462       C\\nATOM   2304  N   ALA A1130      17.300 -17.301  36.894  1.00101.90           N\\nANISOU 2304  N   ALA A1130    13969  12366  12382  -3472    950   -165       N\\nATOM   2305  CA  ALA A1130      17.396 -16.557  38.143  1.00100.47           C\\nANISOU 2305  CA  ALA A1130    13541  12535  12097  -3370   1159    -30       C\\nATOM   2306  C   ALA A1130      17.236 -17.478  39.344  1.00 96.24           C\\nANISOU 2306  C   ALA A1130    13135  11951  11481  -3804   1437    243       C\\nATOM   2307  O   ALA A1130      17.958 -17.340  40.339  1.00 91.99           O\\nANISOU 2307  O   ALA A1130    12752  11434  10767  -3682   1586    498       O\\nATOM   2308  CB  ALA A1130      16.348 -15.446  38.172  1.00102.74           C\\nANISOU 2308  CB  ALA A1130    13205  13359  12471  -3324   1106   -319       C\\nATOM   2309  N   VAL A1131      16.303 -18.428  39.267  1.00 92.07           N\\nANISOU 2309  N   VAL A1131    12568  11350  11062  -4347   1484    213       N\\nATOM   2310  CA  VAL A1131      16.030 -19.294  40.409  1.00 92.71           C\\nANISOU 2310  CA  VAL A1131    12779  11404  11044  -4858   1755    513       C\\nATOM   2311  C   VAL A1131      17.210 -20.220  40.681  1.00 93.11           C\\nANISOU 2311  C   VAL A1131    13506  10845  11028  -4781   1726    899       C\\nATOM   2312  O   VAL A1131      17.533 -20.509  41.839  1.00 94.49           O\\nANISOU 2312  O   VAL A1131    13879  11018  11005  -4935   1900   1255       O\\nATOM   2313  CB  VAL A1131      14.728 -20.083  40.179  1.00 91.93           C\\nANISOU 2313  CB  VAL A1131    12455  11353  11120  -5514   1797    386       C\\nATOM   2314  N   ASN A1132      17.877 -20.696  39.626  1.00 98.73           N\\nANISOU 2314  N   ASN A1132    14580  11039  11893  -4528   1494    823       N\\nATOM   2315  CA  ASN A1132      19.028 -21.572  39.827  1.00 99.57           C\\nANISOU 2315  CA  ASN A1132    15279  10537  12016  -4371   1439   1132       C\\nATOM   2316  C   ASN A1132      20.208 -20.804  40.407  1.00 98.88           C\\nANISOU 2316  C   ASN A1132    15239  10564  11768  -3840   1452   1311       C\\nATOM   2317  O   ASN A1132      20.866 -21.282  41.338  1.00106.13           O\\nANISOU 2317  O   ASN A1132    16469  11262  12593  -3844   1482   1689       O\\nATOM   2318  CB  ASN A1132      19.417 -22.244  38.508  1.00100.70           C\\nANISOU 2318  CB  ASN A1132    15748  10141  12372  -4206   1226    906       C\\nATOM   2319  CG  ASN A1132      20.355 -23.432  38.702  1.00102.63           C\\nANISOU 2319  CG  ASN A1132    16592   9660  12743  -4136   1159   1173       C\\nATOM   2320  OD1 ASN A1132      21.259 -23.402  39.538  1.00 99.29           O\\nANISOU 2320  OD1 ASN A1132    16345   9141  12242  -3883   1185   1501       O\\nATOM   2321  ND2 ASN A1132      20.136 -24.489  37.929  1.00107.31           N\\nANISOU 2321  ND2 ASN A1132    17502   9719  13554  -4348   1034   1014       N\\nATOM   2322  N   LEU A1133      20.483 -19.606  39.881  1.00 85.10           N\\nANISOU 2322  N   LEU A1133    13195   9149   9988  -3405   1394   1062       N\\nATOM   2323  CA  LEU A1133      21.652 -18.849  40.317  1.00 79.83           C\\nANISOU 2323  CA  LEU A1133    12558   8566   9209  -2920   1377   1196       C\\nATOM   2324  C   LEU A1133      21.591 -18.470  41.792  1.00 85.06           C\\nANISOU 2324  C   LEU A1133    13112   9576   9629  -3048   1529   1445       C\\nATOM   2325  O   LEU A1133      22.638 -18.221  42.399  1.00 82.43           O\\nANISOU 2325  O   LEU A1133    12927   9198   9193  -2748   1484   1656       O\\nATOM   2326  CB  LEU A1133      21.813 -17.596  39.454  1.00 84.72           C\\nANISOU 2326  CB  LEU A1133    12879   9469   9842  -2527   1283    893       C\\nATOM   2327  CG  LEU A1133      22.459 -17.798  38.079  1.00 88.21           C\\nANISOU 2327  CG  LEU A1133    13529   9583  10405  -2245   1143    716       C\\nATOM   2328  CD1 LEU A1133      22.334 -16.537  37.242  1.00 90.94           C\\nANISOU 2328  CD1 LEU A1133    13587  10258  10710  -1997   1039    463       C\\nATOM   2329  CD2 LEU A1133      23.920 -18.203  38.219  1.00 83.43           C\\nANISOU 2329  CD2 LEU A1133    13242   8615   9844  -1895   1135    911       C\\nATOM   2330  N   ALA A1134      20.399 -18.433  42.386  1.00 84.49           N\\nANISOU 2330  N   ALA A1134    12774   9880   9449  -3501   1713   1404       N\\nATOM   2331  CA  ALA A1134      20.263 -18.129  43.804  1.00 83.30           C\\nANISOU 2331  CA  ALA A1134    12544  10115   8992  -3684   1912   1604       C\\nATOM   2332  C   ALA A1134      20.570 -19.322  44.697  1.00 95.28           C\\nANISOU 2332  C   ALA A1134    14547  11297  10359  -4027   1952   2087       C\\nATOM   2333  O   ALA A1134      20.536 -19.181  45.925  1.00100.46           O\\nANISOU 2333  O   ALA A1134    15234  12260  10675  -4222   2106   2315       O\\nATOM   2334  CB  ALA A1134      18.855 -17.614  44.103  1.00 88.70           C\\nANISOU 2334  CB  ALA A1134    12701  11389   9612  -4038   2147   1331       C\\nATOM   2335  N   LYS A1135      20.860 -20.486  44.116  1.00 88.10           N\\nANISOU 2335  N   LYS A1135    14044   9751   9678  -4109   1800   2243       N\\nATOM   2336  CA  LYS A1135      21.205 -21.680  44.871  1.00 87.20           C\\nANISOU 2336  CA  LYS A1135    14461   9179   9491  -4398   1755   2737       C\\nATOM   2337  C   LYS A1135      22.701 -21.967  44.852  1.00 86.32           C\\nANISOU 2337  C   LYS A1135    14744   8566   9488  -3866   1479   2966       C\\nATOM   2338  O   LYS A1135      23.109 -23.103  45.109  1.00102.38           O\\nANISOU 2338  O   LYS A1135    17270  10011  11619  -3979   1327   3328       O\\nATOM   2339  CB  LYS A1135      20.432 -22.884  44.332  1.00 91.82           C\\nANISOU 2339  CB  LYS A1135    15253   9320  10313  -4902   1752   2756       C\\nATOM   2340  N   SER A1136      23.523 -20.968  44.553  1.00 82.36           N\\nANISOU 2340  N   SER A1136    14022   8267   9005  -3296   1395   2765       N\\nATOM   2341  CA  SER A1136      24.959 -21.160  44.431  1.00 83.52           C\\nANISOU 2341  CA  SER A1136    14419   8004   9312  -2765   1149   2911       C\\nATOM   2342  C   SER A1136      25.684 -20.619  45.656  1.00 88.67           C\\nANISOU 2342  C   SER A1136    15092   8930   9667  -2607   1075   3205       C\\nATOM   2343  O   SER A1136      25.148 -19.816  46.424  1.00 92.03           O\\nANISOU 2343  O   SER A1136    15281   9935   9752  -2806   1240   3175       O\\nATOM   2344  CB  SER A1136      25.494 -20.477  43.171  1.00 79.24           C\\nANISOU 2344  CB  SER A1136    13626   7476   9007  -2270   1101   2495       C\\nATOM   2345  OG  SER A1136      25.423 -19.068  43.285  1.00 73.97           O\\nANISOU 2345  OG  SER A1136    12540   7401   8165  -2108   1183   2288       O\\nATOM   2346  N   ARG A1137      26.926 -21.078  45.832  1.00 91.39           N\\nANISOU 2346  N   ARG A1137    15712   8855  10158  -2229    806   3459       N\\nATOM   2347  CA  ARG A1137      27.767 -20.540  46.894  1.00 91.41           C\\nANISOU 2347  CA  ARG A1137    15721   9100   9909  -2019    652   3712       C\\nATOM   2348  C   ARG A1137      28.177 -19.101  46.613  1.00 85.85           C\\nANISOU 2348  C   ARG A1137    14558   8882   9179  -1656    695   3357       C\\nATOM   2349  O   ARG A1137      28.655 -18.413  47.521  1.00 85.58           O\\nANISOU 2349  O   ARG A1137    14453   9182   8883  -1561    604   3470       O\\nATOM   2350  CB  ARG A1137      29.009 -21.414  47.089  1.00 94.63           C\\nANISOU 2350  CB  ARG A1137    16484   8915  10557  -1666    293   4057       C\\nATOM   2351  N   TRP A1138      28.013 -18.639  45.372  1.00 85.61           N\\nANISOU 2351  N   TRP A1138    14253   8876   9400  -1476    803   2943       N\\nATOM   2352  CA  TRP A1138      28.240 -17.235  45.053  1.00 83.05           C\\nANISOU 2352  CA  TRP A1138    13523   8984   9049  -1214    846   2628       C\\nATOM   2353  C   TRP A1138      27.118 -16.360  45.596  1.00 83.65           C\\nANISOU 2353  C   TRP A1138    13343   9618   8821  -1522   1044   2460       C\\nATOM   2354  O   TRP A1138      27.378 -15.303  46.181  1.00 74.31           O\\nANISOU 2354  O   TRP A1138    11960   8813   7461  -1395   1022   2377       O\\nATOM   2355  CB  TRP A1138      28.387 -17.069  43.541  1.00 81.72           C\\nANISOU 2355  CB  TRP A1138    13205   8653   9191   -970    885   2291       C\\nATOM   2356  CG  TRP A1138      28.200 -15.675  43.038  1.00 80.37           C\\nANISOU 2356  CG  TRP A1138    12659   8893   8984   -845    952   1971       C\\nATOM   2357  CD1 TRP A1138      29.008 -14.601  43.270  1.00 79.75           C\\nANISOU 2357  CD1 TRP A1138    12375   9046   8880   -571    866   1931       C\\nATOM   2358  CD2 TRP A1138      27.151 -15.209  42.179  1.00 79.40           C\\nANISOU 2358  CD2 TRP A1138    12339   8950   8882   -990   1065   1659       C\\nATOM   2359  NE1 TRP A1138      28.520 -13.492  42.620  1.00 74.10           N\\nANISOU 2359  NE1 TRP A1138    11385   8600   8171   -543    925   1634       N\\nATOM   2360  CE2 TRP A1138      27.381 -13.840  41.944  1.00 77.74           C\\nANISOU 2360  CE2 TRP A1138    11841   9040   8657   -775   1031   1470       C\\nATOM   2361  CE3 TRP A1138      26.036 -15.814  41.592  1.00 70.14           C\\nANISOU 2361  CE3 TRP A1138    11201   7697   7754  -1292   1152   1527       C\\nATOM   2362  CZ2 TRP A1138      26.539 -13.069  41.149  1.00 75.61           C\\nANISOU 2362  CZ2 TRP A1138    11345   8968   8416   -815   1054   1185       C\\nATOM   2363  CZ3 TRP A1138      25.201 -15.044  40.801  1.00 72.99           C\\nANISOU 2363  CZ3 TRP A1138    11290   8307   8136  -1332   1174   1217       C\\nATOM   2364  CH2 TRP A1138      25.457 -13.689  40.588  1.00 72.54           C\\nANISOU 2364  CH2 TRP A1138    10974   8524   8064  -1078   1113   1063       C\\nATOM   2365  N   TYR A1139      25.867 -16.790  45.424  1.00 82.65           N\\nANISOU 2365  N   TYR A1139    13198   9549   8658  -1927   1233   2375       N\\nATOM   2366  CA  TYR A1139      24.743 -16.053  45.987  1.00 86.12           C\\nANISOU 2366  CA  TYR A1139    13337  10541   8845  -2219   1452   2182       C\\nATOM   2367  C   TYR A1139      24.771 -16.040  47.509  1.00 83.42           C\\nANISOU 2367  C   TYR A1139    13129  10492   8073  -2444   1516   2445       C\\nATOM   2368  O   TYR A1139      24.214 -15.122  48.120  1.00 85.20           O\\nANISOU 2368  O   TYR A1139    13075  11244   8055  -2528   1680   2223       O\\nATOM   2369  CB  TYR A1139      23.424 -16.647  45.483  1.00 93.06           C\\nANISOU 2369  CB  TYR A1139    14126  11418   9815  -2639   1632   2048       C\\nATOM   2370  CG  TYR A1139      22.187 -15.947  45.998  1.00 97.27           C\\nANISOU 2370  CG  TYR A1139    14256  12545  10156  -2931   1887   1793       C\\nATOM   2371  CD1 TYR A1139      21.714 -14.791  45.393  1.00 97.09           C\\nANISOU 2371  CD1 TYR A1139    13784  12829  10275  -2703   1891   1360       C\\nATOM   2372  CD2 TYR A1139      21.487 -16.449  47.086  1.00101.31           C\\nANISOU 2372  CD2 TYR A1139    14831  13310  10352  -3435   2125   1984       C\\nATOM   2373  CE1 TYR A1139      20.582 -14.152  45.862  1.00 98.45           C\\nANISOU 2373  CE1 TYR A1139    13534  13534  10340  -2906   2113   1072       C\\nATOM   2374  CE2 TYR A1139      20.357 -15.817  47.560  1.00102.23           C\\nANISOU 2374  CE2 TYR A1139    14515  14020  10307  -3689   2412   1691       C\\nATOM   2375  CZ  TYR A1139      19.909 -14.671  46.946  1.00 98.03           C\\nANISOU 2375  CZ  TYR A1139    13492  13774   9981  -3392   2400   1210       C\\nATOM   2376  OH  TYR A1139      18.781 -14.044  47.424  1.00 96.25           O\\nANISOU 2376  OH  TYR A1139    12784  14130   9656  -3586   2677    868       O\\nATOM   2377  N   ASN A1140      25.410 -17.028  48.134  1.00 84.98           N\\nANISOU 2377  N   ASN A1140    13766  10358   8165  -2531   1372   2902       N\\nATOM   2378  CA  ASN A1140      25.511 -17.069  49.585  1.00 81.09           C\\nANISOU 2378  CA  ASN A1140    13485  10139   7189  -2767   1384   3212       C\\nATOM   2379  C   ASN A1140      26.720 -16.316  50.123  1.00 81.14           C\\nANISOU 2379  C   ASN A1140    13495  10255   7081  -2354   1121   3259       C\\nATOM   2380  O   ASN A1140      26.732 -15.963  51.308  1.00 91.34           O\\nANISOU 2380  O   ASN A1140    14868  11933   7905  -2514   1139   3371       O\\nATOM   2381  CB  ASN A1140      25.564 -18.521  50.073  1.00 83.93           C\\nANISOU 2381  CB  ASN A1140    14351  10066   7474  -3090   1289   3738       C\\nATOM   2382  CG  ASN A1140      24.263 -19.268  49.834  1.00 88.69           C\\nANISOU 2382  CG  ASN A1140    14898  10646   8154  -3583   1553   3682       C\\nATOM   2383  OD1 ASN A1140      23.328 -19.182  50.631  1.00 94.13           O\\nANISOU 2383  OD1 ASN A1140    15427  11795   8542  -3964   1814   3633       O\\nATOM   2384  ND2 ASN A1140      24.203 -20.015  48.739  1.00 88.26           N\\nANISOU 2384  ND2 ASN A1140    14971  10056   8508  -3583   1485   3663       N\\nATOM   2385  N   GLN A1141      27.731 -16.058  49.292  1.00 79.05           N\\nANISOU 2385  N   GLN A1141    13135   9692   7209  -1861    889   3159       N\\nATOM   2386  CA  GLN A1141      28.944 -15.389  49.751  1.00 83.34           C\\nANISOU 2386  CA  GLN A1141    13640  10316   7710  -1493    612   3207       C\\nATOM   2387  C   GLN A1141      28.857 -13.872  49.622  1.00 86.83           C\\nANISOU 2387  C   GLN A1141    13669  11193   8130  -1321    691   2761       C\\nATOM   2388  O   GLN A1141      29.270 -13.148  50.534  1.00 90.33           O\\nANISOU 2388  O   GLN A1141    14085  11948   8290  -1274    578   2742       O\\nATOM   2389  CB  GLN A1141      30.158 -15.908  48.974  1.00 81.76           C\\nANISOU 2389  CB  GLN A1141    13505   9595   7966  -1066    339   3330       C\\nATOM   2390  N   THR A1142      28.341 -13.378  48.497  1.00 81.15           N\\nANISOU 2390  N   THR A1142    12660  10468   7708  -1228    841   2404       N\\nATOM   2391  CA  THR A1142      28.099 -11.952  48.276  1.00 75.62           C\\nANISOU 2391  CA  THR A1142    11594  10099   7040  -1081    896   1987       C\\nATOM   2392  C   THR A1142      26.654 -11.815  47.825  1.00 80.15           C\\nANISOU 2392  C   THR A1142    11953  10861   7638  -1313   1170   1698       C\\nATOM   2393  O   THR A1142      26.373 -11.645  46.629  1.00 76.21           O\\nANISOU 2393  O   THR A1142    11292  10208   7456  -1195   1180   1504       O\\nATOM   2394  CB  THR A1142      29.064 -11.368  47.245  1.00 71.01           C\\nANISOU 2394  CB  THR A1142    10854   9291   6836   -689    721   1873       C\\nATOM   2395  OG1 THR A1142      28.852 -12.004  45.979  1.00 61.90           O\\nANISOU 2395  OG1 THR A1142     9720   7819   5981   -656    792   1847       O\\nATOM   2396  CG2 THR A1142      30.507 -11.581  47.678  1.00 64.20           C\\nANISOU 2396  CG2 THR A1142    10120   8261   6011   -463    447   2144       C\\nATOM   2397  N   PRO A1143      25.702 -11.890  48.760  1.00 78.66           N\\nANISOU 2397  N   PRO A1143    11743  11039   7106  -1659   1396   1658       N\\nATOM   2398  CA  PRO A1143      24.288 -11.947  48.355  1.00 77.44           C\\nANISOU 2398  CA  PRO A1143    11332  11073   7019  -1917   1663   1400       C\\nATOM   2399  C   PRO A1143      23.754 -10.645  47.786  1.00 81.38           C\\nANISOU 2399  C   PRO A1143    11396  11793   7731  -1681   1672    913       C\\nATOM   2400  O   PRO A1143      22.964 -10.679  46.836  1.00 67.23           O\\nANISOU 2400  O   PRO A1143     9390   9947   6208  -1709   1715    723       O\\nATOM   2401  CB  PRO A1143      23.575 -12.337  49.655  1.00 74.02           C\\nANISOU 2401  CB  PRO A1143    10976  11033   6115  -2363   1931   1502       C\\nATOM   2402  CG  PRO A1143      24.484 -11.856  50.733  1.00 74.95           C\\nANISOU 2402  CG  PRO A1143    11275  11318   5883  -2235   1792   1614       C\\nATOM   2403  CD  PRO A1143      25.873 -12.037  50.213  1.00 80.85           C\\nANISOU 2403  CD  PRO A1143    12236  11590   6893  -1870   1423   1866       C\\nATOM   2404  N   ASN A1144      24.148  -9.498  48.346  1.00 79.84           N\\nANISOU 2404  N   ASN A1144    11080  11820   7435  -1453   1593    702       N\\nATOM   2405  CA  ASN A1144      23.656  -8.219  47.839  1.00 82.18           C\\nANISOU 2405  CA  ASN A1144    11000  12248   7977  -1203   1550    249       C\\nATOM   2406  C   ASN A1144      24.024  -8.031  46.372  1.00 83.32           C\\nANISOU 2406  C   ASN A1144    11122  12002   8536   -947   1323    262       C\\nATOM   2407  O   ASN A1144      23.168  -7.712  45.538  1.00 77.89           O\\nANISOU 2407  O   ASN A1144    10184  11322   8089   -907   1317     25       O\\nATOM   2408  CB  ASN A1144      24.209  -7.072  48.683  1.00 86.17           C\\nANISOU 2408  CB  ASN A1144    11466  12947   8328   -999   1448     44       C\\nATOM   2409  CG  ASN A1144      23.399  -6.831  49.942  1.00 91.58           C\\nANISOU 2409  CG  ASN A1144    12020  14149   8626  -1210   1730   -220       C\\nATOM   2410  OD1 ASN A1144      22.445  -6.054  49.938  1.00 89.43           O\\nANISOU 2410  OD1 ASN A1144    11378  14135   8467  -1137   1861   -680       O\\nATOM   2411  ND2 ASN A1144      23.778  -7.496  51.028  1.00 95.06           N\\nANISOU 2411  ND2 ASN A1144    12763  14756   8600  -1466   1818     62       N\\nATOM   2412  N   ARG A1145      25.302  -8.228  46.040  1.00 83.54           N\\nANISOU 2412  N   ARG A1145    11397  11711   8633   -780   1132    536       N\\nATOM   2413  CA  ARG A1145      25.740  -8.103  44.655  1.00 77.75           C\\nANISOU 2413  CA  ARG A1145    10673  10652   8215   -579    973    561       C\\nATOM   2414  C   ARG A1145      25.101  -9.167  43.774  1.00 76.82           C\\nANISOU 2414  C   ARG A1145    10624  10365   8200   -753   1062    630       C\\nATOM   2415  O   ARG A1145      24.721  -8.887  42.631  1.00 82.58           O\\nANISOU 2415  O   ARG A1145    11252  10993   9130   -675    981    488       O\\nATOM   2416  CB  ARG A1145      27.264  -8.189  44.587  1.00 73.67           C\\nANISOU 2416  CB  ARG A1145    10353   9896   7744   -393    814    816       C\\nATOM   2417  CG  ARG A1145      27.829  -8.227  43.179  1.00 69.75           C\\nANISOU 2417  CG  ARG A1145     9893   9104   7505   -234    729    865       C\\nATOM   2418  CD  ARG A1145      29.352  -8.232  43.189  1.00 73.59           C\\nANISOU 2418  CD  ARG A1145    10468   9428   8064    -50    612   1067       C\\nATOM   2419  NE  ARG A1145      29.897  -8.135  41.837  1.00 80.75           N\\nANISOU 2419  NE  ARG A1145    11375  10131   9175     79    594   1070       N\\nATOM   2420  CZ  ARG A1145      31.175  -7.901  41.556  1.00 82.83           C\\nANISOU 2420  CZ  ARG A1145    11612  10298   9561    237    528   1175       C\\nATOM   2421  NH1 ARG A1145      32.054  -7.734  42.535  1.00 82.57           N\\nANISOU 2421  NH1 ARG A1145    11535  10328   9508    307    415   1287       N\\nATOM   2422  NH2 ARG A1145      31.574  -7.829  40.293  1.00 85.74           N\\nANISOU 2422  NH2 ARG A1145    11982  10541  10053    302    578   1158       N\\nATOM   2423  N   ALA A1146      24.974 -10.393  44.287  1.00 78.38           N\\nANISOU 2423  N   ALA A1146    11025  10507   8249  -1011   1196    857       N\\nATOM   2424  CA  ALA A1146      24.412 -11.480  43.491  1.00 77.28           C\\nANISOU 2424  CA  ALA A1146    10992  10148   8224  -1212   1259    913       C\\nATOM   2425  C   ALA A1146      22.965 -11.191  43.114  1.00 83.69           C\\nANISOU 2425  C   ALA A1146    11482  11202   9113  -1389   1341    610       C\\nATOM   2426  O   ALA A1146      22.575 -11.340  41.951  1.00 81.20           O\\nANISOU 2426  O   ALA A1146    11127  10738   8988  -1380   1252    495       O\\nATOM   2427  CB  ALA A1146      24.519 -12.800  44.253  1.00 75.31           C\\nANISOU 2427  CB  ALA A1146    11049   9751   7813  -1491   1359   1239       C\\nATOM   2428  N   LYS A1147      22.154 -10.771  44.090  1.00 81.29           N\\nANISOU 2428  N   LYS A1147    10927  11303   8657  -1547   1506    451       N\\nATOM   2429  CA  LYS A1147      20.760 -10.442  43.804  1.00 80.52           C\\nANISOU 2429  CA  LYS A1147    10420  11486   8686  -1680   1585    116       C\\nATOM   2430  C   LYS A1147      20.649  -9.302  42.799  1.00 83.83           C\\nANISOU 2430  C   LYS A1147    10611  11866   9377  -1325   1329   -152       C\\nATOM   2431  O   LYS A1147      19.710  -9.273  41.995  1.00 68.30           O\\nANISOU 2431  O   LYS A1147     8403   9940   7609  -1375   1246   -350       O\\nATOM   2432  CB  LYS A1147      20.023 -10.088  45.098  1.00 67.35           C\\nANISOU 2432  CB  LYS A1147     8483  10311   6797  -1863   1853    -63       C\\nATOM   2433  N   ARG A1148      21.599  -8.365  42.815  1.00 85.54           N\\nANISOU 2433  N   ARG A1148    10910  11984   9606   -988   1167   -140       N\\nATOM   2434  CA  ARG A1148      21.574  -7.277  41.842  1.00 79.68           C\\nANISOU 2434  CA  ARG A1148    10031  11139   9107   -685    892   -317       C\\nATOM   2435  C   ARG A1148      21.891  -7.783  40.437  1.00 82.33           C\\nANISOU 2435  C   ARG A1148    10589  11152   9539   -673    733   -165       C\\nATOM   2436  O   ARG A1148      21.289  -7.330  39.457  1.00 90.33           O\\nANISOU 2436  O   ARG A1148    11469  12136  10717   -591    526   -312       O\\nATOM   2437  CB  ARG A1148      22.555  -6.182  42.261  1.00 70.66           C\\nANISOU 2437  CB  ARG A1148     8952   9944   7952   -403    768   -316       C\\nATOM   2438  CG  ARG A1148      21.892  -4.860  42.620  1.00 71.12           C\\nANISOU 2438  CG  ARG A1148     8676  10192   8155   -198    669   -688       C\\nATOM   2439  CD  ARG A1148      22.475  -4.260  43.892  1.00 73.19           C\\nANISOU 2439  CD  ARG A1148     8962  10601   8247   -122    743   -769       C\\nATOM   2440  NE  ARG A1148      23.934  -4.303  43.899  1.00 73.07           N\\nANISOU 2440  NE  ARG A1148     9271  10346   8145    -63    641   -461       N\\nATOM   2441  CZ  ARG A1148      24.686  -4.003  44.953  1.00 72.04           C\\nANISOU 2441  CZ  ARG A1148     9236  10306   7829    -40    656   -444       C\\nATOM   2442  NH1 ARG A1148      24.121  -3.632  46.093  1.00 77.77           N\\nANISOU 2442  NH1 ARG A1148     9809  11363   8378    -79    795   -729       N\\nATOM   2443  NH2 ARG A1148      26.005  -4.075  44.867  1.00 70.75           N\\nANISOU 2443  NH2 ARG A1148     9301   9933   7647     15    532   -167       N\\nATOM   2444  N   VAL A1149      22.824  -8.727  40.321  1.00 86.59           N\\nANISOU 2444  N   VAL A1149    11473  11454   9974   -742    812    112       N\\nATOM   2445  CA  VAL A1149      23.201  -9.252  39.011  1.00 82.53           C\\nANISOU 2445  CA  VAL A1149    11189  10655   9513   -723    713    200       C\\nATOM   2446  C   VAL A1149      22.160 -10.240  38.500  1.00 89.46           C\\nANISOU 2446  C   VAL A1149    12052  11515  10424  -1007    747    112       C\\nATOM   2447  O   VAL A1149      21.841 -10.260  37.304  1.00 88.71           O\\nANISOU 2447  O   VAL A1149    11995  11326  10387  -1003    583     17       O\\nATOM   2448  CB  VAL A1149      24.603  -9.881  39.089  1.00 69.15           C\\nANISOU 2448  CB  VAL A1149     9812   8710   7751   -638    790    459       C\\nATOM   2449  CG1 VAL A1149      24.961 -10.583  37.793  1.00 62.41           C\\nANISOU 2449  CG1 VAL A1149     9197   7590   6927   -632    765    483       C\\nATOM   2450  CG2 VAL A1149      25.636  -8.812  39.423  1.00 65.57           C\\nANISOU 2450  CG2 VAL A1149     9323   8286   7303   -385    710    522       C\\nATOM   2451  N   ILE A1150      21.606 -11.063  39.394  1.00 84.73           N\\nANISOU 2451  N   ILE A1150    11413  11014   9767  -1295    945    151       N\\nATOM   2452  CA  ILE A1150      20.566 -12.008  38.997  1.00 83.24           C\\nANISOU 2452  CA  ILE A1150    11179  10809   9639  -1639    980     64       C\\nATOM   2453  C   ILE A1150      19.315 -11.263  38.545  1.00 84.16           C\\nANISOU 2453  C   ILE A1150    10861  11211   9905  -1651    831   -246       C\\nATOM   2454  O   ILE A1150      18.622 -11.692  37.612  1.00 93.69           O\\nANISOU 2454  O   ILE A1150    12028  12360  11209  -1807    688   -369       O\\nATOM   2455  CB  ILE A1150      20.272 -12.986  40.152  1.00 84.83           C\\nANISOU 2455  CB  ILE A1150    11442  11060   9730  -2003   1240    225       C\\nATOM   2456  CG1 ILE A1150      21.486 -13.878  40.414  1.00 82.12           C\\nANISOU 2456  CG1 ILE A1150    11568  10333   9299  -1964   1285    553       C\\nATOM   2457  CG2 ILE A1150      19.059 -13.839  39.844  1.00 86.81           C\\nANISOU 2457  CG2 ILE A1150    11564  11344  10076  -2432   1287    113       C\\nATOM   2458  CD1 ILE A1150      21.367 -14.717  41.663  1.00 70.60           C\\nANISOU 2458  CD1 ILE A1150    10253   8891   7682  -2294   1484    806       C\\nATOM   2459  N   THR A1151      19.009 -10.131  39.188  1.00 79.62           N\\nANISOU 2459  N   THR A1151     9946  10934   9371  -1467    829   -404       N\\nATOM   2460  CA  THR A1151      17.920  -9.283  38.713  1.00 85.27           C\\nANISOU 2460  CA  THR A1151    10223  11875  10301  -1363    618   -716       C\\nATOM   2461  C   THR A1151      18.194  -8.785  37.302  1.00 88.73           C\\nANISOU 2461  C   THR A1151    10820  12078  10815  -1128    245   -709       C\\nATOM   2462  O   THR A1151      17.290  -8.744  36.460  1.00 89.80           O\\nANISOU 2462  O   THR A1151    10761  12268  11090  -1177     -2   -876       O\\nATOM   2463  CB  THR A1151      17.713  -8.098  39.655  1.00 85.11           C\\nANISOU 2463  CB  THR A1151     9861  12141  10338  -1127    668   -919       C\\nATOM   2464  OG1 THR A1151      17.364  -8.577  40.957  1.00 90.34           O\\nANISOU 2464  OG1 THR A1151    10377  13098  10849  -1398   1046   -947       O\\nATOM   2465  CG2 THR A1151      16.602  -7.194  39.144  1.00 80.06           C\\nANISOU 2465  CG2 THR A1151     8743  11680   9998   -942    398  -1262       C\\nATOM   2466  N   THR A1152      19.440  -8.402  37.023  1.00 89.05           N\\nANISOU 2466  N   THR A1152    11208  11880  10745   -898    191   -508       N\\nATOM   2467  CA  THR A1152      19.772  -7.948  35.679  1.00 88.03           C\\nANISOU 2467  CA  THR A1152    11283  11556  10607   -736   -114   -459       C\\nATOM   2468  C   THR A1152      19.666  -9.080  34.665  1.00 84.57           C\\nANISOU 2468  C   THR A1152    11105  10963  10066   -967   -143   -432       C\\nATOM   2469  O   THR A1152      19.276  -8.846  33.516  1.00 88.93           O\\nANISOU 2469  O   THR A1152    11704  11483  10603   -948   -442   -501       O\\nATOM   2470  CB  THR A1152      21.170  -7.335  35.670  1.00 84.93           C\\nANISOU 2470  CB  THR A1152    11169  10986  10115   -508    -96   -248       C\\nATOM   2471  OG1 THR A1152      21.238  -6.314  36.674  1.00 87.26           O\\nANISOU 2471  OG1 THR A1152    11240  11404  10511   -322    -88   -315       O\\nATOM   2472  CG2 THR A1152      21.473  -6.721  34.321  1.00 75.79           C\\nANISOU 2472  CG2 THR A1152    10215   9677   8903   -385   -386   -175       C\\nATOM   2473  N   PHE A1153      19.988 -10.311  35.069  1.00 80.31           N\\nANISOU 2473  N   PHE A1153    10763  10305   9447  -1189    130   -341       N\\nATOM   2474  CA  PHE A1153      19.838 -11.445  34.163  1.00 86.85           C\\nANISOU 2474  CA  PHE A1153    11850  10938  10209  -1417    102   -378       C\\nATOM   2475  C   PHE A1153      18.375 -11.753  33.876  1.00 94.28           C\\nANISOU 2475  C   PHE A1153    12493  12048  11280  -1692    -61   -605       C\\nATOM   2476  O   PHE A1153      18.051 -12.271  32.802  1.00 97.03           O\\nANISOU 2476  O   PHE A1153    13001  12289  11578  -1834   -250   -712       O\\nATOM   2477  CB  PHE A1153      20.524 -12.681  34.744  1.00 85.98           C\\nANISOU 2477  CB  PHE A1153    12033  10584  10052  -1564    394   -224       C\\nATOM   2478  CG  PHE A1153      21.973 -12.790  34.388  1.00 82.81           C\\nANISOU 2478  CG  PHE A1153    11993   9932   9541  -1323    479    -73       C\\nATOM   2479  CD1 PHE A1153      22.400 -12.549  33.096  1.00 87.89           C\\nANISOU 2479  CD1 PHE A1153    12840  10494  10062  -1196    348   -140       C\\nATOM   2480  CD2 PHE A1153      22.908 -13.132  35.345  1.00 77.41           C\\nANISOU 2480  CD2 PHE A1153    11425   9126   8862  -1234    685    132       C\\nATOM   2481  CE1 PHE A1153      23.735 -12.650  32.764  1.00 85.44           C\\nANISOU 2481  CE1 PHE A1153    12792  10012   9660   -991    485    -39       C\\nATOM   2482  CE2 PHE A1153      24.244 -13.233  35.021  1.00 77.07           C\\nANISOU 2482  CE2 PHE A1153    11625   8883   8776   -993    759    238       C\\nATOM   2483  CZ  PHE A1153      24.658 -12.992  33.729  1.00 80.39           C\\nANISOU 2483  CZ  PHE A1153    12194   9251   9099   -874    690    135       C\\nATOM   2484  N   ARG A1154      17.484 -11.446  34.817  1.00 88.53           N\\nANISOU 2484  N   ARG A1154    11311  11612  10713  -1783     15   -710       N\\nATOM   2485  CA  ARG A1154      16.070 -11.771  34.679  1.00 90.56           C\\nANISOU 2485  CA  ARG A1154    11175  12087  11146  -2076    -96   -944       C\\nATOM   2486  C   ARG A1154      15.287 -10.657  33.990  1.00 94.08           C\\nANISOU 2486  C   ARG A1154    11255  12736  11753  -1845   -507  -1151       C\\nATOM   2487  O   ARG A1154      14.589 -10.908  33.004  1.00 98.43           O\\nANISOU 2487  O   ARG A1154    11752  13292  12353  -1977   -823  -1290       O\\nATOM   2488  CB  ARG A1154      15.471 -12.072  36.056  1.00 91.66           C\\nANISOU 2488  CB  ARG A1154    10967  12492  11368  -2333    250   -973       C\\nATOM   2489  CG  ARG A1154      13.953 -12.110  36.087  1.00 98.75           C\\nANISOU 2489  CG  ARG A1154    11273  13741  12505  -2600    179  -1261       C\\nATOM   2490  CD  ARG A1154      13.450 -12.527  37.460  1.00 98.15           C\\nANISOU 2490  CD  ARG A1154    10903  13957  12432  -2937    616  -1264       C\\nATOM   2491  NE  ARG A1154      14.141 -11.809  38.526  1.00 96.23           N\\nANISOU 2491  NE  ARG A1154    10691  13830  12042  -2666    855  -1169       N\\nATOM   2492  CZ  ARG A1154      13.729 -10.656  39.043  1.00 99.35           C\\nANISOU 2492  CZ  ARG A1154    10627  14571  12550  -2384    862  -1413       C\\nATOM   2493  NH1 ARG A1154      12.618 -10.085  38.594  1.00102.81           N\\nANISOU 2493  NH1 ARG A1154    10503  15271  13290  -2299    634  -1752       N\\nATOM   2494  NH2 ARG A1154      14.426 -10.074  40.011  1.00 97.58           N\\nANISOU 2494  NH2 ARG A1154    10500  14418  12157  -2171   1067  -1343       N\\nATOM   2495  N   THR A1155      15.394  -9.425  34.492  1.00 91.70           N\\nANISOU 2495  N   THR A1155    10720  12575  11545  -1493   -553  -1180       N\\nATOM   2496  CA  THR A1155      14.626  -8.327  33.913  1.00 95.66           C\\nANISOU 2496  CA  THR A1155    10869  13211  12265  -1227   -991  -1368       C\\nATOM   2497  C   THR A1155      15.189  -7.887  32.570  1.00 97.84           C\\nANISOU 2497  C   THR A1155    11567  13229  12380  -1038  -1391  -1215       C\\nATOM   2498  O   THR A1155      14.426  -7.500  31.678  1.00103.63           O\\nANISOU 2498  O   THR A1155    12148  14011  13216   -975  -1852  -1325       O\\nATOM   2499  CB  THR A1155      14.590  -7.135  34.871  1.00 96.53           C\\nANISOU 2499  CB  THR A1155    10639  13482  12554   -890   -932  -1480       C\\nATOM   2500  OG1 THR A1155      15.865  -6.481  34.875  1.00 89.26           O\\nANISOU 2500  OG1 THR A1155    10139  12306  11469   -624   -926  -1243       O\\nATOM   2501  CG2 THR A1155      14.254  -7.597  36.282  1.00102.13           C\\nANISOU 2501  CG2 THR A1155    11038  14480  13285  -1108   -443  -1599       C\\nATOM   2502  N   GLY A1156      16.506  -7.938  32.402  1.00 98.59           N\\nANISOU 2502  N   GLY A1156    12176  13074  12209   -961  -1232   -958       N\\nATOM   2503  CA  GLY A1156      17.109  -7.426  31.192  1.00 97.17           C\\nANISOU 2503  CA  GLY A1156    12393  12702  11824   -813  -1538   -796       C\\nATOM   2504  C   GLY A1156      17.208  -5.922  31.139  1.00 94.99           C\\nANISOU 2504  C   GLY A1156    12028  12391  11674   -459  -1843   -727       C\\nATOM   2505  O   GLY A1156      17.414  -5.364  30.057  1.00 94.83           O\\nANISOU 2505  O   GLY A1156    12287  12241  11502   -370  -2199   -582       O\\nATOM   2506  N   THR A1157      17.055  -5.243  32.275  1.00 98.59           N\\nANISOU 2506  N   THR A1157    12130  12944  12386   -269  -1724   -831       N\\nATOM   2507  CA  THR A1157      17.188  -3.793  32.334  1.00 99.99           C\\nANISOU 2507  CA  THR A1157    12241  13012  12740     83  -2014   -798       C\\nATOM   2508  C   THR A1157      18.117  -3.396  33.475  1.00 95.58           C\\nANISOU 2508  C   THR A1157    11722  12408  12187    197  -1666   -741       C\\nATOM   2509  O   THR A1157      18.739  -4.258  34.103  1.00 99.83           O\\nANISOU 2509  O   THR A1157    12385  12993  12552     13  -1238   -673       O\\nATOM   2510  CB  THR A1157      15.819  -3.130  32.503  1.00100.53           C\\nANISOU 2510  CB  THR A1157    11744  13243  13210    283  -2359  -1106       C\\nATOM   2511  N   TRP A1158      18.225  -2.094  33.747  1.00 93.22           N\\nANISOU 2511  N   TRP A1158    11337  11987  12095    500  -1890   -770       N\\nATOM   2512  CA  TRP A1158      19.077  -1.577  34.810  1.00 93.29           C\\nANISOU 2512  CA  TRP A1158    11380  11944  12121    611  -1638   -757       C\\nATOM   2513  C   TRP A1158      18.284  -1.180  36.050  1.00100.83           C\\nANISOU 2513  C   TRP A1158    11839  13130  13343    767  -1520  -1143       C\\nATOM   2514  O   TRP A1158      18.687  -0.262  36.773  1.00104.41           O\\nANISOU 2514  O   TRP A1158    12262  13494  13913    976  -1523  -1234       O\\nATOM   2515  CB  TRP A1158      19.888  -0.380  34.315  1.00 93.24           C\\nANISOU 2515  CB  TRP A1158    11675  11603  12148    796  -1939   -534       C\\nATOM   2516  CG  TRP A1158      20.831  -0.689  33.202  1.00 90.86           C\\nANISOU 2516  CG  TRP A1158    11861  11134  11527    615  -1955   -159       C\\nATOM   2517  CD1 TRP A1158      20.661  -0.401  31.878  1.00 92.31           C\\nANISOU 2517  CD1 TRP A1158    12294  11175  11605    591  -2335     30       C\\nATOM   2518  CD2 TRP A1158      22.100  -1.341  33.312  1.00 84.64           C\\nANISOU 2518  CD2 TRP A1158    11359  10335  10467    435  -1569     52       C\\nATOM   2519  NE1 TRP A1158      21.746  -0.835  31.158  1.00 87.61           N\\nANISOU 2519  NE1 TRP A1158    12125  10516  10649    382  -2146    322       N\\nATOM   2520  CE2 TRP A1158      22.643  -1.417  32.015  1.00 81.33           C\\nANISOU 2520  CE2 TRP A1158    11324   9793   9787    307  -1675    322       C\\nATOM   2521  CE3 TRP A1158      22.829  -1.871  34.381  1.00 79.01           C\\nANISOU 2521  CE3 TRP A1158    10605   9715   9699    377  -1161     35       C\\nATOM   2522  CZ2 TRP A1158      23.881  -2.001  31.759  1.00 77.25           C\\nANISOU 2522  CZ2 TRP A1158    11088   9260   9004    149  -1343    521       C\\nATOM   2523  CZ3 TRP A1158      24.059  -2.452  34.124  1.00 69.87           C\\nANISOU 2523  CZ3 TRP A1158     9733   8502   8314    244   -903    268       C\\nATOM   2524  CH2 TRP A1158      24.572  -2.511  32.824  1.00 69.73           C\\nANISOU 2524  CH2 TRP A1158    10033   8375   8085    144   -972    482       C\\nATOM   2525  N   ASP A1159      17.156  -1.850  36.306  1.00 98.45           N\\nANISOU 2525  N   ASP A1159    11135  13138  13133    646  -1402  -1399       N\\nATOM   2526  CA  ASP A1159      16.331  -1.497  37.457  1.00 97.23           C\\nANISOU 2526  CA  ASP A1159    10456  13283  13205    769  -1227  -1814       C\\nATOM   2527  C   ASP A1159      17.098  -1.638  38.765  1.00 90.66           C\\nANISOU 2527  C   ASP A1159     9725  12569  12151    685   -774  -1819       C\\nATOM   2528  O   ASP A1159      16.820  -0.916  39.727  1.00 92.33           O\\nANISOU 2528  O   ASP A1159     9651  12933  12497    879   -679  -2146       O\\nATOM   2529  CB  ASP A1159      15.076  -2.368  37.498  1.00105.69           C\\nANISOU 2529  CB  ASP A1159    11073  14718  14366    540  -1095  -2046       C\\nATOM   2530  CG  ASP A1159      14.329  -2.379  36.182  1.00109.35           C\\nANISOU 2530  CG  ASP A1159    11447  15092  15007    573  -1581  -2031       C\\nATOM   2531  OD1 ASP A1159      14.839  -2.991  35.220  1.00106.95           O\\nANISOU 2531  OD1 ASP A1159    11588  14593  14457    378  -1693  -1714       O\\nATOM   2532  OD2 ASP A1159      13.231  -1.786  36.115  1.00113.68           O\\nANISOU 2532  OD2 ASP A1159    11472  15783  15940    804  -1860  -2361       O\\nATOM   2533  N   ALA A1160      18.061  -2.558  38.822  1.00 90.75           N\\nANISOU 2533  N   ALA A1160    10142  12514  11824    416   -516  -1483       N\\nATOM   2534  CA  ALA A1160      18.793  -2.777  40.062  1.00 83.07           C\\nANISOU 2534  CA  ALA A1160     9285  11661  10616    322   -147  -1445       C\\nATOM   2535  C   ALA A1160      19.805  -1.671  40.330  1.00 83.07           C\\nANISOU 2535  C   ALA A1160     9492  11427  10644    577   -301  -1398       C\\nATOM   2536  O   ALA A1160      20.159  -1.427  41.488  1.00 80.26           O\\nANISOU 2536  O   ALA A1160     9111  11213  10170    595    -98  -1520       O\\nATOM   2537  CB  ALA A1160      19.490  -4.133  40.023  1.00 69.19           C\\nANISOU 2537  CB  ALA A1160     7878   9858   8554     -5    110  -1098       C\\nATOM   2538  N   TYR A1161      20.270  -0.989  39.289  1.00 85.89           N\\nANISOU 2538  N   TYR A1161    10067  11436  11131    737   -663  -1221       N\\nATOM   2539  CA  TYR A1161      21.312   0.021  39.439  1.00 81.29           C\\nANISOU 2539  CA  TYR A1161     9712  10587  10590    902   -820  -1122       C\\nATOM   2540  C   TYR A1161      20.830   1.413  39.031  1.00 86.56           C\\nANISOU 2540  C   TYR A1161    10259  11009  11620   1221  -1257  -1309       C\\nATOM   2541  O   TYR A1161      19.780   1.882  39.473  1.00 90.75           O\\nANISOU 2541  O   TYR A1161    10405  11678  12398   1423  -1325  -1710       O\\nATOM   2542  CB  TYR A1161      22.541  -0.357  38.608  1.00 78.82           C\\nANISOU 2542  CB  TYR A1161     9822  10037  10089    757   -833   -681       C\\nATOM   2543  CG  TYR A1161      23.144  -1.708  38.932  1.00 79.07           C\\nANISOU 2543  CG  TYR A1161    10004  10209   9831    508   -467   -486       C\\nATOM   2544  CD1 TYR A1161      22.612  -2.876  38.400  1.00 78.87           C\\nANISOU 2544  CD1 TYR A1161     9993  10274   9701    320   -342   -427       C\\nATOM   2545  CD2 TYR A1161      24.263  -1.813  39.748  1.00 75.01           C\\nANISOU 2545  CD2 TYR A1161     9629   9697   9174    468   -297   -359       C\\nATOM   2546  CE1 TYR A1161      23.166  -4.110  38.683  1.00 74.50           C\\nANISOU 2546  CE1 TYR A1161     9613   9760   8934    118    -53   -248       C\\nATOM   2547  CE2 TYR A1161      24.824  -3.042  40.039  1.00 67.83           C\\nANISOU 2547  CE2 TYR A1161     8865   8860   8048    288    -30   -162       C\\nATOM   2548  CZ  TYR A1161      24.272  -4.189  39.504  1.00 71.43           C\\nANISOU 2548  CZ  TYR A1161     9359   9354   8428    123     94   -104       C\\nATOM   2549  OH  TYR A1161      24.829  -5.416  39.787  1.00 69.66           O\\nANISOU 2549  OH  TYR A1161     9313   9118   8037    -32    319     91       O\\nATOM   2550  N   SER A 364      17.508   3.047  36.367  1.00104.00           N\\nATOM   2551  CA  SER A 364      18.568   3.670  35.585  1.00104.92           C\\nATOM   2552  C   SER A 364      18.623   3.097  34.167  1.00111.72           C\\nATOM   2553  O   SER A 364      19.675   3.111  33.526  1.00111.66           O\\nATOM   2554  CB  SER A 364      19.919   3.488  36.282  1.00 97.65           C\\nATOM   2555  N   GLN A 365      17.486   2.600  33.682  1.00122.15           N\\nATOM   2556  CA  GLN A 365      17.397   1.937  32.386  1.00115.38           C\\nATOM   2557  C   GLN A 365      16.553   2.767  31.428  1.00110.61           C\\nATOM   2558  O   GLN A 365      15.419   3.137  31.753  1.00 98.43           O\\nATOM   2559  CB  GLN A 365      16.796   0.536  32.527  1.00106.22           C\\nATOM   2560  N   GLN A 366      17.101   3.039  30.246  1.00120.06           N\\nATOM   2561  CA  GLN A 366      16.385   3.791  29.223  1.00115.06           C\\nATOM   2562  C   GLN A 366      15.363   2.887  28.544  1.00110.82           C\\nATOM   2563  O   GLN A 366      15.719   1.836  27.999  1.00106.83           O\\nATOM   2564  CB  GLN A 366      17.364   4.363  28.199  1.00114.61           C\\nATOM   2565  N   LYS A 367      14.097   3.295  28.574  1.00106.95           N\\nATOM   2566  CA  LYS A 367      13.014   2.529  27.974  1.00112.85           C\\nATOM   2567  C   LYS A 367      12.771   2.895  26.516  1.00109.20           C\\nATOM   2568  O   LYS A 367      11.803   2.410  25.921  1.00103.35           O\\nATOM   2569  CB  LYS A 367      11.727   2.721  28.781  1.00115.42           C\\nATOM   2570  N   GLU A 368      13.626   3.733  25.930  1.00114.20           N\\nATOM   2571  CA  GLU A 368      13.436   4.206  24.566  1.00 99.97           C\\nATOM   2572  C   GLU A 368      14.152   3.361  23.525  1.00100.67           C\\nATOM   2573  O   GLU A 368      13.805   3.444  22.342  1.00 97.34           O\\nATOM   2574  CB  GLU A 368      13.920   5.655  24.437  1.00 81.44           C\\nATOM   2575  CG  GLU A 368      13.087   6.681  25.188  1.00 79.48           C\\nATOM   2576  CD  GLU A 368      11.923   7.216  24.368  1.00 87.69           C\\nATOM   2577  OE1 GLU A 368      11.484   6.529  23.419  1.00 87.57           O\\nATOM   2578  OE2 GLU A 368      11.451   8.332  24.674  1.00 90.78           O\\nATOM   2579  N   LYS A 369      15.139   2.557  23.932  1.00101.97           N\\nATOM   2580  CA  LYS A 369      15.965   1.842  22.963  1.00 93.96           C\\nATOM   2581  C   LYS A 369      15.123   0.959  22.051  1.00 87.89           C\\nATOM   2582  O   LYS A 369      15.377   0.886  20.844  1.00 84.82           O\\nATOM   2583  CB  LYS A 369      17.025   1.012  23.689  1.00 94.15           C\\nATOM   2584  N   LYS A 370      14.107   0.291  22.605  1.00 95.07           N\\nATOM   2585  CA  LYS A 370      13.254  -0.567  21.787  1.00 92.51           C\\nATOM   2586  C   LYS A 370      12.587   0.220  20.665  1.00 85.60           C\\nATOM   2587  O   LYS A 370      12.454  -0.280  19.541  1.00 77.93           O\\nATOM   2588  CB  LYS A 370      12.203  -1.254  22.662  1.00 85.65           C\\nATOM   2589  N   ALA A 371      12.167   1.454  20.944  1.00 85.70           N\\nATOM   2590  CA  ALA A 371      11.556   2.271  19.901  1.00 78.85           C\\nATOM   2591  C   ALA A 371      12.589   2.776  18.902  1.00 73.40           C\\nATOM   2592  O   ALA A 371      12.274   2.940  17.718  1.00 67.94           O\\nATOM   2593  CB  ALA A 371      10.805   3.440  20.520  1.00 20.00           C\\nATOM   2594  N   THR A 372      13.820   3.030  19.357  1.00 75.36           N\\nATOM   2595  CA  THR A 372      14.875   3.470  18.451  1.00 64.07           C\\nATOM   2596  C   THR A 372      15.326   2.343  17.535  1.00 71.79           C\\nATOM   2597  O   THR A 372      15.714   2.593  16.389  1.00 80.74           O\\nATOM   2598  CB  THR A 372      16.066   4.010  19.246  1.00 69.33           C\\nATOM   2599  OG1 THR A 372      15.634   5.071  20.104  1.00 74.68           O\\nATOM   2600  CG2 THR A 372      17.138   4.544  18.316  1.00 68.04           C\\nATOM   2601  N   GLN A 373      15.283   1.100  18.019  1.00 68.72           N\\nATOM   2602  CA  GLN A 373      15.663  -0.031  17.180  1.00 79.96           C\\nATOM   2603  C   GLN A 373      14.624  -0.283  16.095  1.00 79.40           C\\nATOM   2604  O   GLN A 373      14.972  -0.633  14.961  1.00 75.09           O\\nATOM   2605  CB  GLN A 373      15.857  -1.276  18.043  1.00 95.27           C\\nATOM   2606  CG  GLN A 373      17.006  -1.162  19.028  1.00107.01           C\\nATOM   2607  CD  GLN A 373      16.835  -2.074  20.228  1.00113.19           C\\nATOM   2608  OE1 GLN A 373      15.768  -2.652  20.438  1.00109.22           O\\nATOM   2609  NE2 GLN A 373      17.889  -2.204  21.025  1.00117.08           N\\nATOM   2610  N   MET A 374      13.345  -0.105  16.421  1.00 79.17           N\\nATOM   2611  CA  MET A 374      12.307  -0.277  15.413  1.00 76.40           C\\nATOM   2612  C   MET A 374      12.384   0.814  14.350  1.00 70.69           C\\nATOM   2613  O   MET A 374      12.182   0.543  13.160  1.00 68.25           O\\nATOM   2614  CB  MET A 374      10.934  -0.292  16.079  1.00 77.49           C\\nATOM   2615  CG  MET A 374       9.801  -0.689  15.153  1.00 81.14           C\\nATOM   2616  SD  MET A 374       8.219  -0.741  16.009  1.00 84.97           S\\nATOM   2617  CE  MET A 374       8.086   0.958  16.565  1.00103.28           C\\nATOM   2618  N   ALA A 375      12.684   2.052  14.756  1.00 72.85           N\\nATOM   2619  CA  ALA A 375      12.789   3.144  13.793  1.00 69.01           C\\nATOM   2620  C   ALA A 375      13.899   2.887  12.783  1.00 71.99           C\\nATOM   2621  O   ALA A 375      13.756   3.203  11.596  1.00 68.65           O\\nATOM   2622  CB  ALA A 375      13.021   4.464  14.513  1.00 20.00           C\\nATOM   2623  N   ALA A 376      15.014   2.312  13.234  1.00 72.30           N\\nATOM   2624  CA  ALA A 376      16.110   2.018  12.320  1.00 74.21           C\\nATOM   2625  C   ALA A 376      15.790   0.830  11.427  1.00 77.19           C\\nATOM   2626  O   ALA A 376      16.261   0.771  10.285  1.00 87.02           O\\nATOM   2627  CB  ALA A 376      17.398   1.765  13.104  1.00 74.32           C\\nATOM   2628  N   ILE A 377      15.001  -0.125  11.921  1.00 87.67           N\\nATOM   2629  CA  ILE A 377      14.633  -1.265  11.089  1.00 95.90           C\\nATOM   2630  C   ILE A 377      13.706  -0.839   9.957  1.00101.03           C\\nATOM   2631  O   ILE A 377      13.826  -1.331   8.830  1.00 92.85           O\\nATOM   2632  CB  ILE A 377      13.963  -2.361  11.939  1.00 20.00           C\\nATOM   2633  CG1 ILE A 377      14.964  -2.954  12.932  1.00 20.00           C\\nATOM   2634  CG2 ILE A 377      13.385  -3.448  11.046  1.00 20.00           C\\nATOM   2635  CD1 ILE A 377      14.332  -3.844  13.978  1.00 20.00           C\\nATOM   2636  N   VAL A 378      12.786   0.088  10.234  1.00 89.06           N\\nATOM   2637  CA  VAL A 378      11.896   0.596   9.192  1.00 75.68           C\\nATOM   2638  C   VAL A 378      12.683   1.387   8.156  1.00 75.18           C\\nATOM   2639  O   VAL A 378      12.445   1.268   6.948  1.00 76.19           O\\nATOM   2640  CB  VAL A 378      10.775   1.445   9.820  1.00 64.00           C\\nATOM   2641  CG1 VAL A 378       9.960   2.132   8.740  1.00 62.64           C\\nATOM   2642  CG2 VAL A 378       9.887   0.580  10.701  1.00 69.48           C\\nATOM   2643  N   ALA A 379      13.629   2.210   8.612  1.00 84.87           N\\nATOM   2644  CA  ALA A 379      14.470   2.963   7.688  1.00 87.10           C\\nATOM   2645  C   ALA A 379      15.330   2.035   6.842  1.00 88.96           C\\nATOM   2646  O   ALA A 379      15.578   2.310   5.662  1.00 81.40           O\\nATOM   2647  CB  ALA A 379      15.348   3.945   8.463  1.00 44.79           C\\nATOM   2648  N   GLY A 380      15.802   0.935   7.428  1.00 77.23           N\\nATOM   2649  CA  GLY A 380      16.620   0.001   6.670  1.00 80.45           C\\nATOM   2650  C   GLY A 380      15.818  -0.749   5.624  1.00 77.59           C\\nATOM   2651  O   GLY A 380      16.246  -0.884   4.475  1.00 69.34           O\\nATOM   2652  N   VAL A 381      14.642  -1.252   6.012  1.00 81.99           N\\nATOM   2653  CA  VAL A 381      13.758  -1.918   5.057  1.00 83.38           C\\nATOM   2654  C   VAL A 381      13.412  -0.978   3.910  1.00 77.79           C\\nATOM   2655  O   VAL A 381      13.311  -1.397   2.751  1.00 66.26           O\\nATOM   2656  CB  VAL A 381      12.494  -2.434   5.772  1.00 76.89           C\\nATOM   2657  CG1 VAL A 381      11.472  -2.937   4.769  1.00 69.18           C\\nATOM   2658  CG2 VAL A 381      12.858  -3.534   6.752  1.00 75.31           C\\nATOM   2659  N   PHE A 382      13.231   0.308   4.214  1.00 79.75           N\\nATOM   2660  CA  PHE A 382      13.014   1.298   3.166  1.00 68.40           C\\nATOM   2661  C   PHE A 382      14.165   1.294   2.171  1.00 73.80           C\\nATOM   2662  O   PHE A 382      13.953   1.186   0.958  1.00 78.38           O\\nATOM   2663  CB  PHE A 382      12.844   2.679   3.796  1.00 62.89           C\\nATOM   2664  CG  PHE A 382      12.514   3.767   2.815  1.00 69.81           C\\nATOM   2665  CD1 PHE A 382      11.203   4.013   2.452  1.00 78.17           C\\nATOM   2666  CD2 PHE A 382      13.513   4.560   2.276  1.00 67.00           C\\nATOM   2667  CE1 PHE A 382      10.895   5.021   1.557  1.00 75.89           C\\nATOM   2668  CE2 PHE A 382      13.211   5.566   1.380  1.00 62.38           C\\nATOM   2669  CZ  PHE A 382      11.900   5.797   1.021  1.00 65.04           C\\nATOM   2670  N   ILE A 383      15.399   1.395   2.672  1.00 79.94           N\\nATOM   2671  CA  ILE A 383      16.564   1.405   1.792  1.00 76.66           C\\nATOM   2672  C   ILE A 383      16.668   0.093   1.027  1.00 74.25           C\\nATOM   2673  O   ILE A 383      17.053   0.072  -0.148  1.00 81.52           O\\nATOM   2674  CB  ILE A 383      17.840   1.702   2.601  1.00 71.78           C\\nATOM   2675  CG1 ILE A 383      17.851   3.163   3.035  1.00 63.66           C\\nATOM   2676  CG2 ILE A 383      19.084   1.400   1.789  1.00 79.30           C\\nATOM   2677  CD1 ILE A 383      17.701   4.126   1.880  1.00 64.10           C\\nATOM   2678  N   ILE A 384      16.309  -1.019   1.668  1.00 77.47           N\\nANISOU 2678  N   ILE A 384    10269   8636  10532   1676   -785   -446       N\\nATOM   2679  CA  ILE A 384      16.346  -2.312   0.990  1.00 77.09           C\\nANISOU 2679  CA  ILE A 384    10626   8415  10249   1786   -743   -487       C\\nATOM   2680  C   ILE A 384      15.395  -2.323  -0.203  1.00 79.25           C\\nANISOU 2680  C   ILE A 384    11068   8660  10381   1476   -652   -397       C\\nATOM   2681  O   ILE A 384      15.699  -2.905  -1.252  1.00 79.85           O\\nANISOU 2681  O   ILE A 384    11325   8712  10302   1540   -544   -477       O\\nATOM   2682  CB  ILE A 384      16.026  -3.439   1.989  1.00 74.75           C\\nANISOU 2682  CB  ILE A 384    10740   7870   9793   1895   -906   -471       C\\nATOM   2683  CG1 ILE A 384      17.200  -3.648   2.941  1.00 77.41           C\\nANISOU 2683  CG1 ILE A 384    10961   8240  10210   2294  -1026   -570       C\\nATOM   2684  CG2 ILE A 384      15.704  -4.737   1.267  1.00 71.60           C\\nANISOU 2684  CG2 ILE A 384    10844   7191   9169   1898   -891   -497       C\\nATOM   2685  CD1 ILE A 384      18.443  -4.186   2.256  1.00 79.90           C\\nANISOU 2685  CD1 ILE A 384    11224   8571  10564   2673   -951   -738       C\\nATOM   2686  N   CYS A 385      14.245  -1.657  -0.076  1.00 75.66           N\\nANISOU 2686  N   CYS A 385    10540   8236   9971   1156   -704   -252       N\\nATOM   2687  CA  CYS A 385      13.214  -1.744  -1.106  1.00 79.40           C\\nANISOU 2687  CA  CYS A 385    11178   8693  10298    856   -690   -152       C\\nATOM   2688  C   CYS A 385      13.483  -0.807  -2.281  1.00 77.99           C\\nANISOU 2688  C   CYS A 385    10754   8710  10168    769   -575    -84       C\\nATOM   2689  O   CYS A 385      13.199  -1.160  -3.432  1.00 80.47           O\\nANISOU 2689  O   CYS A 385    11270   9043  10261    646   -531    -66       O\\nATOM   2690  CB  CYS A 385      11.842  -1.449  -0.500  1.00 80.67           C\\nANISOU 2690  CB  CYS A 385    11312   8841  10500    576   -801    -23       C\\nATOM   2691  SG  CYS A 385      11.235  -2.722   0.645  1.00 83.19           S\\nANISOU 2691  SG  CYS A 385    12017   8939  10653    532   -901    -25       S\\nATOM   2692  N   TRP A 386      14.018   0.384  -2.024  1.00 68.60           N\\nANISOU 2692  N   TRP A 386     9160   7658   9246    804   -535    -37       N\\nATOM   2693  CA  TRP A 386      14.213   1.350  -3.095  1.00 71.32           C\\nANISOU 2693  CA  TRP A 386     9293   8158   9646    667   -432     98       C\\nATOM   2694  C   TRP A 386      15.618   1.346  -3.677  1.00 73.91           C\\nANISOU 2694  C   TRP A 386     9483   8642   9959    842   -227     12       C\\nATOM   2695  O   TRP A 386      15.812   1.874  -4.776  1.00 77.41           O\\nANISOU 2695  O   TRP A 386     9849   9237  10328    705    -92    139       O\\nATOM   2696  CB  TRP A 386      13.885   2.767  -2.612  1.00 68.85           C\\nANISOU 2696  CB  TRP A 386     8631   7857   9670    543   -510    230       C\\nATOM   2697  CG  TRP A 386      12.415   3.071  -2.565  1.00 72.68           C\\nANISOU 2697  CG  TRP A 386     9161   8279  10174    338   -661    365       C\\nATOM   2698  CD1 TRP A 386      11.648   3.236  -1.448  1.00 67.00           C\\nANISOU 2698  CD1 TRP A 386     8370   7494   9594    332   -777    320       C\\nATOM   2699  CD2 TRP A 386      11.534   3.244  -3.684  1.00 78.89           C\\nANISOU 2699  CD2 TRP A 386    10042   9108  10823    121   -715    558       C\\nATOM   2700  NE1 TRP A 386      10.348   3.502  -1.801  1.00 70.95           N\\nANISOU 2700  NE1 TRP A 386     8865   8000  10093    139   -882    461       N\\nATOM   2701  CE2 TRP A 386      10.251   3.512  -3.168  1.00 76.55           C\\nANISOU 2701  CE2 TRP A 386     9677   8767  10641      9   -876    617       C\\nATOM   2702  CE3 TRP A 386      11.706   3.200  -5.072  1.00 78.88           C\\nANISOU 2702  CE3 TRP A 386    10168   9215  10586     17   -646    682       C\\nATOM   2703  CZ2 TRP A 386       9.146   3.736  -3.988  1.00 75.36           C\\nANISOU 2703  CZ2 TRP A 386     9547   8666  10419   -188  -1008    800       C\\nATOM   2704  CZ3 TRP A 386      10.606   3.421  -5.885  1.00 78.84           C\\nANISOU 2704  CZ3 TRP A 386    10240   9252  10462   -196   -791    875       C\\nATOM   2705  CH2 TRP A 386       9.343   3.684  -5.340  1.00 78.30           C\\nANISOU 2705  CH2 TRP A 386    10069   9128  10555   -289   -989    935       C\\nATOM   2706  N   LEU A 387      16.599   0.779  -2.986  1.00 71.16           N\\nANISOU 2706  N   LEU A 387     9082   8289   9666   1138   -199   -185       N\\nATOM   2707  CA  LEU A 387      17.963   0.908  -3.486  1.00 77.39           C\\nANISOU 2707  CA  LEU A 387     9613   9290  10501   1307     10   -275       C\\nATOM   2708  C   LEU A 387      18.178   0.130  -4.783  1.00 81.59           C\\nANISOU 2708  C   LEU A 387    10394   9919  10687   1358    212   -346       C\\nATOM   2709  O   LEU A 387      18.816   0.661  -5.701  1.00 86.35           O\\nANISOU 2709  O   LEU A 387    10786  10774  11250   1288    442   -288       O\\nATOM   2710  CB  LEU A 387      18.985   0.473  -2.436  1.00 76.08           C\\nANISOU 2710  CB  LEU A 387     9284   9129  10492   1656    -47   -481       C\\nATOM   2711  CG  LEU A 387      20.393   0.933  -2.792  1.00 73.95           C\\nANISOU 2711  CG  LEU A 387     8566   9145  10385   1779    152   -557       C\\nATOM   2712  CD1 LEU A 387      20.380   2.425  -3.067  1.00 70.62           C\\nANISOU 2712  CD1 LEU A 387     7792   8838  10202   1432    210   -352       C\\nATOM   2713  CD2 LEU A 387      21.363   0.599  -1.677  1.00 74.27           C\\nANISOU 2713  CD2 LEU A 387     8384   9220  10617   2125     25   -752       C\\nATOM   2714  N   PRO A 388      17.692  -1.112  -4.913  1.00 79.42           N\\nANISOU 2714  N   PRO A 388    10576   9454  10144   1463    148   -479       N\\nATOM   2715  CA  PRO A 388      17.785  -1.780  -6.223  1.00 83.37           C\\nANISOU 2715  CA  PRO A 388    11355  10040  10283   1481    328   -585       C\\nATOM   2716  C   PRO A 388      17.190  -0.967  -7.356  1.00 88.60           C\\nANISOU 2716  C   PRO A 388    12005  10889  10771   1117    400   -357       C\\nATOM   2717  O   PRO A 388      17.670  -1.054  -8.493  1.00 89.35           O\\nANISOU 2717  O   PRO A 388    12143  11216  10591   1123    637   -407       O\\nATOM   2718  CB  PRO A 388      17.015  -3.085  -5.998  1.00 78.09           C\\nANISOU 2718  CB  PRO A 388    11219   9031   9418   1534    148   -722       C\\nATOM   2719  CG  PRO A 388      17.214  -3.371  -4.563  1.00 73.10           C\\nANISOU 2719  CG  PRO A 388    10537   8200   9037   1742    -22   -758       C\\nATOM   2720  CD  PRO A 388      17.196  -2.039  -3.878  1.00 74.29           C\\nANISOU 2720  CD  PRO A 388    10229   8503   9495   1588    -73   -564       C\\nATOM   2721  N   PHE A 389      16.157  -0.168  -7.077  1.00 87.86           N\\nANISOU 2721  N   PHE A 389    11851  10717  10815    821    202   -105       N\\nATOM   2722  CA  PHE A 389      15.588   0.699  -8.103  1.00 88.83           C\\nANISOU 2722  CA  PHE A 389    11946  10997  10808    504    215    164       C\\nATOM   2723  C   PHE A 389      16.581   1.776  -8.524  1.00 87.11           C\\nANISOU 2723  C   PHE A 389    11342  11030  10726    460    445    317       C\\nATOM   2724  O   PHE A 389      16.791   2.009  -9.719  1.00 91.58           O\\nANISOU 2724  O   PHE A 389    11960  11831  11005    327    627    435       O\\nATOM   2725  CB  PHE A 389      14.287   1.323  -7.592  1.00 81.78           C\\nANISOU 2725  CB  PHE A 389    11019   9946  10106    271    -69    378       C\\nATOM   2726  CG  PHE A 389      13.670   2.319  -8.536  1.00 78.75           C\\nANISOU 2726  CG  PHE A 389    10580   9686   9656    -11   -125    698       C\\nATOM   2727  CD1 PHE A 389      12.947   1.897  -9.638  1.00 72.20           C\\nANISOU 2727  CD1 PHE A 389    10065   8946   8421   -182   -197    758       C\\nATOM   2728  CD2 PHE A 389      13.795   3.677  -8.309  1.00 74.32           C\\nANISOU 2728  CD2 PHE A 389     9675   9124   9438   -104   -142    940       C\\nATOM   2729  CE1 PHE A 389      12.374   2.812 -10.501  1.00 66.21           C\\nANISOU 2729  CE1 PHE A 389     9270   8308   7580   -418   -296   1089       C\\nATOM   2730  CE2 PHE A 389      13.221   4.593  -9.169  1.00 73.66           C\\nANISOU 2730  CE2 PHE A 389     9576   9102   9309   -336   -229   1275       C\\nATOM   2731  CZ  PHE A 389      12.508   4.160 -10.263  1.00 67.96           C\\nANISOU 2731  CZ  PHE A 389     9160   8501   8161   -483   -313   1367       C\\nATOM   2732  N   PHE A 390      17.211   2.438  -7.553  1.00 78.28           N\\nANISOU 2732  N   PHE A 390     9842   9876  10022    542    440    319       N\\nATOM   2733  CA  PHE A 390      18.154   3.503  -7.865  1.00 77.80           C\\nANISOU 2733  CA  PHE A 390     9387  10020  10154    435    640    473       C\\nATOM   2734  C   PHE A 390      19.520   2.977  -8.285  1.00 85.50           C\\nANISOU 2734  C   PHE A 390    10201  11281  11003    650    968    266       C\\nATOM   2735  O   PHE A 390      20.266   3.699  -8.955  1.00 80.65           O\\nANISOU 2735  O   PHE A 390     9313  10928  10401    495   1220    418       O\\nATOM   2736  CB  PHE A 390      18.290   4.441  -6.666  1.00 72.78           C\\nANISOU 2736  CB  PHE A 390     8403   9227  10023    409    479    515       C\\nATOM   2737  CG  PHE A 390      17.046   5.229  -6.384  1.00 71.97           C\\nANISOU 2737  CG  PHE A 390     8367   8891  10086    201    217    731       C\\nATOM   2738  CD1 PHE A 390      16.770   6.384  -7.095  1.00 73.92           C\\nANISOU 2738  CD1 PHE A 390     8531   9132  10422    -77    215   1066       C\\nATOM   2739  CD2 PHE A 390      16.146   4.810  -5.423  1.00 69.40           C\\nANISOU 2739  CD2 PHE A 390     8185   8358   9824    295    -21    611       C\\nATOM   2740  CE1 PHE A 390      15.624   7.110  -6.848  1.00 69.85           C\\nANISOU 2740  CE1 PHE A 390     8056   8392  10093   -202    -42   1247       C\\nATOM   2741  CE2 PHE A 390      14.995   5.533  -5.171  1.00 69.17           C\\nANISOU 2741  CE2 PHE A 390     8161   8162   9960    142   -234    777       C\\nATOM   2742  CZ  PHE A 390      14.735   6.685  -5.884  1.00 63.89           C\\nANISOU 2742  CZ  PHE A 390     7389   7471   9415    -78   -256   1080       C\\nATOM   2743  N   ILE A 391      19.865   1.744  -7.905  1.00 83.05           N\\nANISOU 2743  N   ILE A 391    10043  10926  10586   1005    976    -67       N\\nATOM   2744  CA  ILE A 391      21.044   1.100  -8.477  1.00 88.93           C\\nANISOU 2744  CA  ILE A 391    10677  11954  11158   1273   1299   -305       C\\nATOM   2745  C   ILE A 391      20.854   0.907  -9.975  1.00 91.28           C\\nANISOU 2745  C   ILE A 391    11243  12480  10960   1127   1541   -254       C\\nATOM   2746  O   ILE A 391      21.789   1.084 -10.766  1.00 94.74           O\\nANISOU 2746  O   ILE A 391    11451  13294  11253   1139   1904   -276       O\\nATOM   2747  CB  ILE A 391      21.321  -0.238  -7.761  1.00 85.00           C\\nANISOU 2747  CB  ILE A 391    10370  11271  10655   1728   1197   -664       C\\nATOM   2748  CG1 ILE A 391      21.803   0.004  -6.329  1.00 81.99           C\\nANISOU 2748  CG1 ILE A 391     9657  10782  10715   1901    995   -715       C\\nATOM   2749  CG2 ILE A 391      22.336  -1.068  -8.534  1.00 85.18           C\\nANISOU 2749  CG2 ILE A 391    10376  11551  10438   2063   1525   -960       C\\nATOM   2750  CD1 ILE A 391      22.006  -1.268  -5.531  1.00 79.71           C\\nANISOU 2750  CD1 ILE A 391     9598  10266  10423   2344    833   -991       C\\nATOM   2751  N   THR A 392      19.633   0.564 -10.388  1.00 91.03           N\\nANISOU 2751  N   THR A 392    11682  12262  10642    965   1345   -183       N\\nATOM   2752  CA  THR A 392      19.347   0.341 -11.801  1.00 92.03           C\\nANISOU 2752  CA  THR A 392    12124  12607  10236    813   1511   -151       C\\nATOM   2753  C   THR A 392      19.510   1.622 -12.611  1.00 96.64           C\\nANISOU 2753  C   THR A 392    12473  13487  10758    456   1684    247       C\\nATOM   2754  O   THR A 392      19.972   1.585 -13.759  1.00 99.51           O\\nANISOU 2754  O   THR A 392    12896  14212  10701    394   2002    256       O\\nATOM   2755  CB  THR A 392      17.934  -0.222 -11.949  1.00 85.65           C\\nANISOU 2755  CB  THR A 392    11821  11527   9195    670   1183   -144       C\\nATOM   2756  OG1 THR A 392      17.843  -1.462 -11.238  1.00 86.36           O\\nANISOU 2756  OG1 THR A 392    12169  11313   9330    965   1047   -489       O\\nATOM   2757  CG2 THR A 392      17.589  -0.458 -13.404  1.00 82.50           C\\nANISOU 2757  CG2 THR A 392    11776  11367   8203    498   1292   -131       C\\nATOM   2758  N   HIS A 393      19.187   2.742 -12.031  1.00 88.71           N\\nANISOU 2758  N   HIS A 393    11226  12324  10155    219   1485    579       N\\nATOM   2759  CA  HIS A 393      19.363   3.957 -12.738  1.00 88.98           C\\nANISOU 2759  CA  HIS A 393    11056  12550  10202   -130   1618   1001       C\\nATOM   2760  C   HIS A 393      20.809   4.181 -13.033  1.00 88.31           C\\nANISOU 2760  C   HIS A 393    10554  12829  10172   -105   2051    965       C\\nATOM   2761  O   HIS A 393      21.145   4.651 -14.071  1.00 90.40           O\\nANISOU 2761  O   HIS A 393    10759  13392  10197   -381   2313   1255       O\\nATOM   2762  CB  HIS A 393      18.863   5.074 -11.893  1.00 92.81           C\\nANISOU 2762  CB  HIS A 393    11357  12712  11192   -324   1304   1294       C\\nATOM   2763  CG  HIS A 393      17.412   5.334 -12.064  1.00 96.38           C\\nANISOU 2763  CG  HIS A 393    12141  12922  11557   -443    932   1454       C\\nATOM   2764  ND1 HIS A 393      16.815   5.355 -13.296  1.00101.35           N\\nANISOU 2764  ND1 HIS A 393    12985  13642  11882   -712    860   1815       N\\nATOM   2765  CD2 HIS A 393      16.440   5.591 -11.168  1.00 93.09           C\\nANISOU 2765  CD2 HIS A 393    11851  12212  11307   -333    611   1312       C\\nATOM   2766  CE1 HIS A 393      15.536   5.622 -13.155  1.00 98.51           C\\nANISOU 2766  CE1 HIS A 393    12830  13059  11540   -744    489   1868       C\\nATOM   2767  NE2 HIS A 393      15.282   5.762 -11.872  1.00 93.35           N\\nANISOU 2767  NE2 HIS A 393    12117  12180  11171   -533    357   1563       N\\nATOM   2768  N   ILE A 394      21.675   3.869 -12.094  1.00 95.53           N\\nANISOU 2768  N   ILE A 394    11157  13746  11395    209   2124    635       N\\nATOM   2769  CA  ILE A 394      23.103   4.065 -12.304  1.00100.46           C\\nANISOU 2769  CA  ILE A 394    11300  14765  12104    258   2532    556       C\\nATOM   2770  C   ILE A 394      23.590   3.234 -13.480  1.00110.00           C\\nANISOU 2770  C   ILE A 394    12669  16389  12736    410   2939    349       C\\nATOM   2771  O   ILE A 394      24.530   3.628 -14.181  1.00116.65           O\\nANISOU 2771  O   ILE A 394    13187  17679  13455    283   3367    434       O\\nATOM   2772  CB  ILE A 394      23.876   3.735 -11.014  1.00 95.87           C\\nANISOU 2772  CB  ILE A 394    10335  14092  12001    599   2436    239       C\\nATOM   2773  N   LEU A 395      22.959   2.084 -13.726  1.00109.05           N\\nANISOU 2773  N   LEU A 395    13051  16136  12246    661   2828     65       N\\nATOM   2774  CA  LEU A 395      23.384   1.213 -14.816  1.00115.80           C\\nANISOU 2774  CA  LEU A 395    14119  17349  12533    853   3195   -221       C\\nATOM   2775  C   LEU A 395      22.911   1.731 -16.169  1.00123.98           C\\nANISOU 2775  C   LEU A 395    15434  18666  13007    451   3352    106       C\\nATOM   2776  O   LEU A 395      23.622   1.591 -17.170  1.00132.70           O\\nANISOU 2776  O   LEU A 395    16488  20259  13673    459   3812     22       O\\nATOM   2777  CB  LEU A 395      22.873  -0.208 -14.578  1.00113.04           C\\nANISOU 2777  CB  LEU A 395    14254  16684  12011   1243   2983   -662       C\\nATOM   2778  CG  LEU A 395      23.285  -0.827 -13.242  1.00107.58           C\\nANISOU 2778  CG  LEU A 395    13379  15684  11813   1666   2788   -952       C\\nATOM   2779  CD1 LEU A 395      22.874  -2.287 -13.174  1.00109.94           C\\nANISOU 2779  CD1 LEU A 395    14213  15663  11896   2035   2631  -1369       C\\nATOM   2780  CD2 LEU A 395      24.782  -0.681 -13.009  1.00102.89           C\\nANISOU 2780  CD2 LEU A 395    12151  15454  11490   1927   3132  -1110       C\\nATOM   2781  N   ASN A 396      21.713   2.324 -16.219  1.00120.69           N\\nANISOU 2781  N   ASN A 396    15306  17974  12576    116   2975    478       N\\nATOM   2782  CA  ASN A 396      21.242   2.943 -17.454  1.00120.58           C\\nANISOU 2782  CA  ASN A 396    15547  18214  12053   -278   3052    871       C\\nATOM   2783  C   ASN A 396      22.194   4.031 -17.930  1.00122.42           C\\nANISOU 2783  C   ASN A 396    15355  18837  12322   -573   3455   1241       C\\nATOM   2784  O   ASN A 396      22.387   4.205 -19.139  1.00125.81           O\\nANISOU 2784  O   ASN A 396    15933  19697  12171   -784   3770   1420       O\\nATOM   2785  CB  ASN A 396      19.841   3.523 -17.251  1.00116.75           C\\nANISOU 2785  CB  ASN A 396    15328  17340  11693   -546   2527   1239       C\\nATOM   2786  CG  ASN A 396      18.760   2.676 -17.888  1.00117.94           C\\nANISOU 2786  CG  ASN A 396    16062  17433  11316   -534   2274   1087       C\\nATOM   2787  OD1 ASN A 396      18.987   1.516 -18.228  1.00121.59           O\\nANISOU 2787  OD1 ASN A 396    16780  18007  11413   -276   2424    626       O\\nATOM   2788  ND2 ASN A 396      17.576   3.253 -18.057  1.00116.24           N\\nANISOU 2788  ND2 ASN A 396    16052  17032  11079   -807   1870   1457       N\\nATOM   2789  N   ILE A 397      22.806   4.760 -16.997  1.00128.30           N\\nANISOU 2789  N   ILE A 397    15581  19448  13721   -619   3450   1356       N\\nATOM   2790  CA  ILE A 397      23.706   5.849 -17.357  1.00131.63           C\\nANISOU 2790  CA  ILE A 397    15568  20182  14265   -972   3805   1730       C\\nATOM   2791  C   ILE A 397      25.103   5.322 -17.667  1.00137.13           C\\nANISOU 2791  C   ILE A 397    15858  21427  14818   -764   4380   1392       C\\nATOM   2792  O   ILE A 397      25.789   5.839 -18.556  1.00140.52           O\\nANISOU 2792  O   ILE A 397    16093  22338  14959  -1056   4838   1642       O\\nATOM   2793  CB  ILE A 397      23.731   6.896 -16.228  1.00123.72           C\\nANISOU 2793  CB  ILE A 397    14191  18774  14042  -1149   3517   1971       C\\nATOM   2794  CG1 ILE A 397      22.331   7.473 -16.007  1.00113.56           C\\nANISOU 2794  CG1 ILE A 397    13280  16985  12883  -1327   2987   2301       C\\nATOM   2795  CG2 ILE A 397      24.735   8.002 -16.530  1.00125.40           C\\nANISOU 2795  CG2 ILE A 397    13930  19262  14453  -1557   3873   2337       C\\nATOM   2796  CD1 ILE A 397      22.251   8.459 -14.860  1.00102.21           C\\nANISOU 2796  CD1 ILE A 397    11537  15104  12195  -1449   2680   2462       C\\nATOM   2797  N   HIS A 398      25.537   4.278 -16.959  1.00136.75           N\\nANISOU 2797  N   HIS A 398    15674  21329  14958   -248   4372    832       N\\nATOM   2798  CA  HIS A 398      26.930   3.846 -17.033  1.00140.25           C\\nANISOU 2798  CA  HIS A 398    15599  22260  15431     23   4867    485       C\\nATOM   2799  C   HIS A 398      27.250   3.199 -18.376  1.00154.68           C\\nANISOU 2799  C   HIS A 398    17644  24638  16490    117   5371    293       C\\nATOM   2800  O   HIS A 398      28.121   3.674 -19.114  1.00162.37           O\\nANISOU 2800  O   HIS A 398    18256  26184  17254   -111   5901    448       O\\nATOM   2801  CB  HIS A 398      27.240   2.881 -15.886  1.00132.50           C\\nANISOU 2801  CB  HIS A 398    14462  21019  14861    602   4649    -39       C\\nATOM   2802  N   CYS A 399      26.570   2.103 -18.707  1.00157.99           N\\nANISOU 2802  N   CYS A 399    18652  24908  16468    436   5229    -65       N\\nATOM   2803  CA  CYS A 399      26.929   1.309 -19.875  1.00171.19           C\\nANISOU 2803  CA  CYS A 399    20554  27077  17414    635   5693   -403       C\\nATOM   2804  C   CYS A 399      25.915   1.388 -21.006  1.00172.38           C\\nANISOU 2804  C   CYS A 399    21379  27292  16826    306   5614   -163       C\\nATOM   2805  O   CYS A 399      26.152   0.799 -22.069  1.00171.94           O\\nANISOU 2805  O   CYS A 399    21574  27683  16070    417   5999   -433       O\\nATOM   2806  CB  CYS A 399      27.145  -0.157 -19.472  1.00177.68           C\\nANISOU 2806  CB  CYS A 399    21527  27720  18264   1324   5648  -1118       C\\nATOM   2807  SG  CYS A 399      25.689  -1.129 -18.956  1.00177.65           S\\nANISOU 2807  SG  CYS A 399    22318  26935  18245   1520   4957  -1341       S\\nATOM   2808  N   ASP A 400      24.802   2.093 -20.815  1.00169.42           N\\nANISOU 2808  N   ASP A 400    21292  26506  16572    -73   5118    313       N\\nATOM   2809  CA  ASP A 400      23.708   2.176 -21.779  1.00172.19           C\\nANISOU 2809  CA  ASP A 400    22278  26866  16282   -369   4909    565       C\\nATOM   2810  C   ASP A 400      23.130   0.810 -22.126  1.00178.49           C\\nANISOU 2810  C   ASP A 400    23661  27552  16606    -24   4760      1       C\\nATOM   2811  O   ASP A 400      22.354   0.694 -23.084  1.00180.90           O\\nANISOU 2811  O   ASP A 400    24500  27979  16254   -230   4642     91       O\\nATOM   2812  CB  ASP A 400      24.139   2.903 -23.061  1.00174.58           C\\nANISOU 2812  CB  ASP A 400    22570  27804  15958   -772   5382    965       C\\nATOM   2813  N   CYS A 401      23.494  -0.229 -21.377  1.00180.63           N\\nANISOU 2813  N   CYS A 401    23862  27575  17194    489   4738   -576       N\\nATOM   2814  CA  CYS A 401      22.923  -1.551 -21.583  1.00179.00           C\\nANISOU 2814  CA  CYS A 401    24242  27130  16641    806   4543  -1120       C\\nATOM   2815  C   CYS A 401      21.440  -1.519 -21.252  1.00170.63           C\\nANISOU 2815  C   CYS A 401    23622  25538  15671    556   3881   -897       C\\nATOM   2816  O   CYS A 401      21.063  -1.243 -20.109  1.00166.40           O\\nANISOU 2816  O   CYS A 401    22893  24541  15789    548   3513   -729       O\\nATOM   2817  CB  CYS A 401      23.624  -2.583 -20.701  1.00179.14           C\\nANISOU 2817  CB  CYS A 401    24079  26891  17096   1410   4598  -1700       C\\nATOM   2818  SG  CYS A 401      25.421  -2.457 -20.478  1.00183.37           S\\nANISOU 2818  SG  CYS A 401    23801  27930  17940   1774   5237  -1908       S\\nATOM   2819  N   ASN A 402      20.597  -1.793 -22.244  1.00163.09           N\\nANISOU 2819  N   ASN A 402    23235  24683  14049    348   3727   -908       N\\nATOM   2820  CA  ASN A 402      19.171  -1.877 -21.964  1.00152.09           C\\nANISOU 2820  CA  ASN A 402    22222  22828  12736    126   3092   -755       C\\nATOM   2821  C   ASN A 402      18.914  -3.031 -21.004  1.00144.87           C\\nANISOU 2821  C   ASN A 402    21476  21352  12215    479   2819  -1242       C\\nATOM   2822  O   ASN A 402      19.334  -4.167 -21.242  1.00148.09           O\\nANISOU 2822  O   ASN A 402    22151  21737  12380    836   2997  -1823       O\\nATOM   2823  CB  ASN A 402      18.364  -2.039 -23.255  1.00153.00           C\\nANISOU 2823  CB  ASN A 402    22907  23202  12025   -153   2955   -727       C\\nATOM   2824  CG  ASN A 402      18.644  -3.344 -23.970  1.00154.48           C\\nANISOU 2824  CG  ASN A 402    23550  23525  11619    142   3169  -1424       C\\nATOM   2825  OD1 ASN A 402      18.048  -4.376 -23.657  1.00152.23           O\\nANISOU 2825  OD1 ASN A 402    23645  22801  11394    294   2842  -1846       O\\nATOM   2826  ND2 ASN A 402      19.540  -3.303 -24.949  1.00156.47           N\\nANISOU 2826  ND2 ASN A 402    23784  24383  11285    209   3730  -1554       N\\nATOM   2827  N   ILE A 403      18.259  -2.719 -19.893  1.00137.95           N\\nANISOU 2827  N   ILE A 403    20445  20015  11956    389   2403   -999       N\\nATOM   2828  CA  ILE A 403      18.056  -3.664 -18.801  1.00126.08           C\\nANISOU 2828  CA  ILE A 403    19041  17968  10897    679   2150  -1342       C\\nATOM   2829  C   ILE A 403      16.725  -4.370 -19.025  1.00123.67           C\\nANISOU 2829  C   ILE A 403    19300  17348  10341    476   1691  -1463       C\\nATOM   2830  O   ILE A 403      15.774  -3.737 -19.506  1.00123.23           O\\nANISOU 2830  O   ILE A 403    19345  17396  10082     73   1419  -1099       O\\nATOM   2831  CB  ILE A 403      18.121  -2.936 -17.448  1.00116.57           C\\nANISOU 2831  CB  ILE A 403    17344  16498  10450    680   1990  -1029       C\\nATOM   2832  CG1 ILE A 403      19.571  -2.545 -17.154  1.00117.76           C\\nANISOU 2832  CG1 ILE A 403    16950  16923  10871    944   2430  -1064       C\\nATOM   2833  CG2 ILE A 403      17.524  -3.771 -16.324  1.00111.83           C\\nANISOU 2833  CG2 ILE A 403    16927  15326  10238    834   1619  -1235       C\\nATOM   2834  CD1 ILE A 403      19.744  -1.682 -15.938  1.00115.05           C\\nANISOU 2834  CD1 ILE A 403    16103  16396  11214    903   2293   -760       C\\nATOM   2835  N   PRO A 404      16.628  -5.671 -18.745  1.00118.90           N\\nANISOU 2835  N   PRO A 404    19074  16363   9738    731   1581  -1960       N\\nATOM   2836  CA  PRO A 404      15.360  -6.387 -18.918  1.00118.90           C\\nANISOU 2836  CA  PRO A 404    19598  16036   9542    479   1130  -2089       C\\nATOM   2837  C   PRO A 404      14.199  -5.600 -18.342  1.00114.46           C\\nANISOU 2837  C   PRO A 404    18849  15327   9312     80    700  -1589       C\\nATOM   2838  O   PRO A 404      14.149  -5.345 -17.130  1.00111.06           O\\nANISOU 2838  O   PRO A 404    18106  14611   9479    144    589  -1414       O\\nATOM   2839  CB  PRO A 404      15.590  -7.690 -18.142  1.00118.42           C\\nANISOU 2839  CB  PRO A 404    19799  15435   9759    841   1069  -2563       C\\nATOM   2840  CG  PRO A 404      17.050  -7.938 -18.305  1.00121.83           C\\nANISOU 2840  CG  PRO A 404    20054  16085  10152   1347   1569  -2883       C\\nATOM   2841  CD  PRO A 404      17.718  -6.580 -18.344  1.00119.79           C\\nANISOU 2841  CD  PRO A 404    19169  16331  10014   1271   1867  -2444       C\\nATOM   2842  N   PRO A 405      13.257  -5.175 -19.187  1.00111.48           N\\nANISOU 2842  N   PRO A 405    18639  15168   8549   -316    448  -1354       N\\nATOM   2843  CA  PRO A 405      12.126  -4.381 -18.686  1.00109.02           C\\nANISOU 2843  CA  PRO A 405    18100  14751   8571   -653     36   -886       C\\nATOM   2844  C   PRO A 405      11.320  -5.093 -17.621  1.00107.40           C\\nANISOU 2844  C   PRO A 405    17974  14039   8792   -700   -301  -1012       C\\nATOM   2845  O   PRO A 405      10.656  -4.425 -16.820  1.00106.74           O\\nANISOU 2845  O   PRO A 405    17562  13840   9155   -851   -528   -666       O\\nATOM   2846  CB  PRO A 405      11.292  -4.119 -19.948  1.00110.35           C\\nANISOU 2846  CB  PRO A 405    18539  15248   8141  -1009   -207   -731       C\\nATOM   2847  CG  PRO A 405      11.691  -5.197 -20.899  1.00113.76           C\\nANISOU 2847  CG  PRO A 405    19491  15789   7942   -900    -38  -1264       C\\nATOM   2848  CD  PRO A 405      13.141  -5.456 -20.627  1.00117.16           C\\nANISOU 2848  CD  PRO A 405    19780  16246   8490   -452    496  -1536       C\\nATOM   2849  N   VAL A 406      11.356  -6.428 -17.580  1.00111.87           N\\nANISOU 2849  N   VAL A 406    18978  14290   9236   -579   -329  -1496       N\\nATOM   2850  CA  VAL A 406      10.738  -7.139 -16.469  1.00102.56           C\\nANISOU 2850  CA  VAL A 406    17881  12600   8486   -624   -592  -1581       C\\nATOM   2851  C   VAL A 406      11.508  -6.882 -15.181  1.00104.10           C\\nANISOU 2851  C   VAL A 406    17697  12610   9246   -300   -398  -1479       C\\nATOM   2852  O   VAL A 406      10.926  -6.894 -14.090  1.00102.17           O\\nANISOU 2852  O   VAL A 406    17313  12081   9424   -395   -602  -1324       O\\nATOM   2853  CB  VAL A 406      10.640  -8.644 -16.776  1.00 94.49           C\\nANISOU 2853  CB  VAL A 406    17480  11217   7203   -584   -680  -2114       C\\nATOM   2854  N   LEU A 407      12.818  -6.639 -15.277  1.00103.82           N\\nANISOU 2854  N   LEU A 407    17468  12769   9209     74     -3  -1567       N\\nATOM   2855  CA  LEU A 407      13.592  -6.296 -14.089  1.00100.38           C\\nANISOU 2855  CA  LEU A 407    16623  12220   9296    369    146  -1462       C\\nATOM   2856  C   LEU A 407      13.390  -4.838 -13.698  1.00 94.26           C\\nANISOU 2856  C   LEU A 407    15315  11675   8824    182    114   -975       C\\nATOM   2857  O   LEU A 407      13.200  -4.533 -12.516  1.00 88.29           O\\nANISOU 2857  O   LEU A 407    14299  10718   8529    200     -8   -812       O\\nATOM   2858  CB  LEU A 407      15.077  -6.584 -14.317  1.00101.90           C\\nANISOU 2858  CB  LEU A 407    16737  12562   9418    837    561  -1755       C\\nATOM   2859  N   TYR A 408      13.370  -3.956 -14.650  1.00 94.06           N\\nANISOU 2859  N   TYR A 408    15152  12055   8531      5    218   -738       N\\nATOM   2860  CA  TYR A 408      13.143  -2.599 -14.299  1.00 92.67           C\\nANISOU 2860  CA  TYR A 408    14536  12021   8655   -189    141   -264       C\\nATOM   2861  C   TYR A 408      11.764  -2.493 -13.713  1.00 95.64           C\\nANISOU 2861  C   TYR A 408    14901  12179   9258   -462   -278    -65       C\\nATOM   2862  O   TYR A 408      11.578  -1.795 -12.766  1.00 92.85           O\\nANISOU 2862  O   TYR A 408    14175  11751   9352   -489   -366    194       O\\nATOM   2863  CB  TYR A 408      13.263  -1.746 -15.521  1.00 92.66           C\\nANISOU 2863  CB  TYR A 408    14496  12449   8263   -369    283     -7       C\\nATOM   2864  CG  TYR A 408      13.909  -0.444 -15.274  1.00 92.93           C\\nANISOU 2864  CG  TYR A 408    14043  12651   8617   -377    472    359       C\\nATOM   2865  CD1 TYR A 408      13.694   0.227 -14.129  1.00 88.51           C\\nANISOU 2865  CD1 TYR A 408    13122  11858   8651   -379    316    564       C\\nATOM   2866  CD2 TYR A 408      14.725   0.122 -16.199  1.00 98.66           C\\nANISOU 2866  CD2 TYR A 408    14681  13767   9040   -406    819    487       C\\nATOM   2867  CE1 TYR A 408      14.287   1.434 -13.904  1.00 87.26           C\\nANISOU 2867  CE1 TYR A 408    12549  11797   8809   -413    462    866       C\\nATOM   2868  CE2 TYR A 408      15.323   1.331 -15.973  1.00 98.99           C\\nANISOU 2868  CE2 TYR A 408    14288  13921   9401   -474    985    837       C\\nATOM   2869  CZ  TYR A 408      15.086   1.974 -14.814  1.00 95.40           C\\nANISOU 2869  CZ  TYR A 408    13502  13174   9570   -479    786   1014       C\\nATOM   2870  OH  TYR A 408      15.640   3.178 -14.533  1.00 98.94           O\\nANISOU 2870  OH  TYR A 408    13550  13681  10361   -572    923   1329       O\\nATOM   2871  N   SER A 409      10.781  -3.173 -14.278  1.00105.38           N\\nANISOU 2871  N   SER A 409    16521  13320  10198   -667   -536   -211       N\\nATOM   2872  CA  SER A 409       9.431  -3.119 -13.727  1.00100.18           C\\nANISOU 2872  CA  SER A 409    15802  12496   9765   -940   -916    -53       C\\nATOM   2873  C   SER A 409       9.363  -3.750 -12.341  1.00 91.59           C\\nANISOU 2873  C   SER A 409    14684  11035   9081   -825   -948   -193       C\\nATOM   2874  O   SER A 409       8.543  -3.336 -11.513  1.00 85.61           O\\nANISOU 2874  O   SER A 409    13671  10195   8661   -967  -1137      4       O\\nATOM   2875  CB  SER A 409       8.447  -3.811 -14.672  1.00102.06           C\\nANISOU 2875  CB  SER A 409    16434  12778   9567  -1245  -1202   -175       C\\nATOM   2876  OG  SER A 409       8.493  -3.239 -15.967  1.00105.65           O\\nANISOU 2876  OG  SER A 409    16956  13611   9576  -1354  -1197    -26       O\\nATOM   2877  N   ALA A 410      10.216  -4.740 -12.069  1.00 90.76           N\\nANISOU 2877  N   ALA A 410    14837  10715   8935   -552   -765   -524       N\\nATOM   2878  CA  ALA A 410      10.196  -5.405 -10.769  1.00 84.55           C\\nANISOU 2878  CA  ALA A 410    14089   9558   8478   -436   -813   -622       C\\nATOM   2879  C   ALA A 410      10.716  -4.488  -9.669  1.00 85.46           C\\nANISOU 2879  C   ALA A 410    13726   9716   9028   -244   -702   -420       C\\nATOM   2880  O   ALA A 410      10.097  -4.365  -8.607  1.00 76.26           O\\nANISOU 2880  O   ALA A 410    12411   8410   8155   -337   -841   -294       O\\nATOM   2881  CB  ALA A 410      11.018  -6.693 -10.829  1.00 79.54           C\\nANISOU 2881  CB  ALA A 410    13883   8649   7690   -141   -680  -1016       C\\nATOM   2882  N   PHE A 411      11.858  -3.837  -9.904  1.00 82.88           N\\nANISOU 2882  N   PHE A 411    13149   9606   8736      5   -442   -403       N\\nATOM   2883  CA  PHE A 411      12.446  -2.977  -8.883  1.00 81.51           C\\nANISOU 2883  CA  PHE A 411    12529   9464   8975    175   -355   -259       C\\nATOM   2884  C   PHE A 411      11.593  -1.745  -8.614  1.00 76.95           C\\nANISOU 2884  C   PHE A 411    11608   8991   8637    -75   -511     73       C\\nATOM   2885  O   PHE A 411      11.658  -1.179  -7.516  1.00 76.38           O\\nANISOU 2885  O   PHE A 411    11240   8854   8929      0   -536    155       O\\nATOM   2886  CB  PHE A 411      13.859  -2.567  -9.293  1.00 88.89           C\\nANISOU 2886  CB  PHE A 411    13244  10633   9898    438    -44   -321       C\\nATOM   2887  CG  PHE A 411      14.856  -3.688  -9.233  1.00 94.35           C\\nANISOU 2887  CG  PHE A 411    14147  11212  10488    811    121   -674       C\\nATOM   2888  CD1 PHE A 411      14.562  -4.860  -8.555  1.00 93.62           C\\nANISOU 2888  CD1 PHE A 411    14407  10746  10418    926    -36   -865       C\\nATOM   2889  CD2 PHE A 411      16.092  -3.568  -9.846  1.00 94.90           C\\nANISOU 2889  CD2 PHE A 411    14052  11548  10457   1055    438   -805       C\\nATOM   2890  CE1 PHE A 411      15.480  -5.891  -8.497  1.00 91.66           C\\nANISOU 2890  CE1 PHE A 411    14375  10339  10112   1324     82  -1184       C\\nATOM   2891  CE2 PHE A 411      17.013  -4.595  -9.790  1.00 91.21           C\\nANISOU 2891  CE2 PHE A 411    13738  10988   9931   1464    585  -1156       C\\nATOM   2892  CZ  PHE A 411      16.707  -5.757  -9.115  1.00 90.35           C\\nANISOU 2892  CZ  PHE A 411    14011  10453   9865   1623    389  -1349       C\\nATOM   2893  N   THR A 412      10.799  -1.310  -9.596  1.00 86.37           N\\nANISOU 2893  N   THR A 412    12841  10347   9628   -346   -634    251       N\\nATOM   2894  CA  THR A 412       9.854  -0.225  -9.353  1.00 83.78           C\\nANISOU 2894  CA  THR A 412    12208  10075   9551   -541   -831    553       C\\nATOM   2895  C   THR A 412       8.712  -0.693  -8.459  1.00 78.58           C\\nANISOU 2895  C   THR A 412    11565   9242   9050   -678  -1053    522       C\\nATOM   2896  O   THR A 412       8.335  -0.005  -7.503  1.00 75.36           O\\nANISOU 2896  O   THR A 412    10841   8797   8997   -662  -1111    634       O\\nATOM   2897  CB  THR A 412       9.310   0.315 -10.677  1.00 83.99           C\\nANISOU 2897  CB  THR A 412    12287  10328   9297   -765   -948    775       C\\nATOM   2898  OG1 THR A 412      10.397   0.624 -11.557  1.00 88.79           O\\nANISOU 2898  OG1 THR A 412    12926  11134   9675   -676   -690    805       O\\nATOM   2899  CG2 THR A 412       8.491   1.578 -10.436  1.00 76.49           C\\nANISOU 2899  CG2 THR A 412    10981   9411   8671   -879  -1149   1106       C\\nATOM   2900  N   TRP A 413       8.148  -1.866  -8.758  1.00 79.97           N\\nANISOU 2900  N   TRP A 413    12110   9314   8961   -831  -1168    357       N\\nATOM   2901  CA  TRP A 413       7.078  -2.406  -7.927  1.00 79.43           C\\nANISOU 2901  CA  TRP A 413    12060   9094   9024  -1024  -1347    342       C\\nATOM   2902  C   TRP A 413       7.576  -2.703  -6.520  1.00 73.46           C\\nANISOU 2902  C   TRP A 413    11258   8138   8517   -819  -1224    254       C\\nATOM   2903  O   TRP A 413       6.853  -2.491  -5.539  1.00 70.81           O\\nANISOU 2903  O   TRP A 413    10714   7782   8407   -915  -1295    340       O\\nATOM   2904  CB  TRP A 413       6.498  -3.667  -8.569  1.00 85.80           C\\nANISOU 2904  CB  TRP A 413    13317   9783   9501  -1268  -1494    166       C\\nATOM   2905  CG  TRP A 413       5.728  -3.398  -9.828  1.00 91.51           C\\nANISOU 2905  CG  TRP A 413    14070  10739   9962  -1534  -1703    261       C\\nATOM   2906  CD1 TRP A 413       5.242  -2.195 -10.250  1.00 85.59           C\\nANISOU 2906  CD1 TRP A 413    12966  10256   9299  -1598  -1823    542       C\\nATOM   2907  CD2 TRP A 413       5.358  -4.354 -10.833  1.00 96.72           C\\nANISOU 2907  CD2 TRP A 413    15160  11373  10216  -1760  -1855     72       C\\nATOM   2908  NE1 TRP A 413       4.589  -2.343 -11.449  1.00 88.41           N\\nANISOU 2908  NE1 TRP A 413    13492  10790   9309  -1846  -2056    571       N\\nATOM   2909  CE2 TRP A 413       4.646  -3.658 -11.829  1.00 95.02           C\\nANISOU 2909  CE2 TRP A 413    14808  11468   9826  -1963  -2077    265       C\\nATOM   2910  CE3 TRP A 413       5.558  -5.731 -10.985  1.00100.43           C\\nANISOU 2910  CE3 TRP A 413    16143  11559  10456  -1802  -1850   -252       C\\nATOM   2911  CZ2 TRP A 413       4.135  -4.290 -12.963  1.00 98.69           C\\nANISOU 2911  CZ2 TRP A 413    15618  12022   9858  -2226  -2299    130       C\\nATOM   2912  CZ3 TRP A 413       5.049  -6.356 -12.111  1.00103.40           C\\nANISOU 2912  CZ3 TRP A 413    16876  11980  10432  -2067  -2053   -417       C\\nATOM   2913  CH2 TRP A 413       4.347  -5.636 -13.085  1.00102.66           C\\nANISOU 2913  CH2 TRP A 413    16621  12251  10133  -2286  -2277   -233       C\\nATOM   2914  N   LEU A 414       8.817  -3.184  -6.402  1.00 75.32           N\\nANISOU 2914  N   LEU A 414    11667   8256   8695   -521  -1041     79       N\\nATOM   2915  CA  LEU A 414       9.384  -3.467  -5.087  1.00 69.21           C\\nANISOU 2915  CA  LEU A 414    10863   7310   8123   -291   -967     10       C\\nATOM   2916  C   LEU A 414       9.434  -2.210  -4.226  1.00 77.59           C\\nANISOU 2916  C   LEU A 414    11447   8517   9516   -215   -939    159       C\\nATOM   2917  O   LEU A 414       9.179  -2.265  -3.016  1.00 79.71           O\\nANISOU 2917  O   LEU A 414    11637   8710   9938   -194   -969    169       O\\nATOM   2918  CB  LEU A 414      10.778  -4.078  -5.238  1.00 67.92           C\\nANISOU 2918  CB  LEU A 414    10893   7049   7867     71   -800   -201       C\\nATOM   2919  CG  LEU A 414      11.552  -4.368  -3.947  1.00 71.97           C\\nANISOU 2919  CG  LEU A 414    11370   7408   8567    375   -760   -268       C\\nATOM   2920  CD1 LEU A 414      10.756  -5.279  -3.035  1.00 56.68           C\\nANISOU 2920  CD1 LEU A 414     9726   5197   6611    226   -906   -242       C\\nATOM   2921  CD2 LEU A 414      12.904  -4.980  -4.260  1.00 76.87           C\\nANISOU 2921  CD2 LEU A 414    12133   7966   9108    768   -617   -490       C\\nATOM   2922  N   GLY A 415       9.747  -1.065  -4.832  1.00 76.07           N\\nANISOU 2922  N   GLY A 415    10960   8524   9421   -187   -885    275       N\\nATOM   2923  CA  GLY A 415       9.745   0.179  -4.081  1.00 72.96           C\\nANISOU 2923  CA  GLY A 415    10144   8207   9369   -132   -886    390       C\\nATOM   2924  C   GLY A 415       8.357   0.581  -3.618  1.00 74.19           C\\nANISOU 2924  C   GLY A 415    10131   8394   9665   -339  -1044    507       C\\nATOM   2925  O   GLY A 415       8.180   1.043  -2.488  1.00 75.00           O\\nANISOU 2925  O   GLY A 415    10010   8487   9999   -269  -1044    489       O\\nATOM   2926  N   TYR A 416       7.355   0.423  -4.485  1.00 71.29           N\\nANISOU 2926  N   TYR A 416     9841   8097   9148   -588  -1184    609       N\\nATOM   2927  CA  TYR A 416       5.978   0.695  -4.089  1.00 65.72           C\\nANISOU 2927  CA  TYR A 416     8925   7466   8580   -782  -1337    704       C\\nATOM   2928  C   TYR A 416       5.494  -0.288  -3.030  1.00 74.23           C\\nANISOU 2928  C   TYR A 416    10136   8452   9617   -880  -1320    595       C\\nATOM   2929  O   TYR A 416       4.629   0.058  -2.215  1.00 72.94           O\\nANISOU 2929  O   TYR A 416     9706   8378   9627   -957  -1345    631       O\\nATOM   2930  CB  TYR A 416       5.065   0.646  -5.312  1.00 62.97           C\\nANISOU 2930  CB  TYR A 416     8626   7243   8059  -1034  -1533    831       C\\nATOM   2931  CG  TYR A 416       5.257   1.800  -6.266  1.00 72.57           C\\nANISOU 2931  CG  TYR A 416     9671   8573   9328   -975  -1592   1030       C\\nATOM   2932  CD1 TYR A 416       5.334   3.107  -5.802  1.00 77.77           C\\nANISOU 2932  CD1 TYR A 416     9966   9229  10353   -816  -1582   1149       C\\nATOM   2933  CD2 TYR A 416       5.362   1.584  -7.633  1.00 70.98           C\\nANISOU 2933  CD2 TYR A 416     9709   8467   8795  -1089  -1663   1103       C\\nATOM   2934  CE1 TYR A 416       5.505   4.166  -6.675  1.00 81.18           C\\nANISOU 2934  CE1 TYR A 416    10288   9707  10852   -788  -1652   1381       C\\nATOM   2935  CE2 TYR A 416       5.537   2.637  -8.513  1.00 78.84           C\\nANISOU 2935  CE2 TYR A 416    10587   9572   9796  -1063  -1716   1345       C\\nATOM   2936  CZ  TYR A 416       5.608   3.925  -8.030  1.00 78.01           C\\nANISOU 2936  CZ  TYR A 416    10131   9419  10091   -919  -1715   1507       C\\nATOM   2937  OH  TYR A 416       5.781   4.974  -8.906  1.00 66.59           O\\nANISOU 2937  OH  TYR A 416     8612   8022   8665   -917  -1783   1795       O\\nATOM   2938  N   VAL A 417       6.036  -1.510  -3.031  1.00 75.00           N\\nANISOU 2938  N   VAL A 417    10650   8367   9481   -873  -1268    468       N\\nATOM   2939  CA  VAL A 417       5.682  -2.503  -2.019  1.00 75.22           C\\nANISOU 2939  CA  VAL A 417    10882   8250   9450   -979  -1253    416       C\\nATOM   2940  C   VAL A 417       6.049  -2.017  -0.621  1.00 75.65           C\\nANISOU 2940  C   VAL A 417    10726   8332   9686   -769  -1144    400       C\\nATOM   2941  O   VAL A 417       5.383  -2.367   0.363  1.00 73.28           O\\nANISOU 2941  O   VAL A 417    10419   8044   9381   -909  -1125    429       O\\nATOM   2942  CB  VAL A 417       6.357  -3.847  -2.359  1.00 69.42           C\\nANISOU 2942  CB  VAL A 417    10679   7234   8461   -938  -1241    282       C\\nATOM   2943  CG1 VAL A 417       6.474  -4.740  -1.133  1.00 66.88           C\\nANISOU 2943  CG1 VAL A 417    10605   6693   8112   -911  -1204    262       C\\nATOM   2944  CG2 VAL A 417       5.575  -4.550  -3.446  1.00 68.97           C\\nANISOU 2944  CG2 VAL A 417    10878   7133   8193  -1268  -1387    262       C\\nATOM   2945  N   ASN A 418       7.086  -1.184  -0.510  1.00 69.14           N\\nANISOU 2945  N   ASN A 418     9719   7544   9007   -464  -1071    354       N\\nATOM   2946  CA  ASN A 418       7.506  -0.674   0.790  1.00 59.69           C\\nANISOU 2946  CA  ASN A 418     8331   6385   7962   -263  -1004    296       C\\nATOM   2947  C   ASN A 418       6.365   0.000   1.544  1.00 72.46           C\\nANISOU 2947  C   ASN A 418     9629   8176   9728   -397  -1007    338       C\\nATOM   2948  O   ASN A 418       6.372   0.033   2.780  1.00 78.40           O\\nANISOU 2948  O   ASN A 418    10330   8974  10483   -321   -946    277       O\\nATOM   2949  CB  ASN A 418       8.666   0.302   0.607  1.00 65.48           C\\nANISOU 2949  CB  ASN A 418     8842   7154   8882      6   -958    240       C\\nATOM   2950  CG  ASN A 418       9.105   0.938   1.907  1.00 70.06           C\\nANISOU 2950  CG  ASN A 418     9208   7784   9627    195   -932    141       C\\nATOM   2951  OD1 ASN A 418       9.915   0.373   2.644  1.00 72.31           O\\nANISOU 2951  OD1 ASN A 418     9648   8008   9820    376   -923     50       O\\nATOM   2952  ND2 ASN A 418       8.575   2.123   2.197  1.00 73.88           N\\nANISOU 2952  ND2 ASN A 418     9344   8372  10354    175   -946    143       N\\nATOM   2953  N   SER A 419       5.371   0.528   0.828  1.00 73.71           N\\nANISOU 2953  N   SER A 419     9563   8456   9988   -577  -1081    433       N\\nATOM   2954  CA  SER A 419       4.257   1.208   1.479  1.00 74.87           C\\nANISOU 2954  CA  SER A 419     9342   8795  10311   -653  -1075    444       C\\nATOM   2955  C   SER A 419       3.387   0.269   2.304  1.00 71.13           C\\nANISOU 2955  C   SER A 419     8963   8398   9665   -899  -1010    455       C\\nATOM   2956  O   SER A 419       2.578   0.748   3.105  1.00 79.35           O\\nANISOU 2956  O   SER A 419     9691   9646  10814   -930   -935    423       O\\nATOM   2957  CB  SER A 419       3.402   1.927   0.433  1.00 76.98           C\\nANISOU 2957  CB  SER A 419     9339   9174  10737   -757  -1215    564       C\\nATOM   2958  OG  SER A 419       4.102   3.028  -0.124  1.00 76.00           O\\nANISOU 2958  OG  SER A 419     9078   8985  10813   -542  -1256    597       O\\nATOM   2959  N   ALA A 420       3.532  -1.043   2.146  1.00 64.52           N\\nANISOU 2959  N   ALA A 420     8553   7392   8567  -1076  -1023    494       N\\nATOM   2960  CA  ALA A 420       2.711  -1.998   2.873  1.00 70.62           C\\nANISOU 2960  CA  ALA A 420     9465   8194   9173  -1382   -964    556       C\\nATOM   2961  C   ALA A 420       3.486  -2.802   3.908  1.00 76.87           C\\nANISOU 2961  C   ALA A 420    10638   8808   9762  -1279   -878    546       C\\nATOM   2962  O   ALA A 420       2.886  -3.634   4.598  1.00 79.00           O\\nANISOU 2962  O   ALA A 420    11085   9071   9862  -1550   -815    643       O\\nATOM   2963  CB  ALA A 420       2.026  -2.954   1.892  1.00 69.09           C\\nANISOU 2963  CB  ALA A 420     9496   7901   8853  -1760  -1092    637       C\\nATOM   2964  N   VAL A 421       4.793  -2.590   4.035  1.00 77.91           N\\nANISOU 2964  N   VAL A 421    10893   8806   9904   -910   -888    455       N\\nATOM   2965  CA  VAL A 421       5.579  -3.412   4.946  1.00 79.27           C\\nANISOU 2965  CA  VAL A 421    11443   8799   9879   -770   -869    464       C\\nATOM   2966  C   VAL A 421       5.680  -2.792   6.335  1.00 78.59           C\\nANISOU 2966  C   VAL A 421    11159   8929   9775   -616   -776    415       C\\nATOM   2967  O   VAL A 421       5.844  -3.521   7.319  1.00 80.37           O\\nANISOU 2967  O   VAL A 421    11677   9096   9766   -626   -753    490       O\\nATOM   2968  CB  VAL A 421       6.980  -3.686   4.367  1.00 73.59           C\\nANISOU 2968  CB  VAL A 421    10961   7841   9160   -437   -947    375       C\\nATOM   2969  CG1 VAL A 421       6.871  -4.312   2.991  1.00 71.39           C\\nANISOU 2969  CG1 VAL A 421    10910   7375   8838   -578  -1015    377       C\\nATOM   2970  CG2 VAL A 421       7.810  -2.409   4.324  1.00 65.73           C\\nANISOU 2970  CG2 VAL A 421     9584   7002   8387   -121   -934    246       C\\nATOM   2971  N   ASN A 422       5.581  -1.466   6.440  1.00 74.03           N\\nANISOU 2971  N   ASN A 422    10123   8582   9422   -475   -738    288       N\\nATOM   2972  CA  ASN A 422       5.742  -0.820   7.742  1.00 73.83           C\\nANISOU 2972  CA  ASN A 422     9929   8759   9366   -304   -662    170       C\\nATOM   2973  C   ASN A 422       4.697  -1.265   8.756  1.00 74.68           C\\nANISOU 2973  C   ASN A 422    10063   9076   9236   -564   -510    254       C\\nATOM   2974  O   ASN A 422       5.081  -1.611   9.887  1.00 76.59           O\\nANISOU 2974  O   ASN A 422    10516   9367   9218   -484   -475    261       O\\nATOM   2975  CB  ASN A 422       5.757   0.700   7.560  1.00 72.41           C\\nANISOU 2975  CB  ASN A 422     9279   8717   9517   -120   -663     -7       C\\nATOM   2976  CG  ASN A 422       7.075   1.199   7.026  1.00 70.46           C\\nANISOU 2976  CG  ASN A 422     9018   8305   9448    152   -777    -94       C\\nATOM   2977  OD1 ASN A 422       8.006   0.419   6.829  1.00 69.93           O\\nANISOU 2977  OD1 ASN A 422     9248   8068   9254    251   -842    -54       O\\nATOM   2978  ND2 ASN A 422       7.166   2.500   6.780  1.00 74.23           N\\nANISOU 2978  ND2 ASN A 422     9142   8823  10239    275   -798   -213       N\\nATOM   2979  N   PRO A 423       3.396  -1.299   8.444  1.00 74.98           N\\nANISOU 2979  N   PRO A 423     9889   9275   9326   -884   -418    332       N\\nATOM   2980  CA  PRO A 423       2.439  -1.829   9.431  1.00 79.39           C\\nANISOU 2980  CA  PRO A 423    10466  10068   9629  -1180   -229    435       C\\nATOM   2981  C   PRO A 423       2.722  -3.267   9.832  1.00 83.90           C\\nANISOU 2981  C   PRO A 423    11615  10404   9861  -1378   -249    663       C\\nATOM   2982  O   PRO A 423       2.406  -3.662  10.961  1.00 90.16           O\\nANISOU 2982  O   PRO A 423    12538  11363  10356  -1521    -99    763       O\\nATOM   2983  CB  PRO A 423       1.089  -1.697   8.713  1.00 72.48           C\\nANISOU 2983  CB  PRO A 423     9227   9375   8937  -1503   -180    488       C\\nATOM   2984  CG  PRO A 423       1.299  -0.620   7.719  1.00 68.97           C\\nANISOU 2984  CG  PRO A 423     8463   8890   8854  -1250   -321    353       C\\nATOM   2985  CD  PRO A 423       2.703  -0.792   7.246  1.00 69.67           C\\nANISOU 2985  CD  PRO A 423     8902   8634   8934   -993   -481    335       C\\nATOM   2986  N   ILE A 424       3.313  -4.062   8.939  1.00 83.26           N\\nANISOU 2986  N   ILE A 424    11907   9927   9801  -1380   -427    747       N\\nATOM   2987  CA  ILE A 424       3.682  -5.430   9.285  1.00 83.10           C\\nANISOU 2987  CA  ILE A 424    12489   9580   9504  -1500   -487    952       C\\nATOM   2988  C   ILE A 424       4.819  -5.441  10.300  1.00 81.27           C\\nANISOU 2988  C   ILE A 424    12492   9304   9083  -1119   -542    931       C\\nATOM   2989  O   ILE A 424       4.919  -6.359  11.125  1.00 80.08           O\\nANISOU 2989  O   ILE A 424    12773   9025   8629  -1213   -546   1138       O\\nATOM   2990  CB  ILE A 424       4.040  -6.206   8.002  1.00 78.55           C\\nANISOU 2990  CB  ILE A 424    12237   8582   9027  -1536   -666    971       C\\nATOM   2991  CG1 ILE A 424       2.825  -6.276   7.073  1.00 73.56           C\\nANISOU 2991  CG1 ILE A 424    11398   8028   8524  -1971   -654   1003       C\\nATOM   2992  CG2 ILE A 424       4.560  -7.600   8.325  1.00 80.22           C\\nANISOU 2992  CG2 ILE A 424    13116   8357   9008  -1567   -766   1149       C\\nATOM   2993  CD1 ILE A 424       3.095  -6.975   5.758  1.00 71.89           C\\nANISOU 2993  CD1 ILE A 424    11502   7446   8367  -2028   -834    970       C\\nATOM   2994  N   ILE A 425       5.680  -4.422  10.275  1.00 72.91           N\\nANISOU 2994  N   ILE A 425    11155   8352   8197   -705   -607    699       N\\nATOM   2995  CA  ILE A 425       6.795  -4.363  11.215  1.00 77.19           C\\nANISOU 2995  CA  ILE A 425    11857   8894   8577   -341   -708    646       C\\nATOM   2996  C   ILE A 425       6.320  -3.961  12.608  1.00 86.64           C\\nANISOU 2996  C   ILE A 425    12947  10469   9504   -403   -561    636       C\\nATOM   2997  O   ILE A 425       6.863  -4.432  13.615  1.00 84.58           O\\nANISOU 2997  O   ILE A 425    13008  10207   8921   -280   -633    733       O\\nATOM   2998  CB  ILE A 425       7.877  -3.406  10.689  1.00 71.65           C\\nANISOU 2998  CB  ILE A 425    10863   8188   8172     58   -830    392       C\\nATOM   2999  CG1 ILE A 425       8.343  -3.850   9.303  1.00 71.05           C\\nANISOU 2999  CG1 ILE A 425    10906   7796   8294    111   -926    402       C\\nATOM   3000  CG2 ILE A 425       9.062  -3.360  11.634  1.00 68.37           C\\nANISOU 3000  CG2 ILE A 425    10565   7798   7613    422   -980    318       C\\nATOM   3001  CD1 ILE A 425       9.377  -2.939   8.685  1.00 69.86           C\\nANISOU 3001  CD1 ILE A 425    10448   7667   8427    435  -1000    194       C\\nATOM   3002  N   TYR A 426       5.302  -3.102  12.695  1.00 80.85           N\\nANISOU 3002  N   TYR A 426    11769  10077   8874   -571   -359    514       N\\nATOM   3003  CA  TYR A 426       4.811  -2.668  13.999  1.00 87.40           C\\nANISOU 3003  CA  TYR A 426    12467  11316   9424   -609   -172    444       C\\nATOM   3004  C   TYR A 426       4.159  -3.813  14.767  1.00 95.75           C\\nANISOU 3004  C   TYR A 426    13906  12427  10045   -980    -30    771       C\\nATOM   3005  O   TYR A 426       4.175  -3.815  16.004  1.00 99.16           O\\nANISOU 3005  O   TYR A 426    14463  13130  10085   -961     67    794       O\\nATOM   3006  CB  TYR A 426       3.826  -1.511  13.828  1.00 86.99           C\\nANISOU 3006  CB  TYR A 426    11825  11596   9630   -664     22    214       C\\nATOM   3007  CG  TYR A 426       4.370  -0.345  13.027  1.00 85.70           C\\nANISOU 3007  CG  TYR A 426    11311  11332   9920   -350   -120    -55       C\\nATOM   3008  CD1 TYR A 426       5.706   0.027  13.118  1.00 83.30           C\\nANISOU 3008  CD1 TYR A 426    11097  10869   9684      2   -327   -201       C\\nATOM   3009  CD2 TYR A 426       3.547   0.381  12.176  1.00 83.93           C\\nANISOU 3009  CD2 TYR A 426    10656  11172  10061   -422    -61   -137       C\\nATOM   3010  CE1 TYR A 426       6.206   1.093  12.385  1.00 79.72           C\\nANISOU 3010  CE1 TYR A 426    10330  10311   9648    224   -438   -408       C\\nATOM   3011  CE2 TYR A 426       4.037   1.447  11.441  1.00 82.37           C\\nANISOU 3011  CE2 TYR A 426    10186  10845  10265   -163   -196   -323       C\\nATOM   3012  CZ  TYR A 426       5.368   1.799  11.548  1.00 77.29           C\\nANISOU 3012  CZ  TYR A 426     9656  10030   9679    135   -368   -452       C\\nATOM   3013  OH  TYR A 426       5.859   2.858  10.815  1.00 65.48           O\\nANISOU 3013  OH  TYR A 426     7898   8395   8588    330   -485   -601       O\\nATOM   3014  N   THR A 427       3.583  -4.790  14.059  1.00 94.12           N\\nANISOU 3014  N   THR A 427    13912  11967   9880  -1346    -21   1029       N\\nATOM   3015  CA  THR A 427       2.981  -5.936  14.735  1.00 94.73           C\\nANISOU 3015  CA  THR A 427    14395  12024   9574  -1766    104   1385       C\\nATOM   3016  C   THR A 427       4.036  -6.873  15.301  1.00 93.77           C\\nANISOU 3016  C   THR A 427    14923  11553   9151  -1581   -115   1608       C\\nATOM   3017  O   THR A 427       3.779  -7.565  16.293  1.00107.23           O\\nANISOU 3017  O   THR A 427    16989  13325  10429  -1808    -22   1896       O\\nATOM   3018  CB  THR A 427       2.076  -6.711  13.777  1.00 92.02           C\\nANISOU 3018  CB  THR A 427    14101  11462   9402  -2246    135   1572       C\\nATOM   3019  OG1 THR A 427       2.869  -7.267  12.722  1.00 87.69           O\\nANISOU 3019  OG1 THR A 427    13873  10378   9067  -2083   -148   1577       O\\nATOM   3020  CG2 THR A 427       1.028  -5.801  13.182  1.00 92.49           C\\nANISOU 3020  CG2 THR A 427    13488  11881   9771  -2397    298   1371       C\\nATOM   3021  N   THR A 428       5.216  -6.918  14.687  1.00 86.78           N\\nANISOU 3021  N   THR A 428    14188  10309   8477  -1167   -404   1497       N\\nATOM   3022  CA  THR A 428       6.250  -7.850  15.112  1.00 80.90           C\\nANISOU 3022  CA  THR A 428    14030   9197   7512   -924   -656   1699       C\\nATOM   3023  C   THR A 428       7.087  -7.298  16.260  1.00 88.26           C\\nANISOU 3023  C   THR A 428    14945  10410   8178   -536   -758   1595       C\\nATOM   3024  O   THR A 428       7.228  -7.954  17.297  1.00 98.04           O\\nANISOU 3024  O   THR A 428    16618  11653   8981   -567   -810   1867       O\\nATOM   3025  CB  THR A 428       7.162  -8.200  13.934  1.00 75.14           C\\nANISOU 3025  CB  THR A 428    13433   7992   7124   -626   -905   1599       C\\nATOM   3026  OG1 THR A 428       6.369  -8.438  12.764  1.00 66.95           O\\nANISOU 3026  OG1 THR A 428    12310   6784   6344   -965   -819   1592       O\\nATOM   3027  CG2 THR A 428       7.977  -9.450  14.258  1.00 74.10           C\\nANISOU 3027  CG2 THR A 428    13971   7385   6798   -439  -1156   1861       C\\nATOM   3028  N   PHE A 429       7.642  -6.097  16.092  1.00 82.80           N\\nANISOU 3028  N   PHE A 429    13778   9948   7733   -194   -807   1216       N\\nATOM   3029  CA  PHE A 429       8.628  -5.569  17.024  1.00 85.65           C\\nANISOU 3029  CA  PHE A 429    14115  10520   7909    205   -988   1057       C\\nATOM   3030  C   PHE A 429       8.031  -4.731  18.145  1.00 88.27           C\\nANISOU 3030  C   PHE A 429    14208  11398   7933    109   -780    904       C\\nATOM   3031  O   PHE A 429       8.759  -4.373  19.077  1.00 94.52           O\\nANISOU 3031  O   PHE A 429    15046  12401   8467    386   -940    780       O\\nATOM   3032  CB  PHE A 429       9.666  -4.731  16.274  1.00 81.51           C\\nANISOU 3032  CB  PHE A 429    13220   9923   7826    606  -1176    717       C\\nATOM   3033  CG  PHE A 429      10.610  -5.545  15.451  1.00 86.84           C\\nANISOU 3033  CG  PHE A 429    14151  10141   8702    848  -1415    814       C\\nATOM   3034  CD1 PHE A 429      11.723  -6.132  16.031  1.00 95.71           C\\nANISOU 3034  CD1 PHE A 429    15590  11131   9647   1208  -1714    909       C\\nATOM   3035  CD2 PHE A 429      10.383  -5.736  14.099  1.00 90.50           C\\nANISOU 3035  CD2 PHE A 429    14539  10330   9515    740  -1348    797       C\\nATOM   3036  CE1 PHE A 429      12.597  -6.891  15.275  1.00100.77           C\\nANISOU 3036  CE1 PHE A 429    16434  11359  10493   1488  -1918    962       C\\nATOM   3037  CE2 PHE A 429      11.253  -6.492  13.334  1.00 94.15           C\\nANISOU 3037  CE2 PHE A 429    15239  10395  10137    990  -1533    835       C\\nATOM   3038  CZ  PHE A 429      12.362  -7.070  13.923  1.00 99.97           C\\nANISOU 3038  CZ  PHE A 429    16261  10992  10733   1381  -1805    907       C\\nATOM   3039  N   ASN A 430       6.743  -4.409  18.090  1.00 83.72           N\\nANISOU 3039  N   ASN A 430    13363  11080   7368   -257   -438    882       N\\nATOM   3040  CA  ASN A 430       6.116  -3.571  19.103  1.00 88.98           C\\nANISOU 3040  CA  ASN A 430    13756  12293   7759   -315   -190    673       C\\nATOM   3041  C   ASN A 430       4.910  -4.295  19.678  1.00 94.26           C\\nANISOU 3041  C   ASN A 430    14603  13185   8026   -804    139    994       C\\nATOM   3042  O   ASN A 430       3.949  -4.578  18.954  1.00 90.37           O\\nANISOU 3042  O   ASN A 430    13952  12628   7755  -1162    332   1116       O\\nATOM   3043  CB  ASN A 430       5.708  -2.218  18.523  1.00 82.34           C\\nANISOU 3043  CB  ASN A 430    12274  11632   7378   -219    -60    251       C\\nATOM   3044  CG  ASN A 430       5.177  -1.278  19.577  1.00 86.94           C\\nANISOU 3044  CG  ASN A 430    12575  12746   7711   -183    175    -57       C\\nATOM   3045  OD1 ASN A 430       3.978  -1.247  19.844  1.00 86.57           O\\nANISOU 3045  OD1 ASN A 430    12339  13023   7531   -474    525    -28       O\\nATOM   3046  ND2 ASN A 430       6.069  -0.510  20.193  1.00 93.49           N\\nANISOU 3046  ND2 ASN A 430    13362  13689   8473    174    -14   -380       N\\nATOM   3047  N   ILE A 431       4.963  -4.590  20.979  1.00 96.66           N\\nANISOU 3047  N   ILE A 431    15226  13779   7721   -842    197   1137       N\\nATOM   3048  CA  ILE A 431       3.848  -5.262  21.638  1.00 92.58           C\\nANISOU 3048  CA  ILE A 431    14883  13536   6757  -1346    552   1472       C\\nATOM   3049  C   ILE A 431       2.630  -4.348  21.695  1.00 98.55           C\\nANISOU 3049  C   ILE A 431    15013  14819   7614  -1537    984   1175       C\\nATOM   3050  O   ILE A 431       1.488  -4.806  21.569  1.00 98.81           O\\nANISOU 3050  O   ILE A 431    14936  14997   7611  -2018   1303   1397       O\\nATOM   3051  CB  ILE A 431       4.263  -5.738  23.042  1.00 91.00           C\\nANISOU 3051  CB  ILE A 431    15200  13558   5818  -1318    503   1710       C\\nATOM   3052  N   GLU A 432       2.851  -3.043  21.881  1.00 96.20           N\\nANISOU 3052  N   GLU A 432    14279  14803   7470  -1163    992    657       N\\nATOM   3053  CA  GLU A 432       1.733  -2.109  21.979  1.00 93.30           C\\nANISOU 3053  CA  GLU A 432    13305  14920   7225  -1248   1385    325       C\\nATOM   3054  C   GLU A 432       1.005  -1.971  20.646  1.00 90.82           C\\nANISOU 3054  C   GLU A 432    12560  14400   7549  -1408   1437    316       C\\nATOM   3055  O   GLU A 432      -0.230  -1.927  20.610  1.00 84.30           O\\nANISOU 3055  O   GLU A 432    11363  13912   6757  -1725   1791    333       O\\nATOM   3056  CB  GLU A 432       2.229  -0.750  22.471  1.00 88.42           C\\nANISOU 3056  CB  GLU A 432    12394  14544   6659   -774   1324   -250       C\\nATOM   3057  N   PHE A 433       1.747  -1.901  19.538  1.00 90.26           N\\nANISOU 3057  N   PHE A 433    12509  13817   7970  -1197   1087    288       N\\nATOM   3058  CA  PHE A 433       1.098  -1.850  18.232  1.00 93.03           C\\nANISOU 3058  CA  PHE A 433    12520  13969   8860  -1363   1090    317       C\\nATOM   3059  C   PHE A 433       0.366  -3.155  17.929  1.00 92.59           C\\nANISOU 3059  C   PHE A 433    12717  13789   8674  -1909   1194    776       C\\nATOM   3060  O   PHE A 433      -0.768  -3.136  17.438  1.00 86.48           O\\nANISOU 3060  O   PHE A 433    11554  13195   8111  -2229   1396    805       O\\nATOM   3061  CB  PHE A 433       2.125  -1.540  17.137  1.00 94.23           C\\nANISOU 3061  CB  PHE A 433    12696  13628   9479  -1036    712    208       C\\nATOM   3062  CG  PHE A 433       2.253  -0.070  16.807  1.00 90.02           C\\nANISOU 3062  CG  PHE A 433    11657  13176   9371   -672    669   -233       C\\nATOM   3063  CD1 PHE A 433       1.220   0.604  16.178  1.00 82.18           C\\nANISOU 3063  CD1 PHE A 433    10137  12335   8753   -746    821   -367       C\\nATOM   3064  CD2 PHE A 433       3.413   0.630  17.106  1.00 88.82           C\\nANISOU 3064  CD2 PHE A 433    11559  12920   9269   -265    446   -498       C\\nATOM   3065  CE1 PHE A 433       1.331   1.949  15.867  1.00 78.56           C\\nANISOU 3065  CE1 PHE A 433     9265  11877   8709   -401    756   -738       C\\nATOM   3066  CE2 PHE A 433       3.531   1.976  16.796  1.00 82.75           C\\nANISOU 3066  CE2 PHE A 433    10368  12155   8919     24    394   -882       C\\nATOM   3067  CZ  PHE A 433       2.487   2.635  16.177  1.00 81.74           C\\nANISOU 3067  CZ  PHE A 433     9768  12128   9161    -34    550   -991       C\\nATOM   3068  N   ARG A 434       0.991  -4.296  18.232  1.00 96.08           N\\nANISOU 3068  N   ARG A 434    13805  13913   8786  -2025   1037   1134       N\\nATOM   3069  CA  ARG A 434       0.385  -5.588  17.918  1.00 91.88           C\\nANISOU 3069  CA  ARG A 434    13600  13146   8164  -2562   1089   1576       C\\nATOM   3070  C   ARG A 434      -0.930  -5.778  18.663  1.00 88.38           C\\nANISOU 3070  C   ARG A 434    12942  13229   7411  -3068   1532   1730       C\\nATOM   3071  O   ARG A 434      -1.944  -6.162  18.068  1.00 89.59           O\\nANISOU 3071  O   ARG A 434    12864  13413   7764  -3530   1674   1870       O\\nATOM   3072  CB  ARG A 434       1.360  -6.718  18.249  1.00 91.99           C\\nANISOU 3072  CB  ARG A 434    14390  12689   7871  -2520    823   1923       C\\nATOM   3073  N   LYS A 435      -0.934  -5.515  19.973  1.00 92.30           N\\nANISOU 3073  N   LYS A 435    13491  14183   7397  -3005   1759   1697       N\\nATOM   3074  CA  LYS A 435      -2.157  -5.679  20.753  1.00 95.80           C\\nANISOU 3074  CA  LYS A 435    13709  15207   7485  -3485   2243   1837       C\\nATOM   3075  C   LYS A 435      -3.199  -4.633  20.385  1.00 95.39           C\\nANISOU 3075  C   LYS A 435    12798  15636   7810  -3466   2525   1447       C\\nATOM   3076  O   LYS A 435      -4.399  -4.865  20.566  1.00100.11           O\\nANISOU 3076  O   LYS A 435    13054  16654   8329  -3942   2904   1572       O\\nATOM   3077  CB  LYS A 435      -1.843  -5.617  22.249  1.00100.45           C\\nANISOU 3077  CB  LYS A 435    14594  16206   7366  -3383   2418   1871       C\\nATOM   3078  N   ALA A 436      -2.763  -3.482  19.869  1.00 97.48           N\\nANISOU 3078  N   ALA A 436    12695  15840   8503  -2926   2339    989       N\\nATOM   3079  CA  ALA A 436      -3.711  -2.457  19.446  1.00 99.12           C\\nANISOU 3079  CA  ALA A 436    12109  16422   9131  -2835   2542    627       C\\nATOM   3080  C   ALA A 436      -4.463  -2.884  18.193  1.00 98.71           C\\nANISOU 3080  C   ALA A 436    11791  16164   9549  -3194   2456    809       C\\nATOM   3081  O   ALA A 436      -5.682  -2.702  18.103  1.00 98.79           O\\nANISOU 3081  O   ALA A 436    11222  16613   9701  -3464   2744    764       O\\nATOM   3082  CB  ALA A 436      -2.984  -1.133  19.210  1.00 94.08           C\\nANISOU 3082  CB  ALA A 436    11230  15675   8839  -2179   2321    134       C\\nATOM   3083  N   PHE A 437      -3.753  -3.456  17.217  1.00 90.64           N\\nANISOU 3083  N   PHE A 437    11168  14510   8763  -3193   2056    991       N\\nATOM   3084  CA  PHE A 437      -4.405  -3.888  15.985  1.00 89.75           C\\nANISOU 3084  CA  PHE A 437    10864  14185   9052  -3536   1925   1136       C\\nATOM   3085  C   PHE A 437      -5.403  -5.004  16.256  1.00 98.61           C\\nANISOU 3085  C   PHE A 437    12055  15479   9935  -4263   2173   1518       C\\nATOM   3086  O   PHE A 437      -6.491  -5.031  15.669  1.00 97.68           O\\nANISOU 3086  O   PHE A 437    11436  15585  10092  -4617   2265   1534       O\\nATOM   3087  CB  PHE A 437      -3.365  -4.353  14.965  1.00 85.17           C\\nANISOU 3087  CB  PHE A 437    10775  12904   8681  -3381   1477   1231       C\\nATOM   3088  CG  PHE A 437      -2.480  -3.255  14.437  1.00 86.40           C\\nANISOU 3088  CG  PHE A 437    10779  12886   9165  -2763   1230    890       C\\nATOM   3089  CD1 PHE A 437      -2.661  -1.937  14.822  1.00 90.40           C\\nANISOU 3089  CD1 PHE A 437    10767  13767   9814  -2388   1365    522       C\\nATOM   3090  CD2 PHE A 437      -1.469  -3.548  13.540  1.00 80.59           C\\nANISOU 3090  CD2 PHE A 437    10422  11598   8603  -2569    873    931       C\\nATOM   3091  CE1 PHE A 437      -1.838  -0.938  14.328  1.00 85.90           C\\nANISOU 3091  CE1 PHE A 437    10090  12981   9568  -1879   1127    241       C\\nATOM   3092  CE2 PHE A 437      -0.645  -2.555  13.044  1.00 80.08           C\\nANISOU 3092  CE2 PHE A 437    10206  11388   8833  -2065    672    655       C\\nATOM   3093  CZ  PHE A 437      -0.831  -1.248  13.438  1.00 81.28           C\\nANISOU 3093  CZ  PHE A 437     9867  11875   9140  -1744    789    329       C\\nATOM   3094  N   LEU A 438      -5.047  -5.938  17.144  1.00 97.43           N\\nANISOU 3094  N   LEU A 438    12520  15222   9276  -4511   2262   1848       N\\nATOM   3095  CA  LEU A 438      -5.930  -7.059  17.446  1.00 99.16           C\\nANISOU 3095  CA  LEU A 438    12887  15540   9250  -5265   2497   2270       C\\nATOM   3096  C   LEU A 438      -7.187  -6.605  18.176  1.00104.88           C\\nANISOU 3096  C   LEU A 438    12926  17091   9832  -5548   3020   2189       C\\nATOM   3097  O   LEU A 438      -8.233  -7.257  18.066  1.00112.28           O\\nANISOU 3097  O   LEU A 438    13646  18228  10786  -6211   3228   2440       O\\nATOM   3098  CB  LEU A 438      -5.179  -8.106  18.269  1.00101.79           C\\nANISOU 3098  CB  LEU A 438    14093  15526   9057  -5410   2445   2676       C\\nATOM   3099  N   LYS A 439      -7.108  -5.501  18.923  1.00104.77           N\\nANISOU 3099  N   LYS A 439    12553  17573   9684  -5064   3242   1817       N\\nATOM   3100  CA  LYS A 439      -8.295  -4.960  19.574  1.00111.86           C\\nANISOU 3100  CA  LYS A 439    12728  19296  10480  -5232   3763   1648       C\\nATOM   3101  C   LYS A 439      -9.200  -4.234  18.588  1.00113.57           C\\nANISOU 3101  C   LYS A 439    12089  19730  11334  -5165   3740   1359       C\\nATOM   3102  O   LYS A 439     -10.419  -4.192  18.788  1.00116.22           O\\nANISOU 3102  O   LYS A 439    11788  20658  11710  -5514   4113   1349       O\\nATOM   3103  CB  LYS A 439      -7.894  -4.019  20.711  1.00111.35           C\\nANISOU 3103  CB  LYS A 439    12602  19665  10042  -4703   3997   1288       C\\nATOM   3104  N   ILE A 440      -8.629  -3.664  17.526  1.00111.11           N\\nANISOU 3104  N   ILE A 440    11741  18958  11519  -4713   3295   1139       N\\nATOM   3105  CA  ILE A 440      -9.451  -3.036  16.502  1.00110.51           C\\nANISOU 3105  CA  ILE A 440    10923  19028  12037  -4650   3192    931       C\\nATOM   3106  C   ILE A 440     -10.182  -4.088  15.675  1.00112.85           C\\nANISOU 3106  C   ILE A 440    11191  19185  12503  -5352   3077   1285       C\\nATOM   3107  O   ILE A 440     -11.326  -3.874  15.259  1.00112.91           O\\nANISOU 3107  O   ILE A 440    10465  19613  12823  -5584   3184   1219       O\\nATOM   3108  CB  ILE A 440      -8.581  -2.115  15.629  1.00104.69           C\\nANISOU 3108  CB  ILE A 440    10219  17834  11725  -3988   2753    640       C\\nATOM   3109  CG1 ILE A 440      -7.927  -1.040  16.500  1.00107.61           C\\nANISOU 3109  CG1 ILE A 440    10580  18352  11953  -3351   2868    257       C\\nATOM   3110  CG2 ILE A 440      -9.411  -1.469  14.537  1.00101.39           C\\nANISOU 3110  CG2 ILE A 440     9088  17539  11896  -3905   2594    477       C\\nATOM   3111  CD1 ILE A 440      -7.131  -0.015  15.728  1.00100.57           C\\nANISOU 3111  CD1 ILE A 440     9658  17052  11502  -2734   2483    -35       C\\nATOM   3112  N   LEU A 441      -9.554  -5.245  15.440  1.00112.02           N\\nANISOU 3112  N   LEU A 441    11866  18490  12207  -5698   2844   1648       N\\nATOM   3113  CA  LEU A 441     -10.167  -6.342  14.697  1.00113.38           C\\nANISOU 3113  CA  LEU A 441    12136  18432  12510  -6402   2704   1969       C\\nATOM   3114  C   LEU A 441     -10.959  -7.287  15.593  1.00125.26           C\\nANISOU 3114  C   LEU A 441    13779  20090  13724  -6864   2989   2236       C\\nATOM   3115  O   LEU A 441     -11.000  -8.499  15.335  1.00130.59           O\\nANISOU 3115  O   LEU A 441    14979  20276  14364  -7284   2800   2536       O\\nATOM   3116  CB  LEU A 441      -9.096  -7.115  13.924  1.00105.56           C\\nANISOU 3116  CB  LEU A 441    11981  16582  11546  -6372   2234   2137       C\\nATOM   3117  CG  LEU A 441      -8.272  -6.304  12.915  1.00100.01           C\\nANISOU 3117  CG  LEU A 441    11276  15521  11203  -5710   1825   1833       C\\nATOM   3118  CD1 LEU A 441      -7.049  -7.083  12.435  1.00 92.92           C\\nANISOU 3118  CD1 LEU A 441    11249  13839  10218  -5600   1460   1975       C\\nATOM   3119  CD2 LEU A 441      -9.133  -5.880  11.735  1.00101.27           C\\nANISOU 3119  CD2 LEU A 441    10791  15843  11843  -5803   1635   1687       C\\nATOM   3120  N   HIS A 442     -11.587  -6.766  16.640  1.00118.20           N\\nANISOU 3120  N   HIS A 442    12431  19851  12628  -6779   3439   2114       N\\nATOM   3121  CA  HIS A 442     -12.365  -7.591  17.554  1.00126.48           C\\nANISOU 3121  CA  HIS A 442    13562  21110  13385  -7224   3754   2376       C\\nATOM   3122  C   HIS A 442     -13.375  -6.752  18.337  1.00131.96           C\\nANISOU 3122  C   HIS A 442    13462  22622  14057  -7071   4227   2114       C\\nATOM   3123  O   HIS A 442     -14.028  -5.864  17.785  1.00131.46           O\\nANISOU 3123  O   HIS A 442    12638  22887  14424  -6809   4221   1787       O\\nATOM   3124  CB  HIS A 442     -11.436  -8.335  18.515  1.00127.27           C\\nANISOU 3124  CB  HIS A 442    14545  20900  12913  -7295   3807   2692       C\\nCONECT    1    2\\nCONECT    2    1    5    3\\nCONECT    3    2    4    6\\nCONECT    4    3\\nCONECT    5    2\\nCONECT    6    7    3\\nCONECT    7    6   10    8\\nCONECT    8    7    9   11\\nCONECT    9    8\\nCONECT   10    7\\nCONECT   58   59   53\\nCONECT   59   58   62   60\\nCONECT   60   59   61   63\\nCONECT   61   60\\nCONECT   62   59\\nCONECT  194  195  185\\nCONECT  195  194  198  196\\nCONECT  196  195  197  199\\nCONECT  197  196\\nCONECT  198  195\\nCONECT  199  200  196\\nCONECT  200  199  203  201\\nCONECT  201  200  202  204\\nCONECT  202  201\\nCONECT  203  200\\nCONECT  451  452  444\\nCONECT  452  451  455  453\\nCONECT  453  452  454  456\\nCONECT  454  453\\nCONECT  455  452\\nCONECT  467  468  465\\nCONECT  468  467  471  469\\nCONECT  469  468  470  472\\nCONECT  470  469\\nCONECT  471  468\\nCONECT  486  487  474\\nCONECT  487  486  490  488\\nCONECT  488  487  489  491\\nCONECT  489  488\\nCONECT  490  487\\nCONECT  542 1057  541\\nCONECT  772  778  773  766\\nCONECT  773  772  776  774\\nCONECT  774  773  775\\nCONECT  775  774\\nCONECT  776  773  777\\nCONECT  777  776  778\\nCONECT  778  772  777\\nCONECT  779  780\\nCONECT  780  779  783  781\\nCONECT  781  780  782  784\\nCONECT  782  781\\nCONECT  783  780\\nCONECT  784  785  781\\nCONECT  785  784  788  786\\nCONECT  786  785  787  789\\nCONECT  787  786\\nCONECT  788  785\\nCONECT  801  802  791\\nCONECT  802  801  805  803\\nCONECT  803  802  804  806\\nCONECT  804  803\\nCONECT  805  802\\nCONECT  812  813  808\\nCONECT  813  812  816  814\\nCONECT  814  813  815  817\\nCONECT  815  814\\nCONECT  816  813\\nCONECT  817  818  814\\nCONECT  818  817  821  819\\nCONECT  819  818  820  822\\nCONECT  820  819\\nCONECT  821  818\\nCONECT 1018 1019 1012\\nCONECT 1019 1018 1022 1020\\nCONECT 1020 1019 1021 1023\\nCONECT 1021 1020\\nCONECT 1022 1019\\nCONECT 1028 1029 1025\\nCONECT 1029 1028 1032 1030\\nCONECT 1030 1029 1031 1033\\nCONECT 1031 1030\\nCONECT 1032 1029\\nCONECT 1033 1034 1030\\nCONECT 1034 1033 1037 1035\\nCONECT 1035 1034 1036 1038\\nCONECT 1036 1035\\nCONECT 1037 1034\\nCONECT 1038 1039 1035\\nCONECT 1039 1038 1042 1040\\nCONECT 1040 1039 1041 1043\\nCONECT 1041 1040\\nCONECT 1042 1039\\nCONECT 1057  542 1056\\nCONECT 1282 1283 1276\\nCONECT 1283 1282 1286 1284\\nCONECT 1284 1283 1285 1289\\nCONECT 1285 1284\\nCONECT 1286 1283 1287\\nCONECT 1287 1286 1288\\nCONECT 1288 1287\\nCONECT 1332 1333 1326\\nCONECT 1333 1332 1336 1334\\nCONECT 1334 1333 1335 1337\\nCONECT 1335 1334\\nCONECT 1336 1333\\nCONECT 1337 1338 1334\\nCONECT 1338 1337 1341 1339\\nCONECT 1339 1338 1340 1342\\nCONECT 1340 1339\\nCONECT 1341 1338\\nCONECT 1364 1365 1355\\nCONECT 1365 1364 1368 1366\\nCONECT 1366 1365 1367 1369\\nCONECT 1367 1366\\nCONECT 1368 1365\\nCONECT 1369 1370 1366\\nCONECT 1370 1369 1373 1371\\nCONECT 1371 1370 1372 1374\\nCONECT 1372 1371\\nCONECT 1373 1370\\nCONECT 1493 1494 1487\\nCONECT 1494 1493 1497 1495\\nCONECT 1495 1494 1496 1498\\nCONECT 1496 1495\\nCONECT 1497 1494\\nCONECT 1518 1519 1508\\nCONECT 1519 1518 1522 1520\\nCONECT 1520 1519 1521 1523\\nCONECT 1521 1520\\nCONECT 1522 1519\\nCONECT 1538 1539 1533\\nCONECT 1539 1538 1542 1540\\nCONECT 1540 1539 1541 1543\\nCONECT 1541 1540\\nCONECT 1542 1539\\nCONECT 1612 1613 1604\\nCONECT 1613 1612 1616 1614\\nCONECT 1614 1613 1615 1617\\nCONECT 1615 1614\\nCONECT 1616 1613\\nCONECT 1617 1618 1614\\nCONECT 1618 1617 1621 1619\\nCONECT 1619 1618 1620 1622\\nCONECT 1620 1619\\nCONECT 1621 1618\\nCONECT 1629 1630 1624\\nCONECT 1630 1629 1633 1631\\nCONECT 1631 1630 1632 1634\\nCONECT 1632 1631\\nCONECT 1633 1630\\nCONECT 1634 1635 1631\\nCONECT 1635 1634 1638 1636\\nCONECT 1636 1635 1637 1639\\nCONECT 1637 1636\\nCONECT 1638 1635\\nCONECT 1646 1647 1641\\nCONECT 1647 1646 1650 1648\\nCONECT 1648 1647 1649 1651\\nCONECT 1649 1648\\nCONECT 1650 1647\\nCONECT 1659 1660 1653\\nCONECT 1660 1659 1663 1661\\nCONECT 1661 1660 1662 1664\\nCONECT 1662 1661\\nCONECT 1663 1660\\nCONECT 1683 1684 1676\\nCONECT 1684 1683 1687 1685\\nCONECT 1685 1684 1686 1688\\nCONECT 1686 1685\\nCONECT 1687 1684\\nCONECT 1688 1689 1685\\nCONECT 1689 1688 1692 1690\\nCONECT 1690 1689 1691 1693\\nCONECT 1691 1690\\nCONECT 1692 1689\\nCONECT 1709 1710 1703\\nCONECT 1710 1709 1713 1711\\nCONECT 1711 1710 1712 1714\\nCONECT 1712 1711\\nCONECT 1713 1710\\nCONECT 1719 1720 1716\\nCONECT 1720 1719 1723 1721\\nCONECT 1721 1720 1722 1724\\nCONECT 1722 1721\\nCONECT 1723 1720\\nCONECT 1739 1740 1730\\nCONECT 1740 1739 1743 1741\\nCONECT 1741 1740 1742 1744\\nCONECT 1742 1741\\nCONECT 1743 1740\\nCONECT 1744 1745 1741\\nCONECT 1745 1744 1748 1746\\nCONECT 1746 1745 1747 1749\\nCONECT 1747 1746\\nCONECT 1748 1745\\nCONECT 1749 1750 1746\\nCONECT 1750 1749 1753 1751\\nCONECT 1751 1750 1752 1754\\nCONECT 1752 1751\\nCONECT 1753 1750\\nCONECT 1758 1759 1756\\nCONECT 1759 1758 1762 1760\\nCONECT 1760 1759 1761 1763\\nCONECT 1761 1760\\nCONECT 1762 1759\\nCONECT 1778 1779 1773\\nCONECT 1779 1778 1782 1780\\nCONECT 1780 1779 1781 1783\\nCONECT 1781 1780\\nCONECT 1782 1779\\nCONECT 1814 1815 1807\\nCONECT 1815 1814 1818 1816\\nCONECT 1816 1815 1817 1819\\nCONECT 1817 1816\\nCONECT 1818 1815\\nCONECT 1926 1927 1920\\nCONECT 1927 1926 1930 1928\\nCONECT 1928 1927 1929 1931\\nCONECT 1929 1928\\nCONECT 1930 1927\\nCONECT 1944 1945 1941\\nCONECT 1945 1944 1948 1946\\nCONECT 1946 1945 1947 1949\\nCONECT 1947 1946\\nCONECT 1948 1945\\nCONECT 1957 1958 1951\\nCONECT 1958 1957 1961 1959\\nCONECT 1959 1958 1960 1962\\nCONECT 1960 1959\\nCONECT 1961 1958\\nCONECT 2187 2188 2182\\nCONECT 2188 2187 2191 2189\\nCONECT 2189 2188 2190 2192\\nCONECT 2190 2189\\nCONECT 2191 2188\\nCONECT 2285 2286 2273\\nCONECT 2286 2285 2289 2287\\nCONECT 2287 2286 2288 2290\\nCONECT 2288 2287\\nCONECT 2289 2286\\nCONECT 2309 2310 2306\\nCONECT 2310 2309 2313 2311\\nCONECT 2311 2310 2312 2314\\nCONECT 2312 2311\\nCONECT 2313 2310\\nCONECT 2335 2336 2332\\nCONECT 2336 2335 2339 2337\\nCONECT 2337 2336 2338 2340\\nCONECT 2338 2337\\nCONECT 2339 2336\\nCONECT 2346 2347 2342\\nCONECT 2347 2346 2350 2348\\nCONECT 2348 2347 2349 2351\\nCONECT 2349 2348\\nCONECT 2350 2347\\nCONECT 2385 2386 2379\\nCONECT 2386 2385 2389 2387\\nCONECT 2387 2386 2388 2390\\nCONECT 2388 2387\\nCONECT 2389 2386\\nCONECT 2428 2429 2425\\nCONECT 2429 2428 2432 2430\\nCONECT 2430 2429 2431 2433\\nCONECT 2431 2430\\nCONECT 2432 2429\\nCONECT 2506 2507 2504\\nCONECT 2507 2506 2510 2508\\nCONECT 2508 2507 2509 2511\\nCONECT 2509 2508\\nCONECT 2510 2507\\nCONECT 2538 2539 2535\\nCONECT 2539 2538 2542 2540\\nCONECT 2540 2539 2541\\nCONECT 2541 2540\\nCONECT 2542 2539 2543\\nCONECT 2543 2542 2544 2545\\nCONECT 2544 2543 2546\\nCONECT 2545 2543 2547\\nCONECT 2546 2544 2548\\nCONECT 2547 2545 2548\\nCONECT 2548 2546 2547 2549\\nCONECT 2549 2548\\nCONECT 2550 2551\\nCONECT 2551 2550 2554 2552\\nCONECT 2552 2551 2553 2555\\nCONECT 2553 2552\\nCONECT 2554 2551\\nCONECT 2555 2556 2552\\nCONECT 2556 2555 2559 2557\\nCONECT 2557 2556 2558 2560\\nCONECT 2558 2557\\nCONECT 2559 2556\\nCONECT 2560 2561 2557\\nCONECT 2561 2560 2564 2562\\nCONECT 2562 2561 2563 2565\\nCONECT 2563 2562\\nCONECT 2564 2561\\nCONECT 2565 2566 2562\\nCONECT 2566 2565 2569 2567\\nCONECT 2567 2566 2568 2570\\nCONECT 2568 2567\\nCONECT 2569 2566\\nCONECT 2579 2580 2572\\nCONECT 2580 2579 2583 2581\\nCONECT 2581 2580 2582 2584\\nCONECT 2582 2581\\nCONECT 2583 2580\\nCONECT 2584 2585 2581\\nCONECT 2585 2584 2588 2586\\nCONECT 2586 2585 2587 2589\\nCONECT 2587 2586\\nCONECT 2588 2585\\nCONECT 2768 2769 2760\\nCONECT 2769 2768 2772 2770\\nCONECT 2770 2769 2771 2773\\nCONECT 2771 2770\\nCONECT 2772 2769\\nCONECT 2797 2798 2791\\nCONECT 2798 2797 2801 2799\\nCONECT 2799 2798 2800 2802\\nCONECT 2800 2799\\nCONECT 2801 2798\\nCONECT 2807 2818 2806\\nCONECT 2808 2809 2804\\nCONECT 2809 2808 2812 2810\\nCONECT 2810 2809 2811 2813\\nCONECT 2811 2810\\nCONECT 2812 2809\\nCONECT 2818 2807 2817\\nCONECT 2849 2850 2844\\nCONECT 2850 2849 2853 2851\\nCONECT 2851 2850 2852 2854\\nCONECT 2852 2851\\nCONECT 2853 2850\\nCONECT 2854 2855 2851\\nCONECT 2855 2854 2858 2856\\nCONECT 2856 2855 2857 2859\\nCONECT 2857 2856\\nCONECT 2858 2855\\nCONECT 3047 3048 3041\\nCONECT 3048 3047 3051 3049\\nCONECT 3049 3048 3050 3052\\nCONECT 3050 3049\\nCONECT 3051 3048\\nCONECT 3052 3053 3049\\nCONECT 3053 3052 3056 3054\\nCONECT 3054 3053 3055 3057\\nCONECT 3055 3054\\nCONECT 3056 3053\\nCONECT 3068 3069 3059\\nCONECT 3069 3068 3072 3070\\nCONECT 3070 3069 3071 3073\\nCONECT 3071 3070\\nCONECT 3072 3069\\nCONECT 3073 3074 3070\\nCONECT 3074 3073 3077 3075\\nCONECT 3075 3074 3076 3078\\nCONECT 3076 3075\\nCONECT 3077 3074\\nCONECT 3094 3095 3085\\nCONECT 3095 3094 3098 3096\\nCONECT 3096 3095 3097 3099\\nCONECT 3097 3096\\nCONECT 3098 3095\\nCONECT 3099 3100 3096\\nCONECT 3100 3099 3103 3101\\nCONECT 3101 3100 3102 3104\\nCONECT 3102 3101\\nCONECT 3103 3100\\nCONECT 3120 3121 3114\\nCONECT 3121 3120 3124 3122\\nCONECT 3122 3121 3123\\nCONECT 3123 3122\\nCONECT 3124 3121\\nEND\\n\",\"pdb\");\n",
       "\tviewer_1716807258080235.setStyle({\"model\": 0},{\"cartoon\": {}});\n",
       "\tviewer_1716807258080235.addSurface(null,{\"opacity\": 1, \"color\": \"lightgray\"});\n",
       "\tviewer_1716807258080235.addModels(\"HETATM    1 C72  UNL   1       10.837   5.700 -13.643  1.00  0.00           C  \\nHETATM    2 C73  UNL   1        9.571   4.916 -13.045  1.00  0.00           C  \\nHETATM    3 C74  UNL   1        8.776   4.163 -14.133  1.00  0.00           C  \\nHETATM    4 C75  UNL   1        7.481   3.608 -13.596  1.00  0.00           C  \\nHETATM    5 C76  UNL   1        7.109   2.292 -13.890  1.00  0.00           C  \\nHETATM    6 C77  UNL   1        5.885   1.799 -13.448  1.00  0.00           C  \\nHETATM    7 C78  UNL   1        5.020   2.619 -12.732  1.00  0.00           C  \\nHETATM    8 C79  UNL   1        5.373   3.937 -12.442  1.00  0.00           C  \\nHETATM    9 C80  UNL   1        6.613   4.443 -12.858  1.00  0.00           C  \\nHETATM   10 C81  UNL   1        7.097   5.844 -12.565  1.00  0.00           C  \\nHETATM   11 C82  UNL   1        8.613   5.728 -12.052  1.00  0.00           C  \\nHETATM   12 N9   UNL   1        8.638   5.029 -10.677  1.00  0.00           N1+\\nHETATM   13 N10  UNL   1        6.205   6.617 -11.640  1.00  0.00           N1+\\nHETATM   14 N11  UNL   1       12.101   4.963 -13.384  1.00  0.00           N1+\\nHETATM   15 C83  UNL   1       11.800   5.440 -15.876  1.00  0.00           C  \\nHETATM   16 O7   UNL   1       10.677   5.749 -15.050  1.00  0.00           O  \\nHETATM   17 C84  UNL   1       11.020   7.124 -12.977  1.00  0.00           C  \\nHETATM   18 C85  UNL   1       11.942   7.219 -11.725  1.00  0.00           C  \\nHETATM   19 C86  UNL   1       11.148   7.523 -10.423  1.00  0.00           C  \\nHETATM   20 C87  UNL   1       11.734   8.670  -9.566  1.00  0.00           C  \\nHETATM   21 O8   UNL   1       12.901   8.219  -8.867  1.00  0.00           O  \\nHETATM   22 C88  UNL   1       10.752   9.202  -8.473  1.00  0.00           C  \\nHETATM   23 N12  UNL   1       10.483   8.065  -7.514  1.00  0.00           N1+\\nHETATM   24 C89  UNL   1       10.638   8.197  -6.032  1.00  0.00           C  \\nHETATM   25 C90  UNL   1       11.400   7.030  -5.411  1.00  0.00           C  \\nHETATM   26 C91  UNL   1       11.356   7.156  -3.879  1.00  0.00           C  \\nHETATM   27 C92  UNL   1       11.652   8.560  -3.317  1.00  0.00           C  \\nHETATM   28 O9   UNL   1       11.218   9.629  -4.145  1.00  0.00           O  \\nHETATM   29 C93  UNL   1       11.327   9.481  -5.563  1.00  0.00           C  \\nHETATM   30 N13  UNL   1       13.054   8.692  -2.912  1.00  0.00           N1+\\nCONECT    1    2   14   16   17\\nCONECT    2    1    3   11\\nCONECT   14    1\\nCONECT   16    1   15\\nCONECT   17    1   18\\nCONECT    3    2    4\\nCONECT   11    2   10   12\\nCONECT    4    3    5    5    9\\nCONECT    5    4    4    6\\nCONECT    9    4    8    8   10\\nCONECT    6    5    7    7\\nCONECT    7    6    6    8\\nCONECT    8    7    9    9\\nCONECT   10    9   11   13\\nCONECT   13   10\\nCONECT   12   11\\nCONECT   15   16\\nCONECT   18   17   19\\nCONECT   19   18   20\\nCONECT   20   19   21   22\\nCONECT   21   20\\nCONECT   22   20   23\\nCONECT   23   22   24\\nCONECT   24   23   25   29\\nCONECT   25   24   26\\nCONECT   29   24   28\\nCONECT   26   25   27\\nCONECT   27   26   28   30\\nCONECT   28   27   29\\nCONECT   30   27\\nEND\",\"pdb\");\n",
       "\tviewer_1716807258080235.setStyle({\"model\": 1},{\"stick\": {\"color\": \"cyan\"}});\n",
       "\tviewer_1716807258080235.zoomTo();\n",
       "viewer_1716807258080235.render();\n",
       "});\n",
       "</script>"
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     "metadata": {},
     "output_type": "display_data"
    },
    {
     "data": {
      "application/3dmoljs_load.v0": "<div id=\"3dmolviewer_1716807258097742\"  style=\"position: relative; width: 800px; height: 600px;\">\n        <p id=\"3dmolwarning_1716807258097742\" style=\"background-color:#ffcccc;color:black\">You appear to be running in JupyterLab (or JavaScript failed to load for some other reason).  You need to install the 3dmol extension: <br>\n        <tt>jupyter labextension install jupyterlab_3dmol</tt></p>\n        </div>\n<script>\n\nvar loadScriptAsync = function(uri){\n  return new Promise((resolve, reject) => {\n    //this is to ignore the existence of requirejs amd\n    var savedexports, savedmodule;\n    if (typeof exports !== 'undefined') savedexports = exports;\n    else exports = {}\n    if (typeof module !== 'undefined') savedmodule = module;\n    else module = {}\n\n    var tag = document.createElement('script');\n    tag.src = uri;\n    tag.async = true;\n    tag.onload = () => {\n        exports = savedexports;\n        module = savedmodule;\n        resolve();\n    };\n  var firstScriptTag = document.getElementsByTagName('script')[0];\n  firstScriptTag.parentNode.insertBefore(tag, firstScriptTag);\n});\n};\n\nif(typeof $3Dmolpromise === 'undefined') {\n$3Dmolpromise = null;\n  $3Dmolpromise = loadScriptAsync('https://cdnjs.cloudflare.com/ajax/libs/3Dmol/2.0.3/3Dmol-min.js');\n}\n\nvar viewer_1716807258097742 = null;\nvar warn = document.getElementById(\"3dmolwarning_1716807258097742\");\nif(warn) {\n    warn.parentNode.removeChild(warn);\n}\n$3Dmolpromise.then(function() {\nviewer_1716807258097742 = $3Dmol.createViewer(document.getElementById(\"3dmolviewer_1716807258097742\"),{backgroundColor:\"white\"});\nviewer_1716807258097742.zoomTo();\n\tviewer_1716807258097742.addModels(\"HEADER    MEMBRANE PROTEIN                        02-MAR-18   6CM4              \\nTITLE     STRUCTURE OF THE D2 DOPAMINE RECEPTOR BOUND TO THE ATYPICAL           \\nTITLE    2 ANTIPSYCHOTIC DRUG RISPERIDONE                                       \\nCOMPND    MOL_ID: 1;                                                            \\nCOMPND   2 MOLECULE: D(2) DOPAMINE RECEPTOR, ENDOLYSIN CHIMERA;                 \\nCOMPND   3 CHAIN: A;                                                            \\nCOMPND   4 SYNONYM: DOPAMINE D2 RECEPTOR, LYSIS PROTEIN, LYSOZYME, MURAMIDASE,  \\nCOMPND   5 DOPAMINE D2 RECEPTOR;                                                \\nCOMPND   6 EC: 3.2.1.17;                                                        \\nCOMPND   7 ENGINEERED: YES                                                      \\nSOURCE    MOL_ID: 1;                                                            \\nSOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, ENTEROBACTERIA PHAGE T4;          \\nSOURCE   3 ORGANISM_COMMON: HUMAN, BACTERIOPHAGE T4;                            \\nSOURCE   4 ORGANISM_TAXID: 9606, 10665;                                         \\nSOURCE   5 GENE: DRD2, E, T4TP126;                                              \\nSOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            \\nSOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             \\nSOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;                                       \\nSOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          \\nSOURCE  10 EXPRESSION_SYSTEM_PLASMID: PFASTBAC1-HM                              \\nKEYWDS    GPCR, D2, DOPAMINE RECEPTOR, ANTIPSYCHOTIC, RISPERIDONE, MEMBRANE     \\nKEYWDS   2 PROTEIN                                                              \\nEXPDTA    X-RAY DIFFRACTION                                                     \\nAUTHOR    S.WANG,T.CHE,A.LEVIT,B.K.SHOICHET,D.WACKER,B.L.ROTH                   \\nREVDAT   6   04-OCT-23 6CM4    1       REMARK                                   \\nREVDAT   5   27-NOV-19 6CM4    1       REMARK                                   \\nREVDAT   4   20-FEB-19 6CM4    1       REMARK                                   \\nREVDAT   3   11-APR-18 6CM4    1       DBREF                                    \\nREVDAT   2   21-MAR-18 6CM4    1       JRNL                                     \\nREVDAT   1   14-MAR-18 6CM4    0                                                \\nSPRSDE     14-MAR-18 6CM4      6C38                                             \\nJRNL        AUTH   S.WANG,T.CHE,A.LEVIT,B.K.SHOICHET,D.WACKER,B.L.ROTH          \\nJRNL        TITL   STRUCTURE OF THE D2 DOPAMINE RECEPTOR BOUND TO THE ATYPICAL  \\nJRNL        TITL 2 ANTIPSYCHOTIC DRUG RISPERIDONE.                              \\nJRNL        REF    NATURE                        V. 555   269 2018              \\nJRNL        REFN                   ESSN 1476-4687                               \\nJRNL        PMID   29466326                                                     \\nJRNL        DOI    10.1038/NATURE25758                                          \\nREMARK   2                                                                      \\nREMARK   2 RESOLUTION.    2.87 ANGSTROMS.                                       \\nREMARK   3                                                                      \\nREMARK   3 REFINEMENT.                                                          \\nREMARK   3   PROGRAM     : PHENIX (1.12_2829: ???)                              \\nREMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            \\nREMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           \\nREMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            \\nREMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              \\nREMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               \\nREMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           \\nREMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  \\nREMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  \\nREMARK   3                                                                      \\nREMARK   3    REFINEMENT TARGET : ML                                            \\nREMARK   3                                                                      \\nREMARK   3  DATA USED IN REFINEMENT.                                            \\nREMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.87                           \\nREMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.55                          \\nREMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.360                          \\nREMARK   3   COMPLETENESS FOR RANGE        (%) : 95.2                           \\nREMARK   3   NUMBER OF REFLECTIONS             : 12814                          \\nREMARK   3                                                                      \\nREMARK   3  FIT TO DATA USED IN REFINEMENT.                                     \\nREMARK   3   R VALUE     (WORKING + TEST SET) : 0.227                           \\nREMARK   3   R VALUE            (WORKING SET) : 0.226                           \\nREMARK   3   FREE R VALUE                     : 0.249                           \\nREMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.850                           \\nREMARK   3   FREE R VALUE TEST SET COUNT      : 622                             \\nREMARK   3                                                                      \\nREMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           \\nREMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        \\nREMARK   3     1 29.5504 -  4.5475    0.98     3287   157  0.2103 0.2188        \\nREMARK   3     2  4.5475 -  3.6116    0.99     3151   170  0.2090 0.2511        \\nREMARK   3     3  3.6116 -  3.1556    0.99     3111   162  0.2730 0.3034        \\nREMARK   3     4  3.1556 -  2.8674    0.84     2643   133  0.3166 0.3214        \\nREMARK   3                                                                      \\nREMARK   3  BULK SOLVENT MODELLING.                                             \\nREMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       \\nREMARK   3   SOLVENT RADIUS     : 1.11                                          \\nREMARK   3   SHRINKAGE RADIUS   : 0.90                                          \\nREMARK   3   K_SOL              : NULL                                          \\nREMARK   3   B_SOL              : NULL                                          \\nREMARK   3                                                                      \\nREMARK   3  ERROR ESTIMATES.                                                    \\nREMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.390            \\nREMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.640           \\nREMARK   3                                                                      \\nREMARK   3  B VALUES.                                                           \\nREMARK   3   FROM WILSON PLOT           (A**2) : NULL                           \\nREMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           \\nREMARK   3   OVERALL ANISOTROPIC B VALUE.                                       \\nREMARK   3    B11 (A**2) : NULL                                                 \\nREMARK   3    B22 (A**2) : NULL                                                 \\nREMARK   3    B33 (A**2) : NULL                                                 \\nREMARK   3    B12 (A**2) : NULL                                                 \\nREMARK   3    B13 (A**2) : NULL                                                 \\nREMARK   3    B23 (A**2) : NULL                                                 \\nREMARK   3                                                                      \\nREMARK   3  TWINNING INFORMATION.                                               \\nREMARK   3   FRACTION: NULL                                                     \\nREMARK   3   OPERATOR: NULL                                                     \\nREMARK   3                                                                      \\nREMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       \\nREMARK   3                 RMSD          COUNT                                  \\nREMARK   3   BOND      :  0.003           3283                                  \\nREMARK   3   ANGLE     :  0.516           4483                                  \\nREMARK   3   CHIRALITY :  0.037            544                                  \\nREMARK   3   PLANARITY :  0.003            549                                  \\nREMARK   3   DIHEDRAL  : 10.862           1928                                  \\nREMARK   3                                                                      \\nREMARK   3  TLS DETAILS                                                         \\nREMARK   3   NUMBER OF TLS GROUPS  : 3                                          \\nREMARK   3   TLS GROUP : 1                                                      \\nREMARK   3    SELECTION: CHAIN 'A' AND (RESID 36 THROUGH 222 )                  \\nREMARK   3    ORIGIN FOR THE GROUP (A):   7.6595   9.9883   1.8227              \\nREMARK   3    T TENSOR                                                          \\nREMARK   3      T11:   0.3906 T22:   0.3948                                     \\nREMARK   3      T33:   0.4097 T12:  -0.0409                                     \\nREMARK   3      T13:   0.0298 T23:   0.0323                                     \\nREMARK   3    L TENSOR                                                          \\nREMARK   3      L11:   4.8704 L22:   2.9655                                     \\nREMARK   3      L33:   4.7317 L12:   0.7811                                     \\nREMARK   3      L13:   2.8181 L23:   1.4507                                     \\nREMARK   3    S TENSOR                                                          \\nREMARK   3      S11:   0.0593 S12:  -0.1051 S13:   0.0093                       \\nREMARK   3      S21:   0.1418 S22:  -0.1464 S23:   0.1356                       \\nREMARK   3      S31:   0.4299 S32:  -0.3974 S33:  -0.0137                       \\nREMARK   3   TLS GROUP : 2                                                      \\nREMARK   3    SELECTION: CHAIN 'A' AND (RESID 1002 THROUGH 1161 )               \\nREMARK   3    ORIGIN FOR THE GROUP (A):  32.7700  -7.7446  36.3658              \\nREMARK   3    T TENSOR                                                          \\nREMARK   3      T11:   0.6968 T22:   0.5198                                     \\nREMARK   3      T33:   0.5000 T12:   0.0363                                     \\nREMARK   3      T13:   0.0872 T23:   0.1084                                     \\nREMARK   3    L TENSOR                                                          \\nREMARK   3      L11:   6.6697 L22:   6.8821                                     \\nREMARK   3      L33:   6.4568 L12:   1.6541                                     \\nREMARK   3      L13:   1.9941 L23:   1.4205                                     \\nREMARK   3    S TENSOR                                                          \\nREMARK   3      S11:  -0.2551 S12:   0.1211 S13:  -0.2547                       \\nREMARK   3      S21:  -0.3908 S22:  -0.0566 S23:  -0.4642                       \\nREMARK   3      S31:   0.4711 S32:   0.2364 S33:   0.3147                       \\nREMARK   3   TLS GROUP : 3                                                      \\nREMARK   3    SELECTION: CHAIN 'A' AND (RESID 384 THROUGH 460 )                 \\nREMARK   3    ORIGIN FOR THE GROUP (A):   9.8885  -1.6530  -1.3224              \\nREMARK   3    T TENSOR                                                          \\nREMARK   3      T11:   0.6392 T22:   0.3770                                     \\nREMARK   3      T33:   0.5276 T12:   0.0087                                     \\nREMARK   3      T13:  -0.0908 T23:   0.0140                                     \\nREMARK   3    L TENSOR                                                          \\nREMARK   3      L11:   6.0244 L22:   5.3813                                     \\nREMARK   3      L33:   6.7255 L12:   0.3578                                     \\nREMARK   3      L13:   1.1698 L23:   0.5209                                     \\nREMARK   3    S TENSOR                                                          \\nREMARK   3      S11:  -0.0948 S12:   0.3307 S13:   0.0832                       \\nREMARK   3      S21:  -0.4022 S22:   0.2772 S23:  -0.0581                       \\nREMARK   3      S31:   1.2902 S32:  -0.0417 S33:  -0.2847                       \\nREMARK   3                                                                      \\nREMARK   3  NCS DETAILS                                                         \\nREMARK   3   NUMBER OF NCS GROUPS : NULL                                        \\nREMARK   3                                                                      \\nREMARK   3  OTHER REFINEMENT REMARKS: NULL                                      \\nREMARK   4                                                                      \\nREMARK   4 6CM4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         \\nREMARK 100                                                                      \\nREMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-MAR-18.                  \\nREMARK 100 THE DEPOSITION ID IS D_1000232947.                                   \\nREMARK 200                                                                      \\nREMARK 200 EXPERIMENTAL DETAILS                                                 \\nREMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  \\nREMARK 200  DATE OF DATA COLLECTION        : 13-AUG-17                          \\nREMARK 200  TEMPERATURE           (KELVIN) : 100                                \\nREMARK 200  PH                             : NULL                               \\nREMARK 200  NUMBER OF CRYSTALS USED        : 1                                  \\nREMARK 200                                                                      \\nREMARK 200  SYNCHROTRON              (Y/N) : Y                                  \\nREMARK 200  RADIATION SOURCE               : APS                                \\nREMARK 200  BEAMLINE                       : 23-ID-B                            \\nREMARK 200  X-RAY GENERATOR MODEL          : NULL                               \\nREMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  \\nREMARK 200  WAVELENGTH OR RANGE        (A) : 1.033                              \\nREMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL CRYO-COOLED         \\nREMARK 200                                   SI(111)                            \\nREMARK 200  OPTICS                         : NULL                               \\nREMARK 200                                                                      \\nREMARK 200  DETECTOR TYPE                  : PIXEL                              \\nREMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER X 16M                \\nREMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000                           \\nREMARK 200  DATA SCALING SOFTWARE          : HKL-3000                           \\nREMARK 200                                                                      \\nREMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 12826                              \\nREMARK 200  RESOLUTION RANGE HIGH      (A) : 2.867                              \\nREMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             \\nREMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               \\nREMARK 200                                                                      \\nREMARK 200 OVERALL.                                                             \\nREMARK 200  COMPLETENESS FOR RANGE     (%) : 97.3                               \\nREMARK 200  DATA REDUNDANCY                : 5.500                              \\nREMARK 200  R MERGE                    (I) : 0.13400                            \\nREMARK 200  R SYM                      (I) : NULL                               \\nREMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.2000                            \\nREMARK 200                                                                      \\nREMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     \\nREMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90                     \\nREMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.99                     \\nREMARK 200  COMPLETENESS FOR SHELL     (%) : 86.9                               \\nREMARK 200  DATA REDUNDANCY IN SHELL       : 2.50                               \\nREMARK 200  R MERGE FOR SHELL          (I) : 0.73800                            \\nREMARK 200  R SYM FOR SHELL            (I) : NULL                               \\nREMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.000                              \\nREMARK 200                                                                      \\nREMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              \\nREMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        \\nREMARK 200 SOFTWARE USED: PHASER                                                \\nREMARK 200 STARTING MODEL: PDB ENTRIES 5WIU & 2RH1                              \\nREMARK 200                                                                      \\nREMARK 200 REMARK: NULL                                                         \\nREMARK 280                                                                      \\nREMARK 280 CRYSTAL                                                              \\nREMARK 280 SOLVENT CONTENT, VS   (%): 57.13                                     \\nREMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.87                     \\nREMARK 280                                                                      \\nREMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM TRIS-HCL, PH 7.8, 230 MM          \\nREMARK 280  LITHIUM NITRATE, 25% PEG400, 4% 1,3-BUTANEDIOL, LIPIDIC CUBIC       \\nREMARK 280  PHASE, TEMPERATURE 293K                                             \\nREMARK 290                                                                      \\nREMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            \\nREMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       \\nREMARK 290                                                                      \\nREMARK 290      SYMOP   SYMMETRY                                                \\nREMARK 290     NNNMMM   OPERATOR                                                \\nREMARK 290       1555   X,Y,Z                                                   \\nREMARK 290       2555   -X+1/2,-Y,Z+1/2                                         \\nREMARK 290       3555   -X,Y+1/2,-Z+1/2                                         \\nREMARK 290       4555   X+1/2,-Y+1/2,-Z                                         \\nREMARK 290                                                                      \\nREMARK 290     WHERE NNN -> OPERATOR NUMBER                                     \\nREMARK 290           MMM -> TRANSLATION VECTOR                                  \\nREMARK 290                                                                      \\nREMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            \\nREMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             \\nREMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                \\nREMARK 290 RELATED MOLECULES.                                                   \\nREMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            \\nREMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            \\nREMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            \\nREMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       25.48950            \\nREMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            \\nREMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       75.65350            \\nREMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            \\nREMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       36.26150            \\nREMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       75.65350            \\nREMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       25.48950            \\nREMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       36.26150            \\nREMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            \\nREMARK 290                                                                      \\nREMARK 290 REMARK: NULL                                                         \\nREMARK 300                                                                      \\nREMARK 300 BIOMOLECULE: 1                                                       \\nREMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                \\nREMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  \\nREMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               \\nREMARK 300 BURIED SURFACE AREA.                                                 \\nREMARK 350                                                                      \\nREMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           \\nREMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                \\nREMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          \\nREMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          \\nREMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               \\nREMARK 350                                                                      \\nREMARK 350 BIOMOLECULE: 1                                                       \\nREMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         \\nREMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  \\nREMARK 350 SOFTWARE USED: PISA                                                  \\nREMARK 350 TOTAL BURIED SURFACE AREA: 1850 ANGSTROM**2                          \\nREMARK 350 SURFACE AREA OF THE COMPLEX: 20460 ANGSTROM**2                       \\nREMARK 350 CHANGE IN SOLVENT FREE ENERGY: 12.0 KCAL/MOL                         \\nREMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     \\nREMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            \\nREMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            \\nREMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            \\nREMARK 465                                                                      \\nREMARK 465 MISSING RESIDUES                                                     \\nREMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       \\nREMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               \\nREMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                \\nREMARK 465                                                                      \\nREMARK 465   M RES C SSSEQI                                                     \\nREMARK 465     MET A   140                                                      \\nREMARK 465     LEU A   141                                                      \\nREMARK 465     TYR A   142                                                      \\nREMARK 465     ASN A   143                                                      \\nREMARK 465     LYS A   362                                                      \\nREMARK 465     LEU A   363                                                      \\nREMARK 465     CYS A   443                                                      \\nREMARK 470                                                                      \\nREMARK 470 MISSING ATOM                                                         \\nREMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           \\nREMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          \\nREMARK 470 I=INSERTION CODE):                                                   \\nREMARK 470   M RES CSSEQI  ATOMS                                                \\nREMARK 470     ASN A  35    CG   OD1  ND2                                       \\nREMARK 470     TYR A  36    CG   CD1  CD2  CE1  CE2  CZ   OH                    \\nREMARK 470     LEU A  43    CG   CD1  CD2                                       \\nREMARK 470     GLU A  62    CG   CD   OE1  OE2                                  \\nREMARK 470     LYS A  63    CG   CD   CE   NZ                                   \\nREMARK 470     VAL A  96    CG1  CG2                                            \\nREMARK 470     GLU A  99    CG   CD   OE1  OE2                                  \\nREMARK 470     LYS A 101    CG   CD   CE   NZ                                   \\nREMARK 470     THR A 144    OG1  CG2                                            \\nREMARK 470     ARG A 145    CG   CD   NE   CZ   NH1  NH2                        \\nREMARK 470     SER A 147    OG                                                  \\nREMARK 470     LYS A 149    CG   CD   CE   NZ                                   \\nREMARK 470     ARG A 150    CG   CD   NE   CZ   NH1  NH2                        \\nREMARK 470     ASN A 176    CG   OD1  ND2                                       \\nREMARK 470     ASP A 178    CG   OD1  OD2                                       \\nREMARK 470     GLN A 179    CG   CD   OE1  NE2                                  \\nREMARK 470     ASN A 180    CG   OD1  ND2                                       \\nREMARK 470     LYS A 211    CE   NZ                                             \\nREMARK 470     ARG A 217    CG   CD   NE   CZ   NH1  NH2                        \\nREMARK 470     ARG A 218    CG   CD   NE   CZ   NH1  NH2                        \\nREMARK 470     LYS A 221    CG   CD   CE   NZ                                   \\nREMARK 470     ARG A 222    CG   CD   NE   CZ   NH1  NH2                        \\nREMARK 470     LYS A1016    CG   CD   CE   NZ                                   \\nREMARK 470     LYS A1019    CG   CD   CE   NZ                                   \\nREMARK 470     GLU A1022    CG   CD   OE1  OE2                                  \\nREMARK 470     LEU A1032    CG   CD1  CD2                                       \\nREMARK 470     LEU A1033    CG   CD1  CD2                                       \\nREMARK 470     LYS A1035    CG   CD   CE   NZ                                   \\nREMARK 470     SER A1036    OG                                                  \\nREMARK 470     SER A1038    OG                                                  \\nREMARK 470     ASN A1040    CG   OD1  ND2                                       \\nREMARK 470     SER A1044    OG                                                  \\nREMARK 470     GLU A1045    CG   CD   OE1  OE2                                  \\nREMARK 470     LYS A1048    CG   CD   CE   NZ                                   \\nREMARK 470     ILE A1050    CG1  CG2  CD1                                       \\nREMARK 470     ASN A1053    CG   OD1  ND2                                       \\nREMARK 470     THR A1054    OG1  CG2                                            \\nREMARK 470     ASN A1055    CG   OD1  ND2                                       \\nREMARK 470     VAL A1057    CG1  CG2                                            \\nREMARK 470     LYS A1060    CG   CD   CE   NZ                                   \\nREMARK 470     LYS A1065    CG   CD   CE   NZ                                   \\nREMARK 470     ARG A1080    CG   CD   NE   CZ   NH1  NH2                        \\nREMARK 470     LYS A1083    CG   CD   CE   NZ                                   \\nREMARK 470     LYS A1085    CG   CD   CE   NZ                                   \\nREMARK 470     ASN A1116    CG   OD1  ND2                                       \\nREMARK 470     ASP A1127    CG   OD1  OD2                                       \\nREMARK 470     VAL A1131    CG1  CG2                                            \\nREMARK 470     LYS A1135    CG   CD   CE   NZ                                   \\nREMARK 470     ARG A1137    CG   CD   NE   CZ   NH1  NH2                        \\nREMARK 470     GLN A1141    CG   CD   OE1  NE2                                  \\nREMARK 470     LYS A1147    CG   CD   CE   NZ                                   \\nREMARK 470     THR A1157    OG1  CG2                                            \\nREMARK 470     SER A 364    OG                                                  \\nREMARK 470     GLN A 365    CG   CD   OE1  NE2                                  \\nREMARK 470     GLN A 366    CG   CD   OE1  NE2                                  \\nREMARK 470     LYS A 367    CG   CD   CE   NZ                                   \\nREMARK 470     LYS A 369    CG   CD   CE   NZ                                   \\nREMARK 470     LYS A 370    CG   CD   CE   NZ                                   \\nREMARK 470     ILE A 394    CG1  CG2  CD1                                       \\nREMARK 470     HIS A 398    CG   ND1  CD2  CE1  NE2                             \\nREMARK 470     ASP A 400    CG   OD1  OD2                                       \\nREMARK 470     VAL A 406    CG1  CG2                                            \\nREMARK 470     LEU A 407    CG   CD1  CD2                                       \\nREMARK 470     ILE A 431    CG1  CG2  CD1                                       \\nREMARK 470     GLU A 432    CG   CD   OE1  OE2                                  \\nREMARK 470     ARG A 434    CG   CD   NE   CZ   NH1  NH2                        \\nREMARK 470     LYS A 435    CG   CD   CE   NZ                                   \\nREMARK 470     LEU A 438    CG   CD1  CD2                                       \\nREMARK 470     LYS A 439    CG   CD   CE   NZ                                   \\nREMARK 470     HIS A 442    CG   ND1  CD2  CE1  NE2                             \\nREMARK 500                                                                      \\nREMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         \\nREMARK 500 SUBTOPIC: TORSION ANGLES                                             \\nREMARK 500                                                                      \\nREMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            \\nREMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               \\nREMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             \\nREMARK 500                                                                      \\nREMARK 500 STANDARD TABLE:                                                      \\nREMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    \\nREMARK 500                                                                      \\nREMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           \\nREMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            \\nREMARK 500                                                                      \\nREMARK 500  M RES CSSEQI        PSI       PHI                                   \\nREMARK 500    GLN A  66       70.23   -104.22                                   \\nREMARK 500    VAL A  87      -52.46   -121.67                                   \\nREMARK 500    PHE A 198      -60.72   -124.56                                   \\nREMARK 500    ASN A1055       17.81     58.75                                   \\nREMARK 500    PHE A1114       49.44    -89.78                                   \\nREMARK 500    ASP A 400       11.47     57.92                                   \\nREMARK 500    LEU A 441       33.98    -88.55                                   \\nREMARK 500                                                                      \\nREMARK 500 REMARK: NULL                                                         \\nREMARK 610                                                                      \\nREMARK 610 MISSING HETEROATOM                                                   \\nREMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           \\nREMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          \\nREMARK 610 I=INSERTION CODE):                                                   \\nREMARK 610   M RES C SSEQI                                                      \\nREMARK 610     OLA A 2005                                                       \\nREMARK 610     OLA A 2006                                                       \\nDBREF  6CM4 A   35   222  UNP    P14416   DRD2_HUMAN      35    222             \\nDBREF  6CM4 A 1002  1161  UNP    D9IEF7   D9IEF7_BPT4      2    161             \\nDBREF  6CM4 A  362   443  UNP    P14416   DRD2_HUMAN     362    443             \\nSEQADV 6CM4 ALA A  122  UNP  P14416    ILE   122 CONFLICT                       \\nSEQADV 6CM4 THR A 1054  UNP  D9IEF7    CYS    54 CONFLICT                       \\nSEQADV 6CM4 ALA A 1097  UNP  D9IEF7    CYS    97 CONFLICT                       \\nSEQADV 6CM4 ALA A  375  UNP  P14416    LEU   375 CONFLICT                       \\nSEQADV 6CM4 ALA A  379  UNP  P14416    LEU   379 CONFLICT                       \\nSEQRES   1 A  430  ASN TYR TYR ALA THR LEU LEU THR LEU LEU ILE ALA VAL\\nSEQRES   2 A  430  ILE VAL PHE GLY ASN VAL LEU VAL CYS MET ALA VAL SER\\nSEQRES   3 A  430  ARG GLU LYS ALA LEU GLN THR THR THR ASN TYR LEU ILE\\nSEQRES   4 A  430  VAL SER LEU ALA VAL ALA ASP LEU LEU VAL ALA THR LEU\\nSEQRES   5 A  430  VAL MET PRO TRP VAL VAL TYR LEU GLU VAL VAL GLY GLU\\nSEQRES   6 A  430  TRP LYS PHE SER ARG ILE HIS CYS ASP ILE PHE VAL THR\\nSEQRES   7 A  430  LEU ASP VAL MET MET CYS THR ALA SER ALA LEU ASN LEU\\nSEQRES   8 A  430  CYS ALA ILE SER ILE ASP ARG TYR THR ALA VAL ALA MET\\nSEQRES   9 A  430  PRO MET LEU TYR ASN THR ARG TYR SER SER LYS ARG ARG\\nSEQRES  10 A  430  VAL THR VAL MET ILE SER ILE VAL TRP VAL LEU SER PHE\\nSEQRES  11 A  430  THR ILE SER CYS PRO LEU LEU PHE GLY LEU ASN ASN ALA\\nSEQRES  12 A  430  ASP GLN ASN GLU CYS ILE ILE ALA ASN PRO ALA PHE VAL\\nSEQRES  13 A  430  VAL TYR SER SER ILE VAL SER PHE TYR VAL PRO PHE ILE\\nSEQRES  14 A  430  VAL THR LEU LEU VAL TYR ILE LYS ILE TYR ILE VAL LEU\\nSEQRES  15 A  430  ARG ARG ARG ARG LYS ARG ASN ILE PHE GLU MET LEU ARG\\nSEQRES  16 A  430  ILE ASP GLU GLY LEU ARG LEU LYS ILE TYR LYS ASP THR\\nSEQRES  17 A  430  GLU GLY TYR TYR THR ILE GLY ILE GLY HIS LEU LEU THR\\nSEQRES  18 A  430  LYS SER PRO SER LEU ASN ALA ALA LYS SER GLU LEU ASP\\nSEQRES  19 A  430  LYS ALA ILE GLY ARG ASN THR ASN GLY VAL ILE THR LYS\\nSEQRES  20 A  430  ASP GLU ALA GLU LYS LEU PHE ASN GLN ASP VAL ASP ALA\\nSEQRES  21 A  430  ALA VAL ARG GLY ILE LEU ARG ASN ALA LYS LEU LYS PRO\\nSEQRES  22 A  430  VAL TYR ASP SER LEU ASP ALA VAL ARG ARG ALA ALA LEU\\nSEQRES  23 A  430  ILE ASN MET VAL PHE GLN MET GLY GLU THR GLY VAL ALA\\nSEQRES  24 A  430  GLY PHE THR ASN SER LEU ARG MET LEU GLN GLN LYS ARG\\nSEQRES  25 A  430  TRP ASP GLU ALA ALA VAL ASN LEU ALA LYS SER ARG TRP\\nSEQRES  26 A  430  TYR ASN GLN THR PRO ASN ARG ALA LYS ARG VAL ILE THR\\nSEQRES  27 A  430  THR PHE ARG THR GLY THR TRP ASP ALA TYR LYS LEU SER\\nSEQRES  28 A  430  GLN GLN LYS GLU LYS LYS ALA THR GLN MET ALA ALA ILE\\nSEQRES  29 A  430  VAL ALA GLY VAL PHE ILE ILE CYS TRP LEU PRO PHE PHE\\nSEQRES  30 A  430  ILE THR HIS ILE LEU ASN ILE HIS CYS ASP CYS ASN ILE\\nSEQRES  31 A  430  PRO PRO VAL LEU TYR SER ALA PHE THR TRP LEU GLY TYR\\nSEQRES  32 A  430  VAL ASN SER ALA VAL ASN PRO ILE ILE TYR THR THR PHE\\nSEQRES  33 A  430  ASN ILE GLU PHE ARG LYS ALA PHE LEU LYS ILE LEU HIS\\nSEQRES  34 A  430  CYS\\nHET    8NU  A2001      30                                                       \\nHET    PEG  A2002       7                                                       \\nHET    PEG  A2003       7                                                       \\nHET    PEG  A2004       7                                                       \\nHET    OLA  A2005      13                                                       \\nHET    OLA  A2006      12                                                       \\nHET    OLA  A2007      20                                                       \\nHETNAM     8NU 3-[2-[4-(6-FLUORANYL-1,2-BENZOXAZOL-3-YL)PIPERIDIN-1-            \\nHETNAM   2 8NU  YL]ETHYL]-2-METHYL-6,7,8,9-TETRAHYDROPYRIDO[1,2-                \\nHETNAM   3 8NU  A]PYRIMIDIN-4-ONE                                               \\nHETNAM     PEG DI(HYDROXYETHYL)ETHER                                            \\nHETNAM     OLA OLEIC ACID                                                       \\nFORMUL   2  8NU    C23 H27 F N4 O2                                              \\nFORMUL   3  PEG    3(C4 H10 O3)                                                 \\nFORMUL   6  OLA    3(C18 H34 O2)                                                \\nFORMUL   9  HOH   *16(H2 O)                                                     \\nHELIX    1   1 ASN A   35  GLU A   62  1                                  28\\nHELIX    2   2 LYS A   63  GLN A   66  1                                   4\\nHELIX    3   3 THR A   67  LEU A   86  1                                  20\\nHELIX    4   4 VAL A   87  GLY A   98  1                                  12\\nHELIX    5   5 SER A  103  MET A  138  1                                  36\\nHELIX    6   6 TYR A  146  CYS A  168  1                                  23\\nHELIX    7   7 PRO A  169  ASN A  176  1                                   8\\nHELIX    8   8 CYS A  182  ASN A  186  1                                   5\\nHELIX    9   9 ALA A  188  VAL A  196  1                                   9\\nHELIX   10  10 PHE A  198  GLU A 1011  1                                  35\\nHELIX   11  11 SER A 1038  GLY A 1051  1                                  14\\nHELIX   12  12 THR A 1059  ASN A 1081  1                                  23\\nHELIX   13  13 LEU A 1084  LEU A 1091  1                                   8\\nHELIX   14  14 ASP A 1092  ALA A 1112  1                                  21\\nHELIX   15  15 PHE A 1114  GLN A 1123  1                                  10\\nHELIX   16  16 ARG A 1125  ALA A 1134  1                                  10\\nHELIX   17  17 SER A 1136  GLN A 1141  1                                   6\\nHELIX   18  18 THR A 1142  GLY A 1156  1                                  15\\nHELIX   19  19 GLU A  368  CYS A  399  1                                  32\\nHELIX   20  20 PRO A  404  ASN A  418  1                                  15\\nHELIX   21  21 VAL A  421  PHE A  429  1                                   9\\nHELIX   22  22 ASN A  430  LEU A  441  1                                  12\\nSHEET    1   1 1 ARG A1014  LYS A1019  0\\nSHEET    2   2 1 TYR A1025  GLY A1028  0\\nSHEET    3   3 1 HIS A1031  THR A1034  0\\nSSBOND   1 CYS A  107    CYS A  182                          1555   1555  2.03\\nSSBOND   2 CYS A  399    CYS A  401                          1555   1555  2.04\\nCRYST1   50.979   72.523  151.307  90.00  90.00  90.00 P 21 21 21    4          \\nORIGX1      1.000000  0.000000  0.000000        0.00000                         \\nORIGX2      0.000000  1.000000  0.000000        0.00000                         \\nORIGX3      0.000000  0.000000  1.000000        0.00000                         \\nSCALE1      0.019616  0.000000  0.000000        0.00000                         \\nSCALE2      0.000000  0.013789  0.000000        0.00000                         \\nSCALE3      0.000000  0.000000  0.006609        0.00000                         \\nATOM      1  N   ASN A  35      -5.317  -8.666 -16.658  1.00108.95           N\\nATOM      2  CA  ASN A  35      -3.999  -9.279 -16.550  1.00112.41           C\\nATOM      3  C   ASN A  35      -3.770  -9.829 -15.148  1.00103.98           C\\nATOM      4  O   ASN A  35      -4.596  -9.642 -14.253  1.00111.14           O\\nATOM      5  CB  ASN A  35      -2.903  -8.271 -16.904  1.00115.88           C\\nATOM      6  N   TYR A  36      -2.640 -10.512 -14.962  1.00122.79           N\\nANISOU    6  N   TYR A  36    17290  13079  16284  -1997  -3163  -3043       N\\nATOM      7  CA  TYR A  36      -2.284 -11.046 -13.653  1.00105.49           C\\nANISOU    7  CA  TYR A  36    15314  10451  14315  -2168  -3210  -2776       C\\nATOM      8  C   TYR A  36      -1.522 -10.036 -12.804  1.00100.38           C\\nANISOU    8  C   TYR A  36    14564  10022  13555  -2013  -2870  -2480       C\\nATOM      9  O   TYR A  36      -1.767  -9.933 -11.597  1.00 95.60           O\\nANISOU    9  O   TYR A  36    13979   9308  13038  -2297  -2774  -2120       O\\nATOM     10  CB  TYR A  36      -1.455 -12.323 -13.811  1.00 98.01           C\\nANISOU   10  CB  TYR A  36    14721   8957  13564  -1967  -3571  -3071       C\\nATOM     11  N   TYR A  37      -0.606  -9.280 -13.416  1.00105.86           N\\nANISOU   11  N   TYR A  37    15140  11047  14036  -1589  -2687  -2627       N\\nATOM     12  CA  TYR A  37       0.202  -8.334 -12.652  1.00101.50           C\\nANISOU   12  CA  TYR A  37    14496  10678  13392  -1434  -2394  -2372       C\\nATOM     13  C   TYR A  37      -0.596  -7.105 -12.233  1.00 97.18           C\\nANISOU   13  C   TYR A  37    13669  10521  12732  -1638  -2109  -2055       C\\nATOM     14  O   TYR A  37      -0.269  -6.474 -11.221  1.00 92.55           O\\nANISOU   14  O   TYR A  37    13035   9983  12145  -1663  -1908  -1774       O\\nATOM     15  CB  TYR A  37       1.435  -7.931 -13.459  1.00105.43           C\\nANISOU   15  CB  TYR A  37    14938  11423  13698   -962  -2294  -2627       C\\nATOM     16  CG  TYR A  37       2.442  -9.052 -13.603  1.00112.39           C\\nANISOU   16  CG  TYR A  37    16060  11928  14715   -688  -2547  -2949       C\\nATOM     17  CD1 TYR A  37       2.745  -9.880 -12.528  1.00116.25           C\\nANISOU   17  CD1 TYR A  37    16804  11893  15472   -778  -2740  -2820       C\\nATOM     18  CD2 TYR A  37       3.084  -9.291 -14.814  1.00112.70           C\\nANISOU   18  CD2 TYR A  37    16070  12145  14606   -332  -2615  -3395       C\\nATOM     19  CE1 TYR A  37       3.662 -10.907 -12.650  1.00117.63           C\\nANISOU   19  CE1 TYR A  37    17203  11682  15808   -489  -3027  -3136       C\\nATOM     20  CE2 TYR A  37       4.002 -10.320 -14.944  1.00114.52           C\\nANISOU   20  CE2 TYR A  37    16488  12042  14980    -35  -2866  -3754       C\\nATOM     21  CZ  TYR A  37       4.287 -11.123 -13.860  1.00116.82           C\\nANISOU   21  CZ  TYR A  37    17037  11766  15584    -99  -3089  -3627       C\\nATOM     22  OH  TYR A  37       5.200 -12.147 -13.987  1.00116.76           O\\nANISOU   22  OH  TYR A  37    17222  11387  15756    236  -3393  -4004       O\\nATOM     23  N   ALA A  38      -1.639  -6.750 -12.985  1.00 96.22           N\\nANISOU   23  N   ALA A  38    13359  10676  12525  -1764  -2113  -2120       N\\nATOM     24  CA  ALA A  38      -2.506  -5.655 -12.566  1.00 90.24           C\\nANISOU   24  CA  ALA A  38    12324  10255  11709  -1946  -1899  -1864       C\\nATOM     25  C   ALA A  38      -3.348  -6.039 -11.356  1.00 93.14           C\\nANISOU   25  C   ALA A  38    12686  10447  12255  -2375  -1898  -1620       C\\nATOM     26  O   ALA A  38      -3.625  -5.191 -10.500  1.00 89.27           O\\nANISOU   26  O   ALA A  38    12015  10164  11737  -2476  -1673  -1375       O\\nATOM     27  CB  ALA A  38      -3.409  -5.222 -13.721  1.00 92.04           C\\nANISOU   27  CB  ALA A  38    12349  10812  11811  -1948  -1956  -2018       C\\nATOM     28  N   THR A  39      -3.759  -7.307 -11.265  1.00101.53           N\\nANISOU   28  N   THR A  39    13946  11141  13491  -2646  -2152  -1687       N\\nATOM     29  CA  THR A  39      -4.521  -7.761 -10.105  1.00 98.62           C\\nANISOU   29  CA  THR A  39    13594  10616  13261  -3121  -2155  -1423       C\\nATOM     30  C   THR A  39      -3.673  -7.706  -8.839  1.00 94.46           C\\nANISOU   30  C   THR A  39    13228   9915  12749  -3111  -2033  -1154       C\\nATOM     31  O   THR A  39      -4.127  -7.220  -7.795  1.00 90.19           O\\nANISOU   31  O   THR A  39    12545   9551  12174  -3363  -1831   -884       O\\nATOM     32  CB  THR A  39      -5.041  -9.178 -10.345  1.00 96.91           C\\nANISOU   32  CB  THR A  39    13602   9983  13235  -3430  -2502  -1538       C\\nATOM     33  OG1 THR A  39      -5.673  -9.242 -11.631  1.00 99.65           O\\nANISOU   33  OG1 THR A  39    13821  10489  13554  -3372  -2644  -1841       O\\nATOM     34  CG2 THR A  39      -6.044  -9.566  -9.272  1.00 85.14           C\\nANISOU   34  CG2 THR A  39    12068   8436  11847  -4016  -2487  -1245       C\\nATOM     35  N   LEU A  40      -2.434  -8.202  -8.915  1.00 91.92           N\\nANISOU   35  N   LEU A  40    13187   9271  12469  -2807  -2162  -1251       N\\nATOM     36  CA  LEU A  40      -1.537  -8.138  -7.766  1.00 89.55           C\\nANISOU   36  CA  LEU A  40    13043   8803  12179  -2751  -2081  -1015       C\\nATOM     37  C   LEU A  40      -1.335  -6.702  -7.304  1.00 83.76           C\\nANISOU   37  C   LEU A  40    12038   8512  11276  -2605  -1722   -856       C\\nATOM     38  O   LEU A  40      -1.301  -6.429  -6.098  1.00 87.36           O\\nANISOU   38  O   LEU A  40    12497   8987  11709  -2775  -1584   -580       O\\nATOM     39  CB  LEU A  40      -0.191  -8.777  -8.104  1.00 87.94           C\\nANISOU   39  CB  LEU A  40    13114   8249  12051  -2357  -2285  -1222       C\\nATOM     40  CG  LEU A  40      -0.166 -10.273  -8.417  1.00 86.57           C\\nANISOU   40  CG  LEU A  40    13274   7524  12094  -2433  -2707  -1405       C\\nATOM     41  CD1 LEU A  40       1.260 -10.798  -8.334  1.00 81.27           C\\nANISOU   41  CD1 LEU A  40    12855   6507  11518  -2029  -2890  -1557       C\\nATOM     42  CD2 LEU A  40      -1.085 -11.041  -7.480  1.00 87.43           C\\nANISOU   42  CD2 LEU A  40    13549   7331  12340  -3007  -2857  -1101       C\\nATOM     43  N   LEU A  41      -1.202  -5.770  -8.248  1.00 77.53           N\\nANISOU   43  N   LEU A  41    11027   8075  10356  -2302  -1588  -1023       N\\nATOM     44  CA  LEU A  41      -1.025  -4.372  -7.871  1.00 83.20           C\\nANISOU   44  CA  LEU A  41    11504   9166  10941  -2162  -1296   -879       C\\nATOM     45  C   LEU A  41      -2.242  -3.847  -7.120  1.00 91.88           C\\nANISOU   45  C   LEU A  41    12365  10511  12032  -2501  -1145   -694       C\\nATOM     46  O   LEU A  41      -2.101  -3.145  -6.111  1.00 94.79           O\\nANISOU   46  O   LEU A  41    12646  11017  12354  -2528   -951   -503       O\\nATOM     47  CB  LEU A  41      -0.739  -3.520  -9.108  1.00 84.35           C\\nANISOU   47  CB  LEU A  41    11487   9616  10946  -1830  -1231  -1064       C\\nATOM     48  CG  LEU A  41       0.684  -3.615  -9.668  1.00 84.82           C\\nANISOU   48  CG  LEU A  41    11682   9604  10941  -1449  -1257  -1222       C\\nATOM     49  CD1 LEU A  41       0.863  -2.686 -10.856  1.00 82.66           C\\nANISOU   49  CD1 LEU A  41    11233   9703  10473  -1206  -1167  -1345       C\\nATOM     50  CD2 LEU A  41       1.708  -3.304  -8.588  1.00 84.95           C\\nANISOU   50  CD2 LEU A  41    11768   9527  10981  -1340  -1134  -1042       C\\nATOM     51  N   THR A  42      -3.447  -4.187  -7.587  1.00 91.95           N\\nANISOU   51  N   THR A  42    12247  10603  12085  -2760  -1237   -778       N\\nATOM     52  CA  THR A  42      -4.651  -3.758  -6.883  1.00 87.42           C\\nANISOU   52  CA  THR A  42    11395  10312  11509  -3092  -1095   -650       C\\nATOM     53  C   THR A  42      -4.741  -4.405  -5.507  1.00 89.21           C\\nANISOU   53  C   THR A  42    11759  10370  11767  -3467  -1059   -402       C\\nATOM     54  O   THR A  42      -5.141  -3.757  -4.533  1.00 90.48           O\\nANISOU   54  O   THR A  42    11720  10805  11853  -3617   -841   -252       O\\nATOM     55  CB  THR A  42      -5.894  -4.085  -7.708  1.00 81.63           C\\nANISOU   55  CB  THR A  42    10483   9703  10829  -3302  -1229   -812       C\\nATOM     56  OG1 THR A  42      -5.719  -3.600  -9.045  1.00 80.89           O\\nANISOU   56  OG1 THR A  42    10326   9737  10673  -2956  -1306  -1030       O\\nATOM     57  CG2 THR A  42      -7.122  -3.427  -7.095  1.00 73.78           C\\nANISOU   57  CG2 THR A  42     9102   9107   9822  -3566  -1057   -743       C\\nATOM     58  N   LEU A  43      -4.372  -5.685  -5.408  1.00 89.32           N\\nANISOU   58  N   LEU A  43    12123   9933  11882  -3624  -1291   -363       N\\nATOM     59  CA  LEU A  43      -4.291  -6.324  -4.100  1.00 89.41           C\\nANISOU   59  CA  LEU A  43    12339   9733  11900  -3975  -1300    -78       C\\nATOM     60  C   LEU A  43      -3.297  -5.599  -3.203  1.00 85.76           C\\nANISOU   60  C   LEU A  43    11923   9332  11330  -3737  -1117     75       C\\nATOM     61  O   LEU A  43      -3.540  -5.429  -2.003  1.00 86.73           O\\nANISOU   61  O   LEU A  43    12007   9591  11355  -4009   -965    311       O\\nATOM     62  CB  LEU A  43      -3.907  -7.795  -4.254  1.00 92.73           C\\nANISOU   62  CB  LEU A  43    13182   9571  12480  -4106  -1657    -74       C\\nATOM     63  N   LEU A  44      -2.173  -5.155  -3.773  1.00 83.60           N\\nANISOU   63  N   LEU A  44    11715   8995  11055  -3246  -1124    -66       N\\nATOM     64  CA  LEU A  44      -1.214  -4.375  -3.000  1.00 85.11           C\\nANISOU   64  CA  LEU A  44    11914   9267  11155  -3006   -957     53       C\\nATOM     65  C   LEU A  44      -1.839  -3.078  -2.502  1.00 85.13           C\\nANISOU   65  C   LEU A  44    11557   9754  11035  -3039   -660    109       C\\nATOM     66  O   LEU A  44      -1.633  -2.688  -1.347  1.00 86.93           O\\nANISOU   66  O   LEU A  44    11776  10082  11172  -3118   -515    286       O\\nATOM     67  CB  LEU A  44       0.031  -4.082  -3.838  1.00 87.56           C\\nANISOU   67  CB  LEU A  44    12295   9491  11483  -2502  -1005   -135       C\\nATOM     68  CG  LEU A  44       1.048  -3.125  -3.207  1.00 86.61           C\\nANISOU   68  CG  LEU A  44    12129   9496  11281  -2230   -831    -46       C\\nATOM     69  CD1 LEU A  44       1.618  -3.719  -1.930  1.00 87.91           C\\nANISOU   69  CD1 LEU A  44    12554   9391  11458  -2363   -905    175       C\\nATOM     70  CD2 LEU A  44       2.164  -2.764  -4.177  1.00 83.34           C\\nANISOU   70  CD2 LEU A  44    11712   9091  10864  -1783   -849   -246       C\\nATOM     71  N   ILE A  45      -2.611  -2.400  -3.356  1.00 82.86           N\\nANISOU   71  N   ILE A  45    10974   9766  10745  -2965   -594    -59       N\\nATOM     72  CA  ILE A  45      -3.287  -1.172  -2.940  1.00 83.78           C\\nANISOU   72  CA  ILE A  45    10732  10317  10784  -2961   -364    -56       C\\nATOM     73  C   ILE A  45      -4.154  -1.429  -1.715  1.00 85.75           C\\nANISOU   73  C   ILE A  45    10876  10734  10969  -3402   -243     98       C\\nATOM     74  O   ILE A  45      -4.169  -0.633  -0.767  1.00 85.46           O\\nANISOU   74  O   ILE A  45    10685  10954  10832  -3395    -44    165       O\\nATOM     75  CB  ILE A  45      -4.118  -0.594  -4.101  1.00 80.09           C\\nANISOU   75  CB  ILE A  45     9986  10096  10350  -2847   -391   -260       C\\nATOM     76  CG1 ILE A  45      -3.232  -0.296  -5.309  1.00 82.72           C\\nANISOU   76  CG1 ILE A  45    10426  10322  10681  -2446   -492   -386       C\\nATOM     77  CG2 ILE A  45      -4.845   0.666  -3.657  1.00 71.03           C\\nANISOU   77  CG2 ILE A  45     8464   9363   9163  -2807   -205   -292       C\\nATOM     78  CD1 ILE A  45      -3.998   0.221  -6.511  1.00 85.25           C\\nANISOU   78  CD1 ILE A  45    10525  10865  11002  -2340   -563   -559       C\\nATOM     79  N   ALA A  46      -4.887  -2.544  -1.711  1.00 89.24           N\\nANISOU   79  N   ALA A  46    11398  11053  11455  -3812   -363    150       N\\nATOM     80  CA  ALA A  46      -5.719  -2.875  -0.560  1.00 84.99           C\\nANISOU   80  CA  ALA A  46    10762  10712  10819  -4309   -240    325       C\\nATOM     81  C   ALA A  46      -4.868  -3.120   0.678  1.00 86.02           C\\nANISOU   81  C   ALA A  46    11172  10680  10833  -4395   -199    583       C\\nATOM     82  O   ALA A  46      -5.201  -2.653   1.773  1.00 82.61           O\\nANISOU   82  O   ALA A  46    10575  10580  10232  -4584     19    688       O\\nATOM     83  CB  ALA A  46      -6.581  -4.096  -0.869  1.00 77.37           C\\nANISOU   83  CB  ALA A  46     9868   9590   9938  -4771   -418    360       C\\nATOM     84  N   VAL A  47      -3.758  -3.841   0.522  1.00 84.11           N\\nANISOU   84  N   VAL A  47    11343   9946  10669  -4238   -419    662       N\\nATOM     85  CA  VAL A  47      -2.894  -4.117   1.664  1.00 83.65           C\\nANISOU   85  CA  VAL A  47    11575   9696  10512  -4292   -436    908       C\\nATOM     86  C   VAL A  47      -2.272  -2.829   2.191  1.00 82.63           C\\nANISOU   86  C   VAL A  47    11279   9847  10269  -3948   -212    871       C\\nATOM     87  O   VAL A  47      -2.139  -2.644   3.406  1.00 89.41           O\\nANISOU   87  O   VAL A  47    12171  10845  10957  -4107    -91   1051       O\\nATOM     88  CB  VAL A  47      -1.826  -5.156   1.281  1.00 85.45           C\\nANISOU   88  CB  VAL A  47    12252   9322  10892  -4129   -768    941       C\\nATOM     89  CG1 VAL A  47      -0.873  -5.397   2.438  1.00 84.04           C\\nANISOU   89  CG1 VAL A  47    12375   8931  10627  -4135   -829   1190       C\\nATOM     90  CG2 VAL A  47      -2.490  -6.457   0.863  1.00 89.97           C\\nANISOU   90  CG2 VAL A  47    13015   9574  11594  -4506  -1029    979       C\\nATOM     91  N   ILE A  48      -1.893  -1.915   1.294  1.00 78.76           N\\nANISOU   91  N   ILE A  48    10618   9450   9859  -3495   -165    645       N\\nATOM     92  CA  ILE A  48      -1.320  -0.643   1.730  1.00 77.79           C\\nANISOU   92  CA  ILE A  48    10338   9559   9659  -3180     16    603       C\\nATOM     93  C   ILE A  48      -2.344   0.158   2.522  1.00 82.81           C\\nANISOU   93  C   ILE A  48    10623  10681  10158  -3375    261    582       C\\nATOM     94  O   ILE A  48      -2.025   0.749   3.560  1.00 85.46           O\\nANISOU   94  O   ILE A  48    10924  11187  10359  -3347    400    647       O\\nATOM     95  CB  ILE A  48      -0.797   0.158   0.525  1.00 76.69           C\\nANISOU   95  CB  ILE A  48    10090   9420   9628  -2722     -7    395       C\\nATOM     96  CG1 ILE A  48       0.350  -0.582  -0.162  1.00 81.09           C\\nANISOU   96  CG1 ILE A  48    10957   9571  10283  -2498   -216    373       C\\nATOM     97  CG2 ILE A  48      -0.339   1.535   0.969  1.00 73.83           C\\nANISOU   97  CG2 ILE A  48     9552   9290   9212  -2449    157    360       C\\nATOM     98  CD1 ILE A  48       0.859   0.105  -1.411  1.00 83.26           C\\nANISOU   98  CD1 ILE A  48    11128   9896  10613  -2110   -227    183       C\\nATOM     99  N   VAL A  49      -3.590   0.189   2.047  1.00 85.62           N\\nANISOU   99  N   VAL A  49    10696  11290  10545  -3560    309    458       N\\nATOM    100  CA  VAL A  49      -4.628   0.950   2.736  1.00 86.41           C\\nANISOU  100  CA  VAL A  49    10399  11901  10530  -3713    539    369       C\\nATOM    101  C   VAL A  49      -5.028   0.256   4.033  1.00 86.76           C\\nANISOU  101  C   VAL A  49    10505  12094  10367  -4215    646    582       C\\nATOM    102  O   VAL A  49      -5.154   0.896   5.083  1.00 84.97           O\\nANISOU  102  O   VAL A  49    10110  12216   9958  -4262    848    578       O\\nATOM    103  CB  VAL A  49      -5.837   1.166   1.811  1.00 85.12           C\\nANISOU  103  CB  VAL A  49     9887  11980  10477  -3747    531    151       C\\nATOM    104  CG1 VAL A  49      -7.004   1.745   2.592  1.00 88.42           C\\nANISOU  104  CG1 VAL A  49     9863  12953  10781  -3956    756     30       C\\nATOM    105  CG2 VAL A  49      -5.456   2.084   0.662  1.00 80.88           C\\nANISOU  105  CG2 VAL A  49     9274  11370  10087  -3251    439    -34       C\\nATOM    106  N   PHE A  50      -5.229  -1.063   3.980  1.00 87.95           N\\nANISOU  106  N   PHE A  50    10908  11980  10529  -4611    497    773       N\\nATOM    107  CA  PHE A  50      -5.635  -1.794   5.177  1.00 89.88           C\\nANISOU  107  CA  PHE A  50    11255  12333  10561  -5041    554   1009       C\\nATOM    108  C   PHE A  50      -4.604  -1.654   6.289  1.00 92.06           C\\nANISOU  108  C   PHE A  50    11792  12524  10663  -4962    580   1197       C\\nATOM    109  O   PHE A  50      -4.957  -1.394   7.445  1.00 93.62           O\\nANISOU  109  O   PHE A  50    11871  13085  10613  -5087    752   1242       O\\nATOM    110  CB  PHE A  50      -5.857  -3.269   4.846  1.00 88.37           C\\nANISOU  110  CB  PHE A  50    11370  11743  10463  -5313    300   1176       C\\nATOM    111  CG  PHE A  50      -6.166  -4.119   6.048  1.00 91.54           C\\nANISOU  111  CG  PHE A  50    11945  12184  10651  -5658    293   1438       C\\nATOM    112  CD1 PHE A  50      -7.465  -4.232   6.518  1.00 92.88           C\\nANISOU  112  CD1 PHE A  50    11823  12793  10672  -5976    452   1419       C\\nATOM    113  CD2 PHE A  50      -5.157  -4.805   6.708  1.00 90.81           C\\nANISOU  113  CD2 PHE A  50    12302  11702  10500  -5665    108   1698       C\\nATOM    114  CE1 PHE A  50      -7.752  -5.011   7.623  1.00 96.10           C\\nANISOU  114  CE1 PHE A  50    12394  13265  10853  -6335    441   1672       C\\nATOM    115  CE2 PHE A  50      -5.439  -5.583   7.816  1.00 94.85           C\\nANISOU  115  CE2 PHE A  50    12982  12260  10797  -6003     73   1952       C\\nATOM    116  CZ  PHE A  50      -6.737  -5.688   8.272  1.00 98.38           C\\nANISOU  116  CZ  PHE A  50    13146  13159  11074  -6358    245   1949       C\\nATOM    117  N   GLY A  51      -3.324  -1.822   5.959  1.00 89.17           N\\nANISOU  117  N   GLY A  51    11775  11692  10415  -4731    395   1283       N\\nATOM    118  CA  GLY A  51      -2.301  -1.796   6.988  1.00 84.51           C\\nANISOU  118  CA  GLY A  51    11458  10976   9676  -4664    370   1475       C\\nATOM    119  C   GLY A  51      -2.075  -0.415   7.573  1.00 79.23           C\\nANISOU  119  C   GLY A  51    10517  10705   8881  -4366    607   1313       C\\nATOM    120  O   GLY A  51      -1.800  -0.278   8.767  1.00 79.21           O\\nANISOU  120  O   GLY A  51    10593  10866   8639  -4497    694   1454       O\\nATOM    121  N   ASN A  52      -2.183   0.626   6.746  1.00 74.87           N\\nANISOU  121  N   ASN A  52     9661  10300   8487  -3969    686   1017       N\\nATOM    122  CA  ASN A  52      -1.869   1.971   7.213  1.00 72.04           C\\nANISOU  122  CA  ASN A  52     9081  10223   8066  -3641    847    847       C\\nATOM    123  C   ASN A  52      -3.057   2.680   7.841  1.00 76.56           C\\nANISOU  123  C   ASN A  52     9223  11393   8475  -3813   1107    674       C\\nATOM    124  O   ASN A  52      -2.860   3.566   8.681  1.00 76.05           O\\nANISOU  124  O   ASN A  52     9026  11599   8272  -3672   1243    574       O\\nATOM    125  CB  ASN A  52      -1.305   2.809   6.069  1.00 68.61           C\\nANISOU  125  CB  ASN A  52     8565   9624   7879  -3132    768    642       C\\nATOM    126  CG  ASN A  52       0.113   2.416   5.715  1.00 79.96           C\\nANISOU  126  CG  ASN A  52    10362  10592   9427  -2882    569    754       C\\nATOM    127  OD1 ASN A  52       1.065   2.835   6.370  1.00 77.35           O\\nANISOU  127  OD1 ASN A  52    10144  10206   9041  -2704    566    802       O\\nATOM    128  ND2 ASN A  52       0.261   1.600   4.681  1.00 80.13           N\\nANISOU  128  ND2 ASN A  52    10547  10294   9604  -2861    393    767       N\\nATOM    129  N   VAL A  53      -4.286   2.318   7.468  1.00 82.38           N\\nANISOU  129  N   VAL A  53     9715  12360   9224  -4106   1170    606       N\\nATOM    130  CA  VAL A  53      -5.441   2.817   8.209  1.00 86.81           C\\nANISOU  130  CA  VAL A  53     9853  13535   9597  -4309   1419    435       C\\nATOM    131  C   VAL A  53      -5.398   2.300   9.643  1.00 91.28           C\\nANISOU  131  C   VAL A  53    10607  14230   9845  -4566   1474    633       C\\nATOM    132  O   VAL A  53      -5.768   3.009  10.588  1.00 98.44           O\\nANISOU  132  O   VAL A  53    11273  15582  10548  -4528   1653    471       O\\nATOM    133  CB  VAL A  53      -6.751   2.433   7.494  1.00 83.17           C\\nANISOU  133  CB  VAL A  53     9126  13231   9243  -4473   1406    307       C\\nATOM    134  CG1 VAL A  53      -7.949   2.691   8.387  1.00 78.74           C\\nANISOU  134  CG1 VAL A  53     8217  13227   8475  -4616   1596    143       C\\nATOM    135  CG2 VAL A  53      -6.893   3.217   6.198  1.00 79.84           C\\nANISOU  135  CG2 VAL A  53     8453  12777   9107  -4129   1341     45       C\\nATOM    136  N   LEU A  54      -4.923   1.065   9.827  1.00 86.53           N\\nANISOU  136  N   LEU A  54    10442  13233   9201  -4813   1292    968       N\\nATOM    137  CA  LEU A  54      -4.726   0.529  11.172  1.00 88.26           C\\nANISOU  137  CA  LEU A  54    10891  13520   9123  -5054   1288   1196       C\\nATOM    138  C   LEU A  54      -3.747   1.383  11.968  1.00 86.94           C\\nANISOU  138  C   LEU A  54    10787  13428   8817  -4810   1356   1171       C\\nATOM    139  O   LEU A  54      -4.002   1.722  13.130  1.00 94.33           O\\nANISOU  139  O   LEU A  54    11611  14759   9469  -4901   1496   1127       O\\nATOM    140  CB  LEU A  54      -4.224  -0.914  11.097  1.00 90.28           C\\nANISOU  140  CB  LEU A  54    11637  13240   9427  -5281   1006   1548       C\\nATOM    141  CG  LEU A  54      -5.198  -2.030  10.729  1.00 92.89           C\\nANISOU  141  CG  LEU A  54    11990  13500   9806  -5638    909   1650       C\\nATOM    142  CD1 LEU A  54      -4.459  -3.354  10.614  1.00 97.20           C\\nANISOU  142  CD1 LEU A  54    13055  13428  10449  -5757    575   1961       C\\nATOM    143  CD2 LEU A  54      -6.301  -2.128  11.763  1.00 96.43           C\\nANISOU  143  CD2 LEU A  54    12213  14478   9948  -5990   1090   1654       C\\nATOM    144  N   VAL A  55      -2.613   1.737  11.356  1.00 84.36           N\\nANISOU  144  N   VAL A  55    10638  12737   8678  -4508   1252   1188       N\\nATOM    145  CA  VAL A  55      -1.593   2.518  12.053  1.00 89.47           C\\nANISOU  145  CA  VAL A  55    11371  13417   9208  -4276   1291   1178       C\\nATOM    146  C   VAL A  55      -2.164   3.838  12.551  1.00 92.31           C\\nANISOU  146  C   VAL A  55    11279  14347   9446  -4112   1550    831       C\\nATOM    147  O   VAL A  55      -1.801   4.314  13.634  1.00 95.44           O\\nANISOU  147  O   VAL A  55    11689  14966   9606  -4066   1624    802       O\\nATOM    148  CB  VAL A  55      -0.374   2.741  11.133  1.00 85.96           C\\nANISOU  148  CB  VAL A  55    11134  12447   9082  -3803   1074   1151       C\\nATOM    149  CG1 VAL A  55       0.679   3.587  11.829  1.00 76.85           C\\nANISOU  149  CG1 VAL A  55    10045  11292   7864  -3476   1063   1092       C\\nATOM    150  CG2 VAL A  55       0.217   1.408  10.697  1.00 86.37           C\\nANISOU  150  CG2 VAL A  55    11619  11948   9251  -3934    799   1439       C\\nATOM    151  N   CYS A  56      -3.075   4.442  11.786  1.00 85.56           N\\nANISOU  151  N   CYS A  56    10018  13731   8759  -3998   1660    538       N\\nATOM    152  CA  CYS A  56      -3.627   5.737  12.175  1.00 80.56           C\\nANISOU  152  CA  CYS A  56     8941  13592   8075  -3762   1850    148       C\\nATOM    153  C   CYS A  56      -4.603   5.598  13.334  1.00 86.48           C\\nANISOU  153  C   CYS A  56     9514  14821   8522  -4005   1984     66       C\\nATOM    154  O   CYS A  56      -4.495   6.313  14.337  1.00 84.77           O\\nANISOU  154  O   CYS A  56     9186  14923   8102  -3899   2089   -102       O\\nATOM    155  CB  CYS A  56      -4.301   6.398  10.975  1.00 67.26           C\\nANISOU  155  CB  CYS A  56     6920  11917   6720  -3468   1818   -150       C\\nATOM    156  SG  CYS A  56      -3.139   6.859   9.688  1.00 71.11           S\\nANISOU  156  SG  CYS A  56     7652  11761   7605  -2939   1540   -134       S\\nATOM    157  N   MET A  57      -5.565   4.680  13.217  1.00 89.30           N\\nANISOU  157  N   MET A  57     9839  15250   8838  -4343   1978    170       N\\nATOM    158  CA  MET A  57      -6.547   4.508  14.283  1.00 99.11           C\\nANISOU  158  CA  MET A  57    10893  16987   9777  -4621   2115     99       C\\nATOM    159  C   MET A  57      -5.891   4.028  15.570  1.00100.31           C\\nANISOU  159  C   MET A  57    11370  17145   9601  -4843   2094    365       C\\nATOM    160  O   MET A  57      -6.282   4.448  16.665  1.00109.98           O\\nANISOU  160  O   MET A  57    12410  18838  10541  -4909   2235    210       O\\nATOM    161  CB  MET A  57      -7.633   3.529  13.845  1.00106.16           C\\nANISOU  161  CB  MET A  57    11719  17920  10695  -4975   2095    198       C\\nATOM    162  CG  MET A  57      -8.458   4.012  12.672  1.00104.93           C\\nANISOU  162  CG  MET A  57    11195  17843  10830  -4777   2113    -94       C\\nATOM    163  SD  MET A  57      -9.729   2.811  12.239  1.00106.23           S\\nANISOU  163  SD  MET A  57    11291  18073  11000  -5226   2085     28       S\\nATOM    164  CE  MET A  57      -8.718   1.360  11.965  1.00104.77           C\\nANISOU  164  CE  MET A  57    11736  17203  10870  -5491   1838    545       C\\nATOM    165  N   ALA A  58      -4.891   3.151  15.458  1.00 91.70           N\\nANISOU  165  N   ALA A  58    10761  15535   8547  -4945   1896    749       N\\nATOM    166  CA  ALA A  58      -4.253   2.590  16.647  1.00 94.86           C\\nANISOU  166  CA  ALA A  58    11502  15887   8653  -5159   1819   1033       C\\nATOM    167  C   ALA A  58      -3.578   3.673  17.478  1.00 93.98           C\\nANISOU  167  C   ALA A  58    11323  16005   8380  -4887   1912    851       C\\nATOM    168  O   ALA A  58      -3.795   3.769  18.691  1.00 97.13           O\\nANISOU  168  O   ALA A  58    11671  16787   8447  -5049   2002    828       O\\nATOM    169  CB  ALA A  58      -3.240   1.521  16.244  1.00 92.30           C\\nANISOU  169  CB  ALA A  58    11700  14899   8471  -5223   1532   1429       C\\nATOM    170  N   VAL A  59      -2.740   4.492  16.841  1.00 96.30           N\\nANISOU  170  N   VAL A  59    11619  16077   8895  -4483   1883    717       N\\nATOM    171  CA  VAL A  59      -2.102   5.595  17.551  1.00 91.92           C\\nANISOU  171  CA  VAL A  59    10983  15733   8211  -4197   1959    504       C\\nATOM    172  C   VAL A  59      -3.144   6.585  18.045  1.00 91.74           C\\nANISOU  172  C   VAL A  59    10460  16322   8077  -4097   2177     56       C\\nATOM    173  O   VAL A  59      -2.990   7.184  19.117  1.00 99.07           O\\nANISOU  173  O   VAL A  59    11313  17573   8756  -4030   2251   -105       O\\nATOM    174  CB  VAL A  59      -1.062   6.271  16.638  1.00 84.96           C\\nANISOU  174  CB  VAL A  59    10179  14491   7608  -3805   1881    441       C\\nATOM    175  CG1 VAL A  59      -0.446   7.484  17.318  1.00 88.37           C\\nANISOU  175  CG1 VAL A  59    10505  15150   7923  -3491   1949    173       C\\nATOM    176  CG2 VAL A  59       0.009   5.267  16.235  1.00 77.23           C\\nANISOU  176  CG2 VAL A  59     9704  12913   6729  -3889   1637    864       C\\nATOM    177  N   SER A  60      -4.229   6.759  17.291  1.00 95.26           N\\nANISOU  177  N   SER A  60    10557  16933   8706  -4072   2257   -169       N\\nATOM    178  CA  SER A  60      -5.247   7.733  17.658  1.00 98.05           C\\nANISOU  178  CA  SER A  60    10416  17831   9007  -3917   2417   -638       C\\nATOM    179  C   SER A  60      -6.057   7.307  18.875  1.00104.36           C\\nANISOU  179  C   SER A  60    11113  19121   9420  -4286   2535   -633       C\\nATOM    180  O   SER A  60      -6.732   8.148  19.479  1.00107.43           O\\nANISOU  180  O   SER A  60    11125  20003   9691  -4157   2661  -1033       O\\nATOM    181  CB  SER A  60      -6.183   7.974  16.473  1.00 97.14           C\\nANISOU  181  CB  SER A  60     9973  17730   9205  -3784   2427   -864       C\\nATOM    182  OG  SER A  60      -7.148   8.967  16.770  1.00 99.99           O\\nANISOU  182  OG  SER A  60     9859  18573   9559  -3574   2531  -1349       O\\nATOM    183  N   ARG A  61      -6.003   6.030  19.255  1.00 98.78           N\\nANISOU  183  N   ARG A  61    10729  18286   8518  -4738   2478   -202       N\\nATOM    184  CA  ARG A  61      -6.880   5.512  20.291  1.00103.46           C\\nANISOU  184  CA  ARG A  61    11212  19353   8745  -5156   2589   -162       C\\nATOM    185  C   ARG A  61      -6.159   4.772  21.410  1.00107.55           C\\nANISOU  185  C   ARG A  61    12131  19803   8928  -5464   2513    219       C\\nATOM    186  O   ARG A  61      -6.808   4.395  22.392  1.00117.52           O\\nANISOU  186  O   ARG A  61    13311  21498   9842  -5828   2609    262       O\\nATOM    187  CB  ARG A  61      -7.937   4.590  19.664  1.00104.53           C\\nANISOU  187  CB  ARG A  61    11265  19502   8951  -5497   2593    -37       C\\nATOM    188  CG  ARG A  61      -8.730   5.267  18.557  1.00 96.67           C\\nANISOU  188  CG  ARG A  61     9865  18588   8277  -5209   2647   -407       C\\nATOM    189  CD  ARG A  61     -10.016   4.534  18.248  1.00108.57           C\\nANISOU  189  CD  ARG A  61    11174  20320   9758  -5564   2702   -387       C\\nATOM    190  NE  ARG A  61      -9.801   3.362  17.409  1.00109.71           N\\nANISOU  190  NE  ARG A  61    11662  19943  10079  -5797   2536     11       N\\nATOM    191  CZ  ARG A  61     -10.778   2.566  16.987  1.00115.93           C\\nANISOU  191  CZ  ARG A  61    12357  20800  10890  -6123   2537     93       C\\nATOM    192  NH1 ARG A  61     -12.034   2.820  17.330  1.00116.46           N\\nANISOU  192  NH1 ARG A  61    11988  21459  10801  -6264   2710   -185       N\\nATOM    193  NH2 ARG A  61     -10.501   1.519  16.223  1.00119.11           N\\nANISOU  193  NH2 ARG A  61    13096  20686  11475  -6303   2354    434       N\\nATOM    194  N   GLU A  62      -4.853   4.558  21.301  1.00 96.97           N\\nANISOU  194  N   GLU A  62    11215  17953   7675  -5333   2333    491       N\\nATOM    195  CA  GLU A  62      -4.083   3.859  22.320  1.00101.43           C\\nANISOU  195  CA  GLU A  62    12192  18393   7956  -5580   2207    858       C\\nATOM    196  C   GLU A  62      -3.184   4.851  23.046  1.00102.22           C\\nANISOU  196  C   GLU A  62    12307  18603   7928  -5257   2227    678       C\\nATOM    197  O   GLU A  62      -2.426   5.591  22.409  1.00 92.57           O\\nANISOU  197  O   GLU A  62    11100  17116   6955  -4842   2178    531       O\\nATOM    198  CB  GLU A  62      -3.246   2.737  21.703  1.00100.84           C\\nANISOU  198  CB  GLU A  62    12621  17618   8074  -5678   1928   1315       C\\nATOM    199  N   LYS A  63      -3.269   4.854  24.378  1.00108.00           N\\nANISOU  199  N   LYS A  63    13040  19738   8259  -5463   2293    691       N\\nATOM    200  CA  LYS A  63      -2.467   5.770  25.183  1.00106.16           C\\nANISOU  200  CA  LYS A  63    12820  19652   7864  -5180   2305    504       C\\nATOM    201  C   LYS A  63      -0.976   5.535  24.970  1.00 98.83           C\\nANISOU  201  C   LYS A  63    12367  18125   7059  -4996   2054    800       C\\nATOM    202  O   LYS A  63      -0.243   6.439  24.552  1.00 90.24           O\\nANISOU  202  O   LYS A  63    11250  16879   6157  -4571   2024    584       O\\nATOM    203  CB  LYS A  63      -2.833   5.616  26.660  1.00114.28           C\\nANISOU  203  CB  LYS A  63    13807  21206   8408  -5502   2401    526       C\\nATOM    204  N   ALA A  64      -0.510   4.312  25.239  1.00108.15           N\\nANISOU  204  N   ALA A  64    13988  18956   8148  -5308   1844   1286       N\\nATOM    205  CA  ALA A  64       0.917   4.011  25.200  1.00103.75           C\\nANISOU  205  CA  ALA A  64    13892  17853   7678  -5142   1563   1569       C\\nATOM    206  C   ALA A  64       1.513   4.169  23.805  1.00 99.33           C\\nANISOU  206  C   ALA A  64    13405  16779   7558  -4812   1452   1552       C\\nATOM    207  O   ALA A  64       2.735   4.041  23.649  1.00 84.58           O\\nANISOU  207  O   ALA A  64    11875  14464   5799  -4615   1215   1732       O\\nATOM    208  CB  ALA A  64       1.164   2.590  25.719  1.00103.60           C\\nANISOU  208  CB  ALA A  64    14310  17538   7516  -5540   1320   2073       C\\nATOM    209  N   LEU A  65       0.685   4.450  22.798  1.00 91.85           N\\nANISOU  209  N   LEU A  65    12140  15902   6858  -4745   1606   1334       N\\nATOM    210  CA  LEU A  65       1.126   4.676  21.429  1.00 92.45           C\\nANISOU  210  CA  LEU A  65    12233  15560   7334  -4450   1535   1288       C\\nATOM    211  C   LEU A  65       1.071   6.143  21.021  1.00 91.55           C\\nANISOU  211  C   LEU A  65    11741  15700   7344  -4047   1715    824       C\\nATOM    212  O   LEU A  65       1.216   6.447  19.835  1.00 98.95           O\\nANISOU  212  O   LEU A  65    12606  16387   8603  -3825   1705    736       O\\nATOM    213  CB  LEU A  65       0.282   3.842  20.465  1.00 91.67           C\\nANISOU  213  CB  LEU A  65    12087  15284   7459  -4662   1529   1402       C\\nATOM    214  CG  LEU A  65       0.533   2.337  20.472  1.00 96.52           C\\nANISOU  214  CG  LEU A  65    13133  15448   8091  -4973   1266   1854       C\\nATOM    215  CD1 LEU A  65      -0.389   1.627  19.490  1.00101.66           C\\nANISOU  215  CD1 LEU A  65    13694  15972   8962  -5162   1269   1895       C\\nATOM    216  CD2 LEU A  65       1.987   2.059  20.143  1.00 88.49           C\\nANISOU  216  CD2 LEU A  65    12531  13837   7256  -4733    974   2071       C\\nATOM    217  N   GLN A  66       0.870   7.056  21.966  1.00 97.64           N\\nANISOU  217  N   GLN A  66    12271  16951   7878  -3940   1858    509       N\\nATOM    218  CA  GLN A  66       0.729   8.476  21.643  1.00 91.59           C\\nANISOU  218  CA  GLN A  66    11125  16421   7256  -3531   1991      9       C\\nATOM    219  C   GLN A  66       2.014   9.220  22.003  1.00 88.27           C\\nANISOU  219  C   GLN A  66    10883  15873   6783  -3219   1872    -76       C\\nATOM    220  O   GLN A  66       2.081  10.015  22.940  1.00 95.43           O\\nANISOU  220  O   GLN A  66    11654  17116   7488  -3077   1921   -364       O\\nATOM    221  CB  GLN A  66      -0.488   9.060  22.354  1.00 94.21           C\\nANISOU  221  CB  GLN A  66    11011  17366   7418  -3569   2200   -377       C\\nATOM    222  CG  GLN A  66      -1.806   8.615  21.747  1.00 90.38           C\\nANISOU  222  CG  GLN A  66    10255  17032   7053  -3778   2313   -412       C\\nATOM    223  CD  GLN A  66      -3.010   9.067  22.544  1.00 98.45           C\\nANISOU  223  CD  GLN A  66    10853  18690   7865  -3861   2497   -767       C\\nATOM    224  OE1 GLN A  66      -2.887   9.506  23.689  1.00102.35           O\\nANISOU  224  OE1 GLN A  66    11295  19524   8070  -3847   2548   -921       O\\nATOM    225  NE2 GLN A  66      -4.187   8.960  21.941  1.00101.41           N\\nANISOU  225  NE2 GLN A  66    10914  19243   8376  -3945   2588   -913       N\\nATOM    226  N   THR A  67       3.049   8.942  21.221  1.00 81.40           N\\nANISOU  226  N   THR A  67    10313  14420   6193  -3058   1648    159       N\\nATOM    227  CA  THR A  67       4.366   9.523  21.416  1.00 80.16           C\\nANISOU  227  CA  THR A  67    10341  13928   6189  -2690   1412    112       C\\nATOM    228  C   THR A  67       4.724  10.396  20.219  1.00 81.81           C\\nANISOU  228  C   THR A  67    10385  13739   6959  -2223   1303   -122       C\\nATOM    229  O   THR A  67       4.047  10.388  19.187  1.00 83.11           O\\nANISOU  229  O   THR A  67    10366  13821   7392  -2189   1372   -182       O\\nATOM    230  CB  THR A  67       5.424   8.430  21.618  1.00 74.28           C\\nANISOU  230  CB  THR A  67    10089  12752   5384  -2838   1150    588       C\\nATOM    231  OG1 THR A  67       5.732   7.823  20.359  1.00 77.15           O\\nANISOU  231  OG1 THR A  67    10579  12565   6169  -2749   1000    784       O\\nATOM    232  CG2 THR A  67       4.909   7.358  22.566  1.00 76.90           C\\nANISOU  232  CG2 THR A  67    10631  13398   5190  -3391   1228    928       C\\nATOM    233  N   THR A  68       5.803  11.165  20.370  1.00 86.60           N\\nANISOU  233  N   THR A  68    11062  14111   7731  -1884   1119   -244       N\\nATOM    234  CA  THR A  68       6.274  11.984  19.259  1.00 81.90           C\\nANISOU  234  CA  THR A  68    10353  13120   7646  -1492    990   -405       C\\nATOM    235  C   THR A  68       6.614  11.116  18.055  1.00 76.38           C\\nANISOU  235  C   THR A  68     9828  11956   7236  -1519    883    -94       C\\nATOM    236  O   THR A  68       6.157  11.379  16.939  1.00 74.99           O\\nANISOU  236  O   THR A  68     9479  11652   7360  -1401    915   -182       O\\nATOM    237  CB  THR A  68       7.490  12.816  19.681  1.00 80.77           C\\nANISOU  237  CB  THR A  68    10291  12786   7611  -1198    788   -526       C\\nATOM    238  OG1 THR A  68       8.582  11.948  20.014  1.00 75.97           O\\nANISOU  238  OG1 THR A  68    10037  11917   6911  -1290    604   -182       O\\nATOM    239  CG2 THR A  68       7.155  13.692  20.878  1.00 83.25           C\\nANISOU  239  CG2 THR A  68    10436  13561   7636  -1147    872   -884       C\\nATOM    240  N   THR A  69       7.412  10.066  18.270  1.00 78.37           N\\nANISOU  240  N   THR A  69    10426  11955   7395  -1662    733    255       N\\nATOM    241  CA  THR A  69       7.811   9.195  17.168  1.00 78.88           C\\nANISOU  241  CA  THR A  69    10662  11578   7732  -1656    605    503       C\\nATOM    242  C   THR A  69       6.596   8.584  16.482  1.00 78.27           C\\nANISOU  242  C   THR A  69    10482  11594   7664  -1890    759    558       C\\nATOM    243  O   THR A  69       6.522   8.550  15.247  1.00 73.15           O\\nANISOU  243  O   THR A  69     9763  10702   7330  -1761    732    539       O\\nATOM    244  CB  THR A  69       8.748   8.097  17.676  1.00 76.37           C\\nANISOU  244  CB  THR A  69    10733  11000   7285  -1777    388    839       C\\nATOM    245  OG1 THR A  69       9.982   8.680  18.112  1.00 72.19           O\\nANISOU  245  OG1 THR A  69    10268  10338   6821  -1513    212    771       O\\nATOM    246  CG2 THR A  69       9.035   7.083  16.582  1.00 74.02           C\\nANISOU  246  CG2 THR A  69    10604  10273   7247  -1776    252   1050       C\\nATOM    247  N   ASN A  70       5.625   8.114  17.269  1.00 82.86           N\\nANISOU  247  N   ASN A  70    11039  12561   7884  -2256    925    618       N\\nATOM    248  CA  ASN A  70       4.436   7.496  16.698  1.00 81.91           C\\nANISOU  248  CA  ASN A  70    10800  12565   7757  -2530   1069    672       C\\nATOM    249  C   ASN A  70       3.562   8.494  15.947  1.00 81.00           C\\nANISOU  249  C   ASN A  70    10269  12649   7860  -2327   1221    314       C\\nATOM    250  O   ASN A  70       2.805   8.084  15.063  1.00 74.10           O\\nANISOU  250  O   ASN A  70     9290  11736   7128  -2431   1271    335       O\\nATOM    251  CB  ASN A  70       3.629   6.801  17.798  1.00 79.20           C\\nANISOU  251  CB  ASN A  70    10505  12647   6942  -3020   1221    832       C\\nATOM    252  CG  ASN A  70       4.333   5.581  18.348  1.00 78.28           C\\nANISOU  252  CG  ASN A  70    10856  12250   6638  -3286   1014   1268       C\\nATOM    253  OD1 ASN A  70       5.224   5.030  17.706  1.00 74.09           O\\nANISOU  253  OD1 ASN A  70    10588  11183   6379  -3127    762   1443       O\\nATOM    254  ND2 ASN A  70       3.941   5.152  19.542  1.00 73.15           N\\nANISOU  254  ND2 ASN A  70    10308  11972   5512  -3692   1103   1439       N\\nATOM    255  N   TYR A  71       3.640   9.786  16.274  1.00 84.07           N\\nANISOU  255  N   TYR A  71    10427  13227   8291  -2033   1261    -20       N\\nATOM    256  CA  TYR A  71       2.933  10.782  15.475  1.00 77.80           C\\nANISOU  256  CA  TYR A  71     9275  12516   7768  -1780   1321   -352       C\\nATOM    257  C   TYR A  71       3.632  11.001  14.143  1.00 70.85           C\\nANISOU  257  C   TYR A  71     8477  11134   7310  -1497   1135   -290       C\\nATOM    258  O   TYR A  71       2.978  11.216  13.117  1.00 65.56           O\\nANISOU  258  O   TYR A  71     7626  10422   6864  -1416   1148   -386       O\\nATOM    259  CB  TYR A  71       2.809  12.094  16.246  1.00 74.68           C\\nANISOU  259  CB  TYR A  71     8632  12431   7314  -1540   1370   -746       C\\nATOM    260  CG  TYR A  71       1.783  12.035  17.350  1.00 80.29           C\\nANISOU  260  CG  TYR A  71     9123  13772   7611  -1796   1612   -924       C\\nATOM    261  CD1 TYR A  71       0.690  11.189  17.253  1.00 82.22           C\\nANISOU  261  CD1 TYR A  71     9248  14311   7681  -2164   1796   -825       C\\nATOM    262  CD2 TYR A  71       1.912  12.814  18.492  1.00 84.10           C\\nANISOU  262  CD2 TYR A  71     9504  14589   7861  -1688   1658  -1202       C\\nATOM    263  CE1 TYR A  71      -0.250  11.123  18.258  1.00 91.89           C\\nANISOU  263  CE1 TYR A  71    10236  16183   8495  -2441   2045   -986       C\\nATOM    264  CE2 TYR A  71       0.976  12.756  19.503  1.00 85.39           C\\nANISOU  264  CE2 TYR A  71     9439  15406   7599  -1932   1905  -1392       C\\nATOM    265  CZ  TYR A  71      -0.103  11.907  19.381  1.00 94.33           C\\nANISOU  265  CZ  TYR A  71    10434  16859   8548  -2320   2110  -1275       C\\nATOM    266  OH  TYR A  71      -1.045  11.839  20.381  1.00 99.85           O\\nANISOU  266  OH  TYR A  71    10911  18103   8926  -2541   2275  -1429       O\\nATOM    267  N   LEU A  72       4.963  10.950  14.139  1.00 66.28           N\\nANISOU  267  N   LEU A  72     8155  10205   6825  -1355    960   -134       N\\nATOM    268  CA  LEU A  72       5.688  10.938  12.880  1.00 65.47           C\\nANISOU  268  CA  LEU A  72     8142   9678   7057  -1158    810    -34       C\\nATOM    269  C   LEU A  72       5.520   9.612  12.156  1.00 66.26           C\\nANISOU  269  C   LEU A  72     8411   9590   7173  -1363    790    218       C\\nATOM    270  O   LEU A  72       5.755   9.545  10.947  1.00 70.26           O\\nANISOU  270  O   LEU A  72     8925   9843   7928  -1232    713    248       O\\nATOM    271  CB  LEU A  72       7.166  11.237  13.129  1.00 68.98           C\\nANISOU  271  CB  LEU A  72     8763   9860   7585   -964    640     32       C\\nATOM    272  CG  LEU A  72       7.464  12.668  13.586  1.00 71.02           C\\nANISOU  272  CG  LEU A  72     8861  10200   7924   -721    600   -231       C\\nATOM    273  CD1 LEU A  72       8.795  12.745  14.308  1.00 68.45           C\\nANISOU  273  CD1 LEU A  72     8719   9732   7557   -638    454   -157       C\\nATOM    274  CD2 LEU A  72       7.449  13.618  12.399  1.00 69.98           C\\nANISOU  274  CD2 LEU A  72     8565   9884   8138   -488    531   -351       C\\nATOM    275  N   ILE A  73       5.112   8.562  12.866  1.00 69.01           N\\nANISOU  275  N   ILE A  73     8906  10062   7254  -1697    844    397       N\\nATOM    276  CA  ILE A  73       4.844   7.288  12.214  1.00 67.68           C\\nANISOU  276  CA  ILE A  73     8907   9691   7118  -1917    795    618       C\\nATOM    277  C   ILE A  73       3.522   7.340  11.460  1.00 71.94           C\\nANISOU  277  C   ILE A  73     9183  10422   7728  -2023    929    489       C\\nATOM    278  O   ILE A  73       3.411   6.809  10.350  1.00 75.02           O\\nANISOU  278  O   ILE A  73     9617  10582   8307  -2015    856    546       O\\nATOM    279  CB  ILE A  73       4.880   6.148  13.249  1.00 69.17           C\\nANISOU  279  CB  ILE A  73     9379   9898   7006  -2275    759    894       C\\nATOM    280  CG1 ILE A  73       6.327   5.743  13.542  1.00 66.13           C\\nANISOU  280  CG1 ILE A  73     9319   9150   6659  -2128    522   1069       C\\nATOM    281  CG2 ILE A  73       4.072   4.944  12.777  1.00 68.47           C\\nANISOU  281  CG2 ILE A  73     9386   9730   6900  -2615    755   1076       C\\nATOM    282  CD1 ILE A  73       6.453   4.548  14.461  1.00 67.07           C\\nANISOU  282  CD1 ILE A  73     9782   9188   6514  -2462    402   1387       C\\nATOM    283  N   VAL A  74       2.507   7.996  12.029  1.00 70.79           N\\nANISOU  283  N   VAL A  74     8739  10720   7436  -2102   1115    280       N\\nATOM    284  CA  VAL A  74       1.244   8.128  11.308  1.00 74.58           C\\nANISOU  284  CA  VAL A  74     8921  11407   8009  -2166   1221    118       C\\nATOM    285  C   VAL A  74       1.392   9.116  10.161  1.00 73.54           C\\nANISOU  285  C   VAL A  74     8633  11099   8211  -1776   1127    -73       C\\nATOM    286  O   VAL A  74       0.708   8.995   9.137  1.00 75.63           O\\nANISOU  286  O   VAL A  74     8769  11334   8631  -1776   1112   -121       O\\nATOM    287  CB  VAL A  74       0.095   8.527  12.256  1.00 73.62           C\\nANISOU  287  CB  VAL A  74     8477  11862   7633  -2350   1446    -95       C\\nATOM    288  CG1 VAL A  74       0.133   7.692  13.523  1.00 69.23           C\\nANISOU  288  CG1 VAL A  74     8110  11512   6684  -2747   1535    127       C\\nATOM    289  CG2 VAL A  74       0.126  10.011  12.581  1.00 69.08           C\\nANISOU  289  CG2 VAL A  74     7641  11478   7130  -1988   1471   -451       C\\nATOM    290  N   SER A  75       2.276  10.106  10.306  1.00 69.43           N\\nANISOU  290  N   SER A  75     8129  10455   7797  -1464   1043   -169       N\\nATOM    291  CA  SER A  75       2.644  10.933   9.164  1.00 66.75           C\\nANISOU  291  CA  SER A  75     7729   9871   7764  -1146    912   -253       C\\nATOM    292  C   SER A  75       3.278  10.082   8.075  1.00 68.29           C\\nANISOU  292  C   SER A  75     8151   9714   8082  -1158    801    -30       C\\nATOM    293  O   SER A  75       3.025  10.291   6.882  1.00 67.91           O\\nANISOU  293  O   SER A  75     8025   9564   8214  -1048    739    -65       O\\nATOM    294  CB  SER A  75       3.595  12.044   9.605  1.00 65.59           C\\nANISOU  294  CB  SER A  75     7599   9627   7697   -876    823   -350       C\\nATOM    295  OG  SER A  75       4.148  12.722   8.492  1.00 65.64           O\\nANISOU  295  OG  SER A  75     7609   9355   7975   -636    678   -344       O\\nATOM    296  N   LEU A  76       4.099   9.107   8.470  1.00 69.61           N\\nANISOU  296  N   LEU A  76     8600   9702   8145  -1281    755    185       N\\nATOM    297  CA  LEU A  76       4.653   8.169   7.503  1.00 70.39           C\\nANISOU  297  CA  LEU A  76     8904   9490   8352  -1284    641    344       C\\nATOM    298  C   LEU A  76       3.555   7.304   6.898  1.00 71.56           C\\nANISOU  298  C   LEU A  76     9015   9685   8488  -1514    675    369       C\\nATOM    299  O   LEU A  76       3.587   6.994   5.700  1.00 67.72           O\\nANISOU  299  O   LEU A  76     8556   9030   8146  -1442    597    372       O\\nATOM    300  CB  LEU A  76       5.725   7.307   8.170  1.00 71.65           C\\nANISOU  300  CB  LEU A  76     9365   9437   8421  -1339    541    534       C\\nATOM    301  CG  LEU A  76       6.488   6.311   7.296  1.00 73.93           C\\nANISOU  301  CG  LEU A  76     9872   9386   8833  -1283    387    648       C\\nATOM    302  CD1 LEU A  76       7.050   6.993   6.057  1.00 66.82           C\\nANISOU  302  CD1 LEU A  76     8859   8395   8135  -1003    352    542       C\\nATOM    303  CD2 LEU A  76       7.598   5.643   8.104  1.00 66.32           C\\nANISOU  303  CD2 LEU A  76     9178   8218   7804  -1274    247    796       C\\nATOM    304  N   ALA A  77       2.567   6.918   7.708  1.00 76.17           N\\nANISOU  304  N   ALA A  77     9525  10531   8886  -1810    794    379       N\\nATOM    305  CA  ALA A  77       1.468   6.103   7.203  1.00 75.85           C\\nANISOU  305  CA  ALA A  77     9422  10562   8836  -2078    825    401       C\\nATOM    306  C   ALA A  77       0.603   6.875   6.217  1.00 76.40           C\\nANISOU  306  C   ALA A  77     9182  10781   9066  -1929    853    183       C\\nATOM    307  O   ALA A  77       0.034   6.277   5.295  1.00 74.94           O\\nANISOU  307  O   ALA A  77     8980  10529   8965  -2027    802    189       O\\nATOM    308  CB  ALA A  77       0.618   5.589   8.364  1.00 77.54           C\\nANISOU  308  CB  ALA A  77     9590  11086   8784  -2476    967    470       C\\nATOM    309  N   VAL A  78       0.484   8.192   6.395  1.00 72.57           N\\nANISOU  309  N   VAL A  78     8462  10479   8634  -1687    898    -17       N\\nATOM    310  CA  VAL A  78      -0.263   9.001   5.438  1.00 73.72           C\\nANISOU  310  CA  VAL A  78     8340  10714   8956  -1502    861   -213       C\\nATOM    311  C   VAL A  78       0.492   9.092   4.118  1.00 73.77           C\\nANISOU  311  C   VAL A  78     8495  10392   9143  -1286    699   -137       C\\nATOM    312  O   VAL A  78      -0.108   9.025   3.037  1.00 75.36           O\\nANISOU  312  O   VAL A  78     8606  10583   9444  -1265    631   -185       O\\nATOM    313  CB  VAL A  78      -0.556  10.391   6.030  1.00 69.67           C\\nANISOU  313  CB  VAL A  78     7563  10433   8477  -1281    899   -460       C\\nATOM    314  CG1 VAL A  78      -1.042  11.346   4.951  1.00 67.83           C\\nANISOU  314  CG1 VAL A  78     7129  10169   8475  -1016    769   -625       C\\nATOM    315  CG2 VAL A  78      -1.591  10.281   7.138  1.00 54.88           C\\nANISOU  315  CG2 VAL A  78     5447   9002   6402  -1505   1086   -609       C\\nATOM    316  N   ALA A  79       1.819   9.239   4.180  1.00 71.40           N\\nANISOU  316  N   ALA A  79     8408   9854   8865  -1136    637    -25       N\\nATOM    317  CA  ALA A  79       2.617   9.243   2.959  1.00 72.25           C\\nANISOU  317  CA  ALA A  79     8642   9715   9095   -969    515     48       C\\nATOM    318  C   ALA A  79       2.382   7.976   2.148  1.00 78.12           C\\nANISOU  318  C   ALA A  79     9512  10348   9824  -1122    472    118       C\\nATOM    319  O   ALA A  79       2.254   8.030   0.919  1.00 82.23           O\\nANISOU  319  O   ALA A  79    10005  10818  10420  -1035    394     87       O\\nATOM    320  CB  ALA A  79       4.097   9.398   3.301  1.00 67.24           C\\nANISOU  320  CB  ALA A  79     8191   8894   8464   -836    476    149       C\\nATOM    321  N   ASP A  80       2.306   6.826   2.820  1.00 70.96           N\\nANISOU  321  N   ASP A  80     8756   9392   8812  -1362    499    214       N\\nATOM    322  CA  ASP A  80       2.041   5.580   2.113  1.00 74.85           C\\nANISOU  322  CA  ASP A  80     9387   9736   9318  -1522    420    263       C\\nATOM    323  C   ASP A  80       0.578   5.468   1.707  1.00 70.40           C\\nANISOU  323  C   ASP A  80     8610   9377   8763  -1703    452    165       C\\nATOM    324  O   ASP A  80       0.275   4.919   0.641  1.00 75.04           O\\nANISOU  324  O   ASP A  80     9225   9874   9413  -1725    358    129       O\\nATOM    325  CB  ASP A  80       2.453   4.386   2.975  1.00 85.13           C\\nANISOU  325  CB  ASP A  80    10957  10859  10529  -1735    379    424       C\\nATOM    326  CG  ASP A  80       3.955   4.316   3.193  1.00 91.73           C\\nANISOU  326  CG  ASP A  80    12008  11459  11389  -1526    293    497       C\\nATOM    327  OD1 ASP A  80       4.707   4.814   2.326  1.00 90.12           O\\nANISOU  327  OD1 ASP A  80    11774  11187  11279  -1257    253    424       O\\nATOM    328  OD2 ASP A  80       4.383   3.762   4.231  1.00 93.76           O\\nANISOU  328  OD2 ASP A  80    12452  11616  11555  -1644    259    631       O\\nATOM    329  N   LEU A  81      -0.340   5.974   2.535  1.00 74.65           N\\nANISOU  329  N   LEU A  81     8912  10218   9233  -1827    580     91       N\\nATOM    330  CA  LEU A  81      -1.751   5.961   2.159  1.00 71.55           C\\nANISOU  330  CA  LEU A  81     8249  10074   8865  -1978    612    -40       C\\nATOM    331  C   LEU A  81      -2.001   6.765   0.893  1.00 74.65           C\\nANISOU  331  C   LEU A  81     8488  10471   9406  -1709    505   -178       C\\nATOM    332  O   LEU A  81      -2.886   6.418   0.105  1.00 69.21           O\\nANISOU  332  O   LEU A  81     7680   9851   8766  -1803    444   -254       O\\nATOM    333  CB  LEU A  81      -2.611   6.504   3.297  1.00 69.87           C\\nANISOU  333  CB  LEU A  81     7752  10250   8545  -2106    782   -153       C\\nATOM    334  CG  LEU A  81      -3.075   5.485   4.331  1.00 74.99           C\\nANISOU  334  CG  LEU A  81     8452  11043   8999  -2544    901    -27       C\\nATOM    335  CD1 LEU A  81      -3.852   6.179   5.437  1.00 74.69           C\\nANISOU  335  CD1 LEU A  81     8087  11477   8814  -2632   1099   -186       C\\nATOM    336  CD2 LEU A  81      -3.924   4.409   3.669  1.00 73.03           C\\nANISOU  336  CD2 LEU A  81     8197  10767   8785  -2854    842     14       C\\nATOM    337  N   LEU A  82      -1.237   7.838   0.678  1.00 69.87           N\\nANISOU  337  N   LEU A  82     7892   9789   8867  -1397    460   -196       N\\nATOM    338  CA  LEU A  82      -1.409   8.637  -0.529  1.00 65.99           C\\nANISOU  338  CA  LEU A  82     7299   9280   8492  -1167    327   -272       C\\nATOM    339  C   LEU A  82      -0.757   7.982  -1.740  1.00 70.21           C\\nANISOU  339  C   LEU A  82     8057   9596   9025  -1131    218   -180       C\\nATOM    340  O   LEU A  82      -1.178   8.231  -2.875  1.00 71.57           O\\nANISOU  340  O   LEU A  82     8160   9794   9239  -1047    101   -233       O\\nATOM    341  CB  LEU A  82      -0.848  10.040  -0.313  1.00 59.37           C\\nANISOU  341  CB  LEU A  82     6407   8421   7728   -892    291   -300       C\\nATOM    342  CG  LEU A  82      -1.644  10.851   0.706  1.00 62.33           C\\nANISOU  342  CG  LEU A  82     6510   9044   8130   -856    360   -482       C\\nATOM    343  CD1 LEU A  82      -1.091  12.261   0.855  1.00 55.10           C\\nANISOU  343  CD1 LEU A  82     5564   8044   7327   -570    267   -530       C\\nATOM    344  CD2 LEU A  82      -3.114  10.883   0.314  1.00 64.42           C\\nANISOU  344  CD2 LEU A  82     6475   9550   8451   -907    325   -667       C\\nATOM    345  N   VAL A  83       0.261   7.147  -1.524  1.00 71.76           N\\nANISOU  345  N   VAL A  83     8510   9592   9162  -1179    238    -64       N\\nATOM    346  CA  VAL A  83       0.813   6.355  -2.620  1.00 69.53           C\\nANISOU  346  CA  VAL A  83     8414   9139   8867  -1147    140    -43       C\\nATOM    347  C   VAL A  83      -0.238   5.394  -3.158  1.00 73.89           C\\nANISOU  347  C   VAL A  83     8937   9715   9422  -1353     76   -116       C\\nATOM    348  O   VAL A  83      -0.404   5.247  -4.375  1.00 79.13           O\\nANISOU  348  O   VAL A  83     9606  10373  10087  -1289    -32   -185       O\\nATOM    349  CB  VAL A  83       2.078   5.608  -2.159  1.00 61.51           C\\nANISOU  349  CB  VAL A  83     7653   7900   7818  -1130    147     49       C\\nATOM    350  CG1 VAL A  83       2.537   4.623  -3.222  1.00 56.33           C\\nANISOU  350  CG1 VAL A  83     7164   7084   7153  -1094     37      1       C\\nATOM    351  CG2 VAL A  83       3.187   6.592  -1.827  1.00 55.01           C\\nANISOU  351  CG2 VAL A  83     6836   7065   7001   -921    189    106       C\\nATOM    352  N   ALA A  84      -0.973   4.732  -2.264  1.00 63.07           N\\nANISOU  352  N   ALA A  84     7532   8393   8036  -1628    136   -100       N\\nATOM    353  CA  ALA A  84      -1.979   3.777  -2.713  1.00 68.51           C\\nANISOU  353  CA  ALA A  84     8190   9097   8744  -1877     65   -159       C\\nATOM    354  C   ALA A  84      -3.109   4.458  -3.475  1.00 67.78           C\\nANISOU  354  C   ALA A  84     7803   9251   8701  -1831     21   -306       C\\nATOM    355  O   ALA A  84      -3.668   3.871  -4.408  1.00 63.21           O\\nANISOU  355  O   ALA A  84     7217   8653   8146  -1911   -101   -386       O\\nATOM    356  CB  ALA A  84      -2.540   3.003  -1.520  1.00 70.03           C\\nANISOU  356  CB  ALA A  84     8393   9327   8888  -2241    149    -72       C\\nATOM    357  N   THR A  85      -3.449   5.692  -3.108  1.00 59.88           N\\nANISOU  357  N   THR A  85     6561   8463   7726  -1685     85   -362       N\\nATOM    358  CA  THR A  85      -4.630   6.368  -3.632  1.00 70.05           C\\nANISOU  358  CA  THR A  85     7536   9994   9087  -1632     16   -521       C\\nATOM    359  C   THR A  85      -4.329   7.352  -4.758  1.00 73.23           C\\nANISOU  359  C   THR A  85     7938  10354   9531  -1316   -140   -540       C\\nATOM    360  O   THR A  85      -5.144   7.493  -5.674  1.00 73.60           O\\nANISOU  360  O   THR A  85     7844  10501   9619  -1283   -285   -640       O\\nATOM    361  CB  THR A  85      -5.355   7.103  -2.501  1.00 66.86           C\\nANISOU  361  CB  THR A  85     6829   9873   8704  -1660    148   -625       C\\nATOM    362  OG1 THR A  85      -4.432   7.958  -1.812  1.00 68.22           O\\nANISOU  362  OG1 THR A  85     7080   9977   8864  -1454    215   -567       O\\nATOM    363  CG2 THR A  85      -5.948   6.109  -1.519  1.00 61.69           C\\nANISOU  363  CG2 THR A  85     6117   9358   7964  -2054    299   -604       C\\nATOM    364  N   LEU A  86      -3.186   8.043  -4.718  1.00 62.95           N\\nANISOU  364  N   LEU A  86     6792   8914   8211  -1106   -129   -431       N\\nATOM    365  CA  LEU A  86      -2.875   9.074  -5.699  1.00 69.96           C\\nANISOU  365  CA  LEU A  86     7691   9770   9119   -857   -279   -398       C\\nATOM    366  C   LEU A  86      -1.823   8.663  -6.718  1.00 73.74           C\\nANISOU  366  C   LEU A  86     8430  10102   9484   -805   -327   -290       C\\nATOM    367  O   LEU A  86      -1.627   9.386  -7.700  1.00 78.44           O\\nANISOU  367  O   LEU A  86     9050  10709  10044   -662   -458   -237       O\\nATOM    368  CB  LEU A  86      -2.400  10.356  -5.000  1.00 71.90           C\\nANISOU  368  CB  LEU A  86     7888   9995   9438   -669   -260   -361       C\\nATOM    369  CG  LEU A  86      -3.358  11.015  -4.012  1.00 70.39           C\\nANISOU  369  CG  LEU A  86     7407   9983   9357   -640   -226   -527       C\\nATOM    370  CD1 LEU A  86      -2.805  12.358  -3.572  1.00 66.08           C\\nANISOU  370  CD1 LEU A  86     6851   9355   8902   -408   -280   -511       C\\nATOM    371  CD2 LEU A  86      -4.735  11.169  -4.633  1.00 73.10           C\\nANISOU  371  CD2 LEU A  86     7488  10505   9781   -625   -371   -694       C\\nATOM    372  N   VAL A  87      -1.137   7.538  -6.512  1.00 71.08           N\\nANISOU  372  N   VAL A  87     8285   9640   9081   -916   -240   -262       N\\nATOM    373  CA  VAL A  87      -0.068   7.087  -7.395  1.00 73.29           C\\nANISOU  373  CA  VAL A  87     8777   9820   9251   -840   -268   -222       C\\nATOM    374  C   VAL A  87      -0.364   5.702  -7.963  1.00 77.64           C\\nANISOU  374  C   VAL A  87     9430  10309   9760   -973   -330   -334       C\\nATOM    375  O   VAL A  87      -0.313   5.497  -9.179  1.00 73.98           O\\nANISOU  375  O   VAL A  87     9018   9892   9199   -916   -433   -399       O\\nATOM    376  CB  VAL A  87       1.295   7.094  -6.673  1.00 71.74           C\\nANISOU  376  CB  VAL A  87     8723   9494   9039   -769   -152   -126       C\\nATOM    377  CG1 VAL A  87       2.408   6.688  -7.635  1.00 74.66           C\\nANISOU  377  CG1 VAL A  87     9249   9829   9290   -667   -171   -133       C\\nATOM    378  CG2 VAL A  87       1.561   8.458  -6.054  1.00 66.12           C\\nANISOU  378  CG2 VAL A  87     7914   8818   8388   -656   -114    -33       C\\nATOM    379  N   MET A  88      -0.666   4.743  -7.091  1.00 80.11           N\\nANISOU  379  N   MET A  88     9788  10515  10136  -1166   -284   -354       N\\nATOM    380  CA  MET A  88      -0.910   3.374  -7.543  1.00 77.27           C\\nANISOU  380  CA  MET A  88     9560  10025   9773  -1313   -382   -456       C\\nATOM    381  C   MET A  88      -2.014   3.257  -8.587  1.00 74.77           C\\nANISOU  381  C   MET A  88     9120   9842   9447  -1377   -521   -585       C\\nATOM    382  O   MET A  88      -1.856   2.434  -9.508  1.00 75.54           O\\nANISOU  382  O   MET A  88     9351   9858   9492  -1370   -641   -704       O\\nATOM    383  CB  MET A  88      -1.213   2.478  -6.335  1.00 80.86           C\\nANISOU  383  CB  MET A  88    10082  10339  10303  -1575   -337   -400       C\\nATOM    384  CG  MET A  88      -0.060   2.322  -5.349  1.00 81.25           C\\nANISOU  384  CG  MET A  88    10311  10211  10350  -1521   -256   -278       C\\nATOM    385  SD  MET A  88       1.427   1.569  -6.040  1.00 83.45           S\\nANISOU  385  SD  MET A  88    10860  10245  10603  -1297   -355   -350       S\\nATOM    386  CE  MET A  88       0.780   0.002  -6.622  1.00 86.55           C\\nANISOU  386  CE  MET A  88    11408  10421  11056  -1493   -560   -493       C\\nATOM    387  N   PRO A  89      -3.134   3.998  -8.521  1.00 73.85           N\\nANISOU  387  N   PRO A  89     8745   9932   9382  -1424   -534   -603       N\\nATOM    388  CA  PRO A  89      -4.103   3.930  -9.629  1.00 74.48           C\\nANISOU  388  CA  PRO A  89     8707  10146   9448  -1448   -704   -735       C\\nATOM    389  C   PRO A  89      -3.480   4.213 -10.985  1.00 73.67           C\\nANISOU  389  C   PRO A  89     8725  10074   9192  -1237   -816   -758       C\\nATOM    390  O   PRO A  89      -3.834   3.559 -11.972  1.00 74.04           O\\nANISOU  390  O   PRO A  89     8817  10141   9174  -1277   -962   -893       O\\nATOM    391  CB  PRO A  89      -5.142   4.990  -9.248  1.00 73.14           C\\nANISOU  391  CB  PRO A  89     8221  10200   9368  -1431   -703   -747       C\\nATOM    392  CG  PRO A  89      -5.085   5.041  -7.779  1.00 71.74           C\\nANISOU  392  CG  PRO A  89     7982  10016   9258  -1543   -514   -680       C\\nATOM    393  CD  PRO A  89      -3.645   4.834  -7.418  1.00 67.98           C\\nANISOU  393  CD  PRO A  89     7787   9325   8719  -1455   -417   -550       C\\nATOM    394  N   TRP A  90      -2.552   5.170 -11.056  1.00 69.93           N\\nANISOU  394  N   TRP A  90     8302   9624   8643  -1037   -753   -630       N\\nATOM    395  CA  TRP A  90      -1.831   5.402 -12.301  1.00 70.06           C\\nANISOU  395  CA  TRP A  90     8440   9716   8463   -885   -824   -623       C\\nATOM    396  C   TRP A  90      -0.927   4.229 -12.652  1.00 73.43           C\\nANISOU  396  C   TRP A  90     9074  10033   8794   -879   -795   -740       C\\nATOM    397  O   TRP A  90      -0.713   3.948 -13.836  1.00 80.52           O\\nANISOU  397  O   TRP A  90    10046  11036   9511   -815   -885   -849       O\\nATOM    398  CB  TRP A  90      -0.996   6.677 -12.206  1.00 72.68           C\\nANISOU  398  CB  TRP A  90     8778  10094   8744   -730   -758   -431       C\\nATOM    399  CG  TRP A  90      -1.743   7.924 -11.827  1.00 78.23           C\\nANISOU  399  CG  TRP A  90     9301  10853   9571   -681   -825   -337       C\\nATOM    400  CD1 TRP A  90      -2.061   8.338 -10.567  1.00 78.70           C\\nANISOU  400  CD1 TRP A  90     9229  10858   9814   -696   -738   -319       C\\nATOM    401  CD2 TRP A  90      -2.229   8.939 -12.716  1.00 88.37           C\\nANISOU  401  CD2 TRP A  90    10523  12253  10801   -588  -1022   -264       C\\nATOM    402  NE1 TRP A  90      -2.729   9.539 -10.616  1.00 79.87           N\\nANISOU  402  NE1 TRP A  90     9218  11075  10052   -589   -872   -284       N\\nATOM    403  CE2 TRP A  90      -2.844   9.929 -11.925  1.00 85.91           C\\nANISOU  403  CE2 TRP A  90    10036  11918  10690   -521  -1067   -232       C\\nATOM    404  CE3 TRP A  90      -2.213   9.101 -14.106  1.00 93.09           C\\nANISOU  404  CE3 TRP A  90    11205  12978  11187   -553  -1185   -228       C\\nATOM    405  CZ2 TRP A  90      -3.436  11.064 -12.476  1.00 91.05           C\\nANISOU  405  CZ2 TRP A  90    10603  12614  11379   -398  -1303   -166       C\\nATOM    406  CZ3 TRP A  90      -2.801  10.229 -14.651  1.00 88.71           C\\nANISOU  406  CZ3 TRP A  90    10584  12483  10637   -467  -1412   -117       C\\nATOM    407  CH2 TRP A  90      -3.404  11.195 -13.838  1.00 91.05           C\\nANISOU  407  CH2 TRP A  90    10716  12700  11179   -380  -1486    -87       C\\nATOM    408  N   VAL A  91      -0.382   3.540 -11.646  1.00 69.25           N\\nANISOU  408  N   VAL A  91     8640   9297   8374   -930   -690   -736       N\\nATOM    409  CA  VAL A  91       0.555   2.453 -11.912  1.00 71.26           C\\nANISOU  409  CA  VAL A  91     9090   9406   8578   -872   -701   -873       C\\nATOM    410  C   VAL A  91      -0.181   1.188 -12.341  1.00 81.86           C\\nANISOU  410  C   VAL A  91    10506  10626   9969  -1010   -867  -1076       C\\nATOM    411  O   VAL A  91       0.272   0.468 -13.239  1.00 84.97           O\\nANISOU  411  O   VAL A  91    11020  11005  10261   -913   -961  -1279       O\\nATOM    412  CB  VAL A  91       1.447   2.203 -10.683  1.00 66.23           C\\nANISOU  412  CB  VAL A  91     8549   8562   8051   -856   -583   -782       C\\nATOM    413  CG1 VAL A  91       2.331   0.984 -10.905  1.00 66.75           C\\nANISOU  413  CG1 VAL A  91     8812   8434   8116   -769   -652   -961       C\\nATOM    414  CG2 VAL A  91       2.295   3.427 -10.395  1.00 71.66           C\\nANISOU  414  CG2 VAL A  91     9171   9373   8685   -712   -442   -614       C\\nATOM    415  N   VAL A  92      -1.320   0.890 -11.713  1.00 76.99           N\\nANISOU  415  N   VAL A  92     9808   9938   9507  -1247   -911  -1047       N\\nATOM    416  CA  VAL A  92      -2.100  -0.267 -12.139  1.00 83.11           C\\nANISOU  416  CA  VAL A  92    10641  10591  10346  -1426  -1092  -1225       C\\nATOM    417  C   VAL A  92      -2.714  -0.014 -13.513  1.00 85.39           C\\nANISOU  417  C   VAL A  92    10837  11112  10496  -1365  -1232  -1373       C\\nATOM    418  O   VAL A  92      -2.760  -0.914 -14.362  1.00 87.20           O\\nANISOU  418  O   VAL A  92    11179  11274  10677  -1366  -1396  -1596       O\\nATOM    419  CB  VAL A  92      -3.160  -0.626 -11.077  1.00 86.97           C\\nANISOU  419  CB  VAL A  92    11035  10994  11015  -1752  -1083  -1133       C\\nATOM    420  CG1 VAL A  92      -4.059   0.557 -10.774  1.00 88.40           C\\nANISOU  420  CG1 VAL A  92    10916  11464  11208  -1788   -990  -1030       C\\nATOM    421  CG2 VAL A  92      -3.984  -1.823 -11.526  1.00 90.14           C\\nANISOU  421  CG2 VAL A  92    11495  11253  11500  -1988  -1291  -1301       C\\nATOM    422  N   TYR A  93      -3.173   1.217 -13.762  1.00 86.77           N\\nANISOU  422  N   TYR A  93    10817  11548  10602  -1298  -1201  -1261       N\\nATOM    423  CA  TYR A  93      -3.600   1.598 -15.106  1.00 83.84           C\\nANISOU  423  CA  TYR A  93    10389  11409  10056  -1209  -1354  -1357       C\\nATOM    424  C   TYR A  93      -2.477   1.379 -16.111  1.00 80.40           C\\nANISOU  424  C   TYR A  93    10133  11042   9375  -1017  -1359  -1466       C\\nATOM    425  O   TYR A  93      -2.706   0.878 -17.219  1.00 74.40           O\\nANISOU  425  O   TYR A  93     9423  10381   8465   -997  -1517  -1669       O\\nATOM    426  CB  TYR A  93      -4.062   3.059 -15.102  1.00 86.78           C\\nANISOU  426  CB  TYR A  93    10567  11993  10412  -1130  -1345  -1178       C\\nATOM    427  CG  TYR A  93      -4.289   3.683 -16.465  1.00 96.56           C\\nANISOU  427  CG  TYR A  93    11788  13469  11430  -1012  -1516  -1193       C\\nATOM    428  CD1 TYR A  93      -5.528   3.603 -17.096  1.00 94.66           C\\nANISOU  428  CD1 TYR A  93    11412  13349  11207  -1088  -1737  -1310       C\\nATOM    429  CD2 TYR A  93      -3.274   4.383 -17.106  1.00 98.40           C\\nANISOU  429  CD2 TYR A  93    12135  13829  11423   -849  -1468  -1073       C\\nATOM    430  CE1 TYR A  93      -5.739   4.185 -18.334  1.00 95.59           C\\nANISOU  430  CE1 TYR A  93    11537  13682  11100   -983  -1926  -1302       C\\nATOM    431  CE2 TYR A  93      -3.475   4.965 -18.343  1.00 97.04           C\\nANISOU  431  CE2 TYR A  93    11974  13889  11007   -780  -1636  -1042       C\\nATOM    432  CZ  TYR A  93      -4.707   4.864 -18.952  1.00 96.39           C\\nANISOU  432  CZ  TYR A  93    11785  13900  10937   -837  -1876  -1153       C\\nATOM    433  OH  TYR A  93      -4.903   5.446 -20.182  1.00 95.53           O\\nANISOU  433  OH  TYR A  93    11712  14022  10562   -771  -2074  -1102       O\\nATOM    434  N   LEU A  94      -1.250   1.724 -15.722  1.00 88.56           N\\nANISOU  434  N   LEU A  94    11244  12051  10355   -879  -1185  -1358       N\\nATOM    435  CA  LEU A  94      -0.090   1.590 -16.592  1.00 90.25           C\\nANISOU  435  CA  LEU A  94    11571  12398  10320   -698  -1144  -1470       C\\nATOM    436  C   LEU A  94       0.187   0.143 -16.984  1.00 86.74           C\\nANISOU  436  C   LEU A  94    11276  11802   9879   -668  -1251  -1798       C\\nATOM    437  O   LEU A  94       0.806  -0.096 -18.027  1.00 79.60           O\\nANISOU  437  O   LEU A  94    10426  11091   8726   -524  -1274  -1999       O\\nATOM    438  CB  LEU A  94       1.131   2.192 -15.893  1.00 91.19           C\\nANISOU  438  CB  LEU A  94    11704  12504  10440   -587   -935  -1297       C\\nATOM    439  CG  LEU A  94       2.362   2.481 -16.745  1.00 96.59           C\\nANISOU  439  CG  LEU A  94    12420  13445  10836   -422   -839  -1342       C\\nATOM    440  CD1 LEU A  94       1.952   3.241 -17.987  1.00 95.48           C\\nANISOU  440  CD1 LEU A  94    12233  13639  10407   -435   -921  -1281       C\\nATOM    441  CD2 LEU A  94       3.366   3.277 -15.931  1.00 94.01           C\\nANISOU  441  CD2 LEU A  94    12057  13105  10556   -364   -648  -1120       C\\nATOM    442  N   GLU A  95      -0.244  -0.827 -16.175  1.00 91.64           N\\nANISOU  442  N   GLU A  95    11967  12086  10767   -809  -1328  -1863       N\\nATOM    443  CA  GLU A  95      -0.007  -2.228 -16.505  1.00 89.73           C\\nANISOU  443  CA  GLU A  95    11897  11617  10578   -779  -1491  -2179       C\\nATOM    444  C   GLU A  95      -1.104  -2.803 -17.392  1.00 87.68           C\\nANISOU  444  C   GLU A  95    11631  11388  10293   -904  -1724  -2391       C\\nATOM    445  O   GLU A  95      -0.812  -3.568 -18.317  1.00 89.77           O\\nANISOU  445  O   GLU A  95    12002  11667  10441   -784  -1865  -2717       O\\nATOM    446  CB  GLU A  95       0.121  -3.065 -15.229  1.00 87.59           C\\nANISOU  446  CB  GLU A  95    11758  10917  10607   -899  -1515  -2120       C\\nATOM    447  CG  GLU A  95       0.439  -4.539 -15.480  1.00 93.67           C\\nANISOU  447  CG  GLU A  95    12747  11357  11487   -851  -1741  -2438       C\\nATOM    448  CD  GLU A  95       1.851  -4.758 -16.002  1.00102.62           C\\nANISOU  448  CD  GLU A  95    13952  12557  12482   -504  -1707  -2681       C\\nATOM    449  OE1 GLU A  95       2.722  -3.902 -15.740  1.00104.20           O\\nANISOU  449  OE1 GLU A  95    14062  12957  12571   -357  -1484  -2527       O\\nATOM    450  OE2 GLU A  95       2.093  -5.788 -16.670  1.00107.64           O\\nANISOU  450  OE2 GLU A  95    14717  13056  13125   -376  -1910  -3051       O\\nATOM    451  N   VAL A  96      -2.362  -2.449 -17.129  1.00 78.94           N\\nANISOU  451  N   VAL A  96    10382  10316   9297  -1131  -1774  -2245       N\\nATOM    452  CA  VAL A  96      -3.462  -2.952 -17.947  1.00 80.52           C\\nANISOU  452  CA  VAL A  96    10543  10563   9488  -1267  -2011  -2444       C\\nATOM    453  C   VAL A  96      -3.331  -2.439 -19.375  1.00 85.05           C\\nANISOU  453  C   VAL A  96    11087  11511   9717  -1081  -2072  -2578       C\\nATOM    454  O   VAL A  96      -3.404  -3.209 -20.340  1.00 82.90           O\\nANISOU  454  O   VAL A  96    10906  11266   9327  -1037  -2258  -2893       O\\nATOM    455  CB  VAL A  96      -4.816  -2.561 -17.328  1.00 77.18           C\\nANISOU  455  CB  VAL A  96     9907  10166   9251  -1538  -2032  -2265       C\\nATOM    456  N   VAL A  97      -3.117  -1.130 -19.528  1.00 87.40           N\\nANISOU  456  N   VAL A  97    11271  12099   9836   -979  -1932  -2336       N\\nATOM    457  CA  VAL A  97      -2.995  -0.529 -20.854  1.00 88.86           C\\nANISOU  457  CA  VAL A  97    11446  12664   9653   -847  -1994  -2384       C\\nATOM    458  C   VAL A  97      -1.719  -0.983 -21.554  1.00 90.16           C\\nANISOU  458  C   VAL A  97    11752  12956   9548   -647  -1919  -2608       C\\nATOM    459  O   VAL A  97      -1.694  -1.122 -22.783  1.00 92.93           O\\nANISOU  459  O   VAL A  97    12140  13588   9583   -572  -2028  -2817       O\\nATOM    460  CB  VAL A  97      -3.061   1.005 -20.740  1.00 86.80           C\\nANISOU  460  CB  VAL A  97    11060  12617   9305   -817  -1897  -2025       C\\nATOM    461  CG1 VAL A  97      -2.893   1.659 -22.106  1.00 88.76           C\\nANISOU  461  CG1 VAL A  97    11335  13252   9139   -721  -1981  -2009       C\\nATOM    462  CG2 VAL A  97      -4.372   1.434 -20.086  1.00 86.16           C\\nANISOU  462  CG2 VAL A  97    10792  12448   9495   -970  -1990  -1884       C\\nATOM    463  N   GLY A  98      -0.650  -1.230 -20.800  1.00 88.15           N\\nANISOU  463  N   GLY A  98    11562  12531   9400   -550  -1740  -2596       N\\nATOM    464  CA  GLY A  98       0.613  -1.604 -21.402  1.00 89.34           C\\nANISOU  464  CA  GLY A  98    11789  12846   9310   -334  -1652  -2837       C\\nATOM    465  C   GLY A  98       1.360  -0.469 -22.059  1.00 91.48           C\\nANISOU  465  C   GLY A  98    11987  13570   9202   -247  -1473  -2660       C\\nATOM    466  O   GLY A  98       2.307  -0.717 -22.810  1.00 93.59           O\\nANISOU  466  O   GLY A  98    12270  14114   9177    -92  -1395  -2892       O\\nATOM    467  N   GLU A  99       0.962   0.772 -21.797  1.00 93.52           N\\nANISOU  467  N   GLU A  99    12159  13918   9455   -352  -1418  -2264       N\\nATOM    468  CA  GLU A  99       1.609   1.938 -22.378  1.00 95.54           C\\nANISOU  468  CA  GLU A  99    12373  14557   9372   -328  -1286  -2022       C\\nATOM    469  C   GLU A  99       1.259   3.151 -21.529  1.00 92.97           C\\nANISOU  469  C   GLU A  99    11976  14105   9244   -422  -1241  -1593       C\\nATOM    470  O   GLU A  99       0.253   3.163 -20.815  1.00 85.82           O\\nANISOU  470  O   GLU A  99    11021  12937   8648   -506  -1345  -1519       O\\nATOM    471  CB  GLU A  99       1.181   2.153 -23.835  1.00 94.86           C\\nANISOU  471  CB  GLU A  99    12308  14866   8868   -355  -1437  -2092       C\\nATOM    472  N   TRP A 100       2.110   4.174 -21.614  1.00 89.68           N\\nANISOU  472  N   TRP A 100    11539  13894   8642   -414  -1089  -1330       N\\nATOM    473  CA  TRP A 100       1.871   5.446 -20.932  1.00 88.27           C\\nANISOU  473  CA  TRP A 100    11308  13606   8625   -483  -1080   -935       C\\nATOM    474  C   TRP A 100       0.892   6.302 -21.742  1.00 91.37           C\\nANISOU  474  C   TRP A 100    11702  14149   8867   -556  -1315   -744       C\\nATOM    475  O   TRP A 100       1.217   7.382 -22.236  1.00 95.09           O\\nANISOU  475  O   TRP A 100    12204  14809   9115   -605  -1334   -453       O\\nATOM    476  CB  TRP A 100       3.188   6.177 -20.702  1.00 86.77           C\\nANISOU  476  CB  TRP A 100    11107  13540   8322   -471   -861   -729       C\\nATOM    477  CG  TRP A 100       4.148   5.471 -19.784  1.00 92.86           C\\nANISOU  477  CG  TRP A 100    11859  14140   9283   -376   -663   -888       C\\nATOM    478  CD1 TRP A 100       4.731   4.252 -19.983  1.00 99.53           C\\nANISOU  478  CD1 TRP A 100    12726  15011  10078   -261   -605  -1253       C\\nATOM    479  CD2 TRP A 100       4.655   5.958 -18.534  1.00 93.04           C\\nANISOU  479  CD2 TRP A 100    11841  13932   9577   -369   -533   -700       C\\nATOM    480  NE1 TRP A 100       5.558   3.944 -18.928  1.00 99.78           N\\nANISOU  480  NE1 TRP A 100    12740  14828  10345   -179   -465  -1286       N\\nATOM    481  CE2 TRP A 100       5.530   4.975 -18.027  1.00 94.10           C\\nANISOU  481  CE2 TRP A 100    11981  13965   9809   -254   -408   -944       C\\nATOM    482  CE3 TRP A 100       4.449   7.125 -17.792  1.00 92.42           C\\nANISOU  482  CE3 TRP A 100    11726  13714   9675   -431   -538   -373       C\\nATOM    483  CZ2 TRP A 100       6.198   5.125 -16.811  1.00 92.35           C\\nANISOU  483  CZ2 TRP A 100    11733  13525   9830   -217   -285   -845       C\\nATOM    484  CZ3 TRP A 100       5.114   7.273 -16.583  1.00 87.83           C\\nANISOU  484  CZ3 TRP A 100    11114  12928   9330   -397   -398   -300       C\\nATOM    485  CH2 TRP A 100       5.977   6.279 -16.107  1.00 90.94           C\\nANISOU  485  CH2 TRP A 100    11517  13244   9792   -299   -271   -522       C\\nATOM    486  N   LYS A 101      -0.329   5.791 -21.877  1.00 95.15           N\\nANISOU  486  N   LYS A 101    12148  14527   9477   -577  -1521   -906       N\\nATOM    487  CA  LYS A 101      -1.365   6.446 -22.678  1.00 96.45           C\\nANISOU  487  CA  LYS A 101    12300  14824   9522   -619  -1798   -787       C\\nATOM    488  C   LYS A 101      -2.121   7.498 -21.869  1.00 98.53           C\\nANISOU  488  C   LYS A 101    12457  14876  10104   -621  -1907   -529       C\\nATOM    489  O   LYS A 101      -3.351   7.502 -21.813  1.00100.15           O\\nANISOU  489  O   LYS A 101    12553  15004  10495   -628  -2120   -595       O\\nATOM    490  CB  LYS A 101      -2.319   5.405 -23.251  1.00 91.01           C\\nANISOU  490  CB  LYS A 101    11597  14158   8826   -638  -1991  -1116       C\\nATOM    491  N   PHE A 102      -1.377   8.397 -21.223  1.00 92.76           N\\nANISOU  491  N   PHE A 102    11736  14060   9449   -605  -1768   -264       N\\nATOM    492  CA  PHE A 102      -1.943   9.593 -20.620  1.00 93.22           C\\nANISOU  492  CA  PHE A 102    11716  13947   9756   -575  -1904    -18       C\\nATOM    493  C   PHE A 102      -1.857  10.735 -21.628  1.00 91.71           C\\nANISOU  493  C   PHE A 102    11641  13918   9287   -599  -2119    289       C\\nATOM    494  O   PHE A 102      -1.422  10.558 -22.768  1.00103.07           O\\nANISOU  494  O   PHE A 102    13204  15642  10313   -665  -2138    313       O\\nATOM    495  CB  PHE A 102      -1.202   9.983 -19.340  1.00 94.22           C\\nANISOU  495  CB  PHE A 102    11808  13862  10129   -551  -1677     95       C\\nATOM    496  CG  PHE A 102      -0.815   8.827 -18.469  1.00 91.97           C\\nANISOU  496  CG  PHE A 102    11490  13455  10000   -556  -1432   -141       C\\nATOM    497  CD1 PHE A 102      -1.737   8.243 -17.618  1.00 88.34           C\\nANISOU  497  CD1 PHE A 102    10903  12822   9841   -574  -1444   -314       C\\nATOM    498  CD2 PHE A 102       0.483   8.344 -18.477  1.00 88.17           C\\nANISOU  498  CD2 PHE A 102    11097  13037   9364   -553  -1204   -181       C\\nATOM    499  CE1 PHE A 102      -1.375   7.184 -16.805  1.00 84.23           C\\nANISOU  499  CE1 PHE A 102    10394  12156   9452   -611  -1257   -481       C\\nATOM    500  CE2 PHE A 102       0.849   7.286 -17.667  1.00 83.36           C\\nANISOU  500  CE2 PHE A 102    10485  12270   8917   -538  -1037   -386       C\\nATOM    501  CZ  PHE A 102      -0.082   6.706 -16.830  1.00 81.83           C\\nANISOU  501  CZ  PHE A 102    10213  11865   9014   -578  -1075   -513       C\\nATOM    502  N   SER A 103      -2.265  11.924 -21.210  1.00 88.70           N\\nANISOU  502  N   SER A 103    11226  13356   9120   -550  -2299    526       N\\nATOM    503  CA  SER A 103      -1.855  13.135 -21.896  1.00 82.43           C\\nANISOU  503  CA  SER A 103    10589  12620   8110   -603  -2476    904       C\\nATOM    504  C   SER A 103      -0.586  13.661 -21.237  1.00 83.13           C\\nANISOU  504  C   SER A 103    10732  12623   8230   -660  -2230   1106       C\\nATOM    505  O   SER A 103      -0.135  13.148 -20.210  1.00 83.31           O\\nANISOU  505  O   SER A 103    10661  12526   8466   -622  -1957    945       O\\nATOM    506  CB  SER A 103      -2.969  14.182 -21.869  1.00 79.20           C\\nANISOU  506  CB  SER A 103    10137  12018   7939   -498  -2879   1043       C\\nATOM    507  OG  SER A 103      -3.335  14.521 -20.542  1.00 76.16           O\\nANISOU  507  OG  SER A 103     9579  11344   8016   -372  -2840    955       O\\nATOM    508  N   ARG A 104       0.009  14.689 -21.845  1.00 84.27           N\\nANISOU  508  N   ARG A 104    11037  12833   8148   -776  -2344   1478       N\\nATOM    509  CA  ARG A 104       1.252  15.212 -21.290  1.00 80.60           C\\nANISOU  509  CA  ARG A 104    10612  12312   7701   -868  -2123   1679       C\\nATOM    510  C   ARG A 104       1.025  15.830 -19.921  1.00 77.44           C\\nANISOU  510  C   ARG A 104    10113  11518   7794   -740  -2150   1682       C\\nATOM    511  O   ARG A 104       1.913  15.783 -19.064  1.00 78.86           O\\nANISOU  511  O   ARG A 104    10250  11620   8096   -755  -1890   1666       O\\nATOM    512  CB  ARG A 104       1.881  16.231 -22.235  1.00 80.66           C\\nANISOU  512  CB  ARG A 104    10815  12469   7362  -1078  -2266   2114       C\\nATOM    513  CG  ARG A 104       3.382  16.383 -22.031  1.00 90.20           C\\nANISOU  513  CG  ARG A 104    12038  13815   8417  -1248  -1948   2260       C\\nATOM    514  CD  ARG A 104       3.766  17.736 -21.446  1.00101.17           C\\nANISOU  514  CD  ARG A 104    13504  14894  10041  -1329  -2089   2624       C\\nATOM    515  NE  ARG A 104       3.451  18.831 -22.359  1.00106.68           N\\nANISOU  515  NE  ARG A 104    14414  15562  10556  -1484  -2476   3046       N\\nATOM    516  CZ  ARG A 104       2.650  19.849 -22.059  1.00108.76           C\\nANISOU  516  CZ  ARG A 104    14758  15416  11150  -1381  -2885   3220       C\\nATOM    517  NH1 ARG A 104       2.092  19.927 -20.857  1.00104.63           N\\nANISOU  517  NH1 ARG A 104    14088  14533  11136  -1126  -2918   2984       N\\nATOM    518  NH2 ARG A 104       2.417  20.795 -22.961  1.00112.28           N\\nANISOU  518  NH2 ARG A 104    15433  15822  11408  -1532  -3275   3626       N\\nATOM    519  N   ILE A 105      -0.160  16.392 -19.688  1.00 79.98           N\\nANISOU  519  N   ILE A 105    10379  11613   8397   -597  -2469   1666       N\\nATOM    520  CA  ILE A 105      -0.435  17.000 -18.394  1.00 78.38           C\\nANISOU  520  CA  ILE A 105    10057  11079   8646   -452  -2502   1613       C\\nATOM    521  C   ILE A 105      -0.797  15.939 -17.359  1.00 74.85           C\\nANISOU  521  C   ILE A 105     9401  10617   8423   -355  -2239   1232       C\\nATOM    522  O   ILE A 105      -0.422  16.063 -16.189  1.00 73.96           O\\nANISOU  522  O   ILE A 105     9211  10343   8549   -307  -2066   1171       O\\nATOM    523  CB  ILE A 105      -1.528  18.076 -18.534  1.00 77.26           C\\nANISOU  523  CB  ILE A 105     9910  10715   8730   -308  -2966   1710       C\\nATOM    524  CG1 ILE A 105      -1.691  18.858 -17.227  1.00 76.93           C\\nANISOU  524  CG1 ILE A 105     9750  10345   9133   -142  -3017   1643       C\\nATOM    525  CG2 ILE A 105      -2.847  17.465 -18.989  1.00 71.80           C\\nANISOU  525  CG2 ILE A 105     9083  10142   8055   -199  -3143   1458       C\\nATOM    526  CD1 ILE A 105      -0.522  19.761 -16.903  1.00 63.79           C\\nANISOU  526  CD1 ILE A 105     8244   8504   7489   -248  -2982   1938       C\\nATOM    527  N   HIS A 106      -1.425  14.862 -17.789  1.00 78.10           N\\nANISOU  527  N   HIS A 106     9732  11194   8747   -350  -2214    984       N\\nATOM    528  CA  HIS A 106      -1.751  13.780 -16.889  1.00 72.04           C\\nANISOU  528  CA  HIS A 106     8805  10412   8157   -326  -1967    668       C\\nATOM    529  C   HIS A 106      -0.480  13.081 -16.470  1.00 75.28           C\\nANISOU  529  C   HIS A 106     9289  10863   8451   -409  -1617    644       C\\nATOM    530  O   HIS A 106      -0.345  12.663 -15.351  1.00 70.37           O\\nANISOU  530  O   HIS A 106     8580  10125   8032   -389  -1418    503       O\\nATOM    531  CB  HIS A 106      -2.690  12.806 -17.558  1.00 69.03           C\\nANISOU  531  CB  HIS A 106     8344  10182   7701   -344  -2050    426       C\\nATOM    532  CG  HIS A 106      -4.109  13.257 -17.558  1.00 86.66           C\\nANISOU  532  CG  HIS A 106    10420  12382  10122   -239  -2375    359       C\\nATOM    533  ND1 HIS A 106      -4.497  14.469 -17.043  1.00 93.53           N\\nANISOU  533  ND1 HIS A 106    11265  13098  11175   -109  -2634    518       N\\nATOM    534  CD2 HIS A 106      -5.234  12.662 -18.003  1.00 92.54           C\\nANISOU  534  CD2 HIS A 106    11011  13228  10921   -235  -2507    125       C\\nATOM    535  CE1 HIS A 106      -5.801  14.602 -17.170  1.00 95.16           C\\nANISOU  535  CE1 HIS A 106    11292  13325  11539     -1  -2912    369       C\\nATOM    536  NE2 HIS A 106      -6.273  13.520 -17.751  1.00 94.46           N\\nANISOU  536  NE2 HIS A 106    11111  13409  11371    -89  -2829    134       N\\nATOM    537  N   CYS A 107       0.459  12.953 -17.384  1.00 74.40           N\\nANISOU  537  N   CYS A 107     9326  10942   8001   -501  -1547    768       N\\nATOM    538  CA  CYS A 107       1.750  12.355 -17.073  1.00 74.41           C\\nANISOU  538  CA  CYS A 107     9366  11008   7898   -548  -1239    725       C\\nATOM    539  C   CYS A 107       2.520  13.220 -16.082  1.00 69.26           C\\nANISOU  539  C   CYS A 107     8705  10174   7436   -541  -1146    902       C\\nATOM    540  O   CYS A 107       3.036  12.718 -15.076  1.00 62.15           O\\nANISOU  540  O   CYS A 107     7754   9173   6688   -508   -936    780       O\\nATOM    541  CB  CYS A 107       2.542  12.149 -18.368  1.00 77.98           C\\nANISOU  541  CB  CYS A 107     9930  11782   7918   -646  -1190    790       C\\nATOM    542  SG  CYS A 107       4.200  11.445 -18.193  1.00 79.49           S\\nANISOU  542  SG  CYS A 107    10119  12137   7945   -673   -832    689       S\\nATOM    543  N   ASP A 108       2.590  14.530 -16.341  1.00 68.64           N\\nANISOU  543  N   ASP A 108     8692  10029   7359   -576  -1335   1195       N\\nATOM    544  CA  ASP A 108       3.289  15.433 -15.430  1.00 67.61           C\\nANISOU  544  CA  ASP A 108     8561   9699   7427   -578  -1293   1358       C\\nATOM    545  C   ASP A 108       2.673  15.405 -14.037  1.00 65.65           C\\nANISOU  545  C   ASP A 108     8180   9208   7557   -435  -1270   1167       C\\nATOM    546  O   ASP A 108       3.393  15.362 -13.033  1.00 66.27           O\\nANISOU  546  O   ASP A 108     8226   9190   7765   -423  -1086   1133       O\\nATOM    547  CB  ASP A 108       3.280  16.856 -15.990  1.00 70.02           C\\nANISOU  547  CB  ASP A 108     8985   9912   7707   -648  -1582   1705       C\\nATOM    548  CG  ASP A 108       4.274  17.047 -17.124  1.00 81.41           C\\nANISOU  548  CG  ASP A 108    10562  11623   8747   -867  -1532   1967       C\\nATOM    549  OD1 ASP A 108       5.293  16.329 -17.150  1.00 84.41           O\\nANISOU  549  OD1 ASP A 108    10904  12225   8943   -940  -1226   1879       O\\nATOM    550  OD2 ASP A 108       4.043  17.922 -17.986  1.00 86.93           O\\nANISOU  550  OD2 ASP A 108    11397  12326   9305   -971  -1808   2260       O\\nATOM    551  N   ILE A 109       1.341  15.424 -13.956  1.00 63.48           N\\nANISOU  551  N   ILE A 109     7808   8870   7442   -332  -1455   1030       N\\nATOM    552  CA  ILE A 109       0.665  15.365 -12.662  1.00 61.96           C\\nANISOU  552  CA  ILE A 109     7449   8532   7562   -218  -1412    821       C\\nATOM    553  C   ILE A 109       1.015  14.072 -11.937  1.00 63.72           C\\nANISOU  553  C   ILE A 109     7629   8811   7771   -268  -1106    623       C\\nATOM    554  O   ILE A 109       1.341  14.076 -10.743  1.00 59.23           O\\nANISOU  554  O   ILE A 109     7010   8137   7359   -241   -960    564       O\\nATOM    555  CB  ILE A 109      -0.856  15.511 -12.845  1.00 58.03           C\\nANISOU  555  CB  ILE A 109     6805   8039   7204   -115  -1656    674       C\\nATOM    556  CG1 ILE A 109      -1.212  16.937 -13.262  1.00 58.42           C\\nANISOU  556  CG1 ILE A 109     6896   7940   7362    -12  -2018    855       C\\nATOM    557  CG2 ILE A 109      -1.588  15.133 -11.573  1.00 56.04           C\\nANISOU  557  CG2 ILE A 109     6336   7761   7197    -50  -1535    405       C\\nATOM    558  CD1 ILE A 109      -2.681  17.131 -13.524  1.00 59.89           C\\nANISOU  558  CD1 ILE A 109     6917   8142   7695    126  -2302    693       C\\nATOM    559  N   PHE A 110       0.949  12.945 -12.648  1.00 61.78           N\\nANISOU  559  N   PHE A 110     7422   8717   7335   -338  -1034    516       N\\nATOM    560  CA  PHE A 110       1.250  11.658 -12.031  1.00 58.79           C\\nANISOU  560  CA  PHE A 110     7039   8336   6961   -385   -808    335       C\\nATOM    561  C   PHE A 110       2.679  11.622 -11.510  1.00 63.91           C\\nANISOU  561  C   PHE A 110     7771   8939   7574   -390   -613    414       C\\nATOM    562  O   PHE A 110       2.921  11.236 -10.361  1.00 59.44           O\\nANISOU  562  O   PHE A 110     7180   8260   7146   -384   -476    340       O\\nATOM    563  CB  PHE A 110       0.997  10.530 -13.034  1.00 61.38           C\\nANISOU  563  CB  PHE A 110     7419   8803   7098   -442   -823    194       C\\nATOM    564  CG  PHE A 110       1.692   9.234 -12.700  1.00 68.94           C\\nANISOU  564  CG  PHE A 110     8447   9728   8016   -477   -636     42       C\\nATOM    565  CD1 PHE A 110       1.579   8.662 -11.444  1.00 75.18           C\\nANISOU  565  CD1 PHE A 110     9204  10361   8999   -508   -525    -42       C\\nATOM    566  CD2 PHE A 110       2.437   8.573 -13.660  1.00 71.59           C\\nANISOU  566  CD2 PHE A 110     8887  10201   8115   -474   -595    -28       C\\nATOM    567  CE1 PHE A 110       2.216   7.472 -11.150  1.00 77.40           C\\nANISOU  567  CE1 PHE A 110     9585  10560   9264   -531   -416   -161       C\\nATOM    568  CE2 PHE A 110       3.070   7.383 -13.372  1.00 74.90           C\\nANISOU  568  CE2 PHE A 110     9372  10553   8534   -462   -477   -203       C\\nATOM    569  CZ  PHE A 110       2.960   6.833 -12.116  1.00 77.70           C\\nANISOU  569  CZ  PHE A 110     9724  10690   9110   -489   -407   -255       C\\nATOM    570  N   VAL A 111       3.641  12.034 -12.340  1.00 65.60           N\\nANISOU  570  N   VAL A 111     8072   9264   7587   -416   -603    568       N\\nATOM    571  CA  VAL A 111       5.043  11.987 -11.930  1.00 66.54           C\\nANISOU  571  CA  VAL A 111     8228   9388   7667   -424   -420    620       C\\nATOM    572  C   VAL A 111       5.288  12.924 -10.757  1.00 60.65           C\\nANISOU  572  C   VAL A 111     7442   8452   7150   -393   -417    727       C\\nATOM    573  O   VAL A 111       6.026  12.590  -9.822  1.00 56.21           O\\nANISOU  573  O   VAL A 111     6872   7814   6670   -370   -270    674       O\\nATOM    574  CB  VAL A 111       5.960  12.317 -13.119  1.00 69.81           C\\nANISOU  574  CB  VAL A 111     8700  10035   7791   -499   -401    765       C\\nATOM    575  CG1 VAL A 111       7.405  12.336 -12.671  1.00 60.98           C\\nANISOU  575  CG1 VAL A 111     7563   8955   6651   -512   -214    801       C\\nATOM    576  CG2 VAL A 111       5.758  11.308 -14.235  1.00 72.95           C\\nANISOU  576  CG2 VAL A 111     9130  10652   7937   -508   -394    597       C\\nATOM    577  N   THR A 112       4.669  14.106 -10.784  1.00 59.23           N\\nANISOU  577  N   THR A 112     7242   8180   7083   -374   -610    861       N\\nATOM    578  CA  THR A 112       4.789  15.036  -9.664  1.00 65.31           C\\nANISOU  578  CA  THR A 112     7970   8754   8090   -319   -646    910       C\\nATOM    579  C   THR A 112       4.286  14.407  -8.371  1.00 66.52           C\\nANISOU  579  C   THR A 112     8031   8833   8410   -256   -532    693       C\\nATOM    580  O   THR A 112       4.970  14.440  -7.343  1.00 76.31           O\\nANISOU  580  O   THR A 112     9268   9991   9734   -241   -417    676       O\\nATOM    581  CB  THR A 112       4.019  16.321  -9.963  1.00 64.71           C\\nANISOU  581  CB  THR A 112     7889   8561   8139   -269   -933   1031       C\\nATOM    582  OG1 THR A 112       4.645  17.010 -11.052  1.00 63.73           O\\nANISOU  582  OG1 THR A 112     7888   8484   7843   -379  -1048   1304       O\\nATOM    583  CG2 THR A 112       3.995  17.223  -8.744  1.00 62.38           C\\nANISOU  583  CG2 THR A 112     7534   8052   8116   -171   -994    998       C\\nATOM    584  N   LEU A 113       3.086  13.825  -8.407  1.00 61.29           N\\nANISOU  584  N   LEU A 113     7289   8219   7778   -245   -569    534       N\\nATOM    585  CA  LEU A 113       2.533  13.195  -7.214  1.00 68.29           C\\nANISOU  585  CA  LEU A 113     8081   9085   8780   -248   -453    353       C\\nATOM    586  C   LEU A 113       3.348  11.975  -6.799  1.00 67.53           C\\nANISOU  586  C   LEU A 113     8081   8983   8595   -321   -257    312       C\\nATOM    587  O   LEU A 113       3.573  11.752  -5.604  1.00 68.67           O\\nANISOU  587  O   LEU A 113     8216   9064   8811   -332   -149    267       O\\nATOM    588  CB  LEU A 113       1.075  12.808  -7.454  1.00 70.65           C\\nANISOU  588  CB  LEU A 113     8249   9477   9119   -266   -536    201       C\\nATOM    589  CG  LEU A 113       0.073  13.960  -7.517  1.00 65.91           C\\nANISOU  589  CG  LEU A 113     7497   8872   8673   -146   -751    162       C\\nATOM    590  CD1 LEU A 113      -1.287  13.451  -7.958  1.00 61.41           C\\nANISOU  590  CD1 LEU A 113     6776   8439   8118   -174   -840      2       C\\nATOM    591  CD2 LEU A 113      -0.016  14.648  -6.165  1.00 61.76           C\\nANISOU  591  CD2 LEU A 113     6853   8287   8324    -59   -710     69       C\\nATOM    592  N   ASP A 114       3.794  11.174  -7.768  1.00 63.91           N\\nANISOU  592  N   ASP A 114     7718   8590   7975   -359   -233    311       N\\nATOM    593  CA  ASP A 114       4.598   9.999  -7.445  1.00 66.05           C\\nANISOU  593  CA  ASP A 114     8086   8820   8191   -384   -102    240       C\\nATOM    594  C   ASP A 114       5.885  10.392  -6.734  1.00 66.08           C\\nANISOU  594  C   ASP A 114     8124   8760   8225   -333    -12    324       C\\nATOM    595  O   ASP A 114       6.262   9.778  -5.730  1.00 69.96           O\\nANISOU  595  O   ASP A 114     8658   9151   8773   -337     64    278       O\\nATOM    596  CB  ASP A 114       4.901   9.208  -8.720  1.00 75.01           C\\nANISOU  596  CB  ASP A 114     9296  10059   9148   -388   -118    174       C\\nATOM    597  CG  ASP A 114       5.951   8.133  -8.509  1.00 75.49           C\\nANISOU  597  CG  ASP A 114     9451  10063   9168   -352    -25     76       C\\nATOM    598  OD1 ASP A 114       5.746   7.255  -7.648  1.00 74.37           O\\nANISOU  598  OD1 ASP A 114     9364   9766   9125   -388     -9     -2       O\\nATOM    599  OD2 ASP A 114       6.981   8.161  -9.214  1.00 76.15           O\\nANISOU  599  OD2 ASP A 114     9549  10268   9116   -291     20     74       O\\nATOM    600  N   VAL A 115       6.568  11.421  -7.235  1.00 71.45           N\\nANISOU  600  N   VAL A 115     8790   9494   8864   -306    -41    464       N\\nATOM    601  CA  VAL A 115       7.809  11.865  -6.610  1.00 70.24           C\\nANISOU  601  CA  VAL A 115     8641   9297   8749   -279     30    542       C\\nATOM    602  C   VAL A 115       7.535  12.461  -5.234  1.00 69.24           C\\nANISOU  602  C   VAL A 115     8477   9030   8802   -253     19    542       C\\nATOM    603  O   VAL A 115       8.282  12.220  -4.279  1.00 70.91           O\\nANISOU  603  O   VAL A 115     8710   9175   9059   -230     93    521       O\\nATOM    604  CB  VAL A 115       8.536  12.862  -7.531  1.00 65.07           C\\nANISOU  604  CB  VAL A 115     7975   8750   7999   -319     -9    719       C\\nATOM    605  CG1 VAL A 115       9.683  13.529  -6.804  1.00 60.52           C\\nANISOU  605  CG1 VAL A 115     7374   8118   7505   -321     36    809       C\\nATOM    606  CG2 VAL A 115       9.043  12.156  -8.778  1.00 62.56           C\\nANISOU  606  CG2 VAL A 115     7676   8649   7446   -346     53    680       C\\nATOM    607  N   MET A 116       6.454  13.232  -5.103  1.00 72.12           N\\nANISOU  607  N   MET A 116     8773   9364   9266   -239    -88    539       N\\nATOM    608  CA  MET A 116       6.164  13.889  -3.832  1.00 68.31           C\\nANISOU  608  CA  MET A 116     8226   8792   8936   -191   -103    487       C\\nATOM    609  C   MET A 116       5.814  12.877  -2.746  1.00 67.37           C\\nANISOU  609  C   MET A 116     8106   8685   8808   -232     19    357       C\\nATOM    610  O   MET A 116       6.435  12.860  -1.677  1.00 67.14           O\\nANISOU  610  O   MET A 116     8105   8604   8802   -221     83    349       O\\nATOM    611  CB  MET A 116       5.031  14.896  -4.005  1.00 66.63           C\\nANISOU  611  CB  MET A 116     7912   8564   8843   -129   -269    455       C\\nATOM    612  CG  MET A 116       4.669  15.602  -2.718  1.00 65.54           C\\nANISOU  612  CG  MET A 116     7676   8370   8856    -46   -291    332       C\\nATOM    613  SD  MET A 116       3.209  16.636  -2.880  1.00 73.08           S\\nANISOU  613  SD  MET A 116     8464   9323   9980     85   -509    199       S\\nATOM    614  CE  MET A 116       3.000  17.178  -1.184  1.00 75.15           C\\nANISOU  614  CE  MET A 116     8597   9592  10365    186   -462    -23       C\\nATOM    615  N   MET A 117       4.820  12.023  -3.000  1.00 57.68           N\\nANISOU  615  N   MET A 117     6854   7527   7535   -303     36    271       N\\nATOM    616  CA  MET A 117       4.373  11.084  -1.977  1.00 63.01           C\\nANISOU  616  CA  MET A 117     7536   8218   8187   -406    135    188       C\\nATOM    617  C   MET A 117       5.457  10.093  -1.578  1.00 71.53           C\\nANISOU  617  C   MET A 117     8783   9196   9201   -439    202    236       C\\nATOM    618  O   MET A 117       5.388   9.526  -0.482  1.00 77.20           O\\nANISOU  618  O   MET A 117     9549   9888   9894   -524    260    225       O\\nATOM    619  CB  MET A 117       3.132  10.337  -2.457  1.00 61.50           C\\nANISOU  619  CB  MET A 117     7283   8115   7968   -518    120    103       C\\nATOM    620  CG  MET A 117       1.975  11.258  -2.770  1.00 64.85           C\\nANISOU  620  CG  MET A 117     7509   8654   8476   -463     28     19       C\\nATOM    621  SD  MET A 117       1.790  12.509  -1.489  1.00 62.59           S\\nANISOU  621  SD  MET A 117     7071   8409   8301   -354     37    -66       S\\nATOM    622  CE  MET A 117       0.518  13.548  -2.206  1.00 56.74           C\\nANISOU  622  CE  MET A 117     6109   7754   7697   -221   -153   -189       C\\nATOM    623  N   CYS A 118       6.449   9.867  -2.434  1.00 70.60           N\\nANISOU  623  N   CYS A 118     8747   9036   9042   -373    183    282       N\\nATOM    624  CA  CYS A 118       7.576   9.023  -2.062  1.00 70.67           C\\nANISOU  624  CA  CYS A 118     8885   8946   9021   -346    211    289       C\\nATOM    625  C   CYS A 118       8.689   9.813  -1.387  1.00 68.27           C\\nANISOU  625  C   CYS A 118     8564   8615   8761   -260    228    351       C\\nATOM    626  O   CYS A 118       9.435   9.249  -0.578  1.00 62.32           O\\nANISOU  626  O   CYS A 118     7898   7774   8009   -239    233    351       O\\nATOM    627  CB  CYS A 118       8.121   8.295  -3.295  1.00 71.86           C\\nANISOU  627  CB  CYS A 118     9091   9112   9101   -295    188    239       C\\nATOM    628  SG  CYS A 118       6.974   7.093  -4.021  1.00 68.74           S\\nANISOU  628  SG  CYS A 118     8755   8698   8664   -398    132    131       S\\nATOM    629  N   THR A 119       8.819  11.105  -1.703  1.00 71.90           N\\nANISOU  629  N   THR A 119     8925   9128   9267   -218    203    409       N\\nATOM    630  CA  THR A 119       9.769  11.947  -0.985  1.00 68.93           C\\nANISOU  630  CA  THR A 119     8523   8711   8956   -165    196    461       C\\nATOM    631  C   THR A 119       9.300  12.212   0.440  1.00 62.52           C\\nANISOU  631  C   THR A 119     7704   7861   8191   -175    201    411       C\\nATOM    632  O   THR A 119      10.125  12.295   1.357  1.00 61.89           O\\nANISOU  632  O   THR A 119     7656   7732   8127   -144    202    417       O\\nATOM    633  CB  THR A 119       9.981  13.271  -1.728  1.00 67.89           C\\nANISOU  633  CB  THR A 119     8314   8606   8874   -156    129    558       C\\nATOM    634  OG1 THR A 119      10.268  13.009  -3.105  1.00 63.88           O\\nANISOU  634  OG1 THR A 119     7808   8202   8260   -182    139    610       O\\nATOM    635  CG2 THR A 119      11.148  14.045  -1.129  1.00 64.40           C\\nANISOU  635  CG2 THR A 119     7848   8113   8507   -132    108    616       C\\nATOM    636  N   ALA A 120       7.987  12.343   0.642  1.00 61.79           N\\nANISOU  636  N   ALA A 120     7547   7824   8105   -218    203    341       N\\nATOM    637  CA  ALA A 120       7.457  12.486   1.992  1.00 59.49           C\\nANISOU  637  CA  ALA A 120     7220   7579   7805   -246    240    258       C\\nATOM    638  C   ALA A 120       7.815  11.283   2.852  1.00 61.28           C\\nANISOU  638  C   ALA A 120     7585   7779   7919   -337    300    286       C\\nATOM    639  O   ALA A 120       8.114  11.433   4.041  1.00 62.06           O\\nANISOU  639  O   ALA A 120     7711   7891   7976   -343    316    271       O\\nATOM    640  CB  ALA A 120       5.943  12.676   1.947  1.00 60.06           C\\nANISOU  640  CB  ALA A 120     7153   7780   7886   -287    251    145       C\\nATOM    641  N   SER A 121       7.784  10.080   2.268  1.00 59.91           N\\nANISOU  641  N   SER A 121     7518   7552   7694   -409    305    325       N\\nATOM    642  CA  SER A 121       8.208   8.889   2.998  1.00 65.17           C\\nANISOU  642  CA  SER A 121     8361   8120   8282   -489    296    378       C\\nATOM    643  C   SER A 121       9.662   9.003   3.431  1.00 68.85           C\\nANISOU  643  C   SER A 121     8900   8486   8775   -361    241    416       C\\nATOM    644  O   SER A 121      10.014   8.643   4.561  1.00 69.48           O\\nANISOU  644  O   SER A 121     9088   8521   8792   -399    214    457       O\\nATOM    645  CB  SER A 121       8.013   7.640   2.137  1.00 61.09           C\\nANISOU  645  CB  SER A 121     7954   7505   7753   -550    254    383       C\\nATOM    646  OG  SER A 121       6.661   7.485   1.747  1.00 71.73           O\\nANISOU  646  OG  SER A 121     9221   8952   9081   -688    290    343       O\\nATOM    647  N   ALA A 122      10.522   9.500   2.544  1.00 66.20           N\\nANISOU  647  N   ALA A 122     8498   8140   8516   -228    219    409       N\\nATOM    648  CA  ALA A 122      11.932   9.632   2.882  1.00 64.09           C\\nANISOU  648  CA  ALA A 122     8247   7817   8288   -115    169    424       C\\nATOM    649  C   ALA A 122      12.144  10.731   3.911  1.00 67.35           C\\nANISOU  649  C   ALA A 122     8599   8264   8729    -99    162    428       C\\nATOM    650  O   ALA A 122      12.870  10.544   4.893  1.00 67.60           O\\nANISOU  650  O   ALA A 122     8699   8245   8739    -68    109    438       O\\nATOM    651  CB  ALA A 122      12.746   9.905   1.621  1.00 62.95           C\\nANISOU  651  CB  ALA A 122     8005   7723   8189    -24    175    411       C\\nATOM    652  N   LEU A 123      11.511  11.886   3.707  1.00 62.65           N\\nANISOU  652  N   LEU A 123     7879   7737   8186   -107    182    403       N\\nATOM    653  CA  LEU A 123      11.661  12.982   4.654  1.00 64.73           C\\nANISOU  653  CA  LEU A 123     8084   8013   8499    -71    145    360       C\\nATOM    654  C   LEU A 123      11.002  12.677   5.993  1.00 68.58           C\\nANISOU  654  C   LEU A 123     8623   8569   8865   -134    179    297       C\\nATOM    655  O   LEU A 123      11.397  13.259   7.008  1.00 65.26           O\\nANISOU  655  O   LEU A 123     8197   8165   8435    -96    140    244       O\\nATOM    656  CB  LEU A 123      11.095  14.271   4.056  1.00 60.03           C\\nANISOU  656  CB  LEU A 123     7361   7429   8020    -42    106    331       C\\nATOM    657  CG  LEU A 123      12.060  15.137   3.236  1.00 62.40           C\\nANISOU  657  CG  LEU A 123     7610   7663   8437    -13     31    421       C\\nATOM    658  CD1 LEU A 123      12.857  14.325   2.223  1.00 59.85           C\\nANISOU  658  CD1 LEU A 123     7308   7374   8057    -33     81    508       C\\nATOM    659  CD2 LEU A 123      11.293  16.248   2.540  1.00 58.42           C\\nANISOU  659  CD2 LEU A 123     7032   7125   8039     -7    -54    431       C\\nATOM    660  N   ASN A 124      10.015  11.778   6.022  1.00 64.20           N\\nANISOU  660  N   ASN A 124     8115   8078   8200   -253    250    303       N\\nATOM    661  CA  ASN A 124       9.452  11.343   7.295  1.00 68.55           C\\nANISOU  661  CA  ASN A 124     8724   8742   8580   -376    301    282       C\\nATOM    662  C   ASN A 124      10.430  10.450   8.047  1.00 72.49           C\\nANISOU  662  C   ASN A 124     9424   9133   8985   -402    229    393       C\\nATOM    663  O   ASN A 124      10.617  10.600   9.260  1.00 78.80           O\\nANISOU  663  O   ASN A 124    10273  10006   9661   -433    215    382       O\\nATOM    664  CB  ASN A 124       8.129  10.616   7.067  1.00 63.03           C\\nANISOU  664  CB  ASN A 124     8004   8152   7791   -549    391    281       C\\nATOM    665  CG  ASN A 124       6.940  11.540   7.141  1.00 59.12           C\\nANISOU  665  CG  ASN A 124     7283   7866   7312   -543    463    113       C\\nATOM    666  OD1 ASN A 124       6.864  12.399   8.016  1.00 58.74           O\\nANISOU  666  OD1 ASN A 124     7141   7941   7236   -481    474    -16       O\\nATOM    667  ND2 ASN A 124       6.000  11.373   6.218  1.00 59.97           N\\nANISOU  667  ND2 ASN A 124     7292   8020   7473   -588    490     83       N\\nATOM    668  N   LEU A 125      11.062   9.508   7.343  1.00 66.29           N\\nANISOU  668  N   LEU A 125     8756   8179   8253   -373    162    480       N\\nATOM    669  CA  LEU A 125      12.084   8.682   7.972  1.00 65.46           C\\nANISOU  669  CA  LEU A 125     8836   7929   8106   -343     35    565       C\\nATOM    670  C   LEU A 125      13.243   9.524   8.477  1.00 65.97           C\\nANISOU  670  C   LEU A 125     8840   7991   8234   -191    -37    522       C\\nATOM    671  O   LEU A 125      13.922   9.139   9.436  1.00 61.15           O\\nANISOU  671  O   LEU A 125     8360   7325   7547   -177   -149    572       O\\nATOM    672  CB  LEU A 125      12.583   7.629   6.988  1.00 62.70           C\\nANISOU  672  CB  LEU A 125     8578   7397   7847   -276    -48    593       C\\nATOM    673  CG  LEU A 125      11.555   6.553   6.663  1.00 64.43           C\\nANISOU  673  CG  LEU A 125     8919   7557   8006   -451    -38    646       C\\nATOM    674  CD1 LEU A 125      12.089   5.633   5.597  1.00 62.96           C\\nANISOU  674  CD1 LEU A 125     8802   7188   7932   -337   -140    608       C\\nATOM    675  CD2 LEU A 125      11.214   5.779   7.920  1.00 61.82           C\\nANISOU  675  CD2 LEU A 125     8799   7183   7505   -650   -100    783       C\\nATOM    676  N   CYS A 126      13.482  10.673   7.849  1.00 67.22           N\\nANISOU  676  N   CYS A 126     8812   8199   8530    -94      0    444       N\\nATOM    677  CA  CYS A 126      14.522  11.568   8.333  1.00 68.85           C\\nANISOU  677  CA  CYS A 126     8945   8402   8814     11    -78    401       C\\nATOM    678  C   CYS A 126      14.084  12.257   9.617  1.00 71.84           C\\nANISOU  678  C   CYS A 126     9323   8885   9086    -30    -78    330       C\\nATOM    679  O   CYS A 126      14.848  12.331  10.588  1.00 74.42           O\\nANISOU  679  O   CYS A 126     9709   9205   9362      8   -177    320       O\\nATOM    680  CB  CYS A 126      14.866  12.592   7.257  1.00 64.79           C\\nANISOU  680  CB  CYS A 126     8252   7891   8474     72    -60    375       C\\nATOM    681  SG  CYS A 126      16.409  13.441   7.561  1.00 69.06           S\\nANISOU  681  SG  CYS A 126     8693   8402   9146    160   -175    353       S\\nATOM    682  N   ALA A 127      12.849  12.762   9.642  1.00 60.58           N\\nANISOU  682  N   ALA A 127     7817   7582   7618    -95     24    250       N\\nATOM    683  CA  ALA A 127      12.322  13.375  10.854  1.00 61.10           C\\nANISOU  683  CA  ALA A 127     7852   7809   7555   -121     44    122       C\\nATOM    684  C   ALA A 127      12.220  12.369  11.990  1.00 65.12           C\\nANISOU  684  C   ALA A 127     8538   8411   7794   -256     52    201       C\\nATOM    685  O   ALA A 127      12.407  12.729  13.158  1.00 65.71           O\\nANISOU  685  O   ALA A 127     8640   8603   7724   -258     16    127       O\\nATOM    686  CB  ALA A 127      10.957  13.996  10.570  1.00 60.25           C\\nANISOU  686  CB  ALA A 127     7585   7843   7462   -141    147    -17       C\\nATOM    687  N   ILE A 128      11.925  11.108  11.673  1.00 64.09           N\\nANISOU  687  N   ILE A 128     8546   8221   7582   -384     77    357       N\\nATOM    688  CA  ILE A 128      11.829  10.083  12.705  1.00 61.38           C\\nANISOU  688  CA  ILE A 128     8417   7924   6982   -558     46    492       C\\nATOM    689  C   ILE A 128      13.184   9.868  13.370  1.00 64.99           C\\nANISOU  689  C   ILE A 128     9025   8241   7426   -455   -148    563       C\\nATOM    690  O   ILE A 128      13.286   9.807  14.600  1.00 69.74           O\\nANISOU  690  O   ILE A 128     9740   8959   7800   -534   -198    591       O\\nATOM    691  CB  ILE A 128      11.271   8.779  12.108  1.00 62.32           C\\nANISOU  691  CB  ILE A 128     8673   7934   7072   -722     61    653       C\\nATOM    692  CG1 ILE A 128       9.772   8.923  11.836  1.00 63.83           C\\nANISOU  692  CG1 ILE A 128     8711   8345   7195   -888    252    582       C\\nATOM    693  CG2 ILE A 128      11.548   7.604  13.028  1.00 64.88           C\\nANISOU  693  CG2 ILE A 128     9290   8172   7190   -886    -69    860       C\\nATOM    694  CD1 ILE A 128       9.120   7.668  11.294  1.00 68.59           C\\nANISOU  694  CD1 ILE A 128     9440   8852   7770  -1092    259    730       C\\nATOM    695  N   SER A 129      14.244   9.756  12.565  1.00 66.20           N\\nANISOU  695  N   SER A 129     9164   8178   7810   -278   -262    578       N\\nATOM    696  CA  SER A 129      15.586   9.611  13.121  1.00 63.02           C\\nANISOU  696  CA  SER A 129     8848   7658   7438   -147   -463    607       C\\nATOM    697  C   SER A 129      15.949  10.799  13.998  1.00 65.47           C\\nANISOU  697  C   SER A 129     9055   8109   7713    -86   -487    474       C\\nATOM    698  O   SER A 129      16.527  10.629  15.078  1.00 65.88           O\\nANISOU  698  O   SER A 129     9234   8177   7619    -82   -631    506       O\\nATOM    699  CB  SER A 129      16.603   9.467  11.995  1.00 65.36           C\\nANISOU  699  CB  SER A 129     9050   7784   7998     39   -538    582       C\\nATOM    700  OG  SER A 129      16.749  10.693  11.302  1.00 65.87           O\\nANISOU  700  OG  SER A 129     8871   7922   8235    114   -445    460       O\\nATOM    701  N   ILE A 130      15.624  12.011  13.546  1.00 64.82           N\\nANISOU  701  N   ILE A 130     8755   8106   7766    -35   -383    319       N\\nATOM    702  CA  ILE A 130      15.959  13.208  14.313  1.00 68.76           C\\nANISOU  702  CA  ILE A 130     9156   8695   8276     36   -439    156       C\\nATOM    703  C   ILE A 130      15.205  13.216  15.636  1.00 70.22           C\\nANISOU  703  C   ILE A 130     9425   9110   8144    -76   -395     92       C\\nATOM    704  O   ILE A 130      15.775  13.502  16.695  1.00 76.17           O\\nANISOU  704  O   ILE A 130    10235   9933   8773    -45   -514     30       O\\nATOM    705  CB  ILE A 130      15.668  14.473  13.488  1.00 69.26           C\\nANISOU  705  CB  ILE A 130     9002   8739   8574    105   -379     19       C\\nATOM    706  CG1 ILE A 130      16.553  14.504  12.241  1.00 65.51           C\\nANISOU  706  CG1 ILE A 130     8440   8094   8355    174   -420    103       C\\nATOM    707  CG2 ILE A 130      15.878  15.716  14.329  1.00 65.28           C\\nANISOU  707  CG2 ILE A 130     8415   8293   8097    175   -469   -180       C\\nATOM    708  CD1 ILE A 130      16.380  15.745  11.402  1.00 62.56           C\\nANISOU  708  CD1 ILE A 130     7895   7673   8203    202   -405     32       C\\nATOM    709  N   ASP A 131      13.909  12.904  15.595  1.00 70.28           N\\nANISOU  709  N   ASP A 131     9426   9280   7998   -221   -219     94       N\\nATOM    710  CA  ASP A 131      13.155  12.749  16.833  1.00 71.28           C\\nANISOU  710  CA  ASP A 131     9617   9702   7763   -378   -141     50       C\\nATOM    711  C   ASP A 131      13.708  11.611  17.677  1.00 75.20           C\\nANISOU  711  C   ASP A 131    10397  10170   8008   -506   -269    283       C\\nATOM    712  O   ASP A 131      13.639  11.660  18.910  1.00 73.14           O\\nANISOU  712  O   ASP A 131    10222  10134   7432   -599   -289    255       O\\nATOM    713  CB  ASP A 131      11.678  12.515  16.525  1.00 70.71           C\\nANISOU  713  CB  ASP A 131     9449   9834   7586   -540     79     22       C\\nATOM    714  CG  ASP A 131      10.820  12.477  17.775  1.00 76.68           C\\nANISOU  714  CG  ASP A 131    10201  10991   7942   -727    206    -66       C\\nATOM    715  OD1 ASP A 131      10.819  13.472  18.528  1.00 78.05           O\\nANISOU  715  OD1 ASP A 131    10254  11363   8039   -619    204   -327       O\\nATOM    716  OD2 ASP A 131      10.140  11.455  18.001  1.00 79.31           O\\nANISOU  716  OD2 ASP A 131    10647  11456   8030   -996    304    118       O\\nATOM    717  N   ARG A 132      14.264  10.581  17.036  1.00 72.55           N\\nANISOU  717  N   ARG A 132    10215   9556   7796   -504   -380    502       N\\nATOM    718  CA  ARG A 132      14.921   9.521  17.791  1.00 74.39           C\\nANISOU  718  CA  ARG A 132    10739   9679   7847   -579   -584    726       C\\nATOM    719  C   ARG A 132      16.221  10.003  18.417  1.00 74.84           C\\nANISOU  719  C   ARG A 132    10811   9673   7954   -388   -804    656       C\\nATOM    720  O   ARG A 132      16.614   9.507  19.479  1.00 74.70           O\\nANISOU  720  O   ARG A 132    11012   9686   7686   -458   -973    778       O\\nATOM    721  CB  ARG A 132      15.175   8.307  16.894  1.00 71.71           C\\nANISOU  721  CB  ARG A 132    10547   9024   7674   -578   -687    923       C\\nATOM    722  CG  ARG A 132      13.976   7.378  16.715  1.00 69.10           C\\nANISOU  722  CG  ARG A 132    10338   8727   7188   -858   -567   1086       C\\nATOM    723  CD  ARG A 132      13.493   6.832  18.055  1.00 75.91           C\\nANISOU  723  CD  ARG A 132    11433   9782   7627  -1155   -591   1269       C\\nATOM    724  NE  ARG A 132      12.518   7.717  18.686  1.00 77.94           N\\nANISOU  724  NE  ARG A 132    11497  10480   7636  -1291   -337   1099       N\\nATOM    725  CZ  ARG A 132      12.271   7.756  19.990  1.00 77.58           C\\nANISOU  725  CZ  ARG A 132    11552  10740   7186  -1484   -317   1141       C\\nATOM    726  NH1 ARG A 132      12.931   6.960  20.822  1.00 76.41           N\\nANISOU  726  NH1 ARG A 132    11728  10477   6827  -1585   -559   1394       N\\nATOM    727  NH2 ARG A 132      11.366   8.602  20.464  1.00 79.78           N\\nANISOU  727  NH2 ARG A 132    11599  11452   7261  -1565    -71    912       N\\nATOM    728  N   TYR A 133      16.902  10.960  17.786  1.00 73.32           N\\nANISOU  728  N   TYR A 133    10393   9395   8070   -171   -822    476       N\\nATOM    729  CA  TYR A 133      18.124  11.492  18.379  1.00 72.55           C\\nANISOU  729  CA  TYR A 133    10271   9257   8037    -13  -1032    389       C\\nATOM    730  C   TYR A 133      17.813  12.311  19.624  1.00 76.41           C\\nANISOU  730  C   TYR A 133    10753  10016   8263    -65  -1020    228       C\\nATOM    731  O   TYR A 133      18.475  12.161  20.658  1.00 82.66           O\\nANISOU  731  O   TYR A 133    11685  10852   8869    -54  -1214    255       O\\nATOM    732  CB  TYR A 133      18.894  12.340  17.365  1.00 65.57           C\\nANISOU  732  CB  TYR A 133     9133   8238   7542    169  -1045    254       C\\nATOM    733  CG  TYR A 133      20.160  12.957  17.931  1.00 69.03           C\\nANISOU  733  CG  TYR A 133     9504   8648   8079    305  -1262    149       C\\nATOM    734  CD1 TYR A 133      21.367  12.268  17.901  1.00 73.59           C\\nANISOU  734  CD1 TYR A 133    10124   9075   8760    424  -1482    232       C\\nATOM    735  CD2 TYR A 133      20.148  14.224  18.502  1.00 67.30           C\\nANISOU  735  CD2 TYR A 133     9162   8546   7862    326  -1271    -61       C\\nATOM    736  CE1 TYR A 133      22.526  12.825  18.419  1.00 73.44           C\\nANISOU  736  CE1 TYR A 133    10011   9052   8839    539  -1690    123       C\\nATOM    737  CE2 TYR A 133      21.303  14.789  19.022  1.00 69.25           C\\nANISOU  737  CE2 TYR A 133     9341   8760   8209    429  -1488   -164       C\\nATOM    738  CZ  TYR A 133      22.488  14.084  18.977  1.00 74.54           C\\nANISOU  738  CZ  TYR A 133    10039   9309   8975    524  -1689    -64       C\\nATOM    739  OH  TYR A 133      23.637  14.640  19.490  1.00 78.51           O\\nANISOU  739  OH  TYR A 133    10443   9800   9586    618  -1914   -178       O\\nATOM    740  N   THR A 134      16.813  13.190  19.544  1.00 70.79           N\\nANISOU  740  N   THR A 134     9871   9496   7530   -102   -814     34       N\\nATOM    741  CA  THR A 134      16.526  14.064  20.674  1.00 74.84           C\\nANISOU  741  CA  THR A 134    10337  10284   7814   -106   -805   -201       C\\nATOM    742  C   THR A 134      16.021  13.276  21.876  1.00 73.81           C\\nANISOU  742  C   THR A 134    10425  10433   7188   -319   -780    -82       C\\nATOM    743  O   THR A 134      16.266  13.672  23.021  1.00 83.45           O\\nANISOU  743  O   THR A 134    11696  11863   8150   -318   -870   -208       O\\nATOM    744  CB  THR A 134      15.517  15.137  20.270  1.00 81.04           C\\nANISOU  744  CB  THR A 134    10877  11199   8715    -61   -617   -471       C\\nATOM    745  OG1 THR A 134      14.231  14.541  20.084  1.00 85.24           O\\nANISOU  745  OG1 THR A 134    11407  11920   9060   -236   -387   -405       O\\nATOM    746  CG2 THR A 134      15.945  15.803  18.969  1.00 80.96           C\\nANISOU  746  CG2 THR A 134    10697  10893   9169     91   -653   -505       C\\nATOM    747  N   ALA A 135      15.341  12.151  21.642  1.00 74.49           N\\nANISOU  747  N   ALA A 135    10655  10530   7120   -527   -674    172       N\\nATOM    748  CA  ALA A 135      14.858  11.340  22.756  1.00 76.81           C\\nANISOU  748  CA  ALA A 135    11182  11087   6918   -800   -658    350       C\\nATOM    749  C   ALA A 135      16.008  10.654  23.480  1.00 76.81           C\\nANISOU  749  C   ALA A 135    11471  10921   6791   -787   -978    571       C\\nATOM    750  O   ALA A 135      15.979  10.505  24.707  1.00 82.26           O\\nANISOU  750  O   ALA A 135    12330  11871   7053   -935  -1044    623       O\\nATOM    751  CB  ALA A 135      13.849  10.307  22.259  1.00 69.76           C\\nANISOU  751  CB  ALA A 135    10373  10203   5930  -1063   -492    588       C\\nATOM    752  N   VAL A 136      17.029  10.233  22.739  1.00 76.95           N\\nANISOU  752  N   VAL A 136    11539  10534   7164   -603  -1189    688       N\\nATOM    753  CA  VAL A 136      18.154   9.535  23.350  1.00 82.31           C\\nANISOU  753  CA  VAL A 136    12472  11024   7777   -545  -1537    878       C\\nATOM    754  C   VAL A 136      19.136  10.524  23.967  1.00 82.04           C\\nANISOU  754  C   VAL A 136    12325  11053   7795   -336  -1708    644       C\\nATOM    755  O   VAL A 136      19.554  10.367  25.120  1.00 81.48           O\\nANISOU  755  O   VAL A 136    12446  11103   7411   -382  -1911    704       O\\nATOM    756  CB  VAL A 136      18.839   8.630  22.309  1.00 77.31           C\\nANISOU  756  CB  VAL A 136    11904   9961   7508   -406  -1706   1045       C\\nATOM    757  CG1 VAL A 136      20.246   8.278  22.755  1.00 77.43           C\\nANISOU  757  CG1 VAL A 136    12049   9764   7606   -210  -2095   1106       C\\nATOM    758  CG2 VAL A 136      18.017   7.366  22.083  1.00 72.64           C\\nANISOU  758  CG2 VAL A 136    11557   9266   6777   -655  -1667   1340       C\\nATOM    759  N   ALA A 137      19.501  11.568  23.224  1.00 77.79           N\\nANISOU  759  N   ALA A 137    11484  10437   7637   -128  -1644    384       N\\nATOM    760  CA  ALA A 137      20.609  12.434  23.603  1.00 80.22           C\\nANISOU  760  CA  ALA A 137    11669  10715   8097     69  -1852    182       C\\nATOM    761  C   ALA A 137      20.209  13.605  24.491  1.00 87.12           C\\nANISOU  761  C   ALA A 137    12440  11898   8765     54  -1780   -115       C\\nATOM    762  O   ALA A 137      21.094  14.243  25.073  1.00 87.55           O\\nANISOU  762  O   ALA A 137    12447  11955   8861    179  -1994   -277       O\\nATOM    763  CB  ALA A 137      21.304  12.975  22.349  1.00 74.40           C\\nANISOU  763  CB  ALA A 137    10663   9730   7877    260  -1849     74       C\\nATOM    764  N   MET A 138      18.922  13.910  24.616  1.00 85.65           N\\nANISOU  764  N   MET A 138    12198  11978   8368    -81  -1504   -224       N\\nATOM    765  CA  MET A 138      18.517  15.099  25.348  1.00 91.36           C\\nANISOU  765  CA  MET A 138    12776  12989   8948    -40  -1439   -587       C\\nATOM    766  C   MET A 138      17.450  14.760  26.377  1.00 93.65           C\\nANISOU  766  C   MET A 138    13184  13730   8670   -264  -1268   -595       C\\nATOM    767  O   MET A 138      16.648  13.844  26.169  1.00 90.32           O\\nANISOU  767  O   MET A 138    12865  13389   8064   -478  -1095   -353       O\\nATOM    768  CB  MET A 138      18.001  16.181  24.387  1.00 94.18           C\\nANISOU  768  CB  MET A 138    12839  13259   9687     83  -1276   -847       C\\nATOM    769  CG  MET A 138      19.095  16.769  23.500  1.00 98.65           C\\nANISOU  769  CG  MET A 138    13264  13452  10767    263  -1446   -874       C\\nATOM    770  SD  MET A 138      18.521  18.077  22.402  1.00105.80           S\\nANISOU  770  SD  MET A 138    13881  14215  12101    371  -1319  -1121       S\\nATOM    771  CE  MET A 138      20.031  18.481  21.533  1.00105.56           C\\nANISOU  771  CE  MET A 138    13744  13805  12559    477  -1542  -1039       C\\nATOM    772  N   PRO A 139      17.425  15.482  27.515  1.00104.46           N\\nANISOU  772  N   PRO A 139    14532  15425   9735   -241  -1315   -880       N\\nATOM    773  CA  PRO A 139      16.509  15.224  28.635  1.00105.59           C\\nANISOU  773  CA  PRO A 139    14765  16095   9259   -469  -1152   -923       C\\nATOM    774  C   PRO A 139      15.042  15.103  28.221  1.00104.65           C\\nANISOU  774  C   PRO A 139    14492  16238   9033   -630   -782   -969       C\\nATOM    775  O   PRO A 139      14.317  16.097  28.261  1.00106.02           O\\nANISOU  775  O   PRO A 139    14394  16653   9234   -519   -617  -1385       O\\nATOM    776  CB  PRO A 139      16.714  16.446  29.535  1.00103.32           C\\nANISOU  776  CB  PRO A 139    14347  16058   8852   -301  -1242  -1390       C\\nATOM    777  CG  PRO A 139      18.112  16.868  29.263  1.00100.62           C\\nANISOU  777  CG  PRO A 139    14009  15289   8934    -72  -1575  -1406       C\\nATOM    778  CD  PRO A 139      18.340  16.603  27.805  1.00 97.12           C\\nANISOU  778  CD  PRO A 139    13483  14389   9030     -4  -1545  -1193       C\\nATOM    779  N   THR A 144       8.716  17.350  27.929  1.00103.31           N\\nANISOU  779  N   THR A 144    12885  17966   8400   -718    631  -2535       N\\nATOM    780  CA  THR A 144       7.590  18.233  28.208  1.00111.55           C\\nANISOU  780  CA  THR A 144    13533  19499   9351   -578    832  -3111       C\\nATOM    781  C   THR A 144       6.396  17.895  27.318  1.00111.78           C\\nANISOU  781  C   THR A 144    13322  19627   9521   -685   1084  -3075       C\\nATOM    782  O   THR A 144       6.556  17.666  26.122  1.00115.16           O\\nANISOU  782  O   THR A 144    13802  19541  10411   -631   1006  -2812       O\\nATOM    783  CB  THR A 144       7.971  19.712  28.006  1.00112.47           C\\nANISOU  783  CB  THR A 144    13477  19327   9931   -104    597  -3618       C\\nATOM    784  N   ARG A 145       5.198  17.868  27.907  1.00112.87           N\\nANISOU  784  N   ARG A 145    13181  20279   9425   -824   1334  -3251       N\\nATOM    785  CA  ARG A 145       4.002  17.509  27.151  1.00114.09           C\\nANISOU  785  CA  ARG A 145    13078  20551   9719   -950   1551  -3212       C\\nATOM    786  C   ARG A 145       3.581  18.596  26.170  1.00118.73           C\\nANISOU  786  C   ARG A 145    13352  20930  10830   -531   1477  -3651       C\\nATOM    787  O   ARG A 145       2.846  18.305  25.221  1.00119.01           O\\nANISOU  787  O   ARG A 145    13234  20913  11072   -582   1585  -3578       O\\nATOM    788  CB  ARG A 145       2.846  17.198  28.104  1.00118.50           C\\nANISOU  788  CB  ARG A 145    13396  21689   9937  -1221   1786  -3270       C\\nATOM    789  N   TYR A 146       4.024  19.834  26.375  1.00121.59           N\\nANISOU  789  N   TYR A 146    13630  21133  11434   -123   1259  -4089       N\\nATOM    790  CA  TYR A 146       3.700  20.948  25.491  1.00117.64           C\\nANISOU  790  CA  TYR A 146    12880  20335  11482    295   1102  -4485       C\\nATOM    791  C   TYR A 146       4.829  21.280  24.526  1.00108.31           C\\nANISOU  791  C   TYR A 146    11951  18428  10772    498    805  -4303       C\\nATOM    792  O   TYR A 146       4.573  21.530  23.344  1.00100.71           O\\nANISOU  792  O   TYR A 146    10911  17078  10275    638    718  -4241       O\\nATOM    793  CB  TYR A 146       3.345  22.185  26.325  1.00124.08           C\\nANISOU  793  CB  TYR A 146    13429  21323  12394    606    974  -5030       C\\nATOM    794  CG  TYR A 146       3.156  23.462  25.533  1.00125.41           C\\nANISOU  794  CG  TYR A 146    13400  21084  13165   1062    702  -5422       C\\nATOM    795  CD1 TYR A 146       1.920  23.794  24.993  1.00128.22           C\\nANISOU  795  CD1 TYR A 146    13405  21556  13758   1181    740  -5641       C\\nATOM    796  CD2 TYR A 146       4.211  24.347  25.345  1.00125.84           C\\nANISOU  796  CD2 TYR A 146    13634  20614  13563   1355    362  -5554       C\\nATOM    797  CE1 TYR A 146       1.746  24.966  24.276  1.00131.82           C\\nANISOU  797  CE1 TYR A 146    13721  21595  14769   1588    432  -5955       C\\nATOM    798  CE2 TYR A 146       4.047  25.515  24.631  1.00128.03           C\\nANISOU  798  CE2 TYR A 146    13776  20456  14413   1732     64  -5846       C\\nATOM    799  CZ  TYR A 146       2.815  25.821  24.099  1.00132.64           C\\nANISOU  799  CZ  TYR A 146    14037  21147  15214   1852     92  -6034       C\\nATOM    800  OH  TYR A 146       2.656  26.988  23.388  1.00136.93           O\\nANISOU  800  OH  TYR A 146    14484  21222  16320   2213   -261  -6277       O\\nATOM    801  N   SER A 147       6.076  21.287  25.005  1.00108.97           N\\nANISOU  801  N   SER A 147    12336  18257  10810    490    611  -4125       N\\nATOM    802  CA  SER A 147       7.206  21.602  24.138  1.00104.01           C\\nANISOU  802  CA  SER A 147    11926  16901  10691    633    308  -3860       C\\nATOM    803  C   SER A 147       7.407  20.541  23.065  1.00103.85           C\\nANISOU  803  C   SER A 147    12083  16559  10818    407    370  -3277       C\\nATOM    804  O   SER A 147       7.842  20.861  21.953  1.00 99.45           O\\nANISOU  804  O   SER A 147    11570  15480  10738    539    199  -3123       O\\nATOM    805  CB  SER A 147       8.481  21.758  24.972  1.00101.67           C\\nANISOU  805  CB  SER A 147    11877  16479  10273    647     99  -3814       C\\nATOM    806  N   SER A 148       7.103  19.279  23.375  1.00100.58           N\\nANISOU  806  N   SER A 148    11778  16447   9991     56    598  -2950       N\\nATOM    807  CA  SER A 148       7.325  18.214  22.404  1.00 97.98           C\\nANISOU  807  CA  SER A 148    11636  15794   9798   -147    625  -2427       C\\nATOM    808  C   SER A 148       6.273  18.239  21.303  1.00 88.88           C\\nANISOU  808  C   SER A 148    10254  14611   8905   -117    745  -2472       C\\nATOM    809  O   SER A 148       6.602  18.071  20.125  1.00 80.56           O\\nANISOU  809  O   SER A 148     9283  13109   8218    -74    646  -2217       O\\nATOM    810  CB  SER A 148       7.339  16.858  23.106  1.00103.00           C\\nANISOU  810  CB  SER A 148    12497  16702   9935   -541    771  -2055       C\\nATOM    811  OG  SER A 148       6.089  16.599  23.719  1.00106.17           O\\nANISOU  811  OG  SER A 148    12692  17721   9926   -754   1057  -2228       O\\nATOM    812  N   LYS A 149       5.003  18.446  21.667  1.00 92.05           N\\nANISOU  812  N   LYS A 149    10349  15519   9108   -139    955  -2812       N\\nATOM    813  CA  LYS A 149       3.946  18.506  20.661  1.00 84.26           C\\nANISOU  813  CA  LYS A 149     9110  14536   8369    -93   1046  -2895       C\\nATOM    814  C   LYS A 149       4.192  19.638  19.673  1.00 88.93           C\\nANISOU  814  C   LYS A 149     9627  14634   9529    289    781  -3067       C\\nATOM    815  O   LYS A 149       3.943  19.488  18.470  1.00 93.01           O\\nANISOU  815  O   LYS A 149    10125  14862  10350    308    742  -2887       O\\nATOM    816  CB  LYS A 149       2.585  18.670  21.333  1.00 79.97           C\\nANISOU  816  CB  LYS A 149     8188  14678   7518   -142   1299  -3315       C\\nATOM    817  N   ARG A 150       4.688  20.778  20.160  1.00 87.49           N\\nANISOU  817  N   ARG A 150     9416  14340   9487    578    575  -3405       N\\nATOM    818  CA  ARG A 150       5.060  21.865  19.261  1.00 81.69           C\\nANISOU  818  CA  ARG A 150     8671  13071   9295    893    273  -3505       C\\nATOM    819  C   ARG A 150       6.223  21.474  18.359  1.00 80.21           C\\nANISOU  819  C   ARG A 150     8786  12341   9349    799    130  -2998       C\\nATOM    820  O   ARG A 150       6.317  21.964  17.230  1.00 82.46           O\\nANISOU  820  O   ARG A 150     9071  12222  10039    928    -38  -2909       O\\nATOM    821  CB  ARG A 150       5.411  23.117  20.063  1.00 80.33           C\\nANISOU  821  CB  ARG A 150     8437  12868   9215   1187     52  -3965       C\\nATOM    822  N   ARG A 151       7.111  20.595  18.831  1.00 78.36           N\\nANISOU  822  N   ARG A 151     8802  12110   8862    578    185  -2672       N\\nATOM    823  CA  ARG A 151       8.234  20.166  18.003  1.00 72.71           C\\nANISOU  823  CA  ARG A 151     8328  10937   8361    507     62  -2239       C\\nATOM    824  C   ARG A 151       7.780  19.202  16.916  1.00 79.91           C\\nANISOU  824  C   ARG A 151     9266  11777   9319    342    198  -1915       C\\nATOM    825  O   ARG A 151       8.310  19.226  15.799  1.00 80.42           O\\nANISOU  825  O   ARG A 151     9410  11464   9683    376     87  -1687       O\\nATOM    826  CB  ARG A 151       9.319  19.528  18.870  1.00 74.01           C\\nANISOU  826  CB  ARG A 151     8732  11123   8264    367     34  -2034       C\\nATOM    827  CG  ARG A 151      10.576  19.134  18.110  1.00 82.30           C\\nANISOU  827  CG  ARG A 151     9986  11745   9540    333   -108  -1658       C\\nATOM    828  CD  ARG A 151      11.637  18.577  19.045  1.00 87.06           C\\nANISOU  828  CD  ARG A 151    10798  12374   9905    242   -184  -1509       C\\nATOM    829  NE  ARG A 151      11.097  17.537  19.917  1.00 91.56           N\\nANISOU  829  NE  ARG A 151    11463  13317  10010     18     -7  -1413       N\\nATOM    830  CZ  ARG A 151      11.047  16.249  19.600  1.00 88.57           C\\nANISOU  830  CZ  ARG A 151    11241  12910   9500   -194     83  -1059       C\\nATOM    831  NH1 ARG A 151      10.538  15.370  20.453  1.00 83.32           N\\nANISOU  831  NH1 ARG A 151    10680  12574   8402   -440    216   -953       N\\nATOM    832  NH2 ARG A 151      11.506  15.837  18.428  1.00 87.56           N\\nANISOU  832  NH2 ARG A 151    11174  12429   9667   -175     27   -816       N\\nATOM    833  N   VAL A 152       6.797  18.350  17.218  1.00 81.56           N\\nANISOU  833  N   VAL A 152     9402  12365   9221    140    437  -1897       N\\nATOM    834  CA  VAL A 152       6.288  17.429  16.204  1.00 81.36           C\\nANISOU  834  CA  VAL A 152     9394  12272   9245    -25    549  -1623       C\\nATOM    835  C   VAL A 152       5.564  18.196  15.104  1.00 80.65           C\\nANISOU  835  C   VAL A 152     9093  12045   9504    168    481  -1785       C\\nATOM    836  O   VAL A 152       5.709  17.888  13.915  1.00 78.73           O\\nANISOU  836  O   VAL A 152     8921  11517   9474    149    431  -1543       O\\nATOM    837  CB  VAL A 152       5.377  16.364  16.843  1.00 80.98           C\\nANISOU  837  CB  VAL A 152     9312  12669   8787   -333    803  -1562       C\\nATOM    838  CG1 VAL A 152       5.106  15.241  15.863  1.00 82.24           C\\nANISOU  838  CG1 VAL A 152     9570  12682   8997   -541    871  -1224       C\\nATOM    839  CG2 VAL A 152       6.004  15.810  18.104  1.00 83.35           C\\nANISOU  839  CG2 VAL A 152     9819  13145   8703   -511    831  -1443       C\\nATOM    840  N   THR A 153       4.781  19.211  15.482  1.00 84.22           N\\nANISOU  840  N   THR A 153     9285  12700  10015    371    455  -2213       N\\nATOM    841  CA  THR A 153       4.057  20.004  14.492  1.00 78.54           C\\nANISOU  841  CA  THR A 153     8369  11830   9642    587    332  -2387       C\\nATOM    842  C   THR A 153       5.011  20.696  13.525  1.00 75.61           C\\nANISOU  842  C   THR A 153     8160  10910   9657    737     57  -2208       C\\nATOM    843  O   THR A 153       4.738  20.779  12.322  1.00 76.21           O\\nANISOU  843  O   THR A 153     8221  10766   9967    773    -25  -2073       O\\nATOM    844  CB  THR A 153       3.168  21.031  15.195  1.00 80.46           C\\nANISOU  844  CB  THR A 153     8306  12365   9901    832    300  -2933       C\\nATOM    845  OG1 THR A 153       2.144  20.354  15.937  1.00 82.11           O\\nANISOU  845  OG1 THR A 153     8305  13162   9733    652    595  -3096       O\\nATOM    846  CG2 THR A 153       2.527  21.976  14.186  1.00 77.79           C\\nANISOU  846  CG2 THR A 153     7796  11785   9977   1109     80  -3121       C\\nATOM    847  N   VAL A 154       6.141  21.193  14.030  1.00 73.65           N\\nANISOU  847  N   VAL A 154     8065  10459   9460    799    -90  -2194       N\\nATOM    848  CA  VAL A 154       7.112  21.843  13.156  1.00 71.40           C\\nANISOU  848  CA  VAL A 154     7922   9692   9516    880   -337  -2000       C\\nATOM    849  C   VAL A 154       7.787  20.821  12.246  1.00 67.73           C\\nANISOU  849  C   VAL A 154     7638   9069   9028    675   -255  -1548       C\\nATOM    850  O   VAL A 154       8.007  21.079  11.057  1.00 61.81           O\\nANISOU  850  O   VAL A 154     6927   8041   8515    690   -370  -1361       O\\nATOM    851  CB  VAL A 154       8.137  22.627  13.993  1.00 65.37           C\\nANISOU  851  CB  VAL A 154     7244   8781   8811    974   -518  -2127       C\\nATOM    852  CG1 VAL A 154       9.256  23.154  13.108  1.00 56.93           C\\nANISOU  852  CG1 VAL A 154     6321   7254   8055    968   -742  -1864       C\\nATOM    853  CG2 VAL A 154       7.453  23.767  14.722  1.00 60.75           C\\nANISOU  853  CG2 VAL A 154     6475   8294   8312   1228   -654  -2627       C\\nATOM    854  N   MET A 155       8.122  19.645  12.784  1.00 69.04           N\\nANISOU  854  N   MET A 155     7921   9413   8899    483    -75  -1374       N\\nATOM    855  CA  MET A 155       8.784  18.630  11.972  1.00 68.64           C\\nANISOU  855  CA  MET A 155     8035   9207   8837    329    -24  -1003       C\\nATOM    856  C   MET A 155       7.875  18.134  10.856  1.00 64.55           C\\nANISOU  856  C   MET A 155     7452   8706   8368    269     63   -905       C\\nATOM    857  O   MET A 155       8.316  17.979   9.712  1.00 59.62           O\\nANISOU  857  O   MET A 155     6898   7863   7894    252      8   -690       O\\nATOM    858  CB  MET A 155       9.241  17.467  12.851  1.00 72.37           C\\nANISOU  858  CB  MET A 155     8663   9833   9001    158     94   -859       C\\nATOM    859  CG  MET A 155      10.407  17.803  13.768  1.00 80.64           C\\nANISOU  859  CG  MET A 155     9815  10814  10011    208    -29   -884       C\\nATOM    860  SD  MET A 155      11.031  16.373  14.674  1.00 89.65           S\\nANISOU  860  SD  MET A 155    11184  12069  10810     19     37   -657       S\\nATOM    861  CE  MET A 155      12.405  17.110  15.553  1.00 99.07           C\\nANISOU  861  CE  MET A 155    12443  13153  12047    140   -171   -742       C\\nATOM    862  N   ILE A 156       6.602  17.886  11.166  1.00 67.34           N\\nANISOU  862  N   ILE A 156     7652   9352   8582    227    200  -1075       N\\nATOM    863  CA  ILE A 156       5.685  17.372  10.156  1.00 68.91           C\\nANISOU  863  CA  ILE A 156     7773   9590   8821    157    271  -1001       C\\nATOM    864  C   ILE A 156       5.469  18.403   9.059  1.00 69.08           C\\nANISOU  864  C   ILE A 156     7705   9384   9158    345     81  -1053       C\\nATOM    865  O   ILE A 156       5.484  18.072   7.867  1.00 70.31           O\\nANISOU  865  O   ILE A 156     7916   9392   9407    300     52   -852       O\\nATOM    866  CB  ILE A 156       4.357  16.945  10.806  1.00 70.36           C\\nANISOU  866  CB  ILE A 156     7765  10184   8786     48    458  -1197       C\\nATOM    867  CG1 ILE A 156       4.590  15.773  11.761  1.00 67.02           C\\nANISOU  867  CG1 ILE A 156     7488   9956   8020   -215    628  -1044       C\\nATOM    868  CG2 ILE A 156       3.332  16.571   9.742  1.00 64.85           C\\nANISOU  868  CG2 ILE A 156     6940   9528   8171     -3    496  -1169       C\\nATOM    869  CD1 ILE A 156       3.333  15.249  12.401  1.00 60.59           C\\nANISOU  869  CD1 ILE A 156     6493   9587   6942   -411    838  -1180       C\\nATOM    870  N   SER A 157       5.271  19.668   9.439  1.00 67.59           N\\nANISOU  870  N   SER A 157     7393   9155   9133    558    -76  -1325       N\\nATOM    871  CA  SER A 157       5.081  20.719   8.446  1.00 66.91           C\\nANISOU  871  CA  SER A 157     7261   8799   9364    734   -321  -1352       C\\nATOM    872  C   SER A 157       6.261  20.789   7.488  1.00 65.20           C\\nANISOU  872  C   SER A 157     7252   8247   9275    664   -437  -1006       C\\nATOM    873  O   SER A 157       6.079  20.905   6.271  1.00 70.97           O\\nANISOU  873  O   SER A 157     8005   8831  10130    658   -531   -845       O\\nATOM    874  CB  SER A 157       4.876  22.064   9.138  1.00 53.19           C\\nANISOU  874  CB  SER A 157     5403   7001   7805    983   -525  -1706       C\\nATOM    875  OG  SER A 157       3.770  22.013  10.019  1.00 59.25           O\\nANISOU  875  OG  SER A 157     5930   8154   8428   1059   -395  -2076       O\\nATOM    876  N   ILE A 158       7.481  20.701   8.019  1.00 63.38           N\\nANISOU  876  N   ILE A 158     7159   7930   8993    600   -428   -895       N\\nATOM    877  CA  ILE A 158       8.662  20.757   7.168  1.00 62.29           C\\nANISOU  877  CA  ILE A 158     7167   7544   8955    516   -512   -595       C\\nATOM    878  C   ILE A 158       8.684  19.577   6.207  1.00 66.42           C\\nANISOU  878  C   ILE A 158     7754   8134   9350    369   -356   -352       C\\nATOM    879  O   ILE A 158       9.069  19.717   5.042  1.00 76.92           O\\nANISOU  879  O   ILE A 158     9134   9324  10767    323   -426   -148       O\\nATOM    880  CB  ILE A 158       9.935  20.815   8.030  1.00 62.52           C\\nANISOU  880  CB  ILE A 158     7286   7519   8948    483   -529   -568       C\\nATOM    881  CG1 ILE A 158       9.969  22.114   8.833  1.00 61.54           C\\nANISOU  881  CG1 ILE A 158     7112   7280   8990    635   -734   -823       C\\nATOM    882  CG2 ILE A 158      11.177  20.683   7.165  1.00 56.51           C\\nANISOU  882  CG2 ILE A 158     6625   6594   8253    369   -564   -273       C\\nATOM    883  CD1 ILE A 158      11.102  22.178   9.819  1.00 68.44           C\\nANISOU  883  CD1 ILE A 158     8055   8136   9811    610   -764   -846       C\\nATOM    884  N   VAL A 159       8.260  18.399   6.670  1.00 61.58           N\\nANISOU  884  N   VAL A 159     7145   7737   8515    280   -157   -371       N\\nATOM    885  CA  VAL A 159       8.270  17.217   5.808  1.00 61.95           C\\nANISOU  885  CA  VAL A 159     7267   7816   8456    152    -40   -177       C\\nATOM    886  C   VAL A 159       7.403  17.448   4.578  1.00 58.47           C\\nANISOU  886  C   VAL A 159     6754   7353   8111    173    -97   -152       C\\nATOM    887  O   VAL A 159       7.847  17.270   3.437  1.00 64.62           O\\nANISOU  887  O   VAL A 159     7599   8038   8915    129   -128     32       O\\nATOM    888  CB  VAL A 159       7.811  15.973   6.589  1.00 61.71           C\\nANISOU  888  CB  VAL A 159     7270   7984   8194     28    136   -202       C\\nATOM    889  CG1 VAL A 159       7.571  14.812   5.641  1.00 58.85           C\\nANISOU  889  CG1 VAL A 159     6974   7622   7763    -90    212    -53       C\\nATOM    890  CG2 VAL A 159       8.840  15.593   7.634  1.00 64.69           C\\nANISOU  890  CG2 VAL A 159     7772   8351   8457     -6    154   -157       C\\nATOM    891  N   TRP A 160       6.156  17.865   4.792  1.00 55.67           N\\nANISOU  891  N   TRP A 160     6244   7112   7797    249   -122   -357       N\\nATOM    892  CA  TRP A 160       5.209  17.964   3.688  1.00 61.87           C\\nANISOU  892  CA  TRP A 160     6946   7902   8658    275   -191   -352       C\\nATOM    893  C   TRP A 160       5.414  19.222   2.854  1.00 68.14           C\\nANISOU  893  C   TRP A 160     7758   8458   9675    394   -447   -287       C\\nATOM    894  O   TRP A 160       5.155  19.201   1.645  1.00 72.46           O\\nANISOU  894  O   TRP A 160     8331   8951  10250    369   -527   -148       O\\nATOM    895  CB  TRP A 160       3.778  17.893   4.226  1.00 54.20           C\\nANISOU  895  CB  TRP A 160     5762   7176   7654    313   -130   -618       C\\nATOM    896  CG  TRP A 160       3.447  16.528   4.729  1.00 59.47           C\\nANISOU  896  CG  TRP A 160     6436   8074   8087    111    106   -599       C\\nATOM    897  CD1 TRP A 160       3.428  16.111   6.027  1.00 64.43           C\\nANISOU  897  CD1 TRP A 160     7047   8894   8538     21    258   -694       C\\nATOM    898  CD2 TRP A 160       3.129  15.380   3.933  1.00 65.48           C\\nANISOU  898  CD2 TRP A 160     7253   8873   8755    -53    190   -456       C\\nATOM    899  NE1 TRP A 160       3.105  14.776   6.089  1.00 64.83           N\\nANISOU  899  NE1 TRP A 160     7153   9080   8400   -211    420   -586       N\\nATOM    900  CE2 TRP A 160       2.917  14.305   4.817  1.00 67.13           C\\nANISOU  900  CE2 TRP A 160     7487   9263   8758   -251    374   -455       C\\nATOM    901  CE3 TRP A 160       2.997  15.161   2.558  1.00 66.76           C\\nANISOU  901  CE3 TRP A 160     7455   8935   8975    -62    110   -331       C\\nATOM    902  CZ2 TRP A 160       2.575  13.030   4.371  1.00 70.04           C\\nANISOU  902  CZ2 TRP A 160     7926   9666   9019   -454    457   -337       C\\nATOM    903  CZ3 TRP A 160       2.659  13.895   2.117  1.00 69.12           C\\nANISOU  903  CZ3 TRP A 160     7807   9302   9154   -239    209   -252       C\\nATOM    904  CH2 TRP A 160       2.451  12.846   3.021  1.00 68.25           C\\nANISOU  904  CH2 TRP A 160     7727   9325   8880   -431    370   -257       C\\nATOM    905  N   VAL A 161       5.874  20.317   3.463  1.00 67.95           N\\nANISOU  905  N   VAL A 161     7737   8280   9802    507   -599   -373       N\\nATOM    906  CA  VAL A 161       6.140  21.520   2.680  1.00 69.19           C\\nANISOU  906  CA  VAL A 161     7952   8155  10182    576   -883   -262       C\\nATOM    907  C   VAL A 161       7.379  21.323   1.823  1.00 65.64           C\\nANISOU  907  C   VAL A 161     7665   7597   9678    402   -867     76       C\\nATOM    908  O   VAL A 161       7.447  21.799   0.684  1.00 71.00           O\\nANISOU  908  O   VAL A 161     8411   8144  10420    354  -1023    278       O\\nATOM    909  CB  VAL A 161       6.273  22.747   3.599  1.00 68.92           C\\nANISOU  909  CB  VAL A 161     7883   7953  10351    740  -1087   -473       C\\nATOM    910  CG1 VAL A 161       6.754  23.958   2.810  1.00 55.10           C\\nANISOU  910  CG1 VAL A 161     6251   5845   8841    751  -1414   -291       C\\nATOM    911  CG2 VAL A 161       4.941  23.041   4.271  1.00 68.37           C\\nANISOU  911  CG2 VAL A 161     7604   8033  10340    947  -1123   -858       C\\nATOM    912  N   LEU A 162       8.370  20.607   2.346  1.00 57.34           N\\nANISOU  912  N   LEU A 162     6669   6627   8492    302   -683    137       N\\nATOM    913  CA  LEU A 162       9.567  20.343   1.562  1.00 62.34           C\\nANISOU  913  CA  LEU A 162     7399   7226   9060    152   -640    403       C\\nATOM    914  C   LEU A 162       9.274  19.375   0.424  1.00 64.44           C\\nANISOU  914  C   LEU A 162     7686   7633   9165     68   -521    527       C\\nATOM    915  O   LEU A 162       9.756  19.565  -0.698  1.00 73.70           O\\nANISOU  915  O   LEU A 162     8910   8787  10307    -32   -568    735       O\\nATOM    916  CB  LEU A 162      10.668  19.803   2.467  1.00 66.33           C\\nANISOU  916  CB  LEU A 162     7929   7786   9485    111   -507    389       C\\nATOM    917  CG  LEU A 162      12.083  19.741   1.909  1.00 71.44           C\\nANISOU  917  CG  LEU A 162     8616   8419  10108    -16   -484    596       C\\nATOM    918  CD1 LEU A 162      12.409  21.020   1.165  1.00 63.78           C\\nANISOU  918  CD1 LEU A 162     7665   7275   9293    -96   -691    765       C\\nATOM    919  CD2 LEU A 162      13.044  19.530   3.061  1.00 75.47           C\\nANISOU  919  CD2 LEU A 162     9125   8941  10610      0   -439    519       C\\nATOM    920  N   SER A 163       8.481  18.334   0.691  1.00 62.39           N\\nANISOU  920  N   SER A 163     7390   7531   8786     86   -371    399       N\\nATOM    921  CA  SER A 163       8.099  17.410  -0.371  1.00 64.81           C\\nANISOU  921  CA  SER A 163     7718   7951   8957     15   -289    475       C\\nATOM    922  C   SER A 163       7.384  18.143  -1.499  1.00 65.90           C\\nANISOU  922  C   SER A 163     7840   8039   9160     33   -467    552       C\\nATOM    923  O   SER A 163       7.634  17.874  -2.680  1.00 71.94           O\\nANISOU  923  O   SER A 163     8662   8855   9817    -51   -466    710       O\\nATOM    924  CB  SER A 163       7.213  16.302   0.193  1.00 64.78           C\\nANISOU  924  CB  SER A 163     7674   8087   8852      4   -146    321       C\\nATOM    925  OG  SER A 163       7.785  15.740   1.357  1.00 61.15           O\\nANISOU  925  OG  SER A 163     7254   7650   8329    -18    -31    269       O\\nATOM    926  N   PHE A 164       6.497  19.078  -1.153  1.00 60.59           N\\nANISOU  926  N   PHE A 164     7089   7277   8655    156   -639    427       N\\nATOM    927  CA  PHE A 164       5.825  19.887  -2.164  1.00 61.72           C\\nANISOU  927  CA  PHE A 164     7234   7322   8893    201   -880    505       C\\nATOM    928  C   PHE A 164       6.833  20.691  -2.972  1.00 65.16           C\\nANISOU  928  C   PHE A 164     7806   7601   9350     94  -1027    793       C\\nATOM    929  O   PHE A 164       6.879  20.597  -4.203  1.00 65.92           O\\nANISOU  929  O   PHE A 164     7974   7746   9327    -10  -1074    992       O\\nATOM    930  CB  PHE A 164       4.803  20.813  -1.496  1.00 57.42           C\\nANISOU  930  CB  PHE A 164     6564   6683   8568    400  -1076    267       C\\nATOM    931  CG  PHE A 164       4.135  21.779  -2.443  1.00 61.42           C\\nANISOU  931  CG  PHE A 164     7089   7023   9226    488  -1405    340       C\\nATOM    932  CD1 PHE A 164       3.067  21.374  -3.232  1.00 63.79           C\\nANISOU  932  CD1 PHE A 164     7317   7446   9476    519  -1453    302       C\\nATOM    933  CD2 PHE A 164       4.563  23.097  -2.528  1.00 60.79           C\\nANISOU  933  CD2 PHE A 164     7109   6640   9350    534  -1703    451       C\\nATOM    934  CE1 PHE A 164       2.450  22.259  -4.099  1.00 64.22           C\\nANISOU  934  CE1 PHE A 164     7400   7336   9667    615  -1799    378       C\\nATOM    935  CE2 PHE A 164       3.946  23.988  -3.393  1.00 65.28           C\\nANISOU  935  CE2 PHE A 164     7729   7008  10065    614  -2062    545       C\\nATOM    936  CZ  PHE A 164       2.889  23.566  -4.178  1.00 64.54           C\\nANISOU  936  CZ  PHE A 164     7564   7051   9906    666  -2113    510       C\\nATOM    937  N   THR A 165       7.667  21.477  -2.285  1.00 60.91           N\\nANISOU  937  N   THR A 165     7302   6899   8944     90  -1100    820       N\\nATOM    938  CA  THR A 165       8.590  22.366  -2.984  1.00 68.08           C\\nANISOU  938  CA  THR A 165     8326   7648   9893    -59  -1264   1109       C\\nATOM    939  C   THR A 165       9.585  21.592  -3.836  1.00 67.06           C\\nANISOU  939  C   THR A 165     8237   7731   9511   -266  -1055   1321       C\\nATOM    940  O   THR A 165      10.068  22.114  -4.846  1.00 74.56           O\\nANISOU  940  O   THR A 165     9269   8666  10395   -439  -1158   1596       O\\nATOM    941  CB  THR A 165       9.335  23.256  -1.988  1.00 72.21           C\\nANISOU  941  CB  THR A 165     8862   7963  10613    -43  -1373   1067       C\\nATOM    942  OG1 THR A 165      10.064  22.439  -1.068  1.00 84.36           O\\nANISOU  942  OG1 THR A 165    10343   9656  12055    -52  -1111    946       O\\nATOM    943  CG2 THR A 165       8.362  24.133  -1.215  1.00 69.54           C\\nANISOU  943  CG2 THR A 165     8475   7415  10531    191  -1616    813       C\\nATOM    944  N   ILE A 166       9.898  20.352  -3.455  1.00 69.64           N\\nANISOU  944  N   ILE A 166     8506   8267   9687   -255   -775   1193       N\\nATOM    945  CA  ILE A 166      10.825  19.548  -4.247  1.00 72.15           C\\nANISOU  945  CA  ILE A 166     8831   8805   9778   -397   -585   1317       C\\nATOM    946  C   ILE A 166      10.150  19.043  -5.520  1.00 72.60           C\\nANISOU  946  C   ILE A 166     8918   9016   9653   -435   -578   1379       C\\nATOM    947  O   ILE A 166      10.751  19.045  -6.601  1.00 74.34           O\\nANISOU  947  O   ILE A 166     9167   9388   9690   -588   -548   1564       O\\nATOM    948  CB  ILE A 166      11.383  18.389  -3.402  1.00 64.44           C\\nANISOU  948  CB  ILE A 166     7804   7945   8737   -337   -355   1141       C\\nATOM    949  CG1 ILE A 166      12.401  18.911  -2.386  1.00 65.09           C\\nANISOU  949  CG1 ILE A 166     7859   7927   8946   -345   -368   1133       C\\nATOM    950  CG2 ILE A 166      12.008  17.326  -4.294  1.00 61.90           C\\nANISOU  950  CG2 ILE A 166     7469   7861   8189   -405   -177   1168       C\\nATOM    951  CD1 ILE A 166      12.979  17.825  -1.505  1.00 55.41           C\\nANISOU  951  CD1 ILE A 166     6604   6788   7663   -276   -195    979       C\\nATOM    952  N   SER A 167       8.896  18.605  -5.414  1.00 66.08           N\\nANISOU  952  N   SER A 167     8070   8185   8852   -311   -603   1216       N\\nATOM    953  CA  SER A 167       8.168  18.066  -6.554  1.00 69.77           C\\nANISOU  953  CA  SER A 167     8557   8794   9156   -335   -616   1237       C\\nATOM    954  C   SER A 167       7.500  19.138  -7.404  1.00 70.97           C\\nANISOU  954  C   SER A 167     8769   8841   9355   -354   -900   1407       C\\nATOM    955  O   SER A 167       7.132  18.860  -8.553  1.00 69.63           O\\nANISOU  955  O   SER A 167     8642   8809   9005   -415   -942   1493       O\\nATOM    956  CB  SER A 167       7.104  17.078  -6.070  1.00 67.68           C\\nANISOU  956  CB  SER A 167     8226   8582   8907   -228   -531    989       C\\nATOM    957  OG  SER A 167       6.153  17.737  -5.251  1.00 68.82           O\\nANISOU  957  OG  SER A 167     8295   8591   9261   -104   -663    859       O\\nATOM    958  N   CYS A 168       7.324  20.345  -6.871  1.00 72.75           N\\nANISOU  958  N   CYS A 168     9009   8812   9819   -293  -1126   1446       N\\nATOM    959  CA  CYS A 168       6.648  21.393  -7.631  1.00 73.51           C\\nANISOU  959  CA  CYS A 168     9186   8743  10001   -284  -1466   1607       C\\nATOM    960  C   CYS A 168       7.347  21.747  -8.942  1.00 77.62           C\\nANISOU  960  C   CYS A 168     9848   9341  10301   -524  -1540   1966       C\\nATOM    961  O   CYS A 168       6.638  22.045  -9.918  1.00 81.68           O\\nANISOU  961  O   CYS A 168    10442   9849  10744   -540  -1760   2098       O\\nATOM    962  CB  CYS A 168       6.478  22.640  -6.754  1.00 74.94           C\\nANISOU  962  CB  CYS A 168     9371   8593  10510   -158  -1727   1556       C\\nATOM    963  SG  CYS A 168       5.411  23.906  -7.472  1.00 83.98           S\\nANISOU  963  SG  CYS A 168    10608   9450  11852    -51  -2231   1669       S\\nATOM    964  N   PRO A 169       8.683  21.755  -9.044  1.00 78.38           N\\nANISOU  964  N   PRO A 169     9970   9541  10269   -727  -1380   2136       N\\nATOM    965  CA  PRO A 169       9.296  22.005 -10.360  1.00 83.73           C\\nANISOU  965  CA  PRO A 169    10752  10394  10669   -996  -1410   2471       C\\nATOM    966  C   PRO A 169       8.894  21.001 -11.428  1.00 84.95           C\\nANISOU  966  C   PRO A 169    10900  10878  10501  -1015  -1280   2429       C\\nATOM    967  O   PRO A 169       8.857  21.362 -12.611  1.00 84.19           O\\nANISOU  967  O   PRO A 169    10915  10894  10178  -1189  -1413   2692       O\\nATOM    968  CB  PRO A 169      10.799  21.935 -10.063  1.00 82.55           C\\nANISOU  968  CB  PRO A 169    10540  10383  10443  -1178  -1179   2547       C\\nATOM    969  CG  PRO A 169      10.912  22.332  -8.645  1.00 76.42           C\\nANISOU  969  CG  PRO A 169     9712   9325   9998  -1032  -1220   2380       C\\nATOM    970  CD  PRO A 169       9.698  21.762  -7.973  1.00 74.69           C\\nANISOU  970  CD  PRO A 169     9435   9030   9916   -740  -1219   2057       C\\nATOM    971  N   LEU A 170       8.584  19.755 -11.051  1.00 79.08           N\\nANISOU  971  N   LEU A 170    10044  10281   9723   -856  -1047   2113       N\\nATOM    972  CA  LEU A 170       8.270  18.731 -12.044  1.00 73.43           C\\nANISOU  972  CA  LEU A 170     9322   9863   8714   -871   -932   2033       C\\nATOM    973  C   LEU A 170       7.035  19.090 -12.860  1.00 76.56           C\\nANISOU  973  C   LEU A 170     9801  10208   9081   -835  -1215   2109       C\\nATOM    974  O   LEU A 170       6.917  18.677 -14.020  1.00 77.86           O\\nANISOU  974  O   LEU A 170    10015  10626   8942   -927  -1211   2171       O\\nATOM    975  CB  LEU A 170       8.080  17.380 -11.356  1.00 67.28           C\\nANISOU  975  CB  LEU A 170     8435   9155   7972   -710   -697   1684       C\\nATOM    976  CG  LEU A 170       9.176  16.975 -10.366  1.00 66.79           C\\nANISOU  976  CG  LEU A 170     8297   9091   7988   -692   -470   1577       C\\nATOM    977  CD1 LEU A 170       8.737  15.773  -9.563  1.00 66.74           C\\nANISOU  977  CD1 LEU A 170     8235   9057   8068   -536   -332   1276       C\\nATOM    978  CD2 LEU A 170      10.488  16.689 -11.074  1.00 61.58           C\\nANISOU  978  CD2 LEU A 170     7607   8724   7065   -840   -287   1659       C\\nATOM    979  N   LEU A 171       6.108  19.856 -12.280  1.00 72.91           N\\nANISOU  979  N   LEU A 171     9340   9439   8925   -685  -1477   2076       N\\nATOM    980  CA  LEU A 171       4.945  20.322 -13.024  1.00 75.80           C\\nANISOU  980  CA  LEU A 171     9768   9727   9306   -622  -1806   2146       C\\nATOM    981  C   LEU A 171       5.311  21.339 -14.094  1.00 79.71           C\\nANISOU  981  C   LEU A 171    10460  10190   9637   -830  -2066   2561       C\\nATOM    982  O   LEU A 171       4.541  21.531 -15.041  1.00 84.88           O\\nANISOU  982  O   LEU A 171    11203  10874  10173   -833  -2320   2673       O\\nATOM    983  CB  LEU A 171       3.917  20.942 -12.075  1.00 74.05           C\\nANISOU  983  CB  LEU A 171     9460   9199   9478   -376  -2034   1961       C\\nATOM    984  CG  LEU A 171       2.918  20.015 -11.385  1.00 69.74           C\\nANISOU  984  CG  LEU A 171     8717   8733   9050   -185  -1900   1574       C\\nATOM    985  CD1 LEU A 171       2.056  20.807 -10.416  1.00 68.86           C\\nANISOU  985  CD1 LEU A 171     8486   8373   9305     44  -2112   1385       C\\nATOM    986  CD2 LEU A 171       2.059  19.311 -12.420  1.00 65.45           C\\nANISOU  986  CD2 LEU A 171     8160   8395   8313   -188  -1959   1520       C\\nATOM    987  N   PHE A 172       6.460  21.995 -13.967  1.00 68.04           N\\nANISOU  987  N   PHE A 172     9054   8656   8140  -1028  -2027   2807       N\\nATOM    988  CA  PHE A 172       6.795  23.074 -14.882  1.00 78.77           C\\nANISOU  988  CA  PHE A 172    10620   9942   9366  -1280  -2310   3252       C\\nATOM    989  C   PHE A 172       8.096  22.777 -15.619  1.00 85.91           C\\nANISOU  989  C   PHE A 172    11542  11237   9862  -1615  -2028   3473       C\\nATOM    990  O   PHE A 172       9.011  23.607 -15.641  1.00 88.20           O\\nANISOU  990  O   PHE A 172    11911  11460  10141  -1873  -2078   3779       O\\nATOM    991  CB  PHE A 172       6.876  24.399 -14.118  1.00 84.73           C\\nANISOU  991  CB  PHE A 172    11461  10224  10509  -1254  -2621   3391       C\\nATOM    992  CG  PHE A 172       5.617  24.738 -13.360  1.00 85.93           C\\nANISOU  992  CG  PHE A 172    11551  10035  11063   -893  -2895   3113       C\\nATOM    993  CD1 PHE A 172       4.602  25.461 -13.964  1.00 86.94           C\\nANISOU  993  CD1 PHE A 172    11803   9937  11293   -793  -3356   3232       C\\nATOM    994  CD2 PHE A 172       5.447  24.323 -12.046  1.00 83.56           C\\nANISOU  994  CD2 PHE A 172    11054   9673  11022   -654  -2699   2721       C\\nATOM    995  CE1 PHE A 172       3.443  25.769 -13.275  1.00 83.30           C\\nANISOU  995  CE1 PHE A 172    11232   9212  11208   -436  -3605   2923       C\\nATOM    996  CE2 PHE A 172       4.288  24.629 -11.350  1.00 82.96           C\\nANISOU  996  CE2 PHE A 172    10876   9366  11280   -334  -2919   2431       C\\nATOM    997  CZ  PHE A 172       3.286  25.353 -11.967  1.00 83.10           C\\nANISOU  997  CZ  PHE A 172    10978   9179  11417   -212  -3367   2511       C\\nATOM    998  N   GLY A 173       8.179  21.592 -16.224  1.00 92.00           N\\nANISOU  998  N   GLY A 173    12224  12431  10302  -1618  -1741   3296       N\\nATOM    999  CA  GLY A 173       9.333  21.223 -17.023  1.00 99.29           C\\nANISOU  999  CA  GLY A 173    13120  13810  10797  -1900  -1463   3431       C\\nATOM   1000  C   GLY A 173      10.629  21.114 -16.255  1.00105.40           C\\nANISOU 1000  C   GLY A 173    13746  14661  11642  -1983  -1167   3370       C\\nATOM   1001  O   GLY A 173      11.703  21.225 -16.853  1.00109.34           O\\nANISOU 1001  O   GLY A 173    14209  15498  11836  -2275   -998   3563       O\\nATOM   1002  N   LEU A 174      10.558  20.899 -14.940  1.00100.46           N\\nANISOU 1002  N   LEU A 174    13015  13761  11393  -1742  -1102   3100       N\\nATOM   1003  CA  LEU A 174      11.734  20.873 -14.068  1.00103.35           C\\nANISOU 1003  CA  LEU A 174    13246  14141  11880  -1788   -879   3034       C\\nATOM   1004  C   LEU A 174      12.539  22.163 -14.183  1.00110.64           C\\nANISOU 1004  C   LEU A 174    14250  14960  12828  -2107  -1028   3434       C\\nATOM   1005  O   LEU A 174      13.746  22.179 -13.930  1.00113.38           O\\nANISOU 1005  O   LEU A 174    14470  15481  13128  -2273   -823   3467       O\\nATOM   1006  CB  LEU A 174      12.615  19.654 -14.361  1.00 97.67           C\\nANISOU 1006  CB  LEU A 174    12350  13885  10875  -1796   -492   2806       C\\nATOM   1007  CG  LEU A 174      13.534  19.118 -13.264  1.00 92.37           C\\nANISOU 1007  CG  LEU A 174    11502  13215  10381  -1682   -254   2560       C\\nATOM   1008  CD1 LEU A 174      12.928  19.339 -11.890  1.00 88.80           C\\nANISOU 1008  CD1 LEU A 174    11078  12307  10354  -1450   -387   2419       C\\nATOM   1009  CD2 LEU A 174      13.792  17.638 -13.505  1.00 90.06           C\\nANISOU 1009  CD2 LEU A 174    11076  13252   9891  -1525     22   2210       C\\nATOM   1010  N   ASN A 175      11.863  23.254 -14.556  1.00127.08           N\\nANISOU 1010  N   ASN A 175    16542  16739  15004  -2196  -1417   3738       N\\nATOM   1011  CA  ASN A 175      12.511  24.539 -14.814  1.00131.09           C\\nANISOU 1011  CA  ASN A 175    17185  17092  15530  -2547  -1637   4178       C\\nATOM   1012  C   ASN A 175      13.737  24.358 -15.706  1.00135.52           C\\nANISOU 1012  C   ASN A 175    17627  18169  15696  -2875  -1339   4267       C\\nATOM   1013  O   ASN A 175      14.777  24.991 -15.516  1.00141.49           O\\nANISOU 1013  O   ASN A 175    18317  18930  16514  -3096  -1295   4368       O\\nATOM   1014  CB  ASN A 175      12.876  25.244 -13.504  1.00127.19           C\\nANISOU 1014  CB  ASN A 175    16665  16177  15484  -2475  -1748   4122       C\\nATOM   1015  CG  ASN A 175      11.656  25.790 -12.774  1.00121.37           C\\nANISOU 1015  CG  ASN A 175    16035  14913  15169  -2144  -2109   3974       C\\nATOM   1016  OD1 ASN A 175      10.689  26.228 -13.400  1.00120.30           O\\nANISOU 1016  OD1 ASN A 175    16064  14605  15041  -2092  -2430   4105       O\\nATOM   1017  ND2 ASN A 175      11.697  25.764 -11.445  1.00115.08           N\\nANISOU 1017  ND2 ASN A 175    15127  13886  14713  -1906  -2061   3672       N\\nATOM   1018  N   ASN A 176      13.611  23.469 -16.686  1.00138.51           N\\nANISOU 1018  N   ASN A 176    17960  19005  15662  -2893  -1141   4194       N\\nATOM   1019  CA  ASN A 176      14.702  23.139 -17.593  1.00128.90           C\\nANISOU 1019  CA  ASN A 176    16590  18346  14041  -3148   -837   4194       C\\nATOM   1020  C   ASN A 176      14.143  23.135 -19.012  1.00130.29           C\\nANISOU 1020  C   ASN A 176    16893  18756  13854  -3256   -934   4312       C\\nATOM   1021  O   ASN A 176      13.054  23.656 -19.280  1.00128.25           O\\nANISOU 1021  O   ASN A 176    16856  18174  13701  -3186  -1280   4456       O\\nATOM   1022  CB  ASN A 176      15.347  21.804 -17.188  1.00114.40           C\\nANISOU 1022  CB  ASN A 176    14490  16909  12066  -3004   -416   3849       C\\nATOM   1023  N   ALA A 177      14.888  22.541 -19.940  1.00131.35           N\\nANISOU 1023  N   ALA A 177    16876  19466  13564  -3410   -639   4223       N\\nATOM   1024  CA  ALA A 177      14.518  22.512 -21.354  1.00133.06           C\\nANISOU 1024  CA  ALA A 177    17193  19978  13388  -3547   -695   4324       C\\nATOM   1025  C   ALA A 177      13.850  21.175 -21.665  1.00139.43           C\\nANISOU 1025  C   ALA A 177    17953  21060  13966  -3279   -543   3999       C\\nATOM   1026  O   ALA A 177      14.499  20.218 -22.087  1.00134.42           O\\nANISOU 1026  O   ALA A 177    17113  20932  13028  -3260   -210   3722       O\\nATOM   1027  CB  ALA A 177      15.744  22.740 -22.230  1.00132.82           C\\nANISOU 1027  CB  ALA A 177    17018  20431  13018  -3895   -487   4415       C\\nATOM   1028  N   ASP A 178      12.535  21.113 -21.456  1.00139.56           N\\nANISOU 1028  N   ASP A 178    18147  20737  14141  -3057   -814   4002       N\\nATOM   1029  CA  ASP A 178      11.738  19.985 -21.927  1.00140.00           C\\nANISOU 1029  CA  ASP A 178    18203  21034  13957  -2843   -761   3735       C\\nATOM   1030  C   ASP A 178      10.328  20.465 -22.235  1.00139.46           C\\nANISOU 1030  C   ASP A 178    18375  20618  13994  -2746  -1185   3897       C\\nATOM   1031  O   ASP A 178       9.372  20.082 -21.554  1.00142.64           O\\nANISOU 1031  O   ASP A 178    18808  20766  14622  -2479  -1336   3761       O\\nATOM   1032  CB  ASP A 178      11.711  18.857 -20.894  1.00137.06           C\\nANISOU 1032  CB  ASP A 178    17675  20675  13728  -2556   -547   3368       C\\nATOM   1033  N   GLN A 179      10.191  21.295 -23.270  1.00143.02           N\\nANISOU 1033  N   GLN A 179    18983  21074  14284  -2960  -1392   4178       N\\nATOM   1034  CA  GLN A 179       8.987  22.105 -23.424  1.00133.33           C\\nANISOU 1034  CA  GLN A 179    17987  19403  13269  -2879  -1859   4383       C\\nATOM   1035  C   GLN A 179       7.753  21.243 -23.675  1.00128.51           C\\nANISOU 1035  C   GLN A 179    17406  18844  12578  -2605  -1987   4153       C\\nATOM   1036  O   GLN A 179       6.787  21.279 -22.902  1.00124.40           O\\nANISOU 1036  O   GLN A 179    16911  17946  12410  -2345  -2237   4071       O\\nATOM   1037  CB  GLN A 179       9.188  23.117 -24.553  1.00132.56           C\\nANISOU 1037  CB  GLN A 179    18056  19342  12970  -3191  -2041   4737       C\\nATOM   1038  N   ASN A 180       7.766  20.455 -24.749  1.00126.77           N\\nANISOU 1038  N   ASN A 180    17160  19104  11903  -2656  -1831   4014       N\\nATOM   1039  CA  ASN A 180       6.565  19.780 -25.230  1.00115.92           C\\nANISOU 1039  CA  ASN A 180    15839  17790  10414  -2448  -2017   3825       C\\nATOM   1040  C   ASN A 180       6.535  18.292 -24.886  1.00111.57           C\\nANISOU 1040  C   ASN A 180    15109  17542   9741  -2253  -1745   3379       C\\nATOM   1041  O   ASN A 180       5.949  17.498 -25.625  1.00103.18           O\\nANISOU 1041  O   ASN A 180    14050  16740   8415  -2166  -1771   3154       O\\nATOM   1042  CB  ASN A 180       6.419  19.972 -26.739  1.00115.56           C\\nANISOU 1042  CB  ASN A 180    15926  18028   9952  -2620  -2110   3964       C\\nATOM   1043  N   GLU A 181       7.135  17.896 -23.764  1.00104.62           N\\nANISOU 1043  N   GLU A 181    14065  16578   9107  -2156  -1490   3195       N\\nATOM   1044  CA  GLU A 181       7.136  16.494 -23.369  1.00106.80           C\\nANISOU 1044  CA  GLU A 181    14149  16965   9465  -1902  -1204   2656       C\\nATOM   1045  C   GLU A 181       6.948  16.366 -21.867  1.00100.72           C\\nANISOU 1045  C   GLU A 181    13266  15721   9281  -1661  -1157   2456       C\\nATOM   1046  O   GLU A 181       7.211  17.295 -21.099  1.00102.83           O\\nANISOU 1046  O   GLU A 181    13557  15677   9838  -1708  -1233   2688       O\\nATOM   1047  CB  GLU A 181       8.426  15.780 -23.782  1.00111.20           C\\nANISOU 1047  CB  GLU A 181    14562  18052   9639  -2014   -799   2478       C\\nATOM   1048  CG  GLU A 181       8.455  15.363 -25.237  1.00118.18           C\\nANISOU 1048  CG  GLU A 181    15491  19499   9912  -2150   -768   2439       C\\nATOM   1049  CD  GLU A 181       9.558  14.373 -25.529  1.00125.80           C\\nANISOU 1049  CD  GLU A 181    16244  20936  10620  -2119   -359   2054       C\\nATOM   1050  OE1 GLU A 181       9.649  13.356 -24.809  1.00127.00           O\\nANISOU 1050  OE1 GLU A 181    16258  20997  10999  -1858   -200   1630       O\\nATOM   1051  OE2 GLU A 181      10.339  14.618 -26.473  1.00132.18           O\\nANISOU 1051  OE2 GLU A 181    16999  22090  11133  -2311   -210   2123       O\\nATOM   1052  N   CYS A 182       6.490  15.185 -21.461  1.00 85.77           N\\nANISOU 1052  N   CYS A 182    11262  13784   7544  -1421  -1042   2020       N\\nATOM   1053  CA  CYS A 182       6.326  14.886 -20.051  1.00 85.01           C\\nANISOU 1053  CA  CYS A 182    11057  13309   7934  -1219   -963   1809       C\\nATOM   1054  C   CYS A 182       7.659  15.034 -19.325  1.00 85.25           C\\nANISOU 1054  C   CYS A 182    10998  13354   8038  -1280   -699   1848       C\\nATOM   1055  O   CYS A 182       8.737  14.991 -19.927  1.00 87.66           O\\nANISOU 1055  O   CYS A 182    11266  14030   8011  -1441   -506   1910       O\\nATOM   1056  CB  CYS A 182       5.770  13.473 -19.864  1.00 85.07           C\\nANISOU 1056  CB  CYS A 182    10980  13320   8021  -1022   -869   1364       C\\nATOM   1057  SG  CYS A 182       5.430  13.056 -18.147  1.00 88.55           S\\nANISOU 1057  SG  CYS A 182    11313  13325   9006   -826   -793   1143       S\\nATOM   1058  N   ILE A 183       7.575  15.222 -18.009  1.00 86.69           N\\nANISOU 1058  N   ILE A 183    11127  13162   8650  -1153   -694   1796       N\\nATOM   1059  CA  ILE A 183       8.782  15.505 -17.243  1.00 88.06           C\\nANISOU 1059  CA  ILE A 183    11221  13307   8931  -1209   -498   1856       C\\nATOM   1060  C   ILE A 183       9.631  14.253 -17.070  1.00 90.76           C\\nANISOU 1060  C   ILE A 183    11430  13873   9183  -1113   -193   1518       C\\nATOM   1061  O   ILE A 183      10.856  14.349 -16.944  1.00 89.70           O\\nANISOU 1061  O   ILE A 183    11199  13916   8966  -1199     -1   1550       O\\nATOM   1062  CB  ILE A 183       8.428  16.141 -15.888  1.00 82.65           C\\nANISOU 1062  CB  ILE A 183    10529  12169   8706  -1098   -610   1893       C\\nATOM   1063  CG1 ILE A 183       9.689  16.703 -15.236  1.00 81.90           C\\nANISOU 1063  CG1 ILE A 183    10377  12044   8696  -1203   -475   2026       C\\nATOM   1064  CG2 ILE A 183       7.755  15.134 -14.972  1.00 80.02           C\\nANISOU 1064  CG2 ILE A 183    10121  11657   8626   -869   -543   1542       C\\nATOM   1065  CD1 ILE A 183      10.562  17.486 -16.201  1.00 77.13           C\\nANISOU 1065  CD1 ILE A 183     9815  11711   7778  -1501   -472   2363       C\\nATOM   1066  N   ILE A 184       9.020  13.066 -17.078  1.00 86.05           N\\nANISOU 1066  N   ILE A 184    10817  13266   8612   -938   -167   1182       N\\nATOM   1067  CA  ILE A 184       9.808  11.848 -16.945  1.00 81.50           C\\nANISOU 1067  CA  ILE A 184    10141  12849   7978   -818     61    843       C\\nATOM   1068  C   ILE A 184      10.649  11.603 -18.187  1.00 77.44           C\\nANISOU 1068  C   ILE A 184     9566  12848   7010   -918    205    786       C\\nATOM   1069  O   ILE A 184      11.589  10.802 -18.148  1.00 77.18           O\\nANISOU 1069  O   ILE A 184     9408  13014   6904   -822    403    514       O\\nATOM   1070  CB  ILE A 184       8.907  10.636 -16.645  1.00 80.64           C\\nANISOU 1070  CB  ILE A 184    10060  12549   8030   -635      7    515       C\\nATOM   1071  CG1 ILE A 184       9.694   9.574 -15.876  1.00 78.25           C\\nANISOU 1071  CG1 ILE A 184     9688  12171   7873   -478    168    222       C\\nATOM   1072  CG2 ILE A 184       8.346  10.052 -17.932  1.00 83.92           C\\nANISOU 1072  CG2 ILE A 184    10523  13226   8137   -643    -67    367       C\\nATOM   1073  CD1 ILE A 184       8.861   8.383 -15.456  1.00 80.33           C\\nANISOU 1073  CD1 ILE A 184    10011  12185   8326   -346     90    -54       C\\nATOM   1074  N   ALA A 185      10.335  12.279 -19.291  1.00 80.23           N\\nANISOU 1074  N   ALA A 185     9999  13442   7044  -1105     98   1028       N\\nATOM   1075  CA  ALA A 185      11.162  12.234 -20.487  1.00 83.51           C\\nANISOU 1075  CA  ALA A 185    10349  14420   6960  -1262    251   1031       C\\nATOM   1076  C   ALA A 185      12.352  13.177 -20.411  1.00 83.75           C\\nANISOU 1076  C   ALA A 185    10288  14647   6887  -1499    393   1327       C\\nATOM   1077  O   ALA A 185      13.207  13.143 -21.301  1.00 89.61           O\\nANISOU 1077  O   ALA A 185    10921  15924   7202  -1661    576   1320       O\\nATOM   1078  CB  ALA A 185      10.320  12.565 -21.723  1.00 73.89           C\\nANISOU 1078  CB  ALA A 185     9279  13403   5395  -1401     57   1201       C\\nATOM   1079  N   ASN A 186      12.425  14.011 -19.384  1.00 87.95           N\\nANISOU 1079  N   ASN A 186    10846  14788   7782  -1536    315   1567       N\\nATOM   1080  CA  ASN A 186      13.545  14.931 -19.235  1.00 90.37           C\\nANISOU 1080  CA  ASN A 186    11066  15232   8039  -1784    421   1852       C\\nATOM   1081  C   ASN A 186      14.781  14.156 -18.795  1.00 93.04           C\\nANISOU 1081  C   ASN A 186    11153  15806   8392  -1671    718   1526       C\\nATOM   1082  O   ASN A 186      14.734  13.472 -17.765  1.00 90.82           O\\nANISOU 1082  O   ASN A 186    10830  15214   8462  -1399    737   1252       O\\nATOM   1083  CB  ASN A 186      13.200  16.017 -18.220  1.00 86.22           C\\nANISOU 1083  CB  ASN A 186    10651  14175   7934  -1820    209   2150       C\\nATOM   1084  CG  ASN A 186      14.162  17.185 -18.259  1.00 89.29           C\\nANISOU 1084  CG  ASN A 186    11013  14659   8255  -2152    225   2537       C\\nATOM   1085  OD1 ASN A 186      15.380  17.008 -18.241  1.00 95.97           O\\nANISOU 1085  OD1 ASN A 186    11655  15837   8971  -2255    479   2464       O\\nATOM   1086  ND2 ASN A 186      13.616  18.393 -18.314  1.00 87.60           N\\nANISOU 1086  ND2 ASN A 186    10997  14142   8145  -2325    -71   2943       N\\nATOM   1087  N   PRO A 187      15.895  14.232 -19.527  1.00 95.07           N\\nANISOU 1087  N   PRO A 187    11229  16621   8273  -1873    941   1541       N\\nATOM   1088  CA  PRO A 187      17.095  13.486 -19.110  1.00 94.27           C\\nANISOU 1088  CA  PRO A 187    10845  16765   8209  -1726   1203   1183       C\\nATOM   1089  C   PRO A 187      17.587  13.857 -17.721  1.00 93.98           C\\nANISOU 1089  C   PRO A 187    10749  16330   8627  -1662   1185   1242       C\\nATOM   1090  O   PRO A 187      18.317  13.067 -17.109  1.00 94.56           O\\nANISOU 1090  O   PRO A 187    10638  16436   8855  -1433   1319    896       O\\nATOM   1091  CB  PRO A 187      18.127  13.845 -20.190  1.00 87.30           C\\nANISOU 1091  CB  PRO A 187     9769  16534   6867  -2026   1406   1271       C\\nATOM   1092  CG  PRO A 187      17.630  15.128 -20.784  1.00 81.91           C\\nANISOU 1092  CG  PRO A 187     9311  15710   6102  -2368   1189   1793       C\\nATOM   1093  CD  PRO A 187      16.135  15.035 -20.737  1.00 89.48           C\\nANISOU 1093  CD  PRO A 187    10552  16349   7098  -2256    952   1890       C\\nATOM   1094  N   ALA A 188      17.198  15.020 -17.198  1.00 89.90           N\\nANISOU 1094  N   ALA A 188    10393  15427   8337  -1837    994   1648       N\\nATOM   1095  CA  ALA A 188      17.621  15.462 -15.877  1.00 87.20           C\\nANISOU 1095  CA  ALA A 188    10012  14708   8411  -1788    952   1704       C\\nATOM   1096  C   ALA A 188      16.681  15.017 -14.764  1.00 83.84           C\\nANISOU 1096  C   ALA A 188     9732  13727   8396  -1473    795   1536       C\\nATOM   1097  O   ALA A 188      16.983  15.253 -13.591  1.00 75.80           O\\nANISOU 1097  O   ALA A 188     8687  12406   7707  -1395    761   1530       O\\nATOM   1098  CB  ALA A 188      17.750  16.987 -15.848  1.00 80.85           C\\nANISOU 1098  CB  ALA A 188     9302  13764   7654  -2142    804   2201       C\\nATOM   1099  N   PHE A 189      15.554  14.386 -15.094  1.00 80.92           N\\nANISOU 1099  N   PHE A 189     9504  13244   7997  -1314    698   1400       N\\nATOM   1100  CA  PHE A 189      14.640  13.936 -14.051  1.00 78.27           C\\nANISOU 1100  CA  PHE A 189     9281  12440   8018  -1065    570   1248       C\\nATOM   1101  C   PHE A 189      15.276  12.851 -13.193  1.00 80.35           C\\nANISOU 1101  C   PHE A 189     9430  12648   8450   -824    697    901       C\\nATOM   1102  O   PHE A 189      15.128  12.856 -11.964  1.00 75.11           O\\nANISOU 1102  O   PHE A 189     8806  11626   8105   -710    633    876       O\\nATOM   1103  CB  PHE A 189      13.335  13.437 -14.671  1.00 80.58           C\\nANISOU 1103  CB  PHE A 189     9715  12675   8225   -983    445   1165       C\\nATOM   1104  CG  PHE A 189      12.426  12.754 -13.693  1.00 85.91           C\\nANISOU 1104  CG  PHE A 189    10465  12965   9214   -760    358    965       C\\nATOM   1105  CD1 PHE A 189      11.690  13.490 -12.780  1.00 86.83           C\\nANISOU 1105  CD1 PHE A 189    10658  12708   9625   -749    203   1115       C\\nATOM   1106  CD2 PHE A 189      12.306  11.375 -13.683  1.00 84.50           C\\nANISOU 1106  CD2 PHE A 189    10274  12804   9028   -575    421    619       C\\nATOM   1107  CE1 PHE A 189      10.853  12.861 -11.873  1.00 82.22           C\\nANISOU 1107  CE1 PHE A 189    10115  11841   9283   -588    152    936       C\\nATOM   1108  CE2 PHE A 189      11.471  10.742 -12.779  1.00 79.97           C\\nANISOU 1108  CE2 PHE A 189     9777  11887   8720   -435    339    479       C\\nATOM   1109  CZ  PHE A 189      10.745  11.486 -11.874  1.00 75.49           C\\nANISOU 1109  CZ  PHE A 189     9262  11015   8404   -457    224    645       C\\nATOM   1110  N   VAL A 190      15.990  11.913 -13.820  1.00 82.64           N\\nANISOU 1110  N   VAL A 190     9581  13296   8524   -736    857    620       N\\nATOM   1111  CA  VAL A 190      16.608  10.825 -13.066  1.00 79.80           C\\nANISOU 1111  CA  VAL A 190     9129  12855   8338   -476    921    274       C\\nATOM   1112  C   VAL A 190      17.619  11.375 -12.070  1.00 73.96           C\\nANISOU 1112  C   VAL A 190     8263  12038   7801   -501    965    362       C\\nATOM   1113  O   VAL A 190      17.647  10.963 -10.905  1.00 69.81           O\\nANISOU 1113  O   VAL A 190     7780  11184   7561   -328    899    257       O\\nATOM   1114  CB  VAL A 190      17.246   9.799 -14.024  1.00 76.29           C\\nANISOU 1114  CB  VAL A 190     8531  12834   7621   -350   1058    -85       C\\nATOM   1115  CG1 VAL A 190      18.329   8.997 -13.321  1.00 73.98           C\\nANISOU 1115  CG1 VAL A 190     8071  12543   7496   -111   1121   -401       C\\nATOM   1116  CG2 VAL A 190      16.181   8.863 -14.570  1.00 70.22           C\\nANISOU 1116  CG2 VAL A 190     7922  11973   6787   -219    957   -292       C\\nATOM   1117  N   VAL A 191      18.449  12.327 -12.502  1.00 74.89           N\\nANISOU 1117  N   VAL A 191     8232  12459   7764   -745   1062    574       N\\nATOM   1118  CA  VAL A 191      19.440  12.910 -11.603  1.00 69.99           C\\nANISOU 1118  CA  VAL A 191     7472  11783   7337   -800   1089    659       C\\nATOM   1119  C   VAL A 191      18.756  13.666 -10.472  1.00 71.73           C\\nANISOU 1119  C   VAL A 191     7882  11494   7879   -818    904    880       C\\nATOM   1120  O   VAL A 191      19.167  13.580  -9.308  1.00 74.22           O\\nANISOU 1120  O   VAL A 191     8168  11584   8449   -696    866    802       O\\nATOM   1121  CB  VAL A 191      20.401  13.820 -12.387  1.00 69.86           C\\nANISOU 1121  CB  VAL A 191     7256  12216   7071  -1128   1224    873       C\\nATOM   1122  CG1 VAL A 191      21.588  14.210 -11.518  1.00 61.69           C\\nANISOU 1122  CG1 VAL A 191     6014  11194   6229  -1167   1269    875       C\\nATOM   1123  CG2 VAL A 191      20.860  13.135 -13.669  1.00 71.25           C\\nANISOU 1123  CG2 VAL A 191     7250  12975   6848  -1136   1419    651       C\\nATOM   1124  N   TYR A 192      17.698  14.409 -10.792  1.00 73.30           N\\nANISOU 1124  N   TYR A 192     8269  11519   8064   -952    769   1133       N\\nATOM   1125  CA  TYR A 192      17.008  15.209  -9.786  1.00 69.49           C\\nANISOU 1125  CA  TYR A 192     7937  10591   7877   -952    585   1300       C\\nATOM   1126  C   TYR A 192      16.386  14.323  -8.714  1.00 69.05           C\\nANISOU 1126  C   TYR A 192     7966  10230   8040   -683    540   1063       C\\nATOM   1127  O   TYR A 192      16.743  14.407  -7.534  1.00 70.50           O\\nANISOU 1127  O   TYR A 192     8135  10210   8443   -602    510   1018       O\\nATOM   1128  CB  TYR A 192      15.946  16.079 -10.460  1.00 70.53           C\\nANISOU 1128  CB  TYR A 192     8235  10616   7948  -1102    419   1566       C\\nATOM   1129  CG  TYR A 192      15.223  17.022  -9.524  1.00 71.79           C\\nANISOU 1129  CG  TYR A 192     8522  10343   8412  -1083    204   1704       C\\nATOM   1130  CD1 TYR A 192      15.814  18.212  -9.114  1.00 72.52           C\\nANISOU 1130  CD1 TYR A 192     8604  10305   8647  -1251    105   1926       C\\nATOM   1131  CD2 TYR A 192      13.943  16.733  -9.066  1.00 75.40           C\\nANISOU 1131  CD2 TYR A 192     9093  10543   9014   -904     92   1589       C\\nATOM   1132  CE1 TYR A 192      15.157  19.082  -8.265  1.00 72.60           C\\nANISOU 1132  CE1 TYR A 192     8724   9917   8942  -1200   -114   1996       C\\nATOM   1133  CE2 TYR A 192      13.275  17.600  -8.217  1.00 78.40           C\\nANISOU 1133  CE2 TYR A 192     9549  10580   9658   -860    -96   1656       C\\nATOM   1134  CZ  TYR A 192      13.887  18.772  -7.820  1.00 72.16           C\\nANISOU 1134  CZ  TYR A 192     8758   9648   9013   -988   -206   1843       C\\nATOM   1135  OH  TYR A 192      13.226  19.632  -6.973  1.00 63.34           O\\nANISOU 1135  OH  TYR A 192     7711   8188   8168   -909   -415   1853       O\\nATOM   1136  N   SER A 193      15.457  13.449  -9.114  1.00 72.61           N\\nANISOU 1136  N   SER A 193     8511  10659   8417   -566    526    916       N\\nATOM   1137  CA  SER A 193      14.715  12.654  -8.139  1.00 77.34           C\\nANISOU 1137  CA  SER A 193     9213  10968   9205   -382    469    746       C\\nATOM   1138  C   SER A 193      15.615  11.681  -7.386  1.00 75.22           C\\nANISOU 1138  C   SER A 193     8884  10678   9019   -217    535    524       C\\nATOM   1139  O   SER A 193      15.294  11.286  -6.260  1.00 76.80           O\\nANISOU 1139  O   SER A 193     9170  10614   9397   -116    473    460       O\\nATOM   1140  CB  SER A 193      13.580  11.897  -8.830  1.00 79.11           C\\nANISOU 1140  CB  SER A 193     9536  11195   9327   -336    430    640       C\\nATOM   1141  OG  SER A 193      14.075  10.934  -9.741  1.00 69.99           O\\nANISOU 1141  OG  SER A 193     8324  10300   7968   -274    524    442       O\\nATOM   1142  N   SER A 194      16.739  11.283  -7.980  1.00 71.25           N\\nANISOU 1142  N   SER A 194     8226  10467   8381   -186    646    398       N\\nATOM   1143  CA  SER A 194      17.664  10.407  -7.271  1.00 72.26           C\\nANISOU 1143  CA  SER A 194     8279  10561   8614      6    663    171       C\\nATOM   1144  C   SER A 194      18.401  11.166  -6.177  1.00 76.18           C\\nANISOU 1144  C   SER A 194     8709  10947   9290    -29    635    286       C\\nATOM   1145  O   SER A 194      18.423  10.741  -5.014  1.00 72.02           O\\nANISOU 1145  O   SER A 194     8263  10164   8939     99    550    218       O\\nATOM   1146  CB  SER A 194      18.661   9.784  -8.246  1.00 72.31           C\\nANISOU 1146  CB  SER A 194     8087  10955   8432     84    784    -57       C\\nATOM   1147  OG  SER A 194      17.998   9.092  -9.286  1.00 80.43           O\\nANISOU 1147  OG  SER A 194     9180  12101   9277    122    797   -194       O\\nATOM   1148  N   ILE A 195      19.005  12.300  -6.530  1.00 77.08           N\\nANISOU 1148  N   ILE A 195     8687  11249   9349   -226    688    474       N\\nATOM   1149  CA  ILE A 195      19.847  13.021  -5.580  1.00 70.51           C\\nANISOU 1149  CA  ILE A 195     7763  10342   8685   -272    652    555       C\\nATOM   1150  C   ILE A 195      18.988  13.748  -4.552  1.00 66.52           C\\nANISOU 1150  C   ILE A 195     7438   9466   8370   -304    511    708       C\\nATOM   1151  O   ILE A 195      19.129  13.541  -3.341  1.00 74.63           O\\nANISOU 1151  O   ILE A 195     8511  10286   9557   -186    438    633       O\\nATOM   1152  CB  ILE A 195      20.787  13.987  -6.321  1.00 68.49           C\\nANISOU 1152  CB  ILE A 195     7299  10412   8313   -520    744    715       C\\nATOM   1153  CG1 ILE A 195      21.784  13.200  -7.177  1.00 66.22           C\\nANISOU 1153  CG1 ILE A 195     6764  10568   7828   -459    911    488       C\\nATOM   1154  CG2 ILE A 195      21.510  14.892  -5.337  1.00 63.89           C\\nANISOU 1154  CG2 ILE A 195     6643   9700   7932   -613    668    829       C\\nATOM   1155  CD1 ILE A 195      22.738  14.064  -7.971  1.00 56.97           C\\nANISOU 1155  CD1 ILE A 195     5348   9813   6484   -752   1041    642       C\\nATOM   1156  N   VAL A 196      18.073  14.597  -5.019  1.00 62.66           N\\nANISOU 1156  N   VAL A 196     7052   8902   7854   -450    454    905       N\\nATOM   1157  CA  VAL A 196      17.332  15.463  -4.105  1.00 67.97           C\\nANISOU 1157  CA  VAL A 196     7847   9264   8715   -469    309   1012       C\\nATOM   1158  C   VAL A 196      16.343  14.656  -3.269  1.00 67.07           C\\nANISOU 1158  C   VAL A 196     7868   8944   8670   -296    275    861       C\\nATOM   1159  O   VAL A 196      16.268  14.814  -2.046  1.00 61.49           O\\nANISOU 1159  O   VAL A 196     7206   8054   8102   -231    210    818       O\\nATOM   1160  CB  VAL A 196      16.626  16.582  -4.888  1.00 64.23           C\\nANISOU 1160  CB  VAL A 196     7440   8750   8216   -643    212   1244       C\\nATOM   1161  CG1 VAL A 196      15.849  17.474  -3.945  1.00 52.97           C\\nANISOU 1161  CG1 VAL A 196     6116   7001   7009   -610     37   1287       C\\nATOM   1162  CG2 VAL A 196      17.638  17.392  -5.674  1.00 71.96           C\\nANISOU 1162  CG2 VAL A 196     8304   9935   9102   -883    238   1445       C\\nATOM   1163  N   SER A 197      15.571  13.778  -3.911  1.00 68.31           N\\nANISOU 1163  N   SER A 197     8091   9151   8712   -244    315    780       N\\nATOM   1164  CA  SER A 197      14.505  13.073  -3.211  1.00 64.29           C\\nANISOU 1164  CA  SER A 197     7706   8466   8256   -150    280    676       C\\nATOM   1165  C   SER A 197      14.986  11.839  -2.460  1.00 64.86           C\\nANISOU 1165  C   SER A 197     7819   8478   8346    -22    301    516       C\\nATOM   1166  O   SER A 197      14.304  11.401  -1.528  1.00 71.84           O\\nANISOU 1166  O   SER A 197     8812   9202   9284      7    262    476       O\\nATOM   1167  CB  SER A 197      13.401  12.668  -4.191  1.00 64.34           C\\nANISOU 1167  CB  SER A 197     7768   8525   8155   -175    281    661       C\\nATOM   1168  OG  SER A 197      12.416  13.677  -4.297  1.00 65.40           O\\nANISOU 1168  OG  SER A 197     7921   8583   8345   -241    188    775       O\\nATOM   1169  N   PHE A 198      16.134  11.265  -2.824  1.00 56.65           N\\nANISOU 1169  N   PHE A 198     6693   7571   7259     50    348    422       N\\nATOM   1170  CA  PHE A 198      16.563  10.006  -2.225  1.00 61.84           C\\nANISOU 1170  CA  PHE A 198     7413   8131   7953    205    308    258       C\\nATOM   1171  C   PHE A 198      17.951  10.080  -1.597  1.00 66.94           C\\nANISOU 1171  C   PHE A 198     7945   8814   8677    293    283    207       C\\nATOM   1172  O   PHE A 198      18.076   9.853  -0.391  1.00 63.30           O\\nANISOU 1172  O   PHE A 198     7574   8170   8306    352    191    202       O\\nATOM   1173  CB  PHE A 198      16.518   8.887  -3.269  1.00 62.27           C\\nANISOU 1173  CB  PHE A 198     7477   8279   7904    290    331     91       C\\nATOM   1174  CG  PHE A 198      16.836   7.525  -2.714  1.00 71.87           C\\nANISOU 1174  CG  PHE A 198     8800   9318   9188    461    226    -82       C\\nATOM   1175  CD1 PHE A 198      15.889   6.822  -1.986  1.00 73.26           C\\nANISOU 1175  CD1 PHE A 198     9194   9229   9414    432    130    -54       C\\nATOM   1176  CD2 PHE A 198      18.074   6.944  -2.927  1.00 66.14           C\\nANISOU 1176  CD2 PHE A 198     7955   8695   8481    641    204   -273       C\\nATOM   1177  CE1 PHE A 198      16.173   5.566  -1.481  1.00 70.07           C\\nANISOU 1177  CE1 PHE A 198     8932   8611   9079    560    -15   -171       C\\nATOM   1178  CE2 PHE A 198      18.365   5.687  -2.423  1.00 70.55           C\\nANISOU 1178  CE2 PHE A 198     8637   9036   9134    826     45   -436       C\\nATOM   1179  CZ  PHE A 198      17.412   4.997  -1.700  1.00 69.64           C\\nANISOU 1179  CZ  PHE A 198     8787   8602   9070    775    -79   -363       C\\nATOM   1180  N   TYR A 199      18.996  10.380  -2.373  1.00 67.17           N\\nANISOU 1180  N   TYR A 199     7766   9103   8654    290    360    166       N\\nATOM   1181  CA  TYR A 199      20.356  10.230  -1.861  1.00 67.05           C\\nANISOU 1181  CA  TYR A 199     7598   9159   8719    402    329     58       C\\nATOM   1182  C   TYR A 199      20.656  11.224  -0.746  1.00 67.17           C\\nANISOU 1182  C   TYR A 199     7604   9058   8859    323    261    193       C\\nATOM   1183  O   TYR A 199      21.379  10.897   0.202  1.00 60.26           O\\nANISOU 1183  O   TYR A 199     6716   8098   8082    445    161    112       O\\nATOM   1184  CB  TYR A 199      21.367  10.375  -2.997  1.00 71.88           C\\nANISOU 1184  CB  TYR A 199     7935  10155   9221    380    457    -32       C\\nATOM   1185  CG  TYR A 199      21.372   9.197  -3.942  1.00 81.30           C\\nANISOU 1185  CG  TYR A 199     9102  11489  10299    540    498   -275       C\\nATOM   1186  CD1 TYR A 199      21.185   7.907  -3.469  1.00 86.13           C\\nANISOU 1186  CD1 TYR A 199     9871  11856  10998    769    359   -463       C\\nATOM   1187  CD2 TYR A 199      21.545   9.374  -5.307  1.00 83.10           C\\nANISOU 1187  CD2 TYR A 199     9165  12088  10320    449    652   -315       C\\nATOM   1188  CE1 TYR A 199      21.177   6.825  -4.325  1.00 85.63           C\\nANISOU 1188  CE1 TYR A 199     9799  11878  10859    933    355   -719       C\\nATOM   1189  CE2 TYR A 199      21.538   8.297  -6.171  1.00 80.51           C\\nANISOU 1189  CE2 TYR A 199     8809  11905   9875    615    680   -585       C\\nATOM   1190  CZ  TYR A 199      21.352   7.026  -5.674  1.00 76.43           C\\nANISOU 1190  CZ  TYR A 199     8448  11104   9487    871    522   -803       C\\nATOM   1191  OH  TYR A 199      21.344   5.950  -6.531  1.00 69.70           O\\nANISOU 1191  OH  TYR A 199     7579  10355   8547   1053    510  -1106       O\\nATOM   1192  N   VAL A 200      20.116  12.435  -0.831  1.00 65.74           N\\nANISOU 1192  N   VAL A 200     7439   8856   8685    133    281    383       N\\nATOM   1193  CA  VAL A 200      20.375  13.434   0.206  1.00 71.58           C\\nANISOU 1193  CA  VAL A 200     8173   9468   9555     66    193    476       C\\nATOM   1194  C   VAL A 200      19.616  13.076   1.483  1.00 70.25           C\\nANISOU 1194  C   VAL A 200     8210   9046   9435    156     95    445       C\\nATOM   1195  O   VAL A 200      20.203  13.156   2.571  1.00 66.48           O\\nANISOU 1195  O   VAL A 200     7736   8490   9035    213      0    407       O\\nATOM   1196  CB  VAL A 200      20.038  14.854  -0.281  1.00 71.46           C\\nANISOU 1196  CB  VAL A 200     8129   9461   9562   -148    192    671       C\\nATOM   1197  CG1 VAL A 200      20.109  15.848   0.873  1.00 70.31           C\\nANISOU 1197  CG1 VAL A 200     8017   9123   9575   -187     60    720       C\\nATOM   1198  CG2 VAL A 200      20.992  15.264  -1.393  1.00 67.72           C\\nANISOU 1198  CG2 VAL A 200     7444   9277   9011   -300    285    742       C\\nATOM   1199  N   PRO A 201      18.333  12.691   1.432  1.00 68.63           N\\nANISOU 1199  N   PRO A 201     8167   8739   9171    150    111    459       N\\nATOM   1200  CA  PRO A 201      17.717  12.147   2.655  1.00 67.01           C\\nANISOU 1200  CA  PRO A 201     8135   8363   8962    204     43    424       C\\nATOM   1201  C   PRO A 201      18.416  10.898   3.166  1.00 63.12           C\\nANISOU 1201  C   PRO A 201     7712   7811   8461    342    -32    331       C\\nATOM   1202  O   PRO A 201      18.541  10.711   4.383  1.00 64.72           O\\nANISOU 1202  O   PRO A 201     8019   7903   8669    376   -131    332       O\\nATOM   1203  CB  PRO A 201      16.275  11.860   2.217  1.00 66.92           C\\nANISOU 1203  CB  PRO A 201     8227   8319   8879    142     97    446       C\\nATOM   1204  CG  PRO A 201      16.022  12.833   1.137  1.00 66.63           C\\nANISOU 1204  CG  PRO A 201     8086   8379   8852     55    144    523       C\\nATOM   1205  CD  PRO A 201      17.319  12.916   0.383  1.00 66.70           C\\nANISOU 1205  CD  PRO A 201     7946   8542   8857     61    178    525       C\\nATOM   1206  N   PHE A 202      18.884  10.041   2.258  1.00 56.10           N\\nANISOU 1206  N   PHE A 202     6771   6992   7551    435    -11    238       N\\nATOM   1207  CA  PHE A 202      19.593   8.829   2.655  1.00 63.87           C\\nANISOU 1207  CA  PHE A 202     7821   7882   8566    610   -137    119       C\\nATOM   1208  C   PHE A 202      20.816   9.156   3.509  1.00 70.36           C\\nANISOU 1208  C   PHE A 202     8539   8718   9475    697   -242     86       C\\nATOM   1209  O   PHE A 202      20.977   8.621   4.613  1.00 72.54           O\\nANISOU 1209  O   PHE A 202     8969   8826   9768    771   -400     91       O\\nATOM   1210  CB  PHE A 202      19.992   8.047   1.402  1.00 62.85           C\\nANISOU 1210  CB  PHE A 202     7591   7872   8416    726    -97    -41       C\\nATOM   1211  CG  PHE A 202      20.499   6.659   1.671  1.00 70.17           C\\nANISOU 1211  CG  PHE A 202     8620   8639   9403    941   -273   -200       C\\nATOM   1212  CD1 PHE A 202      20.468   6.114   2.942  1.00 73.47           C\\nANISOU 1212  CD1 PHE A 202     9254   8795   9864    982   -462   -139       C\\nATOM   1213  CD2 PHE A 202      21.014   5.899   0.638  1.00 76.10           C\\nANISOU 1213  CD2 PHE A 202     9257   9501  10156   1108   -271   -423       C\\nATOM   1214  CE1 PHE A 202      20.939   4.847   3.177  1.00 78.88           C\\nANISOU 1214  CE1 PHE A 202    10067   9279  10625   1182   -682   -264       C\\nATOM   1215  CE2 PHE A 202      21.485   4.628   0.866  1.00 75.62           C\\nANISOU 1215  CE2 PHE A 202     9296   9248  10187   1343   -483   -603       C\\nATOM   1216  CZ  PHE A 202      21.447   4.100   2.137  1.00 79.28           C\\nANISOU 1216  CZ  PHE A 202    10003   9395  10724   1380   -707   -507       C\\nATOM   1217  N   ILE A 203      21.692  10.031   3.011  1.00 69.89           N\\nANISOU 1217  N   ILE A 203     8223   8871   9462    667   -169     66       N\\nATOM   1218  CA  ILE A 203      22.931  10.333   3.726  1.00 70.07           C\\nANISOU 1218  CA  ILE A 203     8101   8940   9583    743   -275      9       C\\nATOM   1219  C   ILE A 203      22.628  10.977   5.074  1.00 68.51           C\\nANISOU 1219  C   ILE A 203     8043   8585   9403    671   -375    114       C\\nATOM   1220  O   ILE A 203      23.185  10.584   6.106  1.00 61.96           O\\nANISOU 1220  O   ILE A 203     7279   7659   8605    783   -545     72       O\\nATOM   1221  CB  ILE A 203      23.843  11.227   2.870  1.00 67.00           C\\nANISOU 1221  CB  ILE A 203     7390   8840   9226    648   -158     -7       C\\nATOM   1222  CG1 ILE A 203      24.189  10.534   1.555  1.00 68.52           C\\nANISOU 1222  CG1 ILE A 203     7420   9264   9349    728    -43   -152       C\\nATOM   1223  CG2 ILE A 203      25.111  11.566   3.623  1.00 62.39           C\\nANISOU 1223  CG2 ILE A 203     6625   8319   8761    704   -276    -75       C\\nATOM   1224  CD1 ILE A 203      24.882  11.438   0.566  1.00 75.16           C\\nANISOU 1224  CD1 ILE A 203     7956  10453  10148    555    118   -121       C\\nATOM   1225  N   VAL A 204      21.738  11.974   5.082  1.00 68.09           N\\nANISOU 1225  N   VAL A 204     8035   8512   9324    499   -292    232       N\\nATOM   1226  CA  VAL A 204      21.439  12.706   6.313  1.00 64.98           C\\nANISOU 1226  CA  VAL A 204     7739   8013   8938    443   -378    276       C\\nATOM   1227  C   VAL A 204      20.881  11.767   7.375  1.00 65.55           C\\nANISOU 1227  C   VAL A 204     8061   7945   8902    504   -469    277       C\\nATOM   1228  O   VAL A 204      21.332  11.764   8.527  1.00 66.60           O\\nANISOU 1228  O   VAL A 204     8259   8027   9017    550   -610    260       O\\nATOM   1229  CB  VAL A 204      20.471  13.865   6.027  1.00 56.49           C\\nANISOU 1229  CB  VAL A 204     6664   6928   7872    291   -296    354       C\\nATOM   1230  CG1 VAL A 204      19.900  14.399   7.325  1.00 59.98           C\\nANISOU 1230  CG1 VAL A 204     7227   7276   8289    274   -375    333       C\\nATOM   1231  CG2 VAL A 204      21.185  14.972   5.267  1.00 55.27           C\\nANISOU 1231  CG2 VAL A 204     6299   6869   7831    182   -275    403       C\\nATOM   1232  N   THR A 205      19.886  10.960   7.005  1.00 66.29           N\\nANISOU 1232  N   THR A 205     8302   7982   8903    478   -403    312       N\\nATOM   1233  CA  THR A 205      19.340   9.991   7.947  1.00 66.07           C\\nANISOU 1233  CA  THR A 205     8524   7824   8753    475   -492    356       C\\nATOM   1234  C   THR A 205      20.407   9.003   8.395  1.00 73.22           C\\nANISOU 1234  C   THR A 205     9501   8627   9694    637   -693    319       C\\nATOM   1235  O   THR A 205      20.450   8.611   9.567  1.00 73.97           O\\nANISOU 1235  O   THR A 205     9780   8626   9698    635   -843    376       O\\nATOM   1236  CB  THR A 205      18.162   9.258   7.313  1.00 64.13           C\\nANISOU 1236  CB  THR A 205     8398   7536   8434    391   -397    399       C\\nATOM   1237  OG1 THR A 205      17.159  10.210   6.937  1.00 70.05           O\\nANISOU 1237  OG1 THR A 205     9065   8385   9167    268   -244    415       O\\nATOM   1238  CG2 THR A 205      17.567   8.265   8.291  1.00 59.18           C\\nANISOU 1238  CG2 THR A 205     8038   6780   7668    317   -492    485       C\\nATOM   1239  N   LEU A 206      21.282   8.594   7.476  1.00 71.22           N\\nANISOU 1239  N   LEU A 206     9095   8407   9557    784   -714    211       N\\nATOM   1240  CA  LEU A 206      22.343   7.663   7.839  1.00 69.37           C\\nANISOU 1240  CA  LEU A 206     8891   8070   9395    992   -940    126       C\\nATOM   1241  C   LEU A 206      23.325   8.302   8.810  1.00 67.69           C\\nANISOU 1241  C   LEU A 206     8584   7907   9228   1046  -1074    104       C\\nATOM   1242  O   LEU A 206      23.847   7.629   9.705  1.00 63.83           O\\nANISOU 1242  O   LEU A 206     8237   7281   8736   1166  -1318    106       O\\nATOM   1243  CB  LEU A 206      23.069   7.177   6.586  1.00 68.74           C\\nANISOU 1243  CB  LEU A 206     8603   8086   9429   1162   -911    -54       C\\nATOM   1244  CG  LEU A 206      24.254   6.253   6.864  1.00 66.60           C\\nANISOU 1244  CG  LEU A 206     8300   7728   9276   1438  -1170   -212       C\\nATOM   1245  CD1 LEU A 206      23.779   4.999   7.577  1.00 68.61           C\\nANISOU 1245  CD1 LEU A 206     8929   7645   9495   1492  -1416   -131       C\\nATOM   1246  CD2 LEU A 206      24.981   5.908   5.578  1.00 65.91           C\\nANISOU 1246  CD2 LEU A 206     7933   7826   9284   1614  -1102   -453       C\\nATOM   1247  N   LEU A 207      23.592   9.597   8.647  1.00 71.05           N\\nANISOU 1247  N   LEU A 207     8784   8507   9703    951   -950     91       N\\nATOM   1248  CA  LEU A 207      24.489  10.279   9.572  1.00 68.27           C\\nANISOU 1248  CA  LEU A 207     8336   8199   9405    979  -1088     58       C\\nATOM   1249  C   LEU A 207      23.856  10.418  10.949  1.00 68.21           C\\nANISOU 1249  C   LEU A 207     8586   8088   9244    897  -1186    154       C\\nATOM   1250  O   LEU A 207      24.552  10.352  11.967  1.00 66.32           O\\nANISOU 1250  O   LEU A 207     8392   7815   8989    976  -1395    132       O\\nATOM   1251  CB  LEU A 207      24.875  11.645   9.012  1.00 63.44           C\\nANISOU 1251  CB  LEU A 207     7441   7765   8897    855   -953     35       C\\nATOM   1252  CG  LEU A 207      25.757  11.605   7.765  1.00 58.28           C\\nANISOU 1252  CG  LEU A 207     6481   7306   8356    900   -859    -62       C\\nATOM   1253  CD1 LEU A 207      25.869  12.987   7.135  1.00 58.28           C\\nANISOU 1253  CD1 LEU A 207     6266   7458   8418    685   -713     -2       C\\nATOM   1254  CD2 LEU A 207      27.133  11.057   8.115  1.00 60.06           C\\nANISOU 1254  CD2 LEU A 207     6537   7593   8688   1106  -1049   -219       C\\nATOM   1255  N   VAL A 208      22.536  10.604  11.000  1.00 65.76           N\\nANISOU 1255  N   VAL A 208     8427   7760   8800    740  -1039    244       N\\nATOM   1256  CA  VAL A 208      21.850  10.728  12.283  1.00 70.01           C\\nANISOU 1256  CA  VAL A 208     9179   8279   9143    643  -1090    309       C\\nATOM   1257  C   VAL A 208      21.897   9.408  13.042  1.00 72.90           C\\nANISOU 1257  C   VAL A 208     9821   8505   9370    686  -1284    405       C\\nATOM   1258  O   VAL A 208      22.211   9.371  14.237  1.00 72.29           O\\nANISOU 1258  O   VAL A 208     9878   8422   9167    690  -1459    437       O\\nATOM   1259  CB  VAL A 208      20.403  11.205  12.072  1.00 62.31           C\\nANISOU 1259  CB  VAL A 208     8243   7366   8066    475   -875    344       C\\nATOM   1260  CG1 VAL A 208      19.616  11.100  13.361  1.00 57.35           C\\nANISOU 1260  CG1 VAL A 208     7821   6784   7185    363   -898    391       C\\nATOM   1261  CG2 VAL A 208      20.388  12.634  11.560  1.00 55.34           C\\nANISOU 1261  CG2 VAL A 208     7134   6567   7324    438   -769    263       C\\nATOM   1262  N   TYR A 209      21.584   8.304  12.360  1.00 67.17           N\\nANISOU 1262  N   TYR A 209     9206   7651   8663    711  -1285    458       N\\nATOM   1263  CA  TYR A 209      21.578   7.010  13.032  1.00 62.85           C\\nANISOU 1263  CA  TYR A 209     8966   6907   8008    728  -1515    581       C\\nATOM   1264  C   TYR A 209      22.975   6.598  13.468  1.00 67.38           C\\nANISOU 1264  C   TYR A 209     9528   7379   8695    962  -1822    518       C\\nATOM   1265  O   TYR A 209      23.130   5.942  14.504  1.00 76.08           O\\nANISOU 1265  O   TYR A 209    10894   8346   9666    963  -2077    640       O\\nATOM   1266  CB  TYR A 209      20.960   5.946  12.126  1.00 60.49           C\\nANISOU 1266  CB  TYR A 209     8784   6452   7749    710  -1483    623       C\\nATOM   1267  CG  TYR A 209      19.452   5.927  12.179  1.00 66.56           C\\nANISOU 1267  CG  TYR A 209     9685   7270   8334    437  -1286    750       C\\nATOM   1268  CD1 TYR A 209      18.788   5.544  13.335  1.00 66.30           C\\nANISOU 1268  CD1 TYR A 209     9921   7223   8047    229  -1351    931       C\\nATOM   1269  CD2 TYR A 209      18.693   6.292  11.078  1.00 67.85           C\\nANISOU 1269  CD2 TYR A 209     9692   7530   8559    372  -1040    687       C\\nATOM   1270  CE1 TYR A 209      17.408   5.526  13.397  1.00 71.51           C\\nANISOU 1270  CE1 TYR A 209    10651   7990   8531    -39  -1153   1024       C\\nATOM   1271  CE2 TYR A 209      17.312   6.271  11.129  1.00 67.87           C\\nANISOU 1271  CE2 TYR A 209     9776   7601   8410    135   -874    776       C\\nATOM   1272  CZ  TYR A 209      16.675   5.892  12.292  1.00 73.98           C\\nANISOU 1272  CZ  TYR A 209    10778   8387   8944    -71   -920    933       C\\nATOM   1273  OH  TYR A 209      15.301   5.875  12.350  1.00 78.65           O\\nANISOU 1273  OH  TYR A 209    11400   9107   9378   -325   -736    998       O\\nATOM   1274  N   ILE A 210      24.002   6.972  12.702  1.00 65.59           N\\nANISOU 1274  N   ILE A 210     8989   7235   8698   1151  -1815    332       N\\nATOM   1275  CA  ILE A 210      25.373   6.731  13.144  1.00 66.53           C\\nANISOU 1275  CA  ILE A 210     9020   7316   8943   1384  -2102    228       C\\nATOM   1276  C   ILE A 210      25.669   7.536  14.402  1.00 68.90           C\\nANISOU 1276  C   ILE A 210     9347   7706   9128   1318  -2205    265       C\\nATOM   1277  O   ILE A 210      26.296   7.036  15.343  1.00 66.82           O\\nANISOU 1277  O   ILE A 210     9234   7337   8820   1429  -2518    299       O\\nATOM   1278  CB  ILE A 210      26.368   7.053  12.015  1.00 68.77           C\\nANISOU 1278  CB  ILE A 210     8898   7760   9473   1556  -2020      2       C\\nATOM   1279  CG1 ILE A 210      26.237   6.043  10.879  1.00 66.91           C\\nANISOU 1279  CG1 ILE A 210     8656   7435   9331   1685  -1991    -87       C\\nATOM   1280  CG2 ILE A 210      27.792   7.062  12.545  1.00 69.56           C\\nANISOU 1280  CG2 ILE A 210     8822   7898   9711   1774  -2291   -139       C\\nATOM   1281  CD1 ILE A 210      27.237   6.254   9.771  1.00 66.26           C\\nANISOU 1281  CD1 ILE A 210     8158   7579   9440   1852  -1900   -335       C\\nATOM   1282  N   LYS A 211      25.221   8.797  14.439  1.00 68.09           N\\nANISOU 1282  N   LYS A 211     9108   7786   8977   1147  -1974    247       N\\nATOM   1283  CA  LYS A 211      25.368   9.607  15.645  1.00 72.77           C\\nANISOU 1283  CA  LYS A 211     9739   8468   9442   1077  -2066    245       C\\nATOM   1284  C   LYS A 211      24.551   9.044  16.798  1.00 75.75           C\\nANISOU 1284  C   LYS A 211    10492   8790   9501    949  -2158    418       C\\nATOM   1285  O   LYS A 211      24.918   9.225  17.965  1.00 75.16           O\\nANISOU 1285  O   LYS A 211    10526   8758   9275    949  -2353    430       O\\nATOM   1286  CB  LYS A 211      24.956  11.053  15.367  1.00 72.52           C\\nANISOU 1286  CB  LYS A 211     9503   8598   9455    934  -1825    165       C\\nATOM   1287  CG  LYS A 211      26.059  11.921  14.784  1.00 76.74           C\\nANISOU 1287  CG  LYS A 211     9682   9223  10251    997  -1830     21       C\\nATOM   1288  CD  LYS A 211      27.081  12.304  15.845  1.00 80.50           C\\nANISOU 1288  CD  LYS A 211    10106   9734  10746   1072  -2092    -66       C\\nATOM   1289  N   ILE A 212      23.444   8.363  16.492  1.00 76.82           N\\nANISOU 1289  N   ILE A 212    10821   8858   9510    813  -2022    555       N\\nATOM   1290  CA  ILE A 212      22.634   7.738  17.534  1.00 75.49           C\\nANISOU 1290  CA  ILE A 212    11004   8670   9009    629  -2092    753       C\\nATOM   1291  C   ILE A 212      23.351   6.523  18.110  1.00 78.85           C\\nANISOU 1291  C   ILE A 212    11697   8862   9401    741  -2475    889       C\\nATOM   1292  O   ILE A 212      23.426   6.348  19.332  1.00 81.23           O\\nANISOU 1292  O   ILE A 212    12234   9186   9445    664  -2673   1015       O\\nATOM   1293  CB  ILE A 212      21.244   7.368  16.983  1.00 72.94           C\\nANISOU 1293  CB  ILE A 212    10775   8353   8584    420  -1838    858       C\\nATOM   1294  CG1 ILE A 212      20.367   8.618  16.858  1.00 72.24           C\\nANISOU 1294  CG1 ILE A 212    10488   8519   8442    291  -1522    738       C\\nATOM   1295  CG2 ILE A 212      20.575   6.319  17.861  1.00 71.22           C\\nANISOU 1295  CG2 ILE A 212    10941   8062   8058    211  -1961   1112       C\\nATOM   1296  CD1 ILE A 212      18.962   8.339  16.351  1.00 65.08           C\\nANISOU 1296  CD1 ILE A 212     9627   7664   7437     90  -1276    811       C\\nATOM   1297  N   TYR A 213      23.890   5.666  17.237  1.00 80.40           N\\nANISOU 1297  N   TYR A 213    11866   8833   9849    936  -2607    855       N\\nATOM   1298  CA  TYR A 213      24.609   4.484  17.706  1.00 74.91           C\\nANISOU 1298  CA  TYR A 213    11423   7857   9182   1095  -3032    956       C\\nATOM   1299  C   TYR A 213      25.796   4.871  18.580  1.00 76.60           C\\nANISOU 1299  C   TYR A 213    11566   8127   9414   1272  -3314    873       C\\nATOM   1300  O   TYR A 213      26.091   4.197  19.574  1.00 75.58           O\\nANISOU 1300  O   TYR A 213    11741   7846   9129   1288  -3670   1037       O\\nATOM   1301  CB  TYR A 213      25.070   3.642  16.515  1.00 69.47           C\\nANISOU 1301  CB  TYR A 213    10637   6949   8811   1339  -3122    828       C\\nATOM   1302  CG  TYR A 213      25.850   2.401  16.899  1.00 82.87           C\\nANISOU 1302  CG  TYR A 213    12578   8305  10605   1567  -3612    881       C\\nATOM   1303  CD1 TYR A 213      25.198   1.248  17.317  1.00 88.00           C\\nANISOU 1303  CD1 TYR A 213    13681   8643  11110   1422  -3838   1153       C\\nATOM   1304  CD2 TYR A 213      27.237   2.376  16.828  1.00 83.04           C\\nANISOU 1304  CD2 TYR A 213    12370   8305  10877   1924  -3876    656       C\\nATOM   1305  CE1 TYR A 213      25.906   0.107  17.664  1.00 88.45           C\\nANISOU 1305  CE1 TYR A 213    13945   8382  11281   1597  -4262   1171       C\\nATOM   1306  CE2 TYR A 213      27.955   1.241  17.174  1.00 84.14           C\\nANISOU 1306  CE2 TYR A 213    12701   8139  11130   2144  -4318    655       C\\nATOM   1307  CZ  TYR A 213      27.286   0.109  17.589  1.00 88.74           C\\nANISOU 1307  CZ  TYR A 213    13713   8432  11572   1950  -4461    892       C\\nATOM   1308  OH  TYR A 213      27.998  -1.023  17.933  1.00 93.97           O\\nANISOU 1308  OH  TYR A 213    14524   8828  12351   2091  -4813    843       O\\nATOM   1309  N   ILE A 214      26.491   5.955  18.226  1.00 79.22           N\\nANISOU 1309  N   ILE A 214    11503   8668   9929   1388  -3184    634       N\\nATOM   1310  CA  ILE A 214      27.667   6.368  18.988  1.00 79.71           C\\nANISOU 1310  CA  ILE A 214    11448   8796  10043   1553  -3456    525       C\\nATOM   1311  C   ILE A 214      27.278   6.769  20.407  1.00 82.99           C\\nANISOU 1311  C   ILE A 214    12112   9325  10094   1359  -3536    663       C\\nATOM   1312  O   ILE A 214      27.993   6.468  21.373  1.00 77.18           O\\nANISOU 1312  O   ILE A 214    11526   8534   9267   1459  -3903    709       O\\nATOM   1313  CB  ILE A 214      28.405   7.505  18.256  1.00 74.49           C\\nANISOU 1313  CB  ILE A 214    10301   8350   9651   1642  -3272    259       C\\nATOM   1314  CG1 ILE A 214      28.993   6.995  16.944  1.00 73.37           C\\nANISOU 1314  CG1 ILE A 214     9897   8156   9825   1855  -3239    102       C\\nATOM   1315  CG2 ILE A 214      29.508   8.085  19.125  1.00 79.54           C\\nANISOU 1315  CG2 ILE A 214    10802   9091  10328   1753  -3532    141       C\\nATOM   1316  CD1 ILE A 214      29.840   8.022  16.221  1.00 79.87           C\\nANISOU 1316  CD1 ILE A 214    10233   9224  10891   1906  -3079   -130       C\\nATOM   1317  N   VAL A 215      26.138   7.447  20.558  1.00 80.48           N\\nANISOU 1317  N   VAL A 215    11834   9193   9553   1092  -3207    710       N\\nATOM   1318  CA  VAL A 215      25.693   7.866  21.883  1.00 80.01           C\\nANISOU 1318  CA  VAL A 215    11978   9313   9108    905  -3241    790       C\\nATOM   1319  C   VAL A 215      25.303   6.658  22.722  1.00 86.31           C\\nANISOU 1319  C   VAL A 215    13235   9978   9582    774  -3480   1098       C\\nATOM   1320  O   VAL A 215      25.668   6.557  23.900  1.00 89.76           O\\nANISOU 1320  O   VAL A 215    13882  10466   9758    750  -3755   1189       O\\nATOM   1321  CB  VAL A 215      24.532   8.868  21.764  1.00 69.82           C\\nANISOU 1321  CB  VAL A 215    10575   8272   7681    685  -2829    710       C\\nATOM   1322  CG1 VAL A 215      23.873   9.073  23.115  1.00 70.46           C\\nANISOU 1322  CG1 VAL A 215    10891   8582   7299    474  -2833    787       C\\nATOM   1323  CG2 VAL A 215      25.035  10.188  21.201  1.00 70.96           C\\nANISOU 1323  CG2 VAL A 215    10323   8520   8117    791  -2692    435       C\\nATOM   1324  N   LEU A 216      24.556   5.722  22.131  1.00 88.27           N\\nANISOU 1324  N   LEU A 216    13660  10047   9830    664  -3400   1278       N\\nATOM   1325  CA  LEU A 216      24.129   4.539  22.870  1.00 81.42           C\\nANISOU 1325  CA  LEU A 216    13257   9014   8666    480  -3641   1616       C\\nATOM   1326  C   LEU A 216      25.314   3.682  23.294  1.00 84.21           C\\nANISOU 1326  C   LEU A 216    13802   9063   9129    728  -4180   1700       C\\nATOM   1327  O   LEU A 216      25.268   3.046  24.353  1.00 81.69           O\\nANISOU 1327  O   LEU A 216    13836   8687   8514    577  -4427   1947       O\\nATOM   1328  CB  LEU A 216      23.148   3.725  22.025  1.00 83.40           C\\nANISOU 1328  CB  LEU A 216    13629   9094   8967    318  -3470   1765       C\\nATOM   1329  CG  LEU A 216      21.846   4.440  21.657  1.00 89.34           C\\nANISOU 1329  CG  LEU A 216    14218  10142   9584     56  -2973   1707       C\\nATOM   1330  CD1 LEU A 216      21.017   3.625  20.676  1.00 88.79           C\\nANISOU 1330  CD1 LEU A 216    14221   9881   9633    -62  -2839   1814       C\\nATOM   1331  CD2 LEU A 216      21.046   4.736  22.911  1.00 97.88           C\\nANISOU 1331  CD2 LEU A 216    15482  11550  10159   -274  -2870   1850       C\\nATOM   1332  N   ARG A 217      26.382   3.651  22.492  1.00 81.94           N\\nANISOU 1332  N   ARG A 217    13237   8618   9279   1094  -4322   1464       N\\nATOM   1333  CA  ARG A 217      27.561   2.877  22.871  1.00 83.41           C\\nANISOU 1333  CA  ARG A 217    13486   8566   9641   1348  -4750   1435       C\\nATOM   1334  C   ARG A 217      28.345   3.556  23.985  1.00 85.61           C\\nANISOU 1334  C   ARG A 217    13711   9042   9775   1403  -4934   1364       C\\nATOM   1335  O   ARG A 217      28.952   2.873  24.816  1.00 80.30           O\\nANISOU 1335  O   ARG A 217    13221   8234   9057   1442  -5229   1443       O\\nATOM   1336  CB  ARG A 217      28.460   2.641  21.658  1.00 74.00           C\\nANISOU 1336  CB  ARG A 217    11946   7228   8942   1710  -4789   1141       C\\nATOM   1337  N   ARG A 218      28.347   4.891  24.021  1.00 77.47           N\\nANISOU 1337  N   ARG A 218    12427   8320   8687   1399  -4771   1198       N\\nATOM   1338  CA  ARG A 218      28.948   5.589  25.152  1.00 79.95           C\\nANISOU 1338  CA  ARG A 218    12725   8839   8812   1411  -4955   1127       C\\nATOM   1339  C   ARG A 218      28.170   5.328  26.435  1.00 82.04           C\\nANISOU 1339  C   ARG A 218    13403   9226   8543   1087  -4970   1402       C\\nATOM   1340  O   ARG A 218      28.765   5.243  27.517  1.00 84.60           O\\nANISOU 1340  O   ARG A 218    13838   9600   8707   1097  -5207   1432       O\\nATOM   1341  CB  ARG A 218      29.022   7.089  24.868  1.00 75.14           C\\nANISOU 1341  CB  ARG A 218    11692   8536   8320   1397  -4623    823       C\\nATOM   1342  N   ARG A 219      26.847   5.179  26.326  1.00 85.99           N\\nANISOU 1342  N   ARG A 219    14111   9803   8758    785  -4704   1599       N\\nATOM   1343  CA  ARG A 219      26.016   4.885  27.490  1.00 84.46           C\\nANISOU 1343  CA  ARG A 219    14260   9795   8035    425  -4645   1858       C\\nATOM   1344  C   ARG A 219      26.340   3.511  28.066  1.00 86.08           C\\nANISOU 1344  C   ARG A 219    14765   9710   8230    380  -4920   2118       C\\nATOM   1345  O   ARG A 219      26.501   3.361  29.283  1.00 90.06           O\\nANISOU 1345  O   ARG A 219    15467  10337   8414    256  -5076   2247       O\\nATOM   1346  CB  ARG A 219      24.539   4.978  27.102  1.00 85.75           C\\nANISOU 1346  CB  ARG A 219    14494  10127   7961    100  -4243   1970       C\\nATOM   1347  CG  ARG A 219      23.566   4.985  28.270  1.00 97.90           C\\nANISOU 1347  CG  ARG A 219    16277  12019   8900   -302  -4086   2160       C\\nATOM   1348  CD  ARG A 219      22.137   5.191  27.780  1.00103.51           C\\nANISOU 1348  CD  ARG A 219    16923  12951   9455   -597  -3619   2177       C\\nATOM   1349  NE  ARG A 219      22.015   6.380  26.940  1.00103.98           N\\nANISOU 1349  NE  ARG A 219    16513  13152   9842   -422  -3259   1780       N\\nATOM   1350  CZ  ARG A 219      21.746   7.599  27.400  1.00102.81           C\\nANISOU 1350  CZ  ARG A 219    16138  13388   9536   -439  -3032   1497       C\\nATOM   1351  NH1 ARG A 219      21.567   7.793  28.700  1.00112.25           N\\nANISOU 1351  NH1 ARG A 219    17509  14920  10223   -616  -3093   1534       N\\nATOM   1352  NH2 ARG A 219      21.656   8.624  26.563  1.00 90.07           N\\nANISOU 1352  NH2 ARG A 219    14137  11821   8266   -282  -2765   1173       N\\nATOM   1353  N   ARG A 220      26.443   2.493  27.205  1.00 85.93           N\\nANISOU 1353  N   ARG A 220    14788   9305   8558    483  -5002   2177       N\\nATOM   1354  CA  ARG A 220      26.753   1.145  27.680  1.00 92.53           C\\nANISOU 1354  CA  ARG A 220    15922   9808   9426    451  -5313   2391       C\\nATOM   1355  C   ARG A 220      28.118   1.092  28.355  1.00 98.18           C\\nANISOU 1355  C   ARG A 220    16600  10438  10265    730  -5700   2278       C\\nATOM   1356  O   ARG A 220      28.296   0.384  29.353  1.00 99.06           O\\nANISOU 1356  O   ARG A 220    17008  10452  10178    616  -5960   2492       O\\nATOM   1357  CB  ARG A 220      26.686   0.149  26.522  1.00 94.83           C\\nANISOU 1357  CB  ARG A 220    16221   9701  10109    561  -5350   2378       C\\nATOM   1358  CG  ARG A 220      25.281  -0.055  25.969  1.00100.75           C\\nANISOU 1358  CG  ARG A 220    17071  10487  10720    234  -5015   2543       C\\nATOM   1359  CD  ARG A 220      25.299  -0.715  24.596  1.00102.73           C\\nANISOU 1359  CD  ARG A 220    17220  10409  11403    417  -5011   2417       C\\nATOM   1360  NE  ARG A 220      23.971  -0.712  23.986  1.00105.76           N\\nANISOU 1360  NE  ARG A 220    17640  10872  11673    124  -4663   2533       N\\nATOM   1361  CZ  ARG A 220      23.743  -0.876  22.687  1.00111.13           C\\nANISOU 1361  CZ  ARG A 220    18166  11401  12658    249  -4533   2393       C\\nATOM   1362  NH1 ARG A 220      24.756  -1.052  21.850  1.00115.91           N\\nANISOU 1362  NH1 ARG A 220    18552  11801  13687    664  -4699   2115       N\\nATOM   1363  NH2 ARG A 220      22.500  -0.857  22.220  1.00109.07           N\\nANISOU 1363  NH2 ARG A 220    17943  11230  12267    -44  -4223   2509       N\\nATOM   1364  N   LYS A 221      29.096   1.832  27.826  1.00 87.90           N\\nANISOU 1364  N   LYS A 221    14922   9183   9293   1081  -5746   1943       N\\nATOM   1365  CA  LYS A 221      30.396   1.903  28.485  1.00 91.01           C\\nANISOU 1365  CA  LYS A 221    15227   9552   9800   1332  -6088   1803       C\\nATOM   1366  C   LYS A 221      30.311   2.643  29.815  1.00 92.81           C\\nANISOU 1366  C   LYS A 221    15563  10123   9576   1152  -6111   1881       C\\nATOM   1367  O   LYS A 221      31.080   2.348  30.738  1.00 97.14           O\\nANISOU 1367  O   LYS A 221    16229  10626  10054   1227  -6434   1922       O\\nATOM   1368  CB  LYS A 221      31.420   2.575  27.569  1.00 88.24           C\\nANISOU 1368  CB  LYS A 221    14391   9229   9907   1702  -6082   1409       C\\nATOM   1369  N   ARG A 222      29.386   3.599  29.935  1.00 89.90           N\\nANISOU 1369  N   ARG A 222    15156  10111   8890    923  -5782   1877       N\\nATOM   1370  CA  ARG A 222      29.220   4.328  31.190  1.00 91.86           C\\nANISOU 1370  CA  ARG A 222    15494  10740   8669    746  -5774   1897       C\\nATOM   1371  C   ARG A 222      28.375   3.544  32.190  1.00 96.10           C\\nANISOU 1371  C   ARG A 222    16450  11352   8712    379  -5763   2271       C\\nATOM   1372  O   ARG A 222      28.677   3.536  33.390  1.00100.34           O\\nANISOU 1372  O   ARG A 222    17145  12050   8928    306  -5948   2359       O\\nATOM   1373  CB  ARG A 222      28.596   5.698  30.923  1.00 87.62           C\\nANISOU 1373  CB  ARG A 222    14726  10572   7995    668  -5443   1670       C\\nATOM   1374  N   ASN A1002      27.322   2.874  31.712  1.00 85.72           N\\nANISOU 1374  N   ASN A1002    12716   9421  10431    154  -1889   1403       N\\nATOM   1375  CA  ASN A1002      26.456   2.104  32.601  1.00 78.54           C\\nANISOU 1375  CA  ASN A1002    11488   8720   9636    336  -1772   1042       C\\nATOM   1376  C   ASN A1002      27.206   0.951  33.259  1.00 74.17           C\\nANISOU 1376  C   ASN A1002    10829   8409   8943    253  -1283    980       C\\nATOM   1377  O   ASN A1002      26.974   0.646  34.435  1.00 77.99           O\\nANISOU 1377  O   ASN A1002    11066   9013   9552    361  -1151    748       O\\nATOM   1378  CB  ASN A1002      25.242   1.584  31.828  1.00 72.27           C\\nANISOU 1378  CB  ASN A1002    10694   8018   8747    370  -1959    956       C\\nATOM   1379  CG  ASN A1002      24.296   2.693  31.414  1.00 85.39           C\\nANISOU 1379  CG  ASN A1002    12363   9440  10641    548  -2522    954       C\\nATOM   1380  OD1 ASN A1002      24.569   3.871  31.643  1.00 91.93           O\\nANISOU 1380  OD1 ASN A1002    13249   9977  11701    641  -2774   1033       O\\nATOM   1381  ND2 ASN A1002      23.179   2.324  30.796  1.00 95.12           N\\nANISOU 1381  ND2 ASN A1002    13533  10764  11844    599  -2763    857       N\\nATOM   1382  N   ILE A1003      28.104   0.295  32.520  1.00 69.88           N\\nANISOU 1382  N   ILE A1003    10476   7942   8134     67  -1017   1180       N\\nATOM   1383  CA  ILE A1003      28.844  -0.824  33.094  1.00 75.25           C\\nANISOU 1383  CA  ILE A1003    11058   8796   8739     40   -607   1126       C\\nATOM   1384  C   ILE A1003      29.846  -0.336  34.137  1.00 79.70           C\\nANISOU 1384  C   ILE A1003    11473   9334   9474     69   -527   1154       C\\nATOM   1385  O   ILE A1003      30.117  -1.035  35.121  1.00 81.90           O\\nANISOU 1385  O   ILE A1003    11597   9734   9788    131   -334   1048       O\\nATOM   1386  CB  ILE A1003      29.526  -1.644  31.981  1.00 76.66           C\\nANISOU 1386  CB  ILE A1003    11445   9056   8624   -116   -342   1259       C\\nATOM   1387  CG1 ILE A1003      30.131  -2.927  32.553  1.00 83.23           C\\nANISOU 1387  CG1 ILE A1003    12171  10007   9446    -76     25   1164       C\\nATOM   1388  CG2 ILE A1003      30.599  -0.830  31.276  1.00 75.86           C\\nANISOU 1388  CG2 ILE A1003    11492   8897   8434   -279   -312   1524       C\\nATOM   1389  CD1 ILE A1003      30.765  -3.812  31.509  1.00 89.05           C\\nANISOU 1389  CD1 ILE A1003    13083  10813   9939   -170    311   1194       C\\nATOM   1390  N   PHE A1004      30.403   0.862  33.954  1.00 72.73           N\\nANISOU 1390  N   PHE A1004    10657   8281   8697      0   -708   1309       N\\nATOM   1391  CA  PHE A1004      31.300   1.419  34.961  1.00 72.86           C\\nANISOU 1391  CA  PHE A1004    10523   8260   8901      1   -698   1302       C\\nATOM   1392  C   PHE A1004      30.561   1.658  36.271  1.00 75.78           C\\nANISOU 1392  C   PHE A1004    10709   8641   9442    194   -837   1009       C\\nATOM   1393  O   PHE A1004      31.045   1.293  37.349  1.00 75.51           O\\nANISOU 1393  O   PHE A1004    10525   8740   9424    231   -703    911       O\\nATOM   1394  CB  PHE A1004      31.920   2.718  34.446  1.00 74.85           C\\nANISOU 1394  CB  PHE A1004    10908   8273   9256   -164   -904   1525       C\\nATOM   1395  CG  PHE A1004      32.831   3.387  35.431  1.00 80.49           C\\nANISOU 1395  CG  PHE A1004    11471   8921  10192   -205   -951   1497       C\\nATOM   1396  CD1 PHE A1004      34.093   2.876  35.685  1.00 79.31           C\\nANISOU 1396  CD1 PHE A1004    11166   8951  10018   -317   -675   1584       C\\nATOM   1397  CD2 PHE A1004      32.429   4.533  36.100  1.00 83.97           C\\nANISOU 1397  CD2 PHE A1004    11907   9110  10888   -118  -1297   1351       C\\nATOM   1398  CE1 PHE A1004      34.938   3.492  36.589  1.00 82.95           C\\nANISOU 1398  CE1 PHE A1004    11465   9368  10684   -377   -769   1550       C\\nATOM   1399  CE2 PHE A1004      33.269   5.154  37.007  1.00 85.07           C\\nANISOU 1399  CE2 PHE A1004    11928   9181  11215   -183  -1370   1289       C\\nATOM   1400  CZ  PHE A1004      34.525   4.633  37.251  1.00 84.25           C\\nANISOU 1400  CZ  PHE A1004    11666   9282  11062   -331  -1119   1402       C\\nATOM   1401  N   GLU A1005      29.376   2.270  36.194  1.00 75.34           N\\nANISOU 1401  N   GLU A1005    10654   8467   9503    325  -1114    852       N\\nATOM   1402  CA  GLU A1005      28.576   2.488  37.395  1.00 80.23           C\\nANISOU 1402  CA  GLU A1005    11062   9155  10266    516  -1188    504       C\\nATOM   1403  C   GLU A1005      28.115   1.169  38.000  1.00 86.02           C\\nANISOU 1403  C   GLU A1005    11656  10202  10825    527   -889    366       C\\nATOM   1404  O   GLU A1005      28.046   1.030  39.227  1.00 90.45           O\\nANISOU 1404  O   GLU A1005    12070  10923  11372    580   -788    167       O\\nATOM   1405  CB  GLU A1005      27.375   3.375  37.076  1.00 77.92           C\\nANISOU 1405  CB  GLU A1005    10741   8676  10189    694  -1544    334       C\\nATOM   1406  CG  GLU A1005      27.742   4.831  36.890  1.00 84.80           C\\nANISOU 1406  CG  GLU A1005    11751   9159  11311    720  -1903    409       C\\nATOM   1407  CD  GLU A1005      28.491   5.393  38.081  1.00 89.89           C\\nANISOU 1407  CD  GLU A1005    12315   9761  12076    724  -1883    248       C\\nATOM   1408  OE1 GLU A1005      27.991   5.262  39.219  1.00 89.61           O\\nANISOU 1408  OE1 GLU A1005    12069   9916  12064    880  -1796   -120       O\\nATOM   1409  OE2 GLU A1005      29.591   5.949  37.880  1.00 88.50           O\\nANISOU 1409  OE2 GLU A1005    12285   9394  11947    539  -1944    483       O\\nATOM   1410  N   MET A1006      27.798   0.187  37.153  1.00 78.13           N\\nANISOU 1410  N   MET A1006    10736   9284   9667    448   -755    474       N\\nATOM   1411  CA  MET A1006      27.337  -1.104  37.657  1.00 72.09           C\\nANISOU 1411  CA  MET A1006     9881   8748   8762    410   -494    376       C\\nATOM   1412  C   MET A1006      28.381  -1.755  38.553  1.00 75.65           C\\nANISOU 1412  C   MET A1006    10336   9295   9114    362   -262    468       C\\nATOM   1413  O   MET A1006      28.038  -2.402  39.549  1.00 76.42           O\\nANISOU 1413  O   MET A1006    10345   9565   9126    348   -119    363       O\\nATOM   1414  CB  MET A1006      26.994  -2.033  36.497  1.00 63.48           C\\nANISOU 1414  CB  MET A1006     8926   7661   7531    307   -419    476       C\\nATOM   1415  CG  MET A1006      26.279  -3.292  36.913  1.00 70.23           C\\nANISOU 1415  CG  MET A1006     9703   8684   8298    231   -215    360       C\\nATOM   1416  SD  MET A1006      26.609  -4.663  35.798  1.00 70.93           S\\nANISOU 1416  SD  MET A1006    10037   8714   8198     86    -29    502       S\\nATOM   1417  CE  MET A1006      25.235  -5.747  36.183  1.00 79.60           C\\nANISOU 1417  CE  MET A1006    11010   9948   9288    -46     55    311       C\\nATOM   1418  N   LEU A1007      29.660  -1.591  38.223  1.00 74.32           N\\nANISOU 1418  N   LEU A1007    10257   9030   8951    321   -234    678       N\\nATOM   1419  CA  LEU A1007      30.716  -2.231  38.992  1.00 72.19           C\\nANISOU 1419  CA  LEU A1007     9955   8841   8633    310    -74    777       C\\nATOM   1420  C   LEU A1007      31.310  -1.346  40.078  1.00 77.91           C\\nANISOU 1420  C   LEU A1007    10574   9585   9442    343   -217    715       C\\nATOM   1421  O   LEU A1007      31.846  -1.881  41.054  1.00 81.18           O\\nANISOU 1421  O   LEU A1007    10944  10120   9781    352   -154    740       O\\nATOM   1422  CB  LEU A1007      31.835  -2.718  38.066  1.00 71.02           C\\nANISOU 1422  CB  LEU A1007     9882   8633   8470    261     76    992       C\\nATOM   1423  CG  LEU A1007      31.556  -4.102  37.475  1.00 67.80           C\\nANISOU 1423  CG  LEU A1007     9585   8237   7941    251    288   1010       C\\nATOM   1424  CD1 LEU A1007      30.727  -4.015  36.198  1.00 65.13           C\\nANISOU 1424  CD1 LEU A1007     9386   7844   7514    183    249    974       C\\nATOM   1425  CD2 LEU A1007      32.848  -4.848  37.236  1.00 68.79           C\\nANISOU 1425  CD2 LEU A1007     9698   8348   8090    287    481   1140       C\\nATOM   1426  N   ARG A1008      31.232  -0.018  39.954  1.00 81.15           N\\nANISOU 1426  N   ARG A1008    10972   9855  10007    355   -447    635       N\\nATOM   1427  CA  ARG A1008      31.610   0.793  41.106  1.00 79.83           C\\nANISOU 1427  CA  ARG A1008    10721   9701   9912    383   -602    485       C\\nATOM   1428  C   ARG A1008      30.583   0.693  42.224  1.00 79.95           C\\nANISOU 1428  C   ARG A1008    10660   9903   9815    473   -581    181       C\\nATOM   1429  O   ARG A1008      30.878   1.089  43.357  1.00 82.62           O\\nANISOU 1429  O   ARG A1008    10953  10337  10104    486   -655     22       O\\nATOM   1430  CB  ARG A1008      31.814   2.257  40.711  1.00 75.25           C\\nANISOU 1430  CB  ARG A1008    10178   8848   9565    361   -878    461       C\\nATOM   1431  CG  ARG A1008      30.548   3.009  40.384  1.00 84.73           C\\nANISOU 1431  CG  ARG A1008    11405   9893  10893    488  -1070    258       C\\nATOM   1432  CD  ARG A1008      30.759   4.502  40.562  1.00 91.79           C\\nANISOU 1432  CD  ARG A1008    12342  10481  12053    509  -1399    147       C\\nATOM   1433  NE  ARG A1008      30.802   4.870  41.973  1.00 97.78           N\\nANISOU 1433  NE  ARG A1008    12996  11338  12815    587  -1451   -187       N\\nATOM   1434  CZ  ARG A1008      29.731   5.209  42.684  1.00100.58           C\\nANISOU 1434  CZ  ARG A1008    13254  11756  13206    785  -1504   -595       C\\nATOM   1435  NH1 ARG A1008      28.534   5.231  42.111  1.00 94.43           N\\nANISOU 1435  NH1 ARG A1008    12420  10935  12522    941  -1541   -707       N\\nATOM   1436  NH2 ARG A1008      29.857   5.526  43.966  1.00105.64           N\\nANISOU 1436  NH2 ARG A1008    13834  12529  13777    825  -1520   -917       N\\nATOM   1437  N   ILE A1009      29.394   0.171  41.926  1.00 74.25           N\\nANISOU 1437  N   ILE A1009     9910   9267   9034    507   -473     81       N\\nATOM   1438  CA  ILE A1009      28.416  -0.151  42.956  1.00 75.30           C\\nANISOU 1438  CA  ILE A1009     9929   9661   9019    531   -350   -186       C\\nATOM   1439  C   ILE A1009      28.680  -1.535  43.536  1.00 78.79           C\\nANISOU 1439  C   ILE A1009    10438  10305   9194    403   -107     -8       C\\nATOM   1440  O   ILE A1009      28.534  -1.752  44.743  1.00 85.17           O\\nANISOU 1440  O   ILE A1009    11227  11348   9787    355    -20   -120       O\\nATOM   1441  CB  ILE A1009      26.996  -0.039  42.373  1.00 72.07           C\\nANISOU 1441  CB  ILE A1009     9394   9267   8722    603   -364   -387       C\\nATOM   1442  CG1 ILE A1009      26.670   1.415  42.030  1.00 73.75           C\\nANISOU 1442  CG1 ILE A1009     9547   9243   9230    783   -675   -591       C\\nATOM   1443  CG2 ILE A1009      25.968  -0.620  43.332  1.00 70.49           C\\nANISOU 1443  CG2 ILE A1009     9027   9408   8349    556   -136   -634       C\\nATOM   1444  CD1 ILE A1009      25.423   1.572  41.190  1.00 76.17           C\\nANISOU 1444  CD1 ILE A1009     9730   9499   9713    890   -796   -718       C\\nATOM   1445  N   ASP A1010      29.079  -2.490  42.694  1.00 72.06           N\\nANISOU 1445  N   ASP A1010     9694   9350   8336    343     -7    269       N\\nATOM   1446  CA  ASP A1010      29.286  -3.870  43.127  1.00 72.56           C\\nANISOU 1446  CA  ASP A1010     9858   9501   8210    243    179    457       C\\nATOM   1447  C   ASP A1010      30.708  -4.106  43.629  1.00 75.95           C\\nANISOU 1447  C   ASP A1010    10352   9894   8612    272    117    675       C\\nATOM   1448  O   ASP A1010      30.908  -4.550  44.763  1.00 79.91           O\\nANISOU 1448  O   ASP A1010    10905  10541   8916    226    124    730       O\\nATOM   1449  CB  ASP A1010      28.966  -4.834  41.979  1.00 68.87           C\\nANISOU 1449  CB  ASP A1010     9481   8902   7784    190    300    582       C\\nATOM   1450  CG  ASP A1010      27.482  -4.951  41.709  1.00 73.05           C\\nANISOU 1450  CG  ASP A1010     9921   9528   8308    113    358    385       C\\nATOM   1451  OD1 ASP A1010      26.693  -4.307  42.432  1.00 67.48           O\\nANISOU 1451  OD1 ASP A1010     9046   9009   7582    124    341    140       O\\nATOM   1452  OD2 ASP A1010      27.105  -5.691  40.773  1.00 78.54           O\\nANISOU 1452  OD2 ASP A1010    10691  10123   9026     43    418    440       O\\nATOM   1453  N   GLU A1011      31.702  -3.824  42.788  1.00 76.16           N\\nANISOU 1453  N   GLU A1011    10363   9749   8825    334     50    808       N\\nATOM   1454  CA  GLU A1011      33.088  -4.089  43.149  1.00 80.16           C\\nANISOU 1454  CA  GLU A1011    10842  10236   9377    379    -14    997       C\\nATOM   1455  C   GLU A1011      33.663  -2.965  44.003  1.00 86.62           C\\nANISOU 1455  C   GLU A1011    11560  11131  10222    377   -238    897       C\\nATOM   1456  O   GLU A1011      34.212  -3.213  45.081  1.00 98.58           O\\nANISOU 1456  O   GLU A1011    13076  12768  11614    380   -345    952       O\\nATOM   1457  CB  GLU A1011      33.926  -4.284  41.885  1.00 82.54           C\\nANISOU 1457  CB  GLU A1011    11111  10383   9867    418     68   1140       C\\nATOM   1458  CG  GLU A1011      35.344  -4.765  42.134  1.00 89.74           C\\nANISOU 1458  CG  GLU A1011    11913  11291  10894    502     40   1313       C\\nATOM   1459  CD  GLU A1011      35.393  -6.223  42.539  1.00 95.34           C\\nANISOU 1459  CD  GLU A1011    12731  11959  11534    586    111   1445       C\\nATOM   1460  OE1 GLU A1011      35.895  -6.518  43.646  1.00 99.56           O\\nANISOU 1460  OE1 GLU A1011    13255  12559  12013    632    -51   1549       O\\nATOM   1461  OE2 GLU A1011      34.920  -7.072  41.751  1.00 94.59           O\\nANISOU 1461  OE2 GLU A1011    12763  11742  11436    596    295   1450       O\\nATOM   1462  N   GLY A1012      33.549  -1.725  43.534  1.00 83.15           N\\nANISOU 1462  N   GLY A1012    11062  10592   9938    362   -351    758       N\\nATOM   1463  CA  GLY A1012      34.064  -0.590  44.272  1.00 80.42           C\\nANISOU 1463  CA  GLY A1012    10644  10253   9660    339   -589    621       C\\nATOM   1464  C   GLY A1012      35.145   0.176  43.536  1.00 76.41           C\\nANISOU 1464  C   GLY A1012    10041   9573   9418    270   -701    745       C\\nATOM   1465  O   GLY A1012      36.026  -0.422  42.909  1.00 75.35           O\\nANISOU 1465  O   GLY A1012     9829   9430   9369    254   -588    972       O\\nATOM   1466  N   LEU A1013      35.090   1.505  43.610  1.00 72.47           N\\nANISOU 1466  N   LEU A1013     9539   8928   9066    216   -914    581       N\\nATOM   1467  CA  LEU A1013      36.059   2.381  42.960  1.00 75.06           C\\nANISOU 1467  CA  LEU A1013     9799   9069   9653     69  -1037    711       C\\nATOM   1468  C   LEU A1013      37.076   2.842  43.998  1.00 85.43           C\\nANISOU 1468  C   LEU A1013    10980  10447  11031    -12  -1266    645       C\\nATOM   1469  O   LEU A1013      36.730   3.569  44.935  1.00 92.30           O\\nANISOU 1469  O   LEU A1013    11906  11301  11864      3  -1478    364       O\\nATOM   1470  CB  LEU A1013      35.362   3.575  42.309  1.00 76.93           C\\nANISOU 1470  CB  LEU A1013    10164   9014  10053     35  -1188    614       C\\nATOM   1471  CG  LEU A1013      36.264   4.677  41.743  1.00 81.85           C\\nANISOU 1471  CG  LEU A1013    10778   9382  10939   -188  -1361    759       C\\nATOM   1472  CD1 LEU A1013      37.119   4.145  40.607  1.00 83.65           C\\nANISOU 1472  CD1 LEU A1013    10936   9672  11176   -345  -1119   1104       C\\nATOM   1473  CD2 LEU A1013      35.444   5.879  41.290  1.00 79.42           C\\nANISOU 1473  CD2 LEU A1013    10661   8711  10803   -183  -1600    657       C\\nATOM   1474  N   ARG A1014      38.324   2.416  43.830  1.00 82.30           N\\nANISOU 1474  N   ARG A1014    10388  10143  10740    -92  -1229    865       N\\nATOM   1475  CA  ARG A1014      39.431   2.846  44.673  1.00 87.70           C\\nANISOU 1475  CA  ARG A1014    10885  10900  11537   -200  -1487    834       C\\nATOM   1476  C   ARG A1014      40.374   3.720  43.858  1.00 91.11           C\\nANISOU 1476  C   ARG A1014    11154  11170  12293   -454  -1533    970       C\\nATOM   1477  O   ARG A1014      40.854   3.301  42.800  1.00 93.58           O\\nANISOU 1477  O   ARG A1014    11348  11510  12699   -513  -1278   1201       O\\nATOM   1478  CB  ARG A1014      40.189   1.647  45.242  1.00 89.70           C\\nANISOU 1478  CB  ARG A1014    10969  11409  11702    -83  -1465    977       C\\nATOM   1479  CG  ARG A1014      39.445   0.867  46.311  1.00 95.14           C\\nANISOU 1479  CG  ARG A1014    11845  12266  12037     80  -1493    888       C\\nATOM   1480  CD  ARG A1014      40.338   0.658  47.527  1.00103.70           C\\nANISOU 1480  CD  ARG A1014    12817  13547  13039     82  -1799    903       C\\nATOM   1481  NE  ARG A1014      39.801  -0.327  48.462  1.00107.67           N\\nANISOU 1481  NE  ARG A1014    13522  14230  13160    204  -1802    939       N\\nATOM   1482  CZ  ARG A1014      40.399  -0.677  49.597  1.00111.85           C\\nANISOU 1482  CZ  ARG A1014    14048  14948  13504    219  -2094    997       C\\nATOM   1483  NH1 ARG A1014      41.553  -0.119  49.939  1.00113.46           N\\nANISOU 1483  NH1 ARG A1014    14008  15196  13905    140  -2424    984       N\\nATOM   1484  NH2 ARG A1014      39.844  -1.584  50.391  1.00112.62           N\\nANISOU 1484  NH2 ARG A1014    14392  15192  13208    282  -2078   1085       N\\nATOM   1485  N   LEU A1015      40.648   4.926  44.357  1.00 92.65           N\\nANISOU 1485  N   LEU A1015    11353  11202  12646   -633  -1845    811       N\\nATOM   1486  CA  LEU A1015      41.453   5.897  43.627  1.00 98.42           C\\nANISOU 1486  CA  LEU A1015    11974  11728  13694   -955  -1914    952       C\\nATOM   1487  C   LEU A1015      42.928   5.886  44.013  1.00100.85           C\\nANISOU 1487  C   LEU A1015    11893  12218  14209  -1148  -2036   1034       C\\nATOM   1488  O   LEU A1015      43.750   6.434  43.268  1.00 98.40           O\\nANISOU 1488  O   LEU A1015    11399  11829  14161  -1460  -1984   1214       O\\nATOM   1489  CB  LEU A1015      40.885   7.309  43.827  1.00 99.65           C\\nANISOU 1489  CB  LEU A1015    12381  11497  13985  -1071  -2220    736       C\\nATOM   1490  CG  LEU A1015      39.471   7.567  43.292  1.00 99.54           C\\nANISOU 1490  CG  LEU A1015    12694  11242  13885   -893  -2166    655       C\\nATOM   1491  CD1 LEU A1015      39.000   8.964  43.667  1.00 99.18           C\\nANISOU 1491  CD1 LEU A1015    12859  10780  14044   -939  -2532    377       C\\nATOM   1492  CD2 LEU A1015      39.410   7.369  41.782  1.00 97.70           C\\nANISOU 1492  CD2 LEU A1015    12526  10927  13670   -996  -1904   1008       C\\nATOM   1493  N   LYS A1016      43.285   5.285  45.145  1.00105.59           N\\nANISOU 1493  N   LYS A1016    12353  13074  14693   -995  -2209    921       N\\nATOM   1494  CA  LYS A1016      44.673   5.127  45.549  1.00101.07           C\\nANISOU 1494  CA  LYS A1016    11354  12717  14330  -1119  -2373    997       C\\nATOM   1495  C   LYS A1016      45.057   3.654  45.506  1.00 97.42           C\\nANISOU 1495  C   LYS A1016    10673  12549  13792   -837  -2171   1168       C\\nATOM   1496  O   LYS A1016      44.204   2.765  45.581  1.00 93.98           O\\nANISOU 1496  O   LYS A1016    10480  12152  13076   -558  -2006   1179       O\\nATOM   1497  CB  LYS A1016      44.913   5.693  46.953  1.00 96.36           C\\nANISOU 1497  CB  LYS A1016    10775  12159  13680  -1180  -2856    730       C\\nATOM   1498  N   ILE A1017      46.361   3.401  45.382  1.00 93.92           N\\nANISOU 1498  N   ILE A1017     9745  12296  13643   -915  -2196   1291       N\\nATOM   1499  CA  ILE A1017      46.835   2.030  45.257  1.00 95.27           C\\nANISOU 1499  CA  ILE A1017     9663  12692  13845   -609  -2025   1434       C\\nATOM   1500  C   ILE A1017      46.498   1.247  46.517  1.00 93.58           C\\nANISOU 1500  C   ILE A1017     9634  12578  13344   -317  -2322   1390       C\\nATOM   1501  O   ILE A1017      46.630   1.745  47.643  1.00 98.49           O\\nANISOU 1501  O   ILE A1017    10306  13255  13861   -400  -2751   1258       O\\nATOM   1502  CB  ILE A1017      48.346   2.013  44.968  1.00 99.88           C\\nANISOU 1502  CB  ILE A1017     9604  13484  14862   -733  -2035   1517       C\\nATOM   1503  CG1 ILE A1017      48.641   2.776  43.677  1.00 99.15           C\\nANISOU 1503  CG1 ILE A1017     9368  13325  14980  -1097  -1674   1598       C\\nATOM   1504  CG2 ILE A1017      48.859   0.586  44.863  1.00102.32           C\\nANISOU 1504  CG2 ILE A1017     9624  13983  15272   -342  -1894   1617       C\\nATOM   1505  CD1 ILE A1017      50.072   2.657  43.214  1.00100.19           C\\nANISOU 1505  CD1 ILE A1017     8808  13728  15530  -1237  -1535   1668       C\\nATOM   1506  N   TYR A1018      46.040   0.013  46.328  1.00 96.96           N\\nANISOU 1506  N   TYR A1018    10204  13021  13613     -4  -2100   1503       N\\nATOM   1507  CA  TYR A1018      45.693  -0.867  47.432  1.00100.96           C\\nANISOU 1507  CA  TYR A1018    10937  13603  13821    241  -2341   1544       C\\nATOM   1508  C   TYR A1018      45.961  -2.303  47.006  1.00113.96           C\\nANISOU 1508  C   TYR A1018    12472  15250  15576    569  -2149   1734       C\\nATOM   1509  O   TYR A1018      46.224  -2.587  45.835  1.00121.07           O\\nANISOU 1509  O   TYR A1018    13172  16106  16722    616  -1774   1767       O\\nATOM   1510  CB  TYR A1018      44.232  -0.693  47.850  1.00 93.06           C\\nANISOU 1510  CB  TYR A1018    10474  12514  12372    220  -2278   1421       C\\nATOM   1511  CG  TYR A1018      43.253  -1.208  46.822  1.00 94.64           C\\nANISOU 1511  CG  TYR A1018    10901  12566  12493    308  -1824   1465       C\\nATOM   1512  CD1 TYR A1018      43.069  -0.541  45.617  1.00 98.44           C\\nANISOU 1512  CD1 TYR A1018    11346  12911  13146    160  -1544   1428       C\\nATOM   1513  CD2 TYR A1018      42.513  -2.358  47.053  1.00 92.36           C\\nANISOU 1513  CD2 TYR A1018    10884  12266  11944    505  -1704   1563       C\\nATOM   1514  CE1 TYR A1018      42.179  -1.007  44.669  1.00 97.08           C\\nANISOU 1514  CE1 TYR A1018    11389  12624  12873    230  -1183   1460       C\\nATOM   1515  CE2 TYR A1018      41.614  -2.831  46.111  1.00 95.41           C\\nANISOU 1515  CE2 TYR A1018    11463  12519  12271    556  -1325   1577       C\\nATOM   1516  CZ  TYR A1018      41.450  -2.147  44.923  1.00 96.24           C\\nANISOU 1516  CZ  TYR A1018    11515  12518  12534    430  -1079   1511       C\\nATOM   1517  OH  TYR A1018      40.562  -2.611  43.980  1.00 94.30           O\\nANISOU 1517  OH  TYR A1018    11469  12159  12201    471   -755   1517       O\\nATOM   1518  N   LYS A1019      45.882  -3.212  47.972  1.00112.29           N\\nANISOU 1518  N   LYS A1019    12428  15075  15161    787  -2416   1854       N\\nATOM   1519  CA  LYS A1019      46.124  -4.629  47.736  1.00114.49           C\\nANISOU 1519  CA  LYS A1019    12662  15272  15567   1129  -2330   2040       C\\nATOM   1520  C   LYS A1019      44.796  -5.365  47.616  1.00112.47           C\\nANISOU 1520  C   LYS A1019    12933  14846  14954   1191  -2067   2094       C\\nATOM   1521  O   LYS A1019      43.893  -5.162  48.435  1.00114.99           O\\nANISOU 1521  O   LYS A1019    13645  15200  14846   1061  -2176   2073       O\\nATOM   1522  CB  LYS A1019      46.964  -5.233  48.863  1.00116.93           C\\nANISOU 1522  CB  LYS A1019    12829  15675  15923   1330  -2866   2206       C\\nATOM   1523  N   ASP A1020      44.677  -6.212  46.597  1.00112.39           N\\nANISOU 1523  N   ASP A1020    12914  14672  15118   1369  -1707   2129       N\\nATOM   1524  CA  ASP A1020      43.491  -7.038  46.453  1.00108.38           C\\nANISOU 1524  CA  ASP A1020    12868  13981  14329   1415  -1485   2186       C\\nATOM   1525  C   ASP A1020      43.556  -8.206  47.436  1.00111.34           C\\nANISOU 1525  C   ASP A1020    13459  14255  14590   1619  -1796   2432       C\\nATOM   1526  O   ASP A1020      44.475  -8.316  48.253  1.00111.64           O\\nANISOU 1526  O   ASP A1020    13307  14376  14734   1741  -2219   2559       O\\nATOM   1527  CB  ASP A1020      43.344  -7.520  45.010  1.00103.84           C\\nANISOU 1527  CB  ASP A1020    12244  13254  13957   1507  -1026   2105       C\\nATOM   1528  CG  ASP A1020      44.444  -8.477  44.594  1.00108.01           C\\nANISOU 1528  CG  ASP A1020    12440  13694  14903   1844  -1010   2150       C\\nATOM   1529  OD1 ASP A1020      45.525  -8.453  45.217  1.00113.64           O\\nANISOU 1529  OD1 ASP A1020    12802  14515  15861   1981  -1346   2220       O\\nATOM   1530  OD2 ASP A1020      44.228  -9.253  43.639  1.00105.75           O\\nANISOU 1530  OD2 ASP A1020    12227  13235  14718   1987   -677   2082       O\\nATOM   1531  N   THR A1021      42.571  -9.101  47.357  1.00111.86           N\\nANISOU 1531  N   THR A1021    13936  14124  14441   1634  -1618   2524       N\\nATOM   1532  CA  THR A1021      42.498 -10.201  48.311  1.00111.37           C\\nANISOU 1532  CA  THR A1021    14180  13918  14216   1754  -1913   2816       C\\nATOM   1533  C   THR A1021      43.592 -11.242  48.108  1.00113.87           C\\nANISOU 1533  C   THR A1021    14272  14000  14994   2154  -2104   2966       C\\nATOM   1534  O   THR A1021      43.713 -12.150  48.936  1.00122.97           O\\nANISOU 1534  O   THR A1021    15669  14982  16073   2291  -2453   3261       O\\nATOM   1535  CB  THR A1021      41.130 -10.879  48.236  1.00106.11           C\\nANISOU 1535  CB  THR A1021    14000  13085  13230   1600  -1650   2877       C\\nATOM   1536  OG1 THR A1021      40.997 -11.555  46.980  1.00101.52           O\\nANISOU 1536  OG1 THR A1021    13390  12234  12949   1746  -1308   2783       O\\nATOM   1537  CG2 THR A1021      40.020  -9.844  48.372  1.00105.59           C\\nANISOU 1537  CG2 THR A1021    14074  13265  12778   1259  -1443   2671       C\\nATOM   1538  N   GLU A1022      44.388 -11.136  47.045  1.00109.65           N\\nANISOU 1538  N   GLU A1022    13282  13452  14927   2346  -1889   2772       N\\nATOM   1539  CA  GLU A1022      45.477 -12.070  46.790  1.00109.91           C\\nANISOU 1539  CA  GLU A1022    13002  13289  15472   2780  -2033   2824       C\\nATOM   1540  C   GLU A1022      46.850 -11.447  47.014  1.00110.30           C\\nANISOU 1540  C   GLU A1022    12423  13602  15882   2906  -2315   2766       C\\nATOM   1541  O   GLU A1022      47.866 -12.107  46.769  1.00114.91           O\\nANISOU 1541  O   GLU A1022    12609  14084  16969   3299  -2431   2752       O\\nATOM   1542  CB  GLU A1022      45.376 -12.625  45.367  1.00110.94           C\\nANISOU 1542  CB  GLU A1022    13056  13217  15878   2939  -1526   2594       C\\nATOM   1543  N   GLY A1023      46.907 -10.195  47.471  1.00108.89           N\\nANISOU 1543  N   GLY A1023    12123  13753  15498   2586  -2436   2704       N\\nATOM   1544  CA  GLY A1023      48.156  -9.536  47.793  1.00110.44           C\\nANISOU 1544  CA  GLY A1023    11736  14212  16013   2619  -2755   2653       C\\nATOM   1545  C   GLY A1023      48.709  -8.632  46.710  1.00113.05           C\\nANISOU 1545  C   GLY A1023    11548  14751  16654   2465  -2360   2382       C\\nATOM   1546  O   GLY A1023      49.639  -7.862  46.986  1.00112.39           O\\nANISOU 1546  O   GLY A1023    10982  14921  16798   2361  -2597   2323       O\\nATOM   1547  N   TYR A1024      48.174  -8.700  45.495  1.00108.30           N\\nANISOU 1547  N   TYR A1024    11043  14058  16046   2411  -1784   2230       N\\nATOM   1548  CA  TYR A1024      48.663  -7.880  44.398  1.00113.34           C\\nANISOU 1548  CA  TYR A1024    11259  14900  16907   2217  -1372   2019       C\\nATOM   1549  C   TYR A1024      48.186  -6.439  44.545  1.00111.52           C\\nANISOU 1549  C   TYR A1024    11170  14816  16386   1738  -1381   1979       C\\nATOM   1550  O   TYR A1024      47.084  -6.173  45.033  1.00110.91           O\\nANISOU 1550  O   TYR A1024    11615  14645  15882   1574  -1459   2021       O\\nATOM   1551  CB  TYR A1024      48.188  -8.447  43.060  1.00116.94           C\\nANISOU 1551  CB  TYR A1024    11856  15216  17360   2297   -787   1879       C\\nATOM   1552  CG  TYR A1024      48.578  -9.890  42.820  1.00122.30           C\\nANISOU 1552  CG  TYR A1024    12446  15674  18349   2790   -744   1850       C\\nATOM   1553  CD1 TYR A1024      49.830 -10.364  43.189  1.00128.61           C\\nANISOU 1553  CD1 TYR A1024    12689  16530  19645   3150  -1024   1848       C\\nATOM   1554  CD2 TYR A1024      47.689 -10.779  42.227  1.00118.01           C\\nANISOU 1554  CD2 TYR A1024    12364  14836  17638   2906   -460   1804       C\\nATOM   1555  CE1 TYR A1024      50.188 -11.681  42.970  1.00131.77           C\\nANISOU 1555  CE1 TYR A1024    13011  16664  20391   3655  -1019   1793       C\\nATOM   1556  CE2 TYR A1024      48.037 -12.096  42.004  1.00120.38           C\\nANISOU 1556  CE2 TYR A1024    12621  14859  18257   3363   -444   1744       C\\nATOM   1557  CZ  TYR A1024      49.287 -12.542  42.377  1.00129.11           C\\nANISOU 1557  CZ  TYR A1024    13187  15991  19879   3758   -723   1736       C\\nATOM   1558  OH  TYR A1024      49.639 -13.855  42.158  1.00133.04           O\\nANISOU 1558  OH  TYR A1024    13642  16152  20756   4269   -742   1651       O\\nATOM   1559  N   TYR A1025      49.029  -5.504  44.113  1.00117.71           N\\nANISOU 1559  N   TYR A1025    11469  15821  17433   1507  -1294   1881       N\\nATOM   1560  CA  TYR A1025      48.682  -4.087  44.152  1.00110.35           C\\nANISOU 1560  CA  TYR A1025    10659  14955  16314   1049  -1319   1834       C\\nATOM   1561  C   TYR A1025      47.758  -3.760  42.985  1.00104.43           C\\nANISOU 1561  C   TYR A1025    10246  14092  15339    855   -821   1781       C\\nATOM   1562  O   TYR A1025      48.115  -3.979  41.822  1.00101.17           O\\nANISOU 1562  O   TYR A1025     9617  13740  15082    859   -384   1729       O\\nATOM   1563  CB  TYR A1025      49.939  -3.221  44.101  1.00111.84           C\\nANISOU 1563  CB  TYR A1025    10220  15385  16890    814  -1427   1782       C\\nATOM   1564  CG  TYR A1025      50.892  -3.432  45.257  1.00115.51           C\\nANISOU 1564  CG  TYR A1025    10303  15992  17595    978  -1998   1822       C\\nATOM   1565  CD1 TYR A1025      50.776  -2.688  46.423  1.00114.38           C\\nANISOU 1565  CD1 TYR A1025    10332  15875  17252    775  -2517   1825       C\\nATOM   1566  CD2 TYR A1025      51.915  -4.369  45.177  1.00120.42           C\\nANISOU 1566  CD2 TYR A1025    10384  16722  18646   1352  -2046   1830       C\\nATOM   1567  CE1 TYR A1025      51.647  -2.875  47.481  1.00116.89           C\\nANISOU 1567  CE1 TYR A1025    10328  16345  17742    906  -3095   1869       C\\nATOM   1568  CE2 TYR A1025      52.791  -4.563  46.228  1.00124.27           C\\nANISOU 1568  CE2 TYR A1025    10509  17338  19372   1522  -2643   1887       C\\nATOM   1569  CZ  TYR A1025      52.653  -3.813  47.377  1.00124.31           C\\nANISOU 1569  CZ  TYR A1025    10724  17386  19121   1279  -3180   1923       C\\nATOM   1570  OH  TYR A1025      53.523  -4.004  48.428  1.00131.17           O\\nANISOU 1570  OH  TYR A1025    11258  18402  20177   1430  -3829   1986       O\\nATOM   1571  N   THR A1026      46.569  -3.247  43.288  1.00104.70           N\\nANISOU 1571  N   THR A1026    10799  13985  14997    692   -893   1776       N\\nATOM   1572  CA  THR A1026      45.596  -2.892  42.268  1.00105.81           C\\nANISOU 1572  CA  THR A1026    11282  14002  14919    524   -528   1739       C\\nATOM   1573  C   THR A1026      45.108  -1.467  42.499  1.00102.55           C\\nANISOU 1573  C   THR A1026    11058  13525  14382    179   -701   1694       C\\nATOM   1574  O   THR A1026      45.449  -0.819  43.493  1.00 98.86           O\\nANISOU 1574  O   THR A1026    10500  13102  13962     75  -1083   1653       O\\nATOM   1575  CB  THR A1026      44.400  -3.858  42.255  1.00102.47           C\\nANISOU 1575  CB  THR A1026    11323  13413  14198    735   -413   1745       C\\nATOM   1576  OG1 THR A1026      43.497  -3.517  43.312  1.00 98.43           O\\nANISOU 1576  OG1 THR A1026    11152  12846  13400    677   -704   1728       O\\nATOM   1577  CG2 THR A1026      44.861  -5.301  42.437  1.00103.30           C\\nANISOU 1577  CG2 THR A1026    11315  13487  14447   1108   -410   1798       C\\nATOM   1578  N   ILE A1027      44.296  -0.982  41.560  1.00 99.57           N\\nANISOU 1578  N   ILE A1027    10963  13018  13850     15   -450   1686       N\\nATOM   1579  CA  ILE A1027      43.734   0.361  41.638  1.00 94.27           C\\nANISOU 1579  CA  ILE A1027    10513  12198  13107   -265   -621   1637       C\\nATOM   1580  C   ILE A1027      42.483   0.419  40.770  1.00 89.78           C\\nANISOU 1580  C   ILE A1027    10350  11463  12301   -276   -407   1635       C\\nATOM   1581  O   ILE A1027      42.233  -0.483  39.962  1.00 86.52           O\\nANISOU 1581  O   ILE A1027    10008  11080  11787   -145    -97   1677       O\\nATOM   1582  CB  ILE A1027      44.771   1.417  41.213  1.00 89.65           C\\nANISOU 1582  CB  ILE A1027     9615  11643  12803   -620   -639   1700       C\\nATOM   1583  CG1 ILE A1027      44.397   2.796  41.761  1.00 84.69           C\\nANISOU 1583  CG1 ILE A1027     9187  10803  12189   -869   -988   1614       C\\nATOM   1584  CG2 ILE A1027      44.914   1.453  39.698  1.00 80.58           C\\nANISOU 1584  CG2 ILE A1027     8450  10512  11654   -794   -204   1829       C\\nATOM   1585  CD1 ILE A1027      45.403   3.866  41.434  1.00 82.74           C\\nANISOU 1585  CD1 ILE A1027     8667  10528  12241  -1282  -1056   1694       C\\nATOM   1586  N   GLY A1028      41.681   1.469  40.938  1.00 90.15           N\\nANISOU 1586  N   GLY A1028    10659  11318  12274   -414   -605   1560       N\\nATOM   1587  CA  GLY A1028      40.491   1.617  40.118  1.00 84.64           C\\nANISOU 1587  CA  GLY A1028    10306  10458  11396   -412   -482   1559       C\\nATOM   1588  C   GLY A1028      39.429   0.607  40.504  1.00 83.32           C\\nANISOU 1588  C   GLY A1028    10333  10329  10994   -142   -422   1455       C\\nATOM   1589  O   GLY A1028      39.140   0.390  41.685  1.00 81.04           O\\nANISOU 1589  O   GLY A1028    10066  10102  10624    -17   -599   1333       O\\nATOM   1590  N   ILE A1029      38.832  -0.021  39.494  1.00 90.61           N\\nANISOU 1590  N   ILE A1029    11415  11232  11782    -90   -168   1506       N\\nATOM   1591  CA  ILE A1029      37.857  -1.077  39.728  1.00 88.98           C\\nANISOU 1591  CA  ILE A1029    11375  11052  11381    109    -82   1426       C\\nATOM   1592  C   ILE A1029      38.467  -2.405  39.306  1.00 96.86           C\\nANISOU 1592  C   ILE A1029    12278  12138  12386    239    180   1504       C\\nATOM   1593  O   ILE A1029      38.305  -2.841  38.160  1.00 98.47           O\\nANISOU 1593  O   ILE A1029    12577  12322  12515    224    426   1527       O\\nATOM   1594  CB  ILE A1029      36.538  -0.812  38.980  1.00 75.33           C\\nANISOU 1594  CB  ILE A1029     9908   9202   9511     82    -63   1368       C\\nATOM   1595  CG1 ILE A1029      35.978   0.560  39.350  1.00 71.56           C\\nANISOU 1595  CG1 ILE A1029     9501   8581   9108     11   -352   1261       C\\nATOM   1596  CG2 ILE A1029      35.522  -1.900  39.298  1.00 63.88           C\\nANISOU 1596  CG2 ILE A1029     8583   7799   7889    229     23   1272       C\\nATOM   1597  CD1 ILE A1029      34.589   0.806  38.813  1.00 68.30           C\\nANISOU 1597  CD1 ILE A1029     9287   8054   8610     55   -413   1168       C\\nATOM   1598  N   GLY A1030      39.179  -3.050  40.226  1.00 99.15           N\\nANISOU 1598  N   GLY A1030    12396  12511  12765    380    101   1529       N\\nATOM   1599  CA  GLY A1030      39.787  -4.335  39.947  1.00 98.18           C\\nANISOU 1599  CA  GLY A1030    12171  12410  12722    571    291   1577       C\\nATOM   1600  C   GLY A1030      40.760  -4.288  38.789  1.00 94.57           C\\nANISOU 1600  C   GLY A1030    11485  12025  12421    523    562   1598       C\\nATOM   1601  O   GLY A1030      40.506  -4.869  37.728  1.00 95.69           O\\nANISOU 1601  O   GLY A1030    11749  12138  12469    550    849   1553       O\\nATOM   1602  N   HIS A1031      41.878  -3.592  38.977  1.00 87.03           N\\nANISOU 1602  N   HIS A1031    10189  11192  11687    421    486   1644       N\\nATOM   1603  CA  HIS A1031      42.893  -3.436  37.938  1.00 89.86           C\\nANISOU 1603  CA  HIS A1031    10256  11692  12196    312    785   1660       C\\nATOM   1604  C   HIS A1031      44.259  -3.687  38.565  1.00 92.16           C\\nANISOU 1604  C   HIS A1031    10046  12138  12831    439    693   1664       C\\nATOM   1605  O   HIS A1031      44.848  -2.781  39.162  1.00 95.75           O\\nANISOU 1605  O   HIS A1031    10270  12666  13443    260    450   1711       O\\nATOM   1606  CB  HIS A1031      42.821  -2.053  37.308  1.00 89.34           C\\nANISOU 1606  CB  HIS A1031    10256  11621  12066    -69    797   1742       C\\nATOM   1607  CG  HIS A1031      43.762  -1.865  36.161  1.00 92.70           C\\nANISOU 1607  CG  HIS A1031    10434  12232  12556   -271   1167   1789       C\\nATOM   1608  ND1 HIS A1031      43.332  -1.784  34.855  1.00 93.45           N\\nANISOU 1608  ND1 HIS A1031    10789  12339  12379   -440   1471   1824       N\\nATOM   1609  CD2 HIS A1031      45.109  -1.748  36.123  1.00 96.67           C\\nANISOU 1609  CD2 HIS A1031    10434  12956  13341   -356   1297   1798       C\\nATOM   1610  CE1 HIS A1031      44.375  -1.621  34.061  1.00 97.80           C\\nANISOU 1610  CE1 HIS A1031    11037  13125  12996   -641   1814   1858       C\\nATOM   1611  NE2 HIS A1031      45.465  -1.597  34.805  1.00100.11           N\\nANISOU 1611  NE2 HIS A1031    10830  13554  13654   -592   1731   1833       N\\nATOM   1612  N   LEU A1032      44.761  -4.912  38.422  1.00 91.24           N\\nANISOU 1612  N   LEU A1032     9754  12051  12863    756    853   1596       N\\nATOM   1613  CA  LEU A1032      46.058  -5.267  38.982  1.00 95.11           C\\nANISOU 1613  CA  LEU A1032     9720  12682  13737    952    730   1587       C\\nATOM   1614  C   LEU A1032      47.161  -4.499  38.265  1.00 99.71           C\\nANISOU 1614  C   LEU A1032     9815  13531  14540    697    975   1562       C\\nATOM   1615  O   LEU A1032      47.347  -4.649  37.054  1.00 96.96           O\\nANISOU 1615  O   LEU A1032     9403  13297  14140    624   1442   1479       O\\nATOM   1616  CB  LEU A1032      46.290  -6.772  38.868  1.00 93.50           C\\nANISOU 1616  CB  LEU A1032     9457  12381  13686   1392    849   1495       C\\nATOM   1617  N   LEU A1033      47.887  -3.667  39.013  1.00 97.35           N\\nANISOU 1617  N   LEU A1033     9181  13349  14459    521    666   1628       N\\nATOM   1618  CA  LEU A1033      49.025  -2.964  38.434  1.00104.31           C\\nANISOU 1618  CA  LEU A1033     9528  14502  15604    230    883   1619       C\\nATOM   1619  C   LEU A1033      50.158  -3.934  38.121  1.00112.65           C\\nANISOU 1619  C   LEU A1033     9983  15786  17034    550   1131   1473       C\\nATOM   1620  O   LEU A1033      50.737  -3.897  37.029  1.00115.99           O\\nANISOU 1620  O   LEU A1033    10102  16446  17521    410   1635   1381       O\\nATOM   1621  CB  LEU A1033      49.494  -1.861  39.381  1.00103.46           C\\nANISOU 1621  CB  LEU A1033     9213  14430  15668    -55    434   1699       C\\nATOM   1622  N   THR A1034      50.477  -4.818  39.064  1.00114.71           N\\nANISOU 1622  N   THR A1034    10071  15980  17534    990    782   1443       N\\nATOM   1623  CA  THR A1034      51.514  -5.822  38.866  1.00119.05           C\\nANISOU 1623  CA  THR A1034    10043  16677  18514   1403    933   1278       C\\nATOM   1624  C   THR A1034      51.333  -6.919  39.904  1.00116.13           C\\nANISOU 1624  C   THR A1034     9831  16045  18250   1915    470   1326       C\\nATOM   1625  O   THR A1034      50.615  -6.756  40.893  1.00112.94           O\\nANISOU 1625  O   THR A1034     9869  15449  17593   1873     24   1499       O\\nATOM   1626  CB  THR A1034      52.919  -5.218  38.968  1.00123.11           C\\nANISOU 1626  CB  THR A1034     9729  17558  19489   1237    901   1232       C\\nATOM   1627  OG1 THR A1034      53.898  -6.241  38.746  1.00127.31           O\\nANISOU 1627  OG1 THR A1034     9644  18240  20490   1707   1059   1022       O\\nATOM   1628  CG2 THR A1034      53.135  -4.617  40.344  1.00124.58           C\\nANISOU 1628  CG2 THR A1034     9836  17714  19783   1140    210   1384       C\\nATOM   1629  N   LYS A1035      51.998  -8.046  39.660  1.00124.24           N\\nANISOU 1629  N   LYS A1035    10499  17061  19647   2398    588   1165       N\\nATOM   1630  CA  LYS A1035      52.071  -9.132  40.624  1.00115.60           C\\nANISOU 1630  CA  LYS A1035     9471  15694  18757   2910    100   1245       C\\nATOM   1631  C   LYS A1035      53.350  -9.089  41.448  1.00124.45           C\\nANISOU 1631  C   LYS A1035     9878  17011  20395   3112   -361   1270       C\\nATOM   1632  O   LYS A1035      53.591 -10.004  42.241  1.00126.86           O\\nANISOU 1632  O   LYS A1035    10167  17100  20932   3572   -826   1360       O\\nATOM   1633  CB  LYS A1035      51.953 -10.483  39.911  1.00108.04           C\\nANISOU 1633  CB  LYS A1035     8621  14489  17940   3381    417   1046       C\\nATOM   1634  N   SER A1036      54.169  -8.044  41.282  1.00124.75           N\\nANISOU 1634  N   SER A1036     9333  17441  20626   2756   -279   1212       N\\nATOM   1635  CA  SER A1036      55.429  -7.892  41.994  1.00130.16           C\\nANISOU 1635  CA  SER A1036     9248  18374  21834   2880   -717   1205       C\\nATOM   1636  C   SER A1036      55.191  -7.369  43.411  1.00127.51           C\\nANISOU 1636  C   SER A1036     9199  17961  21290   2719  -1470   1465       C\\nATOM   1637  O   SER A1036      54.249  -6.611  43.652  1.00124.62           O\\nANISOU 1637  O   SER A1036     9437  17497  20415   2316  -1507   1585       O\\nATOM   1638  CB  SER A1036      56.351  -6.937  41.243  1.00133.68           C\\nANISOU 1638  CB  SER A1036     8966  19280  22547   2465   -307   1043       C\\nATOM   1639  N   PRO A1037      56.041  -7.758  44.369  1.00132.59           N\\nANISOU 1639  N   PRO A1037     9408  18656  22314   3043  -2094   1531       N\\nATOM   1640  CA  PRO A1037      55.818  -7.332  45.758  1.00131.46           C\\nANISOU 1640  CA  PRO A1037     9590  18465  21895   2895  -2836   1763       C\\nATOM   1641  C   PRO A1037      56.251  -5.907  46.050  1.00131.07           C\\nANISOU 1641  C   PRO A1037     9233  18724  21845   2324  -3004   1723       C\\nATOM   1642  O   PRO A1037      55.767  -5.327  47.031  1.00128.15           O\\nANISOU 1642  O   PRO A1037     9314  18300  21079   2075  -3470   1849       O\\nATOM   1643  CB  PRO A1037      56.658  -8.330  46.564  1.00137.89           C\\nANISOU 1643  CB  PRO A1037    10022  19225  23144   3474  -3467   1855       C\\nATOM   1644  CG  PRO A1037      57.788  -8.659  45.647  1.00141.32           C\\nANISOU 1644  CG  PRO A1037     9525  19887  24282   3748  -3098   1581       C\\nATOM   1645  CD  PRO A1037      57.205  -8.654  44.250  1.00138.32           C\\nANISOU 1645  CD  PRO A1037     9352  19476  23728   3597  -2186   1384       C\\nATOM   1646  N   SER A1038      57.142  -5.329  45.249  1.00134.97           N\\nANISOU 1646  N   SER A1038     8987  19535  22758   2087  -2636   1539       N\\nATOM   1647  CA  SER A1038      57.615  -3.977  45.512  1.00138.82           C\\nANISOU 1647  CA  SER A1038     9165  20272  23307   1497  -2818   1510       C\\nATOM   1648  C   SER A1038      56.508  -2.965  45.234  1.00142.03           C\\nANISOU 1648  C   SER A1038    10304  20506  23157    966  -2548   1556       C\\nATOM   1649  O   SER A1038      55.905  -2.966  44.156  1.00142.81           O\\nANISOU 1649  O   SER A1038    10685  20515  23061    864  -1905   1526       O\\nATOM   1650  CB  SER A1038      58.845  -3.669  44.659  1.00137.97           C\\nANISOU 1650  CB  SER A1038     8060  20560  23801   1331  -2429   1322       C\\nATOM   1651  N   LEU A1039      56.235  -2.105  46.219  1.00148.93           N\\nANISOU 1651  N   LEU A1039    11491  21326  23772    647  -3071   1607       N\\nATOM   1652  CA  LEU A1039      55.237  -1.059  46.027  1.00137.41           C\\nANISOU 1652  CA  LEU A1039    10670  19674  21866    176  -2887   1609       C\\nATOM   1653  C   LEU A1039      55.728  -0.005  45.042  1.00134.86           C\\nANISOU 1653  C   LEU A1039     9968  19484  21790   -372  -2464   1547       C\\nATOM   1654  O   LEU A1039      54.942   0.522  44.246  1.00128.51           O\\nANISOU 1654  O   LEU A1039     9617  18504  20707   -648  -2029   1577       O\\nATOM   1655  CB  LEU A1039      54.882  -0.422  47.371  1.00133.76           C\\nANISOU 1655  CB  LEU A1039    10606  19126  21088      8  -3557   1606       C\\nATOM   1656  CG  LEU A1039      53.969   0.807  47.351  1.00123.44           C\\nANISOU 1656  CG  LEU A1039     9880  17606  19417   -461  -3487   1537       C\\nATOM   1657  CD1 LEU A1039      52.634   0.486  46.697  1.00115.73           C\\nANISOU 1657  CD1 LEU A1039     9575  16373  18024   -334  -3002   1586       C\\nATOM   1658  CD2 LEU A1039      53.766   1.349  48.759  1.00121.51           C\\nANISOU 1658  CD2 LEU A1039     9948  17332  18887   -575  -4163   1451       C\\nATOM   1659  N   ASN A1040      57.027   0.309  45.078  1.00140.78           N\\nANISOU 1659  N   ASN A1040     9881  20545  23065   -557  -2602   1481       N\\nATOM   1660  CA  ASN A1040      57.584   1.273  44.135  1.00137.59           C\\nANISOU 1660  CA  ASN A1040     9069  20297  22910  -1145  -2171   1458       C\\nATOM   1661  C   ASN A1040      57.424   0.803  42.695  1.00142.78           C\\nANISOU 1661  C   ASN A1040     9696  21027  23528  -1086  -1335   1468       C\\nATOM   1662  O   ASN A1040      57.214   1.623  41.793  1.00129.49           O\\nANISOU 1662  O   ASN A1040     8176  19309  21715  -1595   -895   1536       O\\nATOM   1663  CB  ASN A1040      59.058   1.528  44.452  1.00137.97           C\\nANISOU 1663  CB  ASN A1040     8117  20728  23578  -1326  -2453   1368       C\\nATOM   1664  N   ALA A1041      57.513  -0.508  42.459  1.00141.43           N\\nANISOU 1664  N   ALA A1041     9359  20933  23447   -478  -1132   1401       N\\nATOM   1665  CA  ALA A1041      57.326  -1.032  41.111  1.00146.42           C\\nANISOU 1665  CA  ALA A1041    10009  21635  23988   -388   -344   1347       C\\nATOM   1666  C   ALA A1041      55.865  -0.980  40.683  1.00137.93           C\\nANISOU 1666  C   ALA A1041     9919  20195  22294   -425   -117   1454       C\\nATOM   1667  O   ALA A1041      55.576  -0.783  39.497  1.00137.36           O\\nANISOU 1667  O   ALA A1041    10016  20159  22015   -671    490   1467       O\\nATOM   1668  CB  ALA A1041      57.852  -2.465  41.023  1.00155.04           C\\nANISOU 1668  CB  ALA A1041    10644  22857  25406    310   -239   1186       C\\nATOM   1669  N   ALA A1042      54.935  -1.157  41.626  1.00140.82           N\\nANISOU 1669  N   ALA A1042    10925  20238  22341   -200   -595   1527       N\\nATOM   1670  CA  ALA A1042      53.519  -1.060  41.288  1.00132.90           C\\nANISOU 1670  CA  ALA A1042    10790  18913  20795   -244   -420   1604       C\\nATOM   1671  C   ALA A1042      53.142   0.352  40.863  1.00133.14           C\\nANISOU 1671  C   ALA A1042    11109  18838  20640   -869   -326   1693       C\\nATOM   1672  O   ALA A1042      52.205   0.531  40.075  1.00130.01           O\\nANISOU 1672  O   ALA A1042    11253  18260  19885   -986      1   1755       O\\nATOM   1673  CB  ALA A1042      52.662  -1.505  42.472  1.00126.18           C\\nANISOU 1673  CB  ALA A1042    10481  17801  19659     81   -937   1646       C\\nATOM   1674  N   LYS A1043      53.853   1.361  41.370  1.00137.98           N\\nANISOU 1674  N   LYS A1043    11384  19531  21510  -1275   -652   1703       N\\nATOM   1675  CA  LYS A1043      53.613   2.736  40.950  1.00131.35           C\\nANISOU 1675  CA  LYS A1043    10799  18530  20579  -1894   -598   1802       C\\nATOM   1676  C   LYS A1043      54.204   3.022  39.577  1.00133.43           C\\nANISOU 1676  C   LYS A1043    10730  19015  20952  -2291     34   1891       C\\nATOM   1677  O   LYS A1043      53.705   3.899  38.864  1.00133.13           O\\nANISOU 1677  O   LYS A1043    11108  18782  20694  -2733    227   2044       O\\nATOM   1678  CB  LYS A1043      54.192   3.713  41.976  1.00128.92           C\\nANISOU 1678  CB  LYS A1043    10263  18193  20526  -2230  -1186   1758       C\\nATOM   1679  CG  LYS A1043      53.569   3.618  43.359  1.00124.36           C\\nANISOU 1679  CG  LYS A1043    10090  17422  19739  -1936  -1811   1654       C\\nATOM   1680  CD  LYS A1043      54.054   4.744  44.258  1.00124.45           C\\nANISOU 1680  CD  LYS A1043     9973  17371  19941  -2345  -2374   1565       C\\nATOM   1681  CE  LYS A1043      53.301   4.761  45.577  1.00122.13           C\\nANISOU 1681  CE  LYS A1043    10189  16897  19319  -2105  -2935   1426       C\\nATOM   1682  NZ  LYS A1043      53.698   5.919  46.425  1.00124.65           N\\nANISOU 1682  NZ  LYS A1043    10461  17121  19779  -2520  -3485   1275       N\\nATOM   1683  N   SER A1044      55.263   2.305  39.194  1.00130.51           N\\nANISOU 1683  N   SER A1044     9619  19057  20914  -2142    357   1795       N\\nATOM   1684  CA  SER A1044      55.858   2.511  37.879  1.00137.15           C\\nANISOU 1684  CA  SER A1044    10108  20197  21806  -2533   1041   1845       C\\nATOM   1685  C   SER A1044      54.904   2.086  36.770  1.00136.57           C\\nANISOU 1685  C   SER A1044    10643  20016  21232  -2427   1563   1899       C\\nATOM   1686  O   SER A1044      54.789   2.771  35.747  1.00141.22           O\\nANISOU 1686  O   SER A1044    11441  20628  21589  -2937   1967   2067       O\\nATOM   1687  CB  SER A1044      57.179   1.749  37.775  1.00143.25           C\\nANISOU 1687  CB  SER A1044     9888  21468  23072  -2311   1285   1648       C\\nATOM   1688  N   GLU A1045      54.211   0.960  36.954  1.00136.81           N\\nANISOU 1688  N   GLU A1045    10988  19917  21076  -1800   1534   1777       N\\nATOM   1689  CA  GLU A1045      53.243   0.521  35.955  1.00129.18           C\\nANISOU 1689  CA  GLU A1045    10619  18832  19631  -1695   1960   1797       C\\nATOM   1690  C   GLU A1045      52.010   1.415  35.939  1.00128.34           C\\nANISOU 1690  C   GLU A1045    11333  18313  19118  -1974   1718   2002       C\\nATOM   1691  O   GLU A1045      51.383   1.582  34.887  1.00126.75           O\\nANISOU 1691  O   GLU A1045    11575  18053  18531  -2171   2069   2109       O\\nATOM   1692  CB  GLU A1045      52.847  -0.934  36.210  1.00121.20           C\\nANISOU 1692  CB  GLU A1045     9714  17751  18586   -982   1950   1604       C\\nATOM   1693  N   LEU A1046      51.650   1.998  37.088  1.00131.91           N\\nANISOU 1693  N   LEU A1046    11988  18485  19645  -1980   1106   2037       N\\nATOM   1694  CA  LEU A1046      50.490   2.885  37.146  1.00126.43           C\\nANISOU 1694  CA  LEU A1046    12012  17383  18643  -2189    846   2169       C\\nATOM   1695  C   LEU A1046      50.730   4.156  36.342  1.00134.52           C\\nANISOU 1695  C   LEU A1046    13116  18345  19652  -2860    993   2395       C\\nATOM   1696  O   LEU A1046      49.873   4.579  35.558  1.00138.35           O\\nANISOU 1696  O   LEU A1046    14165  18604  19797  -3036   1114   2555       O\\nATOM   1697  CB  LEU A1046      50.156   3.227  38.600  1.00114.87           C\\nANISOU 1697  CB  LEU A1046    10689  15684  17273  -2043    195   2081       C\\nATOM   1698  CG  LEU A1046      49.189   4.395  38.827  1.00103.62           C\\nANISOU 1698  CG  LEU A1046     9857  13838  15674  -2297   -138   2146       C\\nATOM   1699  CD1 LEU A1046      47.828   4.107  38.217  1.00 96.31           C\\nANISOU 1699  CD1 LEU A1046     9556  12698  14341  -2097     22   2183       C\\nATOM   1700  CD2 LEU A1046      49.056   4.722  40.308  1.00 99.47           C\\nANISOU 1700  CD2 LEU A1046     9379  13170  15245  -2171   -734   1980       C\\nATOM   1701  N   ASP A1047      51.893   4.784  36.529  1.00127.49           N\\nANISOU 1701  N   ASP A1047    11667  17635  19137  -3262    951   2433       N\\nATOM   1702  CA  ASP A1047      52.188   6.012  35.801  1.00131.96           C\\nANISOU 1702  CA  ASP A1047    12311  18112  19714  -3978   1078   2692       C\\nATOM   1703  C   ASP A1047      52.444   5.742  34.324  1.00130.92           C\\nANISOU 1703  C   ASP A1047    12130  18291  19323  -4228   1792   2837       C\\nATOM   1704  O   ASP A1047      52.172   6.607  33.483  1.00133.98           O\\nANISOU 1704  O   ASP A1047    12921  18510  19475  -4745   1927   3128       O\\nATOM   1705  CB  ASP A1047      53.382   6.723  36.435  1.00141.47           C\\nANISOU 1705  CB  ASP A1047    12895  19442  21416  -4390    835   2678       C\\nATOM   1706  CG  ASP A1047      53.050   7.320  37.791  1.00139.91           C\\nANISOU 1706  CG  ASP A1047    12900  18874  21385  -4305     95   2555       C\\nATOM   1707  OD1 ASP A1047      51.910   7.125  38.263  1.00133.93           O\\nANISOU 1707  OD1 ASP A1047    12719  17809  20359  -3898   -178   2466       O\\nATOM   1708  OD2 ASP A1047      53.925   7.988  38.382  1.00142.42           O\\nANISOU 1708  OD2 ASP A1047    12791  19231  22093  -4666   -203   2522       O\\nATOM   1709  N   LYS A1048      52.958   4.557  33.986  1.00136.15           N\\nANISOU 1709  N   LYS A1048    12332  19393  20008  -3866   2239   2634       N\\nATOM   1710  CA  LYS A1048      53.156   4.211  32.584  1.00137.23           C\\nANISOU 1710  CA  LYS A1048    12447  19868  19828  -4059   2961   2691       C\\nATOM   1711  C   LYS A1048      51.836   3.990  31.855  1.00136.24           C\\nANISOU 1711  C   LYS A1048    13159  19483  19123  -3907   3045   2785       C\\nATOM   1712  O   LYS A1048      51.813   4.012  30.619  1.00135.03           O\\nANISOU 1712  O   LYS A1048    13198  19529  18579  -4209   3556   2913       O\\nATOM   1713  CB  LYS A1048      54.036   2.964  32.467  1.00137.25           C\\nANISOU 1713  CB  LYS A1048    11720  20374  20055  -3634   3395   2361       C\\nATOM   1714  N   ALA A1049      50.743   3.782  32.587  1.00134.09           N\\nANISOU 1714  N   ALA A1049    13374  18806  18767  -3471   2557   2719       N\\nATOM   1715  CA  ALA A1049      49.423   3.607  31.993  1.00136.97           C\\nANISOU 1715  CA  ALA A1049    14488  18911  18642  -3319   2551   2790       C\\nATOM   1716  C   ALA A1049      48.555   4.853  32.093  1.00139.86           C\\nANISOU 1716  C   ALA A1049    15461  18785  18895  -3629   2088   3059       C\\nATOM   1717  O   ALA A1049      47.775   5.130  31.178  1.00144.34           O\\nANISOU 1717  O   ALA A1049    16587  19202  19054  -3792   2166   3254       O\\nATOM   1718  CB  ALA A1049      48.697   2.429  32.649  1.00134.83           C\\nANISOU 1718  CB  ALA A1049    14339  18543  18349  -2619   2376   2514       C\\nATOM   1719  N   ILE A1050      48.667   5.615  33.186  1.00147.00           N\\nANISOU 1719  N   ILE A1050    16279  19419  20157  -3696   1573   3052       N\\nATOM   1720  CA  ILE A1050      47.884   6.843  33.320  1.00137.76           C\\nANISOU 1720  CA  ILE A1050    15661  17727  18955  -3954   1109   3250       C\\nATOM   1721  C   ILE A1050      48.527   8.029  32.621  1.00135.31           C\\nANISOU 1721  C   ILE A1050    15376  17334  18700  -4696   1193   3602       C\\nATOM   1722  O   ILE A1050      47.861   9.054  32.425  1.00132.09           O\\nANISOU 1722  O   ILE A1050    15513  16449  18227  -4950    855   3834       O\\nATOM   1723  CB  ILE A1050      47.649   7.192  34.802  1.00112.75           C\\nANISOU 1723  CB  ILE A1050    12459  14272  16111  -3710    512   3036       C\\nATOM   1724  N   GLY A1051      49.800   7.923  32.236  1.00128.26           N\\nANISOU 1724  N   GLY A1051    13902  16884  17947  -5058   1630   3652       N\\nATOM   1725  CA  GLY A1051      50.479   8.964  31.501  1.00126.01           C\\nANISOU 1725  CA  GLY A1051    13606  16592  17681  -5844   1802   4017       C\\nATOM   1726  C   GLY A1051      51.114  10.046  32.350  1.00125.68           C\\nANISOU 1726  C   GLY A1051    13328  16279  18144  -6255   1362   4067       C\\nATOM   1727  O   GLY A1051      52.053  10.703  31.888  1.00131.62           O\\nANISOU 1727  O   GLY A1051    13814  17166  19028  -6906   1590   4283       O\\nATOM   1728  N   ARG A1052      50.638  10.250  33.572  1.00125.39           N\\nANISOU 1728  N   ARG A1052    13398  15875  18368  -5892    754   3830       N\\nATOM   1729  CA  ARG A1052      51.137  11.295  34.452  1.00130.48           C\\nANISOU 1729  CA  ARG A1052    13895  16207  19473  -6249    261   3810       C\\nATOM   1730  C   ARG A1052      51.879  10.681  35.633  1.00133.64           C\\nANISOU 1730  C   ARG A1052    13610  16936  20230  -5922     98   3432       C\\nATOM   1731  O   ARG A1052      51.880   9.465  35.836  1.00139.15           O\\nANISOU 1731  O   ARG A1052    14025  18014  20831  -5363    306   3204       O\\nATOM   1732  CB  ARG A1052      49.986  12.174  34.954  1.00127.22           C\\nANISOU 1732  CB  ARG A1052    14202  15072  19066  -6123   -369   3798       C\\nATOM   1733  CG  ARG A1052      49.063  11.466  35.933  1.00118.27           C\\nANISOU 1733  CG  ARG A1052    13210  13879  17849  -5343   -664   3404       C\\nATOM   1734  CD  ARG A1052      47.922  12.363  36.372  1.00115.96           C\\nANISOU 1734  CD  ARG A1052    13565  12916  17579  -5212  -1224   3339       C\\nATOM   1735  NE  ARG A1052      47.116  11.751  37.424  1.00114.03           N\\nANISOU 1735  NE  ARG A1052    13390  12676  17262  -4541  -1477   2931       N\\nATOM   1736  CZ  ARG A1052      47.303  11.960  38.723  1.00115.93           C\\nANISOU 1736  CZ  ARG A1052    13460  12852  17737  -4403  -1881   2594       C\\nATOM   1737  NH1 ARG A1052      48.271  12.768  39.132  1.00119.81           N\\nANISOU 1737  NH1 ARG A1052    13686  13244  18594  -4875  -2117   2592       N\\nATOM   1738  NH2 ARG A1052      46.523  11.364  39.613  1.00113.10           N\\nANISOU 1738  NH2 ARG A1052    13205  12544  17222  -3834  -2048   2259       N\\nATOM   1739  N   ASN A1053      52.517  11.551  36.419  1.00125.16           N\\nANISOU 1739  N   ASN A1053    12297  15678  19580  -6291   -324   3375       N\\nATOM   1740  CA  ASN A1053      53.118  11.156  37.692  1.00123.03           C\\nANISOU 1740  CA  ASN A1053    11481  15629  19636  -6002   -663   3022       C\\nATOM   1741  C   ASN A1053      52.002  11.117  38.731  1.00122.77           C\\nANISOU 1741  C   ASN A1053    11968  15217  19462  -5447  -1194   2750       C\\nATOM   1742  O   ASN A1053      51.786  12.056  39.502  1.00122.02           O\\nANISOU 1742  O   ASN A1053    12131  14690  19541  -5602  -1734   2626       O\\nATOM   1743  CB  ASN A1053      54.234  12.115  38.089  1.00126.67           C\\nANISOU 1743  CB  ASN A1053    11485  16063  20583  -6663   -923   3047       C\\nATOM   1744  N   THR A1054      51.272   9.995  38.739  1.00124.33           N\\nANISOU 1744  N   THR A1054    12319  15587  19333  -4804  -1013   2632       N\\nATOM   1745  CA  THR A1054      50.060   9.901  39.547  1.00119.55           C\\nANISOU 1745  CA  THR A1054    12244  14668  18513  -4306  -1394   2406       C\\nATOM   1746  C   THR A1054      50.366   9.947  41.037  1.00119.71           C\\nANISOU 1746  C   THR A1054    12048  14716  18720  -4133  -1918   2083       C\\nATOM   1747  O   THR A1054      49.504  10.334  41.835  1.00120.96           O\\nANISOU 1747  O   THR A1054    12645  14548  18764  -3922  -2315   1863       O\\nATOM   1748  CB  THR A1054      49.295   8.620  39.212  1.00115.03           C\\nANISOU 1748  CB  THR A1054    11827  14310  17568  -3728  -1059   2370       C\\nATOM   1749  N   ASN A1055      51.577   9.556  41.433  1.00118.97           N\\nANISOU 1749  N   ASN A1055    11271  15030  18901  -4213  -1934   2029       N\\nATOM   1750  CA  ASN A1055      52.004   9.557  42.830  1.00116.22           C\\nANISOU 1750  CA  ASN A1055    10681  14771  18707  -4084  -2473   1748       C\\nATOM   1751  C   ASN A1055      51.115   8.687  43.711  1.00119.38           C\\nANISOU 1751  C   ASN A1055    11395  15214  18750  -3437  -2650   1539       C\\nATOM   1752  O   ASN A1055      51.131   8.822  44.935  1.00121.96           O\\nANISOU 1752  O   ASN A1055    11754  15533  19052  -3324  -3143   1293       O\\nATOM   1753  CB  ASN A1055      52.071  10.984  43.391  1.00109.11           C\\nANISOU 1753  CB  ASN A1055     9992  13444  18023  -4552  -2980   1627       C\\nATOM   1754  N   GLY A1056      50.340   7.783  43.111  1.00115.78           N\\nANISOU 1754  N   GLY A1056    11183  14819  17987  -3045  -2253   1632       N\\nATOM   1755  CA  GLY A1056      49.518   6.838  43.832  1.00115.99           C\\nANISOU 1755  CA  GLY A1056    11480  14915  17677  -2485  -2341   1489       C\\nATOM   1756  C   GLY A1056      48.027   7.076  43.671  1.00112.88           C\\nANISOU 1756  C   GLY A1056    11762  14182  16944  -2317  -2293   1431       C\\nATOM   1757  O   GLY A1056      47.247   6.120  43.742  1.00109.86           O\\nANISOU 1757  O   GLY A1056    11592  13885  16264  -1902  -2132   1408       O\\nATOM   1758  N   VAL A1057      47.618   8.323  43.454  1.00113.85           N\\nANISOU 1758  N   VAL A1057    12208  13906  17145  -2632  -2448   1405       N\\nATOM   1759  CA  VAL A1057      46.211   8.699  43.361  1.00103.36           C\\nANISOU 1759  CA  VAL A1057    11467  12226  15579  -2456  -2483   1304       C\\nATOM   1760  C   VAL A1057      45.881   9.003  41.907  1.00105.21           C\\nANISOU 1760  C   VAL A1057    11904  12256  15814  -2653  -2149   1598       C\\nATOM   1761  O   VAL A1057      46.708   9.560  41.176  1.00111.08           O\\nANISOU 1761  O   VAL A1057    12459  12960  16785  -3103  -2041   1831       O\\nATOM   1762  CB  VAL A1057      45.900   9.912  44.260  1.00 96.42           C\\nANISOU 1762  CB  VAL A1057    10853  10979  14804  -2591  -2980   1005       C\\nATOM   1763  N   ILE A1058      44.667   8.639  41.488  1.00104.59           N\\nANISOU 1763  N   ILE A1058    12209  12071  15459  -2350  -1994   1597       N\\nATOM   1764  CA  ILE A1058      44.203   8.889  40.131  1.00100.91           C\\nANISOU 1764  CA  ILE A1058    12012  11414  14916  -2498  -1744   1872       C\\nATOM   1765  C   ILE A1058      42.794   9.466  40.170  1.00 98.60           C\\nANISOU 1765  C   ILE A1058    12224  10714  14524  -2295  -1978   1737       C\\nATOM   1766  O   ILE A1058      42.091   9.405  41.182  1.00 92.24           O\\nANISOU 1766  O   ILE A1058    11523   9875  13648  -1976  -2199   1403       O\\nATOM   1767  CB  ILE A1058      44.229   7.619  39.253  1.00 94.08           C\\nANISOU 1767  CB  ILE A1058    11024  10914  13808  -2321  -1243   2041       C\\nATOM   1768  CG1 ILE A1058      43.313   6.543  39.831  1.00 82.54           C\\nANISOU 1768  CG1 ILE A1058     9675   9599  12089  -1804  -1208   1830       C\\nATOM   1769  CG2 ILE A1058      45.650   7.101  39.083  1.00 91.55           C\\nANISOU 1769  CG2 ILE A1058    10149  10986  13649  -2498   -980   2147       C\\nATOM   1770  CD1 ILE A1058      43.175   5.325  38.950  1.00 80.94           C\\nANISOU 1770  CD1 ILE A1058     9440   9653  11661  -1618   -764   1951       C\\nATOM   1771  N   THR A1059      42.391  10.038  39.038  1.00100.27           N\\nANISOU 1771  N   THR A1059    12740  10636  14723  -2488  -1928   2000       N\\nATOM   1772  CA  THR A1059      41.046  10.571  38.887  1.00100.12           C\\nANISOU 1772  CA  THR A1059    13164  10218  14658  -2267  -2166   1907       C\\nATOM   1773  C   THR A1059      40.043   9.431  38.714  1.00 93.93           C\\nANISOU 1773  C   THR A1059    12445   9697  13549  -1832  -1928   1816       C\\nATOM   1774  O   THR A1059      40.390   8.322  38.302  1.00 93.12           O\\nANISOU 1774  O   THR A1059    12152   9988  13239  -1781  -1546   1935       O\\nATOM   1775  CB  THR A1059      40.982  11.515  37.681  1.00103.74           C\\nANISOU 1775  CB  THR A1059    13952  10269  15193  -2630  -2248   2286       C\\nATOM   1776  OG1 THR A1059      42.175  12.306  37.630  1.00105.14           O\\nANISOU 1776  OG1 THR A1059    13991  10320  15636  -3159  -2321   2476       O\\nATOM   1777  CG2 THR A1059      39.778  12.440  37.771  1.00108.32           C\\nANISOU 1777  CG2 THR A1059    14955  10292  15912  -2422  -2687   2144       C\\nATOM   1778  N   LYS A1060      38.780   9.709  39.047  1.00 98.18           N\\nANISOU 1778  N   LYS A1060    13229  10001  14072  -1515  -2161   1570       N\\nATOM   1779  CA  LYS A1060      37.721   8.768  38.697  1.00 98.24           C\\nANISOU 1779  CA  LYS A1060    13319  10201  13806  -1182  -1964   1522       C\\nATOM   1780  C   LYS A1060      37.594   8.635  37.188  1.00 99.60           C\\nANISOU 1780  C   LYS A1060    13688  10335  13819  -1346  -1790   1903       C\\nATOM   1781  O   LYS A1060      37.139   7.599  36.688  1.00 95.67           O\\nANISOU 1781  O   LYS A1060    13192  10106  13053  -1183  -1519   1935       O\\nATOM   1782  CB  LYS A1060      36.389   9.207  39.307  1.00 93.38           C\\nANISOU 1782  CB  LYS A1060    12863   9359  13257   -838  -2249   1162       C\\nATOM   1783  N   ASP A1061      37.997   9.671  36.449  1.00103.09           N\\nANISOU 1783  N   ASP A1061    14329  10441  14400  -1703  -1952   2200       N\\nATOM   1784  CA  ASP A1061      38.006   9.603  34.993  1.00101.97           C\\nANISOU 1784  CA  ASP A1061    14414  10301  14028  -1942  -1780   2607       C\\nATOM   1785  C   ASP A1061      39.176   8.768  34.485  1.00100.34           C\\nANISOU 1785  C   ASP A1061    13939  10555  13629  -2196  -1275   2797       C\\nATOM   1786  O   ASP A1061      39.012   7.961  33.563  1.00 99.43           O\\nANISOU 1786  O   ASP A1061    13894  10699  13185  -2180   -958   2926       O\\nATOM   1787  CB  ASP A1061      38.055  11.015  34.413  1.00102.76           C\\nANISOU 1787  CB  ASP A1061    14862   9863  14320  -2281  -2142   2907       C\\nATOM   1788  CG  ASP A1061      37.962  11.029  32.903  1.00102.52           C\\nANISOU 1788  CG  ASP A1061    15156   9822  13974  -2555  -2021   3367       C\\nATOM   1789  OD1 ASP A1061      36.881  10.700  32.371  1.00 98.49           O\\nANISOU 1789  OD1 ASP A1061    14872   9291  13258  -2289  -2114   3362       O\\nATOM   1790  OD2 ASP A1061      38.970  11.374  32.248  1.00105.90           O\\nANISOU 1790  OD2 ASP A1061    15607  10290  14339  -3064  -1832   3728       O\\nATOM   1791  N   GLU A1062      40.362   8.948  35.075  1.00102.50           N\\nANISOU 1791  N   GLU A1062    13880  10945  14119  -2420  -1205   2776       N\\nATOM   1792  CA  GLU A1062      41.504   8.118  34.707  1.00 96.62           C\\nANISOU 1792  CA  GLU A1062    12770  10671  13271  -2592   -725   2880       C\\nATOM   1793  C   GLU A1062      41.237   6.651  35.014  1.00 88.82           C\\nANISOU 1793  C   GLU A1062    11588  10061  12098  -2156   -455   2641       C\\nATOM   1794  O   GLU A1062      41.657   5.764  34.262  1.00 83.40           O\\nANISOU 1794  O   GLU A1062    10776   9705  11208  -2174    -28   2718       O\\nATOM   1795  CB  GLU A1062      42.761   8.595  35.435  1.00 87.02           C\\nANISOU 1795  CB  GLU A1062    11163   9509  12392  -2870   -785   2852       C\\nATOM   1796  CG  GLU A1062      43.240   9.972  35.025  1.00 95.42           C\\nANISOU 1796  CG  GLU A1062    12385  10212  13658  -3416   -988   3136       C\\nATOM   1797  CD  GLU A1062      44.494  10.395  35.768  1.00 99.73           C\\nANISOU 1797  CD  GLU A1062    12491  10838  14563  -3723  -1061   3077       C\\nATOM   1798  OE1 GLU A1062      44.628  10.042  36.959  1.00 95.17           O\\nANISOU 1798  OE1 GLU A1062    11645  10382  14135  -3431  -1231   2743       O\\nATOM   1799  OE2 GLU A1062      45.347  11.075  35.159  1.00104.48           O\\nANISOU 1799  OE2 GLU A1062    13018  11399  15279  -4288   -958   3375       O\\nATOM   1800  N   ALA A1063      40.542   6.377  36.121  1.00 85.45           N\\nANISOU 1800  N   ALA A1063    11151   9581  11735  -1777   -689   2337       N\\nATOM   1801  CA  ALA A1063      40.186   5.003  36.456  1.00 86.64           C\\nANISOU 1801  CA  ALA A1063    11186  10021  11712  -1400   -477   2151       C\\nATOM   1802  C   ALA A1063      39.112   4.459  35.526  1.00 88.99           C\\nANISOU 1802  C   ALA A1063    11790  10309  11715  -1259   -345   2190       C\\nATOM   1803  O   ALA A1063      39.030   3.242  35.325  1.00 88.77           O\\nANISOU 1803  O   ALA A1063    11692  10524  11512  -1068    -60   2120       O\\nATOM   1804  CB  ALA A1063      39.719   4.914  37.909  1.00 84.46           C\\nANISOU 1804  CB  ALA A1063    10850   9716  11524  -1112   -751   1850       C\\nATOM   1805  N   GLU A1064      38.283   5.337  34.957  1.00 91.39           N\\nANISOU 1805  N   GLU A1064    12438  10307  11980  -1346   -590   2294       N\\nATOM   1806  CA  GLU A1064      37.273   4.882  34.009  1.00 91.30           C\\nANISOU 1806  CA  GLU A1064    12709  10296  11686  -1243   -529   2345       C\\nATOM   1807  C   GLU A1064      37.898   4.478  32.678  1.00 95.38           C\\nANISOU 1807  C   GLU A1064    13297  11022  11922  -1504   -156   2596       C\\nATOM   1808  O   GLU A1064      37.402   3.560  32.016  1.00 93.85           O\\nANISOU 1808  O   GLU A1064    13219  10996  11445  -1384     47   2550       O\\nATOM   1809  CB  GLU A1064      36.216   5.969  33.805  1.00 88.36           C\\nANISOU 1809  CB  GLU A1064    12660   9522  11391  -1222   -972   2387       C\\nATOM   1810  CG  GLU A1064      34.995   5.506  33.022  1.00 85.95           C\\nANISOU 1810  CG  GLU A1064    12598   9220  10839  -1054  -1023   2379       C\\nATOM   1811  CD  GLU A1064      33.877   6.532  33.012  1.00 92.64           C\\nANISOU 1811  CD  GLU A1064    13676   9668  11857   -926  -1527   2353       C\\nATOM   1812  OE1 GLU A1064      32.798   6.224  32.460  1.00 92.14           O\\nANISOU 1812  OE1 GLU A1064    13758   9602  11649   -763  -1648   2318       O\\nATOM   1813  OE2 GLU A1064      34.072   7.641  33.555  1.00 96.90           O\\nANISOU 1813  OE2 GLU A1064    14234   9879  12704   -975  -1826   2343       O\\nATOM   1814  N   LYS A1065      38.982   5.144  32.270  1.00 96.04           N\\nANISOU 1814  N   LYS A1065    13309  11119  12064  -1890    -43   2837       N\\nATOM   1815  CA  LYS A1065      39.706   4.695  31.086  1.00 95.76           C\\nANISOU 1815  CA  LYS A1065    13269  11382  11732  -2158    412   3024       C\\nATOM   1816  C   LYS A1065      40.338   3.328  31.321  1.00 92.50           C\\nANISOU 1816  C   LYS A1065    12480  11360  11306  -1927    838   2784       C\\nATOM   1817  O   LYS A1065      40.296   2.460  30.442  1.00 93.15           O\\nANISOU 1817  O   LYS A1065    12640  11673  11077  -1892   1185   2745       O\\nATOM   1818  CB  LYS A1065      40.767   5.724  30.695  1.00 97.00           C\\nANISOU 1818  CB  LYS A1065    13372  11502  11982  -2673    474   3332       C\\nATOM   1819  N   LEU A1066      40.918   3.114  32.505  1.00 86.38           N\\nANISOU 1819  N   LEU A1066    11317  10638  10865  -1755    781   2609       N\\nATOM   1820  CA  LEU A1066      41.504   1.814  32.815  1.00 89.95           C\\nANISOU 1820  CA  LEU A1066    11422  11389  11367  -1482   1095   2400       C\\nATOM   1821  C   LEU A1066      40.439   0.729  32.871  1.00 88.33           C\\nANISOU 1821  C   LEU A1066    11426  11159  10977  -1113   1097   2208       C\\nATOM   1822  O   LEU A1066      40.672  -0.401  32.428  1.00 91.55           O\\nANISOU 1822  O   LEU A1066    11755  11759  11269   -957   1433   2085       O\\nATOM   1823  CB  LEU A1066      42.265   1.875  34.139  1.00 96.43           C\\nANISOU 1823  CB  LEU A1066    11833  12240  12567  -1373    917   2292       C\\nATOM   1824  CG  LEU A1066      43.442   2.845  34.220  1.00110.23           C\\nANISOU 1824  CG  LEU A1066    13274  14038  14572  -1754    899   2439       C\\nATOM   1825  CD1 LEU A1066      44.173   2.679  35.543  1.00109.37           C\\nANISOU 1825  CD1 LEU A1066    12741  14009  14807  -1592    693   2287       C\\nATOM   1826  CD2 LEU A1066      44.392   2.653  33.043  1.00117.21           C\\nANISOU 1826  CD2 LEU A1066    13951  15231  15353  -2035   1407   2560       C\\nATOM   1827  N   PHE A1067      39.266   1.055  33.417  1.00 88.20           N\\nANISOU 1827  N   PHE A1067    11656  10901  10956   -977    731   2152       N\\nATOM   1828  CA  PHE A1067      38.202   0.064  33.527  1.00 86.10           C\\nANISOU 1828  CA  PHE A1067    11554  10620  10539   -687    725   1975       C\\nATOM   1829  C   PHE A1067      37.743  -0.409  32.155  1.00 85.87           C\\nANISOU 1829  C   PHE A1067    11803  10657  10168   -762    941   2008       C\\nATOM   1830  O   PHE A1067      37.513  -1.606  31.949  1.00 84.89           O\\nANISOU 1830  O   PHE A1067    11703  10627   9925   -580   1146   1847       O\\nATOM   1831  CB  PHE A1067      37.028   0.640  34.316  1.00 89.23           C\\nANISOU 1831  CB  PHE A1067    12101  10796  11006   -569    323   1888       C\\nATOM   1832  CG  PHE A1067      35.849  -0.282  34.400  1.00 87.05           C\\nANISOU 1832  CG  PHE A1067    11964  10525  10586   -347    317   1719       C\\nATOM   1833  CD1 PHE A1067      35.865  -1.372  35.252  1.00 83.17           C\\nANISOU 1833  CD1 PHE A1067    11332  10130  10137   -136    418   1574       C\\nATOM   1834  CD2 PHE A1067      34.724  -0.058  33.627  1.00 86.11           C\\nANISOU 1834  CD2 PHE A1067    12115  10304  10299   -373    179   1726       C\\nATOM   1835  CE1 PHE A1067      34.781  -2.221  35.329  1.00 78.20           C\\nANISOU 1835  CE1 PHE A1067    10832   9493   9387     -3    424   1440       C\\nATOM   1836  CE2 PHE A1067      33.638  -0.903  33.702  1.00 81.95           C\\nANISOU 1836  CE2 PHE A1067    11664   9800   9671   -214    168   1558       C\\nATOM   1837  CZ  PHE A1067      33.666  -1.985  34.553  1.00 78.15           C\\nANISOU 1837  CZ  PHE A1067    11043   9414   9235    -52    312   1415       C\\nATOM   1838  N   ASN A1068      37.604   0.516  31.201  1.00 90.24           N\\nANISOU 1838  N   ASN A1068    12604  11140  10543  -1046    869   2222       N\\nATOM   1839  CA  ASN A1068      37.203   0.127  29.853  1.00 83.46           C\\nANISOU 1839  CA  ASN A1068    12053  10378   9278  -1159   1045   2269       C\\nATOM   1840  C   ASN A1068      38.222  -0.816  29.228  1.00 82.78           C\\nANISOU 1840  C   ASN A1068    11803  10602   9046  -1191   1575   2173       C\\nATOM   1841  O   ASN A1068      37.856  -1.728  28.479  1.00 84.94           O\\nANISOU 1841  O   ASN A1068    12255  10985   9033  -1118   1777   2024       O\\nATOM   1842  CB  ASN A1068      37.008   1.367  28.984  1.00 87.76           C\\nANISOU 1842  CB  ASN A1068    12920  10786   9638  -1498    837   2587       C\\nATOM   1843  CG  ASN A1068      35.631   1.982  29.145  1.00 95.27           C\\nANISOU 1843  CG  ASN A1068    14135  11430  10632  -1379    315   2609       C\\nATOM   1844  OD1 ASN A1068      34.845   2.027  28.198  1.00102.99           O\\nANISOU 1844  OD1 ASN A1068    15454  12372  11305  -1446    169   2702       O\\nATOM   1845  ND2 ASN A1068      35.327   2.448  30.350  1.00 94.72           N\\nANISOU 1845  ND2 ASN A1068    13890  11159  10939  -1190     20   2495       N\\nATOM   1846  N   GLN A1069      39.507  -0.618  29.532  1.00 82.90           N\\nANISOU 1846  N   GLN A1069    11450  10766   9281  -1289   1799   2217       N\\nATOM   1847  CA  GLN A1069      40.533  -1.532  29.041  1.00 93.96           C\\nANISOU 1847  CA  GLN A1069    12588  12479  10633  -1250   2317   2059       C\\nATOM   1848  C   GLN A1069      40.355  -2.926  29.631  1.00 96.67           C\\nANISOU 1848  C   GLN A1069    12801  12800  11129   -811   2383   1749       C\\nATOM   1849  O   GLN A1069      40.472  -3.931  28.918  1.00 96.30           O\\nANISOU 1849  O   GLN A1069    12800  12887  10901   -697   2721   1539       O\\nATOM   1850  CB  GLN A1069      41.922  -0.978  29.364  1.00104.31           C\\nANISOU 1850  CB  GLN A1069    13439  13961  12234  -1436   2488   2158       C\\nATOM   1851  CG  GLN A1069      42.191   0.399  28.770  1.00112.15           C\\nANISOU 1851  CG  GLN A1069    14573  14942  13096  -1947   2442   2503       C\\nATOM   1852  CD  GLN A1069      43.505   1.002  29.237  1.00116.78           C\\nANISOU 1852  CD  GLN A1069    14664  15667  14039  -2175   2548   2595       C\\nATOM   1853  OE1 GLN A1069      44.350   0.314  29.812  1.00124.86           O\\nANISOU 1853  OE1 GLN A1069    15191  16882  15370  -1946   2730   2385       O\\nATOM   1854  NE2 GLN A1069      43.681   2.297  28.993  1.00109.98           N\\nANISOU 1854  NE2 GLN A1069    13937  14684  13167  -2636   2395   2919       N\\nATOM   1855  N   ASP A1070      40.068  -3.007  30.934  1.00 93.20           N\\nANISOU 1855  N   ASP A1070    12231  12176  11004   -577   2056   1715       N\\nATOM   1856  CA  ASP A1070      39.831  -4.304  31.560  1.00 92.78           C\\nANISOU 1856  CA  ASP A1070    12121  12049  11083   -206   2064   1494       C\\nATOM   1857  C   ASP A1070      38.580  -4.968  31.000  1.00 84.10           C\\nANISOU 1857  C   ASP A1070    11427  10832   9697   -148   2030   1376       C\\nATOM   1858  O   ASP A1070      38.532  -6.195  30.858  1.00 74.28           O\\nANISOU 1858  O   ASP A1070    10218   9558   8448     64   2204   1167       O\\nATOM   1859  CB  ASP A1070      39.714  -4.145  33.076  1.00 97.16           C\\nANISOU 1859  CB  ASP A1070    12517  12464  11936    -46   1705   1529       C\\nATOM   1860  CG  ASP A1070      40.993  -3.637  33.711  1.00101.50           C\\nANISOU 1860  CG  ASP A1070    12635  13134  12794    -83   1688   1606       C\\nATOM   1861  OD1 ASP A1070      42.082  -3.940  33.181  1.00105.37           O\\nANISOU 1861  OD1 ASP A1070    12832  13826  13379    -89   2015   1558       O\\nATOM   1862  OD2 ASP A1070      40.905  -2.936  34.743  1.00 98.07           O\\nANISOU 1862  OD2 ASP A1070    12136  12614  12514   -110   1349   1680       O\\nATOM   1863  N   VAL A1071      37.557  -4.174  30.679  1.00 85.78           N\\nANISOU 1863  N   VAL A1071    11939  10950   9704   -328   1771   1495       N\\nATOM   1864  CA  VAL A1071      36.322  -4.733  30.136  1.00 82.23           C\\nANISOU 1864  CA  VAL A1071    11829  10413   9002   -301   1681   1379       C\\nATOM   1865  C   VAL A1071      36.565  -5.310  28.749  1.00 86.97           C\\nANISOU 1865  C   VAL A1071    12623  11169   9251   -401   2023   1266       C\\nATOM   1866  O   VAL A1071      36.169  -6.443  28.455  1.00 91.66           O\\nANISOU 1866  O   VAL A1071    13352  11723   9752   -267   2137   1029       O\\nATOM   1867  CB  VAL A1071      35.214  -3.667  30.113  1.00 77.64           C\\nANISOU 1867  CB  VAL A1071    11459   9702   8338   -435   1276   1525       C\\nATOM   1868  CG1 VAL A1071      34.018  -4.169  29.323  1.00 68.20           C\\nANISOU 1868  CG1 VAL A1071    10579   8473   6862   -455   1173   1415       C\\nATOM   1869  CG2 VAL A1071      34.807  -3.308  31.524  1.00 79.71           C\\nANISOU 1869  CG2 VAL A1071    11544   9829   8913   -289    982   1517       C\\nATOM   1870  N   ASP A1072      37.208  -4.533  27.872  1.00 86.89           N\\nANISOU 1870  N   ASP A1072    12656  11340   9019   -672   2197   1425       N\\nATOM   1871  CA  ASP A1072      37.548  -5.045  26.549  1.00 93.69           C\\nANISOU 1871  CA  ASP A1072    13699  12426   9474   -799   2587   1294       C\\nATOM   1872  C   ASP A1072      38.419  -6.289  26.649  1.00 93.29           C\\nANISOU 1872  C   ASP A1072    13380  12470   9598   -530   3002    969       C\\nATOM   1873  O   ASP A1072      38.186  -7.273  25.940  1.00100.45           O\\nANISOU 1873  O   ASP A1072    14485  13404  10277   -445   3208    683       O\\nATOM   1874  CB  ASP A1072      38.246  -3.964  25.724  1.00101.72           C\\nANISOU 1874  CB  ASP A1072    14764  13660  10224  -1186   2755   1563       C\\nATOM   1875  CG  ASP A1072      37.274  -2.951  25.152  1.00105.64           C\\nANISOU 1875  CG  ASP A1072    15691  14039  10407  -1457   2355   1858       C\\nATOM   1876  OD1 ASP A1072      36.104  -3.321  24.911  1.00105.43           O\\nANISOU 1876  OD1 ASP A1072    15959  13888  10212  -1367   2080   1761       O\\nATOM   1877  OD2 ASP A1072      37.677  -1.787  24.942  1.00108.66           O\\nANISOU 1877  OD2 ASP A1072    16112  14434  10740  -1764   2286   2192       O\\nATOM   1878  N   ALA A1073      39.417  -6.269  27.537  1.00 84.98           N\\nANISOU 1878  N   ALA A1073    11874  11440   8973   -376   3089    988       N\\nATOM   1879  CA  ALA A1073      40.250  -7.451  27.738  1.00 87.42           C\\nANISOU 1879  CA  ALA A1073    11887  11783   9546    -46   3401    685       C\\nATOM   1880  C   ALA A1073      39.418  -8.640  28.199  1.00 88.42           C\\nANISOU 1880  C   ALA A1073    12207  11603   9787    254   3220    480       C\\nATOM   1881  O   ALA A1073      39.645  -9.774  27.760  1.00 91.45           O\\nANISOU 1881  O   ALA A1073    12623  11947  10175    465   3482    159       O\\nATOM   1882  CB  ALA A1073      41.357  -7.149  28.747  1.00 88.38           C\\nANISOU 1882  CB  ALA A1073    11477  11958  10146     77   3385    785       C\\nATOM   1883  N   ALA A1074      38.441  -8.397  29.079  1.00 83.01           N\\nANISOU 1883  N   ALA A1074    11651  10689   9199    259   2785    645       N\\nATOM   1884  CA  ALA A1074      37.590  -9.476  29.567  1.00 85.44           C\\nANISOU 1884  CA  ALA A1074    12143  10714   9605    456   2615    500       C\\nATOM   1885  C   ALA A1074      36.749 -10.084  28.454  1.00 93.89           C\\nANISOU 1885  C   ALA A1074    13614  11749  10313    356   2695    279       C\\nATOM   1886  O   ALA A1074      36.388 -11.263  28.528  1.00 97.64           O\\nANISOU 1886  O   ALA A1074    14228  11998  10874    520   2705     57       O\\nATOM   1887  CB  ALA A1074      36.686  -8.968  30.689  1.00 78.28           C\\nANISOU 1887  CB  ALA A1074    11263   9662   8819    417   2191    709       C\\nATOM   1888  N   VAL A1075      36.430  -9.305  27.419  1.00 95.22           N\\nANISOU 1888  N   VAL A1075    13998  12114  10069     70   2718    348       N\\nATOM   1889  CA  VAL A1075      35.614  -9.821  26.325  1.00 92.66           C\\nANISOU 1889  CA  VAL A1075    14075  11790   9341    -54   2737    139       C\\nATOM   1890  C   VAL A1075      36.457 -10.646  25.357  1.00100.97           C\\nANISOU 1890  C   VAL A1075    15170  12983  10213     22   3217   -207       C\\nATOM   1891  O   VAL A1075      35.987 -11.658  24.824  1.00101.40           O\\nANISOU 1891  O   VAL A1075    15489  12912  10125     79   3272   -531       O\\nATOM   1892  CB  VAL A1075      34.888  -8.661  25.617  1.00 82.73           C\\nANISOU 1892  CB  VAL A1075    13071  10672   7689   -380   2491    377       C\\nATOM   1893  CG1 VAL A1075      34.069  -9.171  24.446  1.00 75.94           C\\nANISOU 1893  CG1 VAL A1075    12635   9852   6368   -528   2457    166       C\\nATOM   1894  CG2 VAL A1075      33.993  -7.930  26.604  1.00 76.88           C\\nANISOU 1894  CG2 VAL A1075    12256   9765   7192   -384   2023    620       C\\nATOM   1895  N   ARG A1076      37.712 -10.240  25.115  1.00100.09           N\\nANISOU 1895  N   ARG A1076    14776  13139  10116     17   3583   -182       N\\nATOM   1896  CA  ARG A1076      38.592 -11.049  24.273  1.00106.02           C\\nANISOU 1896  CA  ARG A1076    15475  14062  10744    139   4103   -579       C\\nATOM   1897  C   ARG A1076      38.740 -12.458  24.828  1.00110.21           C\\nANISOU 1897  C   ARG A1076    15911  14258  11706    564   4141   -922       C\\nATOM   1898  O   ARG A1076      38.867 -13.421  24.062  1.00118.72           O\\nANISOU 1898  O   ARG A1076    17153  15310  12647    690   4425  -1359       O\\nATOM   1899  CB  ARG A1076      39.980 -10.411  24.143  1.00109.75           C\\nANISOU 1899  CB  ARG A1076    15519  14893  11289     84   4503   -500       C\\nATOM   1900  CG  ARG A1076      40.027  -8.904  24.227  1.00109.02           C\\nANISOU 1900  CG  ARG A1076    15378  14979  11066   -286   4338    -22       C\\nATOM   1901  CD  ARG A1076      39.706  -8.229  22.910  1.00113.54           C\\nANISOU 1901  CD  ARG A1076    16360  15831  10947   -724   4457     91       C\\nATOM   1902  NE  ARG A1076      39.657  -6.778  23.063  1.00113.48           N\\nANISOU 1902  NE  ARG A1076    16365  15872  10879  -1069   4203    591       N\\nATOM   1903  CZ  ARG A1076      39.507  -5.923  22.058  1.00114.12           C\\nANISOU 1903  CZ  ARG A1076    16787  16166  10409  -1503   4233    842       C\\nATOM   1904  NH1 ARG A1076      39.395  -6.367  20.812  1.00118.70           N\\nANISOU 1904  NH1 ARG A1076    17722  16997  10383  -1663   4528    629       N\\nATOM   1905  NH2 ARG A1076      39.471  -4.619  22.301  1.00110.17           N\\nANISOU 1905  NH2 ARG A1076    16305  15605   9949  -1786   3945   1307       N\\nATOM   1906  N   GLY A1077      38.727 -12.597  26.152  1.00104.33           N\\nANISOU 1906  N   GLY A1077    14938  13235  11468    780   3843   -732       N\\nATOM   1907  CA  GLY A1077      38.862 -13.893  26.781  1.00103.24           C\\nANISOU 1907  CA  GLY A1077    14749  12715  11761   1164   3801   -960       C\\nATOM   1908  C   GLY A1077      37.555 -14.652  26.832  1.00100.52           C\\nANISOU 1908  C   GLY A1077    14844  12012  11338   1106   3509  -1046       C\\nATOM   1909  O   GLY A1077      37.538 -15.875  26.663  1.00104.59           O\\nANISOU 1909  O   GLY A1077    15516  12220  12003   1321   3586  -1382       O\\nATOM   1910  N   ILE A1078      36.453 -13.936  27.070  1.00 99.32           N\\nANISOU 1910  N   ILE A1078    14869  11880  10988    814   3165   -762       N\\nATOM   1911  CA  ILE A1078      35.138 -14.573  27.087  1.00 95.36           C\\nANISOU 1911  CA  ILE A1078    14721  11103  10410    692   2887   -841       C\\nATOM   1912  C   ILE A1078      34.872 -15.266  25.758  1.00 94.23           C\\nANISOU 1912  C   ILE A1078    14931  10962   9909    611   3076  -1259       C\\nATOM   1913  O   ILE A1078      34.461 -16.432  25.713  1.00 91.07           O\\nANISOU 1913  O   ILE A1078    14757  10213   9633    693   3032  -1537       O\\nATOM   1914  CB  ILE A1078      34.042 -13.542  27.412  1.00 93.90           C\\nANISOU 1914  CB  ILE A1078    14585  11030  10063    404   2522   -518       C\\nATOM   1915  CG1 ILE A1078      33.993 -13.263  28.917  1.00 93.60           C\\nANISOU 1915  CG1 ILE A1078    14291  10873  10400    497   2289   -213       C\\nATOM   1916  CG2 ILE A1078      32.692 -14.024  26.911  1.00 91.88           C\\nANISOU 1916  CG2 ILE A1078    14674  10646   9590    192   2300   -673       C\\nATOM   1917  CD1 ILE A1078      33.002 -12.183  29.313  1.00 86.14           C\\nANISOU 1917  CD1 ILE A1078    13326  10053   9351    273   1966     41       C\\nATOM   1918  N   LEU A1079      35.121 -14.560  24.654  1.00 96.21           N\\nANISOU 1918  N   LEU A1079    15266  11598   9690    421   3283  -1311       N\\nATOM   1919  CA  LEU A1079      34.910 -15.148  23.339  1.00 99.06           C\\nANISOU 1919  CA  LEU A1079    15997  12035   9608    315   3475  -1730       C\\nATOM   1920  C   LEU A1079      35.911 -16.261  23.058  1.00104.43           C\\nANISOU 1920  C   LEU A1079    16609  12586  10483    653   3898  -2204       C\\nATOM   1921  O   LEU A1079      35.576 -17.237  22.375  1.00107.18           O\\nANISOU 1921  O   LEU A1079    17287  12752  10686    675   3966  -2650       O\\nATOM   1922  CB  LEU A1079      34.990 -14.061  22.271  1.00 97.08           C\\nANISOU 1922  CB  LEU A1079    15879  12261   8747     -2   3592  -1606       C\\nATOM   1923  CG  LEU A1079      34.022 -12.896  22.494  1.00 92.62           C\\nANISOU 1923  CG  LEU A1079    15381  11775   8035   -286   3126  -1146       C\\nATOM   1924  CD1 LEU A1079      34.208 -11.832  21.427  1.00 87.85           C\\nANISOU 1924  CD1 LEU A1079    14956  11583   6838   -599   3216   -967       C\\nATOM   1925  CD2 LEU A1079      32.586 -13.395  22.521  1.00 89.61           C\\nANISOU 1925  CD2 LEU A1079    15271  11148   7628   -399   2691  -1233       C\\nATOM   1926  N   ARG A1080      37.134 -16.141  23.574  1.00102.78           N\\nANISOU 1926  N   ARG A1080    15961  12455  10635    932   4161  -2150       N\\nATOM   1927  CA  ARG A1080      38.113 -17.215  23.463  1.00106.42           C\\nANISOU 1927  CA  ARG A1080    16265  12749  11422   1346   4516  -2607       C\\nATOM   1928  C   ARG A1080      37.864 -18.345  24.454  1.00114.00           C\\nANISOU 1928  C   ARG A1080    17260  13084  12971   1658   4225  -2653       C\\nATOM   1929  O   ARG A1080      38.585 -19.348  24.417  1.00121.35           O\\nANISOU 1929  O   ARG A1080    18104  13749  14255   2055   4430  -3041       O\\nATOM   1930  CB  ARG A1080      39.528 -16.662  23.652  1.00 95.46           C\\nANISOU 1930  CB  ARG A1080    14320  11699  10249   1534   4874  -2535       C\\nATOM   1931  N   ASN A1081      36.877 -18.203  25.339  1.00113.30           N\\nANISOU 1931  N   ASN A1081    17292  12754  13003   1487   3760  -2268       N\\nATOM   1932  CA  ASN A1081      36.488 -19.263  26.264  1.00110.82           C\\nANISOU 1932  CA  ASN A1081    17098  11850  13160   1666   3466  -2242       C\\nATOM   1933  C   ASN A1081      35.348 -20.052  25.630  1.00107.85           C\\nANISOU 1933  C   ASN A1081    17225  11189  12565   1437   3324  -2533       C\\nATOM   1934  O   ASN A1081      34.255 -19.516  25.418  1.00 96.74           O\\nANISOU 1934  O   ASN A1081    16004   9943  10809   1044   3098  -2372       O\\nATOM   1935  CB  ASN A1081      36.075 -18.682  27.614  1.00104.89           C\\nANISOU 1935  CB  ASN A1081    16179  11052  12621   1564   3094  -1681       C\\nATOM   1936  CG  ASN A1081      35.935 -19.745  28.696  1.00100.82           C\\nANISOU 1936  CG  ASN A1081    15751   9964  12593   1757   2830  -1573       C\\nATOM   1937  OD1 ASN A1081      35.536 -20.881  28.430  1.00 96.54           O\\nANISOU 1937  OD1 ASN A1081    15540   8975  12166   1793   2783  -1851       O\\nATOM   1938  ND2 ASN A1081      36.265 -19.375  29.927  1.00 99.41           N\\nANISOU 1938  ND2 ASN A1081    15308   9782  12683   1855   2634  -1158       N\\nATOM   1939  N   ALA A1082      35.603 -21.330  25.335  1.00104.72           N\\nANISOU 1939  N   ALA A1082    17030  10346  12412   1693   3425  -2982       N\\nATOM   1940  CA  ALA A1082      34.620 -22.148  24.633  1.00104.56           C\\nANISOU 1940  CA  ALA A1082    17500  10033  12195   1466   3305  -3342       C\\nATOM   1941  C   ALA A1082      33.348 -22.360  25.442  1.00101.54           C\\nANISOU 1941  C   ALA A1082    17302   9334  11945   1142   2845  -3001       C\\nATOM   1942  O   ALA A1082      32.300 -22.654  24.856  1.00101.98           O\\nANISOU 1942  O   ALA A1082    17693   9314  11739    801   2679  -3190       O\\nATOM   1943  CB  ALA A1082      35.231 -23.499  24.264  1.00107.82           C\\nANISOU 1943  CB  ALA A1082    18086   9944  12935   1850   3489  -3914       C\\nATOM   1944  N   LYS A1083      33.409 -22.219  26.764  1.00105.02           N\\nANISOU 1944  N   LYS A1083    17519   9623  12760   1215   2642  -2520       N\\nATOM   1945  CA  LYS A1083      32.243 -22.435  27.607  1.00 99.72           C\\nANISOU 1945  CA  LYS A1083    16986   8701  12202    885   2273  -2194       C\\nATOM   1946  C   LYS A1083      31.446 -21.163  27.871  1.00 97.98           C\\nANISOU 1946  C   LYS A1083    16574   8985  11668    541   2119  -1821       C\\nATOM   1947  O   LYS A1083      30.317 -21.253  28.366  1.00 96.09           O\\nANISOU 1947  O   LYS A1083    16414   8652  11442    209   1857  -1636       O\\nATOM   1948  CB  LYS A1083      32.666 -23.061  28.941  1.00 98.15           C\\nANISOU 1948  CB  LYS A1083    16717   8046  12528   1114   2120  -1873       C\\nATOM   1949  N   LEU A1084      31.992 -19.986  27.551  1.00 99.46           N\\nANISOU 1949  N   LEU A1084    16502   9689  11600    605   2275  -1719       N\\nATOM   1950  CA  LEU A1084      31.288 -18.729  27.771  1.00 97.55           C\\nANISOU 1950  CA  LEU A1084    16090   9867  11109    333   2100  -1390       C\\nATOM   1951  C   LEU A1084      30.919 -17.993  26.491  1.00101.44           C\\nANISOU 1951  C   LEU A1084    16699  10753  11090    121   2131  -1554       C\\nATOM   1952  O   LEU A1084      30.009 -17.161  26.521  1.00102.09           O\\nANISOU 1952  O   LEU A1084    16730  11072  10987   -136   1884  -1351       O\\nATOM   1953  CB  LEU A1084      32.124 -17.790  28.654  1.00 93.67           C\\nANISOU 1953  CB  LEU A1084    15216   9609  10766    522   2147  -1024       C\\nATOM   1954  CG  LEU A1084      32.376 -18.250  30.092  1.00 99.39           C\\nANISOU 1954  CG  LEU A1084    15814  10040  11911    678   2020   -744       C\\nATOM   1955  CD1 LEU A1084      33.068 -17.160  30.896  1.00100.96           C\\nANISOU 1955  CD1 LEU A1084    15645  10540  12174    797   2010   -411       C\\nATOM   1956  CD2 LEU A1084      31.075 -18.668  30.757  1.00 98.30           C\\nANISOU 1956  CD2 LEU A1084    15830   9700  11820    371   1756   -602       C\\nATOM   1957  N   LYS A1085      31.598 -18.269  25.378  1.00102.45           N\\nANISOU 1957  N   LYS A1085    16983  10965  10978    227   2417  -1917       N\\nATOM   1958  CA  LYS A1085      31.262 -17.597  24.126  1.00 99.55           C\\nANISOU 1958  CA  LYS A1085    16799  10990  10037    -13   2431  -2041       C\\nATOM   1959  C   LYS A1085      29.850 -17.899  23.627  1.00 99.81           C\\nANISOU 1959  C   LYS A1085    17128  10950   9847   -354   2083  -2182       C\\nATOM   1960  O   LYS A1085      29.193 -16.966  23.138  1.00 92.79           O\\nANISOU 1960  O   LYS A1085    16268  10388   8598   -594   1861  -2023       O\\nATOM   1961  CB  LYS A1085      32.301 -17.947  23.053  1.00 96.22           C\\nANISOU 1961  CB  LYS A1085    16501  10703   9355    149   2870  -2453       C\\nATOM   1962  N   PRO A1086      29.335 -19.137  23.693  1.00105.32           N\\nANISOU 1962  N   PRO A1086    18044  11220  10751   -402   1987  -2468       N\\nATOM   1963  CA  PRO A1086      27.961 -19.366  23.201  1.00106.72           C\\nANISOU 1963  CA  PRO A1086    18449  11373  10729   -778   1625  -2606       C\\nATOM   1964  C   PRO A1086      26.904 -18.527  23.902  1.00101.72           C\\nANISOU 1964  C   PRO A1086    17551  10915  10184  -1000   1260  -2201       C\\nATOM   1965  O   PRO A1086      26.130 -17.830  23.232  1.00 97.88           O\\nANISOU 1965  O   PRO A1086    17104  10733   9353  -1226    992  -2175       O\\nATOM   1966  CB  PRO A1086      27.759 -20.868  23.445  1.00108.18           C\\nANISOU 1966  CB  PRO A1086    18857  10979  11267   -780   1611  -2917       C\\nATOM   1967  CG  PRO A1086      29.125 -21.438  23.364  1.00108.60           C\\nANISOU 1967  CG  PRO A1086    18951  10834  11479   -369   2012  -3150       C\\nATOM   1968  CD  PRO A1086      30.018 -20.411  23.991  1.00103.81           C\\nANISOU 1968  CD  PRO A1086    17951  10542  10950   -127   2192  -2744       C\\nATOM   1969  N   VAL A1087      26.844 -18.575  25.235  1.00 98.45           N\\nANISOU 1969  N   VAL A1087    16867  10324  10214   -932   1231  -1899       N\\nATOM   1970  CA  VAL A1087      25.825 -17.817  25.956  1.00 96.16           C\\nANISOU 1970  CA  VAL A1087    16290  10223  10024  -1125    937  -1588       C\\nATOM   1971  C   VAL A1087      26.024 -16.321  25.749  1.00 94.05           C\\nANISOU 1971  C   VAL A1087    15830  10386   9517  -1049    881  -1337       C\\nATOM   1972  O   VAL A1087      25.055 -15.564  25.617  1.00 93.16           O\\nANISOU 1972  O   VAL A1087    15592  10501   9302  -1221    565  -1236       O\\nATOM   1973  CB  VAL A1087      25.834 -18.196  27.449  1.00 97.74           C\\nANISOU 1973  CB  VAL A1087    16281  10182  10673  -1078    978  -1328       C\\nATOM   1974  CG1 VAL A1087      27.238 -18.088  28.024  1.00102.40           C\\nANISOU 1974  CG1 VAL A1087    16780  10706  11420   -706   1259  -1166       C\\nATOM   1975  CG2 VAL A1087      24.863 -17.323  28.230  1.00 89.97           C\\nANISOU 1975  CG2 VAL A1087    14954   9465   9765  -1245    754  -1058       C\\nATOM   1976  N   TYR A1088      27.284 -15.876  25.692  1.00 89.69           N\\nANISOU 1976  N   TYR A1088    15242   9934   8902   -793   1168  -1242       N\\nATOM   1977  CA  TYR A1088      27.580 -14.457  25.515  1.00 90.57           C\\nANISOU 1977  CA  TYR A1088    15204  10393   8813   -755   1125   -975       C\\nATOM   1978  C   TYR A1088      26.959 -13.916  24.234  1.00 95.61           C\\nANISOU 1978  C   TYR A1088    16073  11277   8976   -968    892  -1053       C\\nATOM   1979  O   TYR A1088      26.470 -12.781  24.202  1.00 93.98           O\\nANISOU 1979  O   TYR A1088    15753  11275   8682  -1035    611   -805       O\\nATOM   1980  CB  TYR A1088      29.095 -14.250  25.512  1.00 93.94           C\\nANISOU 1980  CB  TYR A1088    15566  10885   9242   -509   1510   -919       C\\nATOM   1981  CG  TYR A1088      29.544 -12.810  25.574  1.00 98.44           C\\nANISOU 1981  CG  TYR A1088    15953  11742   9710   -493   1488   -591       C\\nATOM   1982  CD1 TYR A1088      29.740 -12.178  26.794  1.00 98.86           C\\nANISOU 1982  CD1 TYR A1088    15682  11781  10099   -378   1424   -304       C\\nATOM   1983  CD2 TYR A1088      29.792 -12.088  24.415  1.00103.73           C\\nANISOU 1983  CD2 TYR A1088    16808  12681   9923   -622   1523   -565       C\\nATOM   1984  CE1 TYR A1088      30.162 -10.863  26.860  1.00 99.84           C\\nANISOU 1984  CE1 TYR A1088    15661  12107  10167   -380   1378    -29       C\\nATOM   1985  CE2 TYR A1088      30.213 -10.771  24.470  1.00106.12           C\\nANISOU 1985  CE2 TYR A1088    16981  13181  10158   -650   1482   -232       C\\nATOM   1986  CZ  TYR A1088      30.395 -10.164  25.696  1.00103.83           C\\nANISOU 1986  CZ  TYR A1088    16357  12826  10268   -522   1402     20       C\\nATOM   1987  OH  TYR A1088      30.810  -8.854  25.759  1.00103.35           O\\nANISOU 1987  OH  TYR A1088    16189  12904  10176   -568   1333    326       O\\nATOM   1988  N   ASP A1089      26.969 -14.714  23.164  1.00102.12           N\\nANISOU 1988  N   ASP A1089    17248  12069   9485  -1067    973  -1406       N\\nATOM   1989  CA  ASP A1089      26.320 -14.293  21.927  1.00102.51           C\\nANISOU 1989  CA  ASP A1089    17573  12361   9018  -1301    696  -1486       C\\nATOM   1990  C   ASP A1089      24.810 -14.185  22.110  1.00 97.68           C\\nANISOU 1990  C   ASP A1089    16847  11734   8531  -1503    175  -1453       C\\nATOM   1991  O   ASP A1089      24.193 -13.208  21.669  1.00 94.27           O\\nANISOU 1991  O   ASP A1089    16405  11528   7886  -1603   -198  -1266       O\\nATOM   1992  CB  ASP A1089      26.658 -15.270  20.798  1.00107.75           C\\nANISOU 1992  CB  ASP A1089    18652  12996   9292  -1371    911  -1943       C\\nATOM   1993  CG  ASP A1089      28.153 -15.360  20.522  1.00109.36           C\\nANISOU 1993  CG  ASP A1089    18906  13282   9365  -1158   1468  -2039       C\\nATOM   1994  OD1 ASP A1089      28.859 -14.349  20.724  1.00107.83           O\\nANISOU 1994  OD1 ASP A1089    18522  13306   9142  -1077   1610  -1702       O\\nATOM   1995  OD2 ASP A1089      28.623 -16.442  20.104  1.00108.54           O\\nANISOU 1995  OD2 ASP A1089    19006  13016   9217  -1074   1762  -2478       O\\nATOM   1996  N   SER A1090      24.200 -15.124  22.768  1.00 95.52           N\\nANISOU 1996  N   SER A1090    16469  11190   8635  -1571    131  -1622       N\\nATOM   1997  CA  SER A1090      22.775 -15.087  22.914  1.00100.79           C\\nANISOU 1997  CA  SER A1090    16964  11869   9463  -1805   -311  -1652       C\\nATOM   1998  C   SER A1090      22.220 -13.982  23.739  1.00102.57           C\\nANISOU 1998  C   SER A1090    16755  12269   9949  -1733   -541  -1311       C\\nATOM   1999  O   SER A1090      21.034 -13.763  23.747  1.00106.04           O\\nANISOU 1999  O   SER A1090    16983  12810  10497  -1894   -938  -1340       O\\nATOM   2000  CB  SER A1090      22.377 -16.406  23.588  1.00 99.01           C\\nANISOU 2000  CB  SER A1090    16709  11296   9615  -1937   -227  -1860       C\\nATOM   2001  OG  SER A1090      21.208 -16.357  24.395  1.00 95.53           O\\nANISOU 2001  OG  SER A1090    15874  10901   9522  -2092   -478  -1730       O\\nATOM   2002  N   LEU A1091      23.062 -13.325  24.481  1.00 99.87           N\\nANISOU 2002  N   LEU A1091    16250  11965   9730  -1492   -315  -1031       N\\nATOM   2003  CA  LEU A1091      22.607 -12.416  25.517  1.00 95.87           C\\nANISOU 2003  CA  LEU A1091    15324  11551   9550  -1398   -463   -783       C\\nATOM   2004  C   LEU A1091      22.327 -11.026  24.968  1.00 97.76           C\\nANISOU 2004  C   LEU A1091    15525  12007   9612  -1342   -816   -587       C\\nATOM   2005  O   LEU A1091      23.032 -10.535  24.083  1.00 95.64           O\\nANISOU 2005  O   LEU A1091    15549  11818   8971  -1317   -786   -485       O\\nATOM   2006  CB  LEU A1091      23.641 -12.333  26.638  1.00 87.84           C\\nANISOU 2006  CB  LEU A1091    14159  10436   8780  -1181    -92   -597       C\\nATOM   2007  CG  LEU A1091      23.680 -13.560  27.542  1.00 82.06           C\\nANISOU 2007  CG  LEU A1091    13386   9458   8336  -1224    143   -690       C\\nATOM   2008  CD1 LEU A1091      24.786 -13.425  28.573  1.00 80.82           C\\nANISOU 2008  CD1 LEU A1091    13114   9224   8371   -989    440   -482       C\\nATOM   2009  CD2 LEU A1091      22.327 -13.769  28.206  1.00 80.36           C\\nANISOU 2009  CD2 LEU A1091    12890   9277   8367  -1435    -70   -736       C\\nATOM   2010  N   ASP A1092      21.376 -10.343  25.562  1.00 96.05           N\\nANISOU 2010  N   ASP A1092    14944  11880   9672  -1329  -1151   -538       N\\nATOM   2011  CA  ASP A1092      21.052  -8.988  25.248  1.00 94.58           C\\nANISOU 2011  CA  ASP A1092    14656  11809   9469  -1194  -1512   -321       C\\nATOM   2012  C   ASP A1092      22.222  -8.197  25.771  1.00 90.97           C\\nANISOU 2012  C   ASP A1092    14182  11304   9080   -989  -1249    -61       C\\nATOM   2013  O   ASP A1092      22.961  -8.670  26.567  1.00 94.84           O\\nANISOU 2013  O   ASP A1092    14566  11715   9754   -916   -857    -59       O\\nATOM   2014  CB  ASP A1092      19.780  -8.669  26.007  1.00101.30           C\\nANISOU 2014  CB  ASP A1092    15029  12751  10711  -1166  -1868   -406       C\\nATOM   2015  CG  ASP A1092      19.607  -7.210  26.318  1.00111.33           C\\nANISOU 2015  CG  ASP A1092    16080  14045  12176   -914  -2131   -205       C\\nATOM   2016  OD1 ASP A1092      20.277  -6.361  25.708  1.00117.45           O\\nANISOU 2016  OD1 ASP A1092    17125  14798  12702   -861  -2417     -1       O\\nATOM   2017  OD2 ASP A1092      18.756  -6.904  27.171  1.00112.11           O\\nANISOU 2017  OD2 ASP A1092    15757  14174  12666   -784  -2057   -258       O\\nATOM   2018  N   ALA A1093      22.381  -6.966  25.331  1.00 96.88           N\\nANISOU 2018  N   ALA A1093    15054  12081   9674   -916  -1505    178       N\\nATOM   2019  CA  ALA A1093      23.488  -6.122  25.778  1.00 91.46           C\\nANISOU 2019  CA  ALA A1093    14374  11336   9042   -782  -1292    431       C\\nATOM   2020  C   ALA A1093      23.421  -5.832  27.272  1.00 93.10           C\\nANISOU 2020  C   ALA A1093    14165  11492   9718   -603  -1188    414       C\\nATOM   2021  O   ALA A1093      24.464  -5.712  27.927  1.00 87.73           O\\nANISOU 2021  O   ALA A1093    13451  10765   9118   -524   -866    519       O\\nATOM   2022  CB  ALA A1093      23.503  -4.814  24.988  1.00 88.70           C\\nANISOU 2022  CB  ALA A1093    14227  10970   8505   -779  -1676    717       C\\nATOM   2023  N   VAL A1094      22.214  -5.720  27.829  1.00 97.94           N\\nANISOU 2023  N   VAL A1094    14439  12147  10627   -546  -1450    262       N\\nATOM   2024  CA  VAL A1094      22.076  -5.445  29.257  1.00 93.00           C\\nANISOU 2024  CA  VAL A1094    13427  11531  10378   -399  -1324    200       C\\nATOM   2025  C   VAL A1094      22.441  -6.680  30.072  1.00 88.59           C\\nANISOU 2025  C   VAL A1094    12819  10982   9860   -491   -879     98       C\\nATOM   2026  O   VAL A1094      23.204  -6.601  31.041  1.00 83.02           O\\nANISOU 2026  O   VAL A1094    12036  10247   9261   -400   -616    175       O\\nATOM   2027  CB  VAL A1094      20.652  -4.956  29.576  1.00 91.34           C\\nANISOU 2027  CB  VAL A1094    12822  11413  10469   -310  -1694     21       C\\nATOM   2028  CG1 VAL A1094      20.546  -4.549  31.038  1.00 87.18           C\\nANISOU 2028  CG1 VAL A1094    11914  10940  10271   -155  -1529    -81       C\\nATOM   2029  CG2 VAL A1094      20.261  -3.802  28.656  1.00 92.19           C\\nANISOU 2029  CG2 VAL A1094    13027  11445  10557   -192  -2230    148       C\\nATOM   2030  N   ARG A1095      21.898  -7.840  29.694  1.00 90.63           N\\nANISOU 2030  N   ARG A1095    13144  11253  10038   -685   -833    -66       N\\nATOM   2031  CA  ARG A1095      22.284  -9.087  30.344  1.00 90.96           C\\nANISOU 2031  CA  ARG A1095    13231  11214  10116   -790   -456   -122       C\\nATOM   2032  C   ARG A1095      23.746  -9.427  30.091  1.00 87.34           C\\nANISOU 2032  C   ARG A1095    13078  10619   9487   -715   -154      0       C\\nATOM   2033  O   ARG A1095      24.354 -10.144  30.893  1.00 79.42           O\\nANISOU 2033  O   ARG A1095    12074   9515   8587   -689    132     31       O\\nATOM   2034  CB  ARG A1095      21.389 -10.229  29.864  1.00 87.99           C\\nANISOU 2034  CB  ARG A1095    12907  10817   9709  -1046   -517   -333       C\\nATOM   2035  CG  ARG A1095      19.913  -9.890  29.887  1.00 88.08           C\\nANISOU 2035  CG  ARG A1095    12562  11010   9896  -1139   -853   -486       C\\nATOM   2036  CD  ARG A1095      19.099 -10.979  29.236  1.00 93.06           C\\nANISOU 2036  CD  ARG A1095    13265  11616  10479  -1439   -963   -697       C\\nATOM   2037  NE  ARG A1095      17.793 -10.502  28.791  1.00103.22           N\\nANISOU 2037  NE  ARG A1095    14244  13099  11877  -1501  -1404   -846       N\\nATOM   2038  CZ  ARG A1095      16.679 -10.583  29.511  1.00102.98           C\\nANISOU 2038  CZ  ARG A1095    13724  13246  12157  -1620  -1455   -997       C\\nATOM   2039  NH1 ARG A1095      16.705 -11.126  30.720  1.00101.20           N\\nANISOU 2039  NH1 ARG A1095    13324  13034  12095  -1735  -1072   -988       N\\nATOM   2040  NH2 ARG A1095      15.535 -10.122  29.020  1.00102.93           N\\nANISOU 2040  NH2 ARG A1095    13394  13427  12289  -1634  -1897  -1154       N\\nATOM   2041  N   ARG A1096      24.321  -8.920  29.001  1.00 90.45           N\\nANISOU 2041  N   ARG A1096    13718  11024   9623   -685   -218     78       N\\nATOM   2042  CA  ARG A1096      25.730  -9.168  28.728  1.00 86.04           C\\nANISOU 2042  CA  ARG A1096    13368  10402   8921   -614    110    159       C\\nATOM   2043  C   ARG A1096      26.623  -8.481  29.750  1.00 81.52           C\\nANISOU 2043  C   ARG A1096    12598   9829   8548   -445    250    350       C\\nATOM   2044  O   ARG A1096      27.697  -8.997  30.076  1.00 76.37           O\\nANISOU 2044  O   ARG A1096    11967   9110   7940   -359    548    380       O\\nATOM   2045  CB  ARG A1096      26.072  -8.706  27.313  1.00 85.80           C\\nANISOU 2045  CB  ARG A1096    13637  10453   8510   -686     38    205       C\\nATOM   2046  CG  ARG A1096      26.974  -9.657  26.568  1.00 82.89           C\\nANISOU 2046  CG  ARG A1096    13541  10054   7898   -716    389     63       C\\nATOM   2047  CD  ARG A1096      27.247  -9.180  25.159  1.00 85.44           C\\nANISOU 2047  CD  ARG A1096    14183  10531   7750   -844    350    102       C\\nATOM   2048  NE  ARG A1096      26.098  -9.355  24.282  1.00 94.36           N\\nANISOU 2048  NE  ARG A1096    15514  11710   8629  -1018     -6    -32       N\\nATOM   2049  CZ  ARG A1096      26.167  -9.297  22.957  1.00 97.59           C\\nANISOU 2049  CZ  ARG A1096    16291  12257   8531  -1179    -60    -72       C\\nATOM   2050  NH1 ARG A1096      27.333  -9.075  22.369  1.00 93.17           N\\nANISOU 2050  NH1 ARG A1096    15919  11820   7663  -1201    286      6       N\\nATOM   2051  NH2 ARG A1096      25.078  -9.465  22.222  1.00102.27           N\\nANISOU 2051  NH2 ARG A1096    17053  12899   8906  -1338   -456   -197       N\\nATOM   2052  N   ALA A1097      26.196  -7.325  30.270  1.00 83.15           N\\nANISOU 2052  N   ALA A1097    12599  10095   8899   -381     10    450       N\\nATOM   2053  CA  ALA A1097      26.963  -6.656  31.316  1.00 74.83           C\\nANISOU 2053  CA  ALA A1097    11361   9035   8036   -245    100    585       C\\nATOM   2054  C   ALA A1097      26.946  -7.446  32.617  1.00 73.67           C\\nANISOU 2054  C   ALA A1097    11047   8874   8072   -207    277    525       C\\nATOM   2055  O   ALA A1097      27.942  -7.452  33.348  1.00 74.45           O\\nANISOU 2055  O   ALA A1097    11087   8949   8253   -111    442    628       O\\nATOM   2056  CB  ALA A1097      26.423  -5.246  31.550  1.00 63.51           C\\nANISOU 2056  CB  ALA A1097     9778   7621   6732   -175   -226    643       C\\nATOM   2057  N   ALA A1098      25.832  -8.117  32.923  1.00 71.99           N\\nANISOU 2057  N   ALA A1098    10755   8685   7912   -311    230    379       N\\nATOM   2058  CA  ALA A1098      25.774  -8.940  34.125  1.00 74.69           C\\nANISOU 2058  CA  ALA A1098    11001   9011   8365   -346    407    373       C\\nATOM   2059  C   ALA A1098      26.760 -10.098  34.047  1.00 83.58           C\\nANISOU 2059  C   ALA A1098    12344   9949   9462   -326    646    434       C\\nATOM   2060  O   ALA A1098      27.358 -10.485  35.059  1.00 82.43           O\\nANISOU 2060  O   ALA A1098    12168   9750   9403   -262    768    547       O\\nATOM   2061  CB  ALA A1098      24.351  -9.450  34.338  1.00 76.99           C\\nANISOU 2061  CB  ALA A1098    11160   9381   8710   -537    335    213       C\\nATOM   2062  N   LEU A1099      26.946 -10.665  32.852  1.00 86.05           N\\nANISOU 2062  N   LEU A1099    12886  10156   9651   -363    693    343       N\\nATOM   2063  CA  LEU A1099      27.950 -11.710  32.691  1.00 84.37           C\\nANISOU 2063  CA  LEU A1099    12858   9742   9457   -276    922    336       C\\nATOM   2064  C   LEU A1099      29.360 -11.153  32.838  1.00 75.62           C\\nANISOU 2064  C   LEU A1099    11669   8675   8388    -65   1050    473       C\\nATOM   2065  O   LEU A1099      30.242 -11.829  33.380  1.00 59.72           O\\nANISOU 2065  O   LEU A1099     9651   6525   6517     79   1192    528       O\\nATOM   2066  CB  LEU A1099      27.785 -12.397  31.335  1.00 88.81           C\\nANISOU 2066  CB  LEU A1099    13687  10211   9847   -362    961    126       C\\nATOM   2067  CG  LEU A1099      28.635 -13.647  31.091  1.00 89.13           C\\nANISOU 2067  CG  LEU A1099    13929   9988   9947   -253   1195     11       C\\nATOM   2068  CD1 LEU A1099      28.246 -14.750  32.060  1.00 88.78           C\\nANISOU 2068  CD1 LEU A1099    13929   9678  10126   -318   1188     43       C\\nATOM   2069  CD2 LEU A1099      28.496 -14.118  29.655  1.00 91.08           C\\nANISOU 2069  CD2 LEU A1099    14451  10201   9955   -337   1240   -262       C\\nATOM   2070  N   ILE A1100      29.591  -9.928  32.363  1.00 70.27           N\\nANISOU 2070  N   ILE A1100    10921   8168   7612    -56    974    541       N\\nATOM   2071  CA  ILE A1100      30.888  -9.294  32.557  1.00 70.30           C\\nANISOU 2071  CA  ILE A1100    10796   8234   7680     77   1083    680       C\\nATOM   2072  C   ILE A1100      31.120  -9.006  34.034  1.00 76.98           C\\nANISOU 2072  C   ILE A1100    11428   9092   8729    165   1006    808       C\\nATOM   2073  O   ILE A1100      32.244  -9.120  34.537  1.00 80.54           O\\nANISOU 2073  O   ILE A1100    11764   9529   9310    301   1104    897       O\\nATOM   2074  CB  ILE A1100      30.983  -8.022  31.697  1.00 68.88           C\\nANISOU 2074  CB  ILE A1100    10638   8193   7340    -10    989    761       C\\nATOM   2075  CG1 ILE A1100      30.869  -8.386  30.212  1.00 75.73           C\\nANISOU 2075  CG1 ILE A1100    11771   9090   7912   -120   1082    646       C\\nATOM   2076  CG2 ILE A1100      32.279  -7.281  31.978  1.00 63.94           C\\nANISOU 2076  CG2 ILE A1100     9841   7638   6817     56   1090    917       C\\nATOM   2077  CD1 ILE A1100      30.869  -7.196  29.275  1.00 65.67           C\\nANISOU 2077  CD1 ILE A1100    10607   7938   6405   -260    954    784       C\\nATOM   2078  N   ASN A1101      30.057  -8.645  34.757  1.00 76.26           N\\nANISOU 2078  N   ASN A1101    11262   9055   8656     88    828    795       N\\nATOM   2079  CA  ASN A1101      30.161  -8.449  36.200  1.00 71.74           C\\nANISOU 2079  CA  ASN A1101    10532   8535   8191    138    773    876       C\\nATOM   2080  C   ASN A1101      30.619  -9.725  36.896  1.00 69.64           C\\nANISOU 2080  C   ASN A1101    10339   8134   7987    190    891    949       C\\nATOM   2081  O   ASN A1101      31.439  -9.679  37.821  1.00 64.42           O\\nANISOU 2081  O   ASN A1101     9588   7486   7403    297    869   1078       O\\nATOM   2082  CB  ASN A1101      28.811  -7.981  36.750  1.00 72.99           C\\nANISOU 2082  CB  ASN A1101    10589   8814   8330     34    629    774       C\\nATOM   2083  CG  ASN A1101      28.882  -7.542  38.204  1.00 79.76           C\\nANISOU 2083  CG  ASN A1101    11293   9793   9219     68    586    807       C\\nATOM   2084  OD1 ASN A1101      29.385  -8.264  39.065  1.00 88.11           O\\nANISOU 2084  OD1 ASN A1101    12391  10824  10262     80    664    919       O\\nATOM   2085  ND2 ASN A1101      28.363  -6.353  38.484  1.00 77.04           N\\nANISOU 2085  ND2 ASN A1101    10794   9569   8909     92    434    696       N\\nATOM   2086  N   MET A1102      30.111 -10.877  36.452  1.00 67.47           N\\nANISOU 2086  N   MET A1102    10246   7696   7691    110    973    875       N\\nATOM   2087  CA  MET A1102      30.457 -12.137  37.100  1.00 68.00           C\\nANISOU 2087  CA  MET A1102    10442   7546   7851    150   1035    971       C\\nATOM   2088  C   MET A1102      31.900 -12.539  36.815  1.00 75.21           C\\nANISOU 2088  C   MET A1102    11354   8314   8910    407   1126   1011       C\\nATOM   2089  O   MET A1102      32.611 -12.984  37.723  1.00 77.63           O\\nANISOU 2089  O   MET A1102    11635   8519   9341    543   1075   1172       O\\nATOM   2090  CB  MET A1102      29.492 -13.233  36.655  1.00 70.40           C\\nANISOU 2090  CB  MET A1102    10958   7659   8132    -38   1075    861       C\\nATOM   2091  CG  MET A1102      28.072 -13.024  37.150  1.00 76.57           C\\nANISOU 2091  CG  MET A1102    11663   8605   8824   -310   1005    826       C\\nATOM   2092  SD  MET A1102      27.010 -14.445  36.822  1.00 81.97           S\\nANISOU 2092  SD  MET A1102    12572   9042   9532   -608   1039    733       S\\nATOM   2093  CE  MET A1102      27.916 -15.743  37.652  1.00 80.68           C\\nANISOU 2093  CE  MET A1102    12664   8490   9502   -523   1086    972       C\\nATOM   2094  N   VAL A1103      32.352 -12.395  35.565  1.00 79.58           N\\nANISOU 2094  N   VAL A1103    11918   8879   9439    475   1257    861       N\\nATOM   2095  CA  VAL A1103      33.743 -12.721  35.251  1.00 82.54           C\\nANISOU 2095  CA  VAL A1103    12205   9184   9974    728   1400    840       C\\nATOM   2096  C   VAL A1103      34.689 -11.726  35.912  1.00 80.24           C\\nANISOU 2096  C   VAL A1103    11618   9095   9774    826   1331   1000       C\\nATOM   2097  O   VAL A1103      35.848 -12.053  36.198  1.00 82.23           O\\nANISOU 2097  O   VAL A1103    11705   9299  10238   1051   1366   1045       O\\nATOM   2098  CB  VAL A1103      33.969 -12.782  33.727  1.00 84.75           C\\nANISOU 2098  CB  VAL A1103    12570   9500  10133    729   1619    609       C\\nATOM   2099  CG1 VAL A1103      32.942 -13.689  33.066  1.00 85.19           C\\nANISOU 2099  CG1 VAL A1103    12933   9364  10070    590   1631    415       C\\nATOM   2100  CG2 VAL A1103      33.931 -11.394  33.115  1.00 83.71           C\\nANISOU 2100  CG2 VAL A1103    12339   9665   9801    582   1615    646       C\\nATOM   2101  N   PHE A1104      34.222 -10.502  36.163  1.00 72.46           N\\nANISOU 2101  N   PHE A1104    10543   8321   8669    670   1206   1064       N\\nATOM   2102  CA  PHE A1104      35.025  -9.556  36.927  1.00 74.27           C\\nANISOU 2102  CA  PHE A1104    10521   8703   8994    721   1090   1196       C\\nATOM   2103  C   PHE A1104      35.203 -10.013  38.369  1.00 79.15           C\\nANISOU 2103  C   PHE A1104    11108   9268   9696    808    920   1340       C\\nATOM   2104  O   PHE A1104      36.258  -9.779  38.969  1.00 81.90           O\\nANISOU 2104  O   PHE A1104    11250   9676  10191    937    827   1439       O\\nATOM   2105  CB  PHE A1104      34.382  -8.171  36.883  1.00 67.54           C\\nANISOU 2105  CB  PHE A1104     9633   8010   8019    545    959   1195       C\\nATOM   2106  CG  PHE A1104      35.032  -7.234  35.911  1.00 71.68           C\\nANISOU 2106  CG  PHE A1104    10068   8632   8534    483   1036   1205       C\\nATOM   2107  CD1 PHE A1104      34.785  -7.340  34.554  1.00 74.18           C\\nANISOU 2107  CD1 PHE A1104    10546   8950   8690    396   1191   1126       C\\nATOM   2108  CD2 PHE A1104      35.892  -6.243  36.356  1.00 80.86           C\\nANISOU 2108  CD2 PHE A1104    11011   9893   9821    465    944   1303       C\\nATOM   2109  CE1 PHE A1104      35.384  -6.477  33.659  1.00 78.16           C\\nANISOU 2109  CE1 PHE A1104    11011   9565   9121    278   1280   1183       C\\nATOM   2110  CE2 PHE A1104      36.492  -5.376  35.467  1.00 85.63           C\\nANISOU 2110  CE2 PHE A1104    11550  10576  10412    335   1028   1354       C\\nATOM   2111  CZ  PHE A1104      36.238  -5.493  34.115  1.00 81.25           C\\nANISOU 2111  CZ  PHE A1104    11176  10035   9661    234   1209   1314       C\\nATOM   2112  N   GLN A1105      34.192 -10.669  38.935  1.00 80.45           N\\nANISOU 2112  N   GLN A1105    11475   9341   9754    708    866   1365       N\\nATOM   2113  CA  GLN A1105      34.237 -11.118  40.319  1.00 76.17           C\\nANISOU 2113  CA  GLN A1105    10978   8769   9193    723    706   1544       C\\nATOM   2114  C   GLN A1105      34.839 -12.508  40.465  1.00 79.87           C\\nANISOU 2114  C   GLN A1105    11579   8938   9829    899    695   1660       C\\nATOM   2115  O   GLN A1105      35.670 -12.731  41.352  1.00 77.78           O\\nANISOU 2115  O   GLN A1105    11252   8640   9660   1051    517   1841       O\\nATOM   2116  CB  GLN A1105      32.830 -11.107  40.918  1.00 71.88           C\\nANISOU 2116  CB  GLN A1105    10574   8313   8426    472    687   1531       C\\nATOM   2117  CG  GLN A1105      32.752 -11.692  42.313  1.00 71.95           C\\nANISOU 2117  CG  GLN A1105    10707   8315   8315    408    569   1741       C\\nATOM   2118  CD  GLN A1105      31.379 -11.534  42.928  1.00 72.70           C\\nANISOU 2118  CD  GLN A1105    10864   8598   8159    121    622   1689       C\\nATOM   2119  OE1 GLN A1105      30.414 -11.193  42.241  1.00 76.06           O\\nANISOU 2119  OE1 GLN A1105    11232   9099   8567     -1    727   1488       O\\nATOM   2120  NE2 GLN A1105      31.282 -11.777  44.230  1.00 68.30           N\\nANISOU 2120  NE2 GLN A1105    10410   8146   7396      7    545   1865       N\\nATOM   2121  N   MET A1106      34.433 -13.446  39.607  1.00 80.28           N\\nANISOU 2121  N   MET A1106    11826   8743   9934    892    842   1548       N\\nATOM   2122  CA  MET A1106      34.803 -14.847  39.734  1.00 82.95           C\\nANISOU 2122  CA  MET A1106    12358   8697  10463   1051    807   1630       C\\nATOM   2123  C   MET A1106      35.843 -15.311  38.725  1.00 89.43           C\\nANISOU 2123  C   MET A1106    13075   9350  11554   1362    949   1444       C\\nATOM   2124  O   MET A1106      36.305 -16.452  38.830  1.00 92.75           O\\nANISOU 2124  O   MET A1106    13623   9404  12215   1580    890   1476       O\\nATOM   2125  CB  MET A1106      33.551 -15.727  39.604  1.00 79.57           C\\nANISOU 2125  CB  MET A1106    12259   8043   9930    793    855   1607       C\\nATOM   2126  CG  MET A1106      32.706 -15.755  40.856  1.00 84.73           C\\nANISOU 2126  CG  MET A1106    13038   8785  10370    512    733   1843       C\\nATOM   2127  SD  MET A1106      30.984 -16.135  40.503  1.00 86.03           S\\nANISOU 2127  SD  MET A1106    13388   8937  10364     82    862   1721       S\\nATOM   2128  CE  MET A1106      30.421 -14.540  39.929  1.00 88.27           C\\nANISOU 2128  CE  MET A1106    13356   9694  10490     13    937   1471       C\\nATOM   2129  N   GLY A1107      36.219 -14.477  37.763  1.00 83.47           N\\nANISOU 2129  N   GLY A1107    12104   8844  10768   1383   1136   1249       N\\nATOM   2130  CA  GLY A1107      37.045 -14.923  36.668  1.00 86.98           C\\nANISOU 2130  CA  GLY A1107    12460   9202  11389   1617   1365   1006       C\\nATOM   2131  C   GLY A1107      36.292 -15.824  35.707  1.00 88.79           C\\nANISOU 2131  C   GLY A1107    13014   9179  11544   1543   1521    764       C\\nATOM   2132  O   GLY A1107      35.264 -16.426  36.027  1.00 86.13           O\\nANISOU 2132  O   GLY A1107    12973   8625  11128   1354   1409    824       O\\nATOM   2133  N   GLU A1108      36.843 -15.917  34.497  1.00 89.49           N\\nANISOU 2133  N   GLU A1108    13038   9319  11644   1667   1796    468       N\\nATOM   2134  CA  GLU A1108      36.262 -16.761  33.464  1.00 87.52           C\\nANISOU 2134  CA  GLU A1108    13103   8850  11300   1613   1951    163       C\\nATOM   2135  C   GLU A1108      36.230 -18.231  33.861  1.00 85.64           C\\nANISOU 2135  C   GLU A1108    13113   8070  11356   1798   1837    124       C\\nATOM   2136  O   GLU A1108      35.365 -18.973  33.377  1.00 84.49           O\\nANISOU 2136  O   GLU A1108    13313   7661  11130   1634   1842    -46       O\\nATOM   2137  CB  GLU A1108      37.029 -16.590  32.160  1.00 95.88           C\\nANISOU 2137  CB  GLU A1108    14037  10114  12279   1733   2303   -169       C\\nATOM   2138  CG  GLU A1108      36.931 -15.181  31.598  1.00102.62           C\\nANISOU 2138  CG  GLU A1108    14756  11443  12792   1470   2402   -100       C\\nATOM   2139  CD  GLU A1108      37.375 -15.104  30.157  1.00109.37           C\\nANISOU 2139  CD  GLU A1108    15629  12514  13413   1456   2771   -421       C\\nATOM   2140  OE1 GLU A1108      37.716 -16.168  29.591  1.00113.53           O\\nANISOU 2140  OE1 GLU A1108    16260  12832  14044   1672   2970   -764       O\\nATOM   2141  OE2 GLU A1108      37.380 -13.985  29.593  1.00105.41           O\\nANISOU 2141  OE2 GLU A1108    15063  12377  12612   1221   2859   -335       O\\nATOM   2142  N   THR A1109      37.155 -18.669  34.719  1.00 90.70           N\\nANISOU 2142  N   THR A1109    13597   8510  12353   2124   1695    286       N\\nATOM   2143  CA  THR A1109      37.120 -20.042  35.207  1.00 95.84           C\\nANISOU 2143  CA  THR A1109    14532   8571  13311   2298   1506    331       C\\nATOM   2144  C   THR A1109      35.855 -20.297  36.012  1.00 92.70           C\\nANISOU 2144  C   THR A1109    14477   8003  12741   1906   1273    629       C\\nATOM   2145  O   THR A1109      35.133 -21.269  35.766  1.00 95.09           O\\nANISOU 2145  O   THR A1109    15151   7895  13084   1765   1241    533       O\\nATOM   2146  CB  THR A1109      38.349 -20.335  36.066  1.00 97.86           C\\nANISOU 2146  CB  THR A1109    14535   8674  13974   2728   1309    517       C\\nATOM   2147  OG1 THR A1109      39.538 -19.920  35.381  1.00102.45           O\\nANISOU 2147  OG1 THR A1109    14672   9535  14718   3048   1561    242       O\\nATOM   2148  CG2 THR A1109      38.427 -21.828  36.376  1.00 97.85           C\\nANISOU 2148  CG2 THR A1109    14861   7969  14349   2976   1099    531       C\\nATOM   2149  N   GLY A1110      35.567 -19.420  36.975  1.00 95.75           N\\nANISOU 2149  N   GLY A1110    14731   8720  12931   1701   1128    965       N\\nATOM   2150  CA  GLY A1110      34.456 -19.660  37.880  1.00 94.88           C\\nANISOU 2150  CA  GLY A1110    14887   8513  12649   1331    949   1253       C\\nATOM   2151  C   GLY A1110      33.103 -19.552  37.204  1.00 88.67           C\\nANISOU 2151  C   GLY A1110    14261   7826  11602    922   1075   1072       C\\nATOM   2152  O   GLY A1110      32.191 -20.329  37.497  1.00 82.42           O\\nANISOU 2152  O   GLY A1110    13765   6760  10793    635    997   1160       O\\nATOM   2153  N   VAL A1111      32.952 -18.588  36.296  1.00 85.36           N\\nANISOU 2153  N   VAL A1111    13649   7799  10986    866   1244    836       N\\nATOM   2154  CA  VAL A1111      31.676 -18.422  35.606  1.00 83.59           C\\nANISOU 2154  CA  VAL A1111    13541   7694  10525    508   1297    660       C\\nATOM   2155  C   VAL A1111      31.371 -19.646  34.751  1.00 86.94           C\\nANISOU 2155  C   VAL A1111    14292   7686  11055    469   1346    385       C\\nATOM   2156  O   VAL A1111      30.217 -20.080  34.649  1.00 84.62           O\\nANISOU 2156  O   VAL A1111    14188   7281  10681    116   1284    338       O\\nATOM   2157  CB  VAL A1111      31.689 -17.125  34.776  1.00 78.72           C\\nANISOU 2157  CB  VAL A1111    12692   7539   9679    492   1403    508       C\\nATOM   2158  CG1 VAL A1111      30.403 -16.979  33.994  1.00 82.94           C\\nANISOU 2158  CG1 VAL A1111    13340   8183   9992    166   1385    324       C\\nATOM   2159  CG2 VAL A1111      31.894 -15.925  35.684  1.00 68.67           C\\nANISOU 2159  CG2 VAL A1111    11133   6621   8339    498   1317    755       C\\nATOM   2160  N   ALA A1112      32.402 -20.242  34.147  1.00 83.83           N\\nANISOU 2160  N   ALA A1112    13946   7039  10867    828   1457    166       N\\nATOM   2161  CA  ALA A1112      32.208 -21.434  33.331  1.00 86.95           C\\nANISOU 2161  CA  ALA A1112    14676   6976  11386    838   1502   -166       C\\nATOM   2162  C   ALA A1112      31.727 -22.636  34.137  1.00 97.68           C\\nANISOU 2162  C   ALA A1112    16361   7762  12989    696   1293     31       C\\nATOM   2163  O   ALA A1112      31.408 -23.672  33.541  1.00107.07           O\\nANISOU 2163  O   ALA A1112    17878   8495  14308    634   1283   -236       O\\nATOM   2164  CB  ALA A1112      33.504 -21.784  32.597  1.00 82.87           C\\nANISOU 2164  CB  ALA A1112    14088   6331  11068   1312   1699   -487       C\\nATOM   2165  N   GLY A1113      31.670 -22.528  35.467  1.00 94.08           N\\nANISOU 2165  N   GLY A1113    15859   7311  12576    613   1121    490       N\\nATOM   2166  CA  GLY A1113      31.127 -23.580  36.301  1.00 91.96           C\\nANISOU 2166  CA  GLY A1113    15934   6547  12461    374    924    767       C\\nATOM   2167  C   GLY A1113      29.632 -23.536  36.499  1.00 88.01           C\\nANISOU 2167  C   GLY A1113    15526   6189  11726   -228    907    854       C\\nATOM   2168  O   GLY A1113      29.067 -24.463  37.088  1.00 90.55           O\\nANISOU 2168  O   GLY A1113    16155   6098  12153   -532    780   1074       O\\nATOM   2169  N   PHE A1114      28.975 -22.477  36.030  1.00 89.32           N\\nANISOU 2169  N   PHE A1114    15419   6923  11597   -417   1020    697       N\\nATOM   2170  CA  PHE A1114      27.518 -22.347  36.101  1.00 93.06           C\\nANISOU 2170  CA  PHE A1114    15868   7604  11887   -955   1007    701       C\\nATOM   2171  C   PHE A1114      26.844 -22.935  34.867  1.00 97.68           C\\nANISOU 2171  C   PHE A1114    16640   7982  12490  -1154   1008    293       C\\nATOM   2172  O   PHE A1114      25.996 -22.294  34.250  1.00100.46           O\\nANISOU 2172  O   PHE A1114    16812   8720  12638  -1379   1016     94       O\\nATOM   2173  CB  PHE A1114      27.127 -20.883  36.266  1.00 94.49           C\\nANISOU 2173  CB  PHE A1114    15638   8468  11794  -1010   1062    728       C\\nATOM   2174  CG  PHE A1114      27.602 -20.258  37.542  1.00 95.33           C\\nANISOU 2174  CG  PHE A1114    15570   8818  11834   -900   1044   1086       C\\nATOM   2175  CD1 PHE A1114      26.863 -20.382  38.706  1.00 96.26           C\\nANISOU 2175  CD1 PHE A1114    15694   9032  11847  -1255   1023   1375       C\\nATOM   2176  CD2 PHE A1114      28.773 -19.521  37.572  1.00 93.76           C\\nANISOU 2176  CD2 PHE A1114    15190   8788  11647   -478   1057   1113       C\\nATOM   2177  CE1 PHE A1114      27.293 -19.799  39.881  1.00 93.49           C\\nANISOU 2177  CE1 PHE A1114    15219   8937  11366  -1170    999   1669       C\\nATOM   2178  CE2 PHE A1114      29.209 -18.933  38.743  1.00 90.99           C\\nANISOU 2178  CE2 PHE A1114    14688   8664  11219   -396    999   1410       C\\nATOM   2179  CZ  PHE A1114      28.468 -19.072  39.900  1.00 89.90           C\\nANISOU 2179  CZ  PHE A1114    14603   8619  10937   -731    961   1678       C\\nATOM   2180  N   THR A1115      27.213 -24.163  34.496  1.00 93.63           N\\nANISOU 2180  N   THR A1115    16502   6840  12234  -1062    963    146       N\\nATOM   2181  CA  THR A1115      26.755 -24.715  33.225  1.00 97.80           C\\nANISOU 2181  CA  THR A1115    17241   7160  12760  -1192    960   -325       C\\nATOM   2182  C   THR A1115      25.237 -24.821  33.175  1.00101.53           C\\nANISOU 2182  C   THR A1115    17699   7752  13126  -1809    862   -353       C\\nATOM   2183  O   THR A1115      24.618 -24.467  32.164  1.00100.69           O\\nANISOU 2183  O   THR A1115    17515   7914  12829  -1958    838   -694       O\\nATOM   2184  CB  THR A1115      27.395 -26.081  32.984  1.00104.56           C\\nANISOU 2184  CB  THR A1115    18523   7240  13966   -980    909   -494       C\\nATOM   2185  OG1 THR A1115      26.936 -27.010  33.974  1.00111.74           O\\nANISOU 2185  OG1 THR A1115    19700   7650  15106  -1304    745   -134       O\\nATOM   2186  CG2 THR A1115      28.912 -25.975  33.059  1.00103.25           C\\nANISOU 2186  CG2 THR A1115    18273   6991  13964   -334   1002   -493       C\\nATOM   2187  N   ASN A1116      24.617 -25.292  34.259  1.00109.01           N\\nANISOU 2187  N   ASN A1116    18703   8536  14180  -2193    797     12       N\\nATOM   2188  CA  ASN A1116      23.168 -25.450  34.256  1.00114.25           C\\nANISOU 2188  CA  ASN A1116    19286   9335  14790  -2821    734    -24       C\\nATOM   2189  C   ASN A1116      22.464 -24.103  34.180  1.00108.33           C\\nANISOU 2189  C   ASN A1116    18027   9368  13766  -2910    776    -69       C\\nATOM   2190  O   ASN A1116      21.401 -23.993  33.560  1.00112.39           O\\nANISOU 2190  O   ASN A1116    18389  10096  14219  -3257    688   -317       O\\nATOM   2191  CB  ASN A1116      22.716 -26.227  35.496  1.00119.12           C\\nANISOU 2191  CB  ASN A1116    20066   9646  15546  -3254    712    417       C\\nATOM   2192  N   SER A1117      23.040 -23.071  34.794  1.00107.10           N\\nANISOU 2192  N   SER A1117    17599   9621  13474  -2592    871    149       N\\nATOM   2193  CA  SER A1117      22.434 -21.748  34.719  1.00102.31           C\\nANISOU 2193  CA  SER A1117    16531   9686  12658  -2613    880     85       C\\nATOM   2194  C   SER A1117      22.674 -21.101  33.361  1.00102.29           C\\nANISOU 2194  C   SER A1117    16484   9870  12513  -2343    814   -265       C\\nATOM   2195  O   SER A1117      21.756 -20.507  32.785  1.00100.23           O\\nANISOU 2195  O   SER A1117    15984   9960  12139  -2521    696   -453       O\\nATOM   2196  CB  SER A1117      22.981 -20.857  35.835  1.00 98.47           C\\nANISOU 2196  CB  SER A1117    15811   9527  12076  -2381    982    404       C\\nATOM   2197  OG  SER A1117      22.892 -21.504  37.092  1.00 97.73           O\\nANISOU 2197  OG  SER A1117    15842   9258  12035  -2624   1039    761       O\\nATOM   2198  N   LEU A1118      23.897 -21.215  32.836  1.00104.26           N\\nANISOU 2198  N   LEU A1118    16951   9904  12761  -1923    883   -351       N\\nATOM   2199  CA  LEU A1118      24.243 -20.548  31.585  1.00100.23           C\\nANISOU 2199  CA  LEU A1118    16425   9622  12038  -1690    875   -637       C\\nATOM   2200  C   LEU A1118      23.389 -21.046  30.427  1.00107.73           C\\nANISOU 2200  C   LEU A1118    17547  10492  12892  -1976    724  -1011       C\\nATOM   2201  O   LEU A1118      23.041 -20.274  29.525  1.00110.02           O\\nANISOU 2201  O   LEU A1118    17736  11135  12931  -1982    613  -1185       O\\nATOM   2202  CB  LEU A1118      25.722 -20.757  31.279  1.00 92.05           C\\nANISOU 2202  CB  LEU A1118    15569   8366  11040  -1233   1041   -692       C\\nATOM   2203  CG  LEU A1118      26.695 -19.998  32.171  1.00 86.98           C\\nANISOU 2203  CG  LEU A1118    14695   7910  10443   -907   1144   -375       C\\nATOM   2204  CD1 LEU A1118      28.100 -20.549  32.003  1.00 86.56           C\\nANISOU 2204  CD1 LEU A1118    14792   7548  10551   -488   1291   -444       C\\nATOM   2205  CD2 LEU A1118      26.654 -18.516  31.846  1.00 86.67           C\\nANISOU 2205  CD2 LEU A1118    14359   8413  10159   -835   1133   -349       C\\nATOM   2206  N   ARG A1119      23.046 -22.333  30.429  1.00104.44           N\\nANISOU 2206  N   ARG A1119    17422   9590  12668  -2232    680  -1129       N\\nATOM   2207  CA  ARG A1119      22.191 -22.858  29.372  1.00103.70           C\\nANISOU 2207  CA  ARG A1119    17500   9406  12496  -2554    498  -1514       C\\nATOM   2208  C   ARG A1119      20.795 -22.250  29.433  1.00102.63           C\\nANISOU 2208  C   ARG A1119    16991   9707  12297  -2952    292  -1490       C\\nATOM   2209  O   ARG A1119      20.133 -22.113  28.398  1.00102.11           O\\nANISOU 2209  O   ARG A1119    16930   9811  12055  -3119     75  -1792       O\\nATOM   2210  CB  ARG A1119      22.123 -24.383  29.466  1.00105.66           C\\nANISOU 2210  CB  ARG A1119    18150   8971  13026  -2774    474  -1635       C\\nATOM   2211  CG  ARG A1119      21.461 -25.066  28.282  1.00110.68           C\\nANISOU 2211  CG  ARG A1119    19053   9414  13586  -3068    283  -2116       C\\nATOM   2212  CD  ARG A1119      21.400 -26.576  28.478  1.00119.37           C\\nANISOU 2212  CD  ARG A1119    20574   9750  15030  -3303    239  -2220       C\\nATOM   2213  NE  ARG A1119      20.881 -26.936  29.795  1.00121.59           N\\nANISOU 2213  NE  ARG A1119    20741   9865  15590  -3652    240  -1772       N\\nATOM   2214  CZ  ARG A1119      21.609 -27.484  30.763  1.00120.23           C\\nANISOU 2214  CZ  ARG A1119    20757   9256  15669  -3483    350  -1432       C\\nATOM   2215  NH1 ARG A1119      22.893 -27.748  30.561  1.00119.50           N\\nANISOU 2215  NH1 ARG A1119    20917   8831  15658  -2927    455  -1524       N\\nATOM   2216  NH2 ARG A1119      21.053 -27.772  31.933  1.00120.62           N\\nANISOU 2216  NH2 ARG A1119    20732   9219  15878  -3878    351  -1000       N\\nATOM   2217  N   MET A1120      20.338 -21.863  30.627  1.00100.48           N\\nANISOU 2217  N   MET A1120    16375   9649  12155  -3093    347  -1158       N\\nATOM   2218  CA  MET A1120      19.012 -21.263  30.756  1.00103.10           C\\nANISOU 2218  CA  MET A1120    16260  10430  12486  -3427    184  -1176       C\\nATOM   2219  C   MET A1120      19.000 -19.818  30.272  1.00100.31           C\\nANISOU 2219  C   MET A1120    15604  10594  11915  -3129     66  -1209       C\\nATOM   2220  O   MET A1120      18.009 -19.365  29.686  1.00100.24           O\\nANISOU 2220  O   MET A1120    15342  10888  11857  -3303   -198  -1388       O\\nATOM   2221  CB  MET A1120      18.535 -21.349  32.203  1.00106.18           C\\nANISOU 2221  CB  MET A1120    16380  10910  13054  -3686    341   -856       C\\nATOM   2222  CG  MET A1120      18.420 -22.776  32.714  1.00117.71           C\\nANISOU 2222  CG  MET A1120    18166  11832  14725  -4073    415   -750       C\\nATOM   2223  SD  MET A1120      17.789 -22.885  34.401  1.00123.98           S\\nANISOU 2223  SD  MET A1120    18683  12804  15620  -4485    629   -335       S\\nATOM   2224  CE  MET A1120      17.761 -24.663  34.625  1.00131.09           C\\nANISOU 2224  CE  MET A1120    20134  12916  16760  -4951    624   -214       C\\nATOM   2225  N   LEU A1121      20.082 -19.075  30.519  1.00100.35           N\\nANISOU 2225  N   LEU A1121    15626  10687  11815  -2692    222  -1026       N\\nATOM   2226  CA  LEU A1121      20.236 -17.769  29.884  1.00100.41           C\\nANISOU 2226  CA  LEU A1121    15473  11071  11608  -2415     91  -1049       C\\nATOM   2227  C   LEU A1121      20.299 -17.911  28.369  1.00105.95           C\\nANISOU 2227  C   LEU A1121    16480  11732  12045  -2411    -85  -1340       C\\nATOM   2228  O   LEU A1121      19.794 -17.057  27.629  1.00108.90           O\\nANISOU 2228  O   LEU A1121    16728  12416  12235  -2399   -355  -1411       O\\nATOM   2229  CB  LEU A1121      21.498 -17.077  30.396  1.00 89.96           C\\nANISOU 2229  CB  LEU A1121    14156   9787  10238  -2005    306   -807       C\\nATOM   2230  CG  LEU A1121      21.578 -16.711  31.874  1.00 82.79           C\\nANISOU 2230  CG  LEU A1121    12972   8988   9494  -1956    454   -522       C\\nATOM   2231  CD1 LEU A1121      22.975 -16.220  32.204  1.00 72.92           C\\nANISOU 2231  CD1 LEU A1121    11799   7708   8200  -1566    625   -331       C\\nATOM   2232  CD2 LEU A1121      20.549 -15.649  32.207  1.00 85.66           C\\nANISOU 2232  CD2 LEU A1121    12882   9776   9890  -2027    296   -524       C\\nATOM   2233  N   GLN A1122      20.920 -18.991  27.892  1.00 98.13           N\\nANISOU 2233  N   GLN A1122    15913  10351  11023  -2411     46  -1520       N\\nATOM   2234  CA  GLN A1122      21.020 -19.232  26.459  1.00 98.26           C\\nANISOU 2234  CA  GLN A1122    16271  10336  10727  -2427    -75  -1857       C\\nATOM   2235  C   GLN A1122      19.667 -19.584  25.852  1.00 96.39           C\\nANISOU 2235  C   GLN A1122    15998  10161  10466  -2846   -440  -2111       C\\nATOM   2236  O   GLN A1122      19.425 -19.301  24.674  1.00 98.68           O\\nANISOU 2236  O   GLN A1122    16445  10634  10417  -2889   -682  -2330       O\\nATOM   2237  CB  GLN A1122      22.036 -20.346  26.201  1.00103.05           C\\nANISOU 2237  CB  GLN A1122    17309  10483  11362  -2283    189  -2053       C\\nATOM   2238  CG  GLN A1122      22.347 -20.616  24.747  1.00107.55           C\\nANISOU 2238  CG  GLN A1122    18269  11042  11552  -2252    165  -2458       C\\nATOM   2239  CD  GLN A1122      23.447 -21.645  24.581  1.00111.75           C\\nANISOU 2239  CD  GLN A1122    19160  11128  12172  -2017    475  -2696       C\\nATOM   2240  OE1 GLN A1122      24.039 -22.100  25.559  1.00115.12           O\\nANISOU 2240  OE1 GLN A1122    19540  11237  12962  -1840    666  -2506       O\\nATOM   2241  NE2 GLN A1122      23.726 -22.017  23.338  1.00113.25           N\\nANISOU 2241  NE2 GLN A1122    19714  11294  12023  -1998    511  -3131       N\\nATOM   2242  N   GLN A1123      18.773 -20.184  26.639  1.00102.08           N\\nANISOU 2242  N   GLN A1123    16506  10761  11521  -3189   -495  -2073       N\\nATOM   2243  CA  GLN A1123      17.459 -20.603  26.168  1.00103.74           C\\nANISOU 2243  CA  GLN A1123    16604  11025  11786  -3643   -839  -2321       C\\nATOM   2244  C   GLN A1123      16.362 -19.590  26.496  1.00108.72           C\\nANISOU 2244  C   GLN A1123    16638  12153  12517  -3742  -1093  -2203       C\\nATOM   2245  O   GLN A1123      15.179 -19.947  26.486  1.00110.87           O\\nANISOU 2245  O   GLN A1123    16643  12510  12973  -4152  -1332  -2352       O\\nATOM   2246  CB  GLN A1123      17.101 -21.971  26.754  1.00101.84           C\\nANISOU 2246  CB  GLN A1123    16492  10326  11878  -4039   -744  -2378       C\\nATOM   2247  CG  GLN A1123      17.964 -23.119  26.251  1.00 99.00           C\\nANISOU 2247  CG  GLN A1123    16739   9389  11487  -3971   -604  -2613       C\\nATOM   2248  CD  GLN A1123      17.609 -24.442  26.905  1.00109.60           C\\nANISOU 2248  CD  GLN A1123    18244  10191  13208  -4372   -553  -2607       C\\nATOM   2249  OE1 GLN A1123      17.694 -24.589  28.124  1.00109.83           O\\nANISOU 2249  OE1 GLN A1123    18131  10108  13491  -4423   -352  -2243       O\\nATOM   2250  NE2 GLN A1123      17.200 -25.410  26.095  1.00111.61           N\\nANISOU 2250  NE2 GLN A1123    18833  10095  13478  -4692   -754  -3005       N\\nATOM   2251  N   LYS A1124      16.728 -18.344  26.794  1.00101.10           N\\nANISOU 2251  N   LYS A1124    15436  11503  11475  -3376  -1053  -1965       N\\nATOM   2252  CA  LYS A1124      15.801 -17.264  27.128  1.00102.00           C\\nANISOU 2252  CA  LYS A1124    14979  12055  11722  -3354  -1290  -1880       C\\nATOM   2253  C   LYS A1124      14.956 -17.560  28.362  1.00106.14           C\\nANISOU 2253  C   LYS A1124    15026  12671  12629  -3642  -1145  -1813       C\\nATOM   2254  O   LYS A1124      13.969 -16.858  28.613  1.00108.27           O\\nANISOU 2254  O   LYS A1124    14746  13316  13075  -3688  -1344  -1851       O\\nATOM   2255  CB  LYS A1124      14.875 -16.927  25.950  1.00104.85           C\\nANISOU 2255  CB  LYS A1124    15253  12649  11937  -3482  -1823  -2115       C\\nATOM   2256  CG  LYS A1124      15.585 -16.569  24.655  1.00106.34           C\\nANISOU 2256  CG  LYS A1124    15931  12827  11648  -3267  -1994  -2170       C\\nATOM   2257  CD  LYS A1124      16.318 -15.246  24.762  1.00102.53           C\\nANISOU 2257  CD  LYS A1124    15411  12521  11026  -2834  -1939  -1876       C\\nATOM   2258  CE  LYS A1124      16.710 -14.725  23.392  1.00104.63           C\\nANISOU 2258  CE  LYS A1124    16088  12882  10786  -2721  -2205  -1897       C\\nATOM   2259  NZ  LYS A1124      15.510 -14.429  22.560  1.00109.17           N\\nANISOU 2259  NZ  LYS A1124    16517  13684  11279  -2897  -2828  -2043       N\\nATOM   2260  N   ARG A1125      15.311 -18.583  29.142  1.00109.81           N\\nANISOU 2260  N   ARG A1125    15685  12809  13228  -3839   -806  -1713       N\\nATOM   2261  CA  ARG A1125      14.563 -18.937  30.349  1.00105.46           C\\nANISOU 2261  CA  ARG A1125    14749  12354  12966  -4188   -611  -1603       C\\nATOM   2262  C   ARG A1125      15.011 -18.038  31.502  1.00105.15           C\\nANISOU 2262  C   ARG A1125    14454  12555  12943  -3878   -338  -1327       C\\nATOM   2263  O   ARG A1125      15.645 -18.469  32.467  1.00102.11           O\\nANISOU 2263  O   ARG A1125    14245  11977  12576  -3884    -12  -1083       O\\nATOM   2264  CB  ARG A1125      14.757 -20.408  30.687  1.00100.56           C\\nANISOU 2264  CB  ARG A1125    14519  11232  12456  -4562   -413  -1558       C\\nATOM   2265  CG  ARG A1125      14.118 -21.370  29.702  1.00104.76           C\\nANISOU 2265  CG  ARG A1125    15255  11516  13034  -4972   -689  -1879       C\\nATOM   2266  CD  ARG A1125      14.117 -22.790  30.251  1.00109.68           C\\nANISOU 2266  CD  ARG A1125    16197  11614  13861  -5418   -505  -1800       C\\nATOM   2267  NE  ARG A1125      15.435 -23.419  30.187  1.00111.71           N\\nANISOU 2267  NE  ARG A1125    17086  11317  14042  -5114   -333  -1714       N\\nATOM   2268  CZ  ARG A1125      15.756 -24.551  30.807  1.00114.79           C\\nANISOU 2268  CZ  ARG A1125    17840  11156  14619  -5338   -166  -1549       C\\nATOM   2269  NH1 ARG A1125      14.859 -25.182  31.553  1.00117.33           N\\nANISOU 2269  NH1 ARG A1125    17995  11419  15168  -5934   -115  -1411       N\\nATOM   2270  NH2 ARG A1125      16.978 -25.051  30.689  1.00114.27           N\\nANISOU 2270  NH2 ARG A1125    18294  10594  14529  -4971    -54  -1512       N\\nATOM   2271  N   TRP A1126      14.657 -16.753  31.387  1.00102.43           N\\nANISOU 2271  N   TRP A1126    13702  12620  12595  -3599   -520  -1377       N\\nATOM   2272  CA  TRP A1126      15.103 -15.775  32.375  1.00 99.11           C\\nANISOU 2272  CA  TRP A1126    13061  12418  12179  -3267   -310  -1183       C\\nATOM   2273  C   TRP A1126      14.567 -16.088  33.763  1.00100.00           C\\nANISOU 2273  C   TRP A1126    12842  12708  12447  -3564     17  -1092       C\\nATOM   2274  O   TRP A1126      15.235 -15.807  34.763  1.00 95.88           O\\nANISOU 2274  O   TRP A1126    12367  12211  11852  -3395    296   -877       O\\nATOM   2275  CB  TRP A1126      14.683 -14.363  31.959  1.00 98.18           C\\nANISOU 2275  CB  TRP A1126    12566  12644  12092  -2934   -622  -1293       C\\nATOM   2276  CG  TRP A1126      15.001 -14.027  30.537  1.00 99.97           C\\nANISOU 2276  CG  TRP A1126    13108  12760  12116  -2737   -990  -1360       C\\nATOM   2277  CD1 TRP A1126      14.127 -13.586  29.588  1.00102.49           C\\nANISOU 2277  CD1 TRP A1126    13224  13259  12460  -2750  -1458  -1549       C\\nATOM   2278  CD2 TRP A1126      16.280 -14.113  29.895  1.00100.88           C\\nANISOU 2278  CD2 TRP A1126    13796  12592  11940  -2519   -920  -1236       C\\nATOM   2279  NE1 TRP A1126      14.782 -13.387  28.397  1.00102.69           N\\nANISOU 2279  NE1 TRP A1126    13720  13132  12164  -2582  -1684  -1520       N\\nATOM   2280  CE2 TRP A1126      16.105 -13.705  28.559  1.00102.48           C\\nANISOU 2280  CE2 TRP A1126    14155  12841  11942  -2447  -1322  -1348       C\\nATOM   2281  CE3 TRP A1126      17.558 -14.494  30.321  1.00101.84           C\\nANISOU 2281  CE3 TRP A1126    14288  12451  11954  -2377   -563  -1048       C\\nATOM   2282  CZ2 TRP A1126      17.157 -13.666  27.646  1.00107.44           C\\nANISOU 2282  CZ2 TRP A1126    15302  13297  12222  -2277  -1308  -1288       C\\nATOM   2283  CZ3 TRP A1126      18.601 -14.457  29.411  1.00101.67           C\\nANISOU 2283  CZ3 TRP A1126    14713  12253  11664  -2171   -560  -1020       C\\nATOM   2284  CH2 TRP A1126      18.393 -14.051  28.088  1.00104.96           C\\nANISOU 2284  CH2 TRP A1126    15284  12756  11842  -2142   -895  -1146       C\\nATOM   2285  N   ASP A1127      13.370 -16.667  33.848  1.00105.05           N\\nANISOU 2285  N   ASP A1127    13142  13500  13273  -4040    -10  -1251       N\\nATOM   2286  CA  ASP A1127      12.801 -16.985  35.152  1.00105.65           C\\nANISOU 2286  CA  ASP A1127    12891  13805  13446  -4403    350  -1159       C\\nATOM   2287  C   ASP A1127      13.638 -18.034  35.873  1.00102.58           C\\nANISOU 2287  C   ASP A1127    13044  13002  12929  -4604    661   -828       C\\nATOM   2288  O   ASP A1127      14.085 -17.819  37.005  1.00 97.10           O\\nANISOU 2288  O   ASP A1127    12362  12413  12117  -4531    958   -598       O\\nATOM   2289  CB  ASP A1127      11.355 -17.458  34.988  1.00113.14           C\\nANISOU 2289  CB  ASP A1127    13346  15002  14642  -4937    260  -1403       C\\nATOM   2290  N   GLU A1128      13.877 -19.175  35.221  1.00105.05           N\\nANISOU 2290  N   GLU A1128    13834  12818  13263  -4840    560   -812       N\\nATOM   2291  CA  GLU A1128      14.589 -20.266  35.881  1.00101.37           C\\nANISOU 2291  CA  GLU A1128    13890  11878  12749  -5036    788   -497       C\\nATOM   2292  C   GLU A1128      16.064 -19.940  36.072  1.00 98.59           C\\nANISOU 2292  C   GLU A1128    13939  11292  12227  -4482    856   -278       C\\nATOM   2293  O   GLU A1128      16.652 -20.294  37.101  1.00 98.75           O\\nANISOU 2293  O   GLU A1128    14183  11164  12175  -4507   1075     48       O\\nATOM   2294  CB  GLU A1128      14.433 -21.557  35.083  1.00102.72           C\\nANISOU 2294  CB  GLU A1128    14465  11516  13047  -5400    625   -601       C\\nATOM   2295  CG  GLU A1128      13.004 -22.014  34.909  1.00109.16           C\\nANISOU 2295  CG  GLU A1128    14894  12518  14063  -6031    538   -807       C\\nATOM   2296  CD  GLU A1128      12.920 -23.465  34.496  1.00117.05           C\\nANISOU 2296  CD  GLU A1128    16374  12895  15205  -6501    444   -827       C\\nATOM   2297  OE1 GLU A1128      13.445 -24.324  35.236  1.00119.18           O\\nANISOU 2297  OE1 GLU A1128    17078  12716  15487  -6681    639   -499       O\\nATOM   2298  OE2 GLU A1128      12.343 -23.744  33.426  1.00122.20           O\\nANISOU 2298  OE2 GLU A1128    16997  13477  15956  -6685    137  -1171       O\\nATOM   2299  N   ALA A1129      16.686 -19.280  35.090  1.00106.39           N\\nANISOU 2299  N   ALA A1129    15026  12259  13140  -4007    658   -438       N\\nATOM   2300  CA  ALA A1129      18.089 -18.904  35.232  1.00 98.44           C\\nANISOU 2300  CA  ALA A1129    14315  11087  12002  -3503    734   -256       C\\nATOM   2301  C   ALA A1129      18.313 -18.065  36.481  1.00 99.96           C\\nANISOU 2301  C   ALA A1129    14247  11624  12110  -3345    925    -40       C\\nATOM   2302  O   ALA A1129      19.394 -18.111  37.080  1.00 91.71           O\\nANISOU 2302  O   ALA A1129    13458  10403  10986  -3100   1037    208       O\\nATOM   2303  CB  ALA A1129      18.562 -18.146  33.991  1.00 90.27           C\\nANISOU 2303  CB  ALA A1129    13335  10100  10864  -3097    524   -462       C\\nATOM   2304  N   ALA A1130      17.300 -17.301  36.894  1.00101.90           N\\nANISOU 2304  N   ALA A1130    13969  12366  12382  -3472    950   -165       N\\nATOM   2305  CA  ALA A1130      17.396 -16.557  38.143  1.00100.47           C\\nANISOU 2305  CA  ALA A1130    13541  12535  12097  -3370   1159    -30       C\\nATOM   2306  C   ALA A1130      17.236 -17.478  39.344  1.00 96.24           C\\nANISOU 2306  C   ALA A1130    13135  11951  11481  -3804   1437    243       C\\nATOM   2307  O   ALA A1130      17.958 -17.340  40.339  1.00 91.99           O\\nANISOU 2307  O   ALA A1130    12752  11434  10767  -3682   1586    498       O\\nATOM   2308  CB  ALA A1130      16.348 -15.446  38.172  1.00102.74           C\\nANISOU 2308  CB  ALA A1130    13205  13359  12471  -3324   1106   -319       C\\nATOM   2309  N   VAL A1131      16.303 -18.428  39.267  1.00 92.07           N\\nANISOU 2309  N   VAL A1131    12568  11350  11062  -4347   1484    213       N\\nATOM   2310  CA  VAL A1131      16.030 -19.294  40.409  1.00 92.71           C\\nANISOU 2310  CA  VAL A1131    12779  11404  11044  -4858   1755    513       C\\nATOM   2311  C   VAL A1131      17.210 -20.220  40.681  1.00 93.11           C\\nANISOU 2311  C   VAL A1131    13506  10845  11028  -4781   1726    899       C\\nATOM   2312  O   VAL A1131      17.533 -20.509  41.839  1.00 94.49           O\\nANISOU 2312  O   VAL A1131    13879  11018  11005  -4935   1900   1255       O\\nATOM   2313  CB  VAL A1131      14.728 -20.083  40.179  1.00 91.93           C\\nANISOU 2313  CB  VAL A1131    12455  11353  11120  -5514   1797    386       C\\nATOM   2314  N   ASN A1132      17.877 -20.696  39.626  1.00 98.73           N\\nANISOU 2314  N   ASN A1132    14580  11039  11893  -4528   1494    823       N\\nATOM   2315  CA  ASN A1132      19.028 -21.572  39.827  1.00 99.57           C\\nANISOU 2315  CA  ASN A1132    15279  10537  12016  -4371   1439   1132       C\\nATOM   2316  C   ASN A1132      20.208 -20.804  40.407  1.00 98.88           C\\nANISOU 2316  C   ASN A1132    15239  10564  11768  -3840   1452   1311       C\\nATOM   2317  O   ASN A1132      20.866 -21.282  41.338  1.00106.13           O\\nANISOU 2317  O   ASN A1132    16469  11262  12593  -3844   1482   1689       O\\nATOM   2318  CB  ASN A1132      19.417 -22.244  38.508  1.00100.70           C\\nANISOU 2318  CB  ASN A1132    15748  10141  12372  -4206   1226    906       C\\nATOM   2319  CG  ASN A1132      20.355 -23.432  38.702  1.00102.63           C\\nANISOU 2319  CG  ASN A1132    16592   9660  12743  -4136   1159   1173       C\\nATOM   2320  OD1 ASN A1132      21.259 -23.402  39.538  1.00 99.29           O\\nANISOU 2320  OD1 ASN A1132    16345   9141  12242  -3883   1185   1501       O\\nATOM   2321  ND2 ASN A1132      20.136 -24.489  37.929  1.00107.31           N\\nANISOU 2321  ND2 ASN A1132    17502   9719  13554  -4348   1034   1014       N\\nATOM   2322  N   LEU A1133      20.483 -19.606  39.881  1.00 85.10           N\\nANISOU 2322  N   LEU A1133    13195   9149   9988  -3405   1394   1062       N\\nATOM   2323  CA  LEU A1133      21.652 -18.849  40.317  1.00 79.83           C\\nANISOU 2323  CA  LEU A1133    12558   8566   9209  -2920   1377   1196       C\\nATOM   2324  C   LEU A1133      21.591 -18.470  41.792  1.00 85.06           C\\nANISOU 2324  C   LEU A1133    13112   9576   9629  -3048   1529   1445       C\\nATOM   2325  O   LEU A1133      22.638 -18.221  42.399  1.00 82.43           O\\nANISOU 2325  O   LEU A1133    12927   9198   9193  -2748   1484   1656       O\\nATOM   2326  CB  LEU A1133      21.813 -17.596  39.454  1.00 84.72           C\\nANISOU 2326  CB  LEU A1133    12879   9469   9842  -2527   1283    893       C\\nATOM   2327  CG  LEU A1133      22.459 -17.798  38.079  1.00 88.21           C\\nANISOU 2327  CG  LEU A1133    13529   9583  10405  -2245   1143    716       C\\nATOM   2328  CD1 LEU A1133      22.334 -16.537  37.242  1.00 90.94           C\\nANISOU 2328  CD1 LEU A1133    13587  10258  10710  -1997   1039    463       C\\nATOM   2329  CD2 LEU A1133      23.920 -18.203  38.219  1.00 83.43           C\\nANISOU 2329  CD2 LEU A1133    13242   8615   9844  -1895   1135    911       C\\nATOM   2330  N   ALA A1134      20.399 -18.433  42.386  1.00 84.49           N\\nANISOU 2330  N   ALA A1134    12774   9880   9449  -3501   1713   1404       N\\nATOM   2331  CA  ALA A1134      20.263 -18.129  43.804  1.00 83.30           C\\nANISOU 2331  CA  ALA A1134    12544  10115   8992  -3684   1912   1604       C\\nATOM   2332  C   ALA A1134      20.570 -19.322  44.697  1.00 95.28           C\\nANISOU 2332  C   ALA A1134    14547  11297  10359  -4027   1952   2087       C\\nATOM   2333  O   ALA A1134      20.536 -19.181  45.925  1.00100.46           O\\nANISOU 2333  O   ALA A1134    15234  12260  10675  -4222   2106   2315       O\\nATOM   2334  CB  ALA A1134      18.855 -17.614  44.103  1.00 88.70           C\\nANISOU 2334  CB  ALA A1134    12701  11389   9612  -4038   2147   1331       C\\nATOM   2335  N   LYS A1135      20.860 -20.486  44.116  1.00 88.10           N\\nANISOU 2335  N   LYS A1135    14044   9751   9678  -4109   1800   2243       N\\nATOM   2336  CA  LYS A1135      21.205 -21.680  44.871  1.00 87.20           C\\nANISOU 2336  CA  LYS A1135    14461   9179   9491  -4398   1755   2737       C\\nATOM   2337  C   LYS A1135      22.701 -21.967  44.852  1.00 86.32           C\\nANISOU 2337  C   LYS A1135    14744   8566   9488  -3866   1479   2966       C\\nATOM   2338  O   LYS A1135      23.109 -23.103  45.109  1.00102.38           O\\nANISOU 2338  O   LYS A1135    17270  10011  11619  -3979   1327   3328       O\\nATOM   2339  CB  LYS A1135      20.432 -22.884  44.332  1.00 91.82           C\\nANISOU 2339  CB  LYS A1135    15253   9320  10313  -4902   1752   2756       C\\nATOM   2340  N   SER A1136      23.523 -20.968  44.553  1.00 82.36           N\\nANISOU 2340  N   SER A1136    14022   8267   9005  -3296   1395   2765       N\\nATOM   2341  CA  SER A1136      24.959 -21.160  44.431  1.00 83.52           C\\nANISOU 2341  CA  SER A1136    14419   8004   9312  -2765   1149   2911       C\\nATOM   2342  C   SER A1136      25.684 -20.619  45.656  1.00 88.67           C\\nANISOU 2342  C   SER A1136    15092   8930   9667  -2607   1075   3205       C\\nATOM   2343  O   SER A1136      25.148 -19.816  46.424  1.00 92.03           O\\nANISOU 2343  O   SER A1136    15281   9935   9752  -2806   1240   3175       O\\nATOM   2344  CB  SER A1136      25.494 -20.477  43.171  1.00 79.24           C\\nANISOU 2344  CB  SER A1136    13626   7476   9007  -2270   1101   2495       C\\nATOM   2345  OG  SER A1136      25.423 -19.068  43.285  1.00 73.97           O\\nANISOU 2345  OG  SER A1136    12540   7401   8165  -2108   1183   2288       O\\nATOM   2346  N   ARG A1137      26.926 -21.078  45.832  1.00 91.39           N\\nANISOU 2346  N   ARG A1137    15712   8855  10158  -2229    806   3459       N\\nATOM   2347  CA  ARG A1137      27.767 -20.540  46.894  1.00 91.41           C\\nANISOU 2347  CA  ARG A1137    15721   9100   9909  -2019    652   3712       C\\nATOM   2348  C   ARG A1137      28.177 -19.101  46.613  1.00 85.85           C\\nANISOU 2348  C   ARG A1137    14558   8882   9179  -1656    695   3357       C\\nATOM   2349  O   ARG A1137      28.655 -18.413  47.521  1.00 85.58           O\\nANISOU 2349  O   ARG A1137    14453   9182   8883  -1561    604   3470       O\\nATOM   2350  CB  ARG A1137      29.009 -21.414  47.089  1.00 94.63           C\\nANISOU 2350  CB  ARG A1137    16484   8915  10557  -1666    293   4057       C\\nATOM   2351  N   TRP A1138      28.013 -18.639  45.372  1.00 85.61           N\\nANISOU 2351  N   TRP A1138    14253   8876   9400  -1476    803   2943       N\\nATOM   2352  CA  TRP A1138      28.240 -17.235  45.053  1.00 83.05           C\\nANISOU 2352  CA  TRP A1138    13523   8984   9049  -1214    846   2628       C\\nATOM   2353  C   TRP A1138      27.118 -16.360  45.596  1.00 83.65           C\\nANISOU 2353  C   TRP A1138    13343   9618   8821  -1522   1044   2460       C\\nATOM   2354  O   TRP A1138      27.378 -15.303  46.181  1.00 74.31           O\\nANISOU 2354  O   TRP A1138    11960   8813   7461  -1395   1022   2377       O\\nATOM   2355  CB  TRP A1138      28.387 -17.069  43.541  1.00 81.72           C\\nANISOU 2355  CB  TRP A1138    13205   8653   9191   -970    885   2291       C\\nATOM   2356  CG  TRP A1138      28.200 -15.675  43.038  1.00 80.37           C\\nANISOU 2356  CG  TRP A1138    12659   8893   8984   -845    952   1971       C\\nATOM   2357  CD1 TRP A1138      29.008 -14.601  43.270  1.00 79.75           C\\nANISOU 2357  CD1 TRP A1138    12375   9046   8880   -571    866   1931       C\\nATOM   2358  CD2 TRP A1138      27.151 -15.209  42.179  1.00 79.40           C\\nANISOU 2358  CD2 TRP A1138    12339   8950   8882   -990   1065   1659       C\\nATOM   2359  NE1 TRP A1138      28.520 -13.492  42.620  1.00 74.10           N\\nANISOU 2359  NE1 TRP A1138    11385   8600   8171   -543    925   1634       N\\nATOM   2360  CE2 TRP A1138      27.381 -13.840  41.944  1.00 77.74           C\\nANISOU 2360  CE2 TRP A1138    11841   9040   8657   -775   1031   1470       C\\nATOM   2361  CE3 TRP A1138      26.036 -15.814  41.592  1.00 70.14           C\\nANISOU 2361  CE3 TRP A1138    11201   7697   7754  -1292   1152   1527       C\\nATOM   2362  CZ2 TRP A1138      26.539 -13.069  41.149  1.00 75.61           C\\nANISOU 2362  CZ2 TRP A1138    11345   8968   8416   -815   1054   1185       C\\nATOM   2363  CZ3 TRP A1138      25.201 -15.044  40.801  1.00 72.99           C\\nANISOU 2363  CZ3 TRP A1138    11290   8307   8136  -1332   1174   1217       C\\nATOM   2364  CH2 TRP A1138      25.457 -13.689  40.588  1.00 72.54           C\\nANISOU 2364  CH2 TRP A1138    10974   8524   8064  -1078   1113   1063       C\\nATOM   2365  N   TYR A1139      25.867 -16.790  45.424  1.00 82.65           N\\nANISOU 2365  N   TYR A1139    13198   9549   8658  -1927   1233   2375       N\\nATOM   2366  CA  TYR A1139      24.743 -16.053  45.987  1.00 86.12           C\\nANISOU 2366  CA  TYR A1139    13337  10541   8845  -2219   1452   2182       C\\nATOM   2367  C   TYR A1139      24.771 -16.040  47.509  1.00 83.42           C\\nANISOU 2367  C   TYR A1139    13129  10492   8073  -2444   1516   2445       C\\nATOM   2368  O   TYR A1139      24.214 -15.122  48.120  1.00 85.20           O\\nANISOU 2368  O   TYR A1139    13075  11244   8055  -2528   1680   2223       O\\nATOM   2369  CB  TYR A1139      23.424 -16.647  45.483  1.00 93.06           C\\nANISOU 2369  CB  TYR A1139    14126  11418   9815  -2639   1632   2048       C\\nATOM   2370  CG  TYR A1139      22.187 -15.947  45.998  1.00 97.27           C\\nANISOU 2370  CG  TYR A1139    14256  12545  10156  -2931   1887   1793       C\\nATOM   2371  CD1 TYR A1139      21.714 -14.791  45.393  1.00 97.09           C\\nANISOU 2371  CD1 TYR A1139    13784  12829  10275  -2703   1891   1360       C\\nATOM   2372  CD2 TYR A1139      21.487 -16.449  47.086  1.00101.31           C\\nANISOU 2372  CD2 TYR A1139    14831  13310  10352  -3435   2125   1984       C\\nATOM   2373  CE1 TYR A1139      20.582 -14.152  45.862  1.00 98.45           C\\nANISOU 2373  CE1 TYR A1139    13534  13534  10340  -2906   2113   1072       C\\nATOM   2374  CE2 TYR A1139      20.357 -15.817  47.560  1.00102.23           C\\nANISOU 2374  CE2 TYR A1139    14515  14020  10307  -3689   2412   1691       C\\nATOM   2375  CZ  TYR A1139      19.909 -14.671  46.946  1.00 98.03           C\\nANISOU 2375  CZ  TYR A1139    13492  13774   9981  -3392   2400   1210       C\\nATOM   2376  OH  TYR A1139      18.781 -14.044  47.424  1.00 96.25           O\\nANISOU 2376  OH  TYR A1139    12784  14130   9656  -3586   2677    868       O\\nATOM   2377  N   ASN A1140      25.410 -17.028  48.134  1.00 84.98           N\\nANISOU 2377  N   ASN A1140    13766  10358   8165  -2531   1372   2902       N\\nATOM   2378  CA  ASN A1140      25.511 -17.069  49.585  1.00 81.09           C\\nANISOU 2378  CA  ASN A1140    13485  10139   7189  -2767   1384   3212       C\\nATOM   2379  C   ASN A1140      26.720 -16.316  50.123  1.00 81.14           C\\nANISOU 2379  C   ASN A1140    13495  10255   7081  -2354   1121   3259       C\\nATOM   2380  O   ASN A1140      26.732 -15.963  51.308  1.00 91.34           O\\nANISOU 2380  O   ASN A1140    14868  11933   7905  -2514   1139   3371       O\\nATOM   2381  CB  ASN A1140      25.564 -18.521  50.073  1.00 83.93           C\\nANISOU 2381  CB  ASN A1140    14351  10066   7474  -3090   1289   3738       C\\nATOM   2382  CG  ASN A1140      24.263 -19.268  49.834  1.00 88.69           C\\nANISOU 2382  CG  ASN A1140    14898  10646   8154  -3583   1553   3682       C\\nATOM   2383  OD1 ASN A1140      23.328 -19.182  50.631  1.00 94.13           O\\nANISOU 2383  OD1 ASN A1140    15427  11795   8542  -3964   1814   3633       O\\nATOM   2384  ND2 ASN A1140      24.203 -20.015  48.739  1.00 88.26           N\\nANISOU 2384  ND2 ASN A1140    14971  10056   8508  -3583   1485   3663       N\\nATOM   2385  N   GLN A1141      27.731 -16.058  49.292  1.00 79.05           N\\nANISOU 2385  N   GLN A1141    13135   9692   7209  -1861    889   3159       N\\nATOM   2386  CA  GLN A1141      28.944 -15.389  49.751  1.00 83.34           C\\nANISOU 2386  CA  GLN A1141    13640  10316   7710  -1493    612   3207       C\\nATOM   2387  C   GLN A1141      28.857 -13.872  49.622  1.00 86.83           C\\nANISOU 2387  C   GLN A1141    13669  11193   8130  -1321    691   2761       C\\nATOM   2388  O   GLN A1141      29.270 -13.148  50.534  1.00 90.33           O\\nANISOU 2388  O   GLN A1141    14085  11948   8290  -1274    578   2742       O\\nATOM   2389  CB  GLN A1141      30.158 -15.908  48.974  1.00 81.76           C\\nANISOU 2389  CB  GLN A1141    13505   9595   7966  -1066    339   3330       C\\nATOM   2390  N   THR A1142      28.341 -13.378  48.497  1.00 81.15           N\\nANISOU 2390  N   THR A1142    12660  10468   7708  -1228    841   2404       N\\nATOM   2391  CA  THR A1142      28.099 -11.952  48.276  1.00 75.62           C\\nANISOU 2391  CA  THR A1142    11594  10099   7040  -1081    896   1987       C\\nATOM   2392  C   THR A1142      26.654 -11.815  47.825  1.00 80.15           C\\nANISOU 2392  C   THR A1142    11953  10861   7638  -1313   1170   1698       C\\nATOM   2393  O   THR A1142      26.373 -11.645  46.629  1.00 76.21           O\\nANISOU 2393  O   THR A1142    11292  10208   7456  -1195   1180   1504       O\\nATOM   2394  CB  THR A1142      29.064 -11.368  47.245  1.00 71.01           C\\nANISOU 2394  CB  THR A1142    10854   9291   6836   -689    721   1873       C\\nATOM   2395  OG1 THR A1142      28.852 -12.004  45.979  1.00 61.90           O\\nANISOU 2395  OG1 THR A1142     9720   7819   5981   -656    792   1847       O\\nATOM   2396  CG2 THR A1142      30.507 -11.581  47.678  1.00 64.20           C\\nANISOU 2396  CG2 THR A1142    10120   8261   6011   -463    447   2144       C\\nATOM   2397  N   PRO A1143      25.702 -11.890  48.760  1.00 78.66           N\\nANISOU 2397  N   PRO A1143    11743  11039   7106  -1659   1396   1658       N\\nATOM   2398  CA  PRO A1143      24.288 -11.947  48.355  1.00 77.44           C\\nANISOU 2398  CA  PRO A1143    11332  11073   7019  -1917   1663   1400       C\\nATOM   2399  C   PRO A1143      23.754 -10.645  47.786  1.00 81.38           C\\nANISOU 2399  C   PRO A1143    11396  11793   7731  -1681   1672    913       C\\nATOM   2400  O   PRO A1143      22.964 -10.679  46.836  1.00 67.23           O\\nANISOU 2400  O   PRO A1143     9390   9947   6208  -1709   1715    723       O\\nATOM   2401  CB  PRO A1143      23.575 -12.337  49.655  1.00 74.02           C\\nANISOU 2401  CB  PRO A1143    10976  11033   6115  -2363   1931   1502       C\\nATOM   2402  CG  PRO A1143      24.484 -11.856  50.733  1.00 74.95           C\\nANISOU 2402  CG  PRO A1143    11275  11318   5883  -2235   1792   1614       C\\nATOM   2403  CD  PRO A1143      25.873 -12.037  50.213  1.00 80.85           C\\nANISOU 2403  CD  PRO A1143    12236  11590   6893  -1870   1423   1866       C\\nATOM   2404  N   ASN A1144      24.148  -9.498  48.346  1.00 79.84           N\\nANISOU 2404  N   ASN A1144    11080  11820   7435  -1453   1593    702       N\\nATOM   2405  CA  ASN A1144      23.656  -8.219  47.839  1.00 82.18           C\\nANISOU 2405  CA  ASN A1144    11000  12248   7977  -1203   1550    249       C\\nATOM   2406  C   ASN A1144      24.024  -8.031  46.372  1.00 83.32           C\\nANISOU 2406  C   ASN A1144    11122  12002   8536   -947   1323    262       C\\nATOM   2407  O   ASN A1144      23.168  -7.712  45.538  1.00 77.89           O\\nANISOU 2407  O   ASN A1144    10184  11322   8089   -907   1317     25       O\\nATOM   2408  CB  ASN A1144      24.209  -7.072  48.683  1.00 86.17           C\\nANISOU 2408  CB  ASN A1144    11466  12947   8328   -999   1448     44       C\\nATOM   2409  CG  ASN A1144      23.399  -6.831  49.942  1.00 91.58           C\\nANISOU 2409  CG  ASN A1144    12020  14149   8626  -1210   1730   -220       C\\nATOM   2410  OD1 ASN A1144      22.445  -6.054  49.938  1.00 89.43           O\\nANISOU 2410  OD1 ASN A1144    11378  14135   8467  -1137   1861   -680       O\\nATOM   2411  ND2 ASN A1144      23.778  -7.496  51.028  1.00 95.06           N\\nANISOU 2411  ND2 ASN A1144    12763  14756   8600  -1466   1818     62       N\\nATOM   2412  N   ARG A1145      25.302  -8.228  46.040  1.00 83.54           N\\nANISOU 2412  N   ARG A1145    11397  11711   8633   -780   1132    536       N\\nATOM   2413  CA  ARG A1145      25.740  -8.103  44.655  1.00 77.75           C\\nANISOU 2413  CA  ARG A1145    10673  10652   8215   -579    973    561       C\\nATOM   2414  C   ARG A1145      25.101  -9.167  43.774  1.00 76.82           C\\nANISOU 2414  C   ARG A1145    10624  10365   8200   -753   1062    630       C\\nATOM   2415  O   ARG A1145      24.721  -8.887  42.631  1.00 82.58           O\\nANISOU 2415  O   ARG A1145    11252  10993   9130   -675    981    488       O\\nATOM   2416  CB  ARG A1145      27.264  -8.189  44.587  1.00 73.67           C\\nANISOU 2416  CB  ARG A1145    10353   9896   7744   -393    814    816       C\\nATOM   2417  CG  ARG A1145      27.829  -8.227  43.179  1.00 69.75           C\\nANISOU 2417  CG  ARG A1145     9893   9104   7505   -234    729    865       C\\nATOM   2418  CD  ARG A1145      29.352  -8.232  43.189  1.00 73.59           C\\nANISOU 2418  CD  ARG A1145    10468   9428   8064    -50    612   1067       C\\nATOM   2419  NE  ARG A1145      29.897  -8.135  41.837  1.00 80.75           N\\nANISOU 2419  NE  ARG A1145    11375  10131   9175     79    594   1070       N\\nATOM   2420  CZ  ARG A1145      31.175  -7.901  41.556  1.00 82.83           C\\nANISOU 2420  CZ  ARG A1145    11612  10298   9561    237    528   1175       C\\nATOM   2421  NH1 ARG A1145      32.054  -7.734  42.535  1.00 82.57           N\\nANISOU 2421  NH1 ARG A1145    11535  10328   9508    307    415   1287       N\\nATOM   2422  NH2 ARG A1145      31.574  -7.829  40.293  1.00 85.74           N\\nANISOU 2422  NH2 ARG A1145    11982  10541  10053    302    578   1158       N\\nATOM   2423  N   ALA A1146      24.974 -10.393  44.287  1.00 78.38           N\\nANISOU 2423  N   ALA A1146    11025  10507   8249  -1011   1196    857       N\\nATOM   2424  CA  ALA A1146      24.412 -11.480  43.491  1.00 77.28           C\\nANISOU 2424  CA  ALA A1146    10992  10148   8224  -1212   1259    913       C\\nATOM   2425  C   ALA A1146      22.965 -11.191  43.114  1.00 83.69           C\\nANISOU 2425  C   ALA A1146    11482  11202   9113  -1389   1341    610       C\\nATOM   2426  O   ALA A1146      22.575 -11.340  41.951  1.00 81.20           O\\nANISOU 2426  O   ALA A1146    11127  10738   8988  -1380   1252    495       O\\nATOM   2427  CB  ALA A1146      24.519 -12.800  44.253  1.00 75.31           C\\nANISOU 2427  CB  ALA A1146    11049   9751   7813  -1491   1359   1239       C\\nATOM   2428  N   LYS A1147      22.154 -10.771  44.090  1.00 81.29           N\\nANISOU 2428  N   LYS A1147    10927  11303   8657  -1547   1506    451       N\\nATOM   2429  CA  LYS A1147      20.760 -10.442  43.804  1.00 80.52           C\\nANISOU 2429  CA  LYS A1147    10420  11486   8686  -1680   1585    116       C\\nATOM   2430  C   LYS A1147      20.649  -9.302  42.799  1.00 83.83           C\\nANISOU 2430  C   LYS A1147    10611  11866   9377  -1325   1329   -152       C\\nATOM   2431  O   LYS A1147      19.710  -9.273  41.995  1.00 68.30           O\\nANISOU 2431  O   LYS A1147     8403   9940   7609  -1375   1246   -350       O\\nATOM   2432  CB  LYS A1147      20.023 -10.088  45.098  1.00 67.35           C\\nANISOU 2432  CB  LYS A1147     8483  10311   6797  -1863   1853    -63       C\\nATOM   2433  N   ARG A1148      21.599  -8.365  42.815  1.00 85.54           N\\nANISOU 2433  N   ARG A1148    10910  11984   9606   -988   1167   -140       N\\nATOM   2434  CA  ARG A1148      21.574  -7.277  41.842  1.00 79.68           C\\nANISOU 2434  CA  ARG A1148    10031  11139   9107   -685    892   -317       C\\nATOM   2435  C   ARG A1148      21.891  -7.783  40.437  1.00 82.33           C\\nANISOU 2435  C   ARG A1148    10589  11152   9539   -673    733   -165       C\\nATOM   2436  O   ARG A1148      21.289  -7.330  39.457  1.00 90.33           O\\nANISOU 2436  O   ARG A1148    11469  12136  10717   -591    526   -312       O\\nATOM   2437  CB  ARG A1148      22.555  -6.182  42.261  1.00 70.66           C\\nANISOU 2437  CB  ARG A1148     8952   9944   7952   -403    768   -316       C\\nATOM   2438  CG  ARG A1148      21.892  -4.860  42.620  1.00 71.12           C\\nANISOU 2438  CG  ARG A1148     8676  10192   8155   -198    669   -688       C\\nATOM   2439  CD  ARG A1148      22.475  -4.260  43.892  1.00 73.19           C\\nANISOU 2439  CD  ARG A1148     8962  10601   8247   -122    743   -769       C\\nATOM   2440  NE  ARG A1148      23.934  -4.303  43.899  1.00 73.07           N\\nANISOU 2440  NE  ARG A1148     9271  10346   8145    -63    641   -461       N\\nATOM   2441  CZ  ARG A1148      24.686  -4.003  44.953  1.00 72.04           C\\nANISOU 2441  CZ  ARG A1148     9236  10306   7829    -40    656   -444       C\\nATOM   2442  NH1 ARG A1148      24.121  -3.632  46.093  1.00 77.77           N\\nANISOU 2442  NH1 ARG A1148     9809  11363   8378    -79    795   -729       N\\nATOM   2443  NH2 ARG A1148      26.005  -4.075  44.867  1.00 70.75           N\\nANISOU 2443  NH2 ARG A1148     9301   9933   7647     15    532   -167       N\\nATOM   2444  N   VAL A1149      22.824  -8.727  40.321  1.00 86.59           N\\nANISOU 2444  N   VAL A1149    11473  11454   9974   -742    812    112       N\\nATOM   2445  CA  VAL A1149      23.201  -9.252  39.011  1.00 82.53           C\\nANISOU 2445  CA  VAL A1149    11189  10655   9513   -723    713    200       C\\nATOM   2446  C   VAL A1149      22.160 -10.240  38.500  1.00 89.46           C\\nANISOU 2446  C   VAL A1149    12052  11515  10424  -1007    747    112       C\\nATOM   2447  O   VAL A1149      21.841 -10.260  37.304  1.00 88.71           O\\nANISOU 2447  O   VAL A1149    11995  11326  10387  -1003    583     17       O\\nATOM   2448  CB  VAL A1149      24.603  -9.881  39.089  1.00 69.15           C\\nANISOU 2448  CB  VAL A1149     9812   8710   7751   -638    790    459       C\\nATOM   2449  CG1 VAL A1149      24.961 -10.583  37.793  1.00 62.41           C\\nANISOU 2449  CG1 VAL A1149     9197   7590   6927   -632    765    483       C\\nATOM   2450  CG2 VAL A1149      25.636  -8.812  39.423  1.00 65.57           C\\nANISOU 2450  CG2 VAL A1149     9323   8286   7303   -385    710    522       C\\nATOM   2451  N   ILE A1150      21.606 -11.063  39.394  1.00 84.73           N\\nANISOU 2451  N   ILE A1150    11413  11014   9767  -1295    945    151       N\\nATOM   2452  CA  ILE A1150      20.566 -12.008  38.997  1.00 83.24           C\\nANISOU 2452  CA  ILE A1150    11179  10809   9639  -1639    980     64       C\\nATOM   2453  C   ILE A1150      19.315 -11.263  38.545  1.00 84.16           C\\nANISOU 2453  C   ILE A1150    10861  11211   9905  -1651    831   -246       C\\nATOM   2454  O   ILE A1150      18.622 -11.692  37.612  1.00 93.69           O\\nANISOU 2454  O   ILE A1150    12028  12360  11209  -1807    688   -369       O\\nATOM   2455  CB  ILE A1150      20.272 -12.986  40.152  1.00 84.83           C\\nANISOU 2455  CB  ILE A1150    11442  11060   9730  -2003   1240    225       C\\nATOM   2456  CG1 ILE A1150      21.486 -13.878  40.414  1.00 82.12           C\\nANISOU 2456  CG1 ILE A1150    11568  10333   9299  -1964   1285    553       C\\nATOM   2457  CG2 ILE A1150      19.059 -13.839  39.844  1.00 86.81           C\\nANISOU 2457  CG2 ILE A1150    11564  11344  10076  -2432   1287    113       C\\nATOM   2458  CD1 ILE A1150      21.367 -14.717  41.663  1.00 70.60           C\\nANISOU 2458  CD1 ILE A1150    10253   8891   7682  -2294   1484    806       C\\nATOM   2459  N   THR A1151      19.009 -10.131  39.188  1.00 79.62           N\\nANISOU 2459  N   THR A1151     9946  10934   9371  -1467    829   -404       N\\nATOM   2460  CA  THR A1151      17.920  -9.283  38.713  1.00 85.27           C\\nANISOU 2460  CA  THR A1151    10223  11875  10301  -1363    618   -716       C\\nATOM   2461  C   THR A1151      18.194  -8.785  37.302  1.00 88.73           C\\nANISOU 2461  C   THR A1151    10820  12078  10815  -1128    245   -709       C\\nATOM   2462  O   THR A1151      17.290  -8.744  36.460  1.00 89.80           O\\nANISOU 2462  O   THR A1151    10761  12268  11090  -1177     -2   -876       O\\nATOM   2463  CB  THR A1151      17.713  -8.098  39.655  1.00 85.11           C\\nANISOU 2463  CB  THR A1151     9861  12141  10338  -1127    668   -919       C\\nATOM   2464  OG1 THR A1151      17.364  -8.577  40.957  1.00 90.34           O\\nANISOU 2464  OG1 THR A1151    10377  13098  10849  -1398   1046   -947       O\\nATOM   2465  CG2 THR A1151      16.602  -7.194  39.144  1.00 80.06           C\\nANISOU 2465  CG2 THR A1151     8743  11680   9998   -942    398  -1262       C\\nATOM   2466  N   THR A1152      19.440  -8.402  37.023  1.00 89.05           N\\nANISOU 2466  N   THR A1152    11208  11880  10745   -898    191   -508       N\\nATOM   2467  CA  THR A1152      19.772  -7.948  35.679  1.00 88.03           C\\nANISOU 2467  CA  THR A1152    11283  11556  10607   -736   -114   -459       C\\nATOM   2468  C   THR A1152      19.666  -9.080  34.665  1.00 84.57           C\\nANISOU 2468  C   THR A1152    11105  10963  10066   -967   -143   -432       C\\nATOM   2469  O   THR A1152      19.276  -8.846  33.516  1.00 88.93           O\\nANISOU 2469  O   THR A1152    11704  11483  10603   -948   -442   -501       O\\nATOM   2470  CB  THR A1152      21.170  -7.335  35.670  1.00 84.93           C\\nANISOU 2470  CB  THR A1152    11169  10986  10115   -508    -96   -248       C\\nATOM   2471  OG1 THR A1152      21.238  -6.314  36.674  1.00 87.26           O\\nANISOU 2471  OG1 THR A1152    11240  11404  10511   -322    -88   -315       O\\nATOM   2472  CG2 THR A1152      21.473  -6.721  34.321  1.00 75.79           C\\nANISOU 2472  CG2 THR A1152    10215   9677   8903   -385   -386   -175       C\\nATOM   2473  N   PHE A1153      19.988 -10.311  35.069  1.00 80.31           N\\nANISOU 2473  N   PHE A1153    10763  10305   9447  -1189    130   -341       N\\nATOM   2474  CA  PHE A1153      19.838 -11.445  34.163  1.00 86.85           C\\nANISOU 2474  CA  PHE A1153    11850  10938  10209  -1417    102   -378       C\\nATOM   2475  C   PHE A1153      18.375 -11.753  33.876  1.00 94.28           C\\nANISOU 2475  C   PHE A1153    12493  12048  11280  -1692    -61   -605       C\\nATOM   2476  O   PHE A1153      18.051 -12.271  32.802  1.00 97.03           O\\nANISOU 2476  O   PHE A1153    13001  12289  11578  -1834   -250   -712       O\\nATOM   2477  CB  PHE A1153      20.524 -12.681  34.744  1.00 85.98           C\\nANISOU 2477  CB  PHE A1153    12033  10584  10052  -1564    394   -224       C\\nATOM   2478  CG  PHE A1153      21.973 -12.790  34.388  1.00 82.81           C\\nANISOU 2478  CG  PHE A1153    11993   9932   9541  -1323    479    -73       C\\nATOM   2479  CD1 PHE A1153      22.400 -12.549  33.096  1.00 87.89           C\\nANISOU 2479  CD1 PHE A1153    12840  10494  10062  -1196    348   -140       C\\nATOM   2480  CD2 PHE A1153      22.908 -13.132  35.345  1.00 77.41           C\\nANISOU 2480  CD2 PHE A1153    11425   9126   8862  -1234    685    132       C\\nATOM   2481  CE1 PHE A1153      23.735 -12.650  32.764  1.00 85.44           C\\nANISOU 2481  CE1 PHE A1153    12792  10012   9660   -991    485    -39       C\\nATOM   2482  CE2 PHE A1153      24.244 -13.233  35.021  1.00 77.07           C\\nANISOU 2482  CE2 PHE A1153    11625   8883   8776   -993    759    238       C\\nATOM   2483  CZ  PHE A1153      24.658 -12.992  33.729  1.00 80.39           C\\nANISOU 2483  CZ  PHE A1153    12194   9251   9099   -874    690    135       C\\nATOM   2484  N   ARG A1154      17.484 -11.446  34.817  1.00 88.53           N\\nANISOU 2484  N   ARG A1154    11311  11612  10713  -1783     15   -710       N\\nATOM   2485  CA  ARG A1154      16.070 -11.771  34.679  1.00 90.56           C\\nANISOU 2485  CA  ARG A1154    11175  12087  11146  -2076    -96   -944       C\\nATOM   2486  C   ARG A1154      15.287 -10.657  33.990  1.00 94.08           C\\nANISOU 2486  C   ARG A1154    11255  12736  11753  -1845   -507  -1151       C\\nATOM   2487  O   ARG A1154      14.589 -10.908  33.004  1.00 98.43           O\\nANISOU 2487  O   ARG A1154    11752  13292  12353  -1977   -823  -1290       O\\nATOM   2488  CB  ARG A1154      15.471 -12.072  36.056  1.00 91.66           C\\nANISOU 2488  CB  ARG A1154    10967  12492  11368  -2333    250   -973       C\\nATOM   2489  CG  ARG A1154      13.953 -12.110  36.087  1.00 98.75           C\\nANISOU 2489  CG  ARG A1154    11273  13741  12505  -2600    179  -1261       C\\nATOM   2490  CD  ARG A1154      13.450 -12.527  37.460  1.00 98.15           C\\nANISOU 2490  CD  ARG A1154    10903  13957  12432  -2937    616  -1264       C\\nATOM   2491  NE  ARG A1154      14.141 -11.809  38.526  1.00 96.23           N\\nANISOU 2491  NE  ARG A1154    10691  13830  12042  -2666    855  -1169       N\\nATOM   2492  CZ  ARG A1154      13.729 -10.656  39.043  1.00 99.35           C\\nANISOU 2492  CZ  ARG A1154    10627  14571  12550  -2384    862  -1413       C\\nATOM   2493  NH1 ARG A1154      12.618 -10.085  38.594  1.00102.81           N\\nANISOU 2493  NH1 ARG A1154    10503  15271  13290  -2299    634  -1752       N\\nATOM   2494  NH2 ARG A1154      14.426 -10.074  40.011  1.00 97.58           N\\nANISOU 2494  NH2 ARG A1154    10500  14418  12157  -2171   1067  -1343       N\\nATOM   2495  N   THR A1155      15.394  -9.425  34.492  1.00 91.70           N\\nANISOU 2495  N   THR A1155    10720  12575  11545  -1493   -553  -1180       N\\nATOM   2496  CA  THR A1155      14.626  -8.327  33.913  1.00 95.66           C\\nANISOU 2496  CA  THR A1155    10869  13211  12265  -1227   -991  -1368       C\\nATOM   2497  C   THR A1155      15.189  -7.887  32.570  1.00 97.84           C\\nANISOU 2497  C   THR A1155    11567  13229  12380  -1038  -1391  -1215       C\\nATOM   2498  O   THR A1155      14.426  -7.500  31.678  1.00103.63           O\\nANISOU 2498  O   THR A1155    12148  14011  13216   -975  -1852  -1325       O\\nATOM   2499  CB  THR A1155      14.590  -7.135  34.871  1.00 96.53           C\\nANISOU 2499  CB  THR A1155    10639  13482  12554   -890   -932  -1480       C\\nATOM   2500  OG1 THR A1155      15.865  -6.481  34.875  1.00 89.26           O\\nANISOU 2500  OG1 THR A1155    10139  12306  11469   -624   -926  -1243       O\\nATOM   2501  CG2 THR A1155      14.254  -7.597  36.282  1.00102.13           C\\nANISOU 2501  CG2 THR A1155    11038  14480  13285  -1108   -443  -1599       C\\nATOM   2502  N   GLY A1156      16.506  -7.938  32.402  1.00 98.59           N\\nANISOU 2502  N   GLY A1156    12176  13074  12209   -961  -1232   -958       N\\nATOM   2503  CA  GLY A1156      17.109  -7.426  31.192  1.00 97.17           C\\nANISOU 2503  CA  GLY A1156    12393  12702  11824   -813  -1538   -796       C\\nATOM   2504  C   GLY A1156      17.208  -5.922  31.139  1.00 94.99           C\\nANISOU 2504  C   GLY A1156    12028  12391  11674   -459  -1843   -727       C\\nATOM   2505  O   GLY A1156      17.414  -5.364  30.057  1.00 94.83           O\\nANISOU 2505  O   GLY A1156    12287  12241  11502   -370  -2199   -582       O\\nATOM   2506  N   THR A1157      17.055  -5.243  32.275  1.00 98.59           N\\nANISOU 2506  N   THR A1157    12130  12944  12386   -269  -1724   -831       N\\nATOM   2507  CA  THR A1157      17.188  -3.793  32.334  1.00 99.99           C\\nANISOU 2507  CA  THR A1157    12241  13012  12740     83  -2014   -798       C\\nATOM   2508  C   THR A1157      18.117  -3.396  33.475  1.00 95.58           C\\nANISOU 2508  C   THR A1157    11722  12408  12187    197  -1666   -741       C\\nATOM   2509  O   THR A1157      18.739  -4.258  34.103  1.00 99.83           O\\nANISOU 2509  O   THR A1157    12385  12993  12552     13  -1238   -673       O\\nATOM   2510  CB  THR A1157      15.819  -3.130  32.503  1.00100.53           C\\nANISOU 2510  CB  THR A1157    11744  13243  13210    283  -2359  -1106       C\\nATOM   2511  N   TRP A1158      18.225  -2.094  33.747  1.00 93.22           N\\nANISOU 2511  N   TRP A1158    11337  11987  12095    500  -1890   -770       N\\nATOM   2512  CA  TRP A1158      19.077  -1.577  34.810  1.00 93.29           C\\nANISOU 2512  CA  TRP A1158    11380  11944  12121    611  -1638   -757       C\\nATOM   2513  C   TRP A1158      18.284  -1.180  36.050  1.00100.83           C\\nANISOU 2513  C   TRP A1158    11839  13130  13343    767  -1520  -1143       C\\nATOM   2514  O   TRP A1158      18.687  -0.262  36.773  1.00104.41           O\\nANISOU 2514  O   TRP A1158    12262  13494  13913    976  -1523  -1234       O\\nATOM   2515  CB  TRP A1158      19.888  -0.380  34.315  1.00 93.24           C\\nANISOU 2515  CB  TRP A1158    11675  11603  12148    796  -1939   -534       C\\nATOM   2516  CG  TRP A1158      20.831  -0.689  33.202  1.00 90.86           C\\nANISOU 2516  CG  TRP A1158    11861  11134  11527    615  -1955   -159       C\\nATOM   2517  CD1 TRP A1158      20.661  -0.401  31.878  1.00 92.31           C\\nANISOU 2517  CD1 TRP A1158    12294  11175  11605    591  -2335     30       C\\nATOM   2518  CD2 TRP A1158      22.100  -1.341  33.312  1.00 84.64           C\\nANISOU 2518  CD2 TRP A1158    11359  10335  10467    435  -1569     52       C\\nATOM   2519  NE1 TRP A1158      21.746  -0.835  31.158  1.00 87.61           N\\nANISOU 2519  NE1 TRP A1158    12125  10516  10649    382  -2146    322       N\\nATOM   2520  CE2 TRP A1158      22.643  -1.417  32.015  1.00 81.33           C\\nANISOU 2520  CE2 TRP A1158    11324   9793   9787    307  -1675    322       C\\nATOM   2521  CE3 TRP A1158      22.829  -1.871  34.381  1.00 79.01           C\\nANISOU 2521  CE3 TRP A1158    10605   9715   9699    377  -1161     35       C\\nATOM   2522  CZ2 TRP A1158      23.881  -2.001  31.759  1.00 77.25           C\\nANISOU 2522  CZ2 TRP A1158    11088   9260   9004    149  -1343    521       C\\nATOM   2523  CZ3 TRP A1158      24.059  -2.452  34.124  1.00 69.87           C\\nANISOU 2523  CZ3 TRP A1158     9733   8502   8314    244   -903    268       C\\nATOM   2524  CH2 TRP A1158      24.572  -2.511  32.824  1.00 69.73           C\\nANISOU 2524  CH2 TRP A1158    10033   8375   8085    144   -972    482       C\\nATOM   2525  N   ASP A1159      17.156  -1.850  36.306  1.00 98.45           N\\nANISOU 2525  N   ASP A1159    11135  13138  13133    646  -1402  -1399       N\\nATOM   2526  CA  ASP A1159      16.331  -1.497  37.457  1.00 97.23           C\\nANISOU 2526  CA  ASP A1159    10456  13283  13205    769  -1227  -1814       C\\nATOM   2527  C   ASP A1159      17.098  -1.638  38.765  1.00 90.66           C\\nANISOU 2527  C   ASP A1159     9725  12569  12151    685   -774  -1819       C\\nATOM   2528  O   ASP A1159      16.820  -0.916  39.727  1.00 92.33           O\\nANISOU 2528  O   ASP A1159     9651  12933  12497    879   -679  -2146       O\\nATOM   2529  CB  ASP A1159      15.076  -2.368  37.498  1.00105.69           C\\nANISOU 2529  CB  ASP A1159    11073  14718  14366    540  -1095  -2046       C\\nATOM   2530  CG  ASP A1159      14.329  -2.379  36.182  1.00109.35           C\\nANISOU 2530  CG  ASP A1159    11447  15092  15007    573  -1581  -2031       C\\nATOM   2531  OD1 ASP A1159      14.839  -2.991  35.220  1.00106.95           O\\nANISOU 2531  OD1 ASP A1159    11588  14593  14457    378  -1693  -1714       O\\nATOM   2532  OD2 ASP A1159      13.231  -1.786  36.115  1.00113.68           O\\nANISOU 2532  OD2 ASP A1159    11472  15783  15940    804  -1860  -2361       O\\nATOM   2533  N   ALA A1160      18.061  -2.558  38.822  1.00 90.75           N\\nANISOU 2533  N   ALA A1160    10142  12514  11824    416   -516  -1483       N\\nATOM   2534  CA  ALA A1160      18.793  -2.777  40.062  1.00 83.07           C\\nANISOU 2534  CA  ALA A1160     9285  11661  10616    322   -147  -1445       C\\nATOM   2535  C   ALA A1160      19.805  -1.671  40.330  1.00 83.07           C\\nANISOU 2535  C   ALA A1160     9492  11427  10644    577   -301  -1398       C\\nATOM   2536  O   ALA A1160      20.159  -1.427  41.488  1.00 80.26           O\\nANISOU 2536  O   ALA A1160     9111  11213  10170    595    -98  -1520       O\\nATOM   2537  CB  ALA A1160      19.490  -4.133  40.023  1.00 69.19           C\\nANISOU 2537  CB  ALA A1160     7878   9858   8554     -5    110  -1098       C\\nATOM   2538  N   TYR A1161      20.270  -0.989  39.289  1.00 85.89           N\\nANISOU 2538  N   TYR A1161    10067  11436  11131    737   -663  -1221       N\\nATOM   2539  CA  TYR A1161      21.312   0.021  39.439  1.00 81.29           C\\nANISOU 2539  CA  TYR A1161     9712  10587  10590    902   -820  -1122       C\\nATOM   2540  C   TYR A1161      20.830   1.413  39.031  1.00 86.56           C\\nANISOU 2540  C   TYR A1161    10259  11009  11620   1221  -1257  -1309       C\\nATOM   2541  O   TYR A1161      19.780   1.882  39.473  1.00 90.75           O\\nANISOU 2541  O   TYR A1161    10405  11678  12398   1423  -1325  -1710       O\\nATOM   2542  CB  TYR A1161      22.541  -0.357  38.608  1.00 78.82           C\\nANISOU 2542  CB  TYR A1161     9822  10037  10089    757   -833   -681       C\\nATOM   2543  CG  TYR A1161      23.144  -1.708  38.932  1.00 79.07           C\\nANISOU 2543  CG  TYR A1161    10004  10209   9831    508   -467   -486       C\\nATOM   2544  CD1 TYR A1161      22.612  -2.876  38.400  1.00 78.87           C\\nANISOU 2544  CD1 TYR A1161     9993  10274   9701    320   -342   -427       C\\nATOM   2545  CD2 TYR A1161      24.263  -1.813  39.748  1.00 75.01           C\\nANISOU 2545  CD2 TYR A1161     9629   9697   9174    468   -297   -359       C\\nATOM   2546  CE1 TYR A1161      23.166  -4.110  38.683  1.00 74.50           C\\nANISOU 2546  CE1 TYR A1161     9613   9760   8934    118    -53   -248       C\\nATOM   2547  CE2 TYR A1161      24.824  -3.042  40.039  1.00 67.83           C\\nANISOU 2547  CE2 TYR A1161     8865   8860   8048    288    -30   -162       C\\nATOM   2548  CZ  TYR A1161      24.272  -4.189  39.504  1.00 71.43           C\\nANISOU 2548  CZ  TYR A1161     9359   9354   8428    123     94   -104       C\\nATOM   2549  OH  TYR A1161      24.829  -5.416  39.787  1.00 69.66           O\\nANISOU 2549  OH  TYR A1161     9313   9118   8037    -32    319     91       O\\nATOM   2550  N   SER A 364      17.508   3.047  36.367  1.00104.00           N\\nATOM   2551  CA  SER A 364      18.568   3.670  35.585  1.00104.92           C\\nATOM   2552  C   SER A 364      18.623   3.097  34.167  1.00111.72           C\\nATOM   2553  O   SER A 364      19.675   3.111  33.526  1.00111.66           O\\nATOM   2554  CB  SER A 364      19.919   3.488  36.282  1.00 97.65           C\\nATOM   2555  N   GLN A 365      17.486   2.600  33.682  1.00122.15           N\\nATOM   2556  CA  GLN A 365      17.397   1.937  32.386  1.00115.38           C\\nATOM   2557  C   GLN A 365      16.553   2.767  31.428  1.00110.61           C\\nATOM   2558  O   GLN A 365      15.419   3.137  31.753  1.00 98.43           O\\nATOM   2559  CB  GLN A 365      16.796   0.536  32.527  1.00106.22           C\\nATOM   2560  N   GLN A 366      17.101   3.039  30.246  1.00120.06           N\\nATOM   2561  CA  GLN A 366      16.385   3.791  29.223  1.00115.06           C\\nATOM   2562  C   GLN A 366      15.363   2.887  28.544  1.00110.82           C\\nATOM   2563  O   GLN A 366      15.719   1.836  27.999  1.00106.83           O\\nATOM   2564  CB  GLN A 366      17.364   4.363  28.199  1.00114.61           C\\nATOM   2565  N   LYS A 367      14.097   3.295  28.574  1.00106.95           N\\nATOM   2566  CA  LYS A 367      13.014   2.529  27.974  1.00112.85           C\\nATOM   2567  C   LYS A 367      12.771   2.895  26.516  1.00109.20           C\\nATOM   2568  O   LYS A 367      11.803   2.410  25.921  1.00103.35           O\\nATOM   2569  CB  LYS A 367      11.727   2.721  28.781  1.00115.42           C\\nATOM   2570  N   GLU A 368      13.626   3.733  25.930  1.00114.20           N\\nATOM   2571  CA  GLU A 368      13.436   4.206  24.566  1.00 99.97           C\\nATOM   2572  C   GLU A 368      14.152   3.361  23.525  1.00100.67           C\\nATOM   2573  O   GLU A 368      13.805   3.444  22.342  1.00 97.34           O\\nATOM   2574  CB  GLU A 368      13.920   5.655  24.437  1.00 81.44           C\\nATOM   2575  CG  GLU A 368      13.087   6.681  25.188  1.00 79.48           C\\nATOM   2576  CD  GLU A 368      11.923   7.216  24.368  1.00 87.69           C\\nATOM   2577  OE1 GLU A 368      11.484   6.529  23.419  1.00 87.57           O\\nATOM   2578  OE2 GLU A 368      11.451   8.332  24.674  1.00 90.78           O\\nATOM   2579  N   LYS A 369      15.139   2.557  23.932  1.00101.97           N\\nATOM   2580  CA  LYS A 369      15.965   1.842  22.963  1.00 93.96           C\\nATOM   2581  C   LYS A 369      15.123   0.959  22.051  1.00 87.89           C\\nATOM   2582  O   LYS A 369      15.377   0.886  20.844  1.00 84.82           O\\nATOM   2583  CB  LYS A 369      17.025   1.012  23.689  1.00 94.15           C\\nATOM   2584  N   LYS A 370      14.107   0.291  22.605  1.00 95.07           N\\nATOM   2585  CA  LYS A 370      13.254  -0.567  21.787  1.00 92.51           C\\nATOM   2586  C   LYS A 370      12.587   0.220  20.665  1.00 85.60           C\\nATOM   2587  O   LYS A 370      12.454  -0.280  19.541  1.00 77.93           O\\nATOM   2588  CB  LYS A 370      12.203  -1.254  22.662  1.00 85.65           C\\nATOM   2589  N   ALA A 371      12.167   1.454  20.944  1.00 85.70           N\\nATOM   2590  CA  ALA A 371      11.556   2.271  19.901  1.00 78.85           C\\nATOM   2591  C   ALA A 371      12.589   2.776  18.902  1.00 73.40           C\\nATOM   2592  O   ALA A 371      12.274   2.940  17.718  1.00 67.94           O\\nATOM   2593  CB  ALA A 371      10.805   3.440  20.520  1.00 20.00           C\\nATOM   2594  N   THR A 372      13.820   3.030  19.357  1.00 75.36           N\\nATOM   2595  CA  THR A 372      14.875   3.470  18.451  1.00 64.07           C\\nATOM   2596  C   THR A 372      15.326   2.343  17.535  1.00 71.79           C\\nATOM   2597  O   THR A 372      15.714   2.593  16.389  1.00 80.74           O\\nATOM   2598  CB  THR A 372      16.066   4.010  19.246  1.00 69.33           C\\nATOM   2599  OG1 THR A 372      15.634   5.071  20.104  1.00 74.68           O\\nATOM   2600  CG2 THR A 372      17.138   4.544  18.316  1.00 68.04           C\\nATOM   2601  N   GLN A 373      15.283   1.100  18.019  1.00 68.72           N\\nATOM   2602  CA  GLN A 373      15.663  -0.031  17.180  1.00 79.96           C\\nATOM   2603  C   GLN A 373      14.624  -0.283  16.095  1.00 79.40           C\\nATOM   2604  O   GLN A 373      14.972  -0.633  14.961  1.00 75.09           O\\nATOM   2605  CB  GLN A 373      15.857  -1.276  18.043  1.00 95.27           C\\nATOM   2606  CG  GLN A 373      17.006  -1.162  19.028  1.00107.01           C\\nATOM   2607  CD  GLN A 373      16.835  -2.074  20.228  1.00113.19           C\\nATOM   2608  OE1 GLN A 373      15.768  -2.652  20.438  1.00109.22           O\\nATOM   2609  NE2 GLN A 373      17.889  -2.204  21.025  1.00117.08           N\\nATOM   2610  N   MET A 374      13.345  -0.105  16.421  1.00 79.17           N\\nATOM   2611  CA  MET A 374      12.307  -0.277  15.413  1.00 76.40           C\\nATOM   2612  C   MET A 374      12.384   0.814  14.350  1.00 70.69           C\\nATOM   2613  O   MET A 374      12.182   0.543  13.160  1.00 68.25           O\\nATOM   2614  CB  MET A 374      10.934  -0.292  16.079  1.00 77.49           C\\nATOM   2615  CG  MET A 374       9.801  -0.689  15.153  1.00 81.14           C\\nATOM   2616  SD  MET A 374       8.219  -0.741  16.009  1.00 84.97           S\\nATOM   2617  CE  MET A 374       8.086   0.958  16.565  1.00103.28           C\\nATOM   2618  N   ALA A 375      12.684   2.052  14.756  1.00 72.85           N\\nATOM   2619  CA  ALA A 375      12.789   3.144  13.793  1.00 69.01           C\\nATOM   2620  C   ALA A 375      13.899   2.887  12.783  1.00 71.99           C\\nATOM   2621  O   ALA A 375      13.756   3.203  11.596  1.00 68.65           O\\nATOM   2622  CB  ALA A 375      13.021   4.464  14.513  1.00 20.00           C\\nATOM   2623  N   ALA A 376      15.014   2.312  13.234  1.00 72.30           N\\nATOM   2624  CA  ALA A 376      16.110   2.018  12.320  1.00 74.21           C\\nATOM   2625  C   ALA A 376      15.790   0.830  11.427  1.00 77.19           C\\nATOM   2626  O   ALA A 376      16.261   0.771  10.285  1.00 87.02           O\\nATOM   2627  CB  ALA A 376      17.398   1.765  13.104  1.00 74.32           C\\nATOM   2628  N   ILE A 377      15.001  -0.125  11.921  1.00 87.67           N\\nATOM   2629  CA  ILE A 377      14.633  -1.265  11.089  1.00 95.90           C\\nATOM   2630  C   ILE A 377      13.706  -0.839   9.957  1.00101.03           C\\nATOM   2631  O   ILE A 377      13.826  -1.331   8.830  1.00 92.85           O\\nATOM   2632  CB  ILE A 377      13.963  -2.361  11.939  1.00 20.00           C\\nATOM   2633  CG1 ILE A 377      14.964  -2.954  12.932  1.00 20.00           C\\nATOM   2634  CG2 ILE A 377      13.385  -3.448  11.046  1.00 20.00           C\\nATOM   2635  CD1 ILE A 377      14.332  -3.844  13.978  1.00 20.00           C\\nATOM   2636  N   VAL A 378      12.786   0.088  10.234  1.00 89.06           N\\nATOM   2637  CA  VAL A 378      11.896   0.596   9.192  1.00 75.68           C\\nATOM   2638  C   VAL A 378      12.683   1.387   8.156  1.00 75.18           C\\nATOM   2639  O   VAL A 378      12.445   1.268   6.948  1.00 76.19           O\\nATOM   2640  CB  VAL A 378      10.775   1.445   9.820  1.00 64.00           C\\nATOM   2641  CG1 VAL A 378       9.960   2.132   8.740  1.00 62.64           C\\nATOM   2642  CG2 VAL A 378       9.887   0.580  10.701  1.00 69.48           C\\nATOM   2643  N   ALA A 379      13.629   2.210   8.612  1.00 84.87           N\\nATOM   2644  CA  ALA A 379      14.470   2.963   7.688  1.00 87.10           C\\nATOM   2645  C   ALA A 379      15.330   2.035   6.842  1.00 88.96           C\\nATOM   2646  O   ALA A 379      15.578   2.310   5.662  1.00 81.40           O\\nATOM   2647  CB  ALA A 379      15.348   3.945   8.463  1.00 44.79           C\\nATOM   2648  N   GLY A 380      15.802   0.935   7.428  1.00 77.23           N\\nATOM   2649  CA  GLY A 380      16.620   0.001   6.670  1.00 80.45           C\\nATOM   2650  C   GLY A 380      15.818  -0.749   5.624  1.00 77.59           C\\nATOM   2651  O   GLY A 380      16.246  -0.884   4.475  1.00 69.34           O\\nATOM   2652  N   VAL A 381      14.642  -1.252   6.012  1.00 81.99           N\\nATOM   2653  CA  VAL A 381      13.758  -1.918   5.057  1.00 83.38           C\\nATOM   2654  C   VAL A 381      13.412  -0.978   3.910  1.00 77.79           C\\nATOM   2655  O   VAL A 381      13.311  -1.397   2.751  1.00 66.26           O\\nATOM   2656  CB  VAL A 381      12.494  -2.434   5.772  1.00 76.89           C\\nATOM   2657  CG1 VAL A 381      11.472  -2.937   4.769  1.00 69.18           C\\nATOM   2658  CG2 VAL A 381      12.858  -3.534   6.752  1.00 75.31           C\\nATOM   2659  N   PHE A 382      13.231   0.308   4.214  1.00 79.75           N\\nATOM   2660  CA  PHE A 382      13.014   1.298   3.166  1.00 68.40           C\\nATOM   2661  C   PHE A 382      14.165   1.294   2.171  1.00 73.80           C\\nATOM   2662  O   PHE A 382      13.953   1.186   0.958  1.00 78.38           O\\nATOM   2663  CB  PHE A 382      12.844   2.679   3.796  1.00 62.89           C\\nATOM   2664  CG  PHE A 382      12.514   3.767   2.815  1.00 69.81           C\\nATOM   2665  CD1 PHE A 382      11.203   4.013   2.452  1.00 78.17           C\\nATOM   2666  CD2 PHE A 382      13.513   4.560   2.276  1.00 67.00           C\\nATOM   2667  CE1 PHE A 382      10.895   5.021   1.557  1.00 75.89           C\\nATOM   2668  CE2 PHE A 382      13.211   5.566   1.380  1.00 62.38           C\\nATOM   2669  CZ  PHE A 382      11.900   5.797   1.021  1.00 65.04           C\\nATOM   2670  N   ILE A 383      15.399   1.395   2.672  1.00 79.94           N\\nATOM   2671  CA  ILE A 383      16.564   1.405   1.792  1.00 76.66           C\\nATOM   2672  C   ILE A 383      16.668   0.093   1.027  1.00 74.25           C\\nATOM   2673  O   ILE A 383      17.053   0.072  -0.148  1.00 81.52           O\\nATOM   2674  CB  ILE A 383      17.840   1.702   2.601  1.00 71.78           C\\nATOM   2675  CG1 ILE A 383      17.851   3.163   3.035  1.00 63.66           C\\nATOM   2676  CG2 ILE A 383      19.084   1.400   1.789  1.00 79.30           C\\nATOM   2677  CD1 ILE A 383      17.701   4.126   1.880  1.00 64.10           C\\nATOM   2678  N   ILE A 384      16.309  -1.019   1.668  1.00 77.47           N\\nANISOU 2678  N   ILE A 384    10269   8636  10532   1676   -785   -446       N\\nATOM   2679  CA  ILE A 384      16.346  -2.312   0.990  1.00 77.09           C\\nANISOU 2679  CA  ILE A 384    10626   8415  10249   1786   -743   -487       C\\nATOM   2680  C   ILE A 384      15.395  -2.323  -0.203  1.00 79.25           C\\nANISOU 2680  C   ILE A 384    11068   8660  10381   1476   -652   -397       C\\nATOM   2681  O   ILE A 384      15.699  -2.905  -1.252  1.00 79.85           O\\nANISOU 2681  O   ILE A 384    11325   8712  10302   1540   -544   -477       O\\nATOM   2682  CB  ILE A 384      16.026  -3.439   1.989  1.00 74.75           C\\nANISOU 2682  CB  ILE A 384    10740   7870   9793   1895   -906   -471       C\\nATOM   2683  CG1 ILE A 384      17.200  -3.648   2.941  1.00 77.41           C\\nANISOU 2683  CG1 ILE A 384    10961   8240  10210   2294  -1026   -570       C\\nATOM   2684  CG2 ILE A 384      15.704  -4.737   1.267  1.00 71.60           C\\nANISOU 2684  CG2 ILE A 384    10844   7191   9169   1898   -891   -497       C\\nATOM   2685  CD1 ILE A 384      18.443  -4.186   2.256  1.00 79.90           C\\nANISOU 2685  CD1 ILE A 384    11224   8571  10564   2673   -951   -738       C\\nATOM   2686  N   CYS A 385      14.245  -1.657  -0.076  1.00 75.66           N\\nANISOU 2686  N   CYS A 385    10540   8236   9971   1156   -704   -252       N\\nATOM   2687  CA  CYS A 385      13.214  -1.744  -1.106  1.00 79.40           C\\nANISOU 2687  CA  CYS A 385    11178   8693  10298    856   -690   -152       C\\nATOM   2688  C   CYS A 385      13.483  -0.807  -2.281  1.00 77.99           C\\nANISOU 2688  C   CYS A 385    10754   8710  10168    769   -575    -84       C\\nATOM   2689  O   CYS A 385      13.199  -1.160  -3.432  1.00 80.47           O\\nANISOU 2689  O   CYS A 385    11270   9043  10261    646   -531    -66       O\\nATOM   2690  CB  CYS A 385      11.842  -1.449  -0.500  1.00 80.67           C\\nANISOU 2690  CB  CYS A 385    11312   8841  10500    576   -801    -23       C\\nATOM   2691  SG  CYS A 385      11.235  -2.722   0.645  1.00 83.19           S\\nANISOU 2691  SG  CYS A 385    12017   8939  10653    532   -901    -25       S\\nATOM   2692  N   TRP A 386      14.018   0.384  -2.024  1.00 68.60           N\\nANISOU 2692  N   TRP A 386     9160   7658   9246    804   -535    -37       N\\nATOM   2693  CA  TRP A 386      14.213   1.350  -3.095  1.00 71.32           C\\nANISOU 2693  CA  TRP A 386     9293   8158   9646    667   -432     98       C\\nATOM   2694  C   TRP A 386      15.618   1.346  -3.677  1.00 73.91           C\\nANISOU 2694  C   TRP A 386     9483   8642   9959    842   -227     12       C\\nATOM   2695  O   TRP A 386      15.812   1.874  -4.776  1.00 77.41           O\\nANISOU 2695  O   TRP A 386     9849   9237  10328    705    -92    139       O\\nATOM   2696  CB  TRP A 386      13.885   2.767  -2.612  1.00 68.85           C\\nANISOU 2696  CB  TRP A 386     8631   7857   9670    543   -510    230       C\\nATOM   2697  CG  TRP A 386      12.415   3.071  -2.565  1.00 72.68           C\\nANISOU 2697  CG  TRP A 386     9161   8279  10174    338   -661    365       C\\nATOM   2698  CD1 TRP A 386      11.648   3.236  -1.448  1.00 67.00           C\\nANISOU 2698  CD1 TRP A 386     8370   7494   9594    332   -777    320       C\\nATOM   2699  CD2 TRP A 386      11.534   3.244  -3.684  1.00 78.89           C\\nANISOU 2699  CD2 TRP A 386    10042   9108  10823    121   -715    558       C\\nATOM   2700  NE1 TRP A 386      10.348   3.502  -1.801  1.00 70.95           N\\nANISOU 2700  NE1 TRP A 386     8865   8000  10093    139   -882    461       N\\nATOM   2701  CE2 TRP A 386      10.251   3.512  -3.168  1.00 76.55           C\\nANISOU 2701  CE2 TRP A 386     9677   8767  10641      9   -876    617       C\\nATOM   2702  CE3 TRP A 386      11.706   3.200  -5.072  1.00 78.88           C\\nANISOU 2702  CE3 TRP A 386    10168   9215  10586     17   -646    682       C\\nATOM   2703  CZ2 TRP A 386       9.146   3.736  -3.988  1.00 75.36           C\\nANISOU 2703  CZ2 TRP A 386     9547   8666  10419   -188  -1008    800       C\\nATOM   2704  CZ3 TRP A 386      10.606   3.421  -5.885  1.00 78.84           C\\nANISOU 2704  CZ3 TRP A 386    10240   9252  10462   -196   -791    875       C\\nATOM   2705  CH2 TRP A 386       9.343   3.684  -5.340  1.00 78.30           C\\nANISOU 2705  CH2 TRP A 386    10069   9128  10555   -289   -989    935       C\\nATOM   2706  N   LEU A 387      16.599   0.779  -2.986  1.00 71.16           N\\nANISOU 2706  N   LEU A 387     9082   8289   9666   1138   -199   -185       N\\nATOM   2707  CA  LEU A 387      17.963   0.908  -3.486  1.00 77.39           C\\nANISOU 2707  CA  LEU A 387     9613   9290  10501   1307     10   -275       C\\nATOM   2708  C   LEU A 387      18.178   0.130  -4.783  1.00 81.59           C\\nANISOU 2708  C   LEU A 387    10394   9919  10687   1358    212   -346       C\\nATOM   2709  O   LEU A 387      18.816   0.661  -5.701  1.00 86.35           O\\nANISOU 2709  O   LEU A 387    10786  10774  11250   1288    442   -288       O\\nATOM   2710  CB  LEU A 387      18.985   0.473  -2.436  1.00 76.08           C\\nANISOU 2710  CB  LEU A 387     9284   9129  10492   1656    -47   -481       C\\nATOM   2711  CG  LEU A 387      20.393   0.933  -2.792  1.00 73.95           C\\nANISOU 2711  CG  LEU A 387     8566   9145  10385   1779    152   -557       C\\nATOM   2712  CD1 LEU A 387      20.380   2.425  -3.067  1.00 70.62           C\\nANISOU 2712  CD1 LEU A 387     7792   8838  10202   1432    210   -352       C\\nATOM   2713  CD2 LEU A 387      21.363   0.599  -1.677  1.00 74.27           C\\nANISOU 2713  CD2 LEU A 387     8384   9220  10617   2125     25   -752       C\\nATOM   2714  N   PRO A 388      17.692  -1.112  -4.913  1.00 79.42           N\\nANISOU 2714  N   PRO A 388    10576   9454  10144   1463    148   -479       N\\nATOM   2715  CA  PRO A 388      17.785  -1.780  -6.223  1.00 83.37           C\\nANISOU 2715  CA  PRO A 388    11355  10040  10283   1481    328   -585       C\\nATOM   2716  C   PRO A 388      17.190  -0.967  -7.356  1.00 88.60           C\\nANISOU 2716  C   PRO A 388    12005  10889  10771   1117    400   -357       C\\nATOM   2717  O   PRO A 388      17.670  -1.054  -8.493  1.00 89.35           O\\nANISOU 2717  O   PRO A 388    12143  11216  10591   1123    637   -407       O\\nATOM   2718  CB  PRO A 388      17.015  -3.085  -5.998  1.00 78.09           C\\nANISOU 2718  CB  PRO A 388    11219   9031   9418   1534    148   -722       C\\nATOM   2719  CG  PRO A 388      17.214  -3.371  -4.563  1.00 73.10           C\\nANISOU 2719  CG  PRO A 388    10537   8200   9037   1742    -22   -758       C\\nATOM   2720  CD  PRO A 388      17.196  -2.039  -3.878  1.00 74.29           C\\nANISOU 2720  CD  PRO A 388    10229   8503   9495   1588    -73   -564       C\\nATOM   2721  N   PHE A 389      16.157  -0.168  -7.077  1.00 87.86           N\\nANISOU 2721  N   PHE A 389    11851  10717  10815    821    202   -105       N\\nATOM   2722  CA  PHE A 389      15.588   0.699  -8.103  1.00 88.83           C\\nANISOU 2722  CA  PHE A 389    11946  10997  10808    504    215    164       C\\nATOM   2723  C   PHE A 389      16.581   1.776  -8.524  1.00 87.11           C\\nANISOU 2723  C   PHE A 389    11342  11030  10726    460    445    317       C\\nATOM   2724  O   PHE A 389      16.791   2.009  -9.719  1.00 91.58           O\\nANISOU 2724  O   PHE A 389    11960  11831  11005    327    627    435       O\\nATOM   2725  CB  PHE A 389      14.287   1.323  -7.592  1.00 81.78           C\\nANISOU 2725  CB  PHE A 389    11019   9946  10106    271    -69    378       C\\nATOM   2726  CG  PHE A 389      13.670   2.319  -8.536  1.00 78.75           C\\nANISOU 2726  CG  PHE A 389    10580   9686   9656    -11   -125    698       C\\nATOM   2727  CD1 PHE A 389      12.947   1.897  -9.638  1.00 72.20           C\\nANISOU 2727  CD1 PHE A 389    10065   8946   8421   -182   -197    758       C\\nATOM   2728  CD2 PHE A 389      13.795   3.677  -8.309  1.00 74.32           C\\nANISOU 2728  CD2 PHE A 389     9675   9124   9438   -104   -142    940       C\\nATOM   2729  CE1 PHE A 389      12.374   2.812 -10.501  1.00 66.21           C\\nANISOU 2729  CE1 PHE A 389     9270   8308   7580   -418   -296   1089       C\\nATOM   2730  CE2 PHE A 389      13.221   4.593  -9.169  1.00 73.66           C\\nANISOU 2730  CE2 PHE A 389     9576   9102   9309   -336   -229   1275       C\\nATOM   2731  CZ  PHE A 389      12.508   4.160 -10.263  1.00 67.96           C\\nANISOU 2731  CZ  PHE A 389     9160   8501   8161   -483   -313   1367       C\\nATOM   2732  N   PHE A 390      17.211   2.438  -7.553  1.00 78.28           N\\nANISOU 2732  N   PHE A 390     9842   9876  10022    542    440    319       N\\nATOM   2733  CA  PHE A 390      18.154   3.503  -7.865  1.00 77.80           C\\nANISOU 2733  CA  PHE A 390     9387  10020  10154    435    640    473       C\\nATOM   2734  C   PHE A 390      19.520   2.977  -8.285  1.00 85.50           C\\nANISOU 2734  C   PHE A 390    10201  11281  11003    650    968    266       C\\nATOM   2735  O   PHE A 390      20.266   3.699  -8.955  1.00 80.65           O\\nANISOU 2735  O   PHE A 390     9313  10928  10401    495   1220    418       O\\nATOM   2736  CB  PHE A 390      18.290   4.441  -6.666  1.00 72.78           C\\nANISOU 2736  CB  PHE A 390     8403   9227  10023    409    479    515       C\\nATOM   2737  CG  PHE A 390      17.046   5.229  -6.384  1.00 71.97           C\\nANISOU 2737  CG  PHE A 390     8367   8891  10086    201    217    731       C\\nATOM   2738  CD1 PHE A 390      16.770   6.384  -7.095  1.00 73.92           C\\nANISOU 2738  CD1 PHE A 390     8531   9132  10422    -77    215   1066       C\\nATOM   2739  CD2 PHE A 390      16.146   4.810  -5.423  1.00 69.40           C\\nANISOU 2739  CD2 PHE A 390     8185   8358   9824    295    -21    611       C\\nATOM   2740  CE1 PHE A 390      15.624   7.110  -6.848  1.00 69.85           C\\nANISOU 2740  CE1 PHE A 390     8056   8392  10093   -202    -42   1247       C\\nATOM   2741  CE2 PHE A 390      14.995   5.533  -5.171  1.00 69.17           C\\nANISOU 2741  CE2 PHE A 390     8161   8162   9960    142   -234    777       C\\nATOM   2742  CZ  PHE A 390      14.735   6.685  -5.884  1.00 63.89           C\\nANISOU 2742  CZ  PHE A 390     7389   7471   9415    -78   -256   1080       C\\nATOM   2743  N   ILE A 391      19.865   1.744  -7.905  1.00 83.05           N\\nANISOU 2743  N   ILE A 391    10043  10926  10586   1005    976    -67       N\\nATOM   2744  CA  ILE A 391      21.044   1.100  -8.477  1.00 88.93           C\\nANISOU 2744  CA  ILE A 391    10677  11954  11158   1273   1299   -305       C\\nATOM   2745  C   ILE A 391      20.854   0.907  -9.975  1.00 91.28           C\\nANISOU 2745  C   ILE A 391    11243  12480  10960   1127   1541   -254       C\\nATOM   2746  O   ILE A 391      21.789   1.084 -10.766  1.00 94.74           O\\nANISOU 2746  O   ILE A 391    11451  13294  11253   1139   1904   -276       O\\nATOM   2747  CB  ILE A 391      21.321  -0.238  -7.761  1.00 85.00           C\\nANISOU 2747  CB  ILE A 391    10370  11271  10655   1728   1197   -664       C\\nATOM   2748  CG1 ILE A 391      21.803   0.004  -6.329  1.00 81.99           C\\nANISOU 2748  CG1 ILE A 391     9657  10782  10715   1901    995   -715       C\\nATOM   2749  CG2 ILE A 391      22.336  -1.068  -8.534  1.00 85.18           C\\nANISOU 2749  CG2 ILE A 391    10376  11551  10438   2063   1525   -960       C\\nATOM   2750  CD1 ILE A 391      22.006  -1.268  -5.531  1.00 79.71           C\\nANISOU 2750  CD1 ILE A 391     9598  10266  10423   2344    833   -991       C\\nATOM   2751  N   THR A 392      19.633   0.564 -10.388  1.00 91.03           N\\nANISOU 2751  N   THR A 392    11682  12262  10642    965   1345   -183       N\\nATOM   2752  CA  THR A 392      19.347   0.341 -11.801  1.00 92.03           C\\nANISOU 2752  CA  THR A 392    12124  12607  10236    813   1511   -151       C\\nATOM   2753  C   THR A 392      19.510   1.622 -12.611  1.00 96.64           C\\nANISOU 2753  C   THR A 392    12473  13487  10758    456   1684    247       C\\nATOM   2754  O   THR A 392      19.972   1.585 -13.759  1.00 99.51           O\\nANISOU 2754  O   THR A 392    12896  14212  10701    394   2002    256       O\\nATOM   2755  CB  THR A 392      17.934  -0.222 -11.949  1.00 85.65           C\\nANISOU 2755  CB  THR A 392    11821  11527   9195    670   1183   -144       C\\nATOM   2756  OG1 THR A 392      17.843  -1.462 -11.238  1.00 86.36           O\\nANISOU 2756  OG1 THR A 392    12169  11313   9330    965   1047   -489       O\\nATOM   2757  CG2 THR A 392      17.589  -0.458 -13.404  1.00 82.50           C\\nANISOU 2757  CG2 THR A 392    11776  11367   8203    498   1292   -131       C\\nATOM   2758  N   HIS A 393      19.187   2.742 -12.031  1.00 88.71           N\\nANISOU 2758  N   HIS A 393    11226  12324  10155    219   1485    579       N\\nATOM   2759  CA  HIS A 393      19.363   3.957 -12.738  1.00 88.98           C\\nANISOU 2759  CA  HIS A 393    11056  12550  10202   -130   1618   1001       C\\nATOM   2760  C   HIS A 393      20.809   4.181 -13.033  1.00 88.31           C\\nANISOU 2760  C   HIS A 393    10554  12829  10172   -105   2051    965       C\\nATOM   2761  O   HIS A 393      21.145   4.651 -14.071  1.00 90.40           O\\nANISOU 2761  O   HIS A 393    10759  13392  10197   -381   2313   1255       O\\nATOM   2762  CB  HIS A 393      18.863   5.074 -11.893  1.00 92.81           C\\nANISOU 2762  CB  HIS A 393    11357  12712  11192   -324   1304   1294       C\\nATOM   2763  CG  HIS A 393      17.412   5.334 -12.064  1.00 96.38           C\\nANISOU 2763  CG  HIS A 393    12141  12922  11557   -443    932   1454       C\\nATOM   2764  ND1 HIS A 393      16.815   5.355 -13.296  1.00101.35           N\\nANISOU 2764  ND1 HIS A 393    12985  13642  11882   -712    860   1815       N\\nATOM   2765  CD2 HIS A 393      16.440   5.591 -11.168  1.00 93.09           C\\nANISOU 2765  CD2 HIS A 393    11851  12212  11307   -333    611   1312       C\\nATOM   2766  CE1 HIS A 393      15.536   5.622 -13.155  1.00 98.51           C\\nANISOU 2766  CE1 HIS A 393    12830  13059  11540   -744    489   1868       C\\nATOM   2767  NE2 HIS A 393      15.282   5.762 -11.872  1.00 93.35           N\\nANISOU 2767  NE2 HIS A 393    12117  12180  11171   -533    357   1563       N\\nATOM   2768  N   ILE A 394      21.675   3.869 -12.094  1.00 95.53           N\\nANISOU 2768  N   ILE A 394    11157  13746  11395    209   2124    635       N\\nATOM   2769  CA  ILE A 394      23.103   4.065 -12.304  1.00100.46           C\\nANISOU 2769  CA  ILE A 394    11300  14765  12104    258   2532    556       C\\nATOM   2770  C   ILE A 394      23.590   3.234 -13.480  1.00110.00           C\\nANISOU 2770  C   ILE A 394    12669  16389  12736    410   2939    349       C\\nATOM   2771  O   ILE A 394      24.530   3.628 -14.181  1.00116.65           O\\nANISOU 2771  O   ILE A 394    13187  17679  13455    283   3367    434       O\\nATOM   2772  CB  ILE A 394      23.876   3.735 -11.014  1.00 95.87           C\\nANISOU 2772  CB  ILE A 394    10335  14092  12001    599   2436    239       C\\nATOM   2773  N   LEU A 395      22.959   2.084 -13.726  1.00109.05           N\\nANISOU 2773  N   LEU A 395    13051  16136  12246    661   2828     65       N\\nATOM   2774  CA  LEU A 395      23.384   1.213 -14.816  1.00115.80           C\\nANISOU 2774  CA  LEU A 395    14119  17349  12533    853   3195   -221       C\\nATOM   2775  C   LEU A 395      22.911   1.731 -16.169  1.00123.98           C\\nANISOU 2775  C   LEU A 395    15434  18666  13007    451   3352    106       C\\nATOM   2776  O   LEU A 395      23.622   1.591 -17.170  1.00132.70           O\\nANISOU 2776  O   LEU A 395    16488  20259  13673    459   3812     22       O\\nATOM   2777  CB  LEU A 395      22.873  -0.208 -14.578  1.00113.04           C\\nANISOU 2777  CB  LEU A 395    14254  16684  12011   1243   2983   -662       C\\nATOM   2778  CG  LEU A 395      23.285  -0.827 -13.242  1.00107.58           C\\nANISOU 2778  CG  LEU A 395    13379  15684  11813   1666   2788   -952       C\\nATOM   2779  CD1 LEU A 395      22.874  -2.287 -13.174  1.00109.94           C\\nANISOU 2779  CD1 LEU A 395    14213  15663  11896   2035   2631  -1369       C\\nATOM   2780  CD2 LEU A 395      24.782  -0.681 -13.009  1.00102.89           C\\nANISOU 2780  CD2 LEU A 395    12151  15454  11490   1927   3132  -1110       C\\nATOM   2781  N   ASN A 396      21.713   2.324 -16.219  1.00120.69           N\\nANISOU 2781  N   ASN A 396    15306  17974  12576    116   2975    478       N\\nATOM   2782  CA  ASN A 396      21.242   2.943 -17.454  1.00120.58           C\\nANISOU 2782  CA  ASN A 396    15547  18214  12053   -278   3052    871       C\\nATOM   2783  C   ASN A 396      22.194   4.031 -17.930  1.00122.42           C\\nANISOU 2783  C   ASN A 396    15355  18837  12322   -573   3455   1241       C\\nATOM   2784  O   ASN A 396      22.387   4.205 -19.139  1.00125.81           O\\nANISOU 2784  O   ASN A 396    15933  19697  12171   -784   3770   1420       O\\nATOM   2785  CB  ASN A 396      19.841   3.523 -17.251  1.00116.75           C\\nANISOU 2785  CB  ASN A 396    15328  17340  11693   -546   2527   1239       C\\nATOM   2786  CG  ASN A 396      18.760   2.676 -17.888  1.00117.94           C\\nANISOU 2786  CG  ASN A 396    16062  17433  11316   -534   2274   1087       C\\nATOM   2787  OD1 ASN A 396      18.987   1.516 -18.228  1.00121.59           O\\nANISOU 2787  OD1 ASN A 396    16780  18007  11413   -276   2424    626       O\\nATOM   2788  ND2 ASN A 396      17.576   3.253 -18.057  1.00116.24           N\\nANISOU 2788  ND2 ASN A 396    16052  17032  11079   -807   1870   1457       N\\nATOM   2789  N   ILE A 397      22.806   4.760 -16.997  1.00128.30           N\\nANISOU 2789  N   ILE A 397    15581  19448  13721   -619   3450   1356       N\\nATOM   2790  CA  ILE A 397      23.706   5.849 -17.357  1.00131.63           C\\nANISOU 2790  CA  ILE A 397    15568  20182  14265   -972   3805   1730       C\\nATOM   2791  C   ILE A 397      25.103   5.322 -17.667  1.00137.13           C\\nANISOU 2791  C   ILE A 397    15858  21427  14818   -764   4380   1392       C\\nATOM   2792  O   ILE A 397      25.789   5.839 -18.556  1.00140.52           O\\nANISOU 2792  O   ILE A 397    16093  22338  14959  -1056   4838   1642       O\\nATOM   2793  CB  ILE A 397      23.731   6.896 -16.228  1.00123.72           C\\nANISOU 2793  CB  ILE A 397    14191  18774  14042  -1149   3517   1971       C\\nATOM   2794  CG1 ILE A 397      22.331   7.473 -16.007  1.00113.56           C\\nANISOU 2794  CG1 ILE A 397    13280  16985  12883  -1327   2987   2301       C\\nATOM   2795  CG2 ILE A 397      24.735   8.002 -16.530  1.00125.40           C\\nANISOU 2795  CG2 ILE A 397    13930  19262  14453  -1557   3873   2337       C\\nATOM   2796  CD1 ILE A 397      22.251   8.459 -14.860  1.00102.21           C\\nANISOU 2796  CD1 ILE A 397    11537  15104  12195  -1449   2680   2462       C\\nATOM   2797  N   HIS A 398      25.537   4.278 -16.959  1.00136.75           N\\nANISOU 2797  N   HIS A 398    15674  21329  14958   -248   4372    832       N\\nATOM   2798  CA  HIS A 398      26.930   3.846 -17.033  1.00140.25           C\\nANISOU 2798  CA  HIS A 398    15599  22260  15431     23   4867    485       C\\nATOM   2799  C   HIS A 398      27.250   3.199 -18.376  1.00154.68           C\\nANISOU 2799  C   HIS A 398    17644  24638  16490    117   5371    293       C\\nATOM   2800  O   HIS A 398      28.121   3.674 -19.114  1.00162.37           O\\nANISOU 2800  O   HIS A 398    18256  26184  17254   -111   5901    448       O\\nATOM   2801  CB  HIS A 398      27.240   2.881 -15.886  1.00132.50           C\\nANISOU 2801  CB  HIS A 398    14462  21019  14861    602   4649    -39       C\\nATOM   2802  N   CYS A 399      26.570   2.103 -18.707  1.00157.99           N\\nANISOU 2802  N   CYS A 399    18652  24908  16468    436   5229    -65       N\\nATOM   2803  CA  CYS A 399      26.929   1.309 -19.875  1.00171.19           C\\nANISOU 2803  CA  CYS A 399    20554  27077  17414    635   5693   -403       C\\nATOM   2804  C   CYS A 399      25.915   1.388 -21.006  1.00172.38           C\\nANISOU 2804  C   CYS A 399    21379  27292  16826    306   5614   -163       C\\nATOM   2805  O   CYS A 399      26.152   0.799 -22.069  1.00171.94           O\\nANISOU 2805  O   CYS A 399    21574  27683  16070    417   5999   -433       O\\nATOM   2806  CB  CYS A 399      27.145  -0.157 -19.472  1.00177.68           C\\nANISOU 2806  CB  CYS A 399    21527  27720  18264   1324   5648  -1118       C\\nATOM   2807  SG  CYS A 399      25.689  -1.129 -18.956  1.00177.65           S\\nANISOU 2807  SG  CYS A 399    22318  26935  18245   1520   4957  -1341       S\\nATOM   2808  N   ASP A 400      24.802   2.093 -20.815  1.00169.42           N\\nANISOU 2808  N   ASP A 400    21292  26506  16572    -73   5118    313       N\\nATOM   2809  CA  ASP A 400      23.708   2.176 -21.779  1.00172.19           C\\nANISOU 2809  CA  ASP A 400    22278  26866  16282   -369   4909    565       C\\nATOM   2810  C   ASP A 400      23.130   0.810 -22.126  1.00178.49           C\\nANISOU 2810  C   ASP A 400    23661  27552  16606    -24   4760      1       C\\nATOM   2811  O   ASP A 400      22.354   0.694 -23.084  1.00180.90           O\\nANISOU 2811  O   ASP A 400    24500  27979  16254   -230   4642     91       O\\nATOM   2812  CB  ASP A 400      24.139   2.903 -23.061  1.00174.58           C\\nANISOU 2812  CB  ASP A 400    22570  27804  15958   -772   5382    965       C\\nATOM   2813  N   CYS A 401      23.494  -0.229 -21.377  1.00180.63           N\\nANISOU 2813  N   CYS A 401    23862  27575  17194    489   4738   -576       N\\nATOM   2814  CA  CYS A 401      22.923  -1.551 -21.583  1.00179.00           C\\nANISOU 2814  CA  CYS A 401    24242  27130  16641    806   4543  -1120       C\\nATOM   2815  C   CYS A 401      21.440  -1.519 -21.252  1.00170.63           C\\nANISOU 2815  C   CYS A 401    23622  25538  15671    556   3881   -897       C\\nATOM   2816  O   CYS A 401      21.063  -1.243 -20.109  1.00166.40           O\\nANISOU 2816  O   CYS A 401    22893  24541  15789    548   3513   -729       O\\nATOM   2817  CB  CYS A 401      23.624  -2.583 -20.701  1.00179.14           C\\nANISOU 2817  CB  CYS A 401    24079  26891  17096   1410   4598  -1700       C\\nATOM   2818  SG  CYS A 401      25.421  -2.457 -20.478  1.00183.37           S\\nANISOU 2818  SG  CYS A 401    23801  27930  17940   1774   5237  -1908       S\\nATOM   2819  N   ASN A 402      20.597  -1.793 -22.244  1.00163.09           N\\nANISOU 2819  N   ASN A 402    23235  24683  14049    348   3727   -908       N\\nATOM   2820  CA  ASN A 402      19.171  -1.877 -21.964  1.00152.09           C\\nANISOU 2820  CA  ASN A 402    22222  22828  12736    126   3092   -755       C\\nATOM   2821  C   ASN A 402      18.914  -3.031 -21.004  1.00144.87           C\\nANISOU 2821  C   ASN A 402    21476  21352  12215    479   2819  -1242       C\\nATOM   2822  O   ASN A 402      19.334  -4.167 -21.242  1.00148.09           O\\nANISOU 2822  O   ASN A 402    22151  21737  12380    836   2997  -1823       O\\nATOM   2823  CB  ASN A 402      18.364  -2.039 -23.255  1.00153.00           C\\nANISOU 2823  CB  ASN A 402    22907  23202  12025   -153   2955   -727       C\\nATOM   2824  CG  ASN A 402      18.644  -3.344 -23.970  1.00154.48           C\\nANISOU 2824  CG  ASN A 402    23550  23525  11619    142   3169  -1424       C\\nATOM   2825  OD1 ASN A 402      18.048  -4.376 -23.657  1.00152.23           O\\nANISOU 2825  OD1 ASN A 402    23645  22801  11394    294   2842  -1846       O\\nATOM   2826  ND2 ASN A 402      19.540  -3.303 -24.949  1.00156.47           N\\nANISOU 2826  ND2 ASN A 402    23784  24383  11285    209   3730  -1554       N\\nATOM   2827  N   ILE A 403      18.259  -2.719 -19.893  1.00137.95           N\\nANISOU 2827  N   ILE A 403    20445  20015  11956    389   2403   -999       N\\nATOM   2828  CA  ILE A 403      18.056  -3.664 -18.801  1.00126.08           C\\nANISOU 2828  CA  ILE A 403    19041  17968  10897    679   2150  -1342       C\\nATOM   2829  C   ILE A 403      16.725  -4.370 -19.025  1.00123.67           C\\nANISOU 2829  C   ILE A 403    19300  17348  10341    476   1691  -1463       C\\nATOM   2830  O   ILE A 403      15.774  -3.737 -19.506  1.00123.23           O\\nANISOU 2830  O   ILE A 403    19345  17396  10082     73   1419  -1099       O\\nATOM   2831  CB  ILE A 403      18.121  -2.936 -17.448  1.00116.57           C\\nANISOU 2831  CB  ILE A 403    17344  16498  10450    680   1990  -1029       C\\nATOM   2832  CG1 ILE A 403      19.571  -2.545 -17.154  1.00117.76           C\\nANISOU 2832  CG1 ILE A 403    16950  16923  10871    944   2430  -1064       C\\nATOM   2833  CG2 ILE A 403      17.524  -3.771 -16.324  1.00111.83           C\\nANISOU 2833  CG2 ILE A 403    16927  15326  10238    834   1619  -1235       C\\nATOM   2834  CD1 ILE A 403      19.744  -1.682 -15.938  1.00115.05           C\\nANISOU 2834  CD1 ILE A 403    16103  16396  11214    903   2293   -760       C\\nATOM   2835  N   PRO A 404      16.628  -5.671 -18.745  1.00118.90           N\\nANISOU 2835  N   PRO A 404    19074  16363   9738    731   1581  -1960       N\\nATOM   2836  CA  PRO A 404      15.360  -6.387 -18.918  1.00118.90           C\\nANISOU 2836  CA  PRO A 404    19598  16036   9542    479   1130  -2089       C\\nATOM   2837  C   PRO A 404      14.199  -5.600 -18.342  1.00114.46           C\\nANISOU 2837  C   PRO A 404    18849  15327   9312     80    700  -1589       C\\nATOM   2838  O   PRO A 404      14.149  -5.345 -17.130  1.00111.06           O\\nANISOU 2838  O   PRO A 404    18106  14611   9479    144    589  -1414       O\\nATOM   2839  CB  PRO A 404      15.590  -7.690 -18.142  1.00118.42           C\\nANISOU 2839  CB  PRO A 404    19799  15435   9759    841   1069  -2563       C\\nATOM   2840  CG  PRO A 404      17.050  -7.938 -18.305  1.00121.83           C\\nANISOU 2840  CG  PRO A 404    20054  16085  10152   1347   1569  -2883       C\\nATOM   2841  CD  PRO A 404      17.718  -6.580 -18.344  1.00119.79           C\\nANISOU 2841  CD  PRO A 404    19169  16331  10014   1271   1867  -2444       C\\nATOM   2842  N   PRO A 405      13.257  -5.175 -19.187  1.00111.48           N\\nANISOU 2842  N   PRO A 405    18639  15168   8549   -316    448  -1354       N\\nATOM   2843  CA  PRO A 405      12.126  -4.381 -18.686  1.00109.02           C\\nANISOU 2843  CA  PRO A 405    18100  14751   8571   -653     36   -886       C\\nATOM   2844  C   PRO A 405      11.320  -5.093 -17.621  1.00107.40           C\\nANISOU 2844  C   PRO A 405    17974  14039   8792   -700   -301  -1012       C\\nATOM   2845  O   PRO A 405      10.656  -4.425 -16.820  1.00106.74           O\\nANISOU 2845  O   PRO A 405    17562  13840   9155   -851   -528   -666       O\\nATOM   2846  CB  PRO A 405      11.292  -4.119 -19.948  1.00110.35           C\\nANISOU 2846  CB  PRO A 405    18539  15248   8141  -1009   -207   -731       C\\nATOM   2847  CG  PRO A 405      11.691  -5.197 -20.899  1.00113.76           C\\nANISOU 2847  CG  PRO A 405    19491  15789   7942   -900    -38  -1264       C\\nATOM   2848  CD  PRO A 405      13.141  -5.456 -20.627  1.00117.16           C\\nANISOU 2848  CD  PRO A 405    19780  16246   8490   -452    496  -1536       C\\nATOM   2849  N   VAL A 406      11.356  -6.428 -17.580  1.00111.87           N\\nANISOU 2849  N   VAL A 406    18978  14290   9236   -579   -329  -1496       N\\nATOM   2850  CA  VAL A 406      10.738  -7.139 -16.469  1.00102.56           C\\nANISOU 2850  CA  VAL A 406    17881  12600   8486   -624   -592  -1581       C\\nATOM   2851  C   VAL A 406      11.508  -6.882 -15.181  1.00104.10           C\\nANISOU 2851  C   VAL A 406    17697  12610   9246   -300   -398  -1479       C\\nATOM   2852  O   VAL A 406      10.926  -6.894 -14.090  1.00102.17           O\\nANISOU 2852  O   VAL A 406    17313  12081   9424   -395   -602  -1324       O\\nATOM   2853  CB  VAL A 406      10.640  -8.644 -16.776  1.00 94.49           C\\nANISOU 2853  CB  VAL A 406    17480  11217   7203   -584   -680  -2114       C\\nATOM   2854  N   LEU A 407      12.818  -6.639 -15.277  1.00103.82           N\\nANISOU 2854  N   LEU A 407    17468  12769   9209     74     -3  -1567       N\\nATOM   2855  CA  LEU A 407      13.592  -6.296 -14.089  1.00100.38           C\\nANISOU 2855  CA  LEU A 407    16623  12220   9296    369    146  -1462       C\\nATOM   2856  C   LEU A 407      13.390  -4.838 -13.698  1.00 94.26           C\\nANISOU 2856  C   LEU A 407    15315  11675   8824    182    114   -975       C\\nATOM   2857  O   LEU A 407      13.200  -4.533 -12.516  1.00 88.29           O\\nANISOU 2857  O   LEU A 407    14299  10718   8529    200     -8   -812       O\\nATOM   2858  CB  LEU A 407      15.077  -6.584 -14.317  1.00101.90           C\\nANISOU 2858  CB  LEU A 407    16737  12562   9418    837    561  -1755       C\\nATOM   2859  N   TYR A 408      13.370  -3.956 -14.650  1.00 94.06           N\\nANISOU 2859  N   TYR A 408    15152  12055   8531      5    218   -738       N\\nATOM   2860  CA  TYR A 408      13.143  -2.599 -14.299  1.00 92.67           C\\nANISOU 2860  CA  TYR A 408    14536  12021   8655   -189    141   -264       C\\nATOM   2861  C   TYR A 408      11.764  -2.493 -13.713  1.00 95.64           C\\nANISOU 2861  C   TYR A 408    14901  12179   9258   -462   -278    -65       C\\nATOM   2862  O   TYR A 408      11.578  -1.795 -12.766  1.00 92.85           O\\nANISOU 2862  O   TYR A 408    14175  11751   9352   -489   -366    194       O\\nATOM   2863  CB  TYR A 408      13.263  -1.746 -15.521  1.00 92.66           C\\nANISOU 2863  CB  TYR A 408    14496  12449   8263   -369    283     -7       C\\nATOM   2864  CG  TYR A 408      13.909  -0.444 -15.274  1.00 92.93           C\\nANISOU 2864  CG  TYR A 408    14043  12651   8617   -377    472    359       C\\nATOM   2865  CD1 TYR A 408      13.694   0.227 -14.129  1.00 88.51           C\\nANISOU 2865  CD1 TYR A 408    13122  11858   8651   -379    316    564       C\\nATOM   2866  CD2 TYR A 408      14.725   0.122 -16.199  1.00 98.66           C\\nANISOU 2866  CD2 TYR A 408    14681  13767   9040   -406    819    487       C\\nATOM   2867  CE1 TYR A 408      14.287   1.434 -13.904  1.00 87.26           C\\nANISOU 2867  CE1 TYR A 408    12549  11797   8809   -413    462    866       C\\nATOM   2868  CE2 TYR A 408      15.323   1.331 -15.973  1.00 98.99           C\\nANISOU 2868  CE2 TYR A 408    14288  13921   9401   -474    985    837       C\\nATOM   2869  CZ  TYR A 408      15.086   1.974 -14.814  1.00 95.40           C\\nANISOU 2869  CZ  TYR A 408    13502  13174   9570   -479    786   1014       C\\nATOM   2870  OH  TYR A 408      15.640   3.178 -14.533  1.00 98.94           O\\nANISOU 2870  OH  TYR A 408    13550  13681  10361   -572    923   1329       O\\nATOM   2871  N   SER A 409      10.781  -3.173 -14.278  1.00105.38           N\\nANISOU 2871  N   SER A 409    16521  13320  10198   -667   -536   -211       N\\nATOM   2872  CA  SER A 409       9.431  -3.119 -13.727  1.00100.18           C\\nANISOU 2872  CA  SER A 409    15802  12496   9765   -940   -916    -53       C\\nATOM   2873  C   SER A 409       9.363  -3.750 -12.341  1.00 91.59           C\\nANISOU 2873  C   SER A 409    14684  11035   9081   -825   -948   -193       C\\nATOM   2874  O   SER A 409       8.543  -3.336 -11.513  1.00 85.61           O\\nANISOU 2874  O   SER A 409    13671  10195   8661   -967  -1137      4       O\\nATOM   2875  CB  SER A 409       8.447  -3.811 -14.672  1.00102.06           C\\nANISOU 2875  CB  SER A 409    16434  12778   9567  -1245  -1202   -175       C\\nATOM   2876  OG  SER A 409       8.493  -3.239 -15.967  1.00105.65           O\\nANISOU 2876  OG  SER A 409    16956  13611   9576  -1354  -1197    -26       O\\nATOM   2877  N   ALA A 410      10.216  -4.740 -12.069  1.00 90.76           N\\nANISOU 2877  N   ALA A 410    14837  10715   8935   -552   -765   -524       N\\nATOM   2878  CA  ALA A 410      10.196  -5.405 -10.769  1.00 84.55           C\\nANISOU 2878  CA  ALA A 410    14089   9558   8478   -436   -813   -622       C\\nATOM   2879  C   ALA A 410      10.716  -4.488  -9.669  1.00 85.46           C\\nANISOU 2879  C   ALA A 410    13726   9716   9028   -244   -702   -420       C\\nATOM   2880  O   ALA A 410      10.097  -4.365  -8.607  1.00 76.26           O\\nANISOU 2880  O   ALA A 410    12411   8410   8155   -337   -841   -294       O\\nATOM   2881  CB  ALA A 410      11.018  -6.693 -10.829  1.00 79.54           C\\nANISOU 2881  CB  ALA A 410    13883   8649   7690   -141   -680  -1016       C\\nATOM   2882  N   PHE A 411      11.858  -3.837  -9.904  1.00 82.88           N\\nANISOU 2882  N   PHE A 411    13149   9606   8736      5   -442   -403       N\\nATOM   2883  CA  PHE A 411      12.446  -2.977  -8.883  1.00 81.51           C\\nANISOU 2883  CA  PHE A 411    12529   9464   8975    175   -355   -259       C\\nATOM   2884  C   PHE A 411      11.593  -1.745  -8.614  1.00 76.95           C\\nANISOU 2884  C   PHE A 411    11608   8991   8637    -75   -511     73       C\\nATOM   2885  O   PHE A 411      11.658  -1.179  -7.516  1.00 76.38           O\\nANISOU 2885  O   PHE A 411    11240   8854   8929      0   -536    155       O\\nATOM   2886  CB  PHE A 411      13.859  -2.567  -9.293  1.00 88.89           C\\nANISOU 2886  CB  PHE A 411    13244  10633   9898    438    -44   -321       C\\nATOM   2887  CG  PHE A 411      14.856  -3.688  -9.233  1.00 94.35           C\\nANISOU 2887  CG  PHE A 411    14147  11212  10488    811    121   -674       C\\nATOM   2888  CD1 PHE A 411      14.562  -4.860  -8.555  1.00 93.62           C\\nANISOU 2888  CD1 PHE A 411    14407  10746  10418    926    -36   -865       C\\nATOM   2889  CD2 PHE A 411      16.092  -3.568  -9.846  1.00 94.90           C\\nANISOU 2889  CD2 PHE A 411    14052  11548  10457   1055    438   -805       C\\nATOM   2890  CE1 PHE A 411      15.480  -5.891  -8.497  1.00 91.66           C\\nANISOU 2890  CE1 PHE A 411    14375  10339  10112   1324     82  -1184       C\\nATOM   2891  CE2 PHE A 411      17.013  -4.595  -9.790  1.00 91.21           C\\nANISOU 2891  CE2 PHE A 411    13738  10988   9931   1464    585  -1156       C\\nATOM   2892  CZ  PHE A 411      16.707  -5.757  -9.115  1.00 90.35           C\\nANISOU 2892  CZ  PHE A 411    14011  10453   9865   1623    389  -1349       C\\nATOM   2893  N   THR A 412      10.799  -1.310  -9.596  1.00 86.37           N\\nANISOU 2893  N   THR A 412    12841  10347   9628   -346   -634    251       N\\nATOM   2894  CA  THR A 412       9.854  -0.225  -9.353  1.00 83.78           C\\nANISOU 2894  CA  THR A 412    12208  10075   9551   -541   -831    553       C\\nATOM   2895  C   THR A 412       8.712  -0.693  -8.459  1.00 78.58           C\\nANISOU 2895  C   THR A 412    11565   9242   9050   -678  -1053    522       C\\nATOM   2896  O   THR A 412       8.335  -0.005  -7.503  1.00 75.36           O\\nANISOU 2896  O   THR A 412    10841   8797   8997   -662  -1111    634       O\\nATOM   2897  CB  THR A 412       9.310   0.315 -10.677  1.00 83.99           C\\nANISOU 2897  CB  THR A 412    12287  10328   9297   -765   -948    775       C\\nATOM   2898  OG1 THR A 412      10.397   0.624 -11.557  1.00 88.79           O\\nANISOU 2898  OG1 THR A 412    12926  11134   9675   -676   -690    805       O\\nATOM   2899  CG2 THR A 412       8.491   1.578 -10.436  1.00 76.49           C\\nANISOU 2899  CG2 THR A 412    10981   9411   8671   -879  -1149   1106       C\\nATOM   2900  N   TRP A 413       8.148  -1.866  -8.758  1.00 79.97           N\\nANISOU 2900  N   TRP A 413    12110   9314   8961   -831  -1168    357       N\\nATOM   2901  CA  TRP A 413       7.078  -2.406  -7.927  1.00 79.43           C\\nANISOU 2901  CA  TRP A 413    12060   9094   9024  -1024  -1347    342       C\\nATOM   2902  C   TRP A 413       7.576  -2.703  -6.520  1.00 73.46           C\\nANISOU 2902  C   TRP A 413    11258   8138   8517   -819  -1224    254       C\\nATOM   2903  O   TRP A 413       6.853  -2.491  -5.539  1.00 70.81           O\\nANISOU 2903  O   TRP A 413    10714   7782   8407   -915  -1295    340       O\\nATOM   2904  CB  TRP A 413       6.498  -3.667  -8.569  1.00 85.80           C\\nANISOU 2904  CB  TRP A 413    13317   9783   9501  -1268  -1494    166       C\\nATOM   2905  CG  TRP A 413       5.728  -3.398  -9.828  1.00 91.51           C\\nANISOU 2905  CG  TRP A 413    14070  10739   9962  -1534  -1703    261       C\\nATOM   2906  CD1 TRP A 413       5.242  -2.195 -10.250  1.00 85.59           C\\nANISOU 2906  CD1 TRP A 413    12966  10256   9299  -1598  -1823    542       C\\nATOM   2907  CD2 TRP A 413       5.358  -4.354 -10.833  1.00 96.72           C\\nANISOU 2907  CD2 TRP A 413    15160  11373  10216  -1760  -1855     72       C\\nATOM   2908  NE1 TRP A 413       4.589  -2.343 -11.449  1.00 88.41           N\\nANISOU 2908  NE1 TRP A 413    13492  10790   9309  -1846  -2056    571       N\\nATOM   2909  CE2 TRP A 413       4.646  -3.658 -11.829  1.00 95.02           C\\nANISOU 2909  CE2 TRP A 413    14808  11468   9826  -1963  -2077    265       C\\nATOM   2910  CE3 TRP A 413       5.558  -5.731 -10.985  1.00100.43           C\\nANISOU 2910  CE3 TRP A 413    16143  11559  10456  -1802  -1850   -252       C\\nATOM   2911  CZ2 TRP A 413       4.135  -4.290 -12.963  1.00 98.69           C\\nANISOU 2911  CZ2 TRP A 413    15618  12022   9858  -2226  -2299    130       C\\nATOM   2912  CZ3 TRP A 413       5.049  -6.356 -12.111  1.00103.40           C\\nANISOU 2912  CZ3 TRP A 413    16876  11980  10432  -2067  -2053   -417       C\\nATOM   2913  CH2 TRP A 413       4.347  -5.636 -13.085  1.00102.66           C\\nANISOU 2913  CH2 TRP A 413    16621  12251  10133  -2286  -2277   -233       C\\nATOM   2914  N   LEU A 414       8.817  -3.184  -6.402  1.00 75.32           N\\nANISOU 2914  N   LEU A 414    11667   8256   8695   -521  -1041     79       N\\nATOM   2915  CA  LEU A 414       9.384  -3.467  -5.087  1.00 69.21           C\\nANISOU 2915  CA  LEU A 414    10863   7310   8123   -291   -967     10       C\\nATOM   2916  C   LEU A 414       9.434  -2.210  -4.226  1.00 77.59           C\\nANISOU 2916  C   LEU A 414    11447   8517   9516   -215   -939    159       C\\nATOM   2917  O   LEU A 414       9.179  -2.265  -3.016  1.00 79.71           O\\nANISOU 2917  O   LEU A 414    11637   8710   9938   -194   -969    169       O\\nATOM   2918  CB  LEU A 414      10.778  -4.078  -5.238  1.00 67.92           C\\nANISOU 2918  CB  LEU A 414    10893   7049   7867     71   -800   -201       C\\nATOM   2919  CG  LEU A 414      11.552  -4.368  -3.947  1.00 71.97           C\\nANISOU 2919  CG  LEU A 414    11370   7408   8567    375   -760   -268       C\\nATOM   2920  CD1 LEU A 414      10.756  -5.279  -3.035  1.00 56.68           C\\nANISOU 2920  CD1 LEU A 414     9726   5197   6611    226   -906   -242       C\\nATOM   2921  CD2 LEU A 414      12.904  -4.980  -4.260  1.00 76.87           C\\nANISOU 2921  CD2 LEU A 414    12133   7966   9108    768   -617   -490       C\\nATOM   2922  N   GLY A 415       9.747  -1.065  -4.832  1.00 76.07           N\\nANISOU 2922  N   GLY A 415    10960   8524   9421   -187   -885    275       N\\nATOM   2923  CA  GLY A 415       9.745   0.179  -4.081  1.00 72.96           C\\nANISOU 2923  CA  GLY A 415    10144   8207   9369   -132   -886    390       C\\nATOM   2924  C   GLY A 415       8.357   0.581  -3.618  1.00 74.19           C\\nANISOU 2924  C   GLY A 415    10131   8394   9665   -339  -1044    507       C\\nATOM   2925  O   GLY A 415       8.180   1.043  -2.488  1.00 75.00           O\\nANISOU 2925  O   GLY A 415    10010   8487   9999   -269  -1044    489       O\\nATOM   2926  N   TYR A 416       7.355   0.423  -4.485  1.00 71.29           N\\nANISOU 2926  N   TYR A 416     9841   8097   9148   -588  -1184    609       N\\nATOM   2927  CA  TYR A 416       5.978   0.695  -4.089  1.00 65.72           C\\nANISOU 2927  CA  TYR A 416     8925   7466   8580   -782  -1337    704       C\\nATOM   2928  C   TYR A 416       5.494  -0.288  -3.030  1.00 74.23           C\\nANISOU 2928  C   TYR A 416    10136   8452   9617   -880  -1320    595       C\\nATOM   2929  O   TYR A 416       4.629   0.058  -2.215  1.00 72.94           O\\nANISOU 2929  O   TYR A 416     9706   8378   9627   -957  -1345    631       O\\nATOM   2930  CB  TYR A 416       5.065   0.646  -5.312  1.00 62.97           C\\nANISOU 2930  CB  TYR A 416     8626   7243   8059  -1034  -1533    831       C\\nATOM   2931  CG  TYR A 416       5.257   1.800  -6.266  1.00 72.57           C\\nANISOU 2931  CG  TYR A 416     9671   8573   9328   -975  -1592   1030       C\\nATOM   2932  CD1 TYR A 416       5.334   3.107  -5.802  1.00 77.77           C\\nANISOU 2932  CD1 TYR A 416     9966   9229  10353   -816  -1582   1149       C\\nATOM   2933  CD2 TYR A 416       5.362   1.584  -7.633  1.00 70.98           C\\nANISOU 2933  CD2 TYR A 416     9709   8467   8795  -1089  -1663   1103       C\\nATOM   2934  CE1 TYR A 416       5.505   4.166  -6.675  1.00 81.18           C\\nANISOU 2934  CE1 TYR A 416    10288   9707  10852   -788  -1652   1381       C\\nATOM   2935  CE2 TYR A 416       5.537   2.637  -8.513  1.00 78.84           C\\nANISOU 2935  CE2 TYR A 416    10587   9572   9796  -1063  -1716   1345       C\\nATOM   2936  CZ  TYR A 416       5.608   3.925  -8.030  1.00 78.01           C\\nANISOU 2936  CZ  TYR A 416    10131   9419  10091   -919  -1715   1507       C\\nATOM   2937  OH  TYR A 416       5.781   4.974  -8.906  1.00 66.59           O\\nANISOU 2937  OH  TYR A 416     8612   8022   8665   -917  -1783   1795       O\\nATOM   2938  N   VAL A 417       6.036  -1.510  -3.031  1.00 75.00           N\\nANISOU 2938  N   VAL A 417    10650   8367   9481   -873  -1268    468       N\\nATOM   2939  CA  VAL A 417       5.682  -2.503  -2.019  1.00 75.22           C\\nANISOU 2939  CA  VAL A 417    10882   8250   9450   -979  -1253    416       C\\nATOM   2940  C   VAL A 417       6.049  -2.017  -0.621  1.00 75.65           C\\nANISOU 2940  C   VAL A 417    10726   8332   9686   -769  -1144    400       C\\nATOM   2941  O   VAL A 417       5.383  -2.367   0.363  1.00 73.28           O\\nANISOU 2941  O   VAL A 417    10419   8044   9381   -909  -1125    429       O\\nATOM   2942  CB  VAL A 417       6.357  -3.847  -2.359  1.00 69.42           C\\nANISOU 2942  CB  VAL A 417    10679   7234   8461   -938  -1241    282       C\\nATOM   2943  CG1 VAL A 417       6.474  -4.740  -1.133  1.00 66.88           C\\nANISOU 2943  CG1 VAL A 417    10605   6693   8112   -911  -1204    262       C\\nATOM   2944  CG2 VAL A 417       5.575  -4.550  -3.446  1.00 68.97           C\\nANISOU 2944  CG2 VAL A 417    10878   7133   8193  -1268  -1387    262       C\\nATOM   2945  N   ASN A 418       7.086  -1.184  -0.510  1.00 69.14           N\\nANISOU 2945  N   ASN A 418     9719   7544   9007   -464  -1071    354       N\\nATOM   2946  CA  ASN A 418       7.506  -0.674   0.790  1.00 59.69           C\\nANISOU 2946  CA  ASN A 418     8331   6385   7962   -263  -1004    296       C\\nATOM   2947  C   ASN A 418       6.365   0.000   1.544  1.00 72.46           C\\nANISOU 2947  C   ASN A 418     9629   8176   9728   -397  -1007    338       C\\nATOM   2948  O   ASN A 418       6.372   0.033   2.780  1.00 78.40           O\\nANISOU 2948  O   ASN A 418    10330   8974  10483   -321   -946    277       O\\nATOM   2949  CB  ASN A 418       8.666   0.302   0.607  1.00 65.48           C\\nANISOU 2949  CB  ASN A 418     8842   7154   8882      6   -958    240       C\\nATOM   2950  CG  ASN A 418       9.105   0.938   1.907  1.00 70.06           C\\nANISOU 2950  CG  ASN A 418     9208   7784   9627    195   -932    141       C\\nATOM   2951  OD1 ASN A 418       9.915   0.373   2.644  1.00 72.31           O\\nANISOU 2951  OD1 ASN A 418     9648   8008   9820    376   -923     50       O\\nATOM   2952  ND2 ASN A 418       8.575   2.123   2.197  1.00 73.88           N\\nANISOU 2952  ND2 ASN A 418     9344   8372  10354    175   -946    143       N\\nATOM   2953  N   SER A 419       5.371   0.528   0.828  1.00 73.71           N\\nANISOU 2953  N   SER A 419     9563   8456   9988   -577  -1081    433       N\\nATOM   2954  CA  SER A 419       4.257   1.208   1.479  1.00 74.87           C\\nANISOU 2954  CA  SER A 419     9342   8795  10311   -653  -1075    444       C\\nATOM   2955  C   SER A 419       3.387   0.269   2.304  1.00 71.13           C\\nANISOU 2955  C   SER A 419     8963   8398   9665   -899  -1010    455       C\\nATOM   2956  O   SER A 419       2.578   0.748   3.105  1.00 79.35           O\\nANISOU 2956  O   SER A 419     9691   9646  10814   -930   -935    423       O\\nATOM   2957  CB  SER A 419       3.402   1.927   0.433  1.00 76.98           C\\nANISOU 2957  CB  SER A 419     9339   9174  10737   -757  -1215    564       C\\nATOM   2958  OG  SER A 419       4.102   3.028  -0.124  1.00 76.00           O\\nANISOU 2958  OG  SER A 419     9078   8985  10813   -542  -1256    597       O\\nATOM   2959  N   ALA A 420       3.532  -1.043   2.146  1.00 64.52           N\\nANISOU 2959  N   ALA A 420     8553   7392   8567  -1076  -1023    494       N\\nATOM   2960  CA  ALA A 420       2.711  -1.998   2.873  1.00 70.62           C\\nANISOU 2960  CA  ALA A 420     9465   8194   9173  -1382   -964    556       C\\nATOM   2961  C   ALA A 420       3.486  -2.802   3.908  1.00 76.87           C\\nANISOU 2961  C   ALA A 420    10638   8808   9762  -1279   -878    546       C\\nATOM   2962  O   ALA A 420       2.886  -3.634   4.598  1.00 79.00           O\\nANISOU 2962  O   ALA A 420    11085   9071   9862  -1550   -815    643       O\\nATOM   2963  CB  ALA A 420       2.026  -2.954   1.892  1.00 69.09           C\\nANISOU 2963  CB  ALA A 420     9496   7901   8853  -1760  -1092    637       C\\nATOM   2964  N   VAL A 421       4.793  -2.590   4.035  1.00 77.91           N\\nANISOU 2964  N   VAL A 421    10893   8806   9904   -910   -888    455       N\\nATOM   2965  CA  VAL A 421       5.579  -3.412   4.946  1.00 79.27           C\\nANISOU 2965  CA  VAL A 421    11443   8799   9879   -770   -869    464       C\\nATOM   2966  C   VAL A 421       5.680  -2.792   6.335  1.00 78.59           C\\nANISOU 2966  C   VAL A 421    11159   8929   9775   -616   -776    415       C\\nATOM   2967  O   VAL A 421       5.844  -3.521   7.319  1.00 80.37           O\\nANISOU 2967  O   VAL A 421    11677   9096   9766   -626   -753    490       O\\nATOM   2968  CB  VAL A 421       6.980  -3.686   4.367  1.00 73.59           C\\nANISOU 2968  CB  VAL A 421    10961   7841   9160   -437   -947    375       C\\nATOM   2969  CG1 VAL A 421       6.871  -4.312   2.991  1.00 71.39           C\\nANISOU 2969  CG1 VAL A 421    10910   7375   8838   -578  -1015    377       C\\nATOM   2970  CG2 VAL A 421       7.810  -2.409   4.324  1.00 65.73           C\\nANISOU 2970  CG2 VAL A 421     9584   7002   8387   -121   -934    246       C\\nATOM   2971  N   ASN A 422       5.581  -1.466   6.440  1.00 74.03           N\\nANISOU 2971  N   ASN A 422    10123   8582   9422   -475   -738    288       N\\nATOM   2972  CA  ASN A 422       5.742  -0.820   7.742  1.00 73.83           C\\nANISOU 2972  CA  ASN A 422     9929   8759   9366   -304   -662    170       C\\nATOM   2973  C   ASN A 422       4.697  -1.265   8.756  1.00 74.68           C\\nANISOU 2973  C   ASN A 422    10063   9076   9236   -564   -510    254       C\\nATOM   2974  O   ASN A 422       5.081  -1.611   9.887  1.00 76.59           O\\nANISOU 2974  O   ASN A 422    10516   9367   9218   -484   -475    261       O\\nATOM   2975  CB  ASN A 422       5.757   0.700   7.560  1.00 72.41           C\\nANISOU 2975  CB  ASN A 422     9279   8717   9517   -120   -663     -7       C\\nATOM   2976  CG  ASN A 422       7.075   1.199   7.026  1.00 70.46           C\\nANISOU 2976  CG  ASN A 422     9018   8305   9448    152   -777    -94       C\\nATOM   2977  OD1 ASN A 422       8.006   0.419   6.829  1.00 69.93           O\\nANISOU 2977  OD1 ASN A 422     9248   8068   9254    251   -842    -54       O\\nATOM   2978  ND2 ASN A 422       7.166   2.500   6.780  1.00 74.23           N\\nANISOU 2978  ND2 ASN A 422     9142   8823  10239    275   -798   -213       N\\nATOM   2979  N   PRO A 423       3.396  -1.299   8.444  1.00 74.98           N\\nANISOU 2979  N   PRO A 423     9889   9275   9326   -884   -418    332       N\\nATOM   2980  CA  PRO A 423       2.439  -1.829   9.431  1.00 79.39           C\\nANISOU 2980  CA  PRO A 423    10466  10068   9629  -1180   -229    435       C\\nATOM   2981  C   PRO A 423       2.722  -3.267   9.832  1.00 83.90           C\\nANISOU 2981  C   PRO A 423    11615  10404   9861  -1378   -249    663       C\\nATOM   2982  O   PRO A 423       2.406  -3.662  10.961  1.00 90.16           O\\nANISOU 2982  O   PRO A 423    12538  11363  10356  -1521    -99    763       O\\nATOM   2983  CB  PRO A 423       1.089  -1.697   8.713  1.00 72.48           C\\nANISOU 2983  CB  PRO A 423     9227   9375   8937  -1503   -180    488       C\\nATOM   2984  CG  PRO A 423       1.299  -0.620   7.719  1.00 68.97           C\\nANISOU 2984  CG  PRO A 423     8463   8890   8854  -1250   -321    353       C\\nATOM   2985  CD  PRO A 423       2.703  -0.792   7.246  1.00 69.67           C\\nANISOU 2985  CD  PRO A 423     8902   8634   8934   -993   -481    335       C\\nATOM   2986  N   ILE A 424       3.313  -4.062   8.939  1.00 83.26           N\\nANISOU 2986  N   ILE A 424    11907   9927   9801  -1380   -427    747       N\\nATOM   2987  CA  ILE A 424       3.682  -5.430   9.285  1.00 83.10           C\\nANISOU 2987  CA  ILE A 424    12489   9580   9504  -1500   -487    952       C\\nATOM   2988  C   ILE A 424       4.819  -5.441  10.300  1.00 81.27           C\\nANISOU 2988  C   ILE A 424    12492   9304   9083  -1119   -542    931       C\\nATOM   2989  O   ILE A 424       4.919  -6.359  11.125  1.00 80.08           O\\nANISOU 2989  O   ILE A 424    12773   9025   8629  -1213   -546   1138       O\\nATOM   2990  CB  ILE A 424       4.040  -6.206   8.002  1.00 78.55           C\\nANISOU 2990  CB  ILE A 424    12237   8582   9027  -1536   -666    971       C\\nATOM   2991  CG1 ILE A 424       2.825  -6.276   7.073  1.00 73.56           C\\nANISOU 2991  CG1 ILE A 424    11398   8028   8524  -1971   -654   1003       C\\nATOM   2992  CG2 ILE A 424       4.560  -7.600   8.325  1.00 80.22           C\\nANISOU 2992  CG2 ILE A 424    13116   8357   9008  -1567   -766   1149       C\\nATOM   2993  CD1 ILE A 424       3.095  -6.975   5.758  1.00 71.89           C\\nANISOU 2993  CD1 ILE A 424    11502   7446   8367  -2028   -834    970       C\\nATOM   2994  N   ILE A 425       5.680  -4.422  10.275  1.00 72.91           N\\nANISOU 2994  N   ILE A 425    11155   8352   8197   -705   -607    699       N\\nATOM   2995  CA  ILE A 425       6.795  -4.363  11.215  1.00 77.19           C\\nANISOU 2995  CA  ILE A 425    11857   8894   8577   -341   -708    646       C\\nATOM   2996  C   ILE A 425       6.320  -3.961  12.608  1.00 86.64           C\\nANISOU 2996  C   ILE A 425    12947  10469   9504   -403   -561    636       C\\nATOM   2997  O   ILE A 425       6.863  -4.432  13.615  1.00 84.58           O\\nANISOU 2997  O   ILE A 425    13008  10207   8921   -280   -633    733       O\\nATOM   2998  CB  ILE A 425       7.877  -3.406  10.689  1.00 71.65           C\\nANISOU 2998  CB  ILE A 425    10863   8188   8172     58   -830    392       C\\nATOM   2999  CG1 ILE A 425       8.343  -3.850   9.303  1.00 71.05           C\\nANISOU 2999  CG1 ILE A 425    10906   7796   8294    111   -926    402       C\\nATOM   3000  CG2 ILE A 425       9.062  -3.360  11.634  1.00 68.37           C\\nANISOU 3000  CG2 ILE A 425    10565   7798   7613    422   -980    318       C\\nATOM   3001  CD1 ILE A 425       9.377  -2.939   8.685  1.00 69.86           C\\nANISOU 3001  CD1 ILE A 425    10448   7667   8427    435  -1000    194       C\\nATOM   3002  N   TYR A 426       5.302  -3.102  12.695  1.00 80.85           N\\nANISOU 3002  N   TYR A 426    11769  10077   8874   -571   -359    514       N\\nATOM   3003  CA  TYR A 426       4.811  -2.668  13.999  1.00 87.40           C\\nANISOU 3003  CA  TYR A 426    12467  11316   9424   -609   -172    444       C\\nATOM   3004  C   TYR A 426       4.159  -3.813  14.767  1.00 95.75           C\\nANISOU 3004  C   TYR A 426    13906  12427  10045   -980    -30    771       C\\nATOM   3005  O   TYR A 426       4.175  -3.815  16.004  1.00 99.16           O\\nANISOU 3005  O   TYR A 426    14463  13130  10085   -961     67    794       O\\nATOM   3006  CB  TYR A 426       3.826  -1.511  13.828  1.00 86.99           C\\nANISOU 3006  CB  TYR A 426    11825  11596   9630   -664     22    214       C\\nATOM   3007  CG  TYR A 426       4.370  -0.345  13.027  1.00 85.70           C\\nANISOU 3007  CG  TYR A 426    11311  11332   9920   -350   -120    -55       C\\nATOM   3008  CD1 TYR A 426       5.706   0.027  13.118  1.00 83.30           C\\nANISOU 3008  CD1 TYR A 426    11097  10869   9684      2   -327   -201       C\\nATOM   3009  CD2 TYR A 426       3.547   0.381  12.176  1.00 83.93           C\\nANISOU 3009  CD2 TYR A 426    10656  11172  10061   -422    -61   -137       C\\nATOM   3010  CE1 TYR A 426       6.206   1.093  12.385  1.00 79.72           C\\nANISOU 3010  CE1 TYR A 426    10330  10311   9648    224   -438   -408       C\\nATOM   3011  CE2 TYR A 426       4.037   1.447  11.441  1.00 82.37           C\\nANISOU 3011  CE2 TYR A 426    10186  10845  10265   -163   -196   -323       C\\nATOM   3012  CZ  TYR A 426       5.368   1.799  11.548  1.00 77.29           C\\nANISOU 3012  CZ  TYR A 426     9656  10030   9679    135   -368   -452       C\\nATOM   3013  OH  TYR A 426       5.859   2.858  10.815  1.00 65.48           O\\nANISOU 3013  OH  TYR A 426     7898   8395   8588    330   -485   -601       O\\nATOM   3014  N   THR A 427       3.583  -4.790  14.059  1.00 94.12           N\\nANISOU 3014  N   THR A 427    13912  11967   9880  -1346    -21   1029       N\\nATOM   3015  CA  THR A 427       2.981  -5.936  14.735  1.00 94.73           C\\nANISOU 3015  CA  THR A 427    14395  12024   9574  -1766    104   1385       C\\nATOM   3016  C   THR A 427       4.036  -6.873  15.301  1.00 93.77           C\\nANISOU 3016  C   THR A 427    14923  11553   9151  -1581   -115   1608       C\\nATOM   3017  O   THR A 427       3.779  -7.565  16.293  1.00107.23           O\\nANISOU 3017  O   THR A 427    16989  13325  10429  -1808    -22   1896       O\\nATOM   3018  CB  THR A 427       2.076  -6.711  13.777  1.00 92.02           C\\nANISOU 3018  CB  THR A 427    14101  11462   9402  -2246    135   1572       C\\nATOM   3019  OG1 THR A 427       2.869  -7.267  12.722  1.00 87.69           O\\nANISOU 3019  OG1 THR A 427    13873  10378   9067  -2083   -148   1577       O\\nATOM   3020  CG2 THR A 427       1.028  -5.801  13.182  1.00 92.49           C\\nANISOU 3020  CG2 THR A 427    13488  11881   9771  -2397    298   1371       C\\nATOM   3021  N   THR A 428       5.216  -6.918  14.687  1.00 86.78           N\\nANISOU 3021  N   THR A 428    14188  10309   8477  -1167   -404   1497       N\\nATOM   3022  CA  THR A 428       6.250  -7.850  15.112  1.00 80.90           C\\nANISOU 3022  CA  THR A 428    14030   9197   7512   -924   -656   1699       C\\nATOM   3023  C   THR A 428       7.087  -7.298  16.260  1.00 88.26           C\\nANISOU 3023  C   THR A 428    14945  10410   8178   -536   -758   1595       C\\nATOM   3024  O   THR A 428       7.228  -7.954  17.297  1.00 98.04           O\\nANISOU 3024  O   THR A 428    16618  11653   8981   -567   -810   1867       O\\nATOM   3025  CB  THR A 428       7.162  -8.200  13.934  1.00 75.14           C\\nANISOU 3025  CB  THR A 428    13433   7992   7124   -626   -905   1599       C\\nATOM   3026  OG1 THR A 428       6.369  -8.438  12.764  1.00 66.95           O\\nANISOU 3026  OG1 THR A 428    12310   6784   6344   -965   -819   1592       O\\nATOM   3027  CG2 THR A 428       7.977  -9.450  14.258  1.00 74.10           C\\nANISOU 3027  CG2 THR A 428    13971   7385   6798   -439  -1156   1861       C\\nATOM   3028  N   PHE A 429       7.642  -6.097  16.092  1.00 82.80           N\\nANISOU 3028  N   PHE A 429    13778   9948   7733   -194   -807   1216       N\\nATOM   3029  CA  PHE A 429       8.628  -5.569  17.024  1.00 85.65           C\\nANISOU 3029  CA  PHE A 429    14115  10520   7909    205   -988   1057       C\\nATOM   3030  C   PHE A 429       8.031  -4.731  18.145  1.00 88.27           C\\nANISOU 3030  C   PHE A 429    14208  11398   7933    109   -780    904       C\\nATOM   3031  O   PHE A 429       8.759  -4.373  19.077  1.00 94.52           O\\nANISOU 3031  O   PHE A 429    15046  12401   8467    386   -940    780       O\\nATOM   3032  CB  PHE A 429       9.666  -4.731  16.274  1.00 81.51           C\\nANISOU 3032  CB  PHE A 429    13220   9923   7826    606  -1176    717       C\\nATOM   3033  CG  PHE A 429      10.610  -5.545  15.451  1.00 86.84           C\\nANISOU 3033  CG  PHE A 429    14151  10141   8702    848  -1415    814       C\\nATOM   3034  CD1 PHE A 429      11.723  -6.132  16.031  1.00 95.71           C\\nANISOU 3034  CD1 PHE A 429    15590  11131   9647   1208  -1714    909       C\\nATOM   3035  CD2 PHE A 429      10.383  -5.736  14.099  1.00 90.50           C\\nANISOU 3035  CD2 PHE A 429    14539  10330   9515    740  -1348    797       C\\nATOM   3036  CE1 PHE A 429      12.597  -6.891  15.275  1.00100.77           C\\nANISOU 3036  CE1 PHE A 429    16434  11359  10493   1488  -1918    962       C\\nATOM   3037  CE2 PHE A 429      11.253  -6.492  13.334  1.00 94.15           C\\nANISOU 3037  CE2 PHE A 429    15239  10395  10137    990  -1533    835       C\\nATOM   3038  CZ  PHE A 429      12.362  -7.070  13.923  1.00 99.97           C\\nANISOU 3038  CZ  PHE A 429    16261  10992  10733   1381  -1805    907       C\\nATOM   3039  N   ASN A 430       6.743  -4.409  18.090  1.00 83.72           N\\nANISOU 3039  N   ASN A 430    13363  11080   7368   -257   -438    882       N\\nATOM   3040  CA  ASN A 430       6.116  -3.571  19.103  1.00 88.98           C\\nANISOU 3040  CA  ASN A 430    13756  12293   7759   -315   -190    673       C\\nATOM   3041  C   ASN A 430       4.910  -4.295  19.678  1.00 94.26           C\\nANISOU 3041  C   ASN A 430    14603  13185   8026   -804    139    994       C\\nATOM   3042  O   ASN A 430       3.949  -4.578  18.954  1.00 90.37           O\\nANISOU 3042  O   ASN A 430    13952  12628   7755  -1162    332   1116       O\\nATOM   3043  CB  ASN A 430       5.708  -2.218  18.523  1.00 82.34           C\\nANISOU 3043  CB  ASN A 430    12274  11632   7378   -219    -60    251       C\\nATOM   3044  CG  ASN A 430       5.177  -1.278  19.577  1.00 86.94           C\\nANISOU 3044  CG  ASN A 430    12575  12746   7711   -183    175    -57       C\\nATOM   3045  OD1 ASN A 430       3.978  -1.247  19.844  1.00 86.57           O\\nANISOU 3045  OD1 ASN A 430    12339  13023   7531   -474    525    -28       O\\nATOM   3046  ND2 ASN A 430       6.069  -0.510  20.193  1.00 93.49           N\\nANISOU 3046  ND2 ASN A 430    13362  13689   8473    174    -14   -380       N\\nATOM   3047  N   ILE A 431       4.963  -4.590  20.979  1.00 96.66           N\\nANISOU 3047  N   ILE A 431    15226  13779   7721   -842    197   1137       N\\nATOM   3048  CA  ILE A 431       3.848  -5.262  21.638  1.00 92.58           C\\nANISOU 3048  CA  ILE A 431    14883  13536   6757  -1346    552   1472       C\\nATOM   3049  C   ILE A 431       2.630  -4.348  21.695  1.00 98.55           C\\nANISOU 3049  C   ILE A 431    15013  14819   7614  -1537    984   1175       C\\nATOM   3050  O   ILE A 431       1.488  -4.806  21.569  1.00 98.81           O\\nANISOU 3050  O   ILE A 431    14936  14997   7611  -2018   1303   1397       O\\nATOM   3051  CB  ILE A 431       4.263  -5.738  23.042  1.00 91.00           C\\nANISOU 3051  CB  ILE A 431    15200  13558   5818  -1318    503   1710       C\\nATOM   3052  N   GLU A 432       2.851  -3.043  21.881  1.00 96.20           N\\nANISOU 3052  N   GLU A 432    14279  14803   7470  -1163    992    657       N\\nATOM   3053  CA  GLU A 432       1.733  -2.109  21.979  1.00 93.30           C\\nANISOU 3053  CA  GLU A 432    13305  14920   7225  -1248   1385    325       C\\nATOM   3054  C   GLU A 432       1.005  -1.971  20.646  1.00 90.82           C\\nANISOU 3054  C   GLU A 432    12560  14400   7549  -1408   1437    316       C\\nATOM   3055  O   GLU A 432      -0.230  -1.927  20.610  1.00 84.30           O\\nANISOU 3055  O   GLU A 432    11363  13912   6757  -1725   1791    333       O\\nATOM   3056  CB  GLU A 432       2.229  -0.750  22.471  1.00 88.42           C\\nANISOU 3056  CB  GLU A 432    12394  14544   6659   -774   1324   -250       C\\nATOM   3057  N   PHE A 433       1.747  -1.901  19.538  1.00 90.26           N\\nANISOU 3057  N   PHE A 433    12509  13817   7970  -1197   1087    288       N\\nATOM   3058  CA  PHE A 433       1.098  -1.850  18.232  1.00 93.03           C\\nANISOU 3058  CA  PHE A 433    12520  13969   8860  -1363   1090    317       C\\nATOM   3059  C   PHE A 433       0.366  -3.155  17.929  1.00 92.59           C\\nANISOU 3059  C   PHE A 433    12717  13789   8674  -1909   1194    776       C\\nATOM   3060  O   PHE A 433      -0.768  -3.136  17.438  1.00 86.48           O\\nANISOU 3060  O   PHE A 433    11554  13195   8111  -2229   1396    805       O\\nATOM   3061  CB  PHE A 433       2.125  -1.540  17.137  1.00 94.23           C\\nANISOU 3061  CB  PHE A 433    12696  13628   9479  -1036    712    208       C\\nATOM   3062  CG  PHE A 433       2.253  -0.070  16.807  1.00 90.02           C\\nANISOU 3062  CG  PHE A 433    11657  13176   9371   -672    669   -233       C\\nATOM   3063  CD1 PHE A 433       1.220   0.604  16.178  1.00 82.18           C\\nANISOU 3063  CD1 PHE A 433    10137  12335   8753   -746    821   -367       C\\nATOM   3064  CD2 PHE A 433       3.413   0.630  17.106  1.00 88.82           C\\nANISOU 3064  CD2 PHE A 433    11559  12920   9269   -265    446   -498       C\\nATOM   3065  CE1 PHE A 433       1.331   1.949  15.867  1.00 78.56           C\\nANISOU 3065  CE1 PHE A 433     9265  11877   8709   -401    756   -738       C\\nATOM   3066  CE2 PHE A 433       3.531   1.976  16.796  1.00 82.75           C\\nANISOU 3066  CE2 PHE A 433    10368  12155   8919     24    394   -882       C\\nATOM   3067  CZ  PHE A 433       2.487   2.635  16.177  1.00 81.74           C\\nANISOU 3067  CZ  PHE A 433     9768  12128   9161    -34    550   -991       C\\nATOM   3068  N   ARG A 434       0.991  -4.296  18.232  1.00 96.08           N\\nANISOU 3068  N   ARG A 434    13805  13913   8786  -2025   1037   1134       N\\nATOM   3069  CA  ARG A 434       0.385  -5.588  17.918  1.00 91.88           C\\nANISOU 3069  CA  ARG A 434    13600  13146   8164  -2562   1089   1576       C\\nATOM   3070  C   ARG A 434      -0.930  -5.778  18.663  1.00 88.38           C\\nANISOU 3070  C   ARG A 434    12942  13229   7411  -3068   1532   1730       C\\nATOM   3071  O   ARG A 434      -1.944  -6.162  18.068  1.00 89.59           O\\nANISOU 3071  O   ARG A 434    12864  13413   7764  -3530   1674   1870       O\\nATOM   3072  CB  ARG A 434       1.360  -6.718  18.249  1.00 91.99           C\\nANISOU 3072  CB  ARG A 434    14390  12689   7871  -2520    823   1923       C\\nATOM   3073  N   LYS A 435      -0.934  -5.515  19.973  1.00 92.30           N\\nANISOU 3073  N   LYS A 435    13491  14183   7397  -3005   1759   1697       N\\nATOM   3074  CA  LYS A 435      -2.157  -5.679  20.753  1.00 95.80           C\\nANISOU 3074  CA  LYS A 435    13709  15207   7485  -3485   2243   1837       C\\nATOM   3075  C   LYS A 435      -3.199  -4.633  20.385  1.00 95.39           C\\nANISOU 3075  C   LYS A 435    12798  15636   7810  -3466   2525   1447       C\\nATOM   3076  O   LYS A 435      -4.399  -4.865  20.566  1.00100.11           O\\nANISOU 3076  O   LYS A 435    13054  16654   8329  -3942   2904   1572       O\\nATOM   3077  CB  LYS A 435      -1.843  -5.617  22.249  1.00100.45           C\\nANISOU 3077  CB  LYS A 435    14594  16206   7366  -3383   2418   1871       C\\nATOM   3078  N   ALA A 436      -2.763  -3.482  19.869  1.00 97.48           N\\nANISOU 3078  N   ALA A 436    12695  15840   8503  -2926   2339    989       N\\nATOM   3079  CA  ALA A 436      -3.711  -2.457  19.446  1.00 99.12           C\\nANISOU 3079  CA  ALA A 436    12109  16422   9131  -2835   2542    627       C\\nATOM   3080  C   ALA A 436      -4.463  -2.884  18.193  1.00 98.71           C\\nANISOU 3080  C   ALA A 436    11791  16164   9549  -3194   2456    809       C\\nATOM   3081  O   ALA A 436      -5.682  -2.702  18.103  1.00 98.79           O\\nANISOU 3081  O   ALA A 436    11222  16613   9701  -3464   2744    764       O\\nATOM   3082  CB  ALA A 436      -2.984  -1.133  19.210  1.00 94.08           C\\nANISOU 3082  CB  ALA A 436    11230  15675   8839  -2179   2321    134       C\\nATOM   3083  N   PHE A 437      -3.753  -3.456  17.217  1.00 90.64           N\\nANISOU 3083  N   PHE A 437    11168  14510   8763  -3193   2056    991       N\\nATOM   3084  CA  PHE A 437      -4.405  -3.888  15.985  1.00 89.75           C\\nANISOU 3084  CA  PHE A 437    10864  14185   9052  -3536   1925   1136       C\\nATOM   3085  C   PHE A 437      -5.403  -5.004  16.256  1.00 98.61           C\\nANISOU 3085  C   PHE A 437    12055  15479   9935  -4263   2173   1518       C\\nATOM   3086  O   PHE A 437      -6.491  -5.031  15.669  1.00 97.68           O\\nANISOU 3086  O   PHE A 437    11436  15585  10092  -4617   2265   1534       O\\nATOM   3087  CB  PHE A 437      -3.365  -4.353  14.965  1.00 85.17           C\\nANISOU 3087  CB  PHE A 437    10775  12904   8681  -3381   1477   1231       C\\nATOM   3088  CG  PHE A 437      -2.480  -3.255  14.437  1.00 86.40           C\\nANISOU 3088  CG  PHE A 437    10779  12886   9165  -2763   1230    890       C\\nATOM   3089  CD1 PHE A 437      -2.661  -1.937  14.822  1.00 90.40           C\\nANISOU 3089  CD1 PHE A 437    10767  13767   9814  -2388   1365    522       C\\nATOM   3090  CD2 PHE A 437      -1.469  -3.548  13.540  1.00 80.59           C\\nANISOU 3090  CD2 PHE A 437    10422  11598   8603  -2569    873    931       C\\nATOM   3091  CE1 PHE A 437      -1.838  -0.938  14.328  1.00 85.90           C\\nANISOU 3091  CE1 PHE A 437    10090  12981   9568  -1879   1127    241       C\\nATOM   3092  CE2 PHE A 437      -0.645  -2.555  13.044  1.00 80.08           C\\nANISOU 3092  CE2 PHE A 437    10206  11388   8833  -2065    672    655       C\\nATOM   3093  CZ  PHE A 437      -0.831  -1.248  13.438  1.00 81.28           C\\nANISOU 3093  CZ  PHE A 437     9867  11875   9140  -1744    789    329       C\\nATOM   3094  N   LEU A 438      -5.047  -5.938  17.144  1.00 97.43           N\\nANISOU 3094  N   LEU A 438    12520  15222   9276  -4511   2262   1848       N\\nATOM   3095  CA  LEU A 438      -5.930  -7.059  17.446  1.00 99.16           C\\nANISOU 3095  CA  LEU A 438    12887  15540   9250  -5265   2497   2270       C\\nATOM   3096  C   LEU A 438      -7.187  -6.605  18.176  1.00104.88           C\\nANISOU 3096  C   LEU A 438    12926  17091   9832  -5548   3020   2189       C\\nATOM   3097  O   LEU A 438      -8.233  -7.257  18.066  1.00112.28           O\\nANISOU 3097  O   LEU A 438    13646  18228  10786  -6211   3228   2440       O\\nATOM   3098  CB  LEU A 438      -5.179  -8.106  18.269  1.00101.79           C\\nANISOU 3098  CB  LEU A 438    14093  15526   9057  -5410   2445   2676       C\\nATOM   3099  N   LYS A 439      -7.108  -5.501  18.923  1.00104.77           N\\nANISOU 3099  N   LYS A 439    12553  17573   9684  -5064   3242   1817       N\\nATOM   3100  CA  LYS A 439      -8.295  -4.960  19.574  1.00111.86           C\\nANISOU 3100  CA  LYS A 439    12728  19296  10480  -5232   3763   1648       C\\nATOM   3101  C   LYS A 439      -9.200  -4.234  18.588  1.00113.57           C\\nANISOU 3101  C   LYS A 439    12089  19730  11334  -5165   3740   1359       C\\nATOM   3102  O   LYS A 439     -10.419  -4.192  18.788  1.00116.22           O\\nANISOU 3102  O   LYS A 439    11788  20658  11710  -5514   4113   1349       O\\nATOM   3103  CB  LYS A 439      -7.894  -4.019  20.711  1.00111.35           C\\nANISOU 3103  CB  LYS A 439    12602  19665  10042  -4703   3997   1288       C\\nATOM   3104  N   ILE A 440      -8.629  -3.664  17.526  1.00111.11           N\\nANISOU 3104  N   ILE A 440    11741  18958  11519  -4713   3295   1139       N\\nATOM   3105  CA  ILE A 440      -9.451  -3.036  16.502  1.00110.51           C\\nANISOU 3105  CA  ILE A 440    10923  19028  12037  -4650   3192    931       C\\nATOM   3106  C   ILE A 440     -10.182  -4.088  15.675  1.00112.85           C\\nANISOU 3106  C   ILE A 440    11191  19185  12503  -5352   3077   1285       C\\nATOM   3107  O   ILE A 440     -11.326  -3.874  15.259  1.00112.91           O\\nANISOU 3107  O   ILE A 440    10465  19613  12823  -5584   3184   1219       O\\nATOM   3108  CB  ILE A 440      -8.581  -2.115  15.629  1.00104.69           C\\nANISOU 3108  CB  ILE A 440    10219  17834  11725  -3988   2753    640       C\\nATOM   3109  CG1 ILE A 440      -7.927  -1.040  16.500  1.00107.61           C\\nANISOU 3109  CG1 ILE A 440    10580  18352  11953  -3351   2868    257       C\\nATOM   3110  CG2 ILE A 440      -9.411  -1.469  14.537  1.00101.39           C\\nANISOU 3110  CG2 ILE A 440     9088  17539  11896  -3905   2594    477       C\\nATOM   3111  CD1 ILE A 440      -7.131  -0.015  15.728  1.00100.57           C\\nANISOU 3111  CD1 ILE A 440     9658  17052  11502  -2734   2483    -35       C\\nATOM   3112  N   LEU A 441      -9.554  -5.245  15.440  1.00112.02           N\\nANISOU 3112  N   LEU A 441    11866  18490  12207  -5698   2844   1648       N\\nATOM   3113  CA  LEU A 441     -10.167  -6.342  14.697  1.00113.38           C\\nANISOU 3113  CA  LEU A 441    12136  18432  12510  -6402   2704   1969       C\\nATOM   3114  C   LEU A 441     -10.959  -7.287  15.593  1.00125.26           C\\nANISOU 3114  C   LEU A 441    13779  20090  13724  -6864   2989   2236       C\\nATOM   3115  O   LEU A 441     -11.000  -8.499  15.335  1.00130.59           O\\nANISOU 3115  O   LEU A 441    14979  20276  14364  -7284   2800   2536       O\\nATOM   3116  CB  LEU A 441      -9.096  -7.115  13.924  1.00105.56           C\\nANISOU 3116  CB  LEU A 441    11981  16582  11546  -6372   2234   2137       C\\nATOM   3117  CG  LEU A 441      -8.272  -6.304  12.915  1.00100.01           C\\nANISOU 3117  CG  LEU A 441    11276  15521  11203  -5710   1825   1833       C\\nATOM   3118  CD1 LEU A 441      -7.049  -7.083  12.435  1.00 92.92           C\\nANISOU 3118  CD1 LEU A 441    11249  13839  10218  -5600   1460   1975       C\\nATOM   3119  CD2 LEU A 441      -9.133  -5.880  11.735  1.00101.27           C\\nANISOU 3119  CD2 LEU A 441    10791  15843  11843  -5803   1635   1687       C\\nATOM   3120  N   HIS A 442     -11.587  -6.766  16.640  1.00118.20           N\\nANISOU 3120  N   HIS A 442    12431  19851  12628  -6779   3439   2114       N\\nATOM   3121  CA  HIS A 442     -12.365  -7.591  17.554  1.00126.48           C\\nANISOU 3121  CA  HIS A 442    13562  21110  13385  -7224   3754   2376       C\\nATOM   3122  C   HIS A 442     -13.375  -6.752  18.337  1.00131.96           C\\nANISOU 3122  C   HIS A 442    13462  22622  14057  -7071   4227   2114       C\\nATOM   3123  O   HIS A 442     -14.028  -5.864  17.785  1.00131.46           O\\nANISOU 3123  O   HIS A 442    12638  22887  14424  -6809   4221   1787       O\\nATOM   3124  CB  HIS A 442     -11.436  -8.335  18.515  1.00127.27           C\\nANISOU 3124  CB  HIS A 442    14545  20900  12913  -7295   3807   2692       C\\nCONECT    1    2\\nCONECT    2    1    5    3\\nCONECT    3    2    4    6\\nCONECT    4    3\\nCONECT    5    2\\nCONECT    6    7    3\\nCONECT    7    6   10    8\\nCONECT    8    7    9   11\\nCONECT    9    8\\nCONECT   10    7\\nCONECT   58   59   53\\nCONECT   59   58   62   60\\nCONECT   60   59   61   63\\nCONECT   61   60\\nCONECT   62   59\\nCONECT  194  195  185\\nCONECT  195  194  198  196\\nCONECT  196  195  197  199\\nCONECT  197  196\\nCONECT  198  195\\nCONECT  199  200  196\\nCONECT  200  199  203  201\\nCONECT  201  200  202  204\\nCONECT  202  201\\nCONECT  203  200\\nCONECT  451  452  444\\nCONECT  452  451  455  453\\nCONECT  453  452  454  456\\nCONECT  454  453\\nCONECT  455  452\\nCONECT  467  468  465\\nCONECT  468  467  471  469\\nCONECT  469  468  470  472\\nCONECT  470  469\\nCONECT  471  468\\nCONECT  486  487  474\\nCONECT  487  486  490  488\\nCONECT  488  487  489  491\\nCONECT  489  488\\nCONECT  490  487\\nCONECT  542 1057  541\\nCONECT  772  778  773  766\\nCONECT  773  772  776  774\\nCONECT  774  773  775\\nCONECT  775  774\\nCONECT  776  773  777\\nCONECT  777  776  778\\nCONECT  778  772  777\\nCONECT  779  780\\nCONECT  780  779  783  781\\nCONECT  781  780  782  784\\nCONECT  782  781\\nCONECT  783  780\\nCONECT  784  785  781\\nCONECT  785  784  788  786\\nCONECT  786  785  787  789\\nCONECT  787  786\\nCONECT  788  785\\nCONECT  801  802  791\\nCONECT  802  801  805  803\\nCONECT  803  802  804  806\\nCONECT  804  803\\nCONECT  805  802\\nCONECT  812  813  808\\nCONECT  813  812  816  814\\nCONECT  814  813  815  817\\nCONECT  815  814\\nCONECT  816  813\\nCONECT  817  818  814\\nCONECT  818  817  821  819\\nCONECT  819  818  820  822\\nCONECT  820  819\\nCONECT  821  818\\nCONECT 1018 1019 1012\\nCONECT 1019 1018 1022 1020\\nCONECT 1020 1019 1021 1023\\nCONECT 1021 1020\\nCONECT 1022 1019\\nCONECT 1028 1029 1025\\nCONECT 1029 1028 1032 1030\\nCONECT 1030 1029 1031 1033\\nCONECT 1031 1030\\nCONECT 1032 1029\\nCONECT 1033 1034 1030\\nCONECT 1034 1033 1037 1035\\nCONECT 1035 1034 1036 1038\\nCONECT 1036 1035\\nCONECT 1037 1034\\nCONECT 1038 1039 1035\\nCONECT 1039 1038 1042 1040\\nCONECT 1040 1039 1041 1043\\nCONECT 1041 1040\\nCONECT 1042 1039\\nCONECT 1057  542 1056\\nCONECT 1282 1283 1276\\nCONECT 1283 1282 1286 1284\\nCONECT 1284 1283 1285 1289\\nCONECT 1285 1284\\nCONECT 1286 1283 1287\\nCONECT 1287 1286 1288\\nCONECT 1288 1287\\nCONECT 1332 1333 1326\\nCONECT 1333 1332 1336 1334\\nCONECT 1334 1333 1335 1337\\nCONECT 1335 1334\\nCONECT 1336 1333\\nCONECT 1337 1338 1334\\nCONECT 1338 1337 1341 1339\\nCONECT 1339 1338 1340 1342\\nCONECT 1340 1339\\nCONECT 1341 1338\\nCONECT 1364 1365 1355\\nCONECT 1365 1364 1368 1366\\nCONECT 1366 1365 1367 1369\\nCONECT 1367 1366\\nCONECT 1368 1365\\nCONECT 1369 1370 1366\\nCONECT 1370 1369 1373 1371\\nCONECT 1371 1370 1372 1374\\nCONECT 1372 1371\\nCONECT 1373 1370\\nCONECT 1493 1494 1487\\nCONECT 1494 1493 1497 1495\\nCONECT 1495 1494 1496 1498\\nCONECT 1496 1495\\nCONECT 1497 1494\\nCONECT 1518 1519 1508\\nCONECT 1519 1518 1522 1520\\nCONECT 1520 1519 1521 1523\\nCONECT 1521 1520\\nCONECT 1522 1519\\nCONECT 1538 1539 1533\\nCONECT 1539 1538 1542 1540\\nCONECT 1540 1539 1541 1543\\nCONECT 1541 1540\\nCONECT 1542 1539\\nCONECT 1612 1613 1604\\nCONECT 1613 1612 1616 1614\\nCONECT 1614 1613 1615 1617\\nCONECT 1615 1614\\nCONECT 1616 1613\\nCONECT 1617 1618 1614\\nCONECT 1618 1617 1621 1619\\nCONECT 1619 1618 1620 1622\\nCONECT 1620 1619\\nCONECT 1621 1618\\nCONECT 1629 1630 1624\\nCONECT 1630 1629 1633 1631\\nCONECT 1631 1630 1632 1634\\nCONECT 1632 1631\\nCONECT 1633 1630\\nCONECT 1634 1635 1631\\nCONECT 1635 1634 1638 1636\\nCONECT 1636 1635 1637 1639\\nCONECT 1637 1636\\nCONECT 1638 1635\\nCONECT 1646 1647 1641\\nCONECT 1647 1646 1650 1648\\nCONECT 1648 1647 1649 1651\\nCONECT 1649 1648\\nCONECT 1650 1647\\nCONECT 1659 1660 1653\\nCONECT 1660 1659 1663 1661\\nCONECT 1661 1660 1662 1664\\nCONECT 1662 1661\\nCONECT 1663 1660\\nCONECT 1683 1684 1676\\nCONECT 1684 1683 1687 1685\\nCONECT 1685 1684 1686 1688\\nCONECT 1686 1685\\nCONECT 1687 1684\\nCONECT 1688 1689 1685\\nCONECT 1689 1688 1692 1690\\nCONECT 1690 1689 1691 1693\\nCONECT 1691 1690\\nCONECT 1692 1689\\nCONECT 1709 1710 1703\\nCONECT 1710 1709 1713 1711\\nCONECT 1711 1710 1712 1714\\nCONECT 1712 1711\\nCONECT 1713 1710\\nCONECT 1719 1720 1716\\nCONECT 1720 1719 1723 1721\\nCONECT 1721 1720 1722 1724\\nCONECT 1722 1721\\nCONECT 1723 1720\\nCONECT 1739 1740 1730\\nCONECT 1740 1739 1743 1741\\nCONECT 1741 1740 1742 1744\\nCONECT 1742 1741\\nCONECT 1743 1740\\nCONECT 1744 1745 1741\\nCONECT 1745 1744 1748 1746\\nCONECT 1746 1745 1747 1749\\nCONECT 1747 1746\\nCONECT 1748 1745\\nCONECT 1749 1750 1746\\nCONECT 1750 1749 1753 1751\\nCONECT 1751 1750 1752 1754\\nCONECT 1752 1751\\nCONECT 1753 1750\\nCONECT 1758 1759 1756\\nCONECT 1759 1758 1762 1760\\nCONECT 1760 1759 1761 1763\\nCONECT 1761 1760\\nCONECT 1762 1759\\nCONECT 1778 1779 1773\\nCONECT 1779 1778 1782 1780\\nCONECT 1780 1779 1781 1783\\nCONECT 1781 1780\\nCONECT 1782 1779\\nCONECT 1814 1815 1807\\nCONECT 1815 1814 1818 1816\\nCONECT 1816 1815 1817 1819\\nCONECT 1817 1816\\nCONECT 1818 1815\\nCONECT 1926 1927 1920\\nCONECT 1927 1926 1930 1928\\nCONECT 1928 1927 1929 1931\\nCONECT 1929 1928\\nCONECT 1930 1927\\nCONECT 1944 1945 1941\\nCONECT 1945 1944 1948 1946\\nCONECT 1946 1945 1947 1949\\nCONECT 1947 1946\\nCONECT 1948 1945\\nCONECT 1957 1958 1951\\nCONECT 1958 1957 1961 1959\\nCONECT 1959 1958 1960 1962\\nCONECT 1960 1959\\nCONECT 1961 1958\\nCONECT 2187 2188 2182\\nCONECT 2188 2187 2191 2189\\nCONECT 2189 2188 2190 2192\\nCONECT 2190 2189\\nCONECT 2191 2188\\nCONECT 2285 2286 2273\\nCONECT 2286 2285 2289 2287\\nCONECT 2287 2286 2288 2290\\nCONECT 2288 2287\\nCONECT 2289 2286\\nCONECT 2309 2310 2306\\nCONECT 2310 2309 2313 2311\\nCONECT 2311 2310 2312 2314\\nCONECT 2312 2311\\nCONECT 2313 2310\\nCONECT 2335 2336 2332\\nCONECT 2336 2335 2339 2337\\nCONECT 2337 2336 2338 2340\\nCONECT 2338 2337\\nCONECT 2339 2336\\nCONECT 2346 2347 2342\\nCONECT 2347 2346 2350 2348\\nCONECT 2348 2347 2349 2351\\nCONECT 2349 2348\\nCONECT 2350 2347\\nCONECT 2385 2386 2379\\nCONECT 2386 2385 2389 2387\\nCONECT 2387 2386 2388 2390\\nCONECT 2388 2387\\nCONECT 2389 2386\\nCONECT 2428 2429 2425\\nCONECT 2429 2428 2432 2430\\nCONECT 2430 2429 2431 2433\\nCONECT 2431 2430\\nCONECT 2432 2429\\nCONECT 2506 2507 2504\\nCONECT 2507 2506 2510 2508\\nCONECT 2508 2507 2509 2511\\nCONECT 2509 2508\\nCONECT 2510 2507\\nCONECT 2538 2539 2535\\nCONECT 2539 2538 2542 2540\\nCONECT 2540 2539 2541\\nCONECT 2541 2540\\nCONECT 2542 2539 2543\\nCONECT 2543 2542 2544 2545\\nCONECT 2544 2543 2546\\nCONECT 2545 2543 2547\\nCONECT 2546 2544 2548\\nCONECT 2547 2545 2548\\nCONECT 2548 2546 2547 2549\\nCONECT 2549 2548\\nCONECT 2550 2551\\nCONECT 2551 2550 2554 2552\\nCONECT 2552 2551 2553 2555\\nCONECT 2553 2552\\nCONECT 2554 2551\\nCONECT 2555 2556 2552\\nCONECT 2556 2555 2559 2557\\nCONECT 2557 2556 2558 2560\\nCONECT 2558 2557\\nCONECT 2559 2556\\nCONECT 2560 2561 2557\\nCONECT 2561 2560 2564 2562\\nCONECT 2562 2561 2563 2565\\nCONECT 2563 2562\\nCONECT 2564 2561\\nCONECT 2565 2566 2562\\nCONECT 2566 2565 2569 2567\\nCONECT 2567 2566 2568 2570\\nCONECT 2568 2567\\nCONECT 2569 2566\\nCONECT 2579 2580 2572\\nCONECT 2580 2579 2583 2581\\nCONECT 2581 2580 2582 2584\\nCONECT 2582 2581\\nCONECT 2583 2580\\nCONECT 2584 2585 2581\\nCONECT 2585 2584 2588 2586\\nCONECT 2586 2585 2587 2589\\nCONECT 2587 2586\\nCONECT 2588 2585\\nCONECT 2768 2769 2760\\nCONECT 2769 2768 2772 2770\\nCONECT 2770 2769 2771 2773\\nCONECT 2771 2770\\nCONECT 2772 2769\\nCONECT 2797 2798 2791\\nCONECT 2798 2797 2801 2799\\nCONECT 2799 2798 2800 2802\\nCONECT 2800 2799\\nCONECT 2801 2798\\nCONECT 2807 2818 2806\\nCONECT 2808 2809 2804\\nCONECT 2809 2808 2812 2810\\nCONECT 2810 2809 2811 2813\\nCONECT 2811 2810\\nCONECT 2812 2809\\nCONECT 2818 2807 2817\\nCONECT 2849 2850 2844\\nCONECT 2850 2849 2853 2851\\nCONECT 2851 2850 2852 2854\\nCONECT 2852 2851\\nCONECT 2853 2850\\nCONECT 2854 2855 2851\\nCONECT 2855 2854 2858 2856\\nCONECT 2856 2855 2857 2859\\nCONECT 2857 2856\\nCONECT 2858 2855\\nCONECT 3047 3048 3041\\nCONECT 3048 3047 3051 3049\\nCONECT 3049 3048 3050 3052\\nCONECT 3050 3049\\nCONECT 3051 3048\\nCONECT 3052 3053 3049\\nCONECT 3053 3052 3056 3054\\nCONECT 3054 3053 3055 3057\\nCONECT 3055 3054\\nCONECT 3056 3053\\nCONECT 3068 3069 3059\\nCONECT 3069 3068 3072 3070\\nCONECT 3070 3069 3071 3073\\nCONECT 3071 3070\\nCONECT 3072 3069\\nCONECT 3073 3074 3070\\nCONECT 3074 3073 3077 3075\\nCONECT 3075 3074 3076 3078\\nCONECT 3076 3075\\nCONECT 3077 3074\\nCONECT 3094 3095 3085\\nCONECT 3095 3094 3098 3096\\nCONECT 3096 3095 3097 3099\\nCONECT 3097 3096\\nCONECT 3098 3095\\nCONECT 3099 3100 3096\\nCONECT 3100 3099 3103 3101\\nCONECT 3101 3100 3102 3104\\nCONECT 3102 3101\\nCONECT 3103 3100\\nCONECT 3120 3121 3114\\nCONECT 3121 3120 3124 3122\\nCONECT 3122 3121 3123\\nCONECT 3123 3122\\nCONECT 3124 3121\\nEND\\n\",\"pdb\");\n\tviewer_1716807258097742.setStyle({\"model\": 0},{\"cartoon\": {}});\n\tviewer_1716807258097742.addSurface(null,{\"opacity\": 1, \"color\": \"lightgray\"});\n\tviewer_1716807258097742.addModels(\"HETATM    1 C94  UNL   1        8.221   2.938 -13.874  1.00  0.00           C  \\nHETATM    2 C95  UNL   1        7.345   3.829 -13.234  1.00  0.00           C  \\nHETATM    3 C96  UNL   1        6.076   3.425 -12.847  1.00  0.00           C  \\nHETATM    4 C97  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6.529  -1.190 -13.678  1.00  0.00           O  \\nHETATM   17 N15  UNL   1        5.169   4.344 -12.308  1.00  0.00           N  \\nHETATM   18 N16  UNL   1        8.736   0.743 -14.814  1.00  0.00           N  \\nHETATM   19 C108 UNL   1        9.633   4.281 -15.307  1.00  0.00           C  \\nHETATM   20 C109 UNL   1        9.560   3.472 -14.237  1.00  0.00           C  \\nHETATM   21 N17  UNL   1       10.596   3.098 -13.416  1.00  0.00           N  \\nHETATM   22 C110 UNL   1       10.846   4.978 -15.836  1.00  0.00           C  \\nHETATM   23 N18  UNL   1       13.744   5.012 -16.349  1.00  0.00           N  \\nHETATM   24 C111 UNL   1       12.929   4.168 -16.892  1.00  0.00           C  \\nHETATM   25 N19  UNL   1       11.599   4.020 -16.611  1.00  0.00           N  \\nHETATM   26 N20  UNL   1       15.002   4.934 -16.841  1.00  0.00           N  \\nCONECT    1    2    2    6   20\\nCONECT    2    1    1    3\\nCONECT    6    1    5    5   18\\nCONECT   20    1   19   19   21\\nCONECT    3    2    4    4   17\\nCONECT    4    3    3    5\\nCONECT   17    3\\nCONECT    5    4    6    6    7\\nCONECT    7    5    8   11   16\\nCONECT   18    6\\nCONECT    8    7    9    9\\nCONECT   11    7   10   10   12\\nCONECT   16    7\\nCONECT    9    8    8   10\\nCONECT   10    9   11   11   15\\nCONECT   15   10   14   14\\nCONECT   12   11   13   13\\nCONECT   13   12   12   14\\nCONECT   14   13   15   15\\nCONECT   19   20   20   22\\nCONECT   22   19   25\\nCONECT   21   20\\nCONECT   25   22   24\\nCONECT   23   24   24   26\\nCONECT   24   23   23   25\\nCONECT   26   23\\nEND\",\"pdb\");\n\tviewer_1716807258097742.setStyle({\"model\": 1},{\"stick\": {\"color\": \"cyan\"}});\n\tviewer_1716807258097742.zoomTo();\nviewer_1716807258097742.render();\n});\n</script>",
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       "        <p id=\"3dmolwarning_1716807258097742\" style=\"background-color:#ffcccc;color:black\">You appear to be running in JupyterLab (or JavaScript failed to load for some other reason).  You need to install the 3dmol extension: <br>\n",
       "        <tt>jupyter labextension install jupyterlab_3dmol</tt></p>\n",
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       "viewer_1716807258097742.zoomTo();\n",
       "\tviewer_1716807258097742.addModels(\"HEADER    MEMBRANE PROTEIN                        02-MAR-18   6CM4              \\nTITLE     STRUCTURE OF THE D2 DOPAMINE RECEPTOR BOUND TO THE ATYPICAL           \\nTITLE    2 ANTIPSYCHOTIC DRUG RISPERIDONE                                       \\nCOMPND    MOL_ID: 1;                                                            \\nCOMPND   2 MOLECULE: D(2) DOPAMINE RECEPTOR, ENDOLYSIN CHIMERA;                 \\nCOMPND   3 CHAIN: A;                                                            \\nCOMPND   4 SYNONYM: DOPAMINE D2 RECEPTOR, LYSIS PROTEIN, LYSOZYME, MURAMIDASE,  \\nCOMPND   5 DOPAMINE D2 RECEPTOR;                                                \\nCOMPND   6 EC: 3.2.1.17;                                                        \\nCOMPND   7 ENGINEERED: YES                                                      \\nSOURCE    MOL_ID: 1;                                                            \\nSOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, ENTEROBACTERIA PHAGE T4;          \\nSOURCE   3 ORGANISM_COMMON: HUMAN, BACTERIOPHAGE T4;                            \\nSOURCE   4 ORGANISM_TAXID: 9606, 10665;                                         \\nSOURCE   5 GENE: DRD2, E, T4TP126;                                              \\nSOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            \\nSOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             \\nSOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;                                       \\nSOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          \\nSOURCE  10 EXPRESSION_SYSTEM_PLASMID: PFASTBAC1-HM                              \\nKEYWDS    GPCR, D2, DOPAMINE RECEPTOR, ANTIPSYCHOTIC, RISPERIDONE, MEMBRANE     \\nKEYWDS   2 PROTEIN                                                              \\nEXPDTA    X-RAY DIFFRACTION                                                     \\nAUTHOR    S.WANG,T.CHE,A.LEVIT,B.K.SHOICHET,D.WACKER,B.L.ROTH                   \\nREVDAT   6   04-OCT-23 6CM4    1       REMARK                                   \\nREVDAT   5   27-NOV-19 6CM4    1       REMARK                                   \\nREVDAT   4   20-FEB-19 6CM4    1       REMARK                                   \\nREVDAT   3   11-APR-18 6CM4    1       DBREF                                    \\nREVDAT   2   21-MAR-18 6CM4    1       JRNL                                     \\nREVDAT   1   14-MAR-18 6CM4    0                                                \\nSPRSDE     14-MAR-18 6CM4      6C38                                             \\nJRNL        AUTH   S.WANG,T.CHE,A.LEVIT,B.K.SHOICHET,D.WACKER,B.L.ROTH          \\nJRNL        TITL   STRUCTURE OF THE D2 DOPAMINE RECEPTOR BOUND TO THE ATYPICAL  \\nJRNL        TITL 2 ANTIPSYCHOTIC DRUG RISPERIDONE.                              \\nJRNL        REF    NATURE                        V. 555   269 2018              \\nJRNL        REFN                   ESSN 1476-4687                               \\nJRNL        PMID   29466326                                                     \\nJRNL        DOI    10.1038/NATURE25758                                          \\nREMARK   2                                                                      \\nREMARK   2 RESOLUTION.    2.87 ANGSTROMS.                                       \\nREMARK   3                                                                      \\nREMARK   3 REFINEMENT.                                                          \\nREMARK   3   PROGRAM     : PHENIX (1.12_2829: ???)                              \\nREMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            \\nREMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           \\nREMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            \\nREMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              \\nREMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               \\nREMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           \\nREMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  \\nREMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  \\nREMARK   3                                                                      \\nREMARK   3    REFINEMENT TARGET : ML                                            \\nREMARK   3                                                                      \\nREMARK   3  DATA USED IN REFINEMENT.                                            \\nREMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.87                           \\nREMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.55                          \\nREMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.360                          \\nREMARK   3   COMPLETENESS FOR RANGE        (%) : 95.2                           \\nREMARK   3   NUMBER OF REFLECTIONS             : 12814                          \\nREMARK   3                                                                      \\nREMARK   3  FIT TO DATA USED IN REFINEMENT.                                     \\nREMARK   3   R VALUE     (WORKING + TEST SET) : 0.227                           \\nREMARK   3   R VALUE            (WORKING SET) : 0.226                           \\nREMARK   3   FREE R VALUE                     : 0.249                           \\nREMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.850                           \\nREMARK   3   FREE R VALUE TEST SET COUNT      : 622                             \\nREMARK   3                                                                      \\nREMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           \\nREMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        \\nREMARK   3     1 29.5504 -  4.5475    0.98     3287   157  0.2103 0.2188        \\nREMARK   3     2  4.5475 -  3.6116    0.99     3151   170  0.2090 0.2511        \\nREMARK   3     3  3.6116 -  3.1556    0.99     3111   162  0.2730 0.3034        \\nREMARK   3     4  3.1556 -  2.8674    0.84     2643   133  0.3166 0.3214        \\nREMARK   3                                                                      \\nREMARK   3  BULK SOLVENT MODELLING.                                             \\nREMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       \\nREMARK   3   SOLVENT RADIUS     : 1.11                                          \\nREMARK   3   SHRINKAGE RADIUS   : 0.90                                          \\nREMARK   3   K_SOL              : NULL                                          \\nREMARK   3   B_SOL              : NULL                                          \\nREMARK   3                                                                      \\nREMARK   3  ERROR ESTIMATES.                                                    \\nREMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.390            \\nREMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.640           \\nREMARK   3                                                                      \\nREMARK   3  B VALUES.                                                           \\nREMARK   3   FROM WILSON PLOT           (A**2) : NULL                           \\nREMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           \\nREMARK   3   OVERALL ANISOTROPIC B VALUE.                                       \\nREMARK   3    B11 (A**2) : NULL                                                 \\nREMARK   3    B22 (A**2) : NULL                                                 \\nREMARK   3    B33 (A**2) : NULL                                                 \\nREMARK   3    B12 (A**2) : NULL                                                 \\nREMARK   3    B13 (A**2) : NULL                                                 \\nREMARK   3    B23 (A**2) : NULL                                                 \\nREMARK   3                                                                      \\nREMARK   3  TWINNING INFORMATION.                                               \\nREMARK   3   FRACTION: NULL                                                     \\nREMARK   3   OPERATOR: NULL                                                     \\nREMARK   3                                                                      \\nREMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       \\nREMARK   3                 RMSD          COUNT                                  \\nREMARK   3   BOND      :  0.003           3283                                  \\nREMARK   3   ANGLE     :  0.516           4483                                  \\nREMARK   3   CHIRALITY :  0.037            544                                  \\nREMARK   3   PLANARITY :  0.003            549                                  \\nREMARK   3   DIHEDRAL  : 10.862           1928                                  \\nREMARK   3                                                                      \\nREMARK   3  TLS DETAILS                                                         \\nREMARK   3   NUMBER OF TLS GROUPS  : 3                                          \\nREMARK   3   TLS GROUP : 1                                                      \\nREMARK   3    SELECTION: CHAIN 'A' AND (RESID 36 THROUGH 222 )                  \\nREMARK   3    ORIGIN FOR THE GROUP (A):   7.6595   9.9883   1.8227              \\nREMARK   3    T TENSOR                                                          \\nREMARK   3      T11:   0.3906 T22:   0.3948                                     \\nREMARK   3      T33:   0.4097 T12:  -0.0409                                     \\nREMARK   3      T13:   0.0298 T23:   0.0323                                     \\nREMARK   3    L TENSOR                                                          \\nREMARK   3      L11:   4.8704 L22:   2.9655                                     \\nREMARK   3      L33:   4.7317 L12:   0.7811                                     \\nREMARK   3      L13:   2.8181 L23:   1.4507                                     \\nREMARK   3    S TENSOR                                                          \\nREMARK   3      S11:   0.0593 S12:  -0.1051 S13:   0.0093                       \\nREMARK   3      S21:   0.1418 S22:  -0.1464 S23:   0.1356                       \\nREMARK   3      S31:   0.4299 S32:  -0.3974 S33:  -0.0137                       \\nREMARK   3   TLS GROUP : 2                                                      \\nREMARK   3    SELECTION: CHAIN 'A' AND (RESID 1002 THROUGH 1161 )               \\nREMARK   3    ORIGIN FOR THE GROUP (A):  32.7700  -7.7446  36.3658              \\nREMARK   3    T TENSOR                                                          \\nREMARK   3      T11:   0.6968 T22:   0.5198                                     \\nREMARK   3      T33:   0.5000 T12:   0.0363                                     \\nREMARK   3      T13:   0.0872 T23:   0.1084                                     \\nREMARK   3    L TENSOR                                                          \\nREMARK   3      L11:   6.6697 L22:   6.8821                                     \\nREMARK   3      L33:   6.4568 L12:   1.6541                                     \\nREMARK   3      L13:   1.9941 L23:   1.4205                                     \\nREMARK   3    S TENSOR                                                          \\nREMARK   3      S11:  -0.2551 S12:   0.1211 S13:  -0.2547                       \\nREMARK   3      S21:  -0.3908 S22:  -0.0566 S23:  -0.4642                       \\nREMARK   3      S31:   0.4711 S32:   0.2364 S33:   0.3147                       \\nREMARK   3   TLS GROUP : 3                                                      \\nREMARK   3    SELECTION: CHAIN 'A' AND (RESID 384 THROUGH 460 )                 \\nREMARK   3    ORIGIN FOR THE GROUP (A):   9.8885  -1.6530  -1.3224              \\nREMARK   3    T TENSOR                                                          \\nREMARK   3      T11:   0.6392 T22:   0.3770                                     \\nREMARK   3      T33:   0.5276 T12:   0.0087                                     \\nREMARK   3      T13:  -0.0908 T23:   0.0140                                     \\nREMARK   3    L TENSOR                                                          \\nREMARK   3      L11:   6.0244 L22:   5.3813                                     \\nREMARK   3      L33:   6.7255 L12:   0.3578                                     \\nREMARK   3      L13:   1.1698 L23:   0.5209                                     \\nREMARK   3    S TENSOR                                                          \\nREMARK   3      S11:  -0.0948 S12:   0.3307 S13:   0.0832                       \\nREMARK   3      S21:  -0.4022 S22:   0.2772 S23:  -0.0581                       \\nREMARK   3      S31:   1.2902 S32:  -0.0417 S33:  -0.2847                       \\nREMARK   3                                                                      \\nREMARK   3  NCS DETAILS                                                         \\nREMARK   3   NUMBER OF NCS GROUPS : NULL                                        \\nREMARK   3                                                                      \\nREMARK   3  OTHER REFINEMENT REMARKS: NULL                                      \\nREMARK   4                                                                      \\nREMARK   4 6CM4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         \\nREMARK 100                                                                      \\nREMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-MAR-18.                  \\nREMARK 100 THE DEPOSITION ID IS D_1000232947.                                   \\nREMARK 200                                                                      \\nREMARK 200 EXPERIMENTAL DETAILS                                                 \\nREMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  \\nREMARK 200  DATE OF DATA COLLECTION        : 13-AUG-17                          \\nREMARK 200  TEMPERATURE           (KELVIN) : 100                                \\nREMARK 200  PH                             : NULL                               \\nREMARK 200  NUMBER OF CRYSTALS USED        : 1                                  \\nREMARK 200                                                                      \\nREMARK 200  SYNCHROTRON              (Y/N) : Y                                  \\nREMARK 200  RADIATION SOURCE               : APS                                \\nREMARK 200  BEAMLINE                       : 23-ID-B                            \\nREMARK 200  X-RAY GENERATOR MODEL          : NULL                               \\nREMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  \\nREMARK 200  WAVELENGTH OR RANGE        (A) : 1.033                              \\nREMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL CRYO-COOLED         \\nREMARK 200                                   SI(111)                            \\nREMARK 200  OPTICS                         : NULL                               \\nREMARK 200                                                                      \\nREMARK 200  DETECTOR TYPE                  : PIXEL                              \\nREMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER X 16M                \\nREMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000                           \\nREMARK 200  DATA SCALING SOFTWARE          : HKL-3000                           \\nREMARK 200                                                                      \\nREMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 12826                              \\nREMARK 200  RESOLUTION RANGE HIGH      (A) : 2.867                              \\nREMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             \\nREMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               \\nREMARK 200                                                                      \\nREMARK 200 OVERALL.                                                             \\nREMARK 200  COMPLETENESS FOR RANGE     (%) : 97.3                               \\nREMARK 200  DATA REDUNDANCY                : 5.500                              \\nREMARK 200  R MERGE                    (I) : 0.13400                            \\nREMARK 200  R SYM                      (I) : NULL                               \\nREMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.2000                            \\nREMARK 200                                                                      \\nREMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     \\nREMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90                     \\nREMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.99                     \\nREMARK 200  COMPLETENESS FOR SHELL     (%) : 86.9                               \\nREMARK 200  DATA REDUNDANCY IN SHELL       : 2.50                               \\nREMARK 200  R MERGE FOR SHELL          (I) : 0.73800                            \\nREMARK 200  R SYM FOR SHELL            (I) : NULL                               \\nREMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.000                              \\nREMARK 200                                                                      \\nREMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              \\nREMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        \\nREMARK 200 SOFTWARE USED: PHASER                                                \\nREMARK 200 STARTING MODEL: PDB ENTRIES 5WIU & 2RH1                              \\nREMARK 200                                                                      \\nREMARK 200 REMARK: NULL                                                         \\nREMARK 280                                                                      \\nREMARK 280 CRYSTAL                                                              \\nREMARK 280 SOLVENT CONTENT, VS   (%): 57.13                                     \\nREMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.87                     \\nREMARK 280                                                                      \\nREMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM TRIS-HCL, PH 7.8, 230 MM          \\nREMARK 280  LITHIUM NITRATE, 25% PEG400, 4% 1,3-BUTANEDIOL, LIPIDIC CUBIC       \\nREMARK 280  PHASE, TEMPERATURE 293K                                             \\nREMARK 290                                                                      \\nREMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            \\nREMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       \\nREMARK 290                                                                      \\nREMARK 290      SYMOP   SYMMETRY                                                \\nREMARK 290     NNNMMM   OPERATOR                                                \\nREMARK 290       1555   X,Y,Z                                                   \\nREMARK 290       2555   -X+1/2,-Y,Z+1/2                                         \\nREMARK 290       3555   -X,Y+1/2,-Z+1/2                                         \\nREMARK 290       4555   X+1/2,-Y+1/2,-Z                                         \\nREMARK 290                                                                      \\nREMARK 290     WHERE NNN -> OPERATOR NUMBER                                     \\nREMARK 290           MMM -> TRANSLATION VECTOR                                  \\nREMARK 290                                                                      \\nREMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            \\nREMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             \\nREMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                \\nREMARK 290 RELATED MOLECULES.                                                   \\nREMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            \\nREMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            \\nREMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            \\nREMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       25.48950            \\nREMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            \\nREMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       75.65350            \\nREMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            \\nREMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       36.26150            \\nREMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       75.65350            \\nREMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       25.48950            \\nREMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       36.26150            \\nREMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            \\nREMARK 290                                                                      \\nREMARK 290 REMARK: NULL                                                         \\nREMARK 300                                                                      \\nREMARK 300 BIOMOLECULE: 1                                                       \\nREMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                \\nREMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  \\nREMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               \\nREMARK 300 BURIED SURFACE AREA.                                                 \\nREMARK 350                                                                      \\nREMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           \\nREMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                \\nREMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          \\nREMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          \\nREMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               \\nREMARK 350                                                                      \\nREMARK 350 BIOMOLECULE: 1                                                       \\nREMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         \\nREMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  \\nREMARK 350 SOFTWARE USED: PISA                                                  \\nREMARK 350 TOTAL BURIED SURFACE AREA: 1850 ANGSTROM**2                          \\nREMARK 350 SURFACE AREA OF THE COMPLEX: 20460 ANGSTROM**2                       \\nREMARK 350 CHANGE IN SOLVENT FREE ENERGY: 12.0 KCAL/MOL                         \\nREMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     \\nREMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            \\nREMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            \\nREMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            \\nREMARK 465                                                                      \\nREMARK 465 MISSING RESIDUES                                                     \\nREMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       \\nREMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               \\nREMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                \\nREMARK 465                                                                      \\nREMARK 465   M RES C SSSEQI                                                     \\nREMARK 465     MET A   140                                                      \\nREMARK 465     LEU A   141                                                      \\nREMARK 465     TYR A   142                                                      \\nREMARK 465     ASN A   143                                                      \\nREMARK 465     LYS A   362                                                      \\nREMARK 465     LEU A   363                                                      \\nREMARK 465     CYS A   443                                                      \\nREMARK 470                                                                      \\nREMARK 470 MISSING ATOM                                                         \\nREMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           \\nREMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          \\nREMARK 470 I=INSERTION CODE):                                                   \\nREMARK 470   M RES CSSEQI  ATOMS                                                \\nREMARK 470     ASN A  35    CG   OD1  ND2                                       \\nREMARK 470     TYR A  36    CG   CD1  CD2  CE1  CE2  CZ   OH                    \\nREMARK 470     LEU A  43    CG   CD1  CD2                                       \\nREMARK 470     GLU A  62    CG   CD   OE1  OE2                                  \\nREMARK 470     LYS A  63    CG   CD   CE   NZ                                   \\nREMARK 470     VAL A  96    CG1  CG2                                            \\nREMARK 470     GLU A  99    CG   CD   OE1  OE2                                  \\nREMARK 470     LYS A 101    CG   CD   CE   NZ                                   \\nREMARK 470     THR A 144    OG1  CG2                                            \\nREMARK 470     ARG A 145    CG   CD   NE   CZ   NH1  NH2                        \\nREMARK 470     SER A 147    OG                                                  \\nREMARK 470     LYS A 149    CG   CD   CE   NZ                                   \\nREMARK 470     ARG A 150    CG   CD   NE   CZ   NH1  NH2                        \\nREMARK 470     ASN A 176    CG   OD1  ND2                                       \\nREMARK 470     ASP A 178    CG   OD1  OD2                                       \\nREMARK 470     GLN A 179    CG   CD   OE1  NE2                                  \\nREMARK 470     ASN A 180    CG   OD1  ND2                                       \\nREMARK 470     LYS A 211    CE   NZ                                             \\nREMARK 470     ARG A 217    CG   CD   NE   CZ   NH1  NH2                        \\nREMARK 470     ARG A 218    CG   CD   NE   CZ   NH1  NH2                        \\nREMARK 470     LYS A 221    CG   CD   CE   NZ                                   \\nREMARK 470     ARG A 222    CG   CD   NE   CZ   NH1  NH2                        \\nREMARK 470     LYS A1016    CG   CD   CE   NZ                                   \\nREMARK 470     LYS A1019    CG   CD   CE   NZ                                   \\nREMARK 470     GLU A1022    CG   CD   OE1  OE2                                  \\nREMARK 470     LEU A1032    CG   CD1  CD2                                       \\nREMARK 470     LEU A1033    CG   CD1  CD2                                       \\nREMARK 470     LYS A1035    CG   CD   CE   NZ                                   \\nREMARK 470     SER A1036    OG                                                  \\nREMARK 470     SER A1038    OG                                                  \\nREMARK 470     ASN A1040    CG   OD1  ND2                                       \\nREMARK 470     SER A1044    OG                                                  \\nREMARK 470     GLU A1045    CG   CD   OE1  OE2                                  \\nREMARK 470     LYS A1048    CG   CD   CE   NZ                                   \\nREMARK 470     ILE A1050    CG1  CG2  CD1                                       \\nREMARK 470     ASN A1053    CG   OD1  ND2                                       \\nREMARK 470     THR A1054    OG1  CG2                                            \\nREMARK 470     ASN A1055    CG   OD1  ND2                                       \\nREMARK 470     VAL A1057    CG1  CG2                                            \\nREMARK 470     LYS A1060    CG   CD   CE   NZ                                   \\nREMARK 470     LYS A1065    CG   CD   CE   NZ                                   \\nREMARK 470     ARG A1080    CG   CD   NE   CZ   NH1  NH2                        \\nREMARK 470     LYS A1083    CG   CD   CE   NZ                                   \\nREMARK 470     LYS A1085    CG   CD   CE   NZ                                   \\nREMARK 470     ASN A1116    CG   OD1  ND2                                       \\nREMARK 470     ASP A1127    CG   OD1  OD2                                       \\nREMARK 470     VAL A1131    CG1  CG2                                            \\nREMARK 470     LYS A1135    CG   CD   CE   NZ                                   \\nREMARK 470     ARG A1137    CG   CD   NE   CZ   NH1  NH2                        \\nREMARK 470     GLN A1141    CG   CD   OE1  NE2                                  \\nREMARK 470     LYS A1147    CG   CD   CE   NZ                                   \\nREMARK 470     THR A1157    OG1  CG2                                            \\nREMARK 470     SER A 364    OG                                                  \\nREMARK 470     GLN A 365    CG   CD   OE1  NE2                                  \\nREMARK 470     GLN A 366    CG   CD   OE1  NE2                                  \\nREMARK 470     LYS A 367    CG   CD   CE   NZ                                   \\nREMARK 470     LYS A 369    CG   CD   CE   NZ                                   \\nREMARK 470     LYS A 370    CG   CD   CE   NZ                                   \\nREMARK 470     ILE A 394    CG1  CG2  CD1                                       \\nREMARK 470     HIS A 398    CG   ND1  CD2  CE1  NE2                             \\nREMARK 470     ASP A 400    CG   OD1  OD2                                       \\nREMARK 470     VAL A 406    CG1  CG2                                            \\nREMARK 470     LEU A 407    CG   CD1  CD2                                       \\nREMARK 470     ILE A 431    CG1  CG2  CD1                                       \\nREMARK 470     GLU A 432    CG   CD   OE1  OE2                                  \\nREMARK 470     ARG A 434    CG   CD   NE   CZ   NH1  NH2                        \\nREMARK 470     LYS A 435    CG   CD   CE   NZ                                   \\nREMARK 470     LEU A 438    CG   CD1  CD2                                       \\nREMARK 470     LYS A 439    CG   CD   CE   NZ                                   \\nREMARK 470     HIS A 442    CG   ND1  CD2  CE1  NE2                             \\nREMARK 500                                                                      \\nREMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         \\nREMARK 500 SUBTOPIC: TORSION ANGLES                                             \\nREMARK 500                                                                      \\nREMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            \\nREMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               \\nREMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             \\nREMARK 500                                                                      \\nREMARK 500 STANDARD TABLE:                                                      \\nREMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    \\nREMARK 500                                                                      \\nREMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           \\nREMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            \\nREMARK 500                                                                      \\nREMARK 500  M RES CSSEQI        PSI       PHI                                   \\nREMARK 500    GLN A  66       70.23   -104.22                                   \\nREMARK 500    VAL A  87      -52.46   -121.67                                   \\nREMARK 500    PHE A 198      -60.72   -124.56                                   \\nREMARK 500    ASN A1055       17.81     58.75                                   \\nREMARK 500    PHE A1114       49.44    -89.78                                   \\nREMARK 500    ASP A 400       11.47     57.92                                   \\nREMARK 500    LEU A 441       33.98    -88.55                                   \\nREMARK 500                                                                      \\nREMARK 500 REMARK: NULL                                                         \\nREMARK 610                                                                      \\nREMARK 610 MISSING HETEROATOM                                                   \\nREMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           \\nREMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          \\nREMARK 610 I=INSERTION CODE):                                                   \\nREMARK 610   M RES C SSEQI                                                      \\nREMARK 610     OLA A 2005                                                       \\nREMARK 610     OLA A 2006                                                       \\nDBREF  6CM4 A   35   222  UNP    P14416   DRD2_HUMAN      35    222             \\nDBREF  6CM4 A 1002  1161  UNP    D9IEF7   D9IEF7_BPT4      2    161             \\nDBREF  6CM4 A  362   443  UNP    P14416   DRD2_HUMAN     362    443             \\nSEQADV 6CM4 ALA A  122  UNP  P14416    ILE   122 CONFLICT                       \\nSEQADV 6CM4 THR A 1054  UNP  D9IEF7    CYS    54 CONFLICT                       \\nSEQADV 6CM4 ALA A 1097  UNP  D9IEF7    CYS    97 CONFLICT                       \\nSEQADV 6CM4 ALA A  375  UNP  P14416    LEU   375 CONFLICT                       \\nSEQADV 6CM4 ALA A  379  UNP  P14416    LEU   379 CONFLICT                       \\nSEQRES   1 A  430  ASN TYR TYR ALA THR LEU LEU THR LEU LEU ILE ALA VAL\\nSEQRES   2 A  430  ILE VAL PHE GLY ASN VAL LEU VAL CYS MET ALA VAL SER\\nSEQRES   3 A  430  ARG GLU LYS ALA LEU GLN THR THR THR ASN TYR LEU ILE\\nSEQRES   4 A  430  VAL SER LEU ALA VAL ALA ASP LEU LEU VAL ALA THR LEU\\nSEQRES   5 A  430  VAL MET PRO TRP VAL VAL TYR LEU GLU VAL VAL GLY GLU\\nSEQRES   6 A  430  TRP LYS PHE SER ARG ILE HIS CYS ASP ILE PHE VAL THR\\nSEQRES   7 A  430  LEU ASP VAL MET MET CYS THR ALA SER ALA LEU ASN LEU\\nSEQRES   8 A  430  CYS ALA ILE SER ILE ASP ARG TYR THR ALA VAL ALA MET\\nSEQRES   9 A  430  PRO MET LEU TYR ASN THR ARG TYR SER SER LYS ARG ARG\\nSEQRES  10 A  430  VAL THR VAL MET ILE SER ILE VAL TRP VAL LEU SER PHE\\nSEQRES  11 A  430  THR ILE SER CYS PRO LEU LEU PHE GLY LEU ASN ASN ALA\\nSEQRES  12 A  430  ASP GLN ASN GLU CYS ILE ILE ALA ASN PRO ALA PHE VAL\\nSEQRES  13 A  430  VAL TYR SER SER ILE VAL SER PHE TYR VAL PRO PHE ILE\\nSEQRES  14 A  430  VAL THR LEU LEU VAL TYR ILE LYS ILE TYR ILE VAL LEU\\nSEQRES  15 A  430  ARG ARG ARG ARG LYS ARG ASN ILE PHE GLU MET LEU ARG\\nSEQRES  16 A  430  ILE ASP GLU GLY LEU ARG LEU LYS ILE TYR LYS ASP THR\\nSEQRES  17 A  430  GLU GLY TYR TYR THR ILE GLY ILE GLY HIS LEU LEU THR\\nSEQRES  18 A  430  LYS SER PRO SER LEU ASN ALA ALA LYS SER GLU LEU ASP\\nSEQRES  19 A  430  LYS ALA ILE GLY ARG ASN THR ASN GLY VAL ILE THR LYS\\nSEQRES  20 A  430  ASP GLU ALA GLU LYS LEU PHE ASN GLN ASP VAL ASP ALA\\nSEQRES  21 A  430  ALA VAL ARG GLY ILE LEU ARG ASN ALA LYS LEU LYS PRO\\nSEQRES  22 A  430  VAL TYR ASP SER LEU ASP ALA VAL ARG ARG ALA ALA LEU\\nSEQRES  23 A  430  ILE ASN MET VAL PHE GLN MET GLY GLU THR GLY VAL ALA\\nSEQRES  24 A  430  GLY PHE THR ASN SER LEU ARG MET LEU GLN GLN LYS ARG\\nSEQRES  25 A  430  TRP ASP GLU ALA ALA VAL ASN LEU ALA LYS SER ARG TRP\\nSEQRES  26 A  430  TYR ASN GLN THR PRO ASN ARG ALA LYS ARG VAL ILE THR\\nSEQRES  27 A  430  THR PHE ARG THR GLY THR TRP ASP ALA TYR LYS LEU SER\\nSEQRES  28 A  430  GLN GLN LYS GLU LYS LYS ALA THR GLN MET ALA ALA ILE\\nSEQRES  29 A  430  VAL ALA GLY VAL PHE ILE ILE CYS TRP LEU PRO PHE PHE\\nSEQRES  30 A  430  ILE THR HIS ILE LEU ASN ILE HIS CYS ASP CYS ASN ILE\\nSEQRES  31 A  430  PRO PRO VAL LEU TYR SER ALA PHE THR TRP LEU GLY TYR\\nSEQRES  32 A  430  VAL ASN SER ALA VAL ASN PRO ILE ILE TYR THR THR PHE\\nSEQRES  33 A  430  ASN ILE GLU PHE ARG LYS ALA PHE LEU LYS ILE LEU HIS\\nSEQRES  34 A  430  CYS\\nHET    8NU  A2001      30                                                       \\nHET    PEG  A2002       7                                                       \\nHET    PEG  A2003       7                                                       \\nHET    PEG  A2004       7                                                       \\nHET    OLA  A2005      13                                                       \\nHET    OLA  A2006      12                                                       \\nHET    OLA  A2007      20                                                       \\nHETNAM     8NU 3-[2-[4-(6-FLUORANYL-1,2-BENZOXAZOL-3-YL)PIPERIDIN-1-            \\nHETNAM   2 8NU  YL]ETHYL]-2-METHYL-6,7,8,9-TETRAHYDROPYRIDO[1,2-                \\nHETNAM   3 8NU  A]PYRIMIDIN-4-ONE                                               \\nHETNAM     PEG DI(HYDROXYETHYL)ETHER                                            \\nHETNAM     OLA OLEIC ACID                                                       \\nFORMUL   2  8NU    C23 H27 F N4 O2                                              \\nFORMUL   3  PEG    3(C4 H10 O3)                                                 \\nFORMUL   6  OLA    3(C18 H34 O2)                                                \\nFORMUL   9  HOH   *16(H2 O)                                                     \\nHELIX    1   1 ASN A   35  GLU A   62  1                                  28\\nHELIX    2   2 LYS A   63  GLN A   66  1                                   4\\nHELIX    3   3 THR A   67  LEU A   86  1                                  20\\nHELIX    4   4 VAL A   87  GLY A   98  1                                  12\\nHELIX    5   5 SER A  103  MET A  138  1                                  36\\nHELIX    6   6 TYR A  146  CYS A  168  1                                  23\\nHELIX    7   7 PRO A  169  ASN A  176  1                                   8\\nHELIX    8   8 CYS A  182  ASN A  186  1                                   5\\nHELIX    9   9 ALA A  188  VAL A  196  1                                   9\\nHELIX   10  10 PHE A  198  GLU A 1011  1                                  35\\nHELIX   11  11 SER A 1038  GLY A 1051  1                                  14\\nHELIX   12  12 THR A 1059  ASN A 1081  1                                  23\\nHELIX   13  13 LEU A 1084  LEU A 1091  1                                   8\\nHELIX   14  14 ASP A 1092  ALA A 1112  1                                  21\\nHELIX   15  15 PHE A 1114  GLN A 1123  1                                  10\\nHELIX   16  16 ARG A 1125  ALA A 1134  1                                  10\\nHELIX   17  17 SER A 1136  GLN A 1141  1                                   6\\nHELIX   18  18 THR A 1142  GLY A 1156  1                                  15\\nHELIX   19  19 GLU A  368  CYS A  399  1                                  32\\nHELIX   20  20 PRO A  404  ASN A  418  1                                  15\\nHELIX   21  21 VAL A  421  PHE A  429  1                                   9\\nHELIX   22  22 ASN A  430  LEU A  441  1                                  12\\nSHEET    1   1 1 ARG A1014  LYS A1019  0\\nSHEET    2   2 1 TYR A1025  GLY A1028  0\\nSHEET    3   3 1 HIS A1031  THR A1034  0\\nSSBOND   1 CYS A  107    CYS A  182                          1555   1555  2.03\\nSSBOND   2 CYS A  399    CYS A  401                          1555   1555  2.04\\nCRYST1   50.979   72.523  151.307  90.00  90.00  90.00 P 21 21 21    4          \\nORIGX1      1.000000  0.000000  0.000000        0.00000                         \\nORIGX2      0.000000  1.000000  0.000000        0.00000                         \\nORIGX3      0.000000  0.000000  1.000000        0.00000                         \\nSCALE1      0.019616  0.000000  0.000000        0.00000                         \\nSCALE2      0.000000  0.013789  0.000000        0.00000                         \\nSCALE3      0.000000  0.000000  0.006609        0.00000                         \\nATOM      1  N   ASN A  35      -5.317  -8.666 -16.658  1.00108.95           N\\nATOM      2  CA  ASN A  35      -3.999  -9.279 -16.550  1.00112.41           C\\nATOM      3  C   ASN A  35      -3.770  -9.829 -15.148  1.00103.98           C\\nATOM      4  O   ASN A  35      -4.596  -9.642 -14.253  1.00111.14           O\\nATOM      5  CB  ASN A  35      -2.903  -8.271 -16.904  1.00115.88           C\\nATOM      6  N   TYR A  36      -2.640 -10.512 -14.962  1.00122.79           N\\nANISOU    6  N   TYR A  36    17290  13079  16284  -1997  -3163  -3043       N\\nATOM      7  CA  TYR A  36      -2.284 -11.046 -13.653  1.00105.49           C\\nANISOU    7  CA  TYR A  36    15314  10451  14315  -2168  -3210  -2776       C\\nATOM      8  C   TYR A  36      -1.522 -10.036 -12.804  1.00100.38           C\\nANISOU    8  C   TYR A  36    14564  10022  13555  -2013  -2870  -2480       C\\nATOM      9  O   TYR A  36      -1.767  -9.933 -11.597  1.00 95.60           O\\nANISOU    9  O   TYR A  36    13979   9308  13038  -2297  -2774  -2120       O\\nATOM     10  CB  TYR A  36      -1.455 -12.323 -13.811  1.00 98.01           C\\nANISOU   10  CB  TYR A  36    14721   8957  13564  -1967  -3571  -3071       C\\nATOM     11  N   TYR A  37      -0.606  -9.280 -13.416  1.00105.86           N\\nANISOU   11  N   TYR A  37    15140  11047  14036  -1589  -2687  -2627       N\\nATOM     12  CA  TYR A  37       0.202  -8.334 -12.652  1.00101.50           C\\nANISOU   12  CA  TYR A  37    14496  10678  13392  -1434  -2394  -2372       C\\nATOM     13  C   TYR A  37      -0.596  -7.105 -12.233  1.00 97.18           C\\nANISOU   13  C   TYR A  37    13669  10521  12732  -1638  -2109  -2055       C\\nATOM     14  O   TYR A  37      -0.269  -6.474 -11.221  1.00 92.55           O\\nANISOU   14  O   TYR A  37    13035   9983  12145  -1663  -1908  -1774       O\\nATOM     15  CB  TYR A  37       1.435  -7.931 -13.459  1.00105.43           C\\nANISOU   15  CB  TYR A  37    14938  11423  13698   -962  -2294  -2627       C\\nATOM     16  CG  TYR A  37       2.442  -9.052 -13.603  1.00112.39           C\\nANISOU   16  CG  TYR A  37    16060  11928  14715   -688  -2547  -2949       C\\nATOM     17  CD1 TYR A  37       2.745  -9.880 -12.528  1.00116.25           C\\nANISOU   17  CD1 TYR A  37    16804  11893  15472   -778  -2740  -2820       C\\nATOM     18  CD2 TYR A  37       3.084  -9.291 -14.814  1.00112.70           C\\nANISOU   18  CD2 TYR A  37    16070  12145  14606   -332  -2615  -3395       C\\nATOM     19  CE1 TYR A  37       3.662 -10.907 -12.650  1.00117.63           C\\nANISOU   19  CE1 TYR A  37    17203  11682  15808   -489  -3027  -3136       C\\nATOM     20  CE2 TYR A  37       4.002 -10.320 -14.944  1.00114.52           C\\nANISOU   20  CE2 TYR A  37    16488  12042  14980    -35  -2866  -3754       C\\nATOM     21  CZ  TYR A  37       4.287 -11.123 -13.860  1.00116.82           C\\nANISOU   21  CZ  TYR A  37    17037  11766  15584    -99  -3089  -3627       C\\nATOM     22  OH  TYR A  37       5.200 -12.147 -13.987  1.00116.76           O\\nANISOU   22  OH  TYR A  37    17222  11387  15756    236  -3393  -4004       O\\nATOM     23  N   ALA A  38      -1.639  -6.750 -12.985  1.00 96.22           N\\nANISOU   23  N   ALA A  38    13359  10676  12525  -1764  -2113  -2120       N\\nATOM     24  CA  ALA A  38      -2.506  -5.655 -12.566  1.00 90.24           C\\nANISOU   24  CA  ALA A  38    12324  10255  11709  -1946  -1899  -1864       C\\nATOM     25  C   ALA A  38      -3.348  -6.039 -11.356  1.00 93.14           C\\nANISOU   25  C   ALA A  38    12686  10447  12255  -2375  -1898  -1620       C\\nATOM     26  O   ALA A  38      -3.625  -5.191 -10.500  1.00 89.27           O\\nANISOU   26  O   ALA A  38    12015  10164  11737  -2476  -1673  -1375       O\\nATOM     27  CB  ALA A  38      -3.409  -5.222 -13.721  1.00 92.04           C\\nANISOU   27  CB  ALA A  38    12349  10812  11811  -1948  -1956  -2018       C\\nATOM     28  N   THR A  39      -3.759  -7.307 -11.265  1.00101.53           N\\nANISOU   28  N   THR A  39    13946  11141  13491  -2646  -2152  -1687       N\\nATOM     29  CA  THR A  39      -4.521  -7.761 -10.105  1.00 98.62           C\\nANISOU   29  CA  THR A  39    13594  10616  13261  -3121  -2155  -1423       C\\nATOM     30  C   THR A  39      -3.673  -7.706  -8.839  1.00 94.46           C\\nANISOU   30  C   THR A  39    13228   9915  12749  -3111  -2033  -1154       C\\nATOM     31  O   THR A  39      -4.127  -7.220  -7.795  1.00 90.19           O\\nANISOU   31  O   THR A  39    12545   9551  12174  -3363  -1831   -884       O\\nATOM     32  CB  THR A  39      -5.041  -9.178 -10.345  1.00 96.91           C\\nANISOU   32  CB  THR A  39    13602   9983  13235  -3430  -2502  -1538       C\\nATOM     33  OG1 THR A  39      -5.673  -9.242 -11.631  1.00 99.65           O\\nANISOU   33  OG1 THR A  39    13821  10489  13554  -3372  -2644  -1841       O\\nATOM     34  CG2 THR A  39      -6.044  -9.566  -9.272  1.00 85.14           C\\nANISOU   34  CG2 THR A  39    12068   8436  11847  -4016  -2487  -1245       C\\nATOM     35  N   LEU A  40      -2.434  -8.202  -8.915  1.00 91.92           N\\nANISOU   35  N   LEU A  40    13187   9271  12469  -2807  -2162  -1251       N\\nATOM     36  CA  LEU A  40      -1.537  -8.138  -7.766  1.00 89.55           C\\nANISOU   36  CA  LEU A  40    13043   8803  12179  -2751  -2081  -1015       C\\nATOM     37  C   LEU A  40      -1.335  -6.702  -7.304  1.00 83.76           C\\nANISOU   37  C   LEU A  40    12038   8512  11276  -2605  -1722   -856       C\\nATOM     38  O   LEU A  40      -1.301  -6.429  -6.098  1.00 87.36           O\\nANISOU   38  O   LEU A  40    12497   8987  11709  -2775  -1584   -580       O\\nATOM     39  CB  LEU A  40      -0.191  -8.777  -8.104  1.00 87.94           C\\nANISOU   39  CB  LEU A  40    13114   8249  12051  -2357  -2285  -1222       C\\nATOM     40  CG  LEU A  40      -0.166 -10.273  -8.417  1.00 86.57           C\\nANISOU   40  CG  LEU A  40    13274   7524  12094  -2433  -2707  -1405       C\\nATOM     41  CD1 LEU A  40       1.260 -10.798  -8.334  1.00 81.27           C\\nANISOU   41  CD1 LEU A  40    12855   6507  11518  -2029  -2890  -1557       C\\nATOM     42  CD2 LEU A  40      -1.085 -11.041  -7.480  1.00 87.43           C\\nANISOU   42  CD2 LEU A  40    13549   7331  12340  -3007  -2857  -1101       C\\nATOM     43  N   LEU A  41      -1.202  -5.770  -8.248  1.00 77.53           N\\nANISOU   43  N   LEU A  41    11027   8075  10356  -2302  -1588  -1023       N\\nATOM     44  CA  LEU A  41      -1.025  -4.372  -7.871  1.00 83.20           C\\nANISOU   44  CA  LEU A  41    11504   9166  10941  -2162  -1296   -879       C\\nATOM     45  C   LEU A  41      -2.242  -3.847  -7.120  1.00 91.88           C\\nANISOU   45  C   LEU A  41    12365  10511  12032  -2501  -1145   -694       C\\nATOM     46  O   LEU A  41      -2.101  -3.145  -6.111  1.00 94.79           O\\nANISOU   46  O   LEU A  41    12646  11017  12354  -2528   -951   -503       O\\nATOM     47  CB  LEU A  41      -0.739  -3.520  -9.108  1.00 84.35           C\\nANISOU   47  CB  LEU A  41    11487   9616  10946  -1830  -1231  -1064       C\\nATOM     48  CG  LEU A  41       0.684  -3.615  -9.668  1.00 84.82           C\\nANISOU   48  CG  LEU A  41    11682   9604  10941  -1449  -1257  -1222       C\\nATOM     49  CD1 LEU A  41       0.863  -2.686 -10.856  1.00 82.66           C\\nANISOU   49  CD1 LEU A  41    11233   9703  10473  -1206  -1167  -1345       C\\nATOM     50  CD2 LEU A  41       1.708  -3.304  -8.588  1.00 84.95           C\\nANISOU   50  CD2 LEU A  41    11768   9527  10981  -1340  -1134  -1042       C\\nATOM     51  N   THR A  42      -3.447  -4.187  -7.587  1.00 91.95           N\\nANISOU   51  N   THR A  42    12247  10603  12085  -2760  -1237   -778       N\\nATOM     52  CA  THR A  42      -4.651  -3.758  -6.883  1.00 87.42           C\\nANISOU   52  CA  THR A  42    11395  10312  11509  -3092  -1095   -650       C\\nATOM     53  C   THR A  42      -4.741  -4.405  -5.507  1.00 89.21           C\\nANISOU   53  C   THR A  42    11759  10370  11767  -3467  -1059   -402       C\\nATOM     54  O   THR A  42      -5.141  -3.757  -4.533  1.00 90.48           O\\nANISOU   54  O   THR A  42    11720  10805  11853  -3617   -841   -252       O\\nATOM     55  CB  THR A  42      -5.894  -4.085  -7.708  1.00 81.63           C\\nANISOU   55  CB  THR A  42    10483   9703  10829  -3302  -1229   -812       C\\nATOM     56  OG1 THR A  42      -5.719  -3.600  -9.045  1.00 80.89           O\\nANISOU   56  OG1 THR A  42    10326   9737  10673  -2956  -1306  -1030       O\\nATOM     57  CG2 THR A  42      -7.122  -3.427  -7.095  1.00 73.78           C\\nANISOU   57  CG2 THR A  42     9102   9107   9822  -3566  -1057   -743       C\\nATOM     58  N   LEU A  43      -4.372  -5.685  -5.408  1.00 89.32           N\\nANISOU   58  N   LEU A  43    12123   9933  11882  -3624  -1291   -363       N\\nATOM     59  CA  LEU A  43      -4.291  -6.324  -4.100  1.00 89.41           C\\nANISOU   59  CA  LEU A  43    12339   9733  11900  -3975  -1300    -78       C\\nATOM     60  C   LEU A  43      -3.297  -5.599  -3.203  1.00 85.76           C\\nANISOU   60  C   LEU A  43    11923   9332  11330  -3737  -1117     75       C\\nATOM     61  O   LEU A  43      -3.540  -5.429  -2.003  1.00 86.73           O\\nANISOU   61  O   LEU A  43    12007   9591  11355  -4009   -965    311       O\\nATOM     62  CB  LEU A  43      -3.907  -7.795  -4.254  1.00 92.73           C\\nANISOU   62  CB  LEU A  43    13182   9571  12480  -4106  -1657    -74       C\\nATOM     63  N   LEU A  44      -2.173  -5.155  -3.773  1.00 83.60           N\\nANISOU   63  N   LEU A  44    11715   8995  11055  -3246  -1124    -66       N\\nATOM     64  CA  LEU A  44      -1.214  -4.375  -3.000  1.00 85.11           C\\nANISOU   64  CA  LEU A  44    11914   9267  11155  -3006   -957     53       C\\nATOM     65  C   LEU A  44      -1.839  -3.078  -2.502  1.00 85.13           C\\nANISOU   65  C   LEU A  44    11557   9754  11035  -3039   -660    109       C\\nATOM     66  O   LEU A  44      -1.633  -2.688  -1.347  1.00 86.93           O\\nANISOU   66  O   LEU A  44    11776  10082  11172  -3118   -515    286       O\\nATOM     67  CB  LEU A  44       0.031  -4.082  -3.838  1.00 87.56           C\\nANISOU   67  CB  LEU A  44    12295   9491  11483  -2502  -1005   -135       C\\nATOM     68  CG  LEU A  44       1.048  -3.125  -3.207  1.00 86.61           C\\nANISOU   68  CG  LEU A  44    12129   9496  11281  -2230   -831    -46       C\\nATOM     69  CD1 LEU A  44       1.618  -3.719  -1.930  1.00 87.91           C\\nANISOU   69  CD1 LEU A  44    12554   9391  11458  -2363   -905    175       C\\nATOM     70  CD2 LEU A  44       2.164  -2.764  -4.177  1.00 83.34           C\\nANISOU   70  CD2 LEU A  44    11712   9091  10864  -1783   -849   -246       C\\nATOM     71  N   ILE A  45      -2.611  -2.400  -3.356  1.00 82.86           N\\nANISOU   71  N   ILE A  45    10974   9766  10745  -2965   -594    -59       N\\nATOM     72  CA  ILE A  45      -3.287  -1.172  -2.940  1.00 83.78           C\\nANISOU   72  CA  ILE A  45    10732  10317  10784  -2961   -364    -56       C\\nATOM     73  C   ILE A  45      -4.154  -1.429  -1.715  1.00 85.75           C\\nANISOU   73  C   ILE A  45    10876  10734  10969  -3402   -243     98       C\\nATOM     74  O   ILE A  45      -4.169  -0.633  -0.767  1.00 85.46           O\\nANISOU   74  O   ILE A  45    10685  10954  10832  -3395    -44    165       O\\nATOM     75  CB  ILE A  45      -4.118  -0.594  -4.101  1.00 80.09           C\\nANISOU   75  CB  ILE A  45     9986  10096  10350  -2847   -391   -260       C\\nATOM     76  CG1 ILE A  45      -3.232  -0.296  -5.309  1.00 82.72           C\\nANISOU   76  CG1 ILE A  45    10426  10322  10681  -2446   -492   -386       C\\nATOM     77  CG2 ILE A  45      -4.845   0.666  -3.657  1.00 71.03           C\\nANISOU   77  CG2 ILE A  45     8464   9363   9163  -2807   -205   -292       C\\nATOM     78  CD1 ILE A  45      -3.998   0.221  -6.511  1.00 85.25           C\\nANISOU   78  CD1 ILE A  45    10525  10865  11002  -2340   -563   -559       C\\nATOM     79  N   ALA A  46      -4.887  -2.544  -1.711  1.00 89.24           N\\nANISOU   79  N   ALA A  46    11398  11053  11455  -3812   -363    150       N\\nATOM     80  CA  ALA A  46      -5.719  -2.875  -0.560  1.00 84.99           C\\nANISOU   80  CA  ALA A  46    10762  10712  10819  -4309   -240    325       C\\nATOM     81  C   ALA A  46      -4.868  -3.120   0.678  1.00 86.02           C\\nANISOU   81  C   ALA A  46    11172  10680  10833  -4395   -199    583       C\\nATOM     82  O   ALA A  46      -5.201  -2.653   1.773  1.00 82.61           O\\nANISOU   82  O   ALA A  46    10575  10580  10232  -4584     19    688       O\\nATOM     83  CB  ALA A  46      -6.581  -4.096  -0.869  1.00 77.37           C\\nANISOU   83  CB  ALA A  46     9868   9590   9938  -4771   -418    360       C\\nATOM     84  N   VAL A  47      -3.758  -3.841   0.522  1.00 84.11           N\\nANISOU   84  N   VAL A  47    11343   9946  10669  -4238   -419    662       N\\nATOM     85  CA  VAL A  47      -2.894  -4.117   1.664  1.00 83.65           C\\nANISOU   85  CA  VAL A  47    11575   9696  10512  -4292   -436    908       C\\nATOM     86  C   VAL A  47      -2.272  -2.829   2.191  1.00 82.63           C\\nANISOU   86  C   VAL A  47    11279   9847  10269  -3948   -212    871       C\\nATOM     87  O   VAL A  47      -2.139  -2.644   3.406  1.00 89.41           O\\nANISOU   87  O   VAL A  47    12171  10845  10957  -4107    -91   1051       O\\nATOM     88  CB  VAL A  47      -1.826  -5.156   1.281  1.00 85.45           C\\nANISOU   88  CB  VAL A  47    12252   9322  10892  -4129   -768    941       C\\nATOM     89  CG1 VAL A  47      -0.873  -5.397   2.438  1.00 84.04           C\\nANISOU   89  CG1 VAL A  47    12375   8931  10627  -4135   -829   1190       C\\nATOM     90  CG2 VAL A  47      -2.490  -6.457   0.863  1.00 89.97           C\\nANISOU   90  CG2 VAL A  47    13015   9574  11594  -4506  -1029    979       C\\nATOM     91  N   ILE A  48      -1.893  -1.915   1.294  1.00 78.76           N\\nANISOU   91  N   ILE A  48    10618   9450   9859  -3495   -165    645       N\\nATOM     92  CA  ILE A  48      -1.320  -0.643   1.730  1.00 77.79           C\\nANISOU   92  CA  ILE A  48    10338   9559   9659  -3180     16    603       C\\nATOM     93  C   ILE A  48      -2.344   0.158   2.522  1.00 82.81           C\\nANISOU   93  C   ILE A  48    10623  10681  10158  -3375    261    582       C\\nATOM     94  O   ILE A  48      -2.025   0.749   3.560  1.00 85.46           O\\nANISOU   94  O   ILE A  48    10924  11187  10359  -3347    400    647       O\\nATOM     95  CB  ILE A  48      -0.797   0.158   0.525  1.00 76.69           C\\nANISOU   95  CB  ILE A  48    10090   9420   9628  -2722     -7    395       C\\nATOM     96  CG1 ILE A  48       0.350  -0.582  -0.162  1.00 81.09           C\\nANISOU   96  CG1 ILE A  48    10957   9571  10283  -2498   -216    373       C\\nATOM     97  CG2 ILE A  48      -0.339   1.535   0.969  1.00 73.83           C\\nANISOU   97  CG2 ILE A  48     9552   9290   9212  -2449    157    360       C\\nATOM     98  CD1 ILE A  48       0.859   0.105  -1.411  1.00 83.26           C\\nANISOU   98  CD1 ILE A  48    11128   9896  10613  -2110   -227    183       C\\nATOM     99  N   VAL A  49      -3.590   0.189   2.047  1.00 85.62           N\\nANISOU   99  N   VAL A  49    10696  11290  10545  -3560    309    458       N\\nATOM    100  CA  VAL A  49      -4.628   0.950   2.736  1.00 86.41           C\\nANISOU  100  CA  VAL A  49    10399  11901  10530  -3713    539    369       C\\nATOM    101  C   VAL A  49      -5.028   0.256   4.033  1.00 86.76           C\\nANISOU  101  C   VAL A  49    10505  12094  10367  -4215    646    582       C\\nATOM    102  O   VAL A  49      -5.154   0.896   5.083  1.00 84.97           O\\nANISOU  102  O   VAL A  49    10110  12216   9958  -4262    848    578       O\\nATOM    103  CB  VAL A  49      -5.837   1.166   1.811  1.00 85.12           C\\nANISOU  103  CB  VAL A  49     9887  11980  10477  -3747    531    151       C\\nATOM    104  CG1 VAL A  49      -7.004   1.745   2.592  1.00 88.42           C\\nANISOU  104  CG1 VAL A  49     9863  12953  10781  -3956    756     30       C\\nATOM    105  CG2 VAL A  49      -5.456   2.084   0.662  1.00 80.88           C\\nANISOU  105  CG2 VAL A  49     9274  11370  10087  -3251    439    -34       C\\nATOM    106  N   PHE A  50      -5.229  -1.063   3.980  1.00 87.95           N\\nANISOU  106  N   PHE A  50    10908  11980  10529  -4611    497    773       N\\nATOM    107  CA  PHE A  50      -5.635  -1.794   5.177  1.00 89.88           C\\nANISOU  107  CA  PHE A  50    11255  12333  10561  -5041    554   1009       C\\nATOM    108  C   PHE A  50      -4.604  -1.654   6.289  1.00 92.06           C\\nANISOU  108  C   PHE A  50    11792  12524  10663  -4962    580   1197       C\\nATOM    109  O   PHE A  50      -4.957  -1.394   7.445  1.00 93.62           O\\nANISOU  109  O   PHE A  50    11871  13085  10613  -5087    752   1242       O\\nATOM    110  CB  PHE A  50      -5.857  -3.269   4.846  1.00 88.37           C\\nANISOU  110  CB  PHE A  50    11370  11743  10463  -5313    300   1176       C\\nATOM    111  CG  PHE A  50      -6.166  -4.119   6.048  1.00 91.54           C\\nANISOU  111  CG  PHE A  50    11945  12184  10651  -5658    293   1438       C\\nATOM    112  CD1 PHE A  50      -7.465  -4.232   6.518  1.00 92.88           C\\nANISOU  112  CD1 PHE A  50    11823  12793  10672  -5976    452   1419       C\\nATOM    113  CD2 PHE A  50      -5.157  -4.805   6.708  1.00 90.81           C\\nANISOU  113  CD2 PHE A  50    12302  11702  10500  -5665    108   1698       C\\nATOM    114  CE1 PHE A  50      -7.752  -5.011   7.623  1.00 96.10           C\\nANISOU  114  CE1 PHE A  50    12394  13265  10853  -6335    441   1672       C\\nATOM    115  CE2 PHE A  50      -5.439  -5.583   7.816  1.00 94.85           C\\nANISOU  115  CE2 PHE A  50    12982  12260  10797  -6003     73   1952       C\\nATOM    116  CZ  PHE A  50      -6.737  -5.688   8.272  1.00 98.38           C\\nANISOU  116  CZ  PHE A  50    13146  13159  11074  -6358    245   1949       C\\nATOM    117  N   GLY A  51      -3.324  -1.822   5.959  1.00 89.17           N\\nANISOU  117  N   GLY A  51    11775  11692  10415  -4731    395   1283       N\\nATOM    118  CA  GLY A  51      -2.301  -1.796   6.988  1.00 84.51           C\\nANISOU  118  CA  GLY A  51    11458  10976   9676  -4664    370   1475       C\\nATOM    119  C   GLY A  51      -2.075  -0.415   7.573  1.00 79.23           C\\nANISOU  119  C   GLY A  51    10517  10705   8881  -4366    607   1313       C\\nATOM    120  O   GLY A  51      -1.800  -0.278   8.767  1.00 79.21           O\\nANISOU  120  O   GLY A  51    10593  10866   8639  -4497    694   1454       O\\nATOM    121  N   ASN A  52      -2.183   0.626   6.746  1.00 74.87           N\\nANISOU  121  N   ASN A  52     9661  10300   8487  -3969    686   1017       N\\nATOM    122  CA  ASN A  52      -1.869   1.971   7.213  1.00 72.04           C\\nANISOU  122  CA  ASN A  52     9081  10223   8066  -3641    847    847       C\\nATOM    123  C   ASN A  52      -3.057   2.680   7.841  1.00 76.56           C\\nANISOU  123  C   ASN A  52     9223  11393   8475  -3813   1107    674       C\\nATOM    124  O   ASN A  52      -2.860   3.566   8.681  1.00 76.05           O\\nANISOU  124  O   ASN A  52     9026  11599   8272  -3672   1243    574       O\\nATOM    125  CB  ASN A  52      -1.305   2.809   6.069  1.00 68.61           C\\nANISOU  125  CB  ASN A  52     8565   9624   7879  -3132    768    642       C\\nATOM    126  CG  ASN A  52       0.113   2.416   5.715  1.00 79.96           C\\nANISOU  126  CG  ASN A  52    10362  10592   9427  -2882    569    754       C\\nATOM    127  OD1 ASN A  52       1.065   2.835   6.370  1.00 77.35           O\\nANISOU  127  OD1 ASN A  52    10144  10206   9041  -2704    566    802       O\\nATOM    128  ND2 ASN A  52       0.261   1.600   4.681  1.00 80.13           N\\nANISOU  128  ND2 ASN A  52    10547  10294   9604  -2861    393    767       N\\nATOM    129  N   VAL A  53      -4.286   2.318   7.468  1.00 82.38           N\\nANISOU  129  N   VAL A  53     9715  12360   9224  -4106   1170    606       N\\nATOM    130  CA  VAL A  53      -5.441   2.817   8.209  1.00 86.81           C\\nANISOU  130  CA  VAL A  53     9853  13535   9597  -4309   1419    435       C\\nATOM    131  C   VAL A  53      -5.398   2.300   9.643  1.00 91.28           C\\nANISOU  131  C   VAL A  53    10607  14230   9845  -4566   1474    633       C\\nATOM    132  O   VAL A  53      -5.768   3.009  10.588  1.00 98.44           O\\nANISOU  132  O   VAL A  53    11273  15582  10548  -4528   1653    471       O\\nATOM    133  CB  VAL A  53      -6.751   2.433   7.494  1.00 83.17           C\\nANISOU  133  CB  VAL A  53     9126  13231   9243  -4473   1406    307       C\\nATOM    134  CG1 VAL A  53      -7.949   2.691   8.387  1.00 78.74           C\\nANISOU  134  CG1 VAL A  53     8217  13227   8475  -4616   1596    143       C\\nATOM    135  CG2 VAL A  53      -6.893   3.217   6.198  1.00 79.84           C\\nANISOU  135  CG2 VAL A  53     8453  12777   9107  -4129   1341     45       C\\nATOM    136  N   LEU A  54      -4.923   1.065   9.827  1.00 86.53           N\\nANISOU  136  N   LEU A  54    10442  13233   9201  -4813   1292    968       N\\nATOM    137  CA  LEU A  54      -4.726   0.529  11.172  1.00 88.26           C\\nANISOU  137  CA  LEU A  54    10891  13520   9123  -5054   1288   1196       C\\nATOM    138  C   LEU A  54      -3.747   1.383  11.968  1.00 86.94           C\\nANISOU  138  C   LEU A  54    10787  13428   8817  -4810   1356   1171       C\\nATOM    139  O   LEU A  54      -4.002   1.722  13.130  1.00 94.33           O\\nANISOU  139  O   LEU A  54    11611  14759   9469  -4901   1496   1127       O\\nATOM    140  CB  LEU A  54      -4.224  -0.914  11.097  1.00 90.28           C\\nANISOU  140  CB  LEU A  54    11637  13240   9427  -5281   1006   1548       C\\nATOM    141  CG  LEU A  54      -5.198  -2.030  10.729  1.00 92.89           C\\nANISOU  141  CG  LEU A  54    11990  13500   9806  -5638    909   1650       C\\nATOM    142  CD1 LEU A  54      -4.459  -3.354  10.614  1.00 97.20           C\\nANISOU  142  CD1 LEU A  54    13055  13428  10449  -5757    575   1961       C\\nATOM    143  CD2 LEU A  54      -6.301  -2.128  11.763  1.00 96.43           C\\nANISOU  143  CD2 LEU A  54    12213  14478   9948  -5990   1090   1654       C\\nATOM    144  N   VAL A  55      -2.613   1.737  11.356  1.00 84.36           N\\nANISOU  144  N   VAL A  55    10638  12737   8678  -4508   1252   1188       N\\nATOM    145  CA  VAL A  55      -1.593   2.518  12.053  1.00 89.47           C\\nANISOU  145  CA  VAL A  55    11371  13417   9208  -4276   1291   1178       C\\nATOM    146  C   VAL A  55      -2.164   3.838  12.551  1.00 92.31           C\\nANISOU  146  C   VAL A  55    11279  14347   9446  -4112   1550    831       C\\nATOM    147  O   VAL A  55      -1.801   4.314  13.634  1.00 95.44           O\\nANISOU  147  O   VAL A  55    11689  14966   9606  -4066   1624    802       O\\nATOM    148  CB  VAL A  55      -0.374   2.741  11.133  1.00 85.96           C\\nANISOU  148  CB  VAL A  55    11134  12447   9082  -3803   1074   1151       C\\nATOM    149  CG1 VAL A  55       0.679   3.587  11.829  1.00 76.85           C\\nANISOU  149  CG1 VAL A  55    10045  11292   7864  -3476   1063   1092       C\\nATOM    150  CG2 VAL A  55       0.217   1.408  10.697  1.00 86.37           C\\nANISOU  150  CG2 VAL A  55    11619  11948   9251  -3934    799   1439       C\\nATOM    151  N   CYS A  56      -3.075   4.442  11.786  1.00 85.56           N\\nANISOU  151  N   CYS A  56    10018  13731   8759  -3998   1660    538       N\\nATOM    152  CA  CYS A  56      -3.627   5.737  12.175  1.00 80.56           C\\nANISOU  152  CA  CYS A  56     8941  13592   8075  -3762   1850    148       C\\nATOM    153  C   CYS A  56      -4.603   5.598  13.334  1.00 86.48           C\\nANISOU  153  C   CYS A  56     9514  14821   8522  -4005   1984     66       C\\nATOM    154  O   CYS A  56      -4.495   6.313  14.337  1.00 84.77           O\\nANISOU  154  O   CYS A  56     9186  14923   8102  -3899   2089   -102       O\\nATOM    155  CB  CYS A  56      -4.301   6.398  10.975  1.00 67.26           C\\nANISOU  155  CB  CYS A  56     6920  11917   6720  -3468   1818   -150       C\\nATOM    156  SG  CYS A  56      -3.139   6.859   9.688  1.00 71.11           S\\nANISOU  156  SG  CYS A  56     7652  11761   7605  -2939   1540   -134       S\\nATOM    157  N   MET A  57      -5.565   4.680  13.217  1.00 89.30           N\\nANISOU  157  N   MET A  57     9839  15250   8838  -4343   1978    170       N\\nATOM    158  CA  MET A  57      -6.547   4.508  14.283  1.00 99.11           C\\nANISOU  158  CA  MET A  57    10893  16987   9777  -4621   2115     99       C\\nATOM    159  C   MET A  57      -5.891   4.028  15.570  1.00100.31           C\\nANISOU  159  C   MET A  57    11370  17145   9601  -4843   2094    365       C\\nATOM    160  O   MET A  57      -6.282   4.448  16.665  1.00109.98           O\\nANISOU  160  O   MET A  57    12410  18838  10541  -4909   2235    210       O\\nATOM    161  CB  MET A  57      -7.633   3.529  13.845  1.00106.16           C\\nANISOU  161  CB  MET A  57    11719  17920  10695  -4975   2095    198       C\\nATOM    162  CG  MET A  57      -8.458   4.012  12.672  1.00104.93           C\\nANISOU  162  CG  MET A  57    11195  17843  10830  -4777   2113    -94       C\\nATOM    163  SD  MET A  57      -9.729   2.811  12.239  1.00106.23           S\\nANISOU  163  SD  MET A  57    11291  18073  11000  -5226   2085     28       S\\nATOM    164  CE  MET A  57      -8.718   1.360  11.965  1.00104.77           C\\nANISOU  164  CE  MET A  57    11736  17203  10870  -5491   1838    545       C\\nATOM    165  N   ALA A  58      -4.891   3.151  15.458  1.00 91.70           N\\nANISOU  165  N   ALA A  58    10761  15535   8547  -4945   1896    749       N\\nATOM    166  CA  ALA A  58      -4.253   2.590  16.647  1.00 94.86           C\\nANISOU  166  CA  ALA A  58    11502  15887   8653  -5159   1819   1033       C\\nATOM    167  C   ALA A  58      -3.578   3.673  17.478  1.00 93.98           C\\nANISOU  167  C   ALA A  58    11323  16005   8380  -4887   1912    851       C\\nATOM    168  O   ALA A  58      -3.795   3.769  18.691  1.00 97.13           O\\nANISOU  168  O   ALA A  58    11671  16787   8447  -5049   2002    828       O\\nATOM    169  CB  ALA A  58      -3.240   1.521  16.244  1.00 92.30           C\\nANISOU  169  CB  ALA A  58    11700  14899   8471  -5223   1532   1429       C\\nATOM    170  N   VAL A  59      -2.740   4.492  16.841  1.00 96.30           N\\nANISOU  170  N   VAL A  59    11619  16077   8895  -4483   1883    717       N\\nATOM    171  CA  VAL A  59      -2.102   5.595  17.551  1.00 91.92           C\\nANISOU  171  CA  VAL A  59    10983  15733   8211  -4197   1959    504       C\\nATOM    172  C   VAL A  59      -3.144   6.585  18.045  1.00 91.74           C\\nANISOU  172  C   VAL A  59    10460  16322   8077  -4097   2177     56       C\\nATOM    173  O   VAL A  59      -2.990   7.184  19.117  1.00 99.07           O\\nANISOU  173  O   VAL A  59    11313  17573   8756  -4030   2251   -105       O\\nATOM    174  CB  VAL A  59      -1.062   6.271  16.638  1.00 84.96           C\\nANISOU  174  CB  VAL A  59    10179  14491   7608  -3805   1881    441       C\\nATOM    175  CG1 VAL A  59      -0.446   7.484  17.318  1.00 88.37           C\\nANISOU  175  CG1 VAL A  59    10505  15150   7923  -3491   1949    173       C\\nATOM    176  CG2 VAL A  59       0.009   5.267  16.235  1.00 77.23           C\\nANISOU  176  CG2 VAL A  59     9704  12913   6729  -3889   1637    864       C\\nATOM    177  N   SER A  60      -4.229   6.759  17.291  1.00 95.26           N\\nANISOU  177  N   SER A  60    10557  16933   8706  -4072   2257   -169       N\\nATOM    178  CA  SER A  60      -5.247   7.733  17.658  1.00 98.05           C\\nANISOU  178  CA  SER A  60    10416  17831   9007  -3917   2417   -638       C\\nATOM    179  C   SER A  60      -6.057   7.307  18.875  1.00104.36           C\\nANISOU  179  C   SER A  60    11113  19121   9420  -4286   2535   -633       C\\nATOM    180  O   SER A  60      -6.732   8.148  19.479  1.00107.43           O\\nANISOU  180  O   SER A  60    11125  20003   9691  -4157   2661  -1033       O\\nATOM    181  CB  SER A  60      -6.183   7.974  16.473  1.00 97.14           C\\nANISOU  181  CB  SER A  60     9973  17730   9205  -3784   2427   -864       C\\nATOM    182  OG  SER A  60      -7.148   8.967  16.770  1.00 99.99           O\\nANISOU  182  OG  SER A  60     9859  18573   9559  -3574   2531  -1349       O\\nATOM    183  N   ARG A  61      -6.003   6.030  19.255  1.00 98.78           N\\nANISOU  183  N   ARG A  61    10729  18286   8518  -4738   2478   -202       N\\nATOM    184  CA  ARG A  61      -6.880   5.512  20.291  1.00103.46           C\\nANISOU  184  CA  ARG A  61    11212  19353   8745  -5156   2589   -162       C\\nATOM    185  C   ARG A  61      -6.159   4.772  21.410  1.00107.55           C\\nANISOU  185  C   ARG A  61    12131  19803   8928  -5464   2513    219       C\\nATOM    186  O   ARG A  61      -6.808   4.395  22.392  1.00117.52           O\\nANISOU  186  O   ARG A  61    13311  21498   9842  -5828   2609    262       O\\nATOM    187  CB  ARG A  61      -7.937   4.590  19.664  1.00104.53           C\\nANISOU  187  CB  ARG A  61    11265  19502   8951  -5497   2593    -37       C\\nATOM    188  CG  ARG A  61      -8.730   5.267  18.557  1.00 96.67           C\\nANISOU  188  CG  ARG A  61     9865  18588   8277  -5209   2647   -407       C\\nATOM    189  CD  ARG A  61     -10.016   4.534  18.248  1.00108.57           C\\nANISOU  189  CD  ARG A  61    11174  20320   9758  -5564   2702   -387       C\\nATOM    190  NE  ARG A  61      -9.801   3.362  17.409  1.00109.71           N\\nANISOU  190  NE  ARG A  61    11662  19943  10079  -5797   2536     11       N\\nATOM    191  CZ  ARG A  61     -10.778   2.566  16.987  1.00115.93           C\\nANISOU  191  CZ  ARG A  61    12357  20800  10890  -6123   2537     93       C\\nATOM    192  NH1 ARG A  61     -12.034   2.820  17.330  1.00116.46           N\\nANISOU  192  NH1 ARG A  61    11988  21459  10801  -6264   2710   -185       N\\nATOM    193  NH2 ARG A  61     -10.501   1.519  16.223  1.00119.11           N\\nANISOU  193  NH2 ARG A  61    13096  20686  11475  -6303   2354    434       N\\nATOM    194  N   GLU A  62      -4.853   4.558  21.301  1.00 96.97           N\\nANISOU  194  N   GLU A  62    11215  17953   7675  -5333   2333    491       N\\nATOM    195  CA  GLU A  62      -4.083   3.859  22.320  1.00101.43           C\\nANISOU  195  CA  GLU A  62    12192  18393   7956  -5580   2207    858       C\\nATOM    196  C   GLU A  62      -3.184   4.851  23.046  1.00102.22           C\\nANISOU  196  C   GLU A  62    12307  18603   7928  -5257   2227    678       C\\nATOM    197  O   GLU A  62      -2.426   5.591  22.409  1.00 92.57           O\\nANISOU  197  O   GLU A  62    11100  17116   6955  -4842   2178    531       O\\nATOM    198  CB  GLU A  62      -3.246   2.737  21.703  1.00100.84           C\\nANISOU  198  CB  GLU A  62    12621  17618   8074  -5678   1928   1315       C\\nATOM    199  N   LYS A  63      -3.269   4.854  24.378  1.00108.00           N\\nANISOU  199  N   LYS A  63    13040  19738   8259  -5463   2293    691       N\\nATOM    200  CA  LYS A  63      -2.467   5.770  25.183  1.00106.16           C\\nANISOU  200  CA  LYS A  63    12820  19652   7864  -5180   2305    504       C\\nATOM    201  C   LYS A  63      -0.976   5.535  24.970  1.00 98.83           C\\nANISOU  201  C   LYS A  63    12367  18125   7059  -4996   2054    800       C\\nATOM    202  O   LYS A  63      -0.243   6.439  24.552  1.00 90.24           O\\nANISOU  202  O   LYS A  63    11250  16879   6157  -4571   2024    584       O\\nATOM    203  CB  LYS A  63      -2.833   5.616  26.660  1.00114.28           C\\nANISOU  203  CB  LYS A  63    13807  21206   8408  -5502   2401    526       C\\nATOM    204  N   ALA A  64      -0.510   4.312  25.239  1.00108.15           N\\nANISOU  204  N   ALA A  64    13988  18956   8148  -5308   1844   1286       N\\nATOM    205  CA  ALA A  64       0.917   4.011  25.200  1.00103.75           C\\nANISOU  205  CA  ALA A  64    13892  17853   7678  -5142   1563   1569       C\\nATOM    206  C   ALA A  64       1.513   4.169  23.805  1.00 99.33           C\\nANISOU  206  C   ALA A  64    13405  16779   7558  -4812   1452   1552       C\\nATOM    207  O   ALA A  64       2.735   4.041  23.649  1.00 84.58           O\\nANISOU  207  O   ALA A  64    11875  14464   5799  -4615   1215   1732       O\\nATOM    208  CB  ALA A  64       1.164   2.590  25.719  1.00103.60           C\\nANISOU  208  CB  ALA A  64    14310  17538   7516  -5540   1320   2073       C\\nATOM    209  N   LEU A  65       0.685   4.450  22.798  1.00 91.85           N\\nANISOU  209  N   LEU A  65    12140  15902   6858  -4745   1606   1334       N\\nATOM    210  CA  LEU A  65       1.126   4.676  21.429  1.00 92.45           C\\nANISOU  210  CA  LEU A  65    12233  15560   7334  -4450   1535   1288       C\\nATOM    211  C   LEU A  65       1.071   6.143  21.021  1.00 91.55           C\\nANISOU  211  C   LEU A  65    11741  15700   7344  -4047   1715    824       C\\nATOM    212  O   LEU A  65       1.216   6.447  19.835  1.00 98.95           O\\nANISOU  212  O   LEU A  65    12606  16387   8603  -3825   1705    736       O\\nATOM    213  CB  LEU A  65       0.282   3.842  20.465  1.00 91.67           C\\nANISOU  213  CB  LEU A  65    12087  15284   7459  -4662   1529   1402       C\\nATOM    214  CG  LEU A  65       0.533   2.337  20.472  1.00 96.52           C\\nANISOU  214  CG  LEU A  65    13133  15448   8091  -4973   1266   1854       C\\nATOM    215  CD1 LEU A  65      -0.389   1.627  19.490  1.00101.66           C\\nANISOU  215  CD1 LEU A  65    13694  15972   8962  -5162   1269   1895       C\\nATOM    216  CD2 LEU A  65       1.987   2.059  20.143  1.00 88.49           C\\nANISOU  216  CD2 LEU A  65    12531  13837   7256  -4733    974   2071       C\\nATOM    217  N   GLN A  66       0.870   7.056  21.966  1.00 97.64           N\\nANISOU  217  N   GLN A  66    12271  16951   7878  -3940   1858    509       N\\nATOM    218  CA  GLN A  66       0.729   8.476  21.643  1.00 91.59           C\\nANISOU  218  CA  GLN A  66    11125  16421   7256  -3531   1991      9       C\\nATOM    219  C   GLN A  66       2.014   9.220  22.003  1.00 88.27           C\\nANISOU  219  C   GLN A  66    10883  15873   6783  -3219   1872    -76       C\\nATOM    220  O   GLN A  66       2.081  10.015  22.940  1.00 95.43           O\\nANISOU  220  O   GLN A  66    11654  17116   7488  -3077   1921   -364       O\\nATOM    221  CB  GLN A  66      -0.488   9.060  22.354  1.00 94.21           C\\nANISOU  221  CB  GLN A  66    11011  17366   7418  -3569   2200   -377       C\\nATOM    222  CG  GLN A  66      -1.806   8.615  21.747  1.00 90.38           C\\nANISOU  222  CG  GLN A  66    10255  17032   7053  -3778   2313   -412       C\\nATOM    223  CD  GLN A  66      -3.010   9.067  22.544  1.00 98.45           C\\nANISOU  223  CD  GLN A  66    10853  18690   7865  -3861   2497   -767       C\\nATOM    224  OE1 GLN A  66      -2.887   9.506  23.689  1.00102.35           O\\nANISOU  224  OE1 GLN A  66    11295  19524   8070  -3847   2548   -921       O\\nATOM    225  NE2 GLN A  66      -4.187   8.960  21.941  1.00101.41           N\\nANISOU  225  NE2 GLN A  66    10914  19243   8376  -3945   2588   -913       N\\nATOM    226  N   THR A  67       3.049   8.942  21.221  1.00 81.40           N\\nANISOU  226  N   THR A  67    10313  14420   6193  -3058   1648    159       N\\nATOM    227  CA  THR A  67       4.366   9.523  21.416  1.00 80.16           C\\nANISOU  227  CA  THR A  67    10341  13928   6189  -2690   1412    112       C\\nATOM    228  C   THR A  67       4.724  10.396  20.219  1.00 81.81           C\\nANISOU  228  C   THR A  67    10385  13739   6959  -2223   1303   -122       C\\nATOM    229  O   THR A  67       4.047  10.388  19.187  1.00 83.11           O\\nANISOU  229  O   THR A  67    10366  13821   7392  -2189   1372   -182       O\\nATOM    230  CB  THR A  67       5.424   8.430  21.618  1.00 74.28           C\\nANISOU  230  CB  THR A  67    10089  12752   5384  -2838   1150    588       C\\nATOM    231  OG1 THR A  67       5.732   7.823  20.359  1.00 77.15           O\\nANISOU  231  OG1 THR A  67    10579  12565   6169  -2749   1000    784       O\\nATOM    232  CG2 THR A  67       4.909   7.358  22.566  1.00 76.90           C\\nANISOU  232  CG2 THR A  67    10631  13398   5190  -3391   1228    928       C\\nATOM    233  N   THR A  68       5.803  11.165  20.370  1.00 86.60           N\\nANISOU  233  N   THR A  68    11062  14111   7731  -1884   1119   -244       N\\nATOM    234  CA  THR A  68       6.274  11.984  19.259  1.00 81.90           C\\nANISOU  234  CA  THR A  68    10353  13120   7646  -1492    990   -405       C\\nATOM    235  C   THR A  68       6.614  11.116  18.055  1.00 76.38           C\\nANISOU  235  C   THR A  68     9828  11956   7236  -1519    883    -94       C\\nATOM    236  O   THR A  68       6.157  11.379  16.939  1.00 74.99           O\\nANISOU  236  O   THR A  68     9479  11652   7360  -1401    915   -182       O\\nATOM    237  CB  THR A  68       7.490  12.816  19.681  1.00 80.77           C\\nANISOU  237  CB  THR A  68    10291  12786   7611  -1198    788   -526       C\\nATOM    238  OG1 THR A  68       8.582  11.948  20.014  1.00 75.97           O\\nANISOU  238  OG1 THR A  68    10037  11917   6911  -1290    604   -182       O\\nATOM    239  CG2 THR A  68       7.155  13.692  20.878  1.00 83.25           C\\nANISOU  239  CG2 THR A  68    10436  13561   7636  -1147    872   -884       C\\nATOM    240  N   THR A  69       7.412  10.066  18.270  1.00 78.37           N\\nANISOU  240  N   THR A  69    10426  11955   7395  -1662    733    255       N\\nATOM    241  CA  THR A  69       7.811   9.195  17.168  1.00 78.88           C\\nANISOU  241  CA  THR A  69    10662  11578   7732  -1656    605    503       C\\nATOM    242  C   THR A  69       6.596   8.584  16.482  1.00 78.27           C\\nANISOU  242  C   THR A  69    10482  11594   7664  -1890    759    558       C\\nATOM    243  O   THR A  69       6.522   8.550  15.247  1.00 73.15           O\\nANISOU  243  O   THR A  69     9763  10702   7330  -1761    732    539       O\\nATOM    244  CB  THR A  69       8.748   8.097  17.676  1.00 76.37           C\\nANISOU  244  CB  THR A  69    10733  11000   7285  -1777    388    839       C\\nATOM    245  OG1 THR A  69       9.982   8.680  18.112  1.00 72.19           O\\nANISOU  245  OG1 THR A  69    10268  10338   6821  -1513    212    771       O\\nATOM    246  CG2 THR A  69       9.035   7.083  16.582  1.00 74.02           C\\nANISOU  246  CG2 THR A  69    10604  10273   7247  -1776    252   1050       C\\nATOM    247  N   ASN A  70       5.625   8.114  17.269  1.00 82.86           N\\nANISOU  247  N   ASN A  70    11039  12561   7884  -2256    925    618       N\\nATOM    248  CA  ASN A  70       4.436   7.496  16.698  1.00 81.91           C\\nANISOU  248  CA  ASN A  70    10800  12565   7757  -2530   1069    672       C\\nATOM    249  C   ASN A  70       3.562   8.494  15.947  1.00 81.00           C\\nANISOU  249  C   ASN A  70    10269  12649   7860  -2327   1221    314       C\\nATOM    250  O   ASN A  70       2.805   8.084  15.063  1.00 74.10           O\\nANISOU  250  O   ASN A  70     9290  11736   7128  -2431   1271    335       O\\nATOM    251  CB  ASN A  70       3.629   6.801  17.798  1.00 79.20           C\\nANISOU  251  CB  ASN A  70    10505  12647   6942  -3020   1221    832       C\\nATOM    252  CG  ASN A  70       4.333   5.581  18.348  1.00 78.28           C\\nANISOU  252  CG  ASN A  70    10856  12250   6638  -3286   1014   1268       C\\nATOM    253  OD1 ASN A  70       5.224   5.030  17.706  1.00 74.09           O\\nANISOU  253  OD1 ASN A  70    10588  11183   6379  -3127    762   1443       O\\nATOM    254  ND2 ASN A  70       3.941   5.152  19.542  1.00 73.15           N\\nANISOU  254  ND2 ASN A  70    10308  11972   5512  -3692   1103   1439       N\\nATOM    255  N   TYR A  71       3.640   9.786  16.274  1.00 84.07           N\\nANISOU  255  N   TYR A  71    10427  13227   8291  -2033   1261    -20       N\\nATOM    256  CA  TYR A  71       2.933  10.782  15.475  1.00 77.80           C\\nANISOU  256  CA  TYR A  71     9275  12516   7768  -1780   1321   -352       C\\nATOM    257  C   TYR A  71       3.632  11.001  14.143  1.00 70.85           C\\nANISOU  257  C   TYR A  71     8477  11134   7310  -1497   1135   -290       C\\nATOM    258  O   TYR A  71       2.978  11.216  13.117  1.00 65.56           O\\nANISOU  258  O   TYR A  71     7626  10422   6864  -1416   1148   -386       O\\nATOM    259  CB  TYR A  71       2.809  12.094  16.246  1.00 74.68           C\\nANISOU  259  CB  TYR A  71     8632  12431   7314  -1540   1370   -746       C\\nATOM    260  CG  TYR A  71       1.783  12.035  17.350  1.00 80.29           C\\nANISOU  260  CG  TYR A  71     9123  13772   7611  -1796   1612   -924       C\\nATOM    261  CD1 TYR A  71       0.690  11.189  17.253  1.00 82.22           C\\nANISOU  261  CD1 TYR A  71     9248  14311   7681  -2164   1796   -825       C\\nATOM    262  CD2 TYR A  71       1.912  12.814  18.492  1.00 84.10           C\\nANISOU  262  CD2 TYR A  71     9504  14589   7861  -1688   1658  -1202       C\\nATOM    263  CE1 TYR A  71      -0.250  11.123  18.258  1.00 91.89           C\\nANISOU  263  CE1 TYR A  71    10236  16183   8495  -2441   2045   -986       C\\nATOM    264  CE2 TYR A  71       0.976  12.756  19.503  1.00 85.39           C\\nANISOU  264  CE2 TYR A  71     9439  15406   7599  -1932   1905  -1392       C\\nATOM    265  CZ  TYR A  71      -0.103  11.907  19.381  1.00 94.33           C\\nANISOU  265  CZ  TYR A  71    10434  16859   8548  -2320   2110  -1275       C\\nATOM    266  OH  TYR A  71      -1.045  11.839  20.381  1.00 99.85           O\\nANISOU  266  OH  TYR A  71    10911  18103   8926  -2541   2275  -1429       O\\nATOM    267  N   LEU A  72       4.963  10.950  14.139  1.00 66.28           N\\nANISOU  267  N   LEU A  72     8155  10205   6825  -1355    960   -134       N\\nATOM    268  CA  LEU A  72       5.688  10.938  12.880  1.00 65.47           C\\nANISOU  268  CA  LEU A  72     8142   9678   7057  -1158    810    -34       C\\nATOM    269  C   LEU A  72       5.520   9.612  12.156  1.00 66.26           C\\nANISOU  269  C   LEU A  72     8411   9590   7173  -1363    790    218       C\\nATOM    270  O   LEU A  72       5.755   9.545  10.947  1.00 70.26           O\\nANISOU  270  O   LEU A  72     8925   9843   7928  -1232    713    248       O\\nATOM    271  CB  LEU A  72       7.166  11.237  13.129  1.00 68.98           C\\nANISOU  271  CB  LEU A  72     8763   9860   7585   -964    640     32       C\\nATOM    272  CG  LEU A  72       7.464  12.668  13.586  1.00 71.02           C\\nANISOU  272  CG  LEU A  72     8861  10200   7924   -721    600   -231       C\\nATOM    273  CD1 LEU A  72       8.795  12.745  14.308  1.00 68.45           C\\nANISOU  273  CD1 LEU A  72     8719   9732   7557   -638    454   -157       C\\nATOM    274  CD2 LEU A  72       7.449  13.618  12.399  1.00 69.98           C\\nANISOU  274  CD2 LEU A  72     8565   9884   8138   -488    531   -351       C\\nATOM    275  N   ILE A  73       5.112   8.562  12.866  1.00 69.01           N\\nANISOU  275  N   ILE A  73     8906  10062   7254  -1697    844    397       N\\nATOM    276  CA  ILE A  73       4.844   7.288  12.214  1.00 67.68           C\\nANISOU  276  CA  ILE A  73     8907   9691   7118  -1917    795    618       C\\nATOM    277  C   ILE A  73       3.522   7.340  11.460  1.00 71.94           C\\nANISOU  277  C   ILE A  73     9183  10422   7728  -2023    929    489       C\\nATOM    278  O   ILE A  73       3.411   6.809  10.350  1.00 75.02           O\\nANISOU  278  O   ILE A  73     9617  10582   8307  -2015    856    546       O\\nATOM    279  CB  ILE A  73       4.880   6.148  13.249  1.00 69.17           C\\nANISOU  279  CB  ILE A  73     9379   9898   7006  -2275    759    894       C\\nATOM    280  CG1 ILE A  73       6.327   5.743  13.542  1.00 66.13           C\\nANISOU  280  CG1 ILE A  73     9319   9150   6659  -2128    522   1069       C\\nATOM    281  CG2 ILE A  73       4.072   4.944  12.777  1.00 68.47           C\\nANISOU  281  CG2 ILE A  73     9386   9730   6900  -2615    755   1076       C\\nATOM    282  CD1 ILE A  73       6.453   4.548  14.461  1.00 67.07           C\\nANISOU  282  CD1 ILE A  73     9782   9188   6514  -2462    402   1387       C\\nATOM    283  N   VAL A  74       2.507   7.996  12.029  1.00 70.79           N\\nANISOU  283  N   VAL A  74     8739  10720   7436  -2102   1115    280       N\\nATOM    284  CA  VAL A  74       1.244   8.128  11.308  1.00 74.58           C\\nANISOU  284  CA  VAL A  74     8921  11407   8009  -2166   1221    118       C\\nATOM    285  C   VAL A  74       1.392   9.116  10.161  1.00 73.54           C\\nANISOU  285  C   VAL A  74     8633  11099   8211  -1776   1127    -73       C\\nATOM    286  O   VAL A  74       0.708   8.995   9.137  1.00 75.63           O\\nANISOU  286  O   VAL A  74     8769  11334   8631  -1776   1112   -121       O\\nATOM    287  CB  VAL A  74       0.095   8.527  12.256  1.00 73.62           C\\nANISOU  287  CB  VAL A  74     8477  11862   7633  -2350   1446    -95       C\\nATOM    288  CG1 VAL A  74       0.133   7.692  13.523  1.00 69.23           C\\nANISOU  288  CG1 VAL A  74     8110  11512   6684  -2747   1535    127       C\\nATOM    289  CG2 VAL A  74       0.126  10.011  12.581  1.00 69.08           C\\nANISOU  289  CG2 VAL A  74     7641  11478   7130  -1988   1471   -451       C\\nATOM    290  N   SER A  75       2.276  10.106  10.306  1.00 69.43           N\\nANISOU  290  N   SER A  75     8129  10455   7797  -1464   1043   -169       N\\nATOM    291  CA  SER A  75       2.644  10.933   9.164  1.00 66.75           C\\nANISOU  291  CA  SER A  75     7729   9871   7764  -1146    912   -253       C\\nATOM    292  C   SER A  75       3.278  10.082   8.075  1.00 68.29           C\\nANISOU  292  C   SER A  75     8151   9714   8082  -1158    801    -30       C\\nATOM    293  O   SER A  75       3.025  10.291   6.882  1.00 67.91           O\\nANISOU  293  O   SER A  75     8025   9564   8214  -1048    739    -65       O\\nATOM    294  CB  SER A  75       3.595  12.044   9.605  1.00 65.59           C\\nANISOU  294  CB  SER A  75     7599   9627   7697   -876    823   -350       C\\nATOM    295  OG  SER A  75       4.148  12.722   8.492  1.00 65.64           O\\nANISOU  295  OG  SER A  75     7609   9355   7975   -636    678   -344       O\\nATOM    296  N   LEU A  76       4.099   9.107   8.470  1.00 69.61           N\\nANISOU  296  N   LEU A  76     8600   9702   8145  -1281    755    185       N\\nATOM    297  CA  LEU A  76       4.653   8.169   7.503  1.00 70.39           C\\nANISOU  297  CA  LEU A  76     8904   9490   8352  -1284    641    344       C\\nATOM    298  C   LEU A  76       3.555   7.304   6.898  1.00 71.56           C\\nANISOU  298  C   LEU A  76     9015   9685   8488  -1514    675    369       C\\nATOM    299  O   LEU A  76       3.587   6.994   5.700  1.00 67.72           O\\nANISOU  299  O   LEU A  76     8556   9030   8146  -1442    597    372       O\\nATOM    300  CB  LEU A  76       5.725   7.307   8.170  1.00 71.65           C\\nANISOU  300  CB  LEU A  76     9365   9437   8421  -1339    541    534       C\\nATOM    301  CG  LEU A  76       6.488   6.311   7.296  1.00 73.93           C\\nANISOU  301  CG  LEU A  76     9872   9386   8833  -1283    387    648       C\\nATOM    302  CD1 LEU A  76       7.050   6.993   6.057  1.00 66.82           C\\nANISOU  302  CD1 LEU A  76     8859   8395   8135  -1003    352    542       C\\nATOM    303  CD2 LEU A  76       7.598   5.643   8.104  1.00 66.32           C\\nANISOU  303  CD2 LEU A  76     9178   8218   7804  -1274    247    796       C\\nATOM    304  N   ALA A  77       2.567   6.918   7.708  1.00 76.17           N\\nANISOU  304  N   ALA A  77     9525  10531   8886  -1810    794    379       N\\nATOM    305  CA  ALA A  77       1.468   6.103   7.203  1.00 75.85           C\\nANISOU  305  CA  ALA A  77     9422  10562   8836  -2078    825    401       C\\nATOM    306  C   ALA A  77       0.603   6.875   6.217  1.00 76.40           C\\nANISOU  306  C   ALA A  77     9182  10781   9066  -1929    853    183       C\\nATOM    307  O   ALA A  77       0.034   6.277   5.295  1.00 74.94           O\\nANISOU  307  O   ALA A  77     8980  10529   8965  -2027    802    189       O\\nATOM    308  CB  ALA A  77       0.618   5.589   8.364  1.00 77.54           C\\nANISOU  308  CB  ALA A  77     9590  11086   8784  -2476    967    470       C\\nATOM    309  N   VAL A  78       0.484   8.192   6.395  1.00 72.57           N\\nANISOU  309  N   VAL A  78     8462  10479   8634  -1687    898    -17       N\\nATOM    310  CA  VAL A  78      -0.263   9.001   5.438  1.00 73.72           C\\nANISOU  310  CA  VAL A  78     8340  10714   8956  -1502    861   -213       C\\nATOM    311  C   VAL A  78       0.492   9.092   4.118  1.00 73.77           C\\nANISOU  311  C   VAL A  78     8495  10392   9143  -1286    699   -137       C\\nATOM    312  O   VAL A  78      -0.108   9.025   3.037  1.00 75.36           O\\nANISOU  312  O   VAL A  78     8606  10583   9444  -1265    631   -185       O\\nATOM    313  CB  VAL A  78      -0.556  10.391   6.030  1.00 69.67           C\\nANISOU  313  CB  VAL A  78     7563  10433   8477  -1281    899   -460       C\\nATOM    314  CG1 VAL A  78      -1.042  11.346   4.951  1.00 67.83           C\\nANISOU  314  CG1 VAL A  78     7129  10169   8475  -1016    769   -625       C\\nATOM    315  CG2 VAL A  78      -1.591  10.281   7.138  1.00 54.88           C\\nANISOU  315  CG2 VAL A  78     5447   9002   6402  -1505   1086   -609       C\\nATOM    316  N   ALA A  79       1.819   9.239   4.180  1.00 71.40           N\\nANISOU  316  N   ALA A  79     8408   9854   8865  -1136    637    -25       N\\nATOM    317  CA  ALA A  79       2.617   9.243   2.959  1.00 72.25           C\\nANISOU  317  CA  ALA A  79     8642   9715   9095   -969    515     48       C\\nATOM    318  C   ALA A  79       2.382   7.976   2.148  1.00 78.12           C\\nANISOU  318  C   ALA A  79     9512  10348   9824  -1122    472    118       C\\nATOM    319  O   ALA A  79       2.254   8.030   0.919  1.00 82.23           O\\nANISOU  319  O   ALA A  79    10005  10818  10420  -1035    394     87       O\\nATOM    320  CB  ALA A  79       4.097   9.398   3.301  1.00 67.24           C\\nANISOU  320  CB  ALA A  79     8191   8894   8464   -836    476    149       C\\nATOM    321  N   ASP A  80       2.306   6.826   2.820  1.00 70.96           N\\nANISOU  321  N   ASP A  80     8756   9392   8812  -1362    499    214       N\\nATOM    322  CA  ASP A  80       2.041   5.580   2.113  1.00 74.85           C\\nANISOU  322  CA  ASP A  80     9387   9736   9318  -1522    420    263       C\\nATOM    323  C   ASP A  80       0.578   5.468   1.707  1.00 70.40           C\\nANISOU  323  C   ASP A  80     8610   9377   8763  -1703    452    165       C\\nATOM    324  O   ASP A  80       0.275   4.919   0.641  1.00 75.04           O\\nANISOU  324  O   ASP A  80     9225   9874   9413  -1725    358    129       O\\nATOM    325  CB  ASP A  80       2.453   4.386   2.975  1.00 85.13           C\\nANISOU  325  CB  ASP A  80    10957  10859  10529  -1735    379    424       C\\nATOM    326  CG  ASP A  80       3.955   4.316   3.193  1.00 91.73           C\\nANISOU  326  CG  ASP A  80    12008  11459  11389  -1526    293    497       C\\nATOM    327  OD1 ASP A  80       4.707   4.814   2.326  1.00 90.12           O\\nANISOU  327  OD1 ASP A  80    11774  11187  11279  -1257    253    424       O\\nATOM    328  OD2 ASP A  80       4.383   3.762   4.231  1.00 93.76           O\\nANISOU  328  OD2 ASP A  80    12452  11616  11555  -1644    259    631       O\\nATOM    329  N   LEU A  81      -0.340   5.974   2.535  1.00 74.65           N\\nANISOU  329  N   LEU A  81     8912  10218   9233  -1827    580     91       N\\nATOM    330  CA  LEU A  81      -1.751   5.961   2.159  1.00 71.55           C\\nANISOU  330  CA  LEU A  81     8249  10074   8865  -1978    612    -40       C\\nATOM    331  C   LEU A  81      -2.001   6.765   0.893  1.00 74.65           C\\nANISOU  331  C   LEU A  81     8488  10471   9406  -1709    505   -178       C\\nATOM    332  O   LEU A  81      -2.886   6.418   0.105  1.00 69.21           O\\nANISOU  332  O   LEU A  81     7680   9851   8766  -1803    444   -254       O\\nATOM    333  CB  LEU A  81      -2.611   6.504   3.297  1.00 69.87           C\\nANISOU  333  CB  LEU A  81     7752  10250   8545  -2106    782   -153       C\\nATOM    334  CG  LEU A  81      -3.075   5.485   4.331  1.00 74.99           C\\nANISOU  334  CG  LEU A  81     8452  11043   8999  -2544    901    -27       C\\nATOM    335  CD1 LEU A  81      -3.852   6.179   5.437  1.00 74.69           C\\nANISOU  335  CD1 LEU A  81     8087  11477   8814  -2632   1099   -186       C\\nATOM    336  CD2 LEU A  81      -3.924   4.409   3.669  1.00 73.03           C\\nANISOU  336  CD2 LEU A  81     8197  10767   8785  -2854    842     14       C\\nATOM    337  N   LEU A  82      -1.237   7.838   0.678  1.00 69.87           N\\nANISOU  337  N   LEU A  82     7892   9789   8867  -1397    460   -196       N\\nATOM    338  CA  LEU A  82      -1.409   8.637  -0.529  1.00 65.99           C\\nANISOU  338  CA  LEU A  82     7299   9280   8492  -1167    327   -272       C\\nATOM    339  C   LEU A  82      -0.757   7.982  -1.740  1.00 70.21           C\\nANISOU  339  C   LEU A  82     8057   9596   9025  -1131    218   -180       C\\nATOM    340  O   LEU A  82      -1.178   8.231  -2.875  1.00 71.57           O\\nANISOU  340  O   LEU A  82     8160   9794   9239  -1047    101   -233       O\\nATOM    341  CB  LEU A  82      -0.848  10.040  -0.313  1.00 59.37           C\\nANISOU  341  CB  LEU A  82     6407   8421   7728   -892    291   -300       C\\nATOM    342  CG  LEU A  82      -1.644  10.851   0.706  1.00 62.33           C\\nANISOU  342  CG  LEU A  82     6510   9044   8130   -856    360   -482       C\\nATOM    343  CD1 LEU A  82      -1.091  12.261   0.855  1.00 55.10           C\\nANISOU  343  CD1 LEU A  82     5564   8044   7327   -570    267   -530       C\\nATOM    344  CD2 LEU A  82      -3.114  10.883   0.314  1.00 64.42           C\\nANISOU  344  CD2 LEU A  82     6475   9550   8451   -907    325   -667       C\\nATOM    345  N   VAL A  83       0.261   7.147  -1.524  1.00 71.76           N\\nANISOU  345  N   VAL A  83     8510   9592   9162  -1179    238    -64       N\\nATOM    346  CA  VAL A  83       0.813   6.355  -2.620  1.00 69.53           C\\nANISOU  346  CA  VAL A  83     8414   9139   8867  -1147    140    -43       C\\nATOM    347  C   VAL A  83      -0.238   5.394  -3.158  1.00 73.89           C\\nANISOU  347  C   VAL A  83     8937   9715   9422  -1353     76   -116       C\\nATOM    348  O   VAL A  83      -0.404   5.247  -4.375  1.00 79.13           O\\nANISOU  348  O   VAL A  83     9606  10373  10087  -1289    -32   -185       O\\nATOM    349  CB  VAL A  83       2.078   5.608  -2.159  1.00 61.51           C\\nANISOU  349  CB  VAL A  83     7653   7900   7818  -1130    147     49       C\\nATOM    350  CG1 VAL A  83       2.537   4.623  -3.222  1.00 56.33           C\\nANISOU  350  CG1 VAL A  83     7164   7084   7153  -1094     37      1       C\\nATOM    351  CG2 VAL A  83       3.187   6.592  -1.827  1.00 55.01           C\\nANISOU  351  CG2 VAL A  83     6836   7065   7001   -921    189    106       C\\nATOM    352  N   ALA A  84      -0.973   4.732  -2.264  1.00 63.07           N\\nANISOU  352  N   ALA A  84     7532   8393   8036  -1628    136   -100       N\\nATOM    353  CA  ALA A  84      -1.979   3.777  -2.713  1.00 68.51           C\\nANISOU  353  CA  ALA A  84     8190   9097   8744  -1877     65   -159       C\\nATOM    354  C   ALA A  84      -3.109   4.458  -3.475  1.00 67.78           C\\nANISOU  354  C   ALA A  84     7803   9251   8701  -1831     21   -306       C\\nATOM    355  O   ALA A  84      -3.668   3.871  -4.408  1.00 63.21           O\\nANISOU  355  O   ALA A  84     7217   8653   8146  -1911   -101   -386       O\\nATOM    356  CB  ALA A  84      -2.540   3.003  -1.520  1.00 70.03           C\\nANISOU  356  CB  ALA A  84     8393   9327   8888  -2241    149    -72       C\\nATOM    357  N   THR A  85      -3.449   5.692  -3.108  1.00 59.88           N\\nANISOU  357  N   THR A  85     6561   8463   7726  -1685     85   -362       N\\nATOM    358  CA  THR A  85      -4.630   6.368  -3.632  1.00 70.05           C\\nANISOU  358  CA  THR A  85     7536   9994   9087  -1632     16   -521       C\\nATOM    359  C   THR A  85      -4.329   7.352  -4.758  1.00 73.23           C\\nANISOU  359  C   THR A  85     7938  10354   9531  -1316   -140   -540       C\\nATOM    360  O   THR A  85      -5.144   7.493  -5.674  1.00 73.60           O\\nANISOU  360  O   THR A  85     7844  10501   9619  -1283   -285   -640       O\\nATOM    361  CB  THR A  85      -5.355   7.103  -2.501  1.00 66.86           C\\nANISOU  361  CB  THR A  85     6829   9873   8704  -1660    148   -625       C\\nATOM    362  OG1 THR A  85      -4.432   7.958  -1.812  1.00 68.22           O\\nANISOU  362  OG1 THR A  85     7080   9977   8864  -1454    215   -567       O\\nATOM    363  CG2 THR A  85      -5.948   6.109  -1.519  1.00 61.69           C\\nANISOU  363  CG2 THR A  85     6117   9358   7964  -2054    299   -604       C\\nATOM    364  N   LEU A  86      -3.186   8.043  -4.718  1.00 62.95           N\\nANISOU  364  N   LEU A  86     6792   8914   8211  -1106   -129   -431       N\\nATOM    365  CA  LEU A  86      -2.875   9.074  -5.699  1.00 69.96           C\\nANISOU  365  CA  LEU A  86     7691   9770   9119   -857   -279   -398       C\\nATOM    366  C   LEU A  86      -1.823   8.663  -6.718  1.00 73.74           C\\nANISOU  366  C   LEU A  86     8430  10102   9484   -805   -327   -290       C\\nATOM    367  O   LEU A  86      -1.627   9.386  -7.700  1.00 78.44           O\\nANISOU  367  O   LEU A  86     9050  10709  10044   -662   -458   -237       O\\nATOM    368  CB  LEU A  86      -2.400  10.356  -5.000  1.00 71.90           C\\nANISOU  368  CB  LEU A  86     7888   9995   9438   -669   -260   -361       C\\nATOM    369  CG  LEU A  86      -3.358  11.015  -4.012  1.00 70.39           C\\nANISOU  369  CG  LEU A  86     7407   9983   9357   -640   -226   -527       C\\nATOM    370  CD1 LEU A  86      -2.805  12.358  -3.572  1.00 66.08           C\\nANISOU  370  CD1 LEU A  86     6851   9355   8902   -408   -280   -511       C\\nATOM    371  CD2 LEU A  86      -4.735  11.169  -4.633  1.00 73.10           C\\nANISOU  371  CD2 LEU A  86     7488  10505   9781   -625   -371   -694       C\\nATOM    372  N   VAL A  87      -1.137   7.538  -6.512  1.00 71.08           N\\nANISOU  372  N   VAL A  87     8285   9640   9081   -916   -240   -262       N\\nATOM    373  CA  VAL A  87      -0.068   7.087  -7.395  1.00 73.29           C\\nANISOU  373  CA  VAL A  87     8777   9820   9251   -840   -268   -222       C\\nATOM    374  C   VAL A  87      -0.364   5.702  -7.963  1.00 77.64           C\\nANISOU  374  C   VAL A  87     9430  10309   9760   -973   -330   -334       C\\nATOM    375  O   VAL A  87      -0.313   5.497  -9.179  1.00 73.98           O\\nANISOU  375  O   VAL A  87     9018   9892   9199   -916   -433   -399       O\\nATOM    376  CB  VAL A  87       1.295   7.094  -6.673  1.00 71.74           C\\nANISOU  376  CB  VAL A  87     8723   9494   9039   -769   -152   -126       C\\nATOM    377  CG1 VAL A  87       2.408   6.688  -7.635  1.00 74.66           C\\nANISOU  377  CG1 VAL A  87     9249   9829   9290   -667   -171   -133       C\\nATOM    378  CG2 VAL A  87       1.561   8.458  -6.054  1.00 66.12           C\\nANISOU  378  CG2 VAL A  87     7914   8818   8388   -656   -114    -33       C\\nATOM    379  N   MET A  88      -0.666   4.743  -7.091  1.00 80.11           N\\nANISOU  379  N   MET A  88     9788  10515  10136  -1166   -284   -354       N\\nATOM    380  CA  MET A  88      -0.910   3.374  -7.543  1.00 77.27           C\\nANISOU  380  CA  MET A  88     9560  10025   9773  -1313   -382   -456       C\\nATOM    381  C   MET A  88      -2.014   3.257  -8.587  1.00 74.77           C\\nANISOU  381  C   MET A  88     9120   9842   9447  -1377   -521   -585       C\\nATOM    382  O   MET A  88      -1.856   2.434  -9.508  1.00 75.54           O\\nANISOU  382  O   MET A  88     9351   9858   9492  -1370   -641   -704       O\\nATOM    383  CB  MET A  88      -1.213   2.478  -6.335  1.00 80.86           C\\nANISOU  383  CB  MET A  88    10082  10339  10303  -1575   -337   -400       C\\nATOM    384  CG  MET A  88      -0.060   2.322  -5.349  1.00 81.25           C\\nANISOU  384  CG  MET A  88    10311  10211  10350  -1521   -256   -278       C\\nATOM    385  SD  MET A  88       1.427   1.569  -6.040  1.00 83.45           S\\nANISOU  385  SD  MET A  88    10860  10245  10603  -1297   -355   -350       S\\nATOM    386  CE  MET A  88       0.780   0.002  -6.622  1.00 86.55           C\\nANISOU  386  CE  MET A  88    11408  10421  11056  -1493   -560   -493       C\\nATOM    387  N   PRO A  89      -3.134   3.998  -8.521  1.00 73.85           N\\nANISOU  387  N   PRO A  89     8745   9932   9382  -1424   -534   -603       N\\nATOM    388  CA  PRO A  89      -4.103   3.930  -9.629  1.00 74.48           C\\nANISOU  388  CA  PRO A  89     8707  10146   9448  -1448   -704   -735       C\\nATOM    389  C   PRO A  89      -3.480   4.213 -10.985  1.00 73.67           C\\nANISOU  389  C   PRO A  89     8725  10074   9192  -1237   -816   -758       C\\nATOM    390  O   PRO A  89      -3.834   3.559 -11.972  1.00 74.04           O\\nANISOU  390  O   PRO A  89     8817  10141   9174  -1277   -962   -893       O\\nATOM    391  CB  PRO A  89      -5.142   4.990  -9.248  1.00 73.14           C\\nANISOU  391  CB  PRO A  89     8221  10200   9368  -1431   -703   -747       C\\nATOM    392  CG  PRO A  89      -5.085   5.041  -7.779  1.00 71.74           C\\nANISOU  392  CG  PRO A  89     7982  10016   9258  -1543   -514   -680       C\\nATOM    393  CD  PRO A  89      -3.645   4.834  -7.418  1.00 67.98           C\\nANISOU  393  CD  PRO A  89     7787   9325   8719  -1455   -417   -550       C\\nATOM    394  N   TRP A  90      -2.552   5.170 -11.056  1.00 69.93           N\\nANISOU  394  N   TRP A  90     8302   9624   8643  -1037   -753   -630       N\\nATOM    395  CA  TRP A  90      -1.831   5.402 -12.301  1.00 70.06           C\\nANISOU  395  CA  TRP A  90     8440   9716   8463   -885   -824   -623       C\\nATOM    396  C   TRP A  90      -0.927   4.229 -12.652  1.00 73.43           C\\nANISOU  396  C   TRP A  90     9074  10033   8794   -879   -795   -740       C\\nATOM    397  O   TRP A  90      -0.713   3.948 -13.836  1.00 80.52           O\\nANISOU  397  O   TRP A  90    10046  11036   9511   -815   -885   -849       O\\nATOM    398  CB  TRP A  90      -0.996   6.677 -12.206  1.00 72.68           C\\nANISOU  398  CB  TRP A  90     8778  10094   8744   -730   -758   -431       C\\nATOM    399  CG  TRP A  90      -1.743   7.924 -11.827  1.00 78.23           C\\nANISOU  399  CG  TRP A  90     9301  10853   9571   -681   -825   -337       C\\nATOM    400  CD1 TRP A  90      -2.061   8.338 -10.567  1.00 78.70           C\\nANISOU  400  CD1 TRP A  90     9229  10858   9814   -696   -738   -319       C\\nATOM    401  CD2 TRP A  90      -2.229   8.939 -12.716  1.00 88.37           C\\nANISOU  401  CD2 TRP A  90    10523  12253  10801   -588  -1022   -264       C\\nATOM    402  NE1 TRP A  90      -2.729   9.539 -10.616  1.00 79.87           N\\nANISOU  402  NE1 TRP A  90     9218  11075  10052   -589   -872   -284       N\\nATOM    403  CE2 TRP A  90      -2.844   9.929 -11.925  1.00 85.91           C\\nANISOU  403  CE2 TRP A  90    10036  11918  10690   -521  -1067   -232       C\\nATOM    404  CE3 TRP A  90      -2.213   9.101 -14.106  1.00 93.09           C\\nANISOU  404  CE3 TRP A  90    11205  12978  11187   -553  -1185   -228       C\\nATOM    405  CZ2 TRP A  90      -3.436  11.064 -12.476  1.00 91.05           C\\nANISOU  405  CZ2 TRP A  90    10603  12614  11379   -398  -1303   -166       C\\nATOM    406  CZ3 TRP A  90      -2.801  10.229 -14.651  1.00 88.71           C\\nANISOU  406  CZ3 TRP A  90    10584  12483  10637   -467  -1412   -117       C\\nATOM    407  CH2 TRP A  90      -3.404  11.195 -13.838  1.00 91.05           C\\nANISOU  407  CH2 TRP A  90    10716  12700  11179   -380  -1486    -87       C\\nATOM    408  N   VAL A  91      -0.382   3.540 -11.646  1.00 69.25           N\\nANISOU  408  N   VAL A  91     8640   9297   8374   -930   -690   -736       N\\nATOM    409  CA  VAL A  91       0.555   2.453 -11.912  1.00 71.26           C\\nANISOU  409  CA  VAL A  91     9090   9406   8578   -872   -701   -873       C\\nATOM    410  C   VAL A  91      -0.181   1.188 -12.341  1.00 81.86           C\\nANISOU  410  C   VAL A  91    10506  10626   9969  -1010   -867  -1076       C\\nATOM    411  O   VAL A  91       0.272   0.468 -13.239  1.00 84.97           O\\nANISOU  411  O   VAL A  91    11020  11005  10261   -913   -961  -1279       O\\nATOM    412  CB  VAL A  91       1.447   2.203 -10.683  1.00 66.23           C\\nANISOU  412  CB  VAL A  91     8549   8562   8051   -856   -583   -782       C\\nATOM    413  CG1 VAL A  91       2.331   0.984 -10.905  1.00 66.75           C\\nANISOU  413  CG1 VAL A  91     8812   8434   8116   -769   -652   -961       C\\nATOM    414  CG2 VAL A  91       2.295   3.427 -10.395  1.00 71.66           C\\nANISOU  414  CG2 VAL A  91     9171   9373   8685   -712   -442   -614       C\\nATOM    415  N   VAL A  92      -1.320   0.890 -11.713  1.00 76.99           N\\nANISOU  415  N   VAL A  92     9808   9938   9507  -1247   -911  -1047       N\\nATOM    416  CA  VAL A  92      -2.100  -0.267 -12.139  1.00 83.11           C\\nANISOU  416  CA  VAL A  92    10641  10591  10346  -1426  -1092  -1225       C\\nATOM    417  C   VAL A  92      -2.714  -0.014 -13.513  1.00 85.39           C\\nANISOU  417  C   VAL A  92    10837  11112  10496  -1365  -1232  -1373       C\\nATOM    418  O   VAL A  92      -2.760  -0.914 -14.362  1.00 87.20           O\\nANISOU  418  O   VAL A  92    11179  11274  10677  -1366  -1396  -1596       O\\nATOM    419  CB  VAL A  92      -3.160  -0.626 -11.077  1.00 86.97           C\\nANISOU  419  CB  VAL A  92    11035  10994  11015  -1752  -1083  -1133       C\\nATOM    420  CG1 VAL A  92      -4.059   0.557 -10.774  1.00 88.40           C\\nANISOU  420  CG1 VAL A  92    10916  11464  11208  -1788   -990  -1030       C\\nATOM    421  CG2 VAL A  92      -3.984  -1.823 -11.526  1.00 90.14           C\\nANISOU  421  CG2 VAL A  92    11495  11253  11500  -1988  -1291  -1301       C\\nATOM    422  N   TYR A  93      -3.173   1.217 -13.762  1.00 86.77           N\\nANISOU  422  N   TYR A  93    10817  11548  10602  -1298  -1201  -1261       N\\nATOM    423  CA  TYR A  93      -3.600   1.598 -15.106  1.00 83.84           C\\nANISOU  423  CA  TYR A  93    10389  11409  10056  -1209  -1354  -1357       C\\nATOM    424  C   TYR A  93      -2.477   1.379 -16.111  1.00 80.40           C\\nANISOU  424  C   TYR A  93    10133  11042   9375  -1017  -1359  -1466       C\\nATOM    425  O   TYR A  93      -2.706   0.878 -17.219  1.00 74.40           O\\nANISOU  425  O   TYR A  93     9423  10381   8465   -997  -1517  -1669       O\\nATOM    426  CB  TYR A  93      -4.062   3.059 -15.102  1.00 86.78           C\\nANISOU  426  CB  TYR A  93    10567  11993  10412  -1130  -1345  -1178       C\\nATOM    427  CG  TYR A  93      -4.289   3.683 -16.465  1.00 96.56           C\\nANISOU  427  CG  TYR A  93    11788  13469  11430  -1012  -1516  -1193       C\\nATOM    428  CD1 TYR A  93      -5.528   3.603 -17.096  1.00 94.66           C\\nANISOU  428  CD1 TYR A  93    11412  13349  11207  -1088  -1737  -1310       C\\nATOM    429  CD2 TYR A  93      -3.274   4.383 -17.106  1.00 98.40           C\\nANISOU  429  CD2 TYR A  93    12135  13829  11423   -849  -1468  -1073       C\\nATOM    430  CE1 TYR A  93      -5.739   4.185 -18.334  1.00 95.59           C\\nANISOU  430  CE1 TYR A  93    11537  13682  11100   -983  -1926  -1302       C\\nATOM    431  CE2 TYR A  93      -3.475   4.965 -18.343  1.00 97.04           C\\nANISOU  431  CE2 TYR A  93    11974  13889  11007   -780  -1636  -1042       C\\nATOM    432  CZ  TYR A  93      -4.707   4.864 -18.952  1.00 96.39           C\\nANISOU  432  CZ  TYR A  93    11785  13900  10937   -837  -1876  -1153       C\\nATOM    433  OH  TYR A  93      -4.903   5.446 -20.182  1.00 95.53           O\\nANISOU  433  OH  TYR A  93    11712  14022  10562   -771  -2074  -1102       O\\nATOM    434  N   LEU A  94      -1.250   1.724 -15.722  1.00 88.56           N\\nANISOU  434  N   LEU A  94    11244  12051  10355   -879  -1185  -1358       N\\nATOM    435  CA  LEU A  94      -0.090   1.590 -16.592  1.00 90.25           C\\nANISOU  435  CA  LEU A  94    11571  12398  10320   -698  -1144  -1470       C\\nATOM    436  C   LEU A  94       0.187   0.143 -16.984  1.00 86.74           C\\nANISOU  436  C   LEU A  94    11276  11802   9879   -668  -1251  -1798       C\\nATOM    437  O   LEU A  94       0.806  -0.096 -18.027  1.00 79.60           O\\nANISOU  437  O   LEU A  94    10426  11091   8726   -524  -1274  -1999       O\\nATOM    438  CB  LEU A  94       1.131   2.192 -15.893  1.00 91.19           C\\nANISOU  438  CB  LEU A  94    11704  12504  10440   -587   -935  -1297       C\\nATOM    439  CG  LEU A  94       2.362   2.481 -16.745  1.00 96.59           C\\nANISOU  439  CG  LEU A  94    12420  13445  10836   -422   -839  -1342       C\\nATOM    440  CD1 LEU A  94       1.952   3.241 -17.987  1.00 95.48           C\\nANISOU  440  CD1 LEU A  94    12233  13639  10407   -435   -921  -1281       C\\nATOM    441  CD2 LEU A  94       3.366   3.277 -15.931  1.00 94.01           C\\nANISOU  441  CD2 LEU A  94    12057  13105  10556   -364   -648  -1120       C\\nATOM    442  N   GLU A  95      -0.244  -0.827 -16.175  1.00 91.64           N\\nANISOU  442  N   GLU A  95    11967  12086  10767   -809  -1328  -1863       N\\nATOM    443  CA  GLU A  95      -0.007  -2.228 -16.505  1.00 89.73           C\\nANISOU  443  CA  GLU A  95    11897  11617  10578   -779  -1491  -2179       C\\nATOM    444  C   GLU A  95      -1.104  -2.803 -17.392  1.00 87.68           C\\nANISOU  444  C   GLU A  95    11631  11388  10293   -904  -1724  -2391       C\\nATOM    445  O   GLU A  95      -0.812  -3.568 -18.317  1.00 89.77           O\\nANISOU  445  O   GLU A  95    12002  11667  10441   -784  -1865  -2717       O\\nATOM    446  CB  GLU A  95       0.121  -3.065 -15.229  1.00 87.59           C\\nANISOU  446  CB  GLU A  95    11758  10917  10607   -899  -1515  -2120       C\\nATOM    447  CG  GLU A  95       0.439  -4.539 -15.480  1.00 93.67           C\\nANISOU  447  CG  GLU A  95    12747  11357  11487   -851  -1741  -2438       C\\nATOM    448  CD  GLU A  95       1.851  -4.758 -16.002  1.00102.62           C\\nANISOU  448  CD  GLU A  95    13952  12557  12482   -504  -1707  -2681       C\\nATOM    449  OE1 GLU A  95       2.722  -3.902 -15.740  1.00104.20           O\\nANISOU  449  OE1 GLU A  95    14062  12957  12571   -357  -1484  -2527       O\\nATOM    450  OE2 GLU A  95       2.093  -5.788 -16.670  1.00107.64           O\\nANISOU  450  OE2 GLU A  95    14717  13056  13125   -376  -1910  -3051       O\\nATOM    451  N   VAL A  96      -2.362  -2.449 -17.129  1.00 78.94           N\\nANISOU  451  N   VAL A  96    10382  10316   9297  -1131  -1774  -2245       N\\nATOM    452  CA  VAL A  96      -3.462  -2.952 -17.947  1.00 80.52           C\\nANISOU  452  CA  VAL A  96    10543  10563   9488  -1267  -2011  -2444       C\\nATOM    453  C   VAL A  96      -3.331  -2.439 -19.375  1.00 85.05           C\\nANISOU  453  C   VAL A  96    11087  11511   9717  -1081  -2072  -2578       C\\nATOM    454  O   VAL A  96      -3.404  -3.209 -20.340  1.00 82.90           O\\nANISOU  454  O   VAL A  96    10906  11266   9327  -1037  -2258  -2893       O\\nATOM    455  CB  VAL A  96      -4.816  -2.561 -17.328  1.00 77.18           C\\nANISOU  455  CB  VAL A  96     9907  10166   9251  -1538  -2032  -2265       C\\nATOM    456  N   VAL A  97      -3.117  -1.130 -19.528  1.00 87.40           N\\nANISOU  456  N   VAL A  97    11271  12099   9836   -979  -1932  -2336       N\\nATOM    457  CA  VAL A  97      -2.995  -0.529 -20.854  1.00 88.86           C\\nANISOU  457  CA  VAL A  97    11446  12664   9653   -847  -1994  -2384       C\\nATOM    458  C   VAL A  97      -1.719  -0.983 -21.554  1.00 90.16           C\\nANISOU  458  C   VAL A  97    11752  12956   9548   -647  -1919  -2608       C\\nATOM    459  O   VAL A  97      -1.694  -1.122 -22.783  1.00 92.93           O\\nANISOU  459  O   VAL A  97    12140  13588   9583   -572  -2028  -2817       O\\nATOM    460  CB  VAL A  97      -3.061   1.005 -20.740  1.00 86.80           C\\nANISOU  460  CB  VAL A  97    11060  12617   9305   -817  -1897  -2025       C\\nATOM    461  CG1 VAL A  97      -2.893   1.659 -22.106  1.00 88.76           C\\nANISOU  461  CG1 VAL A  97    11335  13252   9139   -721  -1981  -2009       C\\nATOM    462  CG2 VAL A  97      -4.372   1.434 -20.086  1.00 86.16           C\\nANISOU  462  CG2 VAL A  97    10792  12448   9495   -970  -1990  -1884       C\\nATOM    463  N   GLY A  98      -0.650  -1.230 -20.800  1.00 88.15           N\\nANISOU  463  N   GLY A  98    11562  12531   9400   -550  -1740  -2596       N\\nATOM    464  CA  GLY A  98       0.613  -1.604 -21.402  1.00 89.34           C\\nANISOU  464  CA  GLY A  98    11789  12846   9310   -334  -1652  -2837       C\\nATOM    465  C   GLY A  98       1.360  -0.469 -22.059  1.00 91.48           C\\nANISOU  465  C   GLY A  98    11987  13570   9202   -247  -1473  -2660       C\\nATOM    466  O   GLY A  98       2.307  -0.717 -22.810  1.00 93.59           O\\nANISOU  466  O   GLY A  98    12270  14114   9177    -92  -1395  -2892       O\\nATOM    467  N   GLU A  99       0.962   0.772 -21.797  1.00 93.52           N\\nANISOU  467  N   GLU A  99    12159  13918   9455   -352  -1418  -2264       N\\nATOM    468  CA  GLU A  99       1.609   1.938 -22.378  1.00 95.54           C\\nANISOU  468  CA  GLU A  99    12373  14557   9372   -328  -1286  -2022       C\\nATOM    469  C   GLU A  99       1.259   3.151 -21.529  1.00 92.97           C\\nANISOU  469  C   GLU A  99    11976  14105   9244   -422  -1241  -1593       C\\nATOM    470  O   GLU A  99       0.253   3.163 -20.815  1.00 85.82           O\\nANISOU  470  O   GLU A  99    11021  12937   8648   -506  -1345  -1519       O\\nATOM    471  CB  GLU A  99       1.181   2.153 -23.835  1.00 94.86           C\\nANISOU  471  CB  GLU A  99    12308  14866   8868   -355  -1437  -2092       C\\nATOM    472  N   TRP A 100       2.110   4.174 -21.614  1.00 89.68           N\\nANISOU  472  N   TRP A 100    11539  13894   8642   -414  -1089  -1330       N\\nATOM    473  CA  TRP A 100       1.871   5.446 -20.932  1.00 88.27           C\\nANISOU  473  CA  TRP A 100    11308  13606   8625   -483  -1080   -935       C\\nATOM    474  C   TRP A 100       0.892   6.302 -21.742  1.00 91.37           C\\nANISOU  474  C   TRP A 100    11702  14149   8867   -556  -1315   -744       C\\nATOM    475  O   TRP A 100       1.217   7.382 -22.236  1.00 95.09           O\\nANISOU  475  O   TRP A 100    12204  14809   9115   -605  -1334   -453       O\\nATOM    476  CB  TRP A 100       3.188   6.177 -20.702  1.00 86.77           C\\nANISOU  476  CB  TRP A 100    11107  13540   8322   -471   -861   -729       C\\nATOM    477  CG  TRP A 100       4.148   5.471 -19.784  1.00 92.86           C\\nANISOU  477  CG  TRP A 100    11859  14140   9283   -376   -663   -888       C\\nATOM    478  CD1 TRP A 100       4.731   4.252 -19.983  1.00 99.53           C\\nANISOU  478  CD1 TRP A 100    12726  15011  10078   -261   -605  -1253       C\\nATOM    479  CD2 TRP A 100       4.655   5.958 -18.534  1.00 93.04           C\\nANISOU  479  CD2 TRP A 100    11841  13932   9577   -369   -533   -700       C\\nATOM    480  NE1 TRP A 100       5.558   3.944 -18.928  1.00 99.78           N\\nANISOU  480  NE1 TRP A 100    12740  14828  10345   -179   -465  -1286       N\\nATOM    481  CE2 TRP A 100       5.530   4.975 -18.027  1.00 94.10           C\\nANISOU  481  CE2 TRP A 100    11981  13965   9809   -254   -408   -944       C\\nATOM    482  CE3 TRP A 100       4.449   7.125 -17.792  1.00 92.42           C\\nANISOU  482  CE3 TRP A 100    11726  13714   9675   -431   -538   -373       C\\nATOM    483  CZ2 TRP A 100       6.198   5.125 -16.811  1.00 92.35           C\\nANISOU  483  CZ2 TRP A 100    11733  13525   9830   -217   -285   -845       C\\nATOM    484  CZ3 TRP A 100       5.114   7.273 -16.583  1.00 87.83           C\\nANISOU  484  CZ3 TRP A 100    11114  12928   9330   -397   -398   -300       C\\nATOM    485  CH2 TRP A 100       5.977   6.279 -16.107  1.00 90.94           C\\nANISOU  485  CH2 TRP A 100    11517  13244   9792   -299   -271   -522       C\\nATOM    486  N   LYS A 101      -0.329   5.791 -21.877  1.00 95.15           N\\nANISOU  486  N   LYS A 101    12148  14527   9477   -577  -1521   -906       N\\nATOM    487  CA  LYS A 101      -1.365   6.446 -22.678  1.00 96.45           C\\nANISOU  487  CA  LYS A 101    12300  14824   9522   -619  -1798   -787       C\\nATOM    488  C   LYS A 101      -2.121   7.498 -21.869  1.00 98.53           C\\nANISOU  488  C   LYS A 101    12457  14876  10104   -621  -1907   -529       C\\nATOM    489  O   LYS A 101      -3.351   7.502 -21.813  1.00100.15           O\\nANISOU  489  O   LYS A 101    12553  15004  10495   -628  -2120   -595       O\\nATOM    490  CB  LYS A 101      -2.319   5.405 -23.251  1.00 91.01           C\\nANISOU  490  CB  LYS A 101    11597  14158   8826   -638  -1991  -1116       C\\nATOM    491  N   PHE A 102      -1.377   8.397 -21.223  1.00 92.76           N\\nANISOU  491  N   PHE A 102    11736  14060   9449   -605  -1768   -264       N\\nATOM    492  CA  PHE A 102      -1.943   9.593 -20.620  1.00 93.22           C\\nANISOU  492  CA  PHE A 102    11716  13947   9756   -575  -1904    -18       C\\nATOM    493  C   PHE A 102      -1.857  10.735 -21.628  1.00 91.71           C\\nANISOU  493  C   PHE A 102    11641  13918   9287   -599  -2119    289       C\\nATOM    494  O   PHE A 102      -1.422  10.558 -22.768  1.00103.07           O\\nANISOU  494  O   PHE A 102    13204  15642  10313   -665  -2138    313       O\\nATOM    495  CB  PHE A 102      -1.202   9.983 -19.340  1.00 94.22           C\\nANISOU  495  CB  PHE A 102    11808  13862  10129   -551  -1677     95       C\\nATOM    496  CG  PHE A 102      -0.815   8.827 -18.469  1.00 91.97           C\\nANISOU  496  CG  PHE A 102    11490  13455  10000   -556  -1432   -141       C\\nATOM    497  CD1 PHE A 102      -1.737   8.243 -17.618  1.00 88.34           C\\nANISOU  497  CD1 PHE A 102    10903  12822   9841   -574  -1444   -314       C\\nATOM    498  CD2 PHE A 102       0.483   8.344 -18.477  1.00 88.17           C\\nANISOU  498  CD2 PHE A 102    11097  13037   9364   -553  -1204   -181       C\\nATOM    499  CE1 PHE A 102      -1.375   7.184 -16.805  1.00 84.23           C\\nANISOU  499  CE1 PHE A 102    10394  12156   9452   -611  -1257   -481       C\\nATOM    500  CE2 PHE A 102       0.849   7.286 -17.667  1.00 83.36           C\\nANISOU  500  CE2 PHE A 102    10485  12270   8917   -538  -1037   -386       C\\nATOM    501  CZ  PHE A 102      -0.082   6.706 -16.830  1.00 81.83           C\\nANISOU  501  CZ  PHE A 102    10213  11865   9014   -578  -1075   -513       C\\nATOM    502  N   SER A 103      -2.265  11.924 -21.210  1.00 88.70           N\\nANISOU  502  N   SER A 103    11226  13356   9120   -550  -2299    526       N\\nATOM    503  CA  SER A 103      -1.855  13.135 -21.896  1.00 82.43           C\\nANISOU  503  CA  SER A 103    10589  12620   8110   -603  -2476    904       C\\nATOM    504  C   SER A 103      -0.586  13.661 -21.237  1.00 83.13           C\\nANISOU  504  C   SER A 103    10732  12623   8230   -660  -2230   1106       C\\nATOM    505  O   SER A 103      -0.135  13.148 -20.210  1.00 83.31           O\\nANISOU  505  O   SER A 103    10661  12526   8466   -622  -1957    945       O\\nATOM    506  CB  SER A 103      -2.969  14.182 -21.869  1.00 79.20           C\\nANISOU  506  CB  SER A 103    10137  12018   7939   -498  -2879   1043       C\\nATOM    507  OG  SER A 103      -3.335  14.521 -20.542  1.00 76.16           O\\nANISOU  507  OG  SER A 103     9579  11344   8016   -372  -2840    955       O\\nATOM    508  N   ARG A 104       0.009  14.689 -21.845  1.00 84.27           N\\nANISOU  508  N   ARG A 104    11037  12833   8148   -776  -2344   1478       N\\nATOM    509  CA  ARG A 104       1.252  15.212 -21.290  1.00 80.60           C\\nANISOU  509  CA  ARG A 104    10612  12312   7701   -868  -2123   1679       C\\nATOM    510  C   ARG A 104       1.025  15.830 -19.921  1.00 77.44           C\\nANISOU  510  C   ARG A 104    10113  11518   7794   -740  -2150   1682       C\\nATOM    511  O   ARG A 104       1.913  15.783 -19.064  1.00 78.86           O\\nANISOU  511  O   ARG A 104    10250  11620   8096   -755  -1890   1666       O\\nATOM    512  CB  ARG A 104       1.881  16.231 -22.235  1.00 80.66           C\\nANISOU  512  CB  ARG A 104    10815  12469   7362  -1078  -2266   2114       C\\nATOM    513  CG  ARG A 104       3.382  16.383 -22.031  1.00 90.20           C\\nANISOU  513  CG  ARG A 104    12038  13815   8417  -1248  -1948   2260       C\\nATOM    514  CD  ARG A 104       3.766  17.736 -21.446  1.00101.17           C\\nANISOU  514  CD  ARG A 104    13504  14894  10041  -1329  -2089   2624       C\\nATOM    515  NE  ARG A 104       3.451  18.831 -22.359  1.00106.68           N\\nANISOU  515  NE  ARG A 104    14414  15562  10556  -1484  -2476   3046       N\\nATOM    516  CZ  ARG A 104       2.650  19.849 -22.059  1.00108.76           C\\nANISOU  516  CZ  ARG A 104    14758  15416  11150  -1381  -2885   3220       C\\nATOM    517  NH1 ARG A 104       2.092  19.927 -20.857  1.00104.63           N\\nANISOU  517  NH1 ARG A 104    14088  14533  11136  -1126  -2918   2984       N\\nATOM    518  NH2 ARG A 104       2.417  20.795 -22.961  1.00112.28           N\\nANISOU  518  NH2 ARG A 104    15433  15822  11408  -1532  -3275   3626       N\\nATOM    519  N   ILE A 105      -0.160  16.392 -19.688  1.00 79.98           N\\nANISOU  519  N   ILE A 105    10379  11613   8397   -597  -2469   1666       N\\nATOM    520  CA  ILE A 105      -0.435  17.000 -18.394  1.00 78.38           C\\nANISOU  520  CA  ILE A 105    10057  11079   8646   -452  -2502   1613       C\\nATOM    521  C   ILE A 105      -0.797  15.939 -17.359  1.00 74.85           C\\nANISOU  521  C   ILE A 105     9401  10617   8423   -355  -2239   1232       C\\nATOM    522  O   ILE A 105      -0.422  16.063 -16.189  1.00 73.96           O\\nANISOU  522  O   ILE A 105     9211  10343   8549   -307  -2066   1171       O\\nATOM    523  CB  ILE A 105      -1.528  18.076 -18.534  1.00 77.26           C\\nANISOU  523  CB  ILE A 105     9910  10715   8730   -308  -2966   1710       C\\nATOM    524  CG1 ILE A 105      -1.691  18.858 -17.227  1.00 76.93           C\\nANISOU  524  CG1 ILE A 105     9750  10345   9133   -142  -3017   1643       C\\nATOM    525  CG2 ILE A 105      -2.847  17.465 -18.989  1.00 71.80           C\\nANISOU  525  CG2 ILE A 105     9083  10142   8055   -199  -3143   1458       C\\nATOM    526  CD1 ILE A 105      -0.522  19.761 -16.903  1.00 63.79           C\\nANISOU  526  CD1 ILE A 105     8244   8504   7489   -248  -2982   1938       C\\nATOM    527  N   HIS A 106      -1.425  14.862 -17.789  1.00 78.10           N\\nANISOU  527  N   HIS A 106     9732  11194   8747   -350  -2214    984       N\\nATOM    528  CA  HIS A 106      -1.751  13.780 -16.889  1.00 72.04           C\\nANISOU  528  CA  HIS A 106     8805  10412   8157   -326  -1967    668       C\\nATOM    529  C   HIS A 106      -0.480  13.081 -16.470  1.00 75.28           C\\nANISOU  529  C   HIS A 106     9289  10863   8451   -409  -1617    644       C\\nATOM    530  O   HIS A 106      -0.345  12.663 -15.351  1.00 70.37           O\\nANISOU  530  O   HIS A 106     8580  10125   8032   -389  -1418    503       O\\nATOM    531  CB  HIS A 106      -2.690  12.806 -17.558  1.00 69.03           C\\nANISOU  531  CB  HIS A 106     8344  10182   7701   -344  -2050    426       C\\nATOM    532  CG  HIS A 106      -4.109  13.257 -17.558  1.00 86.66           C\\nANISOU  532  CG  HIS A 106    10420  12382  10122   -239  -2375    359       C\\nATOM    533  ND1 HIS A 106      -4.497  14.469 -17.043  1.00 93.53           N\\nANISOU  533  ND1 HIS A 106    11265  13098  11175   -109  -2634    518       N\\nATOM    534  CD2 HIS A 106      -5.234  12.662 -18.003  1.00 92.54           C\\nANISOU  534  CD2 HIS A 106    11011  13228  10921   -235  -2507    125       C\\nATOM    535  CE1 HIS A 106      -5.801  14.602 -17.170  1.00 95.16           C\\nANISOU  535  CE1 HIS A 106    11292  13325  11539     -1  -2912    369       C\\nATOM    536  NE2 HIS A 106      -6.273  13.520 -17.751  1.00 94.46           N\\nANISOU  536  NE2 HIS A 106    11111  13409  11371    -89  -2829    134       N\\nATOM    537  N   CYS A 107       0.459  12.953 -17.384  1.00 74.40           N\\nANISOU  537  N   CYS A 107     9326  10942   8001   -501  -1547    768       N\\nATOM    538  CA  CYS A 107       1.750  12.355 -17.073  1.00 74.41           C\\nANISOU  538  CA  CYS A 107     9366  11008   7898   -548  -1239    725       C\\nATOM    539  C   CYS A 107       2.520  13.220 -16.082  1.00 69.26           C\\nANISOU  539  C   CYS A 107     8705  10174   7436   -541  -1146    902       C\\nATOM    540  O   CYS A 107       3.036  12.718 -15.076  1.00 62.15           O\\nANISOU  540  O   CYS A 107     7754   9173   6688   -508   -936    780       O\\nATOM    541  CB  CYS A 107       2.542  12.149 -18.368  1.00 77.98           C\\nANISOU  541  CB  CYS A 107     9930  11782   7918   -646  -1190    790       C\\nATOM    542  SG  CYS A 107       4.200  11.445 -18.193  1.00 79.49           S\\nANISOU  542  SG  CYS A 107    10119  12137   7945   -673   -832    689       S\\nATOM    543  N   ASP A 108       2.590  14.530 -16.341  1.00 68.64           N\\nANISOU  543  N   ASP A 108     8692  10029   7359   -576  -1335   1195       N\\nATOM    544  CA  ASP A 108       3.289  15.433 -15.430  1.00 67.61           C\\nANISOU  544  CA  ASP A 108     8561   9699   7427   -578  -1293   1358       C\\nATOM    545  C   ASP A 108       2.673  15.405 -14.037  1.00 65.65           C\\nANISOU  545  C   ASP A 108     8180   9208   7557   -435  -1270   1167       C\\nATOM    546  O   ASP A 108       3.393  15.362 -13.033  1.00 66.27           O\\nANISOU  546  O   ASP A 108     8226   9190   7765   -423  -1086   1133       O\\nATOM    547  CB  ASP A 108       3.280  16.856 -15.990  1.00 70.02           C\\nANISOU  547  CB  ASP A 108     8985   9912   7707   -648  -1582   1705       C\\nATOM    548  CG  ASP A 108       4.274  17.047 -17.124  1.00 81.41           C\\nANISOU  548  CG  ASP A 108    10562  11623   8747   -867  -1532   1967       C\\nATOM    549  OD1 ASP A 108       5.293  16.329 -17.150  1.00 84.41           O\\nANISOU  549  OD1 ASP A 108    10904  12225   8943   -940  -1226   1879       O\\nATOM    550  OD2 ASP A 108       4.043  17.922 -17.986  1.00 86.93           O\\nANISOU  550  OD2 ASP A 108    11397  12326   9305   -971  -1808   2260       O\\nATOM    551  N   ILE A 109       1.341  15.424 -13.956  1.00 63.48           N\\nANISOU  551  N   ILE A 109     7808   8870   7442   -332  -1455   1030       N\\nATOM    552  CA  ILE A 109       0.665  15.365 -12.662  1.00 61.96           C\\nANISOU  552  CA  ILE A 109     7449   8532   7562   -218  -1412    821       C\\nATOM    553  C   ILE A 109       1.015  14.072 -11.937  1.00 63.72           C\\nANISOU  553  C   ILE A 109     7629   8811   7771   -268  -1106    623       C\\nATOM    554  O   ILE A 109       1.341  14.076 -10.743  1.00 59.23           O\\nANISOU  554  O   ILE A 109     7010   8137   7359   -241   -960    564       O\\nATOM    555  CB  ILE A 109      -0.856  15.511 -12.845  1.00 58.03           C\\nANISOU  555  CB  ILE A 109     6805   8039   7204   -115  -1656    674       C\\nATOM    556  CG1 ILE A 109      -1.212  16.937 -13.262  1.00 58.42           C\\nANISOU  556  CG1 ILE A 109     6896   7940   7362    -12  -2018    855       C\\nATOM    557  CG2 ILE A 109      -1.588  15.133 -11.573  1.00 56.04           C\\nANISOU  557  CG2 ILE A 109     6336   7761   7197    -50  -1535    405       C\\nATOM    558  CD1 ILE A 109      -2.681  17.131 -13.524  1.00 59.89           C\\nANISOU  558  CD1 ILE A 109     6917   8142   7695    126  -2302    693       C\\nATOM    559  N   PHE A 110       0.949  12.945 -12.648  1.00 61.78           N\\nANISOU  559  N   PHE A 110     7422   8717   7335   -338  -1034    516       N\\nATOM    560  CA  PHE A 110       1.250  11.658 -12.031  1.00 58.79           C\\nANISOU  560  CA  PHE A 110     7039   8336   6961   -385   -808    335       C\\nATOM    561  C   PHE A 110       2.679  11.622 -11.510  1.00 63.91           C\\nANISOU  561  C   PHE A 110     7771   8939   7574   -390   -613    414       C\\nATOM    562  O   PHE A 110       2.921  11.236 -10.361  1.00 59.44           O\\nANISOU  562  O   PHE A 110     7180   8260   7146   -384   -476    340       O\\nATOM    563  CB  PHE A 110       0.997  10.530 -13.034  1.00 61.38           C\\nANISOU  563  CB  PHE A 110     7419   8803   7098   -442   -823    194       C\\nATOM    564  CG  PHE A 110       1.692   9.234 -12.700  1.00 68.94           C\\nANISOU  564  CG  PHE A 110     8447   9728   8016   -477   -636     42       C\\nATOM    565  CD1 PHE A 110       1.579   8.662 -11.444  1.00 75.18           C\\nANISOU  565  CD1 PHE A 110     9204  10361   8999   -508   -525    -42       C\\nATOM    566  CD2 PHE A 110       2.437   8.573 -13.660  1.00 71.59           C\\nANISOU  566  CD2 PHE A 110     8887  10201   8115   -474   -595    -28       C\\nATOM    567  CE1 PHE A 110       2.216   7.472 -11.150  1.00 77.40           C\\nANISOU  567  CE1 PHE A 110     9585  10560   9264   -531   -416   -161       C\\nATOM    568  CE2 PHE A 110       3.070   7.383 -13.372  1.00 74.90           C\\nANISOU  568  CE2 PHE A 110     9372  10553   8534   -462   -477   -203       C\\nATOM    569  CZ  PHE A 110       2.960   6.833 -12.116  1.00 77.70           C\\nANISOU  569  CZ  PHE A 110     9724  10690   9110   -489   -407   -255       C\\nATOM    570  N   VAL A 111       3.641  12.034 -12.340  1.00 65.60           N\\nANISOU  570  N   VAL A 111     8072   9264   7587   -416   -603    568       N\\nATOM    571  CA  VAL A 111       5.043  11.987 -11.930  1.00 66.54           C\\nANISOU  571  CA  VAL A 111     8228   9388   7667   -424   -420    620       C\\nATOM    572  C   VAL A 111       5.288  12.924 -10.757  1.00 60.65           C\\nANISOU  572  C   VAL A 111     7442   8452   7150   -393   -417    727       C\\nATOM    573  O   VAL A 111       6.026  12.590  -9.822  1.00 56.21           O\\nANISOU  573  O   VAL A 111     6872   7814   6670   -370   -270    674       O\\nATOM    574  CB  VAL A 111       5.960  12.317 -13.119  1.00 69.81           C\\nANISOU  574  CB  VAL A 111     8700  10035   7791   -499   -401    765       C\\nATOM    575  CG1 VAL A 111       7.405  12.336 -12.671  1.00 60.98           C\\nANISOU  575  CG1 VAL A 111     7563   8955   6651   -512   -214    801       C\\nATOM    576  CG2 VAL A 111       5.758  11.308 -14.235  1.00 72.95           C\\nANISOU  576  CG2 VAL A 111     9130  10652   7937   -508   -394    597       C\\nATOM    577  N   THR A 112       4.669  14.106 -10.784  1.00 59.23           N\\nANISOU  577  N   THR A 112     7242   8180   7083   -374   -610    861       N\\nATOM    578  CA  THR A 112       4.789  15.036  -9.664  1.00 65.31           C\\nANISOU  578  CA  THR A 112     7970   8754   8090   -319   -646    910       C\\nATOM    579  C   THR A 112       4.286  14.407  -8.371  1.00 66.52           C\\nANISOU  579  C   THR A 112     8031   8833   8410   -256   -532    693       C\\nATOM    580  O   THR A 112       4.970  14.440  -7.343  1.00 76.31           O\\nANISOU  580  O   THR A 112     9268   9991   9734   -241   -417    676       O\\nATOM    581  CB  THR A 112       4.019  16.321  -9.963  1.00 64.71           C\\nANISOU  581  CB  THR A 112     7889   8561   8139   -269   -933   1031       C\\nATOM    582  OG1 THR A 112       4.645  17.010 -11.052  1.00 63.73           O\\nANISOU  582  OG1 THR A 112     7888   8484   7843   -379  -1048   1304       O\\nATOM    583  CG2 THR A 112       3.995  17.223  -8.744  1.00 62.38           C\\nANISOU  583  CG2 THR A 112     7534   8052   8116   -171   -994    998       C\\nATOM    584  N   LEU A 113       3.086  13.825  -8.407  1.00 61.29           N\\nANISOU  584  N   LEU A 113     7289   8219   7778   -245   -569    534       N\\nATOM    585  CA  LEU A 113       2.533  13.195  -7.214  1.00 68.29           C\\nANISOU  585  CA  LEU A 113     8081   9085   8780   -248   -453    353       C\\nATOM    586  C   LEU A 113       3.348  11.975  -6.799  1.00 67.53           C\\nANISOU  586  C   LEU A 113     8081   8983   8595   -321   -257    312       C\\nATOM    587  O   LEU A 113       3.573  11.752  -5.604  1.00 68.67           O\\nANISOU  587  O   LEU A 113     8216   9064   8811   -332   -149    267       O\\nATOM    588  CB  LEU A 113       1.075  12.808  -7.454  1.00 70.65           C\\nANISOU  588  CB  LEU A 113     8249   9477   9119   -266   -536    201       C\\nATOM    589  CG  LEU A 113       0.073  13.960  -7.517  1.00 65.91           C\\nANISOU  589  CG  LEU A 113     7497   8872   8673   -146   -751    162       C\\nATOM    590  CD1 LEU A 113      -1.287  13.451  -7.958  1.00 61.41           C\\nANISOU  590  CD1 LEU A 113     6776   8439   8118   -174   -840      2       C\\nATOM    591  CD2 LEU A 113      -0.016  14.648  -6.165  1.00 61.76           C\\nANISOU  591  CD2 LEU A 113     6853   8287   8324    -59   -710     69       C\\nATOM    592  N   ASP A 114       3.794  11.174  -7.768  1.00 63.91           N\\nANISOU  592  N   ASP A 114     7718   8590   7975   -359   -233    311       N\\nATOM    593  CA  ASP A 114       4.598   9.999  -7.445  1.00 66.05           C\\nANISOU  593  CA  ASP A 114     8086   8820   8191   -384   -102    240       C\\nATOM    594  C   ASP A 114       5.885  10.392  -6.734  1.00 66.08           C\\nANISOU  594  C   ASP A 114     8124   8760   8225   -333    -12    324       C\\nATOM    595  O   ASP A 114       6.262   9.778  -5.730  1.00 69.96           O\\nANISOU  595  O   ASP A 114     8658   9151   8773   -337     64    278       O\\nATOM    596  CB  ASP A 114       4.901   9.208  -8.720  1.00 75.01           C\\nANISOU  596  CB  ASP A 114     9296  10059   9148   -388   -118    174       C\\nATOM    597  CG  ASP A 114       5.951   8.133  -8.509  1.00 75.49           C\\nANISOU  597  CG  ASP A 114     9451  10063   9168   -352    -25     76       C\\nATOM    598  OD1 ASP A 114       5.746   7.255  -7.648  1.00 74.37           O\\nANISOU  598  OD1 ASP A 114     9364   9766   9125   -388     -9     -2       O\\nATOM    599  OD2 ASP A 114       6.981   8.161  -9.214  1.00 76.15           O\\nANISOU  599  OD2 ASP A 114     9549  10268   9116   -291     20     74       O\\nATOM    600  N   VAL A 115       6.568  11.421  -7.235  1.00 71.45           N\\nANISOU  600  N   VAL A 115     8790   9494   8864   -306    -41    464       N\\nATOM    601  CA  VAL A 115       7.809  11.865  -6.610  1.00 70.24           C\\nANISOU  601  CA  VAL A 115     8641   9297   8749   -279     30    542       C\\nATOM    602  C   VAL A 115       7.535  12.461  -5.234  1.00 69.24           C\\nANISOU  602  C   VAL A 115     8477   9030   8802   -253     19    542       C\\nATOM    603  O   VAL A 115       8.282  12.220  -4.279  1.00 70.91           O\\nANISOU  603  O   VAL A 115     8710   9175   9059   -230     93    521       O\\nATOM    604  CB  VAL A 115       8.536  12.862  -7.531  1.00 65.07           C\\nANISOU  604  CB  VAL A 115     7975   8750   7999   -319     -9    719       C\\nATOM    605  CG1 VAL A 115       9.683  13.529  -6.804  1.00 60.52           C\\nANISOU  605  CG1 VAL A 115     7374   8118   7505   -321     36    809       C\\nATOM    606  CG2 VAL A 115       9.043  12.156  -8.778  1.00 62.56           C\\nANISOU  606  CG2 VAL A 115     7676   8649   7446   -346     53    680       C\\nATOM    607  N   MET A 116       6.454  13.232  -5.103  1.00 72.12           N\\nANISOU  607  N   MET A 116     8773   9364   9266   -239    -88    539       N\\nATOM    608  CA  MET A 116       6.164  13.889  -3.832  1.00 68.31           C\\nANISOU  608  CA  MET A 116     8226   8792   8936   -191   -103    487       C\\nATOM    609  C   MET A 116       5.814  12.877  -2.746  1.00 67.37           C\\nANISOU  609  C   MET A 116     8106   8685   8808   -232     19    357       C\\nATOM    610  O   MET A 116       6.435  12.860  -1.677  1.00 67.14           O\\nANISOU  610  O   MET A 116     8105   8604   8802   -221     83    349       O\\nATOM    611  CB  MET A 116       5.031  14.896  -4.005  1.00 66.63           C\\nANISOU  611  CB  MET A 116     7912   8564   8843   -129   -269    455       C\\nATOM    612  CG  MET A 116       4.669  15.602  -2.718  1.00 65.54           C\\nANISOU  612  CG  MET A 116     7676   8370   8856    -46   -291    332       C\\nATOM    613  SD  MET A 116       3.209  16.636  -2.880  1.00 73.08           S\\nANISOU  613  SD  MET A 116     8464   9323   9980     85   -509    199       S\\nATOM    614  CE  MET A 116       3.000  17.178  -1.184  1.00 75.15           C\\nANISOU  614  CE  MET A 116     8597   9592  10365    186   -462    -23       C\\nATOM    615  N   MET A 117       4.820  12.023  -3.000  1.00 57.68           N\\nANISOU  615  N   MET A 117     6854   7527   7535   -303     36    271       N\\nATOM    616  CA  MET A 117       4.373  11.084  -1.977  1.00 63.01           C\\nANISOU  616  CA  MET A 117     7536   8218   8187   -406    135    188       C\\nATOM    617  C   MET A 117       5.457  10.093  -1.578  1.00 71.53           C\\nANISOU  617  C   MET A 117     8783   9196   9201   -439    202    236       C\\nATOM    618  O   MET A 117       5.388   9.526  -0.482  1.00 77.20           O\\nANISOU  618  O   MET A 117     9549   9888   9894   -524    260    225       O\\nATOM    619  CB  MET A 117       3.132  10.337  -2.457  1.00 61.50           C\\nANISOU  619  CB  MET A 117     7283   8115   7968   -518    120    103       C\\nATOM    620  CG  MET A 117       1.975  11.258  -2.770  1.00 64.85           C\\nANISOU  620  CG  MET A 117     7509   8654   8476   -463     28     19       C\\nATOM    621  SD  MET A 117       1.790  12.509  -1.489  1.00 62.59           S\\nANISOU  621  SD  MET A 117     7071   8409   8301   -354     37    -66       S\\nATOM    622  CE  MET A 117       0.518  13.548  -2.206  1.00 56.74           C\\nANISOU  622  CE  MET A 117     6109   7754   7697   -221   -153   -189       C\\nATOM    623  N   CYS A 118       6.449   9.867  -2.434  1.00 70.60           N\\nANISOU  623  N   CYS A 118     8747   9036   9042   -373    183    282       N\\nATOM    624  CA  CYS A 118       7.576   9.023  -2.062  1.00 70.67           C\\nANISOU  624  CA  CYS A 118     8885   8946   9021   -346    211    289       C\\nATOM    625  C   CYS A 118       8.689   9.813  -1.387  1.00 68.27           C\\nANISOU  625  C   CYS A 118     8564   8615   8761   -260    228    351       C\\nATOM    626  O   CYS A 118       9.435   9.249  -0.578  1.00 62.32           O\\nANISOU  626  O   CYS A 118     7898   7774   8009   -239    233    351       O\\nATOM    627  CB  CYS A 118       8.121   8.295  -3.295  1.00 71.86           C\\nANISOU  627  CB  CYS A 118     9091   9112   9101   -295    188    239       C\\nATOM    628  SG  CYS A 118       6.974   7.093  -4.021  1.00 68.74           S\\nANISOU  628  SG  CYS A 118     8755   8698   8664   -398    132    131       S\\nATOM    629  N   THR A 119       8.819  11.105  -1.703  1.00 71.90           N\\nANISOU  629  N   THR A 119     8925   9128   9267   -218    203    409       N\\nATOM    630  CA  THR A 119       9.769  11.947  -0.985  1.00 68.93           C\\nANISOU  630  CA  THR A 119     8523   8711   8956   -165    196    461       C\\nATOM    631  C   THR A 119       9.300  12.212   0.440  1.00 62.52           C\\nANISOU  631  C   THR A 119     7704   7861   8191   -175    201    411       C\\nATOM    632  O   THR A 119      10.125  12.295   1.357  1.00 61.89           O\\nANISOU  632  O   THR A 119     7656   7732   8127   -144    202    417       O\\nATOM    633  CB  THR A 119       9.981  13.271  -1.728  1.00 67.89           C\\nANISOU  633  CB  THR A 119     8314   8606   8874   -156    129    558       C\\nATOM    634  OG1 THR A 119      10.268  13.009  -3.105  1.00 63.88           O\\nANISOU  634  OG1 THR A 119     7808   8202   8260   -182    139    610       O\\nATOM    635  CG2 THR A 119      11.148  14.045  -1.129  1.00 64.40           C\\nANISOU  635  CG2 THR A 119     7848   8113   8507   -132    108    616       C\\nATOM    636  N   ALA A 120       7.987  12.343   0.642  1.00 61.79           N\\nANISOU  636  N   ALA A 120     7547   7824   8105   -218    203    341       N\\nATOM    637  CA  ALA A 120       7.457  12.486   1.992  1.00 59.49           C\\nANISOU  637  CA  ALA A 120     7220   7579   7805   -246    240    258       C\\nATOM    638  C   ALA A 120       7.815  11.283   2.852  1.00 61.28           C\\nANISOU  638  C   ALA A 120     7585   7779   7919   -337    300    286       C\\nATOM    639  O   ALA A 120       8.114  11.433   4.041  1.00 62.06           O\\nANISOU  639  O   ALA A 120     7711   7891   7976   -343    316    271       O\\nATOM    640  CB  ALA A 120       5.943  12.676   1.947  1.00 60.06           C\\nANISOU  640  CB  ALA A 120     7153   7780   7886   -287    251    145       C\\nATOM    641  N   SER A 121       7.784  10.080   2.268  1.00 59.91           N\\nANISOU  641  N   SER A 121     7518   7552   7694   -409    305    325       N\\nATOM    642  CA  SER A 121       8.208   8.889   2.998  1.00 65.17           C\\nANISOU  642  CA  SER A 121     8361   8120   8282   -489    296    378       C\\nATOM    643  C   SER A 121       9.662   9.003   3.431  1.00 68.85           C\\nANISOU  643  C   SER A 121     8900   8486   8775   -361    241    416       C\\nATOM    644  O   SER A 121      10.014   8.643   4.561  1.00 69.48           O\\nANISOU  644  O   SER A 121     9088   8521   8792   -399    214    457       O\\nATOM    645  CB  SER A 121       8.013   7.640   2.137  1.00 61.09           C\\nANISOU  645  CB  SER A 121     7954   7505   7753   -550    254    383       C\\nATOM    646  OG  SER A 121       6.661   7.485   1.747  1.00 71.73           O\\nANISOU  646  OG  SER A 121     9221   8952   9081   -688    290    343       O\\nATOM    647  N   ALA A 122      10.522   9.500   2.544  1.00 66.20           N\\nANISOU  647  N   ALA A 122     8498   8140   8516   -228    219    409       N\\nATOM    648  CA  ALA A 122      11.932   9.632   2.882  1.00 64.09           C\\nANISOU  648  CA  ALA A 122     8247   7817   8288   -115    169    424       C\\nATOM    649  C   ALA A 122      12.144  10.731   3.911  1.00 67.35           C\\nANISOU  649  C   ALA A 122     8599   8264   8729    -99    162    428       C\\nATOM    650  O   ALA A 122      12.870  10.544   4.893  1.00 67.60           O\\nANISOU  650  O   ALA A 122     8699   8245   8739    -68    109    438       O\\nATOM    651  CB  ALA A 122      12.746   9.905   1.621  1.00 62.95           C\\nANISOU  651  CB  ALA A 122     8005   7723   8189    -24    175    411       C\\nATOM    652  N   LEU A 123      11.511  11.886   3.707  1.00 62.65           N\\nANISOU  652  N   LEU A 123     7879   7737   8186   -107    182    403       N\\nATOM    653  CA  LEU A 123      11.661  12.982   4.654  1.00 64.73           C\\nANISOU  653  CA  LEU A 123     8084   8013   8499    -71    145    360       C\\nATOM    654  C   LEU A 123      11.002  12.677   5.993  1.00 68.58           C\\nANISOU  654  C   LEU A 123     8623   8569   8865   -134    179    297       C\\nATOM    655  O   LEU A 123      11.397  13.259   7.008  1.00 65.26           O\\nANISOU  655  O   LEU A 123     8197   8165   8435    -96    140    244       O\\nATOM    656  CB  LEU A 123      11.095  14.271   4.056  1.00 60.03           C\\nANISOU  656  CB  LEU A 123     7361   7429   8020    -42    106    331       C\\nATOM    657  CG  LEU A 123      12.060  15.137   3.236  1.00 62.40           C\\nANISOU  657  CG  LEU A 123     7610   7663   8437    -13     31    421       C\\nATOM    658  CD1 LEU A 123      12.857  14.325   2.223  1.00 59.85           C\\nANISOU  658  CD1 LEU A 123     7308   7374   8057    -33     81    508       C\\nATOM    659  CD2 LEU A 123      11.293  16.248   2.540  1.00 58.42           C\\nANISOU  659  CD2 LEU A 123     7032   7125   8039     -7    -54    431       C\\nATOM    660  N   ASN A 124      10.015  11.778   6.022  1.00 64.20           N\\nANISOU  660  N   ASN A 124     8115   8078   8200   -253    250    303       N\\nATOM    661  CA  ASN A 124       9.452  11.343   7.295  1.00 68.55           C\\nANISOU  661  CA  ASN A 124     8724   8742   8580   -376    301    282       C\\nATOM    662  C   ASN A 124      10.430  10.450   8.047  1.00 72.49           C\\nANISOU  662  C   ASN A 124     9424   9133   8985   -402    229    393       C\\nATOM    663  O   ASN A 124      10.617  10.600   9.260  1.00 78.80           O\\nANISOU  663  O   ASN A 124    10273  10006   9661   -433    215    382       O\\nATOM    664  CB  ASN A 124       8.129  10.616   7.067  1.00 63.03           C\\nANISOU  664  CB  ASN A 124     8004   8152   7791   -549    391    281       C\\nATOM    665  CG  ASN A 124       6.940  11.540   7.141  1.00 59.12           C\\nANISOU  665  CG  ASN A 124     7283   7866   7312   -543    463    113       C\\nATOM    666  OD1 ASN A 124       6.864  12.399   8.016  1.00 58.74           O\\nANISOU  666  OD1 ASN A 124     7141   7941   7236   -481    474    -16       O\\nATOM    667  ND2 ASN A 124       6.000  11.373   6.218  1.00 59.97           N\\nANISOU  667  ND2 ASN A 124     7292   8020   7473   -588    490     83       N\\nATOM    668  N   LEU A 125      11.062   9.508   7.343  1.00 66.29           N\\nANISOU  668  N   LEU A 125     8756   8179   8253   -373    162    480       N\\nATOM    669  CA  LEU A 125      12.084   8.682   7.972  1.00 65.46           C\\nANISOU  669  CA  LEU A 125     8836   7929   8106   -343     35    565       C\\nATOM    670  C   LEU A 125      13.243   9.524   8.477  1.00 65.97           C\\nANISOU  670  C   LEU A 125     8840   7991   8234   -191    -37    522       C\\nATOM    671  O   LEU A 125      13.922   9.139   9.436  1.00 61.15           O\\nANISOU  671  O   LEU A 125     8360   7325   7547   -177   -149    572       O\\nATOM    672  CB  LEU A 125      12.583   7.629   6.988  1.00 62.70           C\\nANISOU  672  CB  LEU A 125     8578   7397   7847   -276    -48    593       C\\nATOM    673  CG  LEU A 125      11.555   6.553   6.663  1.00 64.43           C\\nANISOU  673  CG  LEU A 125     8919   7557   8006   -451    -38    646       C\\nATOM    674  CD1 LEU A 125      12.089   5.633   5.597  1.00 62.96           C\\nANISOU  674  CD1 LEU A 125     8802   7188   7932   -337   -140    608       C\\nATOM    675  CD2 LEU A 125      11.214   5.779   7.920  1.00 61.82           C\\nANISOU  675  CD2 LEU A 125     8799   7183   7505   -650   -100    783       C\\nATOM    676  N   CYS A 126      13.482  10.673   7.849  1.00 67.22           N\\nANISOU  676  N   CYS A 126     8812   8199   8530    -94      0    444       N\\nATOM    677  CA  CYS A 126      14.522  11.568   8.333  1.00 68.85           C\\nANISOU  677  CA  CYS A 126     8945   8402   8814     11    -78    401       C\\nATOM    678  C   CYS A 126      14.084  12.257   9.617  1.00 71.84           C\\nANISOU  678  C   CYS A 126     9323   8885   9086    -30    -78    330       C\\nATOM    679  O   CYS A 126      14.848  12.331  10.588  1.00 74.42           O\\nANISOU  679  O   CYS A 126     9709   9205   9362      8   -177    320       O\\nATOM    680  CB  CYS A 126      14.866  12.592   7.257  1.00 64.79           C\\nANISOU  680  CB  CYS A 126     8252   7891   8474     72    -60    375       C\\nATOM    681  SG  CYS A 126      16.409  13.441   7.561  1.00 69.06           S\\nANISOU  681  SG  CYS A 126     8693   8402   9146    160   -175    353       S\\nATOM    682  N   ALA A 127      12.849  12.762   9.642  1.00 60.58           N\\nANISOU  682  N   ALA A 127     7817   7582   7618    -95     24    250       N\\nATOM    683  CA  ALA A 127      12.322  13.375  10.854  1.00 61.10           C\\nANISOU  683  CA  ALA A 127     7852   7809   7555   -121     44    122       C\\nATOM    684  C   ALA A 127      12.220  12.369  11.990  1.00 65.12           C\\nANISOU  684  C   ALA A 127     8538   8411   7794   -256     52    201       C\\nATOM    685  O   ALA A 127      12.407  12.729  13.158  1.00 65.71           O\\nANISOU  685  O   ALA A 127     8640   8603   7724   -258     16    127       O\\nATOM    686  CB  ALA A 127      10.957  13.996  10.570  1.00 60.25           C\\nANISOU  686  CB  ALA A 127     7585   7843   7462   -141    147    -17       C\\nATOM    687  N   ILE A 128      11.925  11.108  11.673  1.00 64.09           N\\nANISOU  687  N   ILE A 128     8546   8221   7582   -384     77    357       N\\nATOM    688  CA  ILE A 128      11.829  10.083  12.705  1.00 61.38           C\\nANISOU  688  CA  ILE A 128     8417   7924   6982   -558     46    492       C\\nATOM    689  C   ILE A 128      13.184   9.868  13.370  1.00 64.99           C\\nANISOU  689  C   ILE A 128     9025   8241   7426   -455   -148    563       C\\nATOM    690  O   ILE A 128      13.286   9.807  14.600  1.00 69.74           O\\nANISOU  690  O   ILE A 128     9740   8959   7800   -534   -198    591       O\\nATOM    691  CB  ILE A 128      11.271   8.779  12.108  1.00 62.32           C\\nANISOU  691  CB  ILE A 128     8673   7934   7072   -722     61    653       C\\nATOM    692  CG1 ILE A 128       9.772   8.923  11.836  1.00 63.83           C\\nANISOU  692  CG1 ILE A 128     8711   8345   7195   -888    252    582       C\\nATOM    693  CG2 ILE A 128      11.548   7.604  13.028  1.00 64.88           C\\nANISOU  693  CG2 ILE A 128     9290   8172   7190   -886    -69    860       C\\nATOM    694  CD1 ILE A 128       9.120   7.668  11.294  1.00 68.59           C\\nANISOU  694  CD1 ILE A 128     9440   8852   7770  -1092    259    730       C\\nATOM    695  N   SER A 129      14.244   9.756  12.565  1.00 66.20           N\\nANISOU  695  N   SER A 129     9164   8178   7810   -278   -262    578       N\\nATOM    696  CA  SER A 129      15.586   9.611  13.121  1.00 63.02           C\\nANISOU  696  CA  SER A 129     8848   7658   7438   -147   -463    607       C\\nATOM    697  C   SER A 129      15.949  10.799  13.998  1.00 65.47           C\\nANISOU  697  C   SER A 129     9055   8109   7713    -86   -487    474       C\\nATOM    698  O   SER A 129      16.527  10.629  15.078  1.00 65.88           O\\nANISOU  698  O   SER A 129     9234   8177   7619    -82   -631    506       O\\nATOM    699  CB  SER A 129      16.603   9.467  11.995  1.00 65.36           C\\nANISOU  699  CB  SER A 129     9050   7784   7998     39   -538    582       C\\nATOM    700  OG  SER A 129      16.749  10.693  11.302  1.00 65.87           O\\nANISOU  700  OG  SER A 129     8871   7922   8235    114   -445    460       O\\nATOM    701  N   ILE A 130      15.624  12.011  13.546  1.00 64.82           N\\nANISOU  701  N   ILE A 130     8755   8106   7766    -35   -383    319       N\\nATOM    702  CA  ILE A 130      15.959  13.208  14.313  1.00 68.76           C\\nANISOU  702  CA  ILE A 130     9156   8695   8276     36   -439    156       C\\nATOM    703  C   ILE A 130      15.205  13.216  15.636  1.00 70.22           C\\nANISOU  703  C   ILE A 130     9425   9110   8144    -76   -395     92       C\\nATOM    704  O   ILE A 130      15.775  13.502  16.695  1.00 76.17           O\\nANISOU  704  O   ILE A 130    10235   9933   8773    -45   -514     30       O\\nATOM    705  CB  ILE A 130      15.668  14.473  13.488  1.00 69.26           C\\nANISOU  705  CB  ILE A 130     9002   8739   8574    105   -379     19       C\\nATOM    706  CG1 ILE A 130      16.553  14.504  12.241  1.00 65.51           C\\nANISOU  706  CG1 ILE A 130     8440   8094   8355    174   -420    103       C\\nATOM    707  CG2 ILE A 130      15.878  15.716  14.329  1.00 65.28           C\\nANISOU  707  CG2 ILE A 130     8415   8293   8097    175   -469   -180       C\\nATOM    708  CD1 ILE A 130      16.380  15.745  11.402  1.00 62.56           C\\nANISOU  708  CD1 ILE A 130     7895   7673   8203    202   -405     32       C\\nATOM    709  N   ASP A 131      13.909  12.904  15.595  1.00 70.28           N\\nANISOU  709  N   ASP A 131     9426   9280   7998   -221   -219     94       N\\nATOM    710  CA  ASP A 131      13.155  12.749  16.833  1.00 71.28           C\\nANISOU  710  CA  ASP A 131     9617   9702   7763   -378   -141     50       C\\nATOM    711  C   ASP A 131      13.708  11.611  17.677  1.00 75.20           C\\nANISOU  711  C   ASP A 131    10397  10170   8008   -506   -269    283       C\\nATOM    712  O   ASP A 131      13.639  11.660  18.910  1.00 73.14           O\\nANISOU  712  O   ASP A 131    10222  10134   7432   -599   -289    255       O\\nATOM    713  CB  ASP A 131      11.678  12.515  16.525  1.00 70.71           C\\nANISOU  713  CB  ASP A 131     9449   9834   7586   -540     79     22       C\\nATOM    714  CG  ASP A 131      10.820  12.477  17.775  1.00 76.68           C\\nANISOU  714  CG  ASP A 131    10201  10991   7942   -727    206    -66       C\\nATOM    715  OD1 ASP A 131      10.819  13.472  18.528  1.00 78.05           O\\nANISOU  715  OD1 ASP A 131    10254  11363   8039   -619    204   -327       O\\nATOM    716  OD2 ASP A 131      10.140  11.455  18.001  1.00 79.31           O\\nANISOU  716  OD2 ASP A 131    10647  11456   8030   -996    304    118       O\\nATOM    717  N   ARG A 132      14.264  10.581  17.036  1.00 72.55           N\\nANISOU  717  N   ARG A 132    10215   9556   7796   -504   -380    502       N\\nATOM    718  CA  ARG A 132      14.921   9.521  17.791  1.00 74.39           C\\nANISOU  718  CA  ARG A 132    10739   9679   7847   -579   -584    726       C\\nATOM    719  C   ARG A 132      16.221  10.003  18.417  1.00 74.84           C\\nANISOU  719  C   ARG A 132    10811   9673   7954   -388   -804    656       C\\nATOM    720  O   ARG A 132      16.614   9.507  19.479  1.00 74.70           O\\nANISOU  720  O   ARG A 132    11012   9686   7686   -458   -973    778       O\\nATOM    721  CB  ARG A 132      15.175   8.307  16.894  1.00 71.71           C\\nANISOU  721  CB  ARG A 132    10547   9024   7674   -578   -687    923       C\\nATOM    722  CG  ARG A 132      13.976   7.378  16.715  1.00 69.10           C\\nANISOU  722  CG  ARG A 132    10338   8727   7188   -858   -567   1086       C\\nATOM    723  CD  ARG A 132      13.493   6.832  18.055  1.00 75.91           C\\nANISOU  723  CD  ARG A 132    11433   9782   7627  -1155   -591   1269       C\\nATOM    724  NE  ARG A 132      12.518   7.717  18.686  1.00 77.94           N\\nANISOU  724  NE  ARG A 132    11497  10480   7636  -1291   -337   1099       N\\nATOM    725  CZ  ARG A 132      12.271   7.756  19.990  1.00 77.58           C\\nANISOU  725  CZ  ARG A 132    11552  10740   7186  -1484   -317   1141       C\\nATOM    726  NH1 ARG A 132      12.931   6.960  20.822  1.00 76.41           N\\nANISOU  726  NH1 ARG A 132    11728  10477   6827  -1585   -559   1394       N\\nATOM    727  NH2 ARG A 132      11.366   8.602  20.464  1.00 79.78           N\\nANISOU  727  NH2 ARG A 132    11599  11452   7261  -1565    -71    912       N\\nATOM    728  N   TYR A 133      16.902  10.960  17.786  1.00 73.32           N\\nANISOU  728  N   TYR A 133    10393   9395   8070   -171   -822    476       N\\nATOM    729  CA  TYR A 133      18.124  11.492  18.379  1.00 72.55           C\\nANISOU  729  CA  TYR A 133    10271   9257   8037    -13  -1032    389       C\\nATOM    730  C   TYR A 133      17.813  12.311  19.624  1.00 76.41           C\\nANISOU  730  C   TYR A 133    10753  10016   8263    -65  -1020    228       C\\nATOM    731  O   TYR A 133      18.475  12.161  20.658  1.00 82.66           O\\nANISOU  731  O   TYR A 133    11685  10852   8869    -54  -1214    255       O\\nATOM    732  CB  TYR A 133      18.894  12.340  17.365  1.00 65.57           C\\nANISOU  732  CB  TYR A 133     9133   8238   7542    169  -1045    254       C\\nATOM    733  CG  TYR A 133      20.160  12.957  17.931  1.00 69.03           C\\nANISOU  733  CG  TYR A 133     9504   8648   8079    305  -1262    149       C\\nATOM    734  CD1 TYR A 133      21.367  12.268  17.901  1.00 73.59           C\\nANISOU  734  CD1 TYR A 133    10124   9075   8760    424  -1482    232       C\\nATOM    735  CD2 TYR A 133      20.148  14.224  18.502  1.00 67.30           C\\nANISOU  735  CD2 TYR A 133     9162   8546   7862    326  -1271    -61       C\\nATOM    736  CE1 TYR A 133      22.526  12.825  18.419  1.00 73.44           C\\nANISOU  736  CE1 TYR A 133    10011   9052   8839    539  -1690    123       C\\nATOM    737  CE2 TYR A 133      21.303  14.789  19.022  1.00 69.25           C\\nANISOU  737  CE2 TYR A 133     9341   8760   8209    429  -1488   -164       C\\nATOM    738  CZ  TYR A 133      22.488  14.084  18.977  1.00 74.54           C\\nANISOU  738  CZ  TYR A 133    10039   9309   8975    524  -1689    -64       C\\nATOM    739  OH  TYR A 133      23.637  14.640  19.490  1.00 78.51           O\\nANISOU  739  OH  TYR A 133    10443   9800   9586    618  -1914   -178       O\\nATOM    740  N   THR A 134      16.813  13.190  19.544  1.00 70.79           N\\nANISOU  740  N   THR A 134     9871   9496   7530   -102   -814     34       N\\nATOM    741  CA  THR A 134      16.526  14.064  20.674  1.00 74.84           C\\nANISOU  741  CA  THR A 134    10337  10284   7814   -106   -805   -201       C\\nATOM    742  C   THR A 134      16.021  13.276  21.876  1.00 73.81           C\\nANISOU  742  C   THR A 134    10425  10433   7188   -319   -780    -82       C\\nATOM    743  O   THR A 134      16.266  13.672  23.021  1.00 83.45           O\\nANISOU  743  O   THR A 134    11696  11863   8150   -318   -870   -208       O\\nATOM    744  CB  THR A 134      15.517  15.137  20.270  1.00 81.04           C\\nANISOU  744  CB  THR A 134    10877  11199   8715    -61   -617   -471       C\\nATOM    745  OG1 THR A 134      14.231  14.541  20.084  1.00 85.24           O\\nANISOU  745  OG1 THR A 134    11407  11920   9060   -236   -387   -405       O\\nATOM    746  CG2 THR A 134      15.945  15.803  18.969  1.00 80.96           C\\nANISOU  746  CG2 THR A 134    10697  10893   9169     91   -653   -505       C\\nATOM    747  N   ALA A 135      15.341  12.151  21.642  1.00 74.49           N\\nANISOU  747  N   ALA A 135    10655  10530   7120   -527   -674    172       N\\nATOM    748  CA  ALA A 135      14.858  11.340  22.756  1.00 76.81           C\\nANISOU  748  CA  ALA A 135    11182  11087   6918   -800   -658    350       C\\nATOM    749  C   ALA A 135      16.008  10.654  23.480  1.00 76.81           C\\nANISOU  749  C   ALA A 135    11471  10921   6791   -787   -978    571       C\\nATOM    750  O   ALA A 135      15.979  10.505  24.707  1.00 82.26           O\\nANISOU  750  O   ALA A 135    12330  11871   7053   -935  -1044    623       O\\nATOM    751  CB  ALA A 135      13.849  10.307  22.259  1.00 69.76           C\\nANISOU  751  CB  ALA A 135    10373  10203   5930  -1063   -492    588       C\\nATOM    752  N   VAL A 136      17.029  10.233  22.739  1.00 76.95           N\\nANISOU  752  N   VAL A 136    11539  10534   7164   -603  -1189    688       N\\nATOM    753  CA  VAL A 136      18.154   9.535  23.350  1.00 82.31           C\\nANISOU  753  CA  VAL A 136    12472  11024   7777   -545  -1537    878       C\\nATOM    754  C   VAL A 136      19.136  10.524  23.967  1.00 82.04           C\\nANISOU  754  C   VAL A 136    12325  11053   7795   -336  -1708    644       C\\nATOM    755  O   VAL A 136      19.554  10.367  25.120  1.00 81.48           O\\nANISOU  755  O   VAL A 136    12446  11103   7411   -382  -1911    704       O\\nATOM    756  CB  VAL A 136      18.839   8.630  22.309  1.00 77.31           C\\nANISOU  756  CB  VAL A 136    11904   9961   7508   -406  -1706   1045       C\\nATOM    757  CG1 VAL A 136      20.246   8.278  22.755  1.00 77.43           C\\nANISOU  757  CG1 VAL A 136    12049   9764   7606   -210  -2095   1106       C\\nATOM    758  CG2 VAL A 136      18.017   7.366  22.083  1.00 72.64           C\\nANISOU  758  CG2 VAL A 136    11557   9266   6777   -655  -1667   1340       C\\nATOM    759  N   ALA A 137      19.501  11.568  23.224  1.00 77.79           N\\nANISOU  759  N   ALA A 137    11484  10437   7637   -128  -1644    384       N\\nATOM    760  CA  ALA A 137      20.609  12.434  23.603  1.00 80.22           C\\nANISOU  760  CA  ALA A 137    11669  10715   8097     69  -1852    182       C\\nATOM    761  C   ALA A 137      20.209  13.605  24.491  1.00 87.12           C\\nANISOU  761  C   ALA A 137    12440  11898   8765     54  -1780   -115       C\\nATOM    762  O   ALA A 137      21.094  14.243  25.073  1.00 87.55           O\\nANISOU  762  O   ALA A 137    12447  11955   8861    179  -1994   -277       O\\nATOM    763  CB  ALA A 137      21.304  12.975  22.349  1.00 74.40           C\\nANISOU  763  CB  ALA A 137    10663   9730   7877    260  -1849     74       C\\nATOM    764  N   MET A 138      18.922  13.910  24.616  1.00 85.65           N\\nANISOU  764  N   MET A 138    12198  11978   8368    -81  -1504   -224       N\\nATOM    765  CA  MET A 138      18.517  15.099  25.348  1.00 91.36           C\\nANISOU  765  CA  MET A 138    12776  12989   8948    -40  -1439   -587       C\\nATOM    766  C   MET A 138      17.450  14.760  26.377  1.00 93.65           C\\nANISOU  766  C   MET A 138    13184  13730   8670   -264  -1268   -595       C\\nATOM    767  O   MET A 138      16.648  13.844  26.169  1.00 90.32           O\\nANISOU  767  O   MET A 138    12865  13389   8064   -478  -1095   -353       O\\nATOM    768  CB  MET A 138      18.001  16.181  24.387  1.00 94.18           C\\nANISOU  768  CB  MET A 138    12839  13259   9687     83  -1276   -847       C\\nATOM    769  CG  MET A 138      19.095  16.769  23.500  1.00 98.65           C\\nANISOU  769  CG  MET A 138    13264  13452  10767    263  -1446   -874       C\\nATOM    770  SD  MET A 138      18.521  18.077  22.402  1.00105.80           S\\nANISOU  770  SD  MET A 138    13881  14215  12101    371  -1319  -1121       S\\nATOM    771  CE  MET A 138      20.031  18.481  21.533  1.00105.56           C\\nANISOU  771  CE  MET A 138    13744  13805  12559    477  -1542  -1039       C\\nATOM    772  N   PRO A 139      17.425  15.482  27.515  1.00104.46           N\\nANISOU  772  N   PRO A 139    14532  15425   9735   -241  -1315   -880       N\\nATOM    773  CA  PRO A 139      16.509  15.224  28.635  1.00105.59           C\\nANISOU  773  CA  PRO A 139    14765  16095   9259   -469  -1152   -923       C\\nATOM    774  C   PRO A 139      15.042  15.103  28.221  1.00104.65           C\\nANISOU  774  C   PRO A 139    14492  16238   9033   -630   -782   -969       C\\nATOM    775  O   PRO A 139      14.317  16.097  28.261  1.00106.02           O\\nANISOU  775  O   PRO A 139    14394  16653   9234   -519   -617  -1385       O\\nATOM    776  CB  PRO A 139      16.714  16.446  29.535  1.00103.32           C\\nANISOU  776  CB  PRO A 139    14347  16058   8852   -301  -1242  -1390       C\\nATOM    777  CG  PRO A 139      18.112  16.868  29.263  1.00100.62           C\\nANISOU  777  CG  PRO A 139    14009  15289   8934    -72  -1575  -1406       C\\nATOM    778  CD  PRO A 139      18.340  16.603  27.805  1.00 97.12           C\\nANISOU  778  CD  PRO A 139    13483  14389   9030     -4  -1545  -1193       C\\nATOM    779  N   THR A 144       8.716  17.350  27.929  1.00103.31           N\\nANISOU  779  N   THR A 144    12885  17966   8400   -718    631  -2535       N\\nATOM    780  CA  THR A 144       7.590  18.233  28.208  1.00111.55           C\\nANISOU  780  CA  THR A 144    13533  19499   9351   -578    832  -3111       C\\nATOM    781  C   THR A 144       6.396  17.895  27.318  1.00111.78           C\\nANISOU  781  C   THR A 144    13322  19627   9521   -685   1084  -3075       C\\nATOM    782  O   THR A 144       6.556  17.666  26.122  1.00115.16           O\\nANISOU  782  O   THR A 144    13802  19541  10411   -631   1006  -2812       O\\nATOM    783  CB  THR A 144       7.971  19.712  28.006  1.00112.47           C\\nANISOU  783  CB  THR A 144    13477  19327   9931   -104    597  -3618       C\\nATOM    784  N   ARG A 145       5.198  17.868  27.907  1.00112.87           N\\nANISOU  784  N   ARG A 145    13181  20279   9425   -824   1334  -3251       N\\nATOM    785  CA  ARG A 145       4.002  17.509  27.151  1.00114.09           C\\nANISOU  785  CA  ARG A 145    13078  20551   9719   -950   1551  -3212       C\\nATOM    786  C   ARG A 145       3.581  18.596  26.170  1.00118.73           C\\nANISOU  786  C   ARG A 145    13352  20930  10830   -531   1477  -3651       C\\nATOM    787  O   ARG A 145       2.846  18.305  25.221  1.00119.01           O\\nANISOU  787  O   ARG A 145    13234  20913  11072   -582   1585  -3578       O\\nATOM    788  CB  ARG A 145       2.846  17.198  28.104  1.00118.50           C\\nANISOU  788  CB  ARG A 145    13396  21689   9937  -1221   1786  -3270       C\\nATOM    789  N   TYR A 146       4.024  19.834  26.375  1.00121.59           N\\nANISOU  789  N   TYR A 146    13630  21133  11434   -123   1259  -4089       N\\nATOM    790  CA  TYR A 146       3.700  20.948  25.491  1.00117.64           C\\nANISOU  790  CA  TYR A 146    12880  20335  11482    295   1102  -4485       C\\nATOM    791  C   TYR A 146       4.829  21.280  24.526  1.00108.31           C\\nANISOU  791  C   TYR A 146    11951  18428  10772    498    805  -4303       C\\nATOM    792  O   TYR A 146       4.573  21.530  23.344  1.00100.71           O\\nANISOU  792  O   TYR A 146    10911  17078  10275    638    718  -4241       O\\nATOM    793  CB  TYR A 146       3.345  22.185  26.325  1.00124.08           C\\nANISOU  793  CB  TYR A 146    13429  21323  12394    606    974  -5030       C\\nATOM    794  CG  TYR A 146       3.156  23.462  25.533  1.00125.41           C\\nANISOU  794  CG  TYR A 146    13400  21084  13165   1062    702  -5422       C\\nATOM    795  CD1 TYR A 146       1.920  23.794  24.993  1.00128.22           C\\nANISOU  795  CD1 TYR A 146    13405  21556  13758   1181    740  -5641       C\\nATOM    796  CD2 TYR A 146       4.211  24.347  25.345  1.00125.84           C\\nANISOU  796  CD2 TYR A 146    13634  20614  13563   1355    362  -5554       C\\nATOM    797  CE1 TYR A 146       1.746  24.966  24.276  1.00131.82           C\\nANISOU  797  CE1 TYR A 146    13721  21595  14769   1588    432  -5955       C\\nATOM    798  CE2 TYR A 146       4.047  25.515  24.631  1.00128.03           C\\nANISOU  798  CE2 TYR A 146    13776  20456  14413   1732     64  -5846       C\\nATOM    799  CZ  TYR A 146       2.815  25.821  24.099  1.00132.64           C\\nANISOU  799  CZ  TYR A 146    14037  21147  15214   1852     92  -6034       C\\nATOM    800  OH  TYR A 146       2.656  26.988  23.388  1.00136.93           O\\nANISOU  800  OH  TYR A 146    14484  21222  16320   2213   -261  -6277       O\\nATOM    801  N   SER A 147       6.076  21.287  25.005  1.00108.97           N\\nANISOU  801  N   SER A 147    12336  18257  10810    490    611  -4125       N\\nATOM    802  CA  SER A 147       7.206  21.602  24.138  1.00104.01           C\\nANISOU  802  CA  SER A 147    11926  16901  10691    633    308  -3860       C\\nATOM    803  C   SER A 147       7.407  20.541  23.065  1.00103.85           C\\nANISOU  803  C   SER A 147    12083  16559  10818    407    370  -3277       C\\nATOM    804  O   SER A 147       7.842  20.861  21.953  1.00 99.45           O\\nANISOU  804  O   SER A 147    11570  15480  10738    539    199  -3123       O\\nATOM    805  CB  SER A 147       8.481  21.758  24.972  1.00101.67           C\\nANISOU  805  CB  SER A 147    11877  16479  10273    647     99  -3814       C\\nATOM    806  N   SER A 148       7.103  19.279  23.375  1.00100.58           N\\nANISOU  806  N   SER A 148    11778  16447   9991     56    598  -2950       N\\nATOM    807  CA  SER A 148       7.325  18.214  22.404  1.00 97.98           C\\nANISOU  807  CA  SER A 148    11636  15794   9798   -147    625  -2427       C\\nATOM    808  C   SER A 148       6.273  18.239  21.303  1.00 88.88           C\\nANISOU  808  C   SER A 148    10254  14611   8905   -117    745  -2472       C\\nATOM    809  O   SER A 148       6.602  18.071  20.125  1.00 80.56           O\\nANISOU  809  O   SER A 148     9283  13109   8218    -74    646  -2217       O\\nATOM    810  CB  SER A 148       7.339  16.858  23.106  1.00103.00           C\\nANISOU  810  CB  SER A 148    12497  16702   9935   -541    771  -2055       C\\nATOM    811  OG  SER A 148       6.089  16.599  23.719  1.00106.17           O\\nANISOU  811  OG  SER A 148    12692  17721   9926   -754   1057  -2228       O\\nATOM    812  N   LYS A 149       5.003  18.446  21.667  1.00 92.05           N\\nANISOU  812  N   LYS A 149    10349  15519   9108   -139    955  -2812       N\\nATOM    813  CA  LYS A 149       3.946  18.506  20.661  1.00 84.26           C\\nANISOU  813  CA  LYS A 149     9110  14536   8369    -93   1046  -2895       C\\nATOM    814  C   LYS A 149       4.192  19.638  19.673  1.00 88.93           C\\nANISOU  814  C   LYS A 149     9627  14634   9529    289    781  -3067       C\\nATOM    815  O   LYS A 149       3.943  19.488  18.470  1.00 93.01           O\\nANISOU  815  O   LYS A 149    10125  14862  10350    308    742  -2887       O\\nATOM    816  CB  LYS A 149       2.585  18.670  21.333  1.00 79.97           C\\nANISOU  816  CB  LYS A 149     8188  14678   7518   -142   1299  -3315       C\\nATOM    817  N   ARG A 150       4.688  20.778  20.160  1.00 87.49           N\\nANISOU  817  N   ARG A 150     9416  14340   9487    578    575  -3405       N\\nATOM    818  CA  ARG A 150       5.060  21.865  19.261  1.00 81.69           C\\nANISOU  818  CA  ARG A 150     8671  13071   9295    893    273  -3505       C\\nATOM    819  C   ARG A 150       6.223  21.474  18.359  1.00 80.21           C\\nANISOU  819  C   ARG A 150     8786  12341   9349    799    130  -2998       C\\nATOM    820  O   ARG A 150       6.317  21.964  17.230  1.00 82.46           O\\nANISOU  820  O   ARG A 150     9071  12222  10039    928    -38  -2909       O\\nATOM    821  CB  ARG A 150       5.411  23.117  20.063  1.00 80.33           C\\nANISOU  821  CB  ARG A 150     8437  12868   9215   1187     52  -3965       C\\nATOM    822  N   ARG A 151       7.111  20.595  18.831  1.00 78.36           N\\nANISOU  822  N   ARG A 151     8802  12110   8862    578    185  -2672       N\\nATOM    823  CA  ARG A 151       8.234  20.166  18.003  1.00 72.71           C\\nANISOU  823  CA  ARG A 151     8328  10937   8361    507     62  -2239       C\\nATOM    824  C   ARG A 151       7.780  19.202  16.916  1.00 79.91           C\\nANISOU  824  C   ARG A 151     9266  11777   9319    342    198  -1915       C\\nATOM    825  O   ARG A 151       8.310  19.226  15.799  1.00 80.42           O\\nANISOU  825  O   ARG A 151     9410  11464   9683    376     87  -1687       O\\nATOM    826  CB  ARG A 151       9.319  19.528  18.870  1.00 74.01           C\\nANISOU  826  CB  ARG A 151     8732  11123   8264    367     34  -2034       C\\nATOM    827  CG  ARG A 151      10.576  19.134  18.110  1.00 82.30           C\\nANISOU  827  CG  ARG A 151     9986  11745   9540    333   -108  -1658       C\\nATOM    828  CD  ARG A 151      11.637  18.577  19.045  1.00 87.06           C\\nANISOU  828  CD  ARG A 151    10798  12374   9905    242   -184  -1509       C\\nATOM    829  NE  ARG A 151      11.097  17.537  19.917  1.00 91.56           N\\nANISOU  829  NE  ARG A 151    11463  13317  10010     18     -7  -1413       N\\nATOM    830  CZ  ARG A 151      11.047  16.249  19.600  1.00 88.57           C\\nANISOU  830  CZ  ARG A 151    11241  12910   9500   -194     83  -1059       C\\nATOM    831  NH1 ARG A 151      10.538  15.370  20.453  1.00 83.32           N\\nANISOU  831  NH1 ARG A 151    10680  12574   8402   -440    216   -953       N\\nATOM    832  NH2 ARG A 151      11.506  15.837  18.428  1.00 87.56           N\\nANISOU  832  NH2 ARG A 151    11174  12429   9667   -175     27   -816       N\\nATOM    833  N   VAL A 152       6.797  18.350  17.218  1.00 81.56           N\\nANISOU  833  N   VAL A 152     9402  12365   9221    140    437  -1897       N\\nATOM    834  CA  VAL A 152       6.288  17.429  16.204  1.00 81.36           C\\nANISOU  834  CA  VAL A 152     9394  12272   9245    -25    549  -1623       C\\nATOM    835  C   VAL A 152       5.564  18.196  15.104  1.00 80.65           C\\nANISOU  835  C   VAL A 152     9093  12045   9504    168    481  -1785       C\\nATOM    836  O   VAL A 152       5.709  17.888  13.915  1.00 78.73           O\\nANISOU  836  O   VAL A 152     8921  11517   9474    149    431  -1543       O\\nATOM    837  CB  VAL A 152       5.377  16.364  16.843  1.00 80.98           C\\nANISOU  837  CB  VAL A 152     9312  12669   8787   -333    803  -1562       C\\nATOM    838  CG1 VAL A 152       5.106  15.241  15.863  1.00 82.24           C\\nANISOU  838  CG1 VAL A 152     9570  12682   8997   -541    871  -1224       C\\nATOM    839  CG2 VAL A 152       6.004  15.810  18.104  1.00 83.35           C\\nANISOU  839  CG2 VAL A 152     9819  13145   8703   -511    831  -1443       C\\nATOM    840  N   THR A 153       4.781  19.211  15.482  1.00 84.22           N\\nANISOU  840  N   THR A 153     9285  12700  10015    371    455  -2213       N\\nATOM    841  CA  THR A 153       4.057  20.004  14.492  1.00 78.54           C\\nANISOU  841  CA  THR A 153     8369  11830   9642    587    332  -2387       C\\nATOM    842  C   THR A 153       5.011  20.696  13.525  1.00 75.61           C\\nANISOU  842  C   THR A 153     8160  10910   9657    737     57  -2208       C\\nATOM    843  O   THR A 153       4.738  20.779  12.322  1.00 76.21           O\\nANISOU  843  O   THR A 153     8221  10766   9967    773    -25  -2073       O\\nATOM    844  CB  THR A 153       3.168  21.031  15.195  1.00 80.46           C\\nANISOU  844  CB  THR A 153     8306  12365   9901    832    300  -2933       C\\nATOM    845  OG1 THR A 153       2.144  20.354  15.937  1.00 82.11           O\\nANISOU  845  OG1 THR A 153     8305  13162   9733    652    595  -3096       O\\nATOM    846  CG2 THR A 153       2.527  21.976  14.186  1.00 77.79           C\\nANISOU  846  CG2 THR A 153     7796  11785   9977   1109     80  -3121       C\\nATOM    847  N   VAL A 154       6.141  21.193  14.030  1.00 73.65           N\\nANISOU  847  N   VAL A 154     8065  10459   9460    799    -90  -2194       N\\nATOM    848  CA  VAL A 154       7.112  21.843  13.156  1.00 71.40           C\\nANISOU  848  CA  VAL A 154     7922   9692   9516    880   -337  -2000       C\\nATOM    849  C   VAL A 154       7.787  20.821  12.246  1.00 67.73           C\\nANISOU  849  C   VAL A 154     7638   9069   9028    675   -255  -1548       C\\nATOM    850  O   VAL A 154       8.007  21.079  11.057  1.00 61.81           O\\nANISOU  850  O   VAL A 154     6927   8041   8515    690   -370  -1361       O\\nATOM    851  CB  VAL A 154       8.137  22.627  13.993  1.00 65.37           C\\nANISOU  851  CB  VAL A 154     7244   8781   8811    974   -518  -2127       C\\nATOM    852  CG1 VAL A 154       9.256  23.154  13.108  1.00 56.93           C\\nANISOU  852  CG1 VAL A 154     6321   7254   8055    968   -742  -1864       C\\nATOM    853  CG2 VAL A 154       7.453  23.767  14.722  1.00 60.75           C\\nANISOU  853  CG2 VAL A 154     6475   8294   8312   1228   -654  -2627       C\\nATOM    854  N   MET A 155       8.122  19.645  12.784  1.00 69.04           N\\nANISOU  854  N   MET A 155     7921   9413   8899    483    -75  -1374       N\\nATOM    855  CA  MET A 155       8.784  18.630  11.972  1.00 68.64           C\\nANISOU  855  CA  MET A 155     8035   9207   8837    329    -24  -1003       C\\nATOM    856  C   MET A 155       7.875  18.134  10.856  1.00 64.55           C\\nANISOU  856  C   MET A 155     7452   8706   8368    269     63   -905       C\\nATOM    857  O   MET A 155       8.316  17.979   9.712  1.00 59.62           O\\nANISOU  857  O   MET A 155     6898   7863   7894    252      8   -690       O\\nATOM    858  CB  MET A 155       9.241  17.467  12.851  1.00 72.37           C\\nANISOU  858  CB  MET A 155     8663   9833   9001    158     94   -859       C\\nATOM    859  CG  MET A 155      10.407  17.803  13.768  1.00 80.64           C\\nANISOU  859  CG  MET A 155     9815  10814  10011    208    -29   -884       C\\nATOM    860  SD  MET A 155      11.031  16.373  14.674  1.00 89.65           S\\nANISOU  860  SD  MET A 155    11184  12069  10810     19     37   -657       S\\nATOM    861  CE  MET A 155      12.405  17.110  15.553  1.00 99.07           C\\nANISOU  861  CE  MET A 155    12443  13153  12047    140   -171   -742       C\\nATOM    862  N   ILE A 156       6.602  17.886  11.166  1.00 67.34           N\\nANISOU  862  N   ILE A 156     7652   9352   8582    227    200  -1075       N\\nATOM    863  CA  ILE A 156       5.685  17.372  10.156  1.00 68.91           C\\nANISOU  863  CA  ILE A 156     7773   9590   8821    157    271  -1001       C\\nATOM    864  C   ILE A 156       5.469  18.403   9.059  1.00 69.08           C\\nANISOU  864  C   ILE A 156     7705   9384   9158    345     81  -1053       C\\nATOM    865  O   ILE A 156       5.484  18.072   7.867  1.00 70.31           O\\nANISOU  865  O   ILE A 156     7916   9392   9407    300     52   -852       O\\nATOM    866  CB  ILE A 156       4.357  16.945  10.806  1.00 70.36           C\\nANISOU  866  CB  ILE A 156     7765  10184   8786     48    458  -1197       C\\nATOM    867  CG1 ILE A 156       4.590  15.773  11.761  1.00 67.02           C\\nANISOU  867  CG1 ILE A 156     7488   9956   8020   -215    628  -1044       C\\nATOM    868  CG2 ILE A 156       3.332  16.571   9.742  1.00 64.85           C\\nANISOU  868  CG2 ILE A 156     6940   9528   8171     -3    496  -1169       C\\nATOM    869  CD1 ILE A 156       3.333  15.249  12.401  1.00 60.59           C\\nANISOU  869  CD1 ILE A 156     6493   9587   6942   -411    838  -1180       C\\nATOM    870  N   SER A 157       5.271  19.668   9.439  1.00 67.59           N\\nANISOU  870  N   SER A 157     7393   9155   9133    558    -76  -1325       N\\nATOM    871  CA  SER A 157       5.081  20.719   8.446  1.00 66.91           C\\nANISOU  871  CA  SER A 157     7261   8799   9364    734   -321  -1352       C\\nATOM    872  C   SER A 157       6.261  20.789   7.488  1.00 65.20           C\\nANISOU  872  C   SER A 157     7252   8247   9275    664   -437  -1006       C\\nATOM    873  O   SER A 157       6.079  20.905   6.271  1.00 70.97           O\\nANISOU  873  O   SER A 157     8005   8831  10130    658   -531   -845       O\\nATOM    874  CB  SER A 157       4.876  22.064   9.138  1.00 53.19           C\\nANISOU  874  CB  SER A 157     5403   7001   7805    983   -525  -1706       C\\nATOM    875  OG  SER A 157       3.770  22.013  10.019  1.00 59.25           O\\nANISOU  875  OG  SER A 157     5930   8154   8428   1059   -395  -2076       O\\nATOM    876  N   ILE A 158       7.481  20.701   8.019  1.00 63.38           N\\nANISOU  876  N   ILE A 158     7159   7930   8993    600   -428   -895       N\\nATOM    877  CA  ILE A 158       8.662  20.757   7.168  1.00 62.29           C\\nANISOU  877  CA  ILE A 158     7167   7544   8955    516   -512   -595       C\\nATOM    878  C   ILE A 158       8.684  19.577   6.207  1.00 66.42           C\\nANISOU  878  C   ILE A 158     7754   8134   9350    369   -356   -352       C\\nATOM    879  O   ILE A 158       9.069  19.717   5.042  1.00 76.92           O\\nANISOU  879  O   ILE A 158     9134   9324  10767    323   -426   -148       O\\nATOM    880  CB  ILE A 158       9.935  20.815   8.030  1.00 62.52           C\\nANISOU  880  CB  ILE A 158     7286   7519   8948    483   -529   -568       C\\nATOM    881  CG1 ILE A 158       9.969  22.114   8.833  1.00 61.54           C\\nANISOU  881  CG1 ILE A 158     7112   7280   8990    635   -734   -823       C\\nATOM    882  CG2 ILE A 158      11.177  20.683   7.165  1.00 56.51           C\\nANISOU  882  CG2 ILE A 158     6625   6594   8253    369   -564   -273       C\\nATOM    883  CD1 ILE A 158      11.102  22.178   9.819  1.00 68.44           C\\nANISOU  883  CD1 ILE A 158     8055   8136   9811    610   -764   -846       C\\nATOM    884  N   VAL A 159       8.260  18.399   6.670  1.00 61.58           N\\nANISOU  884  N   VAL A 159     7145   7737   8515    280   -157   -371       N\\nATOM    885  CA  VAL A 159       8.270  17.217   5.808  1.00 61.95           C\\nANISOU  885  CA  VAL A 159     7267   7816   8456    152    -40   -177       C\\nATOM    886  C   VAL A 159       7.403  17.448   4.578  1.00 58.47           C\\nANISOU  886  C   VAL A 159     6754   7353   8111    173    -97   -152       C\\nATOM    887  O   VAL A 159       7.847  17.270   3.437  1.00 64.62           O\\nANISOU  887  O   VAL A 159     7599   8038   8915    129   -128     32       O\\nATOM    888  CB  VAL A 159       7.811  15.973   6.589  1.00 61.71           C\\nANISOU  888  CB  VAL A 159     7270   7984   8194     28    136   -202       C\\nATOM    889  CG1 VAL A 159       7.571  14.812   5.641  1.00 58.85           C\\nANISOU  889  CG1 VAL A 159     6974   7622   7763    -90    212    -53       C\\nATOM    890  CG2 VAL A 159       8.840  15.593   7.634  1.00 64.69           C\\nANISOU  890  CG2 VAL A 159     7772   8351   8457     -6    154   -157       C\\nATOM    891  N   TRP A 160       6.156  17.865   4.792  1.00 55.67           N\\nANISOU  891  N   TRP A 160     6244   7112   7797    249   -122   -357       N\\nATOM    892  CA  TRP A 160       5.209  17.964   3.688  1.00 61.87           C\\nANISOU  892  CA  TRP A 160     6946   7902   8658    275   -191   -352       C\\nATOM    893  C   TRP A 160       5.414  19.222   2.854  1.00 68.14           C\\nANISOU  893  C   TRP A 160     7758   8458   9675    394   -447   -287       C\\nATOM    894  O   TRP A 160       5.155  19.201   1.645  1.00 72.46           O\\nANISOU  894  O   TRP A 160     8331   8951  10250    369   -527   -148       O\\nATOM    895  CB  TRP A 160       3.778  17.893   4.226  1.00 54.20           C\\nANISOU  895  CB  TRP A 160     5762   7176   7654    313   -130   -618       C\\nATOM    896  CG  TRP A 160       3.447  16.528   4.729  1.00 59.47           C\\nANISOU  896  CG  TRP A 160     6436   8074   8087    111    106   -599       C\\nATOM    897  CD1 TRP A 160       3.428  16.111   6.027  1.00 64.43           C\\nANISOU  897  CD1 TRP A 160     7047   8894   8538     21    258   -694       C\\nATOM    898  CD2 TRP A 160       3.129  15.380   3.933  1.00 65.48           C\\nANISOU  898  CD2 TRP A 160     7253   8873   8755    -53    190   -456       C\\nATOM    899  NE1 TRP A 160       3.105  14.776   6.089  1.00 64.83           N\\nANISOU  899  NE1 TRP A 160     7153   9080   8400   -211    420   -586       N\\nATOM    900  CE2 TRP A 160       2.917  14.305   4.817  1.00 67.13           C\\nANISOU  900  CE2 TRP A 160     7487   9263   8758   -251    374   -455       C\\nATOM    901  CE3 TRP A 160       2.997  15.161   2.558  1.00 66.76           C\\nANISOU  901  CE3 TRP A 160     7455   8935   8975    -62    110   -331       C\\nATOM    902  CZ2 TRP A 160       2.575  13.030   4.371  1.00 70.04           C\\nANISOU  902  CZ2 TRP A 160     7926   9666   9019   -454    457   -337       C\\nATOM    903  CZ3 TRP A 160       2.659  13.895   2.117  1.00 69.12           C\\nANISOU  903  CZ3 TRP A 160     7807   9302   9154   -239    209   -252       C\\nATOM    904  CH2 TRP A 160       2.451  12.846   3.021  1.00 68.25           C\\nANISOU  904  CH2 TRP A 160     7727   9325   8880   -431    370   -257       C\\nATOM    905  N   VAL A 161       5.874  20.317   3.463  1.00 67.95           N\\nANISOU  905  N   VAL A 161     7737   8280   9802    507   -599   -373       N\\nATOM    906  CA  VAL A 161       6.140  21.520   2.680  1.00 69.19           C\\nANISOU  906  CA  VAL A 161     7952   8155  10182    576   -883   -262       C\\nATOM    907  C   VAL A 161       7.379  21.323   1.823  1.00 65.64           C\\nANISOU  907  C   VAL A 161     7665   7597   9678    402   -867     76       C\\nATOM    908  O   VAL A 161       7.447  21.799   0.684  1.00 71.00           O\\nANISOU  908  O   VAL A 161     8411   8144  10420    354  -1023    278       O\\nATOM    909  CB  VAL A 161       6.273  22.747   3.599  1.00 68.92           C\\nANISOU  909  CB  VAL A 161     7883   7953  10351    740  -1087   -473       C\\nATOM    910  CG1 VAL A 161       6.754  23.958   2.810  1.00 55.10           C\\nANISOU  910  CG1 VAL A 161     6251   5845   8841    751  -1414   -291       C\\nATOM    911  CG2 VAL A 161       4.941  23.041   4.271  1.00 68.37           C\\nANISOU  911  CG2 VAL A 161     7604   8033  10340    947  -1123   -858       C\\nATOM    912  N   LEU A 162       8.370  20.607   2.346  1.00 57.34           N\\nANISOU  912  N   LEU A 162     6669   6627   8492    302   -683    137       N\\nATOM    913  CA  LEU A 162       9.567  20.343   1.562  1.00 62.34           C\\nANISOU  913  CA  LEU A 162     7399   7226   9060    152   -640    403       C\\nATOM    914  C   LEU A 162       9.274  19.375   0.424  1.00 64.44           C\\nANISOU  914  C   LEU A 162     7686   7633   9165     68   -521    527       C\\nATOM    915  O   LEU A 162       9.756  19.565  -0.698  1.00 73.70           O\\nANISOU  915  O   LEU A 162     8910   8787  10307    -32   -568    735       O\\nATOM    916  CB  LEU A 162      10.668  19.803   2.467  1.00 66.33           C\\nANISOU  916  CB  LEU A 162     7929   7786   9485    111   -507    389       C\\nATOM    917  CG  LEU A 162      12.083  19.741   1.909  1.00 71.44           C\\nANISOU  917  CG  LEU A 162     8616   8419  10108    -16   -484    596       C\\nATOM    918  CD1 LEU A 162      12.409  21.020   1.165  1.00 63.78           C\\nANISOU  918  CD1 LEU A 162     7665   7275   9293    -96   -691    765       C\\nATOM    919  CD2 LEU A 162      13.044  19.530   3.061  1.00 75.47           C\\nANISOU  919  CD2 LEU A 162     9125   8941  10610      0   -439    519       C\\nATOM    920  N   SER A 163       8.481  18.334   0.691  1.00 62.39           N\\nANISOU  920  N   SER A 163     7390   7531   8786     86   -371    399       N\\nATOM    921  CA  SER A 163       8.099  17.410  -0.371  1.00 64.81           C\\nANISOU  921  CA  SER A 163     7718   7951   8957     15   -289    475       C\\nATOM    922  C   SER A 163       7.384  18.143  -1.499  1.00 65.90           C\\nANISOU  922  C   SER A 163     7840   8039   9160     33   -467    552       C\\nATOM    923  O   SER A 163       7.634  17.874  -2.680  1.00 71.94           O\\nANISOU  923  O   SER A 163     8662   8855   9817    -51   -466    710       O\\nATOM    924  CB  SER A 163       7.213  16.302   0.193  1.00 64.78           C\\nANISOU  924  CB  SER A 163     7674   8087   8852      4   -146    321       C\\nATOM    925  OG  SER A 163       7.785  15.740   1.357  1.00 61.15           O\\nANISOU  925  OG  SER A 163     7254   7650   8329    -18    -31    269       O\\nATOM    926  N   PHE A 164       6.497  19.078  -1.153  1.00 60.59           N\\nANISOU  926  N   PHE A 164     7089   7277   8655    156   -639    427       N\\nATOM    927  CA  PHE A 164       5.825  19.887  -2.164  1.00 61.72           C\\nANISOU  927  CA  PHE A 164     7234   7322   8893    201   -880    505       C\\nATOM    928  C   PHE A 164       6.833  20.691  -2.972  1.00 65.16           C\\nANISOU  928  C   PHE A 164     7806   7601   9350     94  -1027    793       C\\nATOM    929  O   PHE A 164       6.879  20.597  -4.203  1.00 65.92           O\\nANISOU  929  O   PHE A 164     7974   7746   9327    -10  -1074    992       O\\nATOM    930  CB  PHE A 164       4.803  20.813  -1.496  1.00 57.42           C\\nANISOU  930  CB  PHE A 164     6564   6683   8568    400  -1076    267       C\\nATOM    931  CG  PHE A 164       4.135  21.779  -2.443  1.00 61.42           C\\nANISOU  931  CG  PHE A 164     7089   7023   9226    488  -1405    340       C\\nATOM    932  CD1 PHE A 164       3.067  21.374  -3.232  1.00 63.79           C\\nANISOU  932  CD1 PHE A 164     7317   7446   9476    519  -1453    302       C\\nATOM    933  CD2 PHE A 164       4.563  23.097  -2.528  1.00 60.79           C\\nANISOU  933  CD2 PHE A 164     7109   6640   9350    534  -1703    451       C\\nATOM    934  CE1 PHE A 164       2.450  22.259  -4.099  1.00 64.22           C\\nANISOU  934  CE1 PHE A 164     7400   7336   9667    615  -1799    378       C\\nATOM    935  CE2 PHE A 164       3.946  23.988  -3.393  1.00 65.28           C\\nANISOU  935  CE2 PHE A 164     7729   7008  10065    614  -2062    545       C\\nATOM    936  CZ  PHE A 164       2.889  23.566  -4.178  1.00 64.54           C\\nANISOU  936  CZ  PHE A 164     7564   7051   9906    666  -2113    510       C\\nATOM    937  N   THR A 165       7.667  21.477  -2.285  1.00 60.91           N\\nANISOU  937  N   THR A 165     7302   6899   8944     90  -1100    820       N\\nATOM    938  CA  THR A 165       8.590  22.366  -2.984  1.00 68.08           C\\nANISOU  938  CA  THR A 165     8326   7648   9893    -59  -1264   1109       C\\nATOM    939  C   THR A 165       9.585  21.592  -3.836  1.00 67.06           C\\nANISOU  939  C   THR A 165     8237   7731   9511   -266  -1055   1321       C\\nATOM    940  O   THR A 165      10.068  22.114  -4.846  1.00 74.56           O\\nANISOU  940  O   THR A 165     9269   8666  10395   -439  -1158   1596       O\\nATOM    941  CB  THR A 165       9.335  23.256  -1.988  1.00 72.21           C\\nANISOU  941  CB  THR A 165     8862   7963  10613    -43  -1373   1067       C\\nATOM    942  OG1 THR A 165      10.064  22.439  -1.068  1.00 84.36           O\\nANISOU  942  OG1 THR A 165    10343   9656  12055    -52  -1111    946       O\\nATOM    943  CG2 THR A 165       8.362  24.133  -1.215  1.00 69.54           C\\nANISOU  943  CG2 THR A 165     8475   7415  10531    191  -1616    813       C\\nATOM    944  N   ILE A 166       9.898  20.352  -3.455  1.00 69.64           N\\nANISOU  944  N   ILE A 166     8506   8267   9687   -255   -775   1193       N\\nATOM    945  CA  ILE A 166      10.825  19.548  -4.247  1.00 72.15           C\\nANISOU  945  CA  ILE A 166     8831   8805   9778   -397   -585   1317       C\\nATOM    946  C   ILE A 166      10.150  19.043  -5.520  1.00 72.60           C\\nANISOU  946  C   ILE A 166     8918   9016   9653   -435   -578   1379       C\\nATOM    947  O   ILE A 166      10.751  19.045  -6.601  1.00 74.34           O\\nANISOU  947  O   ILE A 166     9167   9388   9690   -588   -548   1564       O\\nATOM    948  CB  ILE A 166      11.383  18.389  -3.402  1.00 64.44           C\\nANISOU  948  CB  ILE A 166     7804   7945   8737   -337   -355   1141       C\\nATOM    949  CG1 ILE A 166      12.401  18.911  -2.386  1.00 65.09           C\\nANISOU  949  CG1 ILE A 166     7859   7927   8946   -345   -368   1133       C\\nATOM    950  CG2 ILE A 166      12.008  17.326  -4.294  1.00 61.90           C\\nANISOU  950  CG2 ILE A 166     7469   7861   8189   -405   -177   1168       C\\nATOM    951  CD1 ILE A 166      12.979  17.825  -1.505  1.00 55.41           C\\nANISOU  951  CD1 ILE A 166     6604   6788   7663   -276   -195    979       C\\nATOM    952  N   SER A 167       8.896  18.605  -5.414  1.00 66.08           N\\nANISOU  952  N   SER A 167     8070   8185   8852   -311   -603   1216       N\\nATOM    953  CA  SER A 167       8.168  18.066  -6.554  1.00 69.77           C\\nANISOU  953  CA  SER A 167     8557   8794   9156   -335   -616   1237       C\\nATOM    954  C   SER A 167       7.500  19.138  -7.404  1.00 70.97           C\\nANISOU  954  C   SER A 167     8769   8841   9355   -354   -900   1407       C\\nATOM    955  O   SER A 167       7.132  18.860  -8.553  1.00 69.63           O\\nANISOU  955  O   SER A 167     8642   8809   9005   -415   -942   1493       O\\nATOM    956  CB  SER A 167       7.104  17.078  -6.070  1.00 67.68           C\\nANISOU  956  CB  SER A 167     8226   8582   8907   -228   -531    989       C\\nATOM    957  OG  SER A 167       6.153  17.737  -5.251  1.00 68.82           O\\nANISOU  957  OG  SER A 167     8295   8591   9261   -104   -663    859       O\\nATOM    958  N   CYS A 168       7.324  20.345  -6.871  1.00 72.75           N\\nANISOU  958  N   CYS A 168     9009   8812   9819   -293  -1126   1446       N\\nATOM    959  CA  CYS A 168       6.648  21.393  -7.631  1.00 73.51           C\\nANISOU  959  CA  CYS A 168     9186   8743  10001   -284  -1466   1607       C\\nATOM    960  C   CYS A 168       7.347  21.747  -8.942  1.00 77.62           C\\nANISOU  960  C   CYS A 168     9848   9341  10301   -524  -1540   1966       C\\nATOM    961  O   CYS A 168       6.638  22.045  -9.918  1.00 81.68           O\\nANISOU  961  O   CYS A 168    10442   9849  10744   -540  -1760   2098       O\\nATOM    962  CB  CYS A 168       6.478  22.640  -6.754  1.00 74.94           C\\nANISOU  962  CB  CYS A 168     9371   8593  10510   -158  -1727   1556       C\\nATOM    963  SG  CYS A 168       5.411  23.906  -7.472  1.00 83.98           S\\nANISOU  963  SG  CYS A 168    10608   9450  11852    -51  -2231   1669       S\\nATOM    964  N   PRO A 169       8.683  21.755  -9.044  1.00 78.38           N\\nANISOU  964  N   PRO A 169     9970   9541  10269   -727  -1380   2136       N\\nATOM    965  CA  PRO A 169       9.296  22.005 -10.360  1.00 83.73           C\\nANISOU  965  CA  PRO A 169    10752  10394  10669   -996  -1410   2471       C\\nATOM    966  C   PRO A 169       8.894  21.001 -11.428  1.00 84.95           C\\nANISOU  966  C   PRO A 169    10900  10878  10501  -1015  -1280   2429       C\\nATOM    967  O   PRO A 169       8.857  21.362 -12.611  1.00 84.19           O\\nANISOU  967  O   PRO A 169    10915  10894  10178  -1189  -1413   2692       O\\nATOM    968  CB  PRO A 169      10.799  21.935 -10.063  1.00 82.55           C\\nANISOU  968  CB  PRO A 169    10540  10383  10443  -1178  -1179   2547       C\\nATOM    969  CG  PRO A 169      10.912  22.332  -8.645  1.00 76.42           C\\nANISOU  969  CG  PRO A 169     9712   9325   9998  -1032  -1220   2380       C\\nATOM    970  CD  PRO A 169       9.698  21.762  -7.973  1.00 74.69           C\\nANISOU  970  CD  PRO A 169     9435   9030   9916   -740  -1219   2057       C\\nATOM    971  N   LEU A 170       8.584  19.755 -11.051  1.00 79.08           N\\nANISOU  971  N   LEU A 170    10044  10281   9723   -856  -1047   2113       N\\nATOM    972  CA  LEU A 170       8.270  18.731 -12.044  1.00 73.43           C\\nANISOU  972  CA  LEU A 170     9322   9863   8714   -871   -932   2033       C\\nATOM    973  C   LEU A 170       7.035  19.090 -12.860  1.00 76.56           C\\nANISOU  973  C   LEU A 170     9801  10208   9081   -835  -1215   2109       C\\nATOM    974  O   LEU A 170       6.917  18.677 -14.020  1.00 77.86           O\\nANISOU  974  O   LEU A 170    10015  10626   8942   -927  -1211   2171       O\\nATOM    975  CB  LEU A 170       8.080  17.380 -11.356  1.00 67.28           C\\nANISOU  975  CB  LEU A 170     8435   9155   7972   -710   -697   1684       C\\nATOM    976  CG  LEU A 170       9.176  16.975 -10.366  1.00 66.79           C\\nANISOU  976  CG  LEU A 170     8297   9091   7988   -692   -470   1577       C\\nATOM    977  CD1 LEU A 170       8.737  15.773  -9.563  1.00 66.74           C\\nANISOU  977  CD1 LEU A 170     8235   9057   8068   -536   -332   1276       C\\nATOM    978  CD2 LEU A 170      10.488  16.689 -11.074  1.00 61.58           C\\nANISOU  978  CD2 LEU A 170     7607   8724   7065   -840   -287   1659       C\\nATOM    979  N   LEU A 171       6.108  19.856 -12.280  1.00 72.91           N\\nANISOU  979  N   LEU A 171     9340   9439   8925   -685  -1477   2076       N\\nATOM    980  CA  LEU A 171       4.945  20.322 -13.024  1.00 75.80           C\\nANISOU  980  CA  LEU A 171     9768   9727   9306   -622  -1806   2146       C\\nATOM    981  C   LEU A 171       5.311  21.339 -14.094  1.00 79.71           C\\nANISOU  981  C   LEU A 171    10460  10190   9637   -830  -2066   2561       C\\nATOM    982  O   LEU A 171       4.541  21.531 -15.041  1.00 84.88           O\\nANISOU  982  O   LEU A 171    11203  10874  10173   -833  -2320   2673       O\\nATOM    983  CB  LEU A 171       3.917  20.942 -12.075  1.00 74.05           C\\nANISOU  983  CB  LEU A 171     9460   9199   9478   -376  -2034   1961       C\\nATOM    984  CG  LEU A 171       2.918  20.015 -11.385  1.00 69.74           C\\nANISOU  984  CG  LEU A 171     8717   8733   9050   -185  -1900   1574       C\\nATOM    985  CD1 LEU A 171       2.056  20.807 -10.416  1.00 68.86           C\\nANISOU  985  CD1 LEU A 171     8486   8373   9305     44  -2112   1385       C\\nATOM    986  CD2 LEU A 171       2.059  19.311 -12.420  1.00 65.45           C\\nANISOU  986  CD2 LEU A 171     8160   8395   8313   -188  -1959   1520       C\\nATOM    987  N   PHE A 172       6.460  21.995 -13.967  1.00 68.04           N\\nANISOU  987  N   PHE A 172     9054   8656   8140  -1028  -2027   2807       N\\nATOM    988  CA  PHE A 172       6.795  23.074 -14.882  1.00 78.77           C\\nANISOU  988  CA  PHE A 172    10620   9942   9366  -1280  -2310   3252       C\\nATOM    989  C   PHE A 172       8.096  22.777 -15.619  1.00 85.91           C\\nANISOU  989  C   PHE A 172    11542  11237   9862  -1615  -2028   3473       C\\nATOM    990  O   PHE A 172       9.011  23.607 -15.641  1.00 88.20           O\\nANISOU  990  O   PHE A 172    11911  11460  10141  -1873  -2078   3779       O\\nATOM    991  CB  PHE A 172       6.876  24.399 -14.118  1.00 84.73           C\\nANISOU  991  CB  PHE A 172    11461  10224  10509  -1254  -2621   3391       C\\nATOM    992  CG  PHE A 172       5.617  24.738 -13.360  1.00 85.93           C\\nANISOU  992  CG  PHE A 172    11551  10035  11063   -893  -2895   3113       C\\nATOM    993  CD1 PHE A 172       4.602  25.461 -13.964  1.00 86.94           C\\nANISOU  993  CD1 PHE A 172    11803   9937  11293   -793  -3356   3232       C\\nATOM    994  CD2 PHE A 172       5.447  24.323 -12.046  1.00 83.56           C\\nANISOU  994  CD2 PHE A 172    11054   9673  11022   -654  -2699   2721       C\\nATOM    995  CE1 PHE A 172       3.443  25.769 -13.275  1.00 83.30           C\\nANISOU  995  CE1 PHE A 172    11232   9212  11208   -436  -3605   2923       C\\nATOM    996  CE2 PHE A 172       4.288  24.629 -11.350  1.00 82.96           C\\nANISOU  996  CE2 PHE A 172    10876   9366  11280   -334  -2919   2431       C\\nATOM    997  CZ  PHE A 172       3.286  25.353 -11.967  1.00 83.10           C\\nANISOU  997  CZ  PHE A 172    10978   9179  11417   -212  -3367   2511       C\\nATOM    998  N   GLY A 173       8.179  21.592 -16.224  1.00 92.00           N\\nANISOU  998  N   GLY A 173    12224  12431  10302  -1618  -1741   3296       N\\nATOM    999  CA  GLY A 173       9.333  21.223 -17.023  1.00 99.29           C\\nANISOU  999  CA  GLY A 173    13120  13810  10797  -1900  -1463   3431       C\\nATOM   1000  C   GLY A 173      10.629  21.114 -16.255  1.00105.40           C\\nANISOU 1000  C   GLY A 173    13746  14661  11642  -1983  -1167   3370       C\\nATOM   1001  O   GLY A 173      11.703  21.225 -16.853  1.00109.34           O\\nANISOU 1001  O   GLY A 173    14209  15498  11836  -2275   -998   3563       O\\nATOM   1002  N   LEU A 174      10.558  20.899 -14.940  1.00100.46           N\\nANISOU 1002  N   LEU A 174    13015  13761  11393  -1742  -1102   3100       N\\nATOM   1003  CA  LEU A 174      11.734  20.873 -14.068  1.00103.35           C\\nANISOU 1003  CA  LEU A 174    13246  14141  11880  -1788   -879   3034       C\\nATOM   1004  C   LEU A 174      12.539  22.163 -14.183  1.00110.64           C\\nANISOU 1004  C   LEU A 174    14250  14960  12828  -2107  -1028   3434       C\\nATOM   1005  O   LEU A 174      13.746  22.179 -13.930  1.00113.38           O\\nANISOU 1005  O   LEU A 174    14470  15481  13128  -2273   -823   3467       O\\nATOM   1006  CB  LEU A 174      12.615  19.654 -14.361  1.00 97.67           C\\nANISOU 1006  CB  LEU A 174    12350  13885  10875  -1796   -492   2806       C\\nATOM   1007  CG  LEU A 174      13.534  19.118 -13.264  1.00 92.37           C\\nANISOU 1007  CG  LEU A 174    11502  13215  10381  -1682   -254   2560       C\\nATOM   1008  CD1 LEU A 174      12.928  19.339 -11.890  1.00 88.80           C\\nANISOU 1008  CD1 LEU A 174    11078  12307  10354  -1450   -387   2419       C\\nATOM   1009  CD2 LEU A 174      13.792  17.638 -13.505  1.00 90.06           C\\nANISOU 1009  CD2 LEU A 174    11076  13252   9891  -1525     22   2210       C\\nATOM   1010  N   ASN A 175      11.863  23.254 -14.556  1.00127.08           N\\nANISOU 1010  N   ASN A 175    16542  16739  15004  -2196  -1417   3738       N\\nATOM   1011  CA  ASN A 175      12.511  24.539 -14.814  1.00131.09           C\\nANISOU 1011  CA  ASN A 175    17185  17092  15530  -2547  -1637   4178       C\\nATOM   1012  C   ASN A 175      13.737  24.358 -15.706  1.00135.52           C\\nANISOU 1012  C   ASN A 175    17627  18169  15696  -2875  -1339   4267       C\\nATOM   1013  O   ASN A 175      14.777  24.991 -15.516  1.00141.49           O\\nANISOU 1013  O   ASN A 175    18317  18930  16514  -3096  -1295   4368       O\\nATOM   1014  CB  ASN A 175      12.876  25.244 -13.504  1.00127.19           C\\nANISOU 1014  CB  ASN A 175    16665  16177  15484  -2475  -1748   4122       C\\nATOM   1015  CG  ASN A 175      11.656  25.790 -12.774  1.00121.37           C\\nANISOU 1015  CG  ASN A 175    16035  14913  15169  -2144  -2109   3974       C\\nATOM   1016  OD1 ASN A 175      10.689  26.228 -13.400  1.00120.30           O\\nANISOU 1016  OD1 ASN A 175    16064  14605  15041  -2092  -2430   4105       O\\nATOM   1017  ND2 ASN A 175      11.697  25.764 -11.445  1.00115.08           N\\nANISOU 1017  ND2 ASN A 175    15127  13886  14713  -1906  -2061   3672       N\\nATOM   1018  N   ASN A 176      13.611  23.469 -16.686  1.00138.51           N\\nANISOU 1018  N   ASN A 176    17960  19005  15662  -2893  -1141   4194       N\\nATOM   1019  CA  ASN A 176      14.702  23.139 -17.593  1.00128.90           C\\nANISOU 1019  CA  ASN A 176    16590  18346  14041  -3148   -837   4194       C\\nATOM   1020  C   ASN A 176      14.143  23.135 -19.012  1.00130.29           C\\nANISOU 1020  C   ASN A 176    16893  18756  13854  -3256   -934   4312       C\\nATOM   1021  O   ASN A 176      13.054  23.656 -19.280  1.00128.25           O\\nANISOU 1021  O   ASN A 176    16856  18174  13701  -3186  -1280   4456       O\\nATOM   1022  CB  ASN A 176      15.347  21.804 -17.188  1.00114.40           C\\nANISOU 1022  CB  ASN A 176    14490  16909  12066  -3004   -416   3849       C\\nATOM   1023  N   ALA A 177      14.888  22.541 -19.940  1.00131.35           N\\nANISOU 1023  N   ALA A 177    16876  19466  13564  -3410   -639   4223       N\\nATOM   1024  CA  ALA A 177      14.518  22.512 -21.354  1.00133.06           C\\nANISOU 1024  CA  ALA A 177    17193  19978  13388  -3547   -695   4324       C\\nATOM   1025  C   ALA A 177      13.850  21.175 -21.665  1.00139.43           C\\nANISOU 1025  C   ALA A 177    17953  21060  13966  -3279   -543   3999       C\\nATOM   1026  O   ALA A 177      14.499  20.218 -22.087  1.00134.42           O\\nANISOU 1026  O   ALA A 177    17113  20932  13028  -3260   -210   3722       O\\nATOM   1027  CB  ALA A 177      15.744  22.740 -22.230  1.00132.82           C\\nANISOU 1027  CB  ALA A 177    17018  20431  13018  -3895   -487   4415       C\\nATOM   1028  N   ASP A 178      12.535  21.113 -21.456  1.00139.56           N\\nANISOU 1028  N   ASP A 178    18147  20737  14141  -3057   -814   4002       N\\nATOM   1029  CA  ASP A 178      11.738  19.985 -21.927  1.00140.00           C\\nANISOU 1029  CA  ASP A 178    18203  21034  13957  -2843   -761   3735       C\\nATOM   1030  C   ASP A 178      10.328  20.465 -22.235  1.00139.46           C\\nANISOU 1030  C   ASP A 178    18375  20618  13994  -2746  -1185   3897       C\\nATOM   1031  O   ASP A 178       9.372  20.082 -21.554  1.00142.64           O\\nANISOU 1031  O   ASP A 178    18808  20766  14622  -2479  -1336   3761       O\\nATOM   1032  CB  ASP A 178      11.711  18.857 -20.894  1.00137.06           C\\nANISOU 1032  CB  ASP A 178    17675  20675  13728  -2556   -547   3368       C\\nATOM   1033  N   GLN A 179      10.191  21.295 -23.270  1.00143.02           N\\nANISOU 1033  N   GLN A 179    18983  21074  14284  -2960  -1392   4178       N\\nATOM   1034  CA  GLN A 179       8.987  22.105 -23.424  1.00133.33           C\\nANISOU 1034  CA  GLN A 179    17987  19403  13269  -2879  -1859   4383       C\\nATOM   1035  C   GLN A 179       7.753  21.243 -23.675  1.00128.51           C\\nANISOU 1035  C   GLN A 179    17406  18844  12578  -2605  -1987   4153       C\\nATOM   1036  O   GLN A 179       6.787  21.279 -22.902  1.00124.40           O\\nANISOU 1036  O   GLN A 179    16911  17946  12410  -2345  -2237   4071       O\\nATOM   1037  CB  GLN A 179       9.188  23.117 -24.553  1.00132.56           C\\nANISOU 1037  CB  GLN A 179    18056  19342  12970  -3191  -2041   4737       C\\nATOM   1038  N   ASN A 180       7.766  20.455 -24.749  1.00126.77           N\\nANISOU 1038  N   ASN A 180    17160  19104  11903  -2656  -1831   4014       N\\nATOM   1039  CA  ASN A 180       6.565  19.780 -25.230  1.00115.92           C\\nANISOU 1039  CA  ASN A 180    15839  17790  10414  -2448  -2017   3825       C\\nATOM   1040  C   ASN A 180       6.535  18.292 -24.886  1.00111.57           C\\nANISOU 1040  C   ASN A 180    15109  17542   9741  -2253  -1745   3379       C\\nATOM   1041  O   ASN A 180       5.949  17.498 -25.625  1.00103.18           O\\nANISOU 1041  O   ASN A 180    14050  16740   8415  -2166  -1771   3154       O\\nATOM   1042  CB  ASN A 180       6.419  19.972 -26.739  1.00115.56           C\\nANISOU 1042  CB  ASN A 180    15926  18028   9952  -2620  -2110   3964       C\\nATOM   1043  N   GLU A 181       7.135  17.896 -23.764  1.00104.62           N\\nANISOU 1043  N   GLU A 181    14065  16578   9107  -2156  -1490   3195       N\\nATOM   1044  CA  GLU A 181       7.136  16.494 -23.369  1.00106.80           C\\nANISOU 1044  CA  GLU A 181    14149  16965   9465  -1902  -1204   2656       C\\nATOM   1045  C   GLU A 181       6.948  16.366 -21.867  1.00100.72           C\\nANISOU 1045  C   GLU A 181    13266  15721   9281  -1661  -1157   2456       C\\nATOM   1046  O   GLU A 181       7.211  17.295 -21.099  1.00102.83           O\\nANISOU 1046  O   GLU A 181    13557  15677   9838  -1708  -1233   2688       O\\nATOM   1047  CB  GLU A 181       8.426  15.780 -23.782  1.00111.20           C\\nANISOU 1047  CB  GLU A 181    14562  18052   9639  -2014   -799   2478       C\\nATOM   1048  CG  GLU A 181       8.455  15.363 -25.237  1.00118.18           C\\nANISOU 1048  CG  GLU A 181    15491  19499   9912  -2150   -768   2439       C\\nATOM   1049  CD  GLU A 181       9.558  14.373 -25.529  1.00125.80           C\\nANISOU 1049  CD  GLU A 181    16244  20936  10620  -2119   -359   2054       C\\nATOM   1050  OE1 GLU A 181       9.649  13.356 -24.809  1.00127.00           O\\nANISOU 1050  OE1 GLU A 181    16258  20997  10999  -1858   -200   1630       O\\nATOM   1051  OE2 GLU A 181      10.339  14.618 -26.473  1.00132.18           O\\nANISOU 1051  OE2 GLU A 181    16999  22090  11133  -2311   -210   2123       O\\nATOM   1052  N   CYS A 182       6.490  15.185 -21.461  1.00 85.77           N\\nANISOU 1052  N   CYS A 182    11262  13784   7544  -1421  -1042   2020       N\\nATOM   1053  CA  CYS A 182       6.326  14.886 -20.051  1.00 85.01           C\\nANISOU 1053  CA  CYS A 182    11057  13309   7934  -1219   -963   1809       C\\nATOM   1054  C   CYS A 182       7.659  15.034 -19.325  1.00 85.25           C\\nANISOU 1054  C   CYS A 182    10998  13354   8038  -1280   -699   1848       C\\nATOM   1055  O   CYS A 182       8.737  14.991 -19.927  1.00 87.66           O\\nANISOU 1055  O   CYS A 182    11266  14030   8011  -1441   -506   1910       O\\nATOM   1056  CB  CYS A 182       5.770  13.473 -19.864  1.00 85.07           C\\nANISOU 1056  CB  CYS A 182    10980  13320   8021  -1022   -869   1364       C\\nATOM   1057  SG  CYS A 182       5.430  13.056 -18.147  1.00 88.55           S\\nANISOU 1057  SG  CYS A 182    11313  13325   9006   -826   -793   1143       S\\nATOM   1058  N   ILE A 183       7.575  15.222 -18.009  1.00 86.69           N\\nANISOU 1058  N   ILE A 183    11127  13162   8650  -1153   -694   1796       N\\nATOM   1059  CA  ILE A 183       8.782  15.505 -17.243  1.00 88.06           C\\nANISOU 1059  CA  ILE A 183    11221  13307   8931  -1209   -498   1856       C\\nATOM   1060  C   ILE A 183       9.631  14.253 -17.070  1.00 90.76           C\\nANISOU 1060  C   ILE A 183    11430  13873   9183  -1113   -193   1518       C\\nATOM   1061  O   ILE A 183      10.856  14.349 -16.944  1.00 89.70           O\\nANISOU 1061  O   ILE A 183    11199  13916   8966  -1199     -1   1550       O\\nATOM   1062  CB  ILE A 183       8.428  16.141 -15.888  1.00 82.65           C\\nANISOU 1062  CB  ILE A 183    10529  12169   8706  -1098   -610   1893       C\\nATOM   1063  CG1 ILE A 183       9.689  16.703 -15.236  1.00 81.90           C\\nANISOU 1063  CG1 ILE A 183    10377  12044   8696  -1203   -475   2026       C\\nATOM   1064  CG2 ILE A 183       7.755  15.134 -14.972  1.00 80.02           C\\nANISOU 1064  CG2 ILE A 183    10121  11657   8626   -869   -543   1542       C\\nATOM   1065  CD1 ILE A 183      10.562  17.486 -16.201  1.00 77.13           C\\nANISOU 1065  CD1 ILE A 183     9815  11711   7778  -1501   -472   2363       C\\nATOM   1066  N   ILE A 184       9.020  13.066 -17.078  1.00 86.05           N\\nANISOU 1066  N   ILE A 184    10817  13266   8612   -938   -167   1182       N\\nATOM   1067  CA  ILE A 184       9.808  11.848 -16.945  1.00 81.50           C\\nANISOU 1067  CA  ILE A 184    10141  12849   7978   -818     61    843       C\\nATOM   1068  C   ILE A 184      10.649  11.603 -18.187  1.00 77.44           C\\nANISOU 1068  C   ILE A 184     9566  12848   7010   -918    205    786       C\\nATOM   1069  O   ILE A 184      11.589  10.802 -18.148  1.00 77.18           O\\nANISOU 1069  O   ILE A 184     9408  13014   6904   -822    403    514       O\\nATOM   1070  CB  ILE A 184       8.907  10.636 -16.645  1.00 80.64           C\\nANISOU 1070  CB  ILE A 184    10060  12549   8030   -635      7    515       C\\nATOM   1071  CG1 ILE A 184       9.694   9.574 -15.876  1.00 78.25           C\\nANISOU 1071  CG1 ILE A 184     9688  12171   7873   -478    168    222       C\\nATOM   1072  CG2 ILE A 184       8.346  10.052 -17.932  1.00 83.92           C\\nANISOU 1072  CG2 ILE A 184    10523  13226   8137   -643    -67    367       C\\nATOM   1073  CD1 ILE A 184       8.861   8.383 -15.456  1.00 80.33           C\\nANISOU 1073  CD1 ILE A 184    10011  12185   8326   -346     90    -54       C\\nATOM   1074  N   ALA A 185      10.335  12.279 -19.291  1.00 80.23           N\\nANISOU 1074  N   ALA A 185     9999  13442   7044  -1105     98   1028       N\\nATOM   1075  CA  ALA A 185      11.162  12.234 -20.487  1.00 83.51           C\\nANISOU 1075  CA  ALA A 185    10349  14420   6960  -1262    251   1031       C\\nATOM   1076  C   ALA A 185      12.352  13.177 -20.411  1.00 83.75           C\\nANISOU 1076  C   ALA A 185    10288  14647   6887  -1499    393   1327       C\\nATOM   1077  O   ALA A 185      13.207  13.143 -21.301  1.00 89.61           O\\nANISOU 1077  O   ALA A 185    10921  15924   7202  -1661    576   1320       O\\nATOM   1078  CB  ALA A 185      10.320  12.565 -21.723  1.00 73.89           C\\nANISOU 1078  CB  ALA A 185     9279  13403   5395  -1401     57   1201       C\\nATOM   1079  N   ASN A 186      12.425  14.011 -19.384  1.00 87.95           N\\nANISOU 1079  N   ASN A 186    10846  14788   7782  -1536    315   1567       N\\nATOM   1080  CA  ASN A 186      13.545  14.931 -19.235  1.00 90.37           C\\nANISOU 1080  CA  ASN A 186    11066  15232   8039  -1784    421   1852       C\\nATOM   1081  C   ASN A 186      14.781  14.156 -18.795  1.00 93.04           C\\nANISOU 1081  C   ASN A 186    11153  15806   8392  -1671    718   1526       C\\nATOM   1082  O   ASN A 186      14.734  13.472 -17.765  1.00 90.82           O\\nANISOU 1082  O   ASN A 186    10830  15214   8462  -1399    737   1252       O\\nATOM   1083  CB  ASN A 186      13.200  16.017 -18.220  1.00 86.22           C\\nANISOU 1083  CB  ASN A 186    10651  14175   7934  -1820    209   2150       C\\nATOM   1084  CG  ASN A 186      14.162  17.185 -18.259  1.00 89.29           C\\nANISOU 1084  CG  ASN A 186    11013  14659   8255  -2152    225   2537       C\\nATOM   1085  OD1 ASN A 186      15.380  17.008 -18.241  1.00 95.97           O\\nANISOU 1085  OD1 ASN A 186    11655  15837   8971  -2255    479   2464       O\\nATOM   1086  ND2 ASN A 186      13.616  18.393 -18.314  1.00 87.60           N\\nANISOU 1086  ND2 ASN A 186    10997  14142   8145  -2325    -71   2943       N\\nATOM   1087  N   PRO A 187      15.895  14.232 -19.527  1.00 95.07           N\\nANISOU 1087  N   PRO A 187    11229  16621   8273  -1873    941   1541       N\\nATOM   1088  CA  PRO A 187      17.095  13.486 -19.110  1.00 94.27           C\\nANISOU 1088  CA  PRO A 187    10845  16765   8209  -1726   1203   1183       C\\nATOM   1089  C   PRO A 187      17.587  13.857 -17.721  1.00 93.98           C\\nANISOU 1089  C   PRO A 187    10749  16330   8627  -1662   1185   1242       C\\nATOM   1090  O   PRO A 187      18.317  13.067 -17.109  1.00 94.56           O\\nANISOU 1090  O   PRO A 187    10638  16436   8855  -1433   1319    896       O\\nATOM   1091  CB  PRO A 187      18.127  13.845 -20.190  1.00 87.30           C\\nANISOU 1091  CB  PRO A 187     9769  16534   6867  -2026   1406   1271       C\\nATOM   1092  CG  PRO A 187      17.630  15.128 -20.784  1.00 81.91           C\\nANISOU 1092  CG  PRO A 187     9311  15710   6102  -2368   1189   1793       C\\nATOM   1093  CD  PRO A 187      16.135  15.035 -20.737  1.00 89.48           C\\nANISOU 1093  CD  PRO A 187    10552  16349   7098  -2256    952   1890       C\\nATOM   1094  N   ALA A 188      17.198  15.020 -17.198  1.00 89.90           N\\nANISOU 1094  N   ALA A 188    10393  15427   8337  -1837    994   1648       N\\nATOM   1095  CA  ALA A 188      17.621  15.462 -15.877  1.00 87.20           C\\nANISOU 1095  CA  ALA A 188    10012  14708   8411  -1788    952   1704       C\\nATOM   1096  C   ALA A 188      16.681  15.017 -14.764  1.00 83.84           C\\nANISOU 1096  C   ALA A 188     9732  13727   8396  -1473    795   1536       C\\nATOM   1097  O   ALA A 188      16.983  15.253 -13.591  1.00 75.80           O\\nANISOU 1097  O   ALA A 188     8687  12406   7707  -1395    761   1530       O\\nATOM   1098  CB  ALA A 188      17.750  16.987 -15.848  1.00 80.85           C\\nANISOU 1098  CB  ALA A 188     9302  13764   7654  -2142    804   2201       C\\nATOM   1099  N   PHE A 189      15.554  14.386 -15.094  1.00 80.92           N\\nANISOU 1099  N   PHE A 189     9504  13244   7997  -1314    698   1400       N\\nATOM   1100  CA  PHE A 189      14.640  13.936 -14.051  1.00 78.27           C\\nANISOU 1100  CA  PHE A 189     9281  12440   8018  -1065    570   1248       C\\nATOM   1101  C   PHE A 189      15.276  12.851 -13.193  1.00 80.35           C\\nANISOU 1101  C   PHE A 189     9430  12648   8450   -824    697    901       C\\nATOM   1102  O   PHE A 189      15.128  12.856 -11.964  1.00 75.11           O\\nANISOU 1102  O   PHE A 189     8806  11626   8105   -710    633    876       O\\nATOM   1103  CB  PHE A 189      13.335  13.437 -14.671  1.00 80.58           C\\nANISOU 1103  CB  PHE A 189     9715  12675   8225   -983    445   1165       C\\nATOM   1104  CG  PHE A 189      12.426  12.754 -13.693  1.00 85.91           C\\nANISOU 1104  CG  PHE A 189    10465  12965   9214   -760    358    965       C\\nATOM   1105  CD1 PHE A 189      11.690  13.490 -12.780  1.00 86.83           C\\nANISOU 1105  CD1 PHE A 189    10658  12708   9625   -749    203   1115       C\\nATOM   1106  CD2 PHE A 189      12.306  11.375 -13.683  1.00 84.50           C\\nANISOU 1106  CD2 PHE A 189    10274  12804   9028   -575    421    619       C\\nATOM   1107  CE1 PHE A 189      10.853  12.861 -11.873  1.00 82.22           C\\nANISOU 1107  CE1 PHE A 189    10115  11841   9283   -588    152    936       C\\nATOM   1108  CE2 PHE A 189      11.471  10.742 -12.779  1.00 79.97           C\\nANISOU 1108  CE2 PHE A 189     9777  11887   8720   -435    339    479       C\\nATOM   1109  CZ  PHE A 189      10.745  11.486 -11.874  1.00 75.49           C\\nANISOU 1109  CZ  PHE A 189     9262  11015   8404   -457    224    645       C\\nATOM   1110  N   VAL A 190      15.990  11.913 -13.820  1.00 82.64           N\\nANISOU 1110  N   VAL A 190     9581  13296   8524   -736    857    620       N\\nATOM   1111  CA  VAL A 190      16.608  10.825 -13.066  1.00 79.80           C\\nANISOU 1111  CA  VAL A 190     9129  12855   8338   -476    921    274       C\\nATOM   1112  C   VAL A 190      17.619  11.375 -12.070  1.00 73.96           C\\nANISOU 1112  C   VAL A 190     8263  12038   7801   -501    965    362       C\\nATOM   1113  O   VAL A 190      17.647  10.963 -10.905  1.00 69.81           O\\nANISOU 1113  O   VAL A 190     7780  11184   7561   -328    899    257       O\\nATOM   1114  CB  VAL A 190      17.246   9.799 -14.024  1.00 76.29           C\\nANISOU 1114  CB  VAL A 190     8531  12834   7621   -350   1058    -85       C\\nATOM   1115  CG1 VAL A 190      18.329   8.997 -13.321  1.00 73.98           C\\nANISOU 1115  CG1 VAL A 190     8071  12543   7496   -111   1121   -401       C\\nATOM   1116  CG2 VAL A 190      16.181   8.863 -14.570  1.00 70.22           C\\nANISOU 1116  CG2 VAL A 190     7922  11973   6787   -219    957   -292       C\\nATOM   1117  N   VAL A 191      18.449  12.327 -12.502  1.00 74.89           N\\nANISOU 1117  N   VAL A 191     8232  12459   7764   -745   1062    574       N\\nATOM   1118  CA  VAL A 191      19.440  12.910 -11.603  1.00 69.99           C\\nANISOU 1118  CA  VAL A 191     7472  11783   7337   -800   1089    659       C\\nATOM   1119  C   VAL A 191      18.756  13.666 -10.472  1.00 71.73           C\\nANISOU 1119  C   VAL A 191     7882  11494   7879   -818    904    880       C\\nATOM   1120  O   VAL A 191      19.167  13.580  -9.308  1.00 74.22           O\\nANISOU 1120  O   VAL A 191     8168  11584   8449   -696    866    802       O\\nATOM   1121  CB  VAL A 191      20.401  13.820 -12.387  1.00 69.86           C\\nANISOU 1121  CB  VAL A 191     7256  12216   7071  -1128   1224    873       C\\nATOM   1122  CG1 VAL A 191      21.588  14.210 -11.518  1.00 61.69           C\\nANISOU 1122  CG1 VAL A 191     6014  11194   6229  -1167   1269    875       C\\nATOM   1123  CG2 VAL A 191      20.860  13.135 -13.669  1.00 71.25           C\\nANISOU 1123  CG2 VAL A 191     7250  12975   6848  -1136   1419    651       C\\nATOM   1124  N   TYR A 192      17.698  14.409 -10.792  1.00 73.30           N\\nANISOU 1124  N   TYR A 192     8269  11519   8064   -952    769   1133       N\\nATOM   1125  CA  TYR A 192      17.008  15.209  -9.786  1.00 69.49           C\\nANISOU 1125  CA  TYR A 192     7937  10591   7877   -952    585   1300       C\\nATOM   1126  C   TYR A 192      16.386  14.323  -8.714  1.00 69.05           C\\nANISOU 1126  C   TYR A 192     7966  10230   8040   -683    540   1063       C\\nATOM   1127  O   TYR A 192      16.743  14.407  -7.534  1.00 70.50           O\\nANISOU 1127  O   TYR A 192     8135  10210   8443   -602    510   1018       O\\nATOM   1128  CB  TYR A 192      15.946  16.079 -10.460  1.00 70.53           C\\nANISOU 1128  CB  TYR A 192     8235  10616   7948  -1102    419   1566       C\\nATOM   1129  CG  TYR A 192      15.223  17.022  -9.524  1.00 71.79           C\\nANISOU 1129  CG  TYR A 192     8522  10343   8412  -1083    204   1704       C\\nATOM   1130  CD1 TYR A 192      15.814  18.212  -9.114  1.00 72.52           C\\nANISOU 1130  CD1 TYR A 192     8604  10305   8647  -1251    105   1926       C\\nATOM   1131  CD2 TYR A 192      13.943  16.733  -9.066  1.00 75.40           C\\nANISOU 1131  CD2 TYR A 192     9093  10543   9014   -904     92   1589       C\\nATOM   1132  CE1 TYR A 192      15.157  19.082  -8.265  1.00 72.60           C\\nANISOU 1132  CE1 TYR A 192     8724   9917   8942  -1200   -114   1996       C\\nATOM   1133  CE2 TYR A 192      13.275  17.600  -8.217  1.00 78.40           C\\nANISOU 1133  CE2 TYR A 192     9549  10580   9658   -860    -96   1656       C\\nATOM   1134  CZ  TYR A 192      13.887  18.772  -7.820  1.00 72.16           C\\nANISOU 1134  CZ  TYR A 192     8758   9648   9013   -988   -206   1843       C\\nATOM   1135  OH  TYR A 192      13.226  19.632  -6.973  1.00 63.34           O\\nANISOU 1135  OH  TYR A 192     7711   8188   8168   -909   -415   1853       O\\nATOM   1136  N   SER A 193      15.457  13.449  -9.114  1.00 72.61           N\\nANISOU 1136  N   SER A 193     8511  10659   8417   -566    526    916       N\\nATOM   1137  CA  SER A 193      14.715  12.654  -8.139  1.00 77.34           C\\nANISOU 1137  CA  SER A 193     9213  10968   9205   -382    469    746       C\\nATOM   1138  C   SER A 193      15.615  11.681  -7.386  1.00 75.22           C\\nANISOU 1138  C   SER A 193     8884  10678   9019   -217    535    524       C\\nATOM   1139  O   SER A 193      15.294  11.286  -6.260  1.00 76.80           O\\nANISOU 1139  O   SER A 193     9170  10614   9397   -116    473    460       O\\nATOM   1140  CB  SER A 193      13.580  11.897  -8.830  1.00 79.11           C\\nANISOU 1140  CB  SER A 193     9536  11195   9327   -336    430    640       C\\nATOM   1141  OG  SER A 193      14.075  10.934  -9.741  1.00 69.99           O\\nANISOU 1141  OG  SER A 193     8324  10300   7968   -274    524    442       O\\nATOM   1142  N   SER A 194      16.739  11.283  -7.980  1.00 71.25           N\\nANISOU 1142  N   SER A 194     8226  10467   8381   -186    646    398       N\\nATOM   1143  CA  SER A 194      17.664  10.407  -7.271  1.00 72.26           C\\nANISOU 1143  CA  SER A 194     8279  10561   8614      6    663    171       C\\nATOM   1144  C   SER A 194      18.401  11.166  -6.177  1.00 76.18           C\\nANISOU 1144  C   SER A 194     8709  10947   9290    -29    635    286       C\\nATOM   1145  O   SER A 194      18.423  10.741  -5.014  1.00 72.02           O\\nANISOU 1145  O   SER A 194     8263  10164   8939     99    550    218       O\\nATOM   1146  CB  SER A 194      18.661   9.784  -8.246  1.00 72.31           C\\nANISOU 1146  CB  SER A 194     8087  10955   8432     84    784    -57       C\\nATOM   1147  OG  SER A 194      17.998   9.092  -9.286  1.00 80.43           O\\nANISOU 1147  OG  SER A 194     9180  12101   9277    122    797   -194       O\\nATOM   1148  N   ILE A 195      19.005  12.300  -6.530  1.00 77.08           N\\nANISOU 1148  N   ILE A 195     8687  11249   9349   -226    688    474       N\\nATOM   1149  CA  ILE A 195      19.847  13.021  -5.580  1.00 70.51           C\\nANISOU 1149  CA  ILE A 195     7763  10342   8685   -272    652    555       C\\nATOM   1150  C   ILE A 195      18.988  13.748  -4.552  1.00 66.52           C\\nANISOU 1150  C   ILE A 195     7438   9466   8370   -304    511    708       C\\nATOM   1151  O   ILE A 195      19.129  13.541  -3.341  1.00 74.63           O\\nANISOU 1151  O   ILE A 195     8511  10286   9557   -186    438    633       O\\nATOM   1152  CB  ILE A 195      20.787  13.987  -6.321  1.00 68.49           C\\nANISOU 1152  CB  ILE A 195     7299  10412   8313   -520    744    715       C\\nATOM   1153  CG1 ILE A 195      21.784  13.200  -7.177  1.00 66.22           C\\nANISOU 1153  CG1 ILE A 195     6764  10568   7828   -459    911    488       C\\nATOM   1154  CG2 ILE A 195      21.510  14.892  -5.337  1.00 63.89           C\\nANISOU 1154  CG2 ILE A 195     6643   9700   7932   -613    668    829       C\\nATOM   1155  CD1 ILE A 195      22.738  14.064  -7.971  1.00 56.97           C\\nANISOU 1155  CD1 ILE A 195     5348   9813   6484   -752   1041    642       C\\nATOM   1156  N   VAL A 196      18.073  14.597  -5.019  1.00 62.66           N\\nANISOU 1156  N   VAL A 196     7052   8902   7854   -450    454    905       N\\nATOM   1157  CA  VAL A 196      17.332  15.463  -4.105  1.00 67.97           C\\nANISOU 1157  CA  VAL A 196     7847   9264   8715   -469    309   1012       C\\nATOM   1158  C   VAL A 196      16.343  14.656  -3.269  1.00 67.07           C\\nANISOU 1158  C   VAL A 196     7868   8944   8670   -296    275    861       C\\nATOM   1159  O   VAL A 196      16.268  14.814  -2.046  1.00 61.49           O\\nANISOU 1159  O   VAL A 196     7206   8054   8102   -231    210    818       O\\nATOM   1160  CB  VAL A 196      16.626  16.582  -4.888  1.00 64.23           C\\nANISOU 1160  CB  VAL A 196     7440   8750   8216   -643    212   1244       C\\nATOM   1161  CG1 VAL A 196      15.849  17.474  -3.945  1.00 52.97           C\\nANISOU 1161  CG1 VAL A 196     6116   7001   7009   -610     37   1287       C\\nATOM   1162  CG2 VAL A 196      17.638  17.392  -5.674  1.00 71.96           C\\nANISOU 1162  CG2 VAL A 196     8304   9935   9102   -883    238   1445       C\\nATOM   1163  N   SER A 197      15.571  13.778  -3.911  1.00 68.31           N\\nANISOU 1163  N   SER A 197     8091   9151   8712   -244    315    780       N\\nATOM   1164  CA  SER A 197      14.505  13.073  -3.211  1.00 64.29           C\\nANISOU 1164  CA  SER A 197     7706   8466   8256   -150    280    676       C\\nATOM   1165  C   SER A 197      14.986  11.839  -2.460  1.00 64.86           C\\nANISOU 1165  C   SER A 197     7819   8478   8346    -22    301    516       C\\nATOM   1166  O   SER A 197      14.304  11.401  -1.528  1.00 71.84           O\\nANISOU 1166  O   SER A 197     8812   9202   9284      7    262    476       O\\nATOM   1167  CB  SER A 197      13.401  12.668  -4.191  1.00 64.34           C\\nANISOU 1167  CB  SER A 197     7768   8525   8155   -175    281    661       C\\nATOM   1168  OG  SER A 197      12.416  13.677  -4.297  1.00 65.40           O\\nANISOU 1168  OG  SER A 197     7921   8583   8345   -241    188    775       O\\nATOM   1169  N   PHE A 198      16.134  11.265  -2.824  1.00 56.65           N\\nANISOU 1169  N   PHE A 198     6693   7571   7259     50    348    422       N\\nATOM   1170  CA  PHE A 198      16.563  10.006  -2.225  1.00 61.84           C\\nANISOU 1170  CA  PHE A 198     7413   8131   7953    205    308    258       C\\nATOM   1171  C   PHE A 198      17.951  10.080  -1.597  1.00 66.94           C\\nANISOU 1171  C   PHE A 198     7945   8814   8677    293    283    207       C\\nATOM   1172  O   PHE A 198      18.076   9.853  -0.391  1.00 63.30           O\\nANISOU 1172  O   PHE A 198     7574   8170   8306    352    191    202       O\\nATOM   1173  CB  PHE A 198      16.518   8.887  -3.269  1.00 62.27           C\\nANISOU 1173  CB  PHE A 198     7477   8279   7904    290    331     91       C\\nATOM   1174  CG  PHE A 198      16.836   7.525  -2.714  1.00 71.87           C\\nANISOU 1174  CG  PHE A 198     8800   9318   9188    461    226    -82       C\\nATOM   1175  CD1 PHE A 198      15.889   6.822  -1.986  1.00 73.26           C\\nANISOU 1175  CD1 PHE A 198     9194   9229   9414    432    130    -54       C\\nATOM   1176  CD2 PHE A 198      18.074   6.944  -2.927  1.00 66.14           C\\nANISOU 1176  CD2 PHE A 198     7955   8695   8481    641    204   -273       C\\nATOM   1177  CE1 PHE A 198      16.173   5.566  -1.481  1.00 70.07           C\\nANISOU 1177  CE1 PHE A 198     8932   8611   9079    560    -15   -171       C\\nATOM   1178  CE2 PHE A 198      18.365   5.687  -2.423  1.00 70.55           C\\nANISOU 1178  CE2 PHE A 198     8637   9036   9134    826     45   -436       C\\nATOM   1179  CZ  PHE A 198      17.412   4.997  -1.700  1.00 69.64           C\\nANISOU 1179  CZ  PHE A 198     8787   8602   9070    775    -79   -363       C\\nATOM   1180  N   TYR A 199      18.996  10.380  -2.373  1.00 67.17           N\\nANISOU 1180  N   TYR A 199     7766   9103   8654    290    360    166       N\\nATOM   1181  CA  TYR A 199      20.356  10.230  -1.861  1.00 67.05           C\\nANISOU 1181  CA  TYR A 199     7598   9159   8719    402    329     58       C\\nATOM   1182  C   TYR A 199      20.656  11.224  -0.746  1.00 67.17           C\\nANISOU 1182  C   TYR A 199     7604   9058   8859    323    261    193       C\\nATOM   1183  O   TYR A 199      21.379  10.897   0.202  1.00 60.26           O\\nANISOU 1183  O   TYR A 199     6716   8098   8082    445    161    112       O\\nATOM   1184  CB  TYR A 199      21.367  10.375  -2.997  1.00 71.88           C\\nANISOU 1184  CB  TYR A 199     7935  10155   9221    380    457    -32       C\\nATOM   1185  CG  TYR A 199      21.372   9.197  -3.942  1.00 81.30           C\\nANISOU 1185  CG  TYR A 199     9102  11489  10299    540    498   -275       C\\nATOM   1186  CD1 TYR A 199      21.185   7.907  -3.469  1.00 86.13           C\\nANISOU 1186  CD1 TYR A 199     9871  11856  10998    769    359   -463       C\\nATOM   1187  CD2 TYR A 199      21.545   9.374  -5.307  1.00 83.10           C\\nANISOU 1187  CD2 TYR A 199     9165  12088  10320    449    652   -315       C\\nATOM   1188  CE1 TYR A 199      21.177   6.825  -4.325  1.00 85.63           C\\nANISOU 1188  CE1 TYR A 199     9799  11878  10859    933    355   -719       C\\nATOM   1189  CE2 TYR A 199      21.538   8.297  -6.171  1.00 80.51           C\\nANISOU 1189  CE2 TYR A 199     8809  11905   9875    615    680   -585       C\\nATOM   1190  CZ  TYR A 199      21.352   7.026  -5.674  1.00 76.43           C\\nANISOU 1190  CZ  TYR A 199     8448  11104   9487    871    522   -803       C\\nATOM   1191  OH  TYR A 199      21.344   5.950  -6.531  1.00 69.70           O\\nANISOU 1191  OH  TYR A 199     7579  10355   8547   1053    510  -1106       O\\nATOM   1192  N   VAL A 200      20.116  12.435  -0.831  1.00 65.74           N\\nANISOU 1192  N   VAL A 200     7439   8856   8685    133    281    383       N\\nATOM   1193  CA  VAL A 200      20.375  13.434   0.206  1.00 71.58           C\\nANISOU 1193  CA  VAL A 200     8173   9468   9555     66    193    476       C\\nATOM   1194  C   VAL A 200      19.616  13.076   1.483  1.00 70.25           C\\nANISOU 1194  C   VAL A 200     8210   9046   9435    156     95    445       C\\nATOM   1195  O   VAL A 200      20.203  13.156   2.571  1.00 66.48           O\\nANISOU 1195  O   VAL A 200     7736   8490   9035    213      0    407       O\\nATOM   1196  CB  VAL A 200      20.038  14.854  -0.281  1.00 71.46           C\\nANISOU 1196  CB  VAL A 200     8129   9461   9562   -148    192    671       C\\nATOM   1197  CG1 VAL A 200      20.109  15.848   0.873  1.00 70.31           C\\nANISOU 1197  CG1 VAL A 200     8017   9123   9575   -187     60    720       C\\nATOM   1198  CG2 VAL A 200      20.992  15.264  -1.393  1.00 67.72           C\\nANISOU 1198  CG2 VAL A 200     7444   9277   9011   -300    285    742       C\\nATOM   1199  N   PRO A 201      18.333  12.691   1.432  1.00 68.63           N\\nANISOU 1199  N   PRO A 201     8167   8739   9171    150    111    459       N\\nATOM   1200  CA  PRO A 201      17.717  12.147   2.655  1.00 67.01           C\\nANISOU 1200  CA  PRO A 201     8135   8363   8962    204     43    424       C\\nATOM   1201  C   PRO A 201      18.416  10.898   3.166  1.00 63.12           C\\nANISOU 1201  C   PRO A 201     7712   7811   8461    342    -32    331       C\\nATOM   1202  O   PRO A 201      18.541  10.711   4.383  1.00 64.72           O\\nANISOU 1202  O   PRO A 201     8019   7903   8669    376   -131    332       O\\nATOM   1203  CB  PRO A 201      16.275  11.860   2.217  1.00 66.92           C\\nANISOU 1203  CB  PRO A 201     8227   8319   8879    142     97    446       C\\nATOM   1204  CG  PRO A 201      16.022  12.833   1.137  1.00 66.63           C\\nANISOU 1204  CG  PRO A 201     8086   8379   8852     55    144    523       C\\nATOM   1205  CD  PRO A 201      17.319  12.916   0.383  1.00 66.70           C\\nANISOU 1205  CD  PRO A 201     7946   8542   8857     61    178    525       C\\nATOM   1206  N   PHE A 202      18.884  10.041   2.258  1.00 56.10           N\\nANISOU 1206  N   PHE A 202     6771   6992   7551    435    -11    238       N\\nATOM   1207  CA  PHE A 202      19.593   8.829   2.655  1.00 63.87           C\\nANISOU 1207  CA  PHE A 202     7821   7882   8566    610   -137    119       C\\nATOM   1208  C   PHE A 202      20.816   9.156   3.509  1.00 70.36           C\\nANISOU 1208  C   PHE A 202     8539   8718   9475    697   -242     86       C\\nATOM   1209  O   PHE A 202      20.977   8.621   4.613  1.00 72.54           O\\nANISOU 1209  O   PHE A 202     8969   8826   9768    771   -400     91       O\\nATOM   1210  CB  PHE A 202      19.992   8.047   1.402  1.00 62.85           C\\nANISOU 1210  CB  PHE A 202     7591   7872   8416    726    -97    -41       C\\nATOM   1211  CG  PHE A 202      20.499   6.659   1.671  1.00 70.17           C\\nANISOU 1211  CG  PHE A 202     8620   8639   9403    941   -273   -200       C\\nATOM   1212  CD1 PHE A 202      20.468   6.114   2.942  1.00 73.47           C\\nANISOU 1212  CD1 PHE A 202     9254   8795   9864    982   -462   -139       C\\nATOM   1213  CD2 PHE A 202      21.014   5.899   0.638  1.00 76.10           C\\nANISOU 1213  CD2 PHE A 202     9257   9501  10156   1108   -271   -423       C\\nATOM   1214  CE1 PHE A 202      20.939   4.847   3.177  1.00 78.88           C\\nANISOU 1214  CE1 PHE A 202    10067   9279  10625   1182   -682   -264       C\\nATOM   1215  CE2 PHE A 202      21.485   4.628   0.866  1.00 75.62           C\\nANISOU 1215  CE2 PHE A 202     9296   9248  10187   1343   -483   -603       C\\nATOM   1216  CZ  PHE A 202      21.447   4.100   2.137  1.00 79.28           C\\nANISOU 1216  CZ  PHE A 202    10003   9395  10724   1380   -707   -507       C\\nATOM   1217  N   ILE A 203      21.692  10.031   3.011  1.00 69.89           N\\nANISOU 1217  N   ILE A 203     8223   8871   9462    667   -169     66       N\\nATOM   1218  CA  ILE A 203      22.931  10.333   3.726  1.00 70.07           C\\nANISOU 1218  CA  ILE A 203     8101   8940   9583    743   -275      9       C\\nATOM   1219  C   ILE A 203      22.628  10.977   5.074  1.00 68.51           C\\nANISOU 1219  C   ILE A 203     8043   8585   9403    671   -375    114       C\\nATOM   1220  O   ILE A 203      23.185  10.584   6.106  1.00 61.96           O\\nANISOU 1220  O   ILE A 203     7279   7659   8605    783   -545     72       O\\nATOM   1221  CB  ILE A 203      23.843  11.227   2.870  1.00 67.00           C\\nANISOU 1221  CB  ILE A 203     7390   8840   9226    648   -158     -7       C\\nATOM   1222  CG1 ILE A 203      24.189  10.534   1.555  1.00 68.52           C\\nANISOU 1222  CG1 ILE A 203     7420   9264   9349    728    -43   -152       C\\nATOM   1223  CG2 ILE A 203      25.111  11.566   3.623  1.00 62.39           C\\nANISOU 1223  CG2 ILE A 203     6625   8319   8761    704   -276    -75       C\\nATOM   1224  CD1 ILE A 203      24.882  11.438   0.566  1.00 75.16           C\\nANISOU 1224  CD1 ILE A 203     7956  10453  10148    555    118   -121       C\\nATOM   1225  N   VAL A 204      21.738  11.974   5.082  1.00 68.09           N\\nANISOU 1225  N   VAL A 204     8035   8512   9324    499   -292    232       N\\nATOM   1226  CA  VAL A 204      21.439  12.706   6.313  1.00 64.98           C\\nANISOU 1226  CA  VAL A 204     7739   8013   8938    443   -378    276       C\\nATOM   1227  C   VAL A 204      20.881  11.767   7.375  1.00 65.55           C\\nANISOU 1227  C   VAL A 204     8061   7945   8902    504   -469    277       C\\nATOM   1228  O   VAL A 204      21.332  11.764   8.527  1.00 66.60           O\\nANISOU 1228  O   VAL A 204     8259   8027   9017    550   -610    260       O\\nATOM   1229  CB  VAL A 204      20.471  13.865   6.027  1.00 56.49           C\\nANISOU 1229  CB  VAL A 204     6664   6928   7872    291   -296    354       C\\nATOM   1230  CG1 VAL A 204      19.900  14.399   7.325  1.00 59.98           C\\nANISOU 1230  CG1 VAL A 204     7227   7276   8289    274   -375    333       C\\nATOM   1231  CG2 VAL A 204      21.185  14.972   5.267  1.00 55.27           C\\nANISOU 1231  CG2 VAL A 204     6299   6869   7831    182   -275    403       C\\nATOM   1232  N   THR A 205      19.886  10.960   7.005  1.00 66.29           N\\nANISOU 1232  N   THR A 205     8302   7982   8903    478   -403    312       N\\nATOM   1233  CA  THR A 205      19.340   9.991   7.947  1.00 66.07           C\\nANISOU 1233  CA  THR A 205     8524   7824   8753    475   -492    356       C\\nATOM   1234  C   THR A 205      20.407   9.003   8.395  1.00 73.22           C\\nANISOU 1234  C   THR A 205     9501   8627   9694    637   -693    319       C\\nATOM   1235  O   THR A 205      20.450   8.611   9.567  1.00 73.97           O\\nANISOU 1235  O   THR A 205     9780   8626   9698    635   -843    376       O\\nATOM   1236  CB  THR A 205      18.162   9.258   7.313  1.00 64.13           C\\nANISOU 1236  CB  THR A 205     8398   7536   8434    391   -397    399       C\\nATOM   1237  OG1 THR A 205      17.159  10.210   6.937  1.00 70.05           O\\nANISOU 1237  OG1 THR A 205     9065   8385   9167    268   -244    415       O\\nATOM   1238  CG2 THR A 205      17.567   8.265   8.291  1.00 59.18           C\\nANISOU 1238  CG2 THR A 205     8038   6780   7668    317   -492    485       C\\nATOM   1239  N   LEU A 206      21.282   8.594   7.476  1.00 71.22           N\\nANISOU 1239  N   LEU A 206     9095   8407   9557    784   -714    211       N\\nATOM   1240  CA  LEU A 206      22.343   7.663   7.839  1.00 69.37           C\\nANISOU 1240  CA  LEU A 206     8891   8070   9395    992   -940    126       C\\nATOM   1241  C   LEU A 206      23.325   8.302   8.810  1.00 67.69           C\\nANISOU 1241  C   LEU A 206     8584   7907   9228   1046  -1074    104       C\\nATOM   1242  O   LEU A 206      23.847   7.629   9.705  1.00 63.83           O\\nANISOU 1242  O   LEU A 206     8237   7281   8736   1166  -1318    106       O\\nATOM   1243  CB  LEU A 206      23.069   7.177   6.586  1.00 68.74           C\\nANISOU 1243  CB  LEU A 206     8603   8086   9429   1162   -911    -54       C\\nATOM   1244  CG  LEU A 206      24.254   6.253   6.864  1.00 66.60           C\\nANISOU 1244  CG  LEU A 206     8300   7728   9276   1438  -1170   -212       C\\nATOM   1245  CD1 LEU A 206      23.779   4.999   7.577  1.00 68.61           C\\nANISOU 1245  CD1 LEU A 206     8929   7645   9495   1492  -1416   -131       C\\nATOM   1246  CD2 LEU A 206      24.981   5.908   5.578  1.00 65.91           C\\nANISOU 1246  CD2 LEU A 206     7933   7826   9284   1614  -1102   -453       C\\nATOM   1247  N   LEU A 207      23.592   9.597   8.647  1.00 71.05           N\\nANISOU 1247  N   LEU A 207     8784   8507   9703    951   -950     91       N\\nATOM   1248  CA  LEU A 207      24.489  10.279   9.572  1.00 68.27           C\\nANISOU 1248  CA  LEU A 207     8336   8199   9405    979  -1088     58       C\\nATOM   1249  C   LEU A 207      23.856  10.418  10.949  1.00 68.21           C\\nANISOU 1249  C   LEU A 207     8586   8088   9244    897  -1186    154       C\\nATOM   1250  O   LEU A 207      24.552  10.352  11.967  1.00 66.32           O\\nANISOU 1250  O   LEU A 207     8392   7815   8989    976  -1395    132       O\\nATOM   1251  CB  LEU A 207      24.875  11.645   9.012  1.00 63.44           C\\nANISOU 1251  CB  LEU A 207     7441   7765   8897    855   -953     35       C\\nATOM   1252  CG  LEU A 207      25.757  11.605   7.765  1.00 58.28           C\\nANISOU 1252  CG  LEU A 207     6481   7306   8356    900   -859    -62       C\\nATOM   1253  CD1 LEU A 207      25.869  12.987   7.135  1.00 58.28           C\\nANISOU 1253  CD1 LEU A 207     6266   7458   8418    685   -713     -2       C\\nATOM   1254  CD2 LEU A 207      27.133  11.057   8.115  1.00 60.06           C\\nANISOU 1254  CD2 LEU A 207     6537   7593   8688   1106  -1049   -219       C\\nATOM   1255  N   VAL A 208      22.536  10.604  11.000  1.00 65.76           N\\nANISOU 1255  N   VAL A 208     8427   7760   8800    740  -1039    244       N\\nATOM   1256  CA  VAL A 208      21.850  10.728  12.283  1.00 70.01           C\\nANISOU 1256  CA  VAL A 208     9179   8279   9143    643  -1090    309       C\\nATOM   1257  C   VAL A 208      21.897   9.408  13.042  1.00 72.90           C\\nANISOU 1257  C   VAL A 208     9821   8505   9370    686  -1284    405       C\\nATOM   1258  O   VAL A 208      22.211   9.371  14.237  1.00 72.29           O\\nANISOU 1258  O   VAL A 208     9878   8422   9167    690  -1459    437       O\\nATOM   1259  CB  VAL A 208      20.403  11.205  12.072  1.00 62.31           C\\nANISOU 1259  CB  VAL A 208     8243   7366   8066    475   -875    344       C\\nATOM   1260  CG1 VAL A 208      19.616  11.100  13.361  1.00 57.35           C\\nANISOU 1260  CG1 VAL A 208     7821   6784   7185    363   -898    391       C\\nATOM   1261  CG2 VAL A 208      20.388  12.634  11.560  1.00 55.34           C\\nANISOU 1261  CG2 VAL A 208     7134   6567   7324    438   -769    263       C\\nATOM   1262  N   TYR A 209      21.584   8.304  12.360  1.00 67.17           N\\nANISOU 1262  N   TYR A 209     9206   7651   8663    711  -1285    458       N\\nATOM   1263  CA  TYR A 209      21.578   7.010  13.032  1.00 62.85           C\\nANISOU 1263  CA  TYR A 209     8966   6907   8008    728  -1515    581       C\\nATOM   1264  C   TYR A 209      22.975   6.598  13.468  1.00 67.38           C\\nANISOU 1264  C   TYR A 209     9528   7379   8695    962  -1822    518       C\\nATOM   1265  O   TYR A 209      23.130   5.942  14.504  1.00 76.08           O\\nANISOU 1265  O   TYR A 209    10894   8346   9666    963  -2077    640       O\\nATOM   1266  CB  TYR A 209      20.960   5.946  12.126  1.00 60.49           C\\nANISOU 1266  CB  TYR A 209     8784   6452   7749    710  -1483    623       C\\nATOM   1267  CG  TYR A 209      19.452   5.927  12.179  1.00 66.56           C\\nANISOU 1267  CG  TYR A 209     9685   7270   8334    437  -1286    750       C\\nATOM   1268  CD1 TYR A 209      18.788   5.544  13.335  1.00 66.30           C\\nANISOU 1268  CD1 TYR A 209     9921   7223   8047    229  -1351    931       C\\nATOM   1269  CD2 TYR A 209      18.693   6.292  11.078  1.00 67.85           C\\nANISOU 1269  CD2 TYR A 209     9692   7530   8559    372  -1040    687       C\\nATOM   1270  CE1 TYR A 209      17.408   5.526  13.397  1.00 71.51           C\\nANISOU 1270  CE1 TYR A 209    10651   7990   8531    -39  -1153   1024       C\\nATOM   1271  CE2 TYR A 209      17.312   6.271  11.129  1.00 67.87           C\\nANISOU 1271  CE2 TYR A 209     9776   7601   8410    135   -874    776       C\\nATOM   1272  CZ  TYR A 209      16.675   5.892  12.292  1.00 73.98           C\\nANISOU 1272  CZ  TYR A 209    10778   8387   8944    -71   -920    933       C\\nATOM   1273  OH  TYR A 209      15.301   5.875  12.350  1.00 78.65           O\\nANISOU 1273  OH  TYR A 209    11400   9107   9378   -325   -736    998       O\\nATOM   1274  N   ILE A 210      24.002   6.972  12.702  1.00 65.59           N\\nANISOU 1274  N   ILE A 210     8989   7235   8698   1151  -1815    332       N\\nATOM   1275  CA  ILE A 210      25.373   6.731  13.144  1.00 66.53           C\\nANISOU 1275  CA  ILE A 210     9020   7316   8943   1384  -2102    228       C\\nATOM   1276  C   ILE A 210      25.669   7.536  14.402  1.00 68.90           C\\nANISOU 1276  C   ILE A 210     9347   7706   9128   1318  -2205    265       C\\nATOM   1277  O   ILE A 210      26.296   7.036  15.343  1.00 66.82           O\\nANISOU 1277  O   ILE A 210     9234   7337   8820   1429  -2518    299       O\\nATOM   1278  CB  ILE A 210      26.368   7.053  12.015  1.00 68.77           C\\nANISOU 1278  CB  ILE A 210     8898   7760   9473   1556  -2020      2       C\\nATOM   1279  CG1 ILE A 210      26.237   6.043  10.879  1.00 66.91           C\\nANISOU 1279  CG1 ILE A 210     8656   7435   9331   1685  -1991    -87       C\\nATOM   1280  CG2 ILE A 210      27.792   7.062  12.545  1.00 69.56           C\\nANISOU 1280  CG2 ILE A 210     8822   7898   9711   1774  -2291   -139       C\\nATOM   1281  CD1 ILE A 210      27.237   6.254   9.771  1.00 66.26           C\\nANISOU 1281  CD1 ILE A 210     8158   7579   9440   1852  -1900   -335       C\\nATOM   1282  N   LYS A 211      25.221   8.797  14.439  1.00 68.09           N\\nANISOU 1282  N   LYS A 211     9108   7786   8977   1147  -1974    247       N\\nATOM   1283  CA  LYS A 211      25.368   9.607  15.645  1.00 72.77           C\\nANISOU 1283  CA  LYS A 211     9739   8468   9442   1077  -2066    245       C\\nATOM   1284  C   LYS A 211      24.551   9.044  16.798  1.00 75.75           C\\nANISOU 1284  C   LYS A 211    10492   8790   9501    949  -2158    418       C\\nATOM   1285  O   LYS A 211      24.918   9.225  17.965  1.00 75.16           O\\nANISOU 1285  O   LYS A 211    10526   8758   9275    949  -2353    430       O\\nATOM   1286  CB  LYS A 211      24.956  11.053  15.367  1.00 72.52           C\\nANISOU 1286  CB  LYS A 211     9503   8598   9455    934  -1825    165       C\\nATOM   1287  CG  LYS A 211      26.059  11.921  14.784  1.00 76.74           C\\nANISOU 1287  CG  LYS A 211     9682   9223  10251    997  -1830     21       C\\nATOM   1288  CD  LYS A 211      27.081  12.304  15.845  1.00 80.50           C\\nANISOU 1288  CD  LYS A 211    10106   9734  10746   1072  -2092    -66       C\\nATOM   1289  N   ILE A 212      23.444   8.363  16.492  1.00 76.82           N\\nANISOU 1289  N   ILE A 212    10821   8858   9510    813  -2022    555       N\\nATOM   1290  CA  ILE A 212      22.634   7.738  17.534  1.00 75.49           C\\nANISOU 1290  CA  ILE A 212    11004   8670   9009    629  -2092    753       C\\nATOM   1291  C   ILE A 212      23.351   6.523  18.110  1.00 78.85           C\\nANISOU 1291  C   ILE A 212    11697   8862   9401    741  -2475    889       C\\nATOM   1292  O   ILE A 212      23.426   6.348  19.332  1.00 81.23           O\\nANISOU 1292  O   ILE A 212    12234   9186   9445    664  -2673   1015       O\\nATOM   1293  CB  ILE A 212      21.244   7.368  16.983  1.00 72.94           C\\nANISOU 1293  CB  ILE A 212    10775   8353   8584    420  -1838    858       C\\nATOM   1294  CG1 ILE A 212      20.367   8.618  16.858  1.00 72.24           C\\nANISOU 1294  CG1 ILE A 212    10488   8519   8442    291  -1522    738       C\\nATOM   1295  CG2 ILE A 212      20.575   6.319  17.861  1.00 71.22           C\\nANISOU 1295  CG2 ILE A 212    10941   8062   8058    211  -1961   1112       C\\nATOM   1296  CD1 ILE A 212      18.962   8.339  16.351  1.00 65.08           C\\nANISOU 1296  CD1 ILE A 212     9627   7664   7437     90  -1276    811       C\\nATOM   1297  N   TYR A 213      23.890   5.666  17.237  1.00 80.40           N\\nANISOU 1297  N   TYR A 213    11866   8833   9849    936  -2607    855       N\\nATOM   1298  CA  TYR A 213      24.609   4.484  17.706  1.00 74.91           C\\nANISOU 1298  CA  TYR A 213    11423   7857   9182   1095  -3032    956       C\\nATOM   1299  C   TYR A 213      25.796   4.871  18.580  1.00 76.60           C\\nANISOU 1299  C   TYR A 213    11566   8127   9414   1272  -3314    873       C\\nATOM   1300  O   TYR A 213      26.091   4.197  19.574  1.00 75.58           O\\nANISOU 1300  O   TYR A 213    11741   7846   9129   1288  -3670   1037       O\\nATOM   1301  CB  TYR A 213      25.070   3.642  16.515  1.00 69.47           C\\nANISOU 1301  CB  TYR A 213    10637   6949   8811   1339  -3122    828       C\\nATOM   1302  CG  TYR A 213      25.850   2.401  16.899  1.00 82.87           C\\nANISOU 1302  CG  TYR A 213    12578   8305  10605   1567  -3612    881       C\\nATOM   1303  CD1 TYR A 213      25.198   1.248  17.317  1.00 88.00           C\\nANISOU 1303  CD1 TYR A 213    13681   8643  11110   1422  -3838   1153       C\\nATOM   1304  CD2 TYR A 213      27.237   2.376  16.828  1.00 83.04           C\\nANISOU 1304  CD2 TYR A 213    12370   8305  10877   1924  -3876    656       C\\nATOM   1305  CE1 TYR A 213      25.906   0.107  17.664  1.00 88.45           C\\nANISOU 1305  CE1 TYR A 213    13945   8382  11281   1597  -4262   1171       C\\nATOM   1306  CE2 TYR A 213      27.955   1.241  17.174  1.00 84.14           C\\nANISOU 1306  CE2 TYR A 213    12701   8139  11130   2144  -4318    655       C\\nATOM   1307  CZ  TYR A 213      27.286   0.109  17.589  1.00 88.74           C\\nANISOU 1307  CZ  TYR A 213    13713   8432  11572   1950  -4461    892       C\\nATOM   1308  OH  TYR A 213      27.998  -1.023  17.933  1.00 93.97           O\\nANISOU 1308  OH  TYR A 213    14524   8828  12351   2091  -4813    843       O\\nATOM   1309  N   ILE A 214      26.491   5.955  18.226  1.00 79.22           N\\nANISOU 1309  N   ILE A 214    11503   8668   9929   1388  -3184    634       N\\nATOM   1310  CA  ILE A 214      27.667   6.368  18.988  1.00 79.71           C\\nANISOU 1310  CA  ILE A 214    11448   8796  10043   1553  -3456    525       C\\nATOM   1311  C   ILE A 214      27.278   6.769  20.407  1.00 82.99           C\\nANISOU 1311  C   ILE A 214    12112   9325  10094   1359  -3536    663       C\\nATOM   1312  O   ILE A 214      27.993   6.468  21.373  1.00 77.18           O\\nANISOU 1312  O   ILE A 214    11526   8534   9267   1459  -3903    709       O\\nATOM   1313  CB  ILE A 214      28.405   7.505  18.256  1.00 74.49           C\\nANISOU 1313  CB  ILE A 214    10301   8350   9651   1642  -3272    259       C\\nATOM   1314  CG1 ILE A 214      28.993   6.995  16.944  1.00 73.37           C\\nANISOU 1314  CG1 ILE A 214     9897   8156   9825   1855  -3239    102       C\\nATOM   1315  CG2 ILE A 214      29.508   8.085  19.125  1.00 79.54           C\\nANISOU 1315  CG2 ILE A 214    10802   9091  10328   1753  -3532    141       C\\nATOM   1316  CD1 ILE A 214      29.840   8.022  16.221  1.00 79.87           C\\nANISOU 1316  CD1 ILE A 214    10233   9224  10891   1906  -3079   -130       C\\nATOM   1317  N   VAL A 215      26.138   7.447  20.558  1.00 80.48           N\\nANISOU 1317  N   VAL A 215    11834   9193   9553   1092  -3207    710       N\\nATOM   1318  CA  VAL A 215      25.693   7.866  21.883  1.00 80.01           C\\nANISOU 1318  CA  VAL A 215    11978   9313   9108    905  -3241    790       C\\nATOM   1319  C   VAL A 215      25.303   6.658  22.722  1.00 86.31           C\\nANISOU 1319  C   VAL A 215    13235   9978   9582    774  -3480   1098       C\\nATOM   1320  O   VAL A 215      25.668   6.557  23.900  1.00 89.76           O\\nANISOU 1320  O   VAL A 215    13882  10466   9758    750  -3755   1189       O\\nATOM   1321  CB  VAL A 215      24.532   8.868  21.764  1.00 69.82           C\\nANISOU 1321  CB  VAL A 215    10575   8272   7681    685  -2829    710       C\\nATOM   1322  CG1 VAL A 215      23.873   9.073  23.115  1.00 70.46           C\\nANISOU 1322  CG1 VAL A 215    10891   8582   7299    474  -2833    787       C\\nATOM   1323  CG2 VAL A 215      25.035  10.188  21.201  1.00 70.96           C\\nANISOU 1323  CG2 VAL A 215    10323   8520   8117    791  -2692    435       C\\nATOM   1324  N   LEU A 216      24.556   5.722  22.131  1.00 88.27           N\\nANISOU 1324  N   LEU A 216    13660  10047   9830    664  -3400   1278       N\\nATOM   1325  CA  LEU A 216      24.129   4.539  22.870  1.00 81.42           C\\nANISOU 1325  CA  LEU A 216    13257   9014   8666    480  -3641   1616       C\\nATOM   1326  C   LEU A 216      25.314   3.682  23.294  1.00 84.21           C\\nANISOU 1326  C   LEU A 216    13802   9063   9129    728  -4180   1700       C\\nATOM   1327  O   LEU A 216      25.268   3.046  24.353  1.00 81.69           O\\nANISOU 1327  O   LEU A 216    13836   8687   8514    577  -4427   1947       O\\nATOM   1328  CB  LEU A 216      23.148   3.725  22.025  1.00 83.40           C\\nANISOU 1328  CB  LEU A 216    13629   9094   8967    318  -3470   1765       C\\nATOM   1329  CG  LEU A 216      21.846   4.440  21.657  1.00 89.34           C\\nANISOU 1329  CG  LEU A 216    14218  10142   9584     56  -2973   1707       C\\nATOM   1330  CD1 LEU A 216      21.017   3.625  20.676  1.00 88.79           C\\nANISOU 1330  CD1 LEU A 216    14221   9881   9633    -62  -2839   1814       C\\nATOM   1331  CD2 LEU A 216      21.046   4.736  22.911  1.00 97.88           C\\nANISOU 1331  CD2 LEU A 216    15482  11550  10159   -274  -2870   1850       C\\nATOM   1332  N   ARG A 217      26.382   3.651  22.492  1.00 81.94           N\\nANISOU 1332  N   ARG A 217    13237   8618   9279   1094  -4322   1464       N\\nATOM   1333  CA  ARG A 217      27.561   2.877  22.871  1.00 83.41           C\\nANISOU 1333  CA  ARG A 217    13486   8566   9641   1348  -4750   1435       C\\nATOM   1334  C   ARG A 217      28.345   3.556  23.985  1.00 85.61           C\\nANISOU 1334  C   ARG A 217    13711   9042   9775   1403  -4934   1364       C\\nATOM   1335  O   ARG A 217      28.952   2.873  24.816  1.00 80.30           O\\nANISOU 1335  O   ARG A 217    13221   8234   9057   1442  -5229   1443       O\\nATOM   1336  CB  ARG A 217      28.460   2.641  21.658  1.00 74.00           C\\nANISOU 1336  CB  ARG A 217    11946   7228   8942   1710  -4789   1141       C\\nATOM   1337  N   ARG A 218      28.347   4.891  24.021  1.00 77.47           N\\nANISOU 1337  N   ARG A 218    12427   8320   8687   1399  -4771   1198       N\\nATOM   1338  CA  ARG A 218      28.948   5.589  25.152  1.00 79.95           C\\nANISOU 1338  CA  ARG A 218    12725   8839   8812   1411  -4955   1127       C\\nATOM   1339  C   ARG A 218      28.170   5.328  26.435  1.00 82.04           C\\nANISOU 1339  C   ARG A 218    13403   9226   8543   1087  -4970   1402       C\\nATOM   1340  O   ARG A 218      28.765   5.243  27.517  1.00 84.60           O\\nANISOU 1340  O   ARG A 218    13838   9600   8707   1097  -5207   1432       O\\nATOM   1341  CB  ARG A 218      29.022   7.089  24.868  1.00 75.14           C\\nANISOU 1341  CB  ARG A 218    11692   8536   8320   1397  -4623    823       C\\nATOM   1342  N   ARG A 219      26.847   5.179  26.326  1.00 85.99           N\\nANISOU 1342  N   ARG A 219    14111   9803   8758    785  -4704   1599       N\\nATOM   1343  CA  ARG A 219      26.016   4.885  27.490  1.00 84.46           C\\nANISOU 1343  CA  ARG A 219    14260   9795   8035    425  -4645   1858       C\\nATOM   1344  C   ARG A 219      26.340   3.511  28.066  1.00 86.08           C\\nANISOU 1344  C   ARG A 219    14765   9710   8230    380  -4920   2118       C\\nATOM   1345  O   ARG A 219      26.501   3.361  29.283  1.00 90.06           O\\nANISOU 1345  O   ARG A 219    15467  10337   8414    256  -5076   2247       O\\nATOM   1346  CB  ARG A 219      24.539   4.978  27.102  1.00 85.75           C\\nANISOU 1346  CB  ARG A 219    14494  10127   7961    100  -4243   1970       C\\nATOM   1347  CG  ARG A 219      23.566   4.985  28.270  1.00 97.90           C\\nANISOU 1347  CG  ARG A 219    16277  12019   8900   -302  -4086   2160       C\\nATOM   1348  CD  ARG A 219      22.137   5.191  27.780  1.00103.51           C\\nANISOU 1348  CD  ARG A 219    16923  12951   9455   -597  -3619   2177       C\\nATOM   1349  NE  ARG A 219      22.015   6.380  26.940  1.00103.98           N\\nANISOU 1349  NE  ARG A 219    16513  13152   9842   -422  -3259   1780       N\\nATOM   1350  CZ  ARG A 219      21.746   7.599  27.400  1.00102.81           C\\nANISOU 1350  CZ  ARG A 219    16138  13388   9536   -439  -3032   1497       C\\nATOM   1351  NH1 ARG A 219      21.567   7.793  28.700  1.00112.25           N\\nANISOU 1351  NH1 ARG A 219    17509  14920  10223   -616  -3093   1534       N\\nATOM   1352  NH2 ARG A 219      21.656   8.624  26.563  1.00 90.07           N\\nANISOU 1352  NH2 ARG A 219    14137  11821   8266   -282  -2765   1173       N\\nATOM   1353  N   ARG A 220      26.443   2.493  27.205  1.00 85.93           N\\nANISOU 1353  N   ARG A 220    14788   9305   8558    483  -5002   2177       N\\nATOM   1354  CA  ARG A 220      26.753   1.145  27.680  1.00 92.53           C\\nANISOU 1354  CA  ARG A 220    15922   9808   9426    451  -5313   2391       C\\nATOM   1355  C   ARG A 220      28.118   1.092  28.355  1.00 98.18           C\\nANISOU 1355  C   ARG A 220    16600  10438  10265    730  -5700   2278       C\\nATOM   1356  O   ARG A 220      28.296   0.384  29.353  1.00 99.06           O\\nANISOU 1356  O   ARG A 220    17008  10452  10178    616  -5960   2492       O\\nATOM   1357  CB  ARG A 220      26.686   0.149  26.522  1.00 94.83           C\\nANISOU 1357  CB  ARG A 220    16221   9701  10109    561  -5350   2378       C\\nATOM   1358  CG  ARG A 220      25.281  -0.055  25.969  1.00100.75           C\\nANISOU 1358  CG  ARG A 220    17071  10487  10720    234  -5015   2543       C\\nATOM   1359  CD  ARG A 220      25.299  -0.715  24.596  1.00102.73           C\\nANISOU 1359  CD  ARG A 220    17220  10409  11403    417  -5011   2417       C\\nATOM   1360  NE  ARG A 220      23.971  -0.712  23.986  1.00105.76           N\\nANISOU 1360  NE  ARG A 220    17640  10872  11673    124  -4663   2533       N\\nATOM   1361  CZ  ARG A 220      23.743  -0.876  22.687  1.00111.13           C\\nANISOU 1361  CZ  ARG A 220    18166  11401  12658    249  -4533   2393       C\\nATOM   1362  NH1 ARG A 220      24.756  -1.052  21.850  1.00115.91           N\\nANISOU 1362  NH1 ARG A 220    18552  11801  13687    664  -4699   2115       N\\nATOM   1363  NH2 ARG A 220      22.500  -0.857  22.220  1.00109.07           N\\nANISOU 1363  NH2 ARG A 220    17943  11230  12267    -44  -4223   2509       N\\nATOM   1364  N   LYS A 221      29.096   1.832  27.826  1.00 87.90           N\\nANISOU 1364  N   LYS A 221    14922   9183   9293   1081  -5746   1943       N\\nATOM   1365  CA  LYS A 221      30.396   1.903  28.485  1.00 91.01           C\\nANISOU 1365  CA  LYS A 221    15227   9552   9800   1332  -6088   1803       C\\nATOM   1366  C   LYS A 221      30.311   2.643  29.815  1.00 92.81           C\\nANISOU 1366  C   LYS A 221    15563  10123   9576   1152  -6111   1881       C\\nATOM   1367  O   LYS A 221      31.080   2.348  30.738  1.00 97.14           O\\nANISOU 1367  O   LYS A 221    16229  10626  10054   1227  -6434   1922       O\\nATOM   1368  CB  LYS A 221      31.420   2.575  27.569  1.00 88.24           C\\nANISOU 1368  CB  LYS A 221    14391   9229   9907   1702  -6082   1409       C\\nATOM   1369  N   ARG A 222      29.386   3.599  29.935  1.00 89.90           N\\nANISOU 1369  N   ARG A 222    15156  10111   8890    923  -5782   1877       N\\nATOM   1370  CA  ARG A 222      29.220   4.328  31.190  1.00 91.86           C\\nANISOU 1370  CA  ARG A 222    15494  10740   8669    746  -5774   1897       C\\nATOM   1371  C   ARG A 222      28.375   3.544  32.190  1.00 96.10           C\\nANISOU 1371  C   ARG A 222    16450  11352   8712    379  -5763   2271       C\\nATOM   1372  O   ARG A 222      28.677   3.536  33.390  1.00100.34           O\\nANISOU 1372  O   ARG A 222    17145  12050   8928    306  -5948   2359       O\\nATOM   1373  CB  ARG A 222      28.596   5.698  30.923  1.00 87.62           C\\nANISOU 1373  CB  ARG A 222    14726  10572   7995    668  -5443   1670       C\\nATOM   1374  N   ASN A1002      27.322   2.874  31.712  1.00 85.72           N\\nANISOU 1374  N   ASN A1002    12716   9421  10431    154  -1889   1403       N\\nATOM   1375  CA  ASN A1002      26.456   2.104  32.601  1.00 78.54           C\\nANISOU 1375  CA  ASN A1002    11488   8720   9636    336  -1772   1042       C\\nATOM   1376  C   ASN A1002      27.206   0.951  33.259  1.00 74.17           C\\nANISOU 1376  C   ASN A1002    10829   8409   8943    253  -1283    980       C\\nATOM   1377  O   ASN A1002      26.974   0.646  34.435  1.00 77.99           O\\nANISOU 1377  O   ASN A1002    11066   9013   9552    361  -1151    748       O\\nATOM   1378  CB  ASN A1002      25.242   1.584  31.828  1.00 72.27           C\\nANISOU 1378  CB  ASN A1002    10694   8018   8747    370  -1959    956       C\\nATOM   1379  CG  ASN A1002      24.296   2.693  31.414  1.00 85.39           C\\nANISOU 1379  CG  ASN A1002    12363   9440  10641    548  -2522    954       C\\nATOM   1380  OD1 ASN A1002      24.569   3.871  31.643  1.00 91.93           O\\nANISOU 1380  OD1 ASN A1002    13249   9977  11701    641  -2774   1033       O\\nATOM   1381  ND2 ASN A1002      23.179   2.324  30.796  1.00 95.12           N\\nANISOU 1381  ND2 ASN A1002    13533  10764  11844    599  -2763    857       N\\nATOM   1382  N   ILE A1003      28.104   0.295  32.520  1.00 69.88           N\\nANISOU 1382  N   ILE A1003    10476   7942   8134     67  -1017   1180       N\\nATOM   1383  CA  ILE A1003      28.844  -0.824  33.094  1.00 75.25           C\\nANISOU 1383  CA  ILE A1003    11058   8796   8739     40   -607   1126       C\\nATOM   1384  C   ILE A1003      29.846  -0.336  34.137  1.00 79.70           C\\nANISOU 1384  C   ILE A1003    11473   9334   9474     69   -527   1154       C\\nATOM   1385  O   ILE A1003      30.117  -1.035  35.121  1.00 81.90           O\\nANISOU 1385  O   ILE A1003    11597   9734   9788    131   -334   1048       O\\nATOM   1386  CB  ILE A1003      29.526  -1.644  31.981  1.00 76.66           C\\nANISOU 1386  CB  ILE A1003    11445   9056   8624   -116   -342   1259       C\\nATOM   1387  CG1 ILE A1003      30.131  -2.927  32.553  1.00 83.23           C\\nANISOU 1387  CG1 ILE A1003    12171  10007   9446    -76     25   1164       C\\nATOM   1388  CG2 ILE A1003      30.599  -0.830  31.276  1.00 75.86           C\\nANISOU 1388  CG2 ILE A1003    11492   8897   8434   -279   -312   1524       C\\nATOM   1389  CD1 ILE A1003      30.765  -3.812  31.509  1.00 89.05           C\\nANISOU 1389  CD1 ILE A1003    13083  10813   9939   -170    311   1194       C\\nATOM   1390  N   PHE A1004      30.403   0.862  33.954  1.00 72.73           N\\nANISOU 1390  N   PHE A1004    10657   8281   8697      0   -708   1309       N\\nATOM   1391  CA  PHE A1004      31.300   1.419  34.961  1.00 72.86           C\\nANISOU 1391  CA  PHE A1004    10523   8260   8901      1   -698   1302       C\\nATOM   1392  C   PHE A1004      30.561   1.658  36.271  1.00 75.78           C\\nANISOU 1392  C   PHE A1004    10709   8641   9442    194   -837   1009       C\\nATOM   1393  O   PHE A1004      31.045   1.293  37.349  1.00 75.51           O\\nANISOU 1393  O   PHE A1004    10525   8740   9424    231   -703    911       O\\nATOM   1394  CB  PHE A1004      31.920   2.718  34.446  1.00 74.85           C\\nANISOU 1394  CB  PHE A1004    10908   8273   9256   -164   -904   1525       C\\nATOM   1395  CG  PHE A1004      32.831   3.387  35.431  1.00 80.49           C\\nANISOU 1395  CG  PHE A1004    11471   8921  10192   -205   -951   1497       C\\nATOM   1396  CD1 PHE A1004      34.093   2.876  35.685  1.00 79.31           C\\nANISOU 1396  CD1 PHE A1004    11166   8951  10018   -317   -675   1584       C\\nATOM   1397  CD2 PHE A1004      32.429   4.533  36.100  1.00 83.97           C\\nANISOU 1397  CD2 PHE A1004    11907   9110  10888   -118  -1297   1351       C\\nATOM   1398  CE1 PHE A1004      34.938   3.492  36.589  1.00 82.95           C\\nANISOU 1398  CE1 PHE A1004    11465   9368  10684   -377   -769   1550       C\\nATOM   1399  CE2 PHE A1004      33.269   5.154  37.007  1.00 85.07           C\\nANISOU 1399  CE2 PHE A1004    11928   9181  11215   -183  -1370   1289       C\\nATOM   1400  CZ  PHE A1004      34.525   4.633  37.251  1.00 84.25           C\\nANISOU 1400  CZ  PHE A1004    11666   9282  11062   -331  -1119   1402       C\\nATOM   1401  N   GLU A1005      29.376   2.270  36.194  1.00 75.34           N\\nANISOU 1401  N   GLU A1005    10654   8467   9503    325  -1114    852       N\\nATOM   1402  CA  GLU A1005      28.576   2.488  37.395  1.00 80.23           C\\nANISOU 1402  CA  GLU A1005    11062   9155  10266    516  -1188    504       C\\nATOM   1403  C   GLU A1005      28.115   1.169  38.000  1.00 86.02           C\\nANISOU 1403  C   GLU A1005    11656  10202  10825    527   -889    366       C\\nATOM   1404  O   GLU A1005      28.046   1.030  39.227  1.00 90.45           O\\nANISOU 1404  O   GLU A1005    12070  10923  11372    580   -788    167       O\\nATOM   1405  CB  GLU A1005      27.375   3.375  37.076  1.00 77.92           C\\nANISOU 1405  CB  GLU A1005    10741   8676  10189    694  -1544    334       C\\nATOM   1406  CG  GLU A1005      27.742   4.831  36.890  1.00 84.80           C\\nANISOU 1406  CG  GLU A1005    11751   9159  11311    720  -1903    409       C\\nATOM   1407  CD  GLU A1005      28.491   5.393  38.081  1.00 89.89           C\\nANISOU 1407  CD  GLU A1005    12315   9761  12076    724  -1883    248       C\\nATOM   1408  OE1 GLU A1005      27.991   5.262  39.219  1.00 89.61           O\\nANISOU 1408  OE1 GLU A1005    12069   9916  12064    880  -1796   -120       O\\nATOM   1409  OE2 GLU A1005      29.591   5.949  37.880  1.00 88.50           O\\nANISOU 1409  OE2 GLU A1005    12285   9394  11947    539  -1944    483       O\\nATOM   1410  N   MET A1006      27.798   0.187  37.153  1.00 78.13           N\\nANISOU 1410  N   MET A1006    10736   9284   9667    448   -755    474       N\\nATOM   1411  CA  MET A1006      27.337  -1.104  37.657  1.00 72.09           C\\nANISOU 1411  CA  MET A1006     9881   8748   8762    410   -494    376       C\\nATOM   1412  C   MET A1006      28.381  -1.755  38.553  1.00 75.65           C\\nANISOU 1412  C   MET A1006    10336   9295   9114    362   -262    468       C\\nATOM   1413  O   MET A1006      28.038  -2.402  39.549  1.00 76.42           O\\nANISOU 1413  O   MET A1006    10345   9565   9126    348   -119    363       O\\nATOM   1414  CB  MET A1006      26.994  -2.033  36.497  1.00 63.48           C\\nANISOU 1414  CB  MET A1006     8926   7661   7531    307   -419    476       C\\nATOM   1415  CG  MET A1006      26.279  -3.292  36.913  1.00 70.23           C\\nANISOU 1415  CG  MET A1006     9703   8684   8298    231   -215    360       C\\nATOM   1416  SD  MET A1006      26.609  -4.663  35.798  1.00 70.93           S\\nANISOU 1416  SD  MET A1006    10037   8714   8198     86    -29    502       S\\nATOM   1417  CE  MET A1006      25.235  -5.747  36.183  1.00 79.60           C\\nANISOU 1417  CE  MET A1006    11010   9948   9288    -46     55    311       C\\nATOM   1418  N   LEU A1007      29.660  -1.591  38.223  1.00 74.32           N\\nANISOU 1418  N   LEU A1007    10257   9030   8951    321   -234    678       N\\nATOM   1419  CA  LEU A1007      30.716  -2.231  38.992  1.00 72.19           C\\nANISOU 1419  CA  LEU A1007     9955   8841   8633    310    -74    777       C\\nATOM   1420  C   LEU A1007      31.310  -1.346  40.078  1.00 77.91           C\\nANISOU 1420  C   LEU A1007    10574   9585   9442    343   -217    715       C\\nATOM   1421  O   LEU A1007      31.846  -1.881  41.054  1.00 81.18           O\\nANISOU 1421  O   LEU A1007    10944  10120   9781    352   -154    740       O\\nATOM   1422  CB  LEU A1007      31.835  -2.718  38.066  1.00 71.02           C\\nANISOU 1422  CB  LEU A1007     9882   8633   8470    261     76    992       C\\nATOM   1423  CG  LEU A1007      31.556  -4.102  37.475  1.00 67.80           C\\nANISOU 1423  CG  LEU A1007     9585   8237   7941    251    288   1010       C\\nATOM   1424  CD1 LEU A1007      30.727  -4.015  36.198  1.00 65.13           C\\nANISOU 1424  CD1 LEU A1007     9386   7844   7514    183    249    974       C\\nATOM   1425  CD2 LEU A1007      32.848  -4.848  37.236  1.00 68.79           C\\nANISOU 1425  CD2 LEU A1007     9698   8348   8090    287    481   1140       C\\nATOM   1426  N   ARG A1008      31.232  -0.018  39.954  1.00 81.15           N\\nANISOU 1426  N   ARG A1008    10972   9855  10007    355   -447    635       N\\nATOM   1427  CA  ARG A1008      31.610   0.793  41.106  1.00 79.83           C\\nANISOU 1427  CA  ARG A1008    10721   9701   9912    383   -602    485       C\\nATOM   1428  C   ARG A1008      30.583   0.693  42.224  1.00 79.95           C\\nANISOU 1428  C   ARG A1008    10660   9903   9815    473   -581    181       C\\nATOM   1429  O   ARG A1008      30.878   1.089  43.357  1.00 82.62           O\\nANISOU 1429  O   ARG A1008    10953  10337  10104    486   -655     22       O\\nATOM   1430  CB  ARG A1008      31.814   2.257  40.711  1.00 75.25           C\\nANISOU 1430  CB  ARG A1008    10178   8848   9565    361   -878    461       C\\nATOM   1431  CG  ARG A1008      30.548   3.009  40.384  1.00 84.73           C\\nANISOU 1431  CG  ARG A1008    11405   9893  10893    488  -1070    258       C\\nATOM   1432  CD  ARG A1008      30.759   4.502  40.562  1.00 91.79           C\\nANISOU 1432  CD  ARG A1008    12342  10481  12053    509  -1399    147       C\\nATOM   1433  NE  ARG A1008      30.802   4.870  41.973  1.00 97.78           N\\nANISOU 1433  NE  ARG A1008    12996  11338  12815    587  -1451   -187       N\\nATOM   1434  CZ  ARG A1008      29.731   5.209  42.684  1.00100.58           C\\nANISOU 1434  CZ  ARG A1008    13254  11756  13206    785  -1504   -595       C\\nATOM   1435  NH1 ARG A1008      28.534   5.231  42.111  1.00 94.43           N\\nANISOU 1435  NH1 ARG A1008    12420  10935  12522    941  -1541   -707       N\\nATOM   1436  NH2 ARG A1008      29.857   5.526  43.966  1.00105.64           N\\nANISOU 1436  NH2 ARG A1008    13834  12529  13777    825  -1520   -917       N\\nATOM   1437  N   ILE A1009      29.394   0.171  41.926  1.00 74.25           N\\nANISOU 1437  N   ILE A1009     9910   9267   9034    507   -473     81       N\\nATOM   1438  CA  ILE A1009      28.416  -0.151  42.956  1.00 75.30           C\\nANISOU 1438  CA  ILE A1009     9929   9661   9019    531   -350   -186       C\\nATOM   1439  C   ILE A1009      28.680  -1.535  43.536  1.00 78.79           C\\nANISOU 1439  C   ILE A1009    10438  10305   9194    403   -107     -8       C\\nATOM   1440  O   ILE A1009      28.534  -1.752  44.743  1.00 85.17           O\\nANISOU 1440  O   ILE A1009    11227  11348   9787    355    -20   -120       O\\nATOM   1441  CB  ILE A1009      26.996  -0.039  42.373  1.00 72.07           C\\nANISOU 1441  CB  ILE A1009     9394   9267   8722    603   -364   -387       C\\nATOM   1442  CG1 ILE A1009      26.670   1.415  42.030  1.00 73.75           C\\nANISOU 1442  CG1 ILE A1009     9547   9243   9230    783   -675   -591       C\\nATOM   1443  CG2 ILE A1009      25.968  -0.620  43.332  1.00 70.49           C\\nANISOU 1443  CG2 ILE A1009     9027   9408   8349    556   -136   -634       C\\nATOM   1444  CD1 ILE A1009      25.423   1.572  41.190  1.00 76.17           C\\nANISOU 1444  CD1 ILE A1009     9730   9499   9713    890   -796   -718       C\\nATOM   1445  N   ASP A1010      29.079  -2.490  42.694  1.00 72.06           N\\nANISOU 1445  N   ASP A1010     9694   9350   8336    343     -7    269       N\\nATOM   1446  CA  ASP A1010      29.286  -3.870  43.127  1.00 72.56           C\\nANISOU 1446  CA  ASP A1010     9858   9501   8210    243    179    457       C\\nATOM   1447  C   ASP A1010      30.708  -4.106  43.629  1.00 75.95           C\\nANISOU 1447  C   ASP A1010    10352   9894   8612    272    117    675       C\\nATOM   1448  O   ASP A1010      30.908  -4.550  44.763  1.00 79.91           O\\nANISOU 1448  O   ASP A1010    10905  10541   8916    226    124    730       O\\nATOM   1449  CB  ASP A1010      28.966  -4.834  41.979  1.00 68.87           C\\nANISOU 1449  CB  ASP A1010     9481   8902   7784    190    300    582       C\\nATOM   1450  CG  ASP A1010      27.482  -4.951  41.709  1.00 73.05           C\\nANISOU 1450  CG  ASP A1010     9921   9528   8308    113    358    385       C\\nATOM   1451  OD1 ASP A1010      26.693  -4.307  42.432  1.00 67.48           O\\nANISOU 1451  OD1 ASP A1010     9046   9009   7582    124    341    140       O\\nATOM   1452  OD2 ASP A1010      27.105  -5.691  40.773  1.00 78.54           O\\nANISOU 1452  OD2 ASP A1010    10691  10123   9026     43    418    440       O\\nATOM   1453  N   GLU A1011      31.702  -3.824  42.788  1.00 76.16           N\\nANISOU 1453  N   GLU A1011    10363   9749   8825    334     50    808       N\\nATOM   1454  CA  GLU A1011      33.088  -4.089  43.149  1.00 80.16           C\\nANISOU 1454  CA  GLU A1011    10842  10236   9377    379    -14    997       C\\nATOM   1455  C   GLU A1011      33.663  -2.965  44.003  1.00 86.62           C\\nANISOU 1455  C   GLU A1011    11560  11131  10222    377   -238    897       C\\nATOM   1456  O   GLU A1011      34.212  -3.213  45.081  1.00 98.58           O\\nANISOU 1456  O   GLU A1011    13076  12768  11614    380   -345    952       O\\nATOM   1457  CB  GLU A1011      33.926  -4.284  41.885  1.00 82.54           C\\nANISOU 1457  CB  GLU A1011    11111  10383   9867    418     68   1140       C\\nATOM   1458  CG  GLU A1011      35.344  -4.765  42.134  1.00 89.74           C\\nANISOU 1458  CG  GLU A1011    11913  11291  10894    502     40   1313       C\\nATOM   1459  CD  GLU A1011      35.393  -6.223  42.539  1.00 95.34           C\\nANISOU 1459  CD  GLU A1011    12731  11959  11534    586    111   1445       C\\nATOM   1460  OE1 GLU A1011      35.895  -6.518  43.646  1.00 99.56           O\\nANISOU 1460  OE1 GLU A1011    13255  12559  12013    632    -51   1549       O\\nATOM   1461  OE2 GLU A1011      34.920  -7.072  41.751  1.00 94.59           O\\nANISOU 1461  OE2 GLU A1011    12763  11742  11436    596    295   1450       O\\nATOM   1462  N   GLY A1012      33.549  -1.725  43.534  1.00 83.15           N\\nANISOU 1462  N   GLY A1012    11062  10592   9938    362   -351    758       N\\nATOM   1463  CA  GLY A1012      34.064  -0.590  44.272  1.00 80.42           C\\nANISOU 1463  CA  GLY A1012    10644  10253   9660    339   -589    621       C\\nATOM   1464  C   GLY A1012      35.145   0.176  43.536  1.00 76.41           C\\nANISOU 1464  C   GLY A1012    10041   9573   9418    270   -701    745       C\\nATOM   1465  O   GLY A1012      36.026  -0.422  42.909  1.00 75.35           O\\nANISOU 1465  O   GLY A1012     9829   9430   9369    254   -588    972       O\\nATOM   1466  N   LEU A1013      35.090   1.505  43.610  1.00 72.47           N\\nANISOU 1466  N   LEU A1013     9539   8928   9066    216   -914    581       N\\nATOM   1467  CA  LEU A1013      36.059   2.381  42.960  1.00 75.06           C\\nANISOU 1467  CA  LEU A1013     9799   9069   9653     69  -1037    711       C\\nATOM   1468  C   LEU A1013      37.076   2.842  43.998  1.00 85.43           C\\nANISOU 1468  C   LEU A1013    10980  10447  11031    -12  -1266    645       C\\nATOM   1469  O   LEU A1013      36.730   3.569  44.935  1.00 92.30           O\\nANISOU 1469  O   LEU A1013    11906  11301  11864      3  -1478    364       O\\nATOM   1470  CB  LEU A1013      35.362   3.575  42.309  1.00 76.93           C\\nANISOU 1470  CB  LEU A1013    10164   9014  10053     35  -1188    614       C\\nATOM   1471  CG  LEU A1013      36.264   4.677  41.743  1.00 81.85           C\\nANISOU 1471  CG  LEU A1013    10778   9382  10939   -188  -1361    759       C\\nATOM   1472  CD1 LEU A1013      37.119   4.145  40.607  1.00 83.65           C\\nANISOU 1472  CD1 LEU A1013    10936   9672  11176   -345  -1119   1104       C\\nATOM   1473  CD2 LEU A1013      35.444   5.879  41.290  1.00 79.42           C\\nANISOU 1473  CD2 LEU A1013    10661   8711  10803   -183  -1600    657       C\\nATOM   1474  N   ARG A1014      38.324   2.416  43.830  1.00 82.30           N\\nANISOU 1474  N   ARG A1014    10388  10143  10740    -92  -1229    865       N\\nATOM   1475  CA  ARG A1014      39.431   2.846  44.673  1.00 87.70           C\\nANISOU 1475  CA  ARG A1014    10885  10900  11537   -200  -1487    834       C\\nATOM   1476  C   ARG A1014      40.374   3.720  43.858  1.00 91.11           C\\nANISOU 1476  C   ARG A1014    11154  11170  12293   -454  -1533    970       C\\nATOM   1477  O   ARG A1014      40.854   3.301  42.800  1.00 93.58           O\\nANISOU 1477  O   ARG A1014    11348  11510  12699   -513  -1278   1201       O\\nATOM   1478  CB  ARG A1014      40.189   1.647  45.242  1.00 89.70           C\\nANISOU 1478  CB  ARG A1014    10969  11409  11702    -83  -1465    977       C\\nATOM   1479  CG  ARG A1014      39.445   0.867  46.311  1.00 95.14           C\\nANISOU 1479  CG  ARG A1014    11845  12266  12037     80  -1493    888       C\\nATOM   1480  CD  ARG A1014      40.338   0.658  47.527  1.00103.70           C\\nANISOU 1480  CD  ARG A1014    12817  13547  13039     82  -1799    903       C\\nATOM   1481  NE  ARG A1014      39.801  -0.327  48.462  1.00107.67           N\\nANISOU 1481  NE  ARG A1014    13522  14230  13160    204  -1802    939       N\\nATOM   1482  CZ  ARG A1014      40.399  -0.677  49.597  1.00111.85           C\\nANISOU 1482  CZ  ARG A1014    14048  14948  13504    219  -2094    997       C\\nATOM   1483  NH1 ARG A1014      41.553  -0.119  49.939  1.00113.46           N\\nANISOU 1483  NH1 ARG A1014    14008  15196  13905    140  -2424    984       N\\nATOM   1484  NH2 ARG A1014      39.844  -1.584  50.391  1.00112.62           N\\nANISOU 1484  NH2 ARG A1014    14392  15192  13208    282  -2078   1085       N\\nATOM   1485  N   LEU A1015      40.648   4.926  44.357  1.00 92.65           N\\nANISOU 1485  N   LEU A1015    11353  11202  12646   -633  -1845    811       N\\nATOM   1486  CA  LEU A1015      41.453   5.897  43.627  1.00 98.42           C\\nANISOU 1486  CA  LEU A1015    11974  11728  13694   -955  -1914    952       C\\nATOM   1487  C   LEU A1015      42.928   5.886  44.013  1.00100.85           C\\nANISOU 1487  C   LEU A1015    11893  12218  14209  -1148  -2036   1034       C\\nATOM   1488  O   LEU A1015      43.750   6.434  43.268  1.00 98.40           O\\nANISOU 1488  O   LEU A1015    11399  11829  14161  -1460  -1984   1214       O\\nATOM   1489  CB  LEU A1015      40.885   7.309  43.827  1.00 99.65           C\\nANISOU 1489  CB  LEU A1015    12381  11497  13985  -1071  -2220    736       C\\nATOM   1490  CG  LEU A1015      39.471   7.567  43.292  1.00 99.54           C\\nANISOU 1490  CG  LEU A1015    12694  11242  13885   -893  -2166    655       C\\nATOM   1491  CD1 LEU A1015      39.000   8.964  43.667  1.00 99.18           C\\nANISOU 1491  CD1 LEU A1015    12859  10780  14044   -939  -2532    377       C\\nATOM   1492  CD2 LEU A1015      39.410   7.369  41.782  1.00 97.70           C\\nANISOU 1492  CD2 LEU A1015    12526  10927  13670   -996  -1904   1008       C\\nATOM   1493  N   LYS A1016      43.285   5.285  45.145  1.00105.59           N\\nANISOU 1493  N   LYS A1016    12353  13074  14693   -995  -2209    921       N\\nATOM   1494  CA  LYS A1016      44.673   5.127  45.549  1.00101.07           C\\nANISOU 1494  CA  LYS A1016    11354  12717  14330  -1119  -2373    997       C\\nATOM   1495  C   LYS A1016      45.057   3.654  45.506  1.00 97.42           C\\nANISOU 1495  C   LYS A1016    10673  12549  13792   -837  -2171   1168       C\\nATOM   1496  O   LYS A1016      44.204   2.765  45.581  1.00 93.98           O\\nANISOU 1496  O   LYS A1016    10480  12152  13076   -558  -2006   1179       O\\nATOM   1497  CB  LYS A1016      44.913   5.693  46.953  1.00 96.36           C\\nANISOU 1497  CB  LYS A1016    10775  12159  13680  -1180  -2856    730       C\\nATOM   1498  N   ILE A1017      46.361   3.401  45.382  1.00 93.92           N\\nANISOU 1498  N   ILE A1017     9745  12296  13643   -915  -2196   1291       N\\nATOM   1499  CA  ILE A1017      46.835   2.030  45.257  1.00 95.27           C\\nANISOU 1499  CA  ILE A1017     9663  12692  13845   -609  -2025   1434       C\\nATOM   1500  C   ILE A1017      46.498   1.247  46.517  1.00 93.58           C\\nANISOU 1500  C   ILE A1017     9634  12578  13344   -317  -2322   1390       C\\nATOM   1501  O   ILE A1017      46.630   1.745  47.643  1.00 98.49           O\\nANISOU 1501  O   ILE A1017    10306  13255  13861   -400  -2751   1258       O\\nATOM   1502  CB  ILE A1017      48.346   2.013  44.968  1.00 99.88           C\\nANISOU 1502  CB  ILE A1017     9604  13484  14862   -733  -2035   1517       C\\nATOM   1503  CG1 ILE A1017      48.641   2.776  43.677  1.00 99.15           C\\nANISOU 1503  CG1 ILE A1017     9368  13325  14980  -1097  -1674   1598       C\\nATOM   1504  CG2 ILE A1017      48.859   0.586  44.863  1.00102.32           C\\nANISOU 1504  CG2 ILE A1017     9624  13983  15272   -342  -1894   1617       C\\nATOM   1505  CD1 ILE A1017      50.072   2.657  43.214  1.00100.19           C\\nANISOU 1505  CD1 ILE A1017     8808  13728  15530  -1237  -1535   1668       C\\nATOM   1506  N   TYR A1018      46.040   0.013  46.328  1.00 96.96           N\\nANISOU 1506  N   TYR A1018    10204  13021  13613     -4  -2100   1503       N\\nATOM   1507  CA  TYR A1018      45.693  -0.867  47.432  1.00100.96           C\\nANISOU 1507  CA  TYR A1018    10937  13603  13821    241  -2341   1544       C\\nATOM   1508  C   TYR A1018      45.961  -2.303  47.006  1.00113.96           C\\nANISOU 1508  C   TYR A1018    12472  15250  15576    569  -2149   1734       C\\nATOM   1509  O   TYR A1018      46.224  -2.587  45.835  1.00121.07           O\\nANISOU 1509  O   TYR A1018    13172  16106  16722    616  -1774   1767       O\\nATOM   1510  CB  TYR A1018      44.232  -0.693  47.850  1.00 93.06           C\\nANISOU 1510  CB  TYR A1018    10474  12514  12372    220  -2278   1421       C\\nATOM   1511  CG  TYR A1018      43.253  -1.208  46.822  1.00 94.64           C\\nANISOU 1511  CG  TYR A1018    10901  12566  12493    308  -1824   1465       C\\nATOM   1512  CD1 TYR A1018      43.069  -0.541  45.617  1.00 98.44           C\\nANISOU 1512  CD1 TYR A1018    11346  12911  13146    160  -1544   1428       C\\nATOM   1513  CD2 TYR A1018      42.513  -2.358  47.053  1.00 92.36           C\\nANISOU 1513  CD2 TYR A1018    10884  12266  11944    505  -1704   1563       C\\nATOM   1514  CE1 TYR A1018      42.179  -1.007  44.669  1.00 97.08           C\\nANISOU 1514  CE1 TYR A1018    11389  12624  12873    230  -1183   1460       C\\nATOM   1515  CE2 TYR A1018      41.614  -2.831  46.111  1.00 95.41           C\\nANISOU 1515  CE2 TYR A1018    11463  12519  12271    556  -1325   1577       C\\nATOM   1516  CZ  TYR A1018      41.450  -2.147  44.923  1.00 96.24           C\\nANISOU 1516  CZ  TYR A1018    11515  12518  12534    430  -1079   1511       C\\nATOM   1517  OH  TYR A1018      40.562  -2.611  43.980  1.00 94.30           O\\nANISOU 1517  OH  TYR A1018    11469  12159  12201    471   -755   1517       O\\nATOM   1518  N   LYS A1019      45.882  -3.212  47.972  1.00112.29           N\\nANISOU 1518  N   LYS A1019    12428  15075  15161    787  -2416   1854       N\\nATOM   1519  CA  LYS A1019      46.124  -4.629  47.736  1.00114.49           C\\nANISOU 1519  CA  LYS A1019    12662  15272  15567   1129  -2330   2040       C\\nATOM   1520  C   LYS A1019      44.796  -5.365  47.616  1.00112.47           C\\nANISOU 1520  C   LYS A1019    12933  14846  14954   1191  -2067   2094       C\\nATOM   1521  O   LYS A1019      43.893  -5.162  48.435  1.00114.99           O\\nANISOU 1521  O   LYS A1019    13645  15200  14846   1061  -2176   2073       O\\nATOM   1522  CB  LYS A1019      46.964  -5.233  48.863  1.00116.93           C\\nANISOU 1522  CB  LYS A1019    12829  15675  15923   1330  -2866   2206       C\\nATOM   1523  N   ASP A1020      44.677  -6.212  46.597  1.00112.39           N\\nANISOU 1523  N   ASP A1020    12914  14672  15118   1369  -1707   2129       N\\nATOM   1524  CA  ASP A1020      43.491  -7.038  46.453  1.00108.38           C\\nANISOU 1524  CA  ASP A1020    12868  13981  14329   1415  -1485   2186       C\\nATOM   1525  C   ASP A1020      43.556  -8.206  47.436  1.00111.34           C\\nANISOU 1525  C   ASP A1020    13459  14255  14590   1619  -1796   2432       C\\nATOM   1526  O   ASP A1020      44.475  -8.316  48.253  1.00111.64           O\\nANISOU 1526  O   ASP A1020    13307  14376  14734   1741  -2219   2559       O\\nATOM   1527  CB  ASP A1020      43.344  -7.520  45.010  1.00103.84           C\\nANISOU 1527  CB  ASP A1020    12244  13254  13957   1507  -1026   2105       C\\nATOM   1528  CG  ASP A1020      44.444  -8.477  44.594  1.00108.01           C\\nANISOU 1528  CG  ASP A1020    12440  13694  14903   1844  -1010   2150       C\\nATOM   1529  OD1 ASP A1020      45.525  -8.453  45.217  1.00113.64           O\\nANISOU 1529  OD1 ASP A1020    12802  14515  15861   1981  -1346   2220       O\\nATOM   1530  OD2 ASP A1020      44.228  -9.253  43.639  1.00105.75           O\\nANISOU 1530  OD2 ASP A1020    12227  13235  14718   1987   -677   2082       O\\nATOM   1531  N   THR A1021      42.571  -9.101  47.357  1.00111.86           N\\nANISOU 1531  N   THR A1021    13936  14124  14441   1634  -1618   2524       N\\nATOM   1532  CA  THR A1021      42.498 -10.201  48.311  1.00111.37           C\\nANISOU 1532  CA  THR A1021    14180  13918  14216   1754  -1913   2816       C\\nATOM   1533  C   THR A1021      43.592 -11.242  48.108  1.00113.87           C\\nANISOU 1533  C   THR A1021    14272  14000  14994   2154  -2104   2966       C\\nATOM   1534  O   THR A1021      43.713 -12.150  48.936  1.00122.97           O\\nANISOU 1534  O   THR A1021    15669  14982  16073   2291  -2453   3261       O\\nATOM   1535  CB  THR A1021      41.130 -10.879  48.236  1.00106.11           C\\nANISOU 1535  CB  THR A1021    14000  13085  13230   1600  -1650   2877       C\\nATOM   1536  OG1 THR A1021      40.997 -11.555  46.980  1.00101.52           O\\nANISOU 1536  OG1 THR A1021    13390  12234  12949   1746  -1308   2783       O\\nATOM   1537  CG2 THR A1021      40.020  -9.844  48.372  1.00105.59           C\\nANISOU 1537  CG2 THR A1021    14074  13265  12778   1259  -1443   2671       C\\nATOM   1538  N   GLU A1022      44.388 -11.136  47.045  1.00109.65           N\\nANISOU 1538  N   GLU A1022    13282  13452  14927   2346  -1889   2772       N\\nATOM   1539  CA  GLU A1022      45.477 -12.070  46.790  1.00109.91           C\\nANISOU 1539  CA  GLU A1022    13002  13289  15472   2780  -2033   2824       C\\nATOM   1540  C   GLU A1022      46.850 -11.447  47.014  1.00110.30           C\\nANISOU 1540  C   GLU A1022    12423  13602  15882   2906  -2315   2766       C\\nATOM   1541  O   GLU A1022      47.866 -12.107  46.769  1.00114.91           O\\nANISOU 1541  O   GLU A1022    12609  14084  16969   3299  -2431   2752       O\\nATOM   1542  CB  GLU A1022      45.376 -12.625  45.367  1.00110.94           C\\nANISOU 1542  CB  GLU A1022    13056  13217  15878   2939  -1526   2594       C\\nATOM   1543  N   GLY A1023      46.907 -10.195  47.471  1.00108.89           N\\nANISOU 1543  N   GLY A1023    12123  13753  15498   2586  -2436   2704       N\\nATOM   1544  CA  GLY A1023      48.156  -9.536  47.793  1.00110.44           C\\nANISOU 1544  CA  GLY A1023    11736  14212  16013   2619  -2755   2653       C\\nATOM   1545  C   GLY A1023      48.709  -8.632  46.710  1.00113.05           C\\nANISOU 1545  C   GLY A1023    11548  14751  16654   2465  -2360   2382       C\\nATOM   1546  O   GLY A1023      49.639  -7.862  46.986  1.00112.39           O\\nANISOU 1546  O   GLY A1023    10982  14921  16798   2361  -2597   2323       O\\nATOM   1547  N   TYR A1024      48.174  -8.700  45.495  1.00108.30           N\\nANISOU 1547  N   TYR A1024    11043  14058  16046   2411  -1784   2230       N\\nATOM   1548  CA  TYR A1024      48.663  -7.880  44.398  1.00113.34           C\\nANISOU 1548  CA  TYR A1024    11259  14900  16907   2217  -1372   2019       C\\nATOM   1549  C   TYR A1024      48.186  -6.439  44.545  1.00111.52           C\\nANISOU 1549  C   TYR A1024    11170  14816  16386   1738  -1381   1979       C\\nATOM   1550  O   TYR A1024      47.084  -6.173  45.033  1.00110.91           O\\nANISOU 1550  O   TYR A1024    11615  14645  15882   1574  -1459   2021       O\\nATOM   1551  CB  TYR A1024      48.188  -8.447  43.060  1.00116.94           C\\nANISOU 1551  CB  TYR A1024    11856  15216  17360   2297   -787   1879       C\\nATOM   1552  CG  TYR A1024      48.578  -9.890  42.820  1.00122.30           C\\nANISOU 1552  CG  TYR A1024    12446  15674  18349   2790   -744   1850       C\\nATOM   1553  CD1 TYR A1024      49.830 -10.364  43.189  1.00128.61           C\\nANISOU 1553  CD1 TYR A1024    12689  16530  19645   3150  -1024   1848       C\\nATOM   1554  CD2 TYR A1024      47.689 -10.779  42.227  1.00118.01           C\\nANISOU 1554  CD2 TYR A1024    12364  14836  17638   2906   -460   1804       C\\nATOM   1555  CE1 TYR A1024      50.188 -11.681  42.970  1.00131.77           C\\nANISOU 1555  CE1 TYR A1024    13011  16664  20391   3655  -1019   1793       C\\nATOM   1556  CE2 TYR A1024      48.037 -12.096  42.004  1.00120.38           C\\nANISOU 1556  CE2 TYR A1024    12621  14859  18257   3363   -444   1744       C\\nATOM   1557  CZ  TYR A1024      49.287 -12.542  42.377  1.00129.11           C\\nANISOU 1557  CZ  TYR A1024    13187  15991  19879   3758   -723   1736       C\\nATOM   1558  OH  TYR A1024      49.639 -13.855  42.158  1.00133.04           O\\nANISOU 1558  OH  TYR A1024    13642  16152  20756   4269   -742   1651       O\\nATOM   1559  N   TYR A1025      49.029  -5.504  44.113  1.00117.71           N\\nANISOU 1559  N   TYR A1025    11469  15821  17433   1507  -1294   1881       N\\nATOM   1560  CA  TYR A1025      48.682  -4.087  44.152  1.00110.35           C\\nANISOU 1560  CA  TYR A1025    10659  14955  16314   1049  -1319   1834       C\\nATOM   1561  C   TYR A1025      47.758  -3.760  42.985  1.00104.43           C\\nANISOU 1561  C   TYR A1025    10246  14092  15339    855   -821   1781       C\\nATOM   1562  O   TYR A1025      48.115  -3.979  41.822  1.00101.17           O\\nANISOU 1562  O   TYR A1025     9617  13740  15082    859   -384   1729       O\\nATOM   1563  CB  TYR A1025      49.939  -3.221  44.101  1.00111.84           C\\nANISOU 1563  CB  TYR A1025    10220  15385  16890    814  -1427   1782       C\\nATOM   1564  CG  TYR A1025      50.892  -3.432  45.257  1.00115.51           C\\nANISOU 1564  CG  TYR A1025    10303  15992  17595    978  -1998   1822       C\\nATOM   1565  CD1 TYR A1025      50.776  -2.688  46.423  1.00114.38           C\\nANISOU 1565  CD1 TYR A1025    10332  15875  17252    775  -2517   1825       C\\nATOM   1566  CD2 TYR A1025      51.915  -4.369  45.177  1.00120.42           C\\nANISOU 1566  CD2 TYR A1025    10384  16722  18646   1352  -2046   1830       C\\nATOM   1567  CE1 TYR A1025      51.647  -2.875  47.481  1.00116.89           C\\nANISOU 1567  CE1 TYR A1025    10328  16345  17742    906  -3095   1869       C\\nATOM   1568  CE2 TYR A1025      52.791  -4.563  46.228  1.00124.27           C\\nANISOU 1568  CE2 TYR A1025    10509  17338  19372   1522  -2643   1887       C\\nATOM   1569  CZ  TYR A1025      52.653  -3.813  47.377  1.00124.31           C\\nANISOU 1569  CZ  TYR A1025    10724  17386  19121   1279  -3180   1923       C\\nATOM   1570  OH  TYR A1025      53.523  -4.004  48.428  1.00131.17           O\\nANISOU 1570  OH  TYR A1025    11258  18402  20177   1430  -3829   1986       O\\nATOM   1571  N   THR A1026      46.569  -3.247  43.288  1.00104.70           N\\nANISOU 1571  N   THR A1026    10799  13985  14997    692   -893   1776       N\\nATOM   1572  CA  THR A1026      45.596  -2.892  42.268  1.00105.81           C\\nANISOU 1572  CA  THR A1026    11282  14002  14919    524   -528   1739       C\\nATOM   1573  C   THR A1026      45.108  -1.467  42.499  1.00102.55           C\\nANISOU 1573  C   THR A1026    11058  13525  14382    179   -701   1694       C\\nATOM   1574  O   THR A1026      45.449  -0.819  43.493  1.00 98.86           O\\nANISOU 1574  O   THR A1026    10500  13102  13962     75  -1083   1653       O\\nATOM   1575  CB  THR A1026      44.400  -3.858  42.255  1.00102.47           C\\nANISOU 1575  CB  THR A1026    11323  13413  14198    735   -413   1745       C\\nATOM   1576  OG1 THR A1026      43.497  -3.517  43.312  1.00 98.43           O\\nANISOU 1576  OG1 THR A1026    11152  12846  13400    677   -704   1728       O\\nATOM   1577  CG2 THR A1026      44.861  -5.301  42.437  1.00103.30           C\\nANISOU 1577  CG2 THR A1026    11315  13487  14447   1108   -410   1798       C\\nATOM   1578  N   ILE A1027      44.296  -0.982  41.560  1.00 99.57           N\\nANISOU 1578  N   ILE A1027    10963  13018  13850     15   -450   1686       N\\nATOM   1579  CA  ILE A1027      43.734   0.361  41.638  1.00 94.27           C\\nANISOU 1579  CA  ILE A1027    10513  12198  13107   -265   -621   1637       C\\nATOM   1580  C   ILE A1027      42.483   0.419  40.770  1.00 89.78           C\\nANISOU 1580  C   ILE A1027    10350  11463  12301   -276   -407   1635       C\\nATOM   1581  O   ILE A1027      42.233  -0.483  39.962  1.00 86.52           O\\nANISOU 1581  O   ILE A1027    10008  11080  11787   -145    -97   1677       O\\nATOM   1582  CB  ILE A1027      44.771   1.417  41.213  1.00 89.65           C\\nANISOU 1582  CB  ILE A1027     9615  11643  12803   -620   -639   1700       C\\nATOM   1583  CG1 ILE A1027      44.397   2.796  41.761  1.00 84.69           C\\nANISOU 1583  CG1 ILE A1027     9187  10803  12189   -869   -988   1614       C\\nATOM   1584  CG2 ILE A1027      44.914   1.453  39.698  1.00 80.58           C\\nANISOU 1584  CG2 ILE A1027     8450  10512  11654   -794   -204   1829       C\\nATOM   1585  CD1 ILE A1027      45.403   3.866  41.434  1.00 82.74           C\\nANISOU 1585  CD1 ILE A1027     8667  10528  12241  -1282  -1056   1694       C\\nATOM   1586  N   GLY A1028      41.681   1.469  40.938  1.00 90.15           N\\nANISOU 1586  N   GLY A1028    10659  11318  12274   -414   -605   1560       N\\nATOM   1587  CA  GLY A1028      40.491   1.617  40.118  1.00 84.64           C\\nANISOU 1587  CA  GLY A1028    10306  10458  11396   -412   -482   1559       C\\nATOM   1588  C   GLY A1028      39.429   0.607  40.504  1.00 83.32           C\\nANISOU 1588  C   GLY A1028    10333  10329  10994   -142   -422   1455       C\\nATOM   1589  O   GLY A1028      39.140   0.390  41.685  1.00 81.04           O\\nANISOU 1589  O   GLY A1028    10066  10102  10624    -17   -599   1333       O\\nATOM   1590  N   ILE A1029      38.832  -0.021  39.494  1.00 90.61           N\\nANISOU 1590  N   ILE A1029    11415  11232  11782    -90   -168   1506       N\\nATOM   1591  CA  ILE A1029      37.857  -1.077  39.728  1.00 88.98           C\\nANISOU 1591  CA  ILE A1029    11375  11052  11381    109    -82   1426       C\\nATOM   1592  C   ILE A1029      38.467  -2.405  39.306  1.00 96.86           C\\nANISOU 1592  C   ILE A1029    12278  12138  12386    239    180   1504       C\\nATOM   1593  O   ILE A1029      38.305  -2.841  38.160  1.00 98.47           O\\nANISOU 1593  O   ILE A1029    12577  12322  12515    224    426   1527       O\\nATOM   1594  CB  ILE A1029      36.538  -0.812  38.980  1.00 75.33           C\\nANISOU 1594  CB  ILE A1029     9908   9202   9511     82    -63   1368       C\\nATOM   1595  CG1 ILE A1029      35.978   0.560  39.350  1.00 71.56           C\\nANISOU 1595  CG1 ILE A1029     9501   8581   9108     11   -352   1261       C\\nATOM   1596  CG2 ILE A1029      35.522  -1.900  39.298  1.00 63.88           C\\nANISOU 1596  CG2 ILE A1029     8583   7799   7889    229     23   1272       C\\nATOM   1597  CD1 ILE A1029      34.589   0.806  38.813  1.00 68.30           C\\nANISOU 1597  CD1 ILE A1029     9287   8054   8610     55   -413   1168       C\\nATOM   1598  N   GLY A1030      39.179  -3.050  40.226  1.00 99.15           N\\nANISOU 1598  N   GLY A1030    12396  12511  12765    380    101   1529       N\\nATOM   1599  CA  GLY A1030      39.787  -4.335  39.947  1.00 98.18           C\\nANISOU 1599  CA  GLY A1030    12171  12410  12722    571    291   1577       C\\nATOM   1600  C   GLY A1030      40.760  -4.288  38.789  1.00 94.57           C\\nANISOU 1600  C   GLY A1030    11485  12025  12421    523    562   1598       C\\nATOM   1601  O   GLY A1030      40.506  -4.869  37.728  1.00 95.69           O\\nANISOU 1601  O   GLY A1030    11749  12138  12469    550    849   1553       O\\nATOM   1602  N   HIS A1031      41.878  -3.592  38.977  1.00 87.03           N\\nANISOU 1602  N   HIS A1031    10189  11192  11687    421    486   1644       N\\nATOM   1603  CA  HIS A1031      42.893  -3.436  37.938  1.00 89.86           C\\nANISOU 1603  CA  HIS A1031    10256  11692  12196    312    785   1660       C\\nATOM   1604  C   HIS A1031      44.259  -3.687  38.565  1.00 92.16           C\\nANISOU 1604  C   HIS A1031    10046  12138  12831    439    693   1664       C\\nATOM   1605  O   HIS A1031      44.848  -2.781  39.162  1.00 95.75           O\\nANISOU 1605  O   HIS A1031    10270  12666  13443    260    450   1711       O\\nATOM   1606  CB  HIS A1031      42.821  -2.053  37.308  1.00 89.34           C\\nANISOU 1606  CB  HIS A1031    10256  11621  12066    -69    797   1742       C\\nATOM   1607  CG  HIS A1031      43.762  -1.865  36.161  1.00 92.70           C\\nANISOU 1607  CG  HIS A1031    10434  12232  12556   -271   1167   1789       C\\nATOM   1608  ND1 HIS A1031      43.332  -1.784  34.855  1.00 93.45           N\\nANISOU 1608  ND1 HIS A1031    10789  12339  12379   -440   1471   1824       N\\nATOM   1609  CD2 HIS A1031      45.109  -1.748  36.123  1.00 96.67           C\\nANISOU 1609  CD2 HIS A1031    10434  12956  13341   -356   1297   1798       C\\nATOM   1610  CE1 HIS A1031      44.375  -1.621  34.061  1.00 97.80           C\\nANISOU 1610  CE1 HIS A1031    11037  13125  12996   -641   1814   1858       C\\nATOM   1611  NE2 HIS A1031      45.465  -1.597  34.805  1.00100.11           N\\nANISOU 1611  NE2 HIS A1031    10830  13554  13654   -592   1731   1833       N\\nATOM   1612  N   LEU A1032      44.761  -4.912  38.422  1.00 91.24           N\\nANISOU 1612  N   LEU A1032     9754  12051  12863    756    853   1596       N\\nATOM   1613  CA  LEU A1032      46.058  -5.267  38.982  1.00 95.11           C\\nANISOU 1613  CA  LEU A1032     9720  12682  13737    952    730   1587       C\\nATOM   1614  C   LEU A1032      47.161  -4.499  38.265  1.00 99.71           C\\nANISOU 1614  C   LEU A1032     9815  13531  14540    697    975   1562       C\\nATOM   1615  O   LEU A1032      47.347  -4.649  37.054  1.00 96.96           O\\nANISOU 1615  O   LEU A1032     9403  13297  14140    624   1442   1479       O\\nATOM   1616  CB  LEU A1032      46.290  -6.772  38.868  1.00 93.50           C\\nANISOU 1616  CB  LEU A1032     9457  12381  13686   1392    849   1495       C\\nATOM   1617  N   LEU A1033      47.887  -3.667  39.013  1.00 97.35           N\\nANISOU 1617  N   LEU A1033     9181  13349  14459    521    666   1628       N\\nATOM   1618  CA  LEU A1033      49.025  -2.964  38.434  1.00104.31           C\\nANISOU 1618  CA  LEU A1033     9528  14502  15604    230    883   1619       C\\nATOM   1619  C   LEU A1033      50.158  -3.934  38.121  1.00112.65           C\\nANISOU 1619  C   LEU A1033     9983  15786  17034    550   1131   1473       C\\nATOM   1620  O   LEU A1033      50.737  -3.897  37.029  1.00115.99           O\\nANISOU 1620  O   LEU A1033    10102  16446  17521    410   1635   1381       O\\nATOM   1621  CB  LEU A1033      49.494  -1.861  39.381  1.00103.46           C\\nANISOU 1621  CB  LEU A1033     9213  14430  15668    -55    434   1699       C\\nATOM   1622  N   THR A1034      50.477  -4.818  39.064  1.00114.71           N\\nANISOU 1622  N   THR A1034    10071  15980  17534    990    782   1443       N\\nATOM   1623  CA  THR A1034      51.514  -5.822  38.866  1.00119.05           C\\nANISOU 1623  CA  THR A1034    10043  16677  18514   1403    933   1278       C\\nATOM   1624  C   THR A1034      51.333  -6.919  39.904  1.00116.13           C\\nANISOU 1624  C   THR A1034     9831  16045  18250   1915    470   1326       C\\nATOM   1625  O   THR A1034      50.615  -6.756  40.893  1.00112.94           O\\nANISOU 1625  O   THR A1034     9869  15449  17593   1873     24   1499       O\\nATOM   1626  CB  THR A1034      52.919  -5.218  38.968  1.00123.11           C\\nANISOU 1626  CB  THR A1034     9729  17558  19489   1237    901   1232       C\\nATOM   1627  OG1 THR A1034      53.898  -6.241  38.746  1.00127.31           O\\nANISOU 1627  OG1 THR A1034     9644  18240  20490   1707   1059   1022       O\\nATOM   1628  CG2 THR A1034      53.135  -4.617  40.344  1.00124.58           C\\nANISOU 1628  CG2 THR A1034     9836  17714  19783   1140    210   1384       C\\nATOM   1629  N   LYS A1035      51.998  -8.046  39.660  1.00124.24           N\\nANISOU 1629  N   LYS A1035    10499  17061  19647   2398    588   1165       N\\nATOM   1630  CA  LYS A1035      52.071  -9.132  40.624  1.00115.60           C\\nANISOU 1630  CA  LYS A1035     9471  15694  18757   2910    100   1245       C\\nATOM   1631  C   LYS A1035      53.350  -9.089  41.448  1.00124.45           C\\nANISOU 1631  C   LYS A1035     9878  17011  20395   3112   -361   1270       C\\nATOM   1632  O   LYS A1035      53.591 -10.004  42.241  1.00126.86           O\\nANISOU 1632  O   LYS A1035    10167  17100  20932   3572   -826   1360       O\\nATOM   1633  CB  LYS A1035      51.953 -10.483  39.911  1.00108.04           C\\nANISOU 1633  CB  LYS A1035     8621  14489  17940   3381    417   1046       C\\nATOM   1634  N   SER A1036      54.169  -8.044  41.282  1.00124.75           N\\nANISOU 1634  N   SER A1036     9333  17441  20626   2756   -279   1212       N\\nATOM   1635  CA  SER A1036      55.429  -7.892  41.994  1.00130.16           C\\nANISOU 1635  CA  SER A1036     9248  18374  21834   2880   -717   1205       C\\nATOM   1636  C   SER A1036      55.191  -7.369  43.411  1.00127.51           C\\nANISOU 1636  C   SER A1036     9199  17961  21290   2719  -1470   1465       C\\nATOM   1637  O   SER A1036      54.249  -6.611  43.652  1.00124.62           O\\nANISOU 1637  O   SER A1036     9437  17497  20415   2316  -1507   1585       O\\nATOM   1638  CB  SER A1036      56.351  -6.937  41.243  1.00133.68           C\\nANISOU 1638  CB  SER A1036     8966  19280  22547   2465   -307   1043       C\\nATOM   1639  N   PRO A1037      56.041  -7.758  44.369  1.00132.59           N\\nANISOU 1639  N   PRO A1037     9408  18656  22314   3043  -2094   1531       N\\nATOM   1640  CA  PRO A1037      55.818  -7.332  45.758  1.00131.46           C\\nANISOU 1640  CA  PRO A1037     9590  18465  21895   2895  -2836   1763       C\\nATOM   1641  C   PRO A1037      56.251  -5.907  46.050  1.00131.07           C\\nANISOU 1641  C   PRO A1037     9233  18724  21845   2324  -3004   1723       C\\nATOM   1642  O   PRO A1037      55.767  -5.327  47.031  1.00128.15           O\\nANISOU 1642  O   PRO A1037     9314  18300  21079   2075  -3470   1849       O\\nATOM   1643  CB  PRO A1037      56.658  -8.330  46.564  1.00137.89           C\\nANISOU 1643  CB  PRO A1037    10022  19225  23144   3474  -3467   1855       C\\nATOM   1644  CG  PRO A1037      57.788  -8.659  45.647  1.00141.32           C\\nANISOU 1644  CG  PRO A1037     9525  19887  24282   3748  -3098   1581       C\\nATOM   1645  CD  PRO A1037      57.205  -8.654  44.250  1.00138.32           C\\nANISOU 1645  CD  PRO A1037     9352  19476  23728   3597  -2186   1384       C\\nATOM   1646  N   SER A1038      57.142  -5.329  45.249  1.00134.97           N\\nANISOU 1646  N   SER A1038     8987  19535  22758   2087  -2636   1539       N\\nATOM   1647  CA  SER A1038      57.615  -3.977  45.512  1.00138.82           C\\nANISOU 1647  CA  SER A1038     9165  20272  23307   1497  -2818   1510       C\\nATOM   1648  C   SER A1038      56.508  -2.965  45.234  1.00142.03           C\\nANISOU 1648  C   SER A1038    10304  20506  23157    966  -2548   1556       C\\nATOM   1649  O   SER A1038      55.905  -2.966  44.156  1.00142.81           O\\nANISOU 1649  O   SER A1038    10685  20515  23061    864  -1905   1526       O\\nATOM   1650  CB  SER A1038      58.845  -3.669  44.659  1.00137.97           C\\nANISOU 1650  CB  SER A1038     8060  20560  23801   1331  -2429   1322       C\\nATOM   1651  N   LEU A1039      56.235  -2.105  46.219  1.00148.93           N\\nANISOU 1651  N   LEU A1039    11491  21326  23772    647  -3071   1607       N\\nATOM   1652  CA  LEU A1039      55.237  -1.059  46.027  1.00137.41           C\\nANISOU 1652  CA  LEU A1039    10670  19674  21866    176  -2887   1609       C\\nATOM   1653  C   LEU A1039      55.728  -0.005  45.042  1.00134.86           C\\nANISOU 1653  C   LEU A1039     9968  19484  21790   -372  -2464   1547       C\\nATOM   1654  O   LEU A1039      54.942   0.522  44.246  1.00128.51           O\\nANISOU 1654  O   LEU A1039     9617  18504  20707   -648  -2029   1577       O\\nATOM   1655  CB  LEU A1039      54.882  -0.422  47.371  1.00133.76           C\\nANISOU 1655  CB  LEU A1039    10606  19126  21088      8  -3557   1606       C\\nATOM   1656  CG  LEU A1039      53.969   0.807  47.351  1.00123.44           C\\nANISOU 1656  CG  LEU A1039     9880  17606  19417   -461  -3487   1537       C\\nATOM   1657  CD1 LEU A1039      52.634   0.486  46.697  1.00115.73           C\\nANISOU 1657  CD1 LEU A1039     9575  16373  18024   -334  -3002   1586       C\\nATOM   1658  CD2 LEU A1039      53.766   1.349  48.759  1.00121.51           C\\nANISOU 1658  CD2 LEU A1039     9948  17332  18887   -575  -4163   1451       C\\nATOM   1659  N   ASN A1040      57.027   0.309  45.078  1.00140.78           N\\nANISOU 1659  N   ASN A1040     9881  20545  23065   -557  -2602   1481       N\\nATOM   1660  CA  ASN A1040      57.584   1.273  44.135  1.00137.59           C\\nANISOU 1660  CA  ASN A1040     9069  20297  22910  -1145  -2171   1458       C\\nATOM   1661  C   ASN A1040      57.424   0.803  42.695  1.00142.78           C\\nANISOU 1661  C   ASN A1040     9696  21027  23528  -1086  -1335   1468       C\\nATOM   1662  O   ASN A1040      57.214   1.623  41.793  1.00129.49           O\\nANISOU 1662  O   ASN A1040     8176  19309  21715  -1595   -895   1536       O\\nATOM   1663  CB  ASN A1040      59.058   1.528  44.452  1.00137.97           C\\nANISOU 1663  CB  ASN A1040     8117  20728  23578  -1326  -2453   1368       C\\nATOM   1664  N   ALA A1041      57.513  -0.508  42.459  1.00141.43           N\\nANISOU 1664  N   ALA A1041     9359  20933  23447   -478  -1132   1401       N\\nATOM   1665  CA  ALA A1041      57.326  -1.032  41.111  1.00146.42           C\\nANISOU 1665  CA  ALA A1041    10009  21635  23988   -388   -344   1347       C\\nATOM   1666  C   ALA A1041      55.865  -0.980  40.683  1.00137.93           C\\nANISOU 1666  C   ALA A1041     9919  20195  22294   -425   -117   1454       C\\nATOM   1667  O   ALA A1041      55.576  -0.783  39.497  1.00137.36           O\\nANISOU 1667  O   ALA A1041    10016  20159  22015   -671    490   1467       O\\nATOM   1668  CB  ALA A1041      57.852  -2.465  41.023  1.00155.04           C\\nANISOU 1668  CB  ALA A1041    10644  22857  25406    310   -239   1186       C\\nATOM   1669  N   ALA A1042      54.935  -1.157  41.626  1.00140.82           N\\nANISOU 1669  N   ALA A1042    10925  20238  22341   -200   -595   1527       N\\nATOM   1670  CA  ALA A1042      53.519  -1.060  41.288  1.00132.90           C\\nANISOU 1670  CA  ALA A1042    10790  18913  20795   -244   -420   1604       C\\nATOM   1671  C   ALA A1042      53.142   0.352  40.863  1.00133.14           C\\nANISOU 1671  C   ALA A1042    11109  18838  20640   -869   -326   1693       C\\nATOM   1672  O   ALA A1042      52.205   0.531  40.075  1.00130.01           O\\nANISOU 1672  O   ALA A1042    11253  18260  19885   -986      1   1755       O\\nATOM   1673  CB  ALA A1042      52.662  -1.505  42.472  1.00126.18           C\\nANISOU 1673  CB  ALA A1042    10481  17801  19659     81   -937   1646       C\\nATOM   1674  N   LYS A1043      53.853   1.361  41.370  1.00137.98           N\\nANISOU 1674  N   LYS A1043    11384  19531  21510  -1275   -652   1703       N\\nATOM   1675  CA  LYS A1043      53.613   2.736  40.950  1.00131.35           C\\nANISOU 1675  CA  LYS A1043    10799  18530  20579  -1894   -598   1802       C\\nATOM   1676  C   LYS A1043      54.204   3.022  39.577  1.00133.43           C\\nANISOU 1676  C   LYS A1043    10730  19015  20952  -2291     34   1891       C\\nATOM   1677  O   LYS A1043      53.705   3.899  38.864  1.00133.13           O\\nANISOU 1677  O   LYS A1043    11108  18782  20694  -2733    227   2044       O\\nATOM   1678  CB  LYS A1043      54.192   3.713  41.976  1.00128.92           C\\nANISOU 1678  CB  LYS A1043    10263  18193  20526  -2230  -1186   1758       C\\nATOM   1679  CG  LYS A1043      53.569   3.618  43.359  1.00124.36           C\\nANISOU 1679  CG  LYS A1043    10090  17422  19739  -1936  -1811   1654       C\\nATOM   1680  CD  LYS A1043      54.054   4.744  44.258  1.00124.45           C\\nANISOU 1680  CD  LYS A1043     9973  17371  19941  -2345  -2374   1565       C\\nATOM   1681  CE  LYS A1043      53.301   4.761  45.577  1.00122.13           C\\nANISOU 1681  CE  LYS A1043    10189  16897  19319  -2105  -2935   1426       C\\nATOM   1682  NZ  LYS A1043      53.698   5.919  46.425  1.00124.65           N\\nANISOU 1682  NZ  LYS A1043    10461  17121  19779  -2520  -3485   1275       N\\nATOM   1683  N   SER A1044      55.263   2.305  39.194  1.00130.51           N\\nANISOU 1683  N   SER A1044     9619  19057  20914  -2142    357   1795       N\\nATOM   1684  CA  SER A1044      55.858   2.511  37.879  1.00137.15           C\\nANISOU 1684  CA  SER A1044    10108  20197  21806  -2533   1041   1845       C\\nATOM   1685  C   SER A1044      54.904   2.086  36.770  1.00136.57           C\\nANISOU 1685  C   SER A1044    10643  20016  21232  -2427   1563   1899       C\\nATOM   1686  O   SER A1044      54.789   2.771  35.747  1.00141.22           O\\nANISOU 1686  O   SER A1044    11441  20628  21589  -2937   1967   2067       O\\nATOM   1687  CB  SER A1044      57.179   1.749  37.775  1.00143.25           C\\nANISOU 1687  CB  SER A1044     9888  21468  23072  -2311   1285   1648       C\\nATOM   1688  N   GLU A1045      54.211   0.960  36.954  1.00136.81           N\\nANISOU 1688  N   GLU A1045    10988  19917  21076  -1800   1534   1777       N\\nATOM   1689  CA  GLU A1045      53.243   0.521  35.955  1.00129.18           C\\nANISOU 1689  CA  GLU A1045    10619  18832  19631  -1695   1960   1797       C\\nATOM   1690  C   GLU A1045      52.010   1.415  35.939  1.00128.34           C\\nANISOU 1690  C   GLU A1045    11333  18313  19118  -1974   1718   2002       C\\nATOM   1691  O   GLU A1045      51.383   1.582  34.887  1.00126.75           O\\nANISOU 1691  O   GLU A1045    11575  18053  18531  -2171   2069   2109       O\\nATOM   1692  CB  GLU A1045      52.847  -0.934  36.210  1.00121.20           C\\nANISOU 1692  CB  GLU A1045     9714  17751  18586   -982   1950   1604       C\\nATOM   1693  N   LEU A1046      51.650   1.998  37.088  1.00131.91           N\\nANISOU 1693  N   LEU A1046    11988  18485  19645  -1980   1106   2037       N\\nATOM   1694  CA  LEU A1046      50.490   2.885  37.146  1.00126.43           C\\nANISOU 1694  CA  LEU A1046    12012  17383  18643  -2189    846   2169       C\\nATOM   1695  C   LEU A1046      50.730   4.156  36.342  1.00134.52           C\\nANISOU 1695  C   LEU A1046    13116  18345  19652  -2860    993   2395       C\\nATOM   1696  O   LEU A1046      49.873   4.579  35.558  1.00138.35           O\\nANISOU 1696  O   LEU A1046    14165  18604  19797  -3036   1114   2555       O\\nATOM   1697  CB  LEU A1046      50.156   3.227  38.600  1.00114.87           C\\nANISOU 1697  CB  LEU A1046    10689  15684  17273  -2043    195   2081       C\\nATOM   1698  CG  LEU A1046      49.189   4.395  38.827  1.00103.62           C\\nANISOU 1698  CG  LEU A1046     9857  13838  15674  -2297   -138   2146       C\\nATOM   1699  CD1 LEU A1046      47.828   4.107  38.217  1.00 96.31           C\\nANISOU 1699  CD1 LEU A1046     9556  12698  14341  -2097     22   2183       C\\nATOM   1700  CD2 LEU A1046      49.056   4.722  40.308  1.00 99.47           C\\nANISOU 1700  CD2 LEU A1046     9379  13170  15245  -2171   -734   1980       C\\nATOM   1701  N   ASP A1047      51.893   4.784  36.529  1.00127.49           N\\nANISOU 1701  N   ASP A1047    11667  17635  19137  -3262    951   2433       N\\nATOM   1702  CA  ASP A1047      52.188   6.012  35.801  1.00131.96           C\\nANISOU 1702  CA  ASP A1047    12311  18112  19714  -3978   1078   2692       C\\nATOM   1703  C   ASP A1047      52.444   5.742  34.324  1.00130.92           C\\nANISOU 1703  C   ASP A1047    12130  18291  19323  -4228   1792   2837       C\\nATOM   1704  O   ASP A1047      52.172   6.607  33.483  1.00133.98           O\\nANISOU 1704  O   ASP A1047    12921  18510  19475  -4745   1927   3128       O\\nATOM   1705  CB  ASP A1047      53.382   6.723  36.435  1.00141.47           C\\nANISOU 1705  CB  ASP A1047    12895  19442  21416  -4390    835   2678       C\\nATOM   1706  CG  ASP A1047      53.050   7.320  37.791  1.00139.91           C\\nANISOU 1706  CG  ASP A1047    12900  18874  21385  -4305     95   2555       C\\nATOM   1707  OD1 ASP A1047      51.910   7.125  38.263  1.00133.93           O\\nANISOU 1707  OD1 ASP A1047    12719  17809  20359  -3898   -178   2466       O\\nATOM   1708  OD2 ASP A1047      53.925   7.988  38.382  1.00142.42           O\\nANISOU 1708  OD2 ASP A1047    12791  19231  22093  -4666   -203   2522       O\\nATOM   1709  N   LYS A1048      52.958   4.557  33.986  1.00136.15           N\\nANISOU 1709  N   LYS A1048    12332  19393  20008  -3866   2239   2634       N\\nATOM   1710  CA  LYS A1048      53.156   4.211  32.584  1.00137.23           C\\nANISOU 1710  CA  LYS A1048    12447  19868  19828  -4059   2961   2691       C\\nATOM   1711  C   LYS A1048      51.836   3.990  31.855  1.00136.24           C\\nANISOU 1711  C   LYS A1048    13159  19483  19123  -3907   3045   2785       C\\nATOM   1712  O   LYS A1048      51.813   4.012  30.619  1.00135.03           O\\nANISOU 1712  O   LYS A1048    13198  19529  18579  -4209   3556   2913       O\\nATOM   1713  CB  LYS A1048      54.036   2.964  32.467  1.00137.25           C\\nANISOU 1713  CB  LYS A1048    11720  20374  20055  -3634   3395   2361       C\\nATOM   1714  N   ALA A1049      50.743   3.782  32.587  1.00134.09           N\\nANISOU 1714  N   ALA A1049    13374  18806  18767  -3471   2557   2719       N\\nATOM   1715  CA  ALA A1049      49.423   3.607  31.993  1.00136.97           C\\nANISOU 1715  CA  ALA A1049    14488  18911  18642  -3319   2551   2790       C\\nATOM   1716  C   ALA A1049      48.555   4.853  32.093  1.00139.86           C\\nANISOU 1716  C   ALA A1049    15461  18785  18895  -3629   2088   3059       C\\nATOM   1717  O   ALA A1049      47.775   5.130  31.178  1.00144.34           O\\nANISOU 1717  O   ALA A1049    16587  19202  19054  -3792   2166   3254       O\\nATOM   1718  CB  ALA A1049      48.697   2.429  32.649  1.00134.83           C\\nANISOU 1718  CB  ALA A1049    14339  18543  18349  -2619   2376   2514       C\\nATOM   1719  N   ILE A1050      48.667   5.615  33.186  1.00147.00           N\\nANISOU 1719  N   ILE A1050    16279  19419  20157  -3696   1573   3052       N\\nATOM   1720  CA  ILE A1050      47.884   6.843  33.320  1.00137.76           C\\nANISOU 1720  CA  ILE A1050    15661  17727  18955  -3954   1109   3250       C\\nATOM   1721  C   ILE A1050      48.527   8.029  32.621  1.00135.31           C\\nANISOU 1721  C   ILE A1050    15376  17334  18700  -4696   1193   3602       C\\nATOM   1722  O   ILE A1050      47.861   9.054  32.425  1.00132.09           O\\nANISOU 1722  O   ILE A1050    15513  16449  18227  -4950    855   3834       O\\nATOM   1723  CB  ILE A1050      47.649   7.192  34.802  1.00112.75           C\\nANISOU 1723  CB  ILE A1050    12459  14272  16111  -3710    512   3036       C\\nATOM   1724  N   GLY A1051      49.800   7.923  32.236  1.00128.26           N\\nANISOU 1724  N   GLY A1051    13902  16884  17947  -5058   1630   3652       N\\nATOM   1725  CA  GLY A1051      50.479   8.964  31.501  1.00126.01           C\\nANISOU 1725  CA  GLY A1051    13606  16592  17681  -5844   1802   4017       C\\nATOM   1726  C   GLY A1051      51.114  10.046  32.350  1.00125.68           C\\nANISOU 1726  C   GLY A1051    13328  16279  18144  -6255   1362   4067       C\\nATOM   1727  O   GLY A1051      52.053  10.703  31.888  1.00131.62           O\\nANISOU 1727  O   GLY A1051    13814  17166  19028  -6906   1590   4283       O\\nATOM   1728  N   ARG A1052      50.638  10.250  33.572  1.00125.39           N\\nANISOU 1728  N   ARG A1052    13398  15875  18368  -5892    754   3830       N\\nATOM   1729  CA  ARG A1052      51.137  11.295  34.452  1.00130.48           C\\nANISOU 1729  CA  ARG A1052    13895  16207  19473  -6249    261   3810       C\\nATOM   1730  C   ARG A1052      51.879  10.681  35.633  1.00133.64           C\\nANISOU 1730  C   ARG A1052    13610  16936  20230  -5922     98   3432       C\\nATOM   1731  O   ARG A1052      51.880   9.465  35.836  1.00139.15           O\\nANISOU 1731  O   ARG A1052    14025  18014  20831  -5363    306   3204       O\\nATOM   1732  CB  ARG A1052      49.986  12.174  34.954  1.00127.22           C\\nANISOU 1732  CB  ARG A1052    14202  15072  19066  -6123   -369   3798       C\\nATOM   1733  CG  ARG A1052      49.063  11.466  35.933  1.00118.27           C\\nANISOU 1733  CG  ARG A1052    13210  13879  17849  -5343   -664   3404       C\\nATOM   1734  CD  ARG A1052      47.922  12.363  36.372  1.00115.96           C\\nANISOU 1734  CD  ARG A1052    13565  12916  17579  -5212  -1224   3339       C\\nATOM   1735  NE  ARG A1052      47.116  11.751  37.424  1.00114.03           N\\nANISOU 1735  NE  ARG A1052    13390  12676  17262  -4541  -1477   2931       N\\nATOM   1736  CZ  ARG A1052      47.303  11.960  38.723  1.00115.93           C\\nANISOU 1736  CZ  ARG A1052    13460  12852  17737  -4403  -1881   2594       C\\nATOM   1737  NH1 ARG A1052      48.271  12.768  39.132  1.00119.81           N\\nANISOU 1737  NH1 ARG A1052    13686  13244  18594  -4875  -2117   2592       N\\nATOM   1738  NH2 ARG A1052      46.523  11.364  39.613  1.00113.10           N\\nANISOU 1738  NH2 ARG A1052    13205  12544  17222  -3834  -2048   2259       N\\nATOM   1739  N   ASN A1053      52.517  11.551  36.419  1.00125.16           N\\nANISOU 1739  N   ASN A1053    12297  15678  19580  -6291   -324   3375       N\\nATOM   1740  CA  ASN A1053      53.118  11.156  37.692  1.00123.03           C\\nANISOU 1740  CA  ASN A1053    11481  15629  19636  -6002   -663   3022       C\\nATOM   1741  C   ASN A1053      52.002  11.117  38.731  1.00122.77           C\\nANISOU 1741  C   ASN A1053    11968  15217  19462  -5447  -1194   2750       C\\nATOM   1742  O   ASN A1053      51.786  12.056  39.502  1.00122.02           O\\nANISOU 1742  O   ASN A1053    12131  14690  19541  -5602  -1734   2626       O\\nATOM   1743  CB  ASN A1053      54.234  12.115  38.089  1.00126.67           C\\nANISOU 1743  CB  ASN A1053    11485  16063  20583  -6663   -923   3047       C\\nATOM   1744  N   THR A1054      51.272   9.995  38.739  1.00124.33           N\\nANISOU 1744  N   THR A1054    12319  15587  19333  -4804  -1013   2632       N\\nATOM   1745  CA  THR A1054      50.060   9.901  39.547  1.00119.55           C\\nANISOU 1745  CA  THR A1054    12244  14668  18513  -4306  -1394   2406       C\\nATOM   1746  C   THR A1054      50.366   9.947  41.037  1.00119.71           C\\nANISOU 1746  C   THR A1054    12048  14716  18720  -4133  -1918   2083       C\\nATOM   1747  O   THR A1054      49.504  10.334  41.835  1.00120.96           O\\nANISOU 1747  O   THR A1054    12645  14548  18764  -3922  -2315   1863       O\\nATOM   1748  CB  THR A1054      49.295   8.620  39.212  1.00115.03           C\\nANISOU 1748  CB  THR A1054    11827  14310  17568  -3728  -1059   2370       C\\nATOM   1749  N   ASN A1055      51.577   9.556  41.433  1.00118.97           N\\nANISOU 1749  N   ASN A1055    11271  15030  18901  -4213  -1934   2029       N\\nATOM   1750  CA  ASN A1055      52.004   9.557  42.830  1.00116.22           C\\nANISOU 1750  CA  ASN A1055    10681  14771  18707  -4084  -2473   1748       C\\nATOM   1751  C   ASN A1055      51.115   8.687  43.711  1.00119.38           C\\nANISOU 1751  C   ASN A1055    11395  15214  18750  -3437  -2650   1539       C\\nATOM   1752  O   ASN A1055      51.131   8.822  44.935  1.00121.96           O\\nANISOU 1752  O   ASN A1055    11754  15533  19052  -3324  -3143   1293       O\\nATOM   1753  CB  ASN A1055      52.071  10.984  43.391  1.00109.11           C\\nANISOU 1753  CB  ASN A1055     9992  13444  18023  -4552  -2980   1627       C\\nATOM   1754  N   GLY A1056      50.340   7.783  43.111  1.00115.78           N\\nANISOU 1754  N   GLY A1056    11183  14819  17987  -3045  -2253   1632       N\\nATOM   1755  CA  GLY A1056      49.518   6.838  43.832  1.00115.99           C\\nANISOU 1755  CA  GLY A1056    11480  14915  17677  -2485  -2341   1489       C\\nATOM   1756  C   GLY A1056      48.027   7.076  43.671  1.00112.88           C\\nANISOU 1756  C   GLY A1056    11762  14182  16944  -2317  -2293   1431       C\\nATOM   1757  O   GLY A1056      47.247   6.120  43.742  1.00109.86           O\\nANISOU 1757  O   GLY A1056    11592  13885  16264  -1902  -2132   1408       O\\nATOM   1758  N   VAL A1057      47.618   8.323  43.454  1.00113.85           N\\nANISOU 1758  N   VAL A1057    12208  13906  17145  -2632  -2448   1405       N\\nATOM   1759  CA  VAL A1057      46.211   8.699  43.361  1.00103.36           C\\nANISOU 1759  CA  VAL A1057    11467  12226  15579  -2456  -2483   1304       C\\nATOM   1760  C   VAL A1057      45.881   9.003  41.907  1.00105.21           C\\nANISOU 1760  C   VAL A1057    11904  12256  15814  -2653  -2149   1598       C\\nATOM   1761  O   VAL A1057      46.708   9.560  41.176  1.00111.08           O\\nANISOU 1761  O   VAL A1057    12459  12960  16785  -3103  -2041   1831       O\\nATOM   1762  CB  VAL A1057      45.900   9.912  44.260  1.00 96.42           C\\nANISOU 1762  CB  VAL A1057    10853  10979  14804  -2591  -2980   1005       C\\nATOM   1763  N   ILE A1058      44.667   8.639  41.488  1.00104.59           N\\nANISOU 1763  N   ILE A1058    12209  12071  15459  -2350  -1994   1597       N\\nATOM   1764  CA  ILE A1058      44.203   8.889  40.131  1.00100.91           C\\nANISOU 1764  CA  ILE A1058    12012  11414  14916  -2498  -1744   1872       C\\nATOM   1765  C   ILE A1058      42.794   9.466  40.170  1.00 98.60           C\\nANISOU 1765  C   ILE A1058    12224  10714  14524  -2295  -1978   1737       C\\nATOM   1766  O   ILE A1058      42.091   9.405  41.182  1.00 92.24           O\\nANISOU 1766  O   ILE A1058    11523   9875  13648  -1976  -2199   1403       O\\nATOM   1767  CB  ILE A1058      44.229   7.619  39.253  1.00 94.08           C\\nANISOU 1767  CB  ILE A1058    11024  10914  13808  -2321  -1243   2041       C\\nATOM   1768  CG1 ILE A1058      43.313   6.543  39.831  1.00 82.54           C\\nANISOU 1768  CG1 ILE A1058     9675   9599  12089  -1804  -1208   1830       C\\nATOM   1769  CG2 ILE A1058      45.650   7.101  39.083  1.00 91.55           C\\nANISOU 1769  CG2 ILE A1058    10149  10986  13649  -2498   -980   2147       C\\nATOM   1770  CD1 ILE A1058      43.175   5.325  38.950  1.00 80.94           C\\nANISOU 1770  CD1 ILE A1058     9440   9653  11661  -1618   -764   1951       C\\nATOM   1771  N   THR A1059      42.391  10.038  39.038  1.00100.27           N\\nANISOU 1771  N   THR A1059    12740  10636  14723  -2488  -1928   2000       N\\nATOM   1772  CA  THR A1059      41.046  10.571  38.887  1.00100.12           C\\nANISOU 1772  CA  THR A1059    13164  10218  14658  -2267  -2166   1907       C\\nATOM   1773  C   THR A1059      40.043   9.431  38.714  1.00 93.93           C\\nANISOU 1773  C   THR A1059    12445   9697  13549  -1832  -1928   1816       C\\nATOM   1774  O   THR A1059      40.390   8.322  38.302  1.00 93.12           O\\nANISOU 1774  O   THR A1059    12152   9988  13239  -1781  -1546   1935       O\\nATOM   1775  CB  THR A1059      40.982  11.515  37.681  1.00103.74           C\\nANISOU 1775  CB  THR A1059    13952  10269  15193  -2630  -2248   2286       C\\nATOM   1776  OG1 THR A1059      42.175  12.306  37.630  1.00105.14           O\\nANISOU 1776  OG1 THR A1059    13991  10320  15636  -3159  -2321   2476       O\\nATOM   1777  CG2 THR A1059      39.778  12.440  37.771  1.00108.32           C\\nANISOU 1777  CG2 THR A1059    14955  10292  15912  -2422  -2687   2144       C\\nATOM   1778  N   LYS A1060      38.780   9.709  39.047  1.00 98.18           N\\nANISOU 1778  N   LYS A1060    13229  10001  14072  -1515  -2161   1570       N\\nATOM   1779  CA  LYS A1060      37.721   8.768  38.697  1.00 98.24           C\\nANISOU 1779  CA  LYS A1060    13319  10201  13806  -1182  -1964   1522       C\\nATOM   1780  C   LYS A1060      37.594   8.635  37.188  1.00 99.60           C\\nANISOU 1780  C   LYS A1060    13688  10335  13819  -1346  -1790   1903       C\\nATOM   1781  O   LYS A1060      37.139   7.599  36.688  1.00 95.67           O\\nANISOU 1781  O   LYS A1060    13192  10106  13053  -1183  -1519   1935       O\\nATOM   1782  CB  LYS A1060      36.389   9.207  39.307  1.00 93.38           C\\nANISOU 1782  CB  LYS A1060    12863   9359  13257   -838  -2249   1162       C\\nATOM   1783  N   ASP A1061      37.997   9.671  36.449  1.00103.09           N\\nANISOU 1783  N   ASP A1061    14329  10441  14400  -1703  -1952   2200       N\\nATOM   1784  CA  ASP A1061      38.006   9.603  34.993  1.00101.97           C\\nANISOU 1784  CA  ASP A1061    14414  10301  14028  -1942  -1780   2607       C\\nATOM   1785  C   ASP A1061      39.176   8.768  34.485  1.00100.34           C\\nANISOU 1785  C   ASP A1061    13939  10555  13629  -2196  -1275   2797       C\\nATOM   1786  O   ASP A1061      39.012   7.961  33.563  1.00 99.43           O\\nANISOU 1786  O   ASP A1061    13894  10699  13185  -2180   -958   2926       O\\nATOM   1787  CB  ASP A1061      38.055  11.015  34.413  1.00102.76           C\\nANISOU 1787  CB  ASP A1061    14862   9863  14320  -2281  -2142   2907       C\\nATOM   1788  CG  ASP A1061      37.962  11.029  32.903  1.00102.52           C\\nANISOU 1788  CG  ASP A1061    15156   9822  13974  -2555  -2021   3367       C\\nATOM   1789  OD1 ASP A1061      36.881  10.700  32.371  1.00 98.49           O\\nANISOU 1789  OD1 ASP A1061    14872   9291  13258  -2289  -2114   3362       O\\nATOM   1790  OD2 ASP A1061      38.970  11.374  32.248  1.00105.90           O\\nANISOU 1790  OD2 ASP A1061    15607  10290  14339  -3064  -1832   3728       O\\nATOM   1791  N   GLU A1062      40.362   8.948  35.075  1.00102.50           N\\nANISOU 1791  N   GLU A1062    13880  10945  14119  -2420  -1205   2776       N\\nATOM   1792  CA  GLU A1062      41.504   8.118  34.707  1.00 96.62           C\\nANISOU 1792  CA  GLU A1062    12770  10671  13271  -2592   -725   2880       C\\nATOM   1793  C   GLU A1062      41.237   6.651  35.014  1.00 88.82           C\\nANISOU 1793  C   GLU A1062    11588  10061  12098  -2156   -455   2641       C\\nATOM   1794  O   GLU A1062      41.657   5.764  34.262  1.00 83.40           O\\nANISOU 1794  O   GLU A1062    10776   9705  11208  -2174    -28   2718       O\\nATOM   1795  CB  GLU A1062      42.761   8.595  35.435  1.00 87.02           C\\nANISOU 1795  CB  GLU A1062    11163   9509  12392  -2870   -785   2852       C\\nATOM   1796  CG  GLU A1062      43.240   9.972  35.025  1.00 95.42           C\\nANISOU 1796  CG  GLU A1062    12385  10212  13658  -3416   -988   3136       C\\nATOM   1797  CD  GLU A1062      44.494  10.395  35.768  1.00 99.73           C\\nANISOU 1797  CD  GLU A1062    12491  10838  14563  -3723  -1061   3077       C\\nATOM   1798  OE1 GLU A1062      44.628  10.042  36.959  1.00 95.17           O\\nANISOU 1798  OE1 GLU A1062    11645  10382  14135  -3431  -1231   2743       O\\nATOM   1799  OE2 GLU A1062      45.347  11.075  35.159  1.00104.48           O\\nANISOU 1799  OE2 GLU A1062    13018  11399  15279  -4288   -958   3375       O\\nATOM   1800  N   ALA A1063      40.542   6.377  36.121  1.00 85.45           N\\nANISOU 1800  N   ALA A1063    11151   9581  11735  -1777   -689   2337       N\\nATOM   1801  CA  ALA A1063      40.186   5.003  36.456  1.00 86.64           C\\nANISOU 1801  CA  ALA A1063    11186  10021  11712  -1400   -477   2151       C\\nATOM   1802  C   ALA A1063      39.112   4.459  35.526  1.00 88.99           C\\nANISOU 1802  C   ALA A1063    11790  10309  11715  -1259   -345   2190       C\\nATOM   1803  O   ALA A1063      39.030   3.242  35.325  1.00 88.77           O\\nANISOU 1803  O   ALA A1063    11692  10524  11512  -1068    -60   2120       O\\nATOM   1804  CB  ALA A1063      39.719   4.914  37.909  1.00 84.46           C\\nANISOU 1804  CB  ALA A1063    10850   9716  11524  -1112   -751   1850       C\\nATOM   1805  N   GLU A1064      38.283   5.337  34.957  1.00 91.39           N\\nANISOU 1805  N   GLU A1064    12438  10307  11980  -1346   -590   2294       N\\nATOM   1806  CA  GLU A1064      37.273   4.882  34.009  1.00 91.30           C\\nANISOU 1806  CA  GLU A1064    12709  10296  11686  -1243   -529   2345       C\\nATOM   1807  C   GLU A1064      37.898   4.478  32.678  1.00 95.38           C\\nANISOU 1807  C   GLU A1064    13297  11022  11922  -1504   -156   2596       C\\nATOM   1808  O   GLU A1064      37.402   3.560  32.016  1.00 93.85           O\\nANISOU 1808  O   GLU A1064    13219  10996  11445  -1384     47   2550       O\\nATOM   1809  CB  GLU A1064      36.216   5.969  33.805  1.00 88.36           C\\nANISOU 1809  CB  GLU A1064    12660   9522  11391  -1222   -972   2387       C\\nATOM   1810  CG  GLU A1064      34.995   5.506  33.022  1.00 85.95           C\\nANISOU 1810  CG  GLU A1064    12598   9220  10839  -1054  -1023   2379       C\\nATOM   1811  CD  GLU A1064      33.877   6.532  33.012  1.00 92.64           C\\nANISOU 1811  CD  GLU A1064    13676   9668  11857   -926  -1527   2353       C\\nATOM   1812  OE1 GLU A1064      32.798   6.224  32.460  1.00 92.14           O\\nANISOU 1812  OE1 GLU A1064    13758   9602  11649   -763  -1648   2318       O\\nATOM   1813  OE2 GLU A1064      34.072   7.641  33.555  1.00 96.90           O\\nANISOU 1813  OE2 GLU A1064    14234   9879  12704   -975  -1826   2343       O\\nATOM   1814  N   LYS A1065      38.982   5.144  32.270  1.00 96.04           N\\nANISOU 1814  N   LYS A1065    13309  11119  12064  -1890    -43   2837       N\\nATOM   1815  CA  LYS A1065      39.706   4.695  31.086  1.00 95.76           C\\nANISOU 1815  CA  LYS A1065    13269  11382  11732  -2158    412   3024       C\\nATOM   1816  C   LYS A1065      40.338   3.328  31.321  1.00 92.50           C\\nANISOU 1816  C   LYS A1065    12480  11360  11306  -1927    838   2784       C\\nATOM   1817  O   LYS A1065      40.296   2.460  30.442  1.00 93.15           O\\nANISOU 1817  O   LYS A1065    12640  11673  11077  -1892   1185   2745       O\\nATOM   1818  CB  LYS A1065      40.767   5.724  30.695  1.00 97.00           C\\nANISOU 1818  CB  LYS A1065    13372  11502  11982  -2673    474   3332       C\\nATOM   1819  N   LEU A1066      40.918   3.114  32.505  1.00 86.38           N\\nANISOU 1819  N   LEU A1066    11317  10638  10865  -1755    781   2609       N\\nATOM   1820  CA  LEU A1066      41.504   1.814  32.815  1.00 89.95           C\\nANISOU 1820  CA  LEU A1066    11422  11389  11367  -1482   1095   2400       C\\nATOM   1821  C   LEU A1066      40.439   0.729  32.871  1.00 88.33           C\\nANISOU 1821  C   LEU A1066    11426  11159  10977  -1113   1097   2208       C\\nATOM   1822  O   LEU A1066      40.672  -0.401  32.428  1.00 91.55           O\\nANISOU 1822  O   LEU A1066    11755  11759  11269   -957   1433   2085       O\\nATOM   1823  CB  LEU A1066      42.265   1.875  34.139  1.00 96.43           C\\nANISOU 1823  CB  LEU A1066    11833  12240  12567  -1373    917   2292       C\\nATOM   1824  CG  LEU A1066      43.442   2.845  34.220  1.00110.23           C\\nANISOU 1824  CG  LEU A1066    13274  14038  14572  -1754    899   2439       C\\nATOM   1825  CD1 LEU A1066      44.173   2.679  35.543  1.00109.37           C\\nANISOU 1825  CD1 LEU A1066    12741  14009  14807  -1592    693   2287       C\\nATOM   1826  CD2 LEU A1066      44.392   2.653  33.043  1.00117.21           C\\nANISOU 1826  CD2 LEU A1066    13951  15231  15353  -2035   1407   2560       C\\nATOM   1827  N   PHE A1067      39.266   1.055  33.417  1.00 88.20           N\\nANISOU 1827  N   PHE A1067    11656  10901  10956   -977    731   2152       N\\nATOM   1828  CA  PHE A1067      38.202   0.064  33.527  1.00 86.10           C\\nANISOU 1828  CA  PHE A1067    11554  10620  10539   -687    725   1975       C\\nATOM   1829  C   PHE A1067      37.743  -0.409  32.155  1.00 85.87           C\\nANISOU 1829  C   PHE A1067    11803  10657  10168   -762    941   2008       C\\nATOM   1830  O   PHE A1067      37.513  -1.606  31.949  1.00 84.89           O\\nANISOU 1830  O   PHE A1067    11703  10627   9925   -580   1146   1847       O\\nATOM   1831  CB  PHE A1067      37.028   0.640  34.316  1.00 89.23           C\\nANISOU 1831  CB  PHE A1067    12101  10796  11006   -569    323   1888       C\\nATOM   1832  CG  PHE A1067      35.849  -0.282  34.400  1.00 87.05           C\\nANISOU 1832  CG  PHE A1067    11964  10525  10586   -347    317   1719       C\\nATOM   1833  CD1 PHE A1067      35.865  -1.372  35.252  1.00 83.17           C\\nANISOU 1833  CD1 PHE A1067    11332  10130  10137   -136    418   1574       C\\nATOM   1834  CD2 PHE A1067      34.724  -0.058  33.627  1.00 86.11           C\\nANISOU 1834  CD2 PHE A1067    12115  10304  10299   -373    179   1726       C\\nATOM   1835  CE1 PHE A1067      34.781  -2.221  35.329  1.00 78.20           C\\nANISOU 1835  CE1 PHE A1067    10832   9493   9387     -3    424   1440       C\\nATOM   1836  CE2 PHE A1067      33.638  -0.903  33.702  1.00 81.95           C\\nANISOU 1836  CE2 PHE A1067    11664   9800   9671   -214    168   1558       C\\nATOM   1837  CZ  PHE A1067      33.666  -1.985  34.553  1.00 78.15           C\\nANISOU 1837  CZ  PHE A1067    11043   9414   9235    -52    312   1415       C\\nATOM   1838  N   ASN A1068      37.604   0.516  31.201  1.00 90.24           N\\nANISOU 1838  N   ASN A1068    12604  11140  10543  -1046    869   2222       N\\nATOM   1839  CA  ASN A1068      37.203   0.127  29.853  1.00 83.46           C\\nANISOU 1839  CA  ASN A1068    12053  10378   9278  -1159   1045   2269       C\\nATOM   1840  C   ASN A1068      38.222  -0.816  29.228  1.00 82.78           C\\nANISOU 1840  C   ASN A1068    11803  10602   9046  -1191   1575   2173       C\\nATOM   1841  O   ASN A1068      37.856  -1.728  28.479  1.00 84.94           O\\nANISOU 1841  O   ASN A1068    12255  10985   9033  -1118   1777   2024       O\\nATOM   1842  CB  ASN A1068      37.008   1.367  28.984  1.00 87.76           C\\nANISOU 1842  CB  ASN A1068    12920  10786   9638  -1498    837   2587       C\\nATOM   1843  CG  ASN A1068      35.631   1.982  29.145  1.00 95.27           C\\nANISOU 1843  CG  ASN A1068    14135  11430  10632  -1379    315   2609       C\\nATOM   1844  OD1 ASN A1068      34.845   2.027  28.198  1.00102.99           O\\nANISOU 1844  OD1 ASN A1068    15454  12372  11305  -1446    169   2702       O\\nATOM   1845  ND2 ASN A1068      35.327   2.448  30.350  1.00 94.72           N\\nANISOU 1845  ND2 ASN A1068    13890  11159  10939  -1190     20   2495       N\\nATOM   1846  N   GLN A1069      39.507  -0.618  29.532  1.00 82.90           N\\nANISOU 1846  N   GLN A1069    11450  10766   9281  -1289   1799   2217       N\\nATOM   1847  CA  GLN A1069      40.533  -1.532  29.041  1.00 93.96           C\\nANISOU 1847  CA  GLN A1069    12588  12479  10633  -1250   2317   2059       C\\nATOM   1848  C   GLN A1069      40.355  -2.926  29.631  1.00 96.67           C\\nANISOU 1848  C   GLN A1069    12801  12800  11129   -811   2383   1749       C\\nATOM   1849  O   GLN A1069      40.472  -3.931  28.918  1.00 96.30           O\\nANISOU 1849  O   GLN A1069    12800  12887  10901   -697   2721   1539       O\\nATOM   1850  CB  GLN A1069      41.922  -0.978  29.364  1.00104.31           C\\nANISOU 1850  CB  GLN A1069    13439  13961  12234  -1436   2488   2158       C\\nATOM   1851  CG  GLN A1069      42.191   0.399  28.770  1.00112.15           C\\nANISOU 1851  CG  GLN A1069    14573  14942  13096  -1947   2442   2503       C\\nATOM   1852  CD  GLN A1069      43.505   1.002  29.237  1.00116.78           C\\nANISOU 1852  CD  GLN A1069    14664  15667  14039  -2175   2548   2595       C\\nATOM   1853  OE1 GLN A1069      44.350   0.314  29.812  1.00124.86           O\\nANISOU 1853  OE1 GLN A1069    15191  16882  15370  -1946   2730   2385       O\\nATOM   1854  NE2 GLN A1069      43.681   2.297  28.993  1.00109.98           N\\nANISOU 1854  NE2 GLN A1069    13937  14684  13167  -2636   2395   2919       N\\nATOM   1855  N   ASP A1070      40.068  -3.007  30.934  1.00 93.20           N\\nANISOU 1855  N   ASP A1070    12231  12176  11004   -577   2056   1715       N\\nATOM   1856  CA  ASP A1070      39.831  -4.304  31.560  1.00 92.78           C\\nANISOU 1856  CA  ASP A1070    12121  12049  11083   -206   2064   1494       C\\nATOM   1857  C   ASP A1070      38.580  -4.968  31.000  1.00 84.10           C\\nANISOU 1857  C   ASP A1070    11427  10832   9697   -148   2030   1376       C\\nATOM   1858  O   ASP A1070      38.532  -6.195  30.858  1.00 74.28           O\\nANISOU 1858  O   ASP A1070    10218   9558   8448     64   2204   1167       O\\nATOM   1859  CB  ASP A1070      39.714  -4.145  33.076  1.00 97.16           C\\nANISOU 1859  CB  ASP A1070    12517  12464  11936    -46   1705   1529       C\\nATOM   1860  CG  ASP A1070      40.993  -3.637  33.711  1.00101.50           C\\nANISOU 1860  CG  ASP A1070    12635  13134  12794    -83   1688   1606       C\\nATOM   1861  OD1 ASP A1070      42.082  -3.940  33.181  1.00105.37           O\\nANISOU 1861  OD1 ASP A1070    12832  13826  13379    -89   2015   1558       O\\nATOM   1862  OD2 ASP A1070      40.905  -2.936  34.743  1.00 98.07           O\\nANISOU 1862  OD2 ASP A1070    12136  12614  12514   -110   1349   1680       O\\nATOM   1863  N   VAL A1071      37.557  -4.174  30.679  1.00 85.78           N\\nANISOU 1863  N   VAL A1071    11939  10950   9704   -328   1771   1495       N\\nATOM   1864  CA  VAL A1071      36.322  -4.733  30.136  1.00 82.23           C\\nANISOU 1864  CA  VAL A1071    11829  10413   9002   -301   1681   1379       C\\nATOM   1865  C   VAL A1071      36.565  -5.310  28.749  1.00 86.97           C\\nANISOU 1865  C   VAL A1071    12623  11169   9251   -401   2023   1266       C\\nATOM   1866  O   VAL A1071      36.169  -6.443  28.455  1.00 91.66           O\\nANISOU 1866  O   VAL A1071    13352  11723   9752   -267   2137   1029       O\\nATOM   1867  CB  VAL A1071      35.214  -3.667  30.113  1.00 77.64           C\\nANISOU 1867  CB  VAL A1071    11459   9702   8338   -435   1276   1525       C\\nATOM   1868  CG1 VAL A1071      34.018  -4.169  29.323  1.00 68.20           C\\nANISOU 1868  CG1 VAL A1071    10579   8473   6862   -455   1173   1415       C\\nATOM   1869  CG2 VAL A1071      34.807  -3.308  31.524  1.00 79.71           C\\nANISOU 1869  CG2 VAL A1071    11544   9829   8913   -289    982   1517       C\\nATOM   1870  N   ASP A1072      37.208  -4.533  27.872  1.00 86.89           N\\nANISOU 1870  N   ASP A1072    12656  11340   9019   -672   2197   1425       N\\nATOM   1871  CA  ASP A1072      37.548  -5.045  26.549  1.00 93.69           C\\nANISOU 1871  CA  ASP A1072    13699  12426   9474   -799   2587   1294       C\\nATOM   1872  C   ASP A1072      38.419  -6.289  26.649  1.00 93.29           C\\nANISOU 1872  C   ASP A1072    13380  12470   9598   -530   3002    969       C\\nATOM   1873  O   ASP A1072      38.186  -7.273  25.940  1.00100.45           O\\nANISOU 1873  O   ASP A1072    14485  13404  10277   -445   3208    683       O\\nATOM   1874  CB  ASP A1072      38.246  -3.964  25.724  1.00101.72           C\\nANISOU 1874  CB  ASP A1072    14764  13660  10224  -1186   2755   1563       C\\nATOM   1875  CG  ASP A1072      37.274  -2.951  25.152  1.00105.64           C\\nANISOU 1875  CG  ASP A1072    15691  14039  10407  -1457   2355   1858       C\\nATOM   1876  OD1 ASP A1072      36.104  -3.321  24.911  1.00105.43           O\\nANISOU 1876  OD1 ASP A1072    15959  13888  10212  -1367   2080   1761       O\\nATOM   1877  OD2 ASP A1072      37.677  -1.787  24.942  1.00108.66           O\\nANISOU 1877  OD2 ASP A1072    16112  14434  10740  -1764   2286   2192       O\\nATOM   1878  N   ALA A1073      39.417  -6.269  27.537  1.00 84.98           N\\nANISOU 1878  N   ALA A1073    11874  11440   8973   -376   3089    988       N\\nATOM   1879  CA  ALA A1073      40.250  -7.451  27.738  1.00 87.42           C\\nANISOU 1879  CA  ALA A1073    11887  11783   9546    -46   3401    685       C\\nATOM   1880  C   ALA A1073      39.418  -8.640  28.199  1.00 88.42           C\\nANISOU 1880  C   ALA A1073    12207  11603   9787    254   3220    480       C\\nATOM   1881  O   ALA A1073      39.645  -9.774  27.760  1.00 91.45           O\\nANISOU 1881  O   ALA A1073    12623  11947  10175    465   3482    159       O\\nATOM   1882  CB  ALA A1073      41.357  -7.149  28.747  1.00 88.38           C\\nANISOU 1882  CB  ALA A1073    11477  11958  10146     77   3385    785       C\\nATOM   1883  N   ALA A1074      38.441  -8.397  29.079  1.00 83.01           N\\nANISOU 1883  N   ALA A1074    11651  10689   9199    259   2785    645       N\\nATOM   1884  CA  ALA A1074      37.590  -9.476  29.567  1.00 85.44           C\\nANISOU 1884  CA  ALA A1074    12143  10714   9605    456   2615    500       C\\nATOM   1885  C   ALA A1074      36.749 -10.084  28.454  1.00 93.89           C\\nANISOU 1885  C   ALA A1074    13614  11749  10313    356   2695    279       C\\nATOM   1886  O   ALA A1074      36.388 -11.263  28.528  1.00 97.64           O\\nANISOU 1886  O   ALA A1074    14228  11998  10874    520   2705     57       O\\nATOM   1887  CB  ALA A1074      36.686  -8.968  30.689  1.00 78.28           C\\nANISOU 1887  CB  ALA A1074    11263   9662   8819    417   2191    709       C\\nATOM   1888  N   VAL A1075      36.430  -9.305  27.419  1.00 95.22           N\\nANISOU 1888  N   VAL A1075    13998  12114  10069     70   2718    348       N\\nATOM   1889  CA  VAL A1075      35.614  -9.821  26.325  1.00 92.66           C\\nANISOU 1889  CA  VAL A1075    14075  11790   9341    -54   2737    139       C\\nATOM   1890  C   VAL A1075      36.457 -10.646  25.357  1.00100.97           C\\nANISOU 1890  C   VAL A1075    15170  12983  10213     22   3217   -207       C\\nATOM   1891  O   VAL A1075      35.987 -11.658  24.824  1.00101.40           O\\nANISOU 1891  O   VAL A1075    15489  12912  10125     79   3272   -531       O\\nATOM   1892  CB  VAL A1075      34.888  -8.661  25.617  1.00 82.73           C\\nANISOU 1892  CB  VAL A1075    13071  10672   7689   -380   2491    377       C\\nATOM   1893  CG1 VAL A1075      34.069  -9.171  24.446  1.00 75.94           C\\nANISOU 1893  CG1 VAL A1075    12635   9852   6368   -528   2457    166       C\\nATOM   1894  CG2 VAL A1075      33.993  -7.930  26.604  1.00 76.88           C\\nANISOU 1894  CG2 VAL A1075    12256   9765   7192   -384   2023    620       C\\nATOM   1895  N   ARG A1076      37.712 -10.240  25.115  1.00100.09           N\\nANISOU 1895  N   ARG A1076    14776  13139  10116     17   3583   -182       N\\nATOM   1896  CA  ARG A1076      38.592 -11.049  24.273  1.00106.02           C\\nANISOU 1896  CA  ARG A1076    15475  14062  10744    139   4103   -579       C\\nATOM   1897  C   ARG A1076      38.740 -12.458  24.828  1.00110.21           C\\nANISOU 1897  C   ARG A1076    15911  14258  11706    564   4141   -922       C\\nATOM   1898  O   ARG A1076      38.867 -13.421  24.062  1.00118.72           O\\nANISOU 1898  O   ARG A1076    17153  15310  12647    690   4425  -1359       O\\nATOM   1899  CB  ARG A1076      39.980 -10.411  24.143  1.00109.75           C\\nANISOU 1899  CB  ARG A1076    15519  14893  11289     84   4503   -500       C\\nATOM   1900  CG  ARG A1076      40.027  -8.904  24.227  1.00109.02           C\\nANISOU 1900  CG  ARG A1076    15378  14979  11066   -286   4338    -22       C\\nATOM   1901  CD  ARG A1076      39.706  -8.229  22.910  1.00113.54           C\\nANISOU 1901  CD  ARG A1076    16360  15831  10947   -724   4457     91       C\\nATOM   1902  NE  ARG A1076      39.657  -6.778  23.063  1.00113.48           N\\nANISOU 1902  NE  ARG A1076    16365  15872  10879  -1069   4203    591       N\\nATOM   1903  CZ  ARG A1076      39.507  -5.923  22.058  1.00114.12           C\\nANISOU 1903  CZ  ARG A1076    16787  16166  10409  -1503   4233    842       C\\nATOM   1904  NH1 ARG A1076      39.395  -6.367  20.812  1.00118.70           N\\nANISOU 1904  NH1 ARG A1076    17722  16997  10383  -1663   4528    629       N\\nATOM   1905  NH2 ARG A1076      39.471  -4.619  22.301  1.00110.17           N\\nANISOU 1905  NH2 ARG A1076    16305  15605   9949  -1786   3945   1307       N\\nATOM   1906  N   GLY A1077      38.727 -12.597  26.152  1.00104.33           N\\nANISOU 1906  N   GLY A1077    14938  13235  11468    780   3843   -732       N\\nATOM   1907  CA  GLY A1077      38.862 -13.893  26.781  1.00103.24           C\\nANISOU 1907  CA  GLY A1077    14749  12715  11761   1164   3801   -960       C\\nATOM   1908  C   GLY A1077      37.555 -14.652  26.832  1.00100.52           C\\nANISOU 1908  C   GLY A1077    14844  12012  11338   1106   3509  -1046       C\\nATOM   1909  O   GLY A1077      37.538 -15.875  26.663  1.00104.59           O\\nANISOU 1909  O   GLY A1077    15516  12220  12003   1321   3586  -1382       O\\nATOM   1910  N   ILE A1078      36.453 -13.936  27.070  1.00 99.32           N\\nANISOU 1910  N   ILE A1078    14869  11880  10988    814   3165   -762       N\\nATOM   1911  CA  ILE A1078      35.138 -14.573  27.087  1.00 95.36           C\\nANISOU 1911  CA  ILE A1078    14721  11103  10410    692   2887   -841       C\\nATOM   1912  C   ILE A1078      34.872 -15.266  25.758  1.00 94.23           C\\nANISOU 1912  C   ILE A1078    14931  10962   9909    611   3076  -1259       C\\nATOM   1913  O   ILE A1078      34.461 -16.432  25.713  1.00 91.07           O\\nANISOU 1913  O   ILE A1078    14757  10213   9633    693   3032  -1537       O\\nATOM   1914  CB  ILE A1078      34.042 -13.542  27.412  1.00 93.90           C\\nANISOU 1914  CB  ILE A1078    14585  11030  10063    404   2522   -518       C\\nATOM   1915  CG1 ILE A1078      33.993 -13.263  28.917  1.00 93.60           C\\nANISOU 1915  CG1 ILE A1078    14291  10873  10400    497   2289   -213       C\\nATOM   1916  CG2 ILE A1078      32.692 -14.024  26.911  1.00 91.88           C\\nANISOU 1916  CG2 ILE A1078    14674  10646   9590    192   2300   -673       C\\nATOM   1917  CD1 ILE A1078      33.002 -12.183  29.313  1.00 86.14           C\\nANISOU 1917  CD1 ILE A1078    13326  10053   9351    273   1966     41       C\\nATOM   1918  N   LEU A1079      35.121 -14.560  24.654  1.00 96.21           N\\nANISOU 1918  N   LEU A1079    15266  11598   9690    421   3283  -1311       N\\nATOM   1919  CA  LEU A1079      34.910 -15.148  23.339  1.00 99.06           C\\nANISOU 1919  CA  LEU A1079    15997  12035   9608    315   3475  -1730       C\\nATOM   1920  C   LEU A1079      35.911 -16.261  23.058  1.00104.43           C\\nANISOU 1920  C   LEU A1079    16609  12586  10483    653   3898  -2204       C\\nATOM   1921  O   LEU A1079      35.576 -17.237  22.375  1.00107.18           O\\nANISOU 1921  O   LEU A1079    17287  12752  10686    675   3966  -2650       O\\nATOM   1922  CB  LEU A1079      34.990 -14.061  22.271  1.00 97.08           C\\nANISOU 1922  CB  LEU A1079    15879  12261   8747     -2   3592  -1606       C\\nATOM   1923  CG  LEU A1079      34.022 -12.896  22.494  1.00 92.62           C\\nANISOU 1923  CG  LEU A1079    15381  11775   8035   -286   3126  -1146       C\\nATOM   1924  CD1 LEU A1079      34.208 -11.832  21.427  1.00 87.85           C\\nANISOU 1924  CD1 LEU A1079    14956  11583   6838   -599   3216   -967       C\\nATOM   1925  CD2 LEU A1079      32.586 -13.395  22.521  1.00 89.61           C\\nANISOU 1925  CD2 LEU A1079    15271  11148   7628   -399   2691  -1233       C\\nATOM   1926  N   ARG A1080      37.134 -16.141  23.574  1.00102.78           N\\nANISOU 1926  N   ARG A1080    15961  12455  10635    932   4161  -2150       N\\nATOM   1927  CA  ARG A1080      38.113 -17.215  23.463  1.00106.42           C\\nANISOU 1927  CA  ARG A1080    16265  12749  11422   1346   4516  -2607       C\\nATOM   1928  C   ARG A1080      37.864 -18.345  24.454  1.00114.00           C\\nANISOU 1928  C   ARG A1080    17260  13084  12971   1658   4225  -2653       C\\nATOM   1929  O   ARG A1080      38.585 -19.348  24.417  1.00121.35           O\\nANISOU 1929  O   ARG A1080    18104  13749  14255   2055   4430  -3041       O\\nATOM   1930  CB  ARG A1080      39.528 -16.662  23.652  1.00 95.46           C\\nANISOU 1930  CB  ARG A1080    14320  11699  10249   1534   4874  -2535       C\\nATOM   1931  N   ASN A1081      36.877 -18.203  25.339  1.00113.30           N\\nANISOU 1931  N   ASN A1081    17292  12754  13003   1487   3760  -2268       N\\nATOM   1932  CA  ASN A1081      36.488 -19.263  26.264  1.00110.82           C\\nANISOU 1932  CA  ASN A1081    17098  11850  13160   1666   3466  -2242       C\\nATOM   1933  C   ASN A1081      35.348 -20.052  25.630  1.00107.85           C\\nANISOU 1933  C   ASN A1081    17225  11189  12565   1437   3324  -2533       C\\nATOM   1934  O   ASN A1081      34.255 -19.516  25.418  1.00 96.74           O\\nANISOU 1934  O   ASN A1081    16004   9943  10809   1044   3098  -2372       O\\nATOM   1935  CB  ASN A1081      36.075 -18.682  27.614  1.00104.89           C\\nANISOU 1935  CB  ASN A1081    16179  11052  12621   1564   3094  -1681       C\\nATOM   1936  CG  ASN A1081      35.935 -19.745  28.696  1.00100.82           C\\nANISOU 1936  CG  ASN A1081    15751   9964  12593   1757   2830  -1573       C\\nATOM   1937  OD1 ASN A1081      35.536 -20.881  28.430  1.00 96.54           O\\nANISOU 1937  OD1 ASN A1081    15540   8975  12166   1793   2783  -1851       O\\nATOM   1938  ND2 ASN A1081      36.265 -19.375  29.927  1.00 99.41           N\\nANISOU 1938  ND2 ASN A1081    15308   9782  12683   1855   2634  -1158       N\\nATOM   1939  N   ALA A1082      35.603 -21.330  25.335  1.00104.72           N\\nANISOU 1939  N   ALA A1082    17030  10346  12412   1693   3425  -2982       N\\nATOM   1940  CA  ALA A1082      34.620 -22.148  24.633  1.00104.56           C\\nANISOU 1940  CA  ALA A1082    17500  10033  12195   1466   3305  -3342       C\\nATOM   1941  C   ALA A1082      33.348 -22.360  25.442  1.00101.54           C\\nANISOU 1941  C   ALA A1082    17302   9334  11945   1142   2845  -3001       C\\nATOM   1942  O   ALA A1082      32.300 -22.654  24.856  1.00101.98           O\\nANISOU 1942  O   ALA A1082    17693   9314  11739    801   2679  -3190       O\\nATOM   1943  CB  ALA A1082      35.231 -23.499  24.264  1.00107.82           C\\nANISOU 1943  CB  ALA A1082    18086   9944  12935   1850   3489  -3914       C\\nATOM   1944  N   LYS A1083      33.409 -22.219  26.764  1.00105.02           N\\nANISOU 1944  N   LYS A1083    17519   9623  12760   1215   2642  -2520       N\\nATOM   1945  CA  LYS A1083      32.243 -22.435  27.607  1.00 99.72           C\\nANISOU 1945  CA  LYS A1083    16986   8701  12202    885   2273  -2194       C\\nATOM   1946  C   LYS A1083      31.446 -21.163  27.871  1.00 97.98           C\\nANISOU 1946  C   LYS A1083    16574   8985  11668    541   2119  -1821       C\\nATOM   1947  O   LYS A1083      30.317 -21.253  28.366  1.00 96.09           O\\nANISOU 1947  O   LYS A1083    16414   8652  11442    209   1857  -1636       O\\nATOM   1948  CB  LYS A1083      32.666 -23.061  28.941  1.00 98.15           C\\nANISOU 1948  CB  LYS A1083    16717   8046  12528   1114   2120  -1873       C\\nATOM   1949  N   LEU A1084      31.992 -19.986  27.551  1.00 99.46           N\\nANISOU 1949  N   LEU A1084    16502   9689  11600    605   2275  -1719       N\\nATOM   1950  CA  LEU A1084      31.288 -18.729  27.771  1.00 97.55           C\\nANISOU 1950  CA  LEU A1084    16090   9867  11109    333   2100  -1390       C\\nATOM   1951  C   LEU A1084      30.919 -17.993  26.491  1.00101.44           C\\nANISOU 1951  C   LEU A1084    16699  10753  11090    121   2131  -1554       C\\nATOM   1952  O   LEU A1084      30.009 -17.161  26.521  1.00102.09           O\\nANISOU 1952  O   LEU A1084    16730  11072  10987   -136   1884  -1351       O\\nATOM   1953  CB  LEU A1084      32.124 -17.790  28.654  1.00 93.67           C\\nANISOU 1953  CB  LEU A1084    15216   9609  10766    522   2147  -1024       C\\nATOM   1954  CG  LEU A1084      32.376 -18.250  30.092  1.00 99.39           C\\nANISOU 1954  CG  LEU A1084    15814  10040  11911    678   2020   -744       C\\nATOM   1955  CD1 LEU A1084      33.068 -17.160  30.896  1.00100.96           C\\nANISOU 1955  CD1 LEU A1084    15645  10540  12174    797   2010   -411       C\\nATOM   1956  CD2 LEU A1084      31.075 -18.668  30.757  1.00 98.30           C\\nANISOU 1956  CD2 LEU A1084    15830   9700  11820    371   1756   -602       C\\nATOM   1957  N   LYS A1085      31.598 -18.269  25.378  1.00102.45           N\\nANISOU 1957  N   LYS A1085    16983  10965  10978    227   2417  -1917       N\\nATOM   1958  CA  LYS A1085      31.262 -17.597  24.126  1.00 99.55           C\\nANISOU 1958  CA  LYS A1085    16799  10990  10037    -13   2431  -2041       C\\nATOM   1959  C   LYS A1085      29.850 -17.899  23.627  1.00 99.81           C\\nANISOU 1959  C   LYS A1085    17128  10950   9847   -354   2083  -2182       C\\nATOM   1960  O   LYS A1085      29.193 -16.966  23.138  1.00 92.79           O\\nANISOU 1960  O   LYS A1085    16268  10388   8598   -594   1861  -2023       O\\nATOM   1961  CB  LYS A1085      32.301 -17.947  23.053  1.00 96.22           C\\nANISOU 1961  CB  LYS A1085    16501  10703   9355    149   2870  -2453       C\\nATOM   1962  N   PRO A1086      29.335 -19.137  23.693  1.00105.32           N\\nANISOU 1962  N   PRO A1086    18044  11220  10751   -402   1987  -2468       N\\nATOM   1963  CA  PRO A1086      27.961 -19.366  23.201  1.00106.72           C\\nANISOU 1963  CA  PRO A1086    18449  11373  10729   -778   1625  -2606       C\\nATOM   1964  C   PRO A1086      26.904 -18.527  23.902  1.00101.72           C\\nANISOU 1964  C   PRO A1086    17551  10915  10184  -1000   1260  -2201       C\\nATOM   1965  O   PRO A1086      26.130 -17.830  23.232  1.00 97.88           O\\nANISOU 1965  O   PRO A1086    17104  10733   9353  -1226    992  -2175       O\\nATOM   1966  CB  PRO A1086      27.759 -20.868  23.445  1.00108.18           C\\nANISOU 1966  CB  PRO A1086    18857  10979  11267   -780   1611  -2917       C\\nATOM   1967  CG  PRO A1086      29.125 -21.438  23.364  1.00108.60           C\\nANISOU 1967  CG  PRO A1086    18951  10834  11479   -369   2012  -3150       C\\nATOM   1968  CD  PRO A1086      30.018 -20.411  23.991  1.00103.81           C\\nANISOU 1968  CD  PRO A1086    17951  10542  10950   -127   2192  -2744       C\\nATOM   1969  N   VAL A1087      26.844 -18.575  25.235  1.00 98.45           N\\nANISOU 1969  N   VAL A1087    16867  10324  10214   -932   1231  -1899       N\\nATOM   1970  CA  VAL A1087      25.825 -17.817  25.956  1.00 96.16           C\\nANISOU 1970  CA  VAL A1087    16290  10223  10024  -1125    937  -1588       C\\nATOM   1971  C   VAL A1087      26.024 -16.321  25.749  1.00 94.05           C\\nANISOU 1971  C   VAL A1087    15830  10386   9517  -1049    881  -1337       C\\nATOM   1972  O   VAL A1087      25.055 -15.564  25.617  1.00 93.16           O\\nANISOU 1972  O   VAL A1087    15592  10501   9302  -1221    565  -1236       O\\nATOM   1973  CB  VAL A1087      25.834 -18.196  27.449  1.00 97.74           C\\nANISOU 1973  CB  VAL A1087    16281  10182  10673  -1078    978  -1328       C\\nATOM   1974  CG1 VAL A1087      27.238 -18.088  28.024  1.00102.40           C\\nANISOU 1974  CG1 VAL A1087    16780  10706  11420   -706   1259  -1166       C\\nATOM   1975  CG2 VAL A1087      24.863 -17.323  28.230  1.00 89.97           C\\nANISOU 1975  CG2 VAL A1087    14954   9465   9765  -1245    754  -1058       C\\nATOM   1976  N   TYR A1088      27.284 -15.876  25.692  1.00 89.69           N\\nANISOU 1976  N   TYR A1088    15242   9934   8902   -793   1168  -1242       N\\nATOM   1977  CA  TYR A1088      27.580 -14.457  25.515  1.00 90.57           C\\nANISOU 1977  CA  TYR A1088    15204  10393   8813   -755   1125   -975       C\\nATOM   1978  C   TYR A1088      26.959 -13.916  24.234  1.00 95.61           C\\nANISOU 1978  C   TYR A1088    16073  11277   8976   -968    892  -1053       C\\nATOM   1979  O   TYR A1088      26.470 -12.781  24.202  1.00 93.98           O\\nANISOU 1979  O   TYR A1088    15753  11275   8682  -1035    611   -805       O\\nATOM   1980  CB  TYR A1088      29.095 -14.250  25.512  1.00 93.94           C\\nANISOU 1980  CB  TYR A1088    15566  10885   9242   -509   1510   -919       C\\nATOM   1981  CG  TYR A1088      29.544 -12.810  25.574  1.00 98.44           C\\nANISOU 1981  CG  TYR A1088    15953  11742   9710   -493   1488   -591       C\\nATOM   1982  CD1 TYR A1088      29.740 -12.178  26.794  1.00 98.86           C\\nANISOU 1982  CD1 TYR A1088    15682  11781  10099   -378   1424   -304       C\\nATOM   1983  CD2 TYR A1088      29.792 -12.088  24.415  1.00103.73           C\\nANISOU 1983  CD2 TYR A1088    16808  12681   9923   -622   1523   -565       C\\nATOM   1984  CE1 TYR A1088      30.162 -10.863  26.860  1.00 99.84           C\\nANISOU 1984  CE1 TYR A1088    15661  12107  10167   -380   1378    -29       C\\nATOM   1985  CE2 TYR A1088      30.213 -10.771  24.470  1.00106.12           C\\nANISOU 1985  CE2 TYR A1088    16981  13181  10158   -650   1482   -232       C\\nATOM   1986  CZ  TYR A1088      30.395 -10.164  25.696  1.00103.83           C\\nANISOU 1986  CZ  TYR A1088    16357  12826  10268   -522   1402     20       C\\nATOM   1987  OH  TYR A1088      30.810  -8.854  25.759  1.00103.35           O\\nANISOU 1987  OH  TYR A1088    16189  12904  10176   -568   1333    326       O\\nATOM   1988  N   ASP A1089      26.969 -14.714  23.164  1.00102.12           N\\nANISOU 1988  N   ASP A1089    17248  12069   9485  -1067    973  -1406       N\\nATOM   1989  CA  ASP A1089      26.320 -14.293  21.927  1.00102.51           C\\nANISOU 1989  CA  ASP A1089    17573  12361   9018  -1301    696  -1486       C\\nATOM   1990  C   ASP A1089      24.810 -14.185  22.110  1.00 97.68           C\\nANISOU 1990  C   ASP A1089    16847  11734   8531  -1503    175  -1453       C\\nATOM   1991  O   ASP A1089      24.193 -13.208  21.669  1.00 94.27           O\\nANISOU 1991  O   ASP A1089    16405  11528   7886  -1603   -198  -1266       O\\nATOM   1992  CB  ASP A1089      26.658 -15.270  20.798  1.00107.75           C\\nANISOU 1992  CB  ASP A1089    18652  12996   9292  -1371    911  -1943       C\\nATOM   1993  CG  ASP A1089      28.153 -15.360  20.522  1.00109.36           C\\nANISOU 1993  CG  ASP A1089    18906  13282   9365  -1158   1468  -2039       C\\nATOM   1994  OD1 ASP A1089      28.859 -14.349  20.724  1.00107.83           O\\nANISOU 1994  OD1 ASP A1089    18522  13306   9142  -1077   1610  -1702       O\\nATOM   1995  OD2 ASP A1089      28.623 -16.442  20.104  1.00108.54           O\\nANISOU 1995  OD2 ASP A1089    19006  13016   9217  -1074   1762  -2478       O\\nATOM   1996  N   SER A1090      24.200 -15.124  22.768  1.00 95.52           N\\nANISOU 1996  N   SER A1090    16469  11190   8635  -1571    131  -1622       N\\nATOM   1997  CA  SER A1090      22.775 -15.087  22.914  1.00100.79           C\\nANISOU 1997  CA  SER A1090    16964  11869   9463  -1805   -311  -1652       C\\nATOM   1998  C   SER A1090      22.220 -13.982  23.739  1.00102.57           C\\nANISOU 1998  C   SER A1090    16755  12269   9949  -1733   -541  -1311       C\\nATOM   1999  O   SER A1090      21.034 -13.763  23.747  1.00106.04           O\\nANISOU 1999  O   SER A1090    16983  12810  10497  -1894   -938  -1340       O\\nATOM   2000  CB  SER A1090      22.377 -16.406  23.588  1.00 99.01           C\\nANISOU 2000  CB  SER A1090    16709  11296   9615  -1937   -227  -1860       C\\nATOM   2001  OG  SER A1090      21.208 -16.357  24.395  1.00 95.53           O\\nANISOU 2001  OG  SER A1090    15874  10901   9522  -2092   -478  -1730       O\\nATOM   2002  N   LEU A1091      23.062 -13.325  24.481  1.00 99.87           N\\nANISOU 2002  N   LEU A1091    16250  11965   9730  -1492   -315  -1031       N\\nATOM   2003  CA  LEU A1091      22.607 -12.416  25.517  1.00 95.87           C\\nANISOU 2003  CA  LEU A1091    15324  11551   9550  -1398   -463   -783       C\\nATOM   2004  C   LEU A1091      22.327 -11.026  24.968  1.00 97.76           C\\nANISOU 2004  C   LEU A1091    15525  12007   9612  -1342   -816   -587       C\\nATOM   2005  O   LEU A1091      23.032 -10.535  24.083  1.00 95.64           O\\nANISOU 2005  O   LEU A1091    15549  11818   8971  -1317   -786   -485       O\\nATOM   2006  CB  LEU A1091      23.641 -12.333  26.638  1.00 87.84           C\\nANISOU 2006  CB  LEU A1091    14159  10436   8780  -1181    -92   -597       C\\nATOM   2007  CG  LEU A1091      23.680 -13.560  27.542  1.00 82.06           C\\nANISOU 2007  CG  LEU A1091    13386   9458   8336  -1224    143   -690       C\\nATOM   2008  CD1 LEU A1091      24.786 -13.425  28.573  1.00 80.82           C\\nANISOU 2008  CD1 LEU A1091    13114   9224   8371   -989    440   -482       C\\nATOM   2009  CD2 LEU A1091      22.327 -13.769  28.206  1.00 80.36           C\\nANISOU 2009  CD2 LEU A1091    12890   9277   8367  -1435    -70   -736       C\\nATOM   2010  N   ASP A1092      21.376 -10.343  25.562  1.00 96.05           N\\nANISOU 2010  N   ASP A1092    14944  11880   9672  -1329  -1151   -538       N\\nATOM   2011  CA  ASP A1092      21.052  -8.988  25.248  1.00 94.58           C\\nANISOU 2011  CA  ASP A1092    14656  11809   9469  -1194  -1512   -321       C\\nATOM   2012  C   ASP A1092      22.222  -8.197  25.771  1.00 90.97           C\\nANISOU 2012  C   ASP A1092    14182  11304   9080   -989  -1249    -61       C\\nATOM   2013  O   ASP A1092      22.961  -8.670  26.567  1.00 94.84           O\\nANISOU 2013  O   ASP A1092    14566  11715   9754   -916   -857    -59       O\\nATOM   2014  CB  ASP A1092      19.780  -8.669  26.007  1.00101.30           C\\nANISOU 2014  CB  ASP A1092    15029  12751  10711  -1166  -1868   -406       C\\nATOM   2015  CG  ASP A1092      19.607  -7.210  26.318  1.00111.33           C\\nANISOU 2015  CG  ASP A1092    16080  14045  12176   -914  -2131   -205       C\\nATOM   2016  OD1 ASP A1092      20.277  -6.361  25.708  1.00117.45           O\\nANISOU 2016  OD1 ASP A1092    17125  14798  12702   -861  -2417     -1       O\\nATOM   2017  OD2 ASP A1092      18.756  -6.904  27.171  1.00112.11           O\\nANISOU 2017  OD2 ASP A1092    15757  14174  12666   -784  -2057   -258       O\\nATOM   2018  N   ALA A1093      22.381  -6.966  25.331  1.00 96.88           N\\nANISOU 2018  N   ALA A1093    15054  12081   9674   -916  -1505    178       N\\nATOM   2019  CA  ALA A1093      23.488  -6.122  25.778  1.00 91.46           C\\nANISOU 2019  CA  ALA A1093    14374  11336   9042   -782  -1292    431       C\\nATOM   2020  C   ALA A1093      23.421  -5.832  27.272  1.00 93.10           C\\nANISOU 2020  C   ALA A1093    14165  11492   9718   -603  -1188    414       C\\nATOM   2021  O   ALA A1093      24.464  -5.712  27.927  1.00 87.73           O\\nANISOU 2021  O   ALA A1093    13451  10765   9118   -524   -866    519       O\\nATOM   2022  CB  ALA A1093      23.503  -4.814  24.988  1.00 88.70           C\\nANISOU 2022  CB  ALA A1093    14227  10970   8505   -779  -1676    717       C\\nATOM   2023  N   VAL A1094      22.214  -5.720  27.829  1.00 97.94           N\\nANISOU 2023  N   VAL A1094    14439  12147  10627   -546  -1450    262       N\\nATOM   2024  CA  VAL A1094      22.076  -5.445  29.257  1.00 93.00           C\\nANISOU 2024  CA  VAL A1094    13427  11531  10378   -399  -1324    200       C\\nATOM   2025  C   VAL A1094      22.441  -6.680  30.072  1.00 88.59           C\\nANISOU 2025  C   VAL A1094    12819  10982   9860   -491   -879     98       C\\nATOM   2026  O   VAL A1094      23.204  -6.601  31.041  1.00 83.02           O\\nANISOU 2026  O   VAL A1094    12036  10247   9261   -400   -616    175       O\\nATOM   2027  CB  VAL A1094      20.652  -4.956  29.576  1.00 91.34           C\\nANISOU 2027  CB  VAL A1094    12822  11413  10469   -310  -1694     21       C\\nATOM   2028  CG1 VAL A1094      20.546  -4.549  31.038  1.00 87.18           C\\nANISOU 2028  CG1 VAL A1094    11914  10940  10271   -155  -1529    -81       C\\nATOM   2029  CG2 VAL A1094      20.261  -3.802  28.656  1.00 92.19           C\\nANISOU 2029  CG2 VAL A1094    13027  11445  10557   -192  -2230    148       C\\nATOM   2030  N   ARG A1095      21.898  -7.840  29.694  1.00 90.63           N\\nANISOU 2030  N   ARG A1095    13144  11253  10038   -685   -833    -66       N\\nATOM   2031  CA  ARG A1095      22.284  -9.087  30.344  1.00 90.96           C\\nANISOU 2031  CA  ARG A1095    13231  11214  10116   -790   -456   -122       C\\nATOM   2032  C   ARG A1095      23.746  -9.427  30.091  1.00 87.34           C\\nANISOU 2032  C   ARG A1095    13078  10619   9487   -715   -154      0       C\\nATOM   2033  O   ARG A1095      24.354 -10.144  30.893  1.00 79.42           O\\nANISOU 2033  O   ARG A1095    12074   9515   8587   -689    132     31       O\\nATOM   2034  CB  ARG A1095      21.389 -10.229  29.864  1.00 87.99           C\\nANISOU 2034  CB  ARG A1095    12907  10817   9709  -1046   -517   -333       C\\nATOM   2035  CG  ARG A1095      19.913  -9.890  29.887  1.00 88.08           C\\nANISOU 2035  CG  ARG A1095    12562  11010   9896  -1139   -853   -486       C\\nATOM   2036  CD  ARG A1095      19.099 -10.979  29.236  1.00 93.06           C\\nANISOU 2036  CD  ARG A1095    13265  11616  10479  -1439   -963   -697       C\\nATOM   2037  NE  ARG A1095      17.793 -10.502  28.791  1.00103.22           N\\nANISOU 2037  NE  ARG A1095    14244  13099  11877  -1501  -1404   -846       N\\nATOM   2038  CZ  ARG A1095      16.679 -10.583  29.511  1.00102.98           C\\nANISOU 2038  CZ  ARG A1095    13724  13246  12157  -1620  -1455   -997       C\\nATOM   2039  NH1 ARG A1095      16.705 -11.126  30.720  1.00101.20           N\\nANISOU 2039  NH1 ARG A1095    13324  13034  12095  -1735  -1072   -988       N\\nATOM   2040  NH2 ARG A1095      15.535 -10.122  29.020  1.00102.93           N\\nANISOU 2040  NH2 ARG A1095    13394  13427  12289  -1634  -1897  -1154       N\\nATOM   2041  N   ARG A1096      24.321  -8.920  29.001  1.00 90.45           N\\nANISOU 2041  N   ARG A1096    13718  11024   9623   -685   -218     78       N\\nATOM   2042  CA  ARG A1096      25.730  -9.168  28.728  1.00 86.04           C\\nANISOU 2042  CA  ARG A1096    13368  10402   8921   -614    110    159       C\\nATOM   2043  C   ARG A1096      26.623  -8.481  29.750  1.00 81.52           C\\nANISOU 2043  C   ARG A1096    12598   9829   8548   -445    250    350       C\\nATOM   2044  O   ARG A1096      27.697  -8.997  30.076  1.00 76.37           O\\nANISOU 2044  O   ARG A1096    11967   9110   7940   -359    548    380       O\\nATOM   2045  CB  ARG A1096      26.072  -8.706  27.313  1.00 85.80           C\\nANISOU 2045  CB  ARG A1096    13637  10453   8510   -686     38    205       C\\nATOM   2046  CG  ARG A1096      26.974  -9.657  26.568  1.00 82.89           C\\nANISOU 2046  CG  ARG A1096    13541  10054   7898   -716    389     63       C\\nATOM   2047  CD  ARG A1096      27.247  -9.180  25.159  1.00 85.44           C\\nANISOU 2047  CD  ARG A1096    14183  10531   7750   -844    350    102       C\\nATOM   2048  NE  ARG A1096      26.098  -9.355  24.282  1.00 94.36           N\\nANISOU 2048  NE  ARG A1096    15514  11710   8629  -1018     -6    -32       N\\nATOM   2049  CZ  ARG A1096      26.167  -9.297  22.957  1.00 97.59           C\\nANISOU 2049  CZ  ARG A1096    16291  12257   8531  -1179    -60    -72       C\\nATOM   2050  NH1 ARG A1096      27.333  -9.075  22.369  1.00 93.17           N\\nANISOU 2050  NH1 ARG A1096    15919  11820   7663  -1201    286      6       N\\nATOM   2051  NH2 ARG A1096      25.078  -9.465  22.222  1.00102.27           N\\nANISOU 2051  NH2 ARG A1096    17053  12899   8906  -1338   -456   -197       N\\nATOM   2052  N   ALA A1097      26.196  -7.325  30.270  1.00 83.15           N\\nANISOU 2052  N   ALA A1097    12599  10095   8899   -381     10    450       N\\nATOM   2053  CA  ALA A1097      26.963  -6.656  31.316  1.00 74.83           C\\nANISOU 2053  CA  ALA A1097    11361   9035   8036   -245    100    585       C\\nATOM   2054  C   ALA A1097      26.946  -7.446  32.617  1.00 73.67           C\\nANISOU 2054  C   ALA A1097    11047   8874   8072   -207    277    525       C\\nATOM   2055  O   ALA A1097      27.942  -7.452  33.348  1.00 74.45           O\\nANISOU 2055  O   ALA A1097    11087   8949   8253   -111    442    628       O\\nATOM   2056  CB  ALA A1097      26.423  -5.246  31.550  1.00 63.51           C\\nANISOU 2056  CB  ALA A1097     9778   7621   6732   -175   -226    643       C\\nATOM   2057  N   ALA A1098      25.832  -8.117  32.923  1.00 71.99           N\\nANISOU 2057  N   ALA A1098    10755   8685   7912   -311    230    379       N\\nATOM   2058  CA  ALA A1098      25.774  -8.940  34.125  1.00 74.69           C\\nANISOU 2058  CA  ALA A1098    11001   9011   8365   -346    407    373       C\\nATOM   2059  C   ALA A1098      26.760 -10.098  34.047  1.00 83.58           C\\nANISOU 2059  C   ALA A1098    12344   9949   9462   -326    646    434       C\\nATOM   2060  O   ALA A1098      27.358 -10.485  35.059  1.00 82.43           O\\nANISOU 2060  O   ALA A1098    12168   9750   9403   -262    768    547       O\\nATOM   2061  CB  ALA A1098      24.351  -9.450  34.338  1.00 76.99           C\\nANISOU 2061  CB  ALA A1098    11160   9381   8710   -537    335    213       C\\nATOM   2062  N   LEU A1099      26.946 -10.665  32.852  1.00 86.05           N\\nANISOU 2062  N   LEU A1099    12886  10156   9651   -363    693    343       N\\nATOM   2063  CA  LEU A1099      27.950 -11.710  32.691  1.00 84.37           C\\nANISOU 2063  CA  LEU A1099    12858   9742   9457   -276    922    336       C\\nATOM   2064  C   LEU A1099      29.360 -11.153  32.838  1.00 75.62           C\\nANISOU 2064  C   LEU A1099    11669   8675   8388    -65   1050    473       C\\nATOM   2065  O   LEU A1099      30.242 -11.829  33.380  1.00 59.72           O\\nANISOU 2065  O   LEU A1099     9651   6525   6517     79   1192    528       O\\nATOM   2066  CB  LEU A1099      27.785 -12.397  31.335  1.00 88.81           C\\nANISOU 2066  CB  LEU A1099    13687  10211   9847   -362    961    126       C\\nATOM   2067  CG  LEU A1099      28.635 -13.647  31.091  1.00 89.13           C\\nANISOU 2067  CG  LEU A1099    13929   9988   9947   -253   1195     11       C\\nATOM   2068  CD1 LEU A1099      28.246 -14.750  32.060  1.00 88.78           C\\nANISOU 2068  CD1 LEU A1099    13929   9678  10126   -318   1188     43       C\\nATOM   2069  CD2 LEU A1099      28.496 -14.118  29.655  1.00 91.08           C\\nANISOU 2069  CD2 LEU A1099    14451  10201   9955   -337   1240   -262       C\\nATOM   2070  N   ILE A1100      29.591  -9.928  32.363  1.00 70.27           N\\nANISOU 2070  N   ILE A1100    10921   8168   7612    -56    974    541       N\\nATOM   2071  CA  ILE A1100      30.888  -9.294  32.557  1.00 70.30           C\\nANISOU 2071  CA  ILE A1100    10796   8234   7680     77   1083    680       C\\nATOM   2072  C   ILE A1100      31.120  -9.006  34.034  1.00 76.98           C\\nANISOU 2072  C   ILE A1100    11428   9092   8729    165   1006    808       C\\nATOM   2073  O   ILE A1100      32.244  -9.120  34.537  1.00 80.54           O\\nANISOU 2073  O   ILE A1100    11764   9529   9310    301   1104    897       O\\nATOM   2074  CB  ILE A1100      30.983  -8.022  31.697  1.00 68.88           C\\nANISOU 2074  CB  ILE A1100    10638   8193   7340    -10    989    761       C\\nATOM   2075  CG1 ILE A1100      30.869  -8.386  30.212  1.00 75.73           C\\nANISOU 2075  CG1 ILE A1100    11771   9090   7912   -120   1082    646       C\\nATOM   2076  CG2 ILE A1100      32.279  -7.281  31.978  1.00 63.94           C\\nANISOU 2076  CG2 ILE A1100     9841   7638   6817     56   1090    917       C\\nATOM   2077  CD1 ILE A1100      30.869  -7.196  29.275  1.00 65.67           C\\nANISOU 2077  CD1 ILE A1100    10607   7938   6405   -260    954    784       C\\nATOM   2078  N   ASN A1101      30.057  -8.645  34.757  1.00 76.26           N\\nANISOU 2078  N   ASN A1101    11262   9055   8656     88    828    795       N\\nATOM   2079  CA  ASN A1101      30.161  -8.449  36.200  1.00 71.74           C\\nANISOU 2079  CA  ASN A1101    10532   8535   8191    138    773    876       C\\nATOM   2080  C   ASN A1101      30.619  -9.725  36.896  1.00 69.64           C\\nANISOU 2080  C   ASN A1101    10339   8134   7987    190    891    949       C\\nATOM   2081  O   ASN A1101      31.439  -9.679  37.821  1.00 64.42           O\\nANISOU 2081  O   ASN A1101     9588   7486   7403    297    869   1078       O\\nATOM   2082  CB  ASN A1101      28.811  -7.981  36.750  1.00 72.99           C\\nANISOU 2082  CB  ASN A1101    10589   8814   8330     34    629    774       C\\nATOM   2083  CG  ASN A1101      28.882  -7.542  38.204  1.00 79.76           C\\nANISOU 2083  CG  ASN A1101    11293   9793   9219     68    586    807       C\\nATOM   2084  OD1 ASN A1101      29.385  -8.264  39.065  1.00 88.11           O\\nANISOU 2084  OD1 ASN A1101    12391  10824  10262     80    664    919       O\\nATOM   2085  ND2 ASN A1101      28.363  -6.353  38.484  1.00 77.04           N\\nANISOU 2085  ND2 ASN A1101    10794   9569   8909     92    434    696       N\\nATOM   2086  N   MET A1102      30.111 -10.877  36.452  1.00 67.47           N\\nANISOU 2086  N   MET A1102    10246   7696   7691    110    973    875       N\\nATOM   2087  CA  MET A1102      30.457 -12.137  37.100  1.00 68.00           C\\nANISOU 2087  CA  MET A1102    10442   7546   7851    150   1035    971       C\\nATOM   2088  C   MET A1102      31.900 -12.539  36.815  1.00 75.21           C\\nANISOU 2088  C   MET A1102    11354   8314   8910    407   1126   1011       C\\nATOM   2089  O   MET A1102      32.611 -12.984  37.723  1.00 77.63           O\\nANISOU 2089  O   MET A1102    11635   8519   9341    543   1075   1172       O\\nATOM   2090  CB  MET A1102      29.492 -13.233  36.655  1.00 70.40           C\\nANISOU 2090  CB  MET A1102    10958   7659   8132    -38   1075    861       C\\nATOM   2091  CG  MET A1102      28.072 -13.024  37.150  1.00 76.57           C\\nANISOU 2091  CG  MET A1102    11663   8605   8824   -310   1005    826       C\\nATOM   2092  SD  MET A1102      27.010 -14.445  36.822  1.00 81.97           S\\nANISOU 2092  SD  MET A1102    12572   9042   9532   -608   1039    733       S\\nATOM   2093  CE  MET A1102      27.916 -15.743  37.652  1.00 80.68           C\\nANISOU 2093  CE  MET A1102    12664   8490   9502   -523   1086    972       C\\nATOM   2094  N   VAL A1103      32.352 -12.395  35.565  1.00 79.58           N\\nANISOU 2094  N   VAL A1103    11918   8879   9439    475   1257    861       N\\nATOM   2095  CA  VAL A1103      33.743 -12.721  35.251  1.00 82.54           C\\nANISOU 2095  CA  VAL A1103    12205   9184   9974    728   1400    840       C\\nATOM   2096  C   VAL A1103      34.689 -11.726  35.912  1.00 80.24           C\\nANISOU 2096  C   VAL A1103    11618   9095   9774    826   1331   1000       C\\nATOM   2097  O   VAL A1103      35.848 -12.053  36.198  1.00 82.23           O\\nANISOU 2097  O   VAL A1103    11705   9299  10238   1051   1366   1045       O\\nATOM   2098  CB  VAL A1103      33.969 -12.782  33.727  1.00 84.75           C\\nANISOU 2098  CB  VAL A1103    12570   9500  10133    729   1619    609       C\\nATOM   2099  CG1 VAL A1103      32.942 -13.689  33.066  1.00 85.19           C\\nANISOU 2099  CG1 VAL A1103    12933   9364  10070    590   1631    415       C\\nATOM   2100  CG2 VAL A1103      33.931 -11.394  33.115  1.00 83.71           C\\nANISOU 2100  CG2 VAL A1103    12339   9665   9801    582   1615    646       C\\nATOM   2101  N   PHE A1104      34.222 -10.502  36.163  1.00 72.46           N\\nANISOU 2101  N   PHE A1104    10543   8321   8669    670   1206   1064       N\\nATOM   2102  CA  PHE A1104      35.025  -9.556  36.927  1.00 74.27           C\\nANISOU 2102  CA  PHE A1104    10521   8703   8994    721   1090   1196       C\\nATOM   2103  C   PHE A1104      35.203 -10.013  38.369  1.00 79.15           C\\nANISOU 2103  C   PHE A1104    11108   9268   9696    808    920   1340       C\\nATOM   2104  O   PHE A1104      36.258  -9.779  38.969  1.00 81.90           O\\nANISOU 2104  O   PHE A1104    11250   9676  10191    937    827   1439       O\\nATOM   2105  CB  PHE A1104      34.382  -8.171  36.883  1.00 67.54           C\\nANISOU 2105  CB  PHE A1104     9633   8010   8019    545    959   1195       C\\nATOM   2106  CG  PHE A1104      35.032  -7.234  35.911  1.00 71.68           C\\nANISOU 2106  CG  PHE A1104    10068   8632   8534    483   1036   1205       C\\nATOM   2107  CD1 PHE A1104      34.785  -7.340  34.554  1.00 74.18           C\\nANISOU 2107  CD1 PHE A1104    10546   8950   8690    396   1191   1126       C\\nATOM   2108  CD2 PHE A1104      35.892  -6.243  36.356  1.00 80.86           C\\nANISOU 2108  CD2 PHE A1104    11011   9893   9821    465    944   1303       C\\nATOM   2109  CE1 PHE A1104      35.384  -6.477  33.659  1.00 78.16           C\\nANISOU 2109  CE1 PHE A1104    11011   9565   9121    278   1280   1183       C\\nATOM   2110  CE2 PHE A1104      36.492  -5.376  35.467  1.00 85.63           C\\nANISOU 2110  CE2 PHE A1104    11550  10576  10412    335   1028   1354       C\\nATOM   2111  CZ  PHE A1104      36.238  -5.493  34.115  1.00 81.25           C\\nANISOU 2111  CZ  PHE A1104    11176  10035   9661    234   1209   1314       C\\nATOM   2112  N   GLN A1105      34.192 -10.669  38.935  1.00 80.45           N\\nANISOU 2112  N   GLN A1105    11475   9341   9754    708    866   1365       N\\nATOM   2113  CA  GLN A1105      34.237 -11.118  40.319  1.00 76.17           C\\nANISOU 2113  CA  GLN A1105    10978   8769   9193    723    706   1544       C\\nATOM   2114  C   GLN A1105      34.839 -12.508  40.465  1.00 79.87           C\\nANISOU 2114  C   GLN A1105    11579   8938   9829    899    695   1660       C\\nATOM   2115  O   GLN A1105      35.670 -12.731  41.352  1.00 77.78           O\\nANISOU 2115  O   GLN A1105    11252   8640   9660   1051    517   1841       O\\nATOM   2116  CB  GLN A1105      32.830 -11.107  40.918  1.00 71.88           C\\nANISOU 2116  CB  GLN A1105    10574   8313   8426    472    687   1531       C\\nATOM   2117  CG  GLN A1105      32.752 -11.692  42.313  1.00 71.95           C\\nANISOU 2117  CG  GLN A1105    10707   8315   8315    408    569   1741       C\\nATOM   2118  CD  GLN A1105      31.379 -11.534  42.928  1.00 72.70           C\\nANISOU 2118  CD  GLN A1105    10864   8598   8159    121    622   1689       C\\nATOM   2119  OE1 GLN A1105      30.414 -11.193  42.241  1.00 76.06           O\\nANISOU 2119  OE1 GLN A1105    11232   9099   8567     -1    727   1488       O\\nATOM   2120  NE2 GLN A1105      31.282 -11.777  44.230  1.00 68.30           N\\nANISOU 2120  NE2 GLN A1105    10410   8146   7396      7    545   1865       N\\nATOM   2121  N   MET A1106      34.433 -13.446  39.607  1.00 80.28           N\\nANISOU 2121  N   MET A1106    11826   8743   9934    892    842   1548       N\\nATOM   2122  CA  MET A1106      34.803 -14.847  39.734  1.00 82.95           C\\nANISOU 2122  CA  MET A1106    12358   8697  10463   1051    807   1630       C\\nATOM   2123  C   MET A1106      35.843 -15.311  38.725  1.00 89.43           C\\nANISOU 2123  C   MET A1106    13075   9350  11554   1362    949   1444       C\\nATOM   2124  O   MET A1106      36.305 -16.452  38.830  1.00 92.75           O\\nANISOU 2124  O   MET A1106    13623   9404  12215   1580    890   1476       O\\nATOM   2125  CB  MET A1106      33.551 -15.727  39.604  1.00 79.57           C\\nANISOU 2125  CB  MET A1106    12259   8043   9930    793    855   1607       C\\nATOM   2126  CG  MET A1106      32.706 -15.755  40.856  1.00 84.73           C\\nANISOU 2126  CG  MET A1106    13038   8785  10370    512    733   1843       C\\nATOM   2127  SD  MET A1106      30.984 -16.135  40.503  1.00 86.03           S\\nANISOU 2127  SD  MET A1106    13388   8937  10364     82    862   1721       S\\nATOM   2128  CE  MET A1106      30.421 -14.540  39.929  1.00 88.27           C\\nANISOU 2128  CE  MET A1106    13356   9694  10490     13    937   1471       C\\nATOM   2129  N   GLY A1107      36.219 -14.477  37.763  1.00 83.47           N\\nANISOU 2129  N   GLY A1107    12104   8844  10768   1383   1136   1249       N\\nATOM   2130  CA  GLY A1107      37.045 -14.923  36.668  1.00 86.98           C\\nANISOU 2130  CA  GLY A1107    12460   9202  11389   1617   1365   1006       C\\nATOM   2131  C   GLY A1107      36.292 -15.824  35.707  1.00 88.79           C\\nANISOU 2131  C   GLY A1107    13014   9179  11544   1543   1521    764       C\\nATOM   2132  O   GLY A1107      35.264 -16.426  36.027  1.00 86.13           O\\nANISOU 2132  O   GLY A1107    12973   8625  11128   1354   1409    824       O\\nATOM   2133  N   GLU A1108      36.843 -15.917  34.497  1.00 89.49           N\\nANISOU 2133  N   GLU A1108    13038   9319  11644   1667   1796    468       N\\nATOM   2134  CA  GLU A1108      36.262 -16.761  33.464  1.00 87.52           C\\nANISOU 2134  CA  GLU A1108    13103   8850  11300   1613   1951    163       C\\nATOM   2135  C   GLU A1108      36.230 -18.231  33.861  1.00 85.64           C\\nANISOU 2135  C   GLU A1108    13113   8070  11356   1798   1837    124       C\\nATOM   2136  O   GLU A1108      35.365 -18.973  33.377  1.00 84.49           O\\nANISOU 2136  O   GLU A1108    13313   7661  11130   1634   1842    -46       O\\nATOM   2137  CB  GLU A1108      37.029 -16.590  32.160  1.00 95.88           C\\nANISOU 2137  CB  GLU A1108    14037  10114  12279   1733   2303   -169       C\\nATOM   2138  CG  GLU A1108      36.931 -15.181  31.598  1.00102.62           C\\nANISOU 2138  CG  GLU A1108    14756  11443  12792   1470   2402   -100       C\\nATOM   2139  CD  GLU A1108      37.375 -15.104  30.157  1.00109.37           C\\nANISOU 2139  CD  GLU A1108    15629  12514  13413   1456   2771   -421       C\\nATOM   2140  OE1 GLU A1108      37.716 -16.168  29.591  1.00113.53           O\\nANISOU 2140  OE1 GLU A1108    16260  12832  14044   1672   2970   -764       O\\nATOM   2141  OE2 GLU A1108      37.380 -13.985  29.593  1.00105.41           O\\nANISOU 2141  OE2 GLU A1108    15063  12377  12612   1221   2859   -335       O\\nATOM   2142  N   THR A1109      37.155 -18.669  34.719  1.00 90.70           N\\nANISOU 2142  N   THR A1109    13597   8510  12353   2124   1695    286       N\\nATOM   2143  CA  THR A1109      37.120 -20.042  35.207  1.00 95.84           C\\nANISOU 2143  CA  THR A1109    14532   8571  13311   2298   1506    331       C\\nATOM   2144  C   THR A1109      35.855 -20.297  36.012  1.00 92.70           C\\nANISOU 2144  C   THR A1109    14477   8003  12741   1906   1273    629       C\\nATOM   2145  O   THR A1109      35.133 -21.269  35.766  1.00 95.09           O\\nANISOU 2145  O   THR A1109    15151   7895  13084   1765   1241    533       O\\nATOM   2146  CB  THR A1109      38.349 -20.335  36.066  1.00 97.86           C\\nANISOU 2146  CB  THR A1109    14535   8674  13974   2728   1309    517       C\\nATOM   2147  OG1 THR A1109      39.538 -19.920  35.381  1.00102.45           O\\nANISOU 2147  OG1 THR A1109    14672   9535  14718   3048   1561    242       O\\nATOM   2148  CG2 THR A1109      38.427 -21.828  36.376  1.00 97.85           C\\nANISOU 2148  CG2 THR A1109    14861   7969  14349   2976   1099    531       C\\nATOM   2149  N   GLY A1110      35.567 -19.420  36.975  1.00 95.75           N\\nANISOU 2149  N   GLY A1110    14731   8720  12931   1701   1128    965       N\\nATOM   2150  CA  GLY A1110      34.456 -19.660  37.880  1.00 94.88           C\\nANISOU 2150  CA  GLY A1110    14887   8513  12649   1331    949   1253       C\\nATOM   2151  C   GLY A1110      33.103 -19.552  37.204  1.00 88.67           C\\nANISOU 2151  C   GLY A1110    14261   7826  11602    922   1075   1072       C\\nATOM   2152  O   GLY A1110      32.191 -20.329  37.497  1.00 82.42           O\\nANISOU 2152  O   GLY A1110    13765   6760  10793    635    997   1160       O\\nATOM   2153  N   VAL A1111      32.952 -18.588  36.296  1.00 85.36           N\\nANISOU 2153  N   VAL A1111    13649   7799  10986    866   1244    836       N\\nATOM   2154  CA  VAL A1111      31.676 -18.422  35.606  1.00 83.59           C\\nANISOU 2154  CA  VAL A1111    13541   7694  10525    508   1297    660       C\\nATOM   2155  C   VAL A1111      31.371 -19.646  34.751  1.00 86.94           C\\nANISOU 2155  C   VAL A1111    14292   7686  11055    469   1346    385       C\\nATOM   2156  O   VAL A1111      30.217 -20.080  34.649  1.00 84.62           O\\nANISOU 2156  O   VAL A1111    14188   7281  10681    116   1284    338       O\\nATOM   2157  CB  VAL A1111      31.689 -17.125  34.776  1.00 78.72           C\\nANISOU 2157  CB  VAL A1111    12692   7539   9679    492   1403    508       C\\nATOM   2158  CG1 VAL A1111      30.403 -16.979  33.994  1.00 82.94           C\\nANISOU 2158  CG1 VAL A1111    13340   8183   9992    166   1385    324       C\\nATOM   2159  CG2 VAL A1111      31.894 -15.925  35.684  1.00 68.67           C\\nANISOU 2159  CG2 VAL A1111    11133   6621   8339    498   1317    755       C\\nATOM   2160  N   ALA A1112      32.402 -20.242  34.147  1.00 83.83           N\\nANISOU 2160  N   ALA A1112    13946   7039  10867    828   1457    166       N\\nATOM   2161  CA  ALA A1112      32.208 -21.434  33.331  1.00 86.95           C\\nANISOU 2161  CA  ALA A1112    14676   6976  11386    838   1502   -166       C\\nATOM   2162  C   ALA A1112      31.727 -22.636  34.137  1.00 97.68           C\\nANISOU 2162  C   ALA A1112    16361   7762  12989    696   1293     31       C\\nATOM   2163  O   ALA A1112      31.408 -23.672  33.541  1.00107.07           O\\nANISOU 2163  O   ALA A1112    17878   8495  14308    634   1283   -236       O\\nATOM   2164  CB  ALA A1112      33.504 -21.784  32.597  1.00 82.87           C\\nANISOU 2164  CB  ALA A1112    14088   6331  11068   1312   1699   -487       C\\nATOM   2165  N   GLY A1113      31.670 -22.528  35.467  1.00 94.08           N\\nANISOU 2165  N   GLY A1113    15859   7311  12576    613   1121    490       N\\nATOM   2166  CA  GLY A1113      31.127 -23.580  36.301  1.00 91.96           C\\nANISOU 2166  CA  GLY A1113    15934   6547  12461    374    924    767       C\\nATOM   2167  C   GLY A1113      29.632 -23.536  36.499  1.00 88.01           C\\nANISOU 2167  C   GLY A1113    15526   6189  11726   -228    907    854       C\\nATOM   2168  O   GLY A1113      29.067 -24.463  37.088  1.00 90.55           O\\nANISOU 2168  O   GLY A1113    16155   6098  12153   -532    780   1074       O\\nATOM   2169  N   PHE A1114      28.975 -22.477  36.030  1.00 89.32           N\\nANISOU 2169  N   PHE A1114    15419   6923  11597   -417   1020    697       N\\nATOM   2170  CA  PHE A1114      27.518 -22.347  36.101  1.00 93.06           C\\nANISOU 2170  CA  PHE A1114    15868   7604  11887   -955   1007    701       C\\nATOM   2171  C   PHE A1114      26.844 -22.935  34.867  1.00 97.68           C\\nANISOU 2171  C   PHE A1114    16640   7982  12490  -1154   1008    293       C\\nATOM   2172  O   PHE A1114      25.996 -22.294  34.250  1.00100.46           O\\nANISOU 2172  O   PHE A1114    16812   8720  12638  -1379   1016     94       O\\nATOM   2173  CB  PHE A1114      27.127 -20.883  36.266  1.00 94.49           C\\nANISOU 2173  CB  PHE A1114    15638   8468  11794  -1010   1062    728       C\\nATOM   2174  CG  PHE A1114      27.602 -20.258  37.542  1.00 95.33           C\\nANISOU 2174  CG  PHE A1114    15570   8818  11834   -900   1044   1086       C\\nATOM   2175  CD1 PHE A1114      26.863 -20.382  38.706  1.00 96.26           C\\nANISOU 2175  CD1 PHE A1114    15694   9032  11847  -1255   1023   1375       C\\nATOM   2176  CD2 PHE A1114      28.773 -19.521  37.572  1.00 93.76           C\\nANISOU 2176  CD2 PHE A1114    15190   8788  11647   -478   1057   1113       C\\nATOM   2177  CE1 PHE A1114      27.293 -19.799  39.881  1.00 93.49           C\\nANISOU 2177  CE1 PHE A1114    15219   8937  11366  -1170    999   1669       C\\nATOM   2178  CE2 PHE A1114      29.209 -18.933  38.743  1.00 90.99           C\\nANISOU 2178  CE2 PHE A1114    14688   8664  11219   -396    999   1410       C\\nATOM   2179  CZ  PHE A1114      28.468 -19.072  39.900  1.00 89.90           C\\nANISOU 2179  CZ  PHE A1114    14603   8619  10937   -731    961   1678       C\\nATOM   2180  N   THR A1115      27.213 -24.163  34.496  1.00 93.63           N\\nANISOU 2180  N   THR A1115    16502   6840  12234  -1062    963    146       N\\nATOM   2181  CA  THR A1115      26.755 -24.715  33.225  1.00 97.80           C\\nANISOU 2181  CA  THR A1115    17241   7160  12760  -1192    960   -325       C\\nATOM   2182  C   THR A1115      25.237 -24.821  33.175  1.00101.53           C\\nANISOU 2182  C   THR A1115    17699   7752  13126  -1809    862   -353       C\\nATOM   2183  O   THR A1115      24.618 -24.467  32.164  1.00100.69           O\\nANISOU 2183  O   THR A1115    17515   7914  12829  -1958    838   -694       O\\nATOM   2184  CB  THR A1115      27.395 -26.081  32.984  1.00104.56           C\\nANISOU 2184  CB  THR A1115    18523   7240  13966   -980    909   -494       C\\nATOM   2185  OG1 THR A1115      26.936 -27.010  33.974  1.00111.74           O\\nANISOU 2185  OG1 THR A1115    19700   7650  15106  -1304    745   -134       O\\nATOM   2186  CG2 THR A1115      28.912 -25.975  33.059  1.00103.25           C\\nANISOU 2186  CG2 THR A1115    18273   6991  13964   -334   1002   -493       C\\nATOM   2187  N   ASN A1116      24.617 -25.292  34.259  1.00109.01           N\\nANISOU 2187  N   ASN A1116    18703   8536  14180  -2193    797     12       N\\nATOM   2188  CA  ASN A1116      23.168 -25.450  34.256  1.00114.25           C\\nANISOU 2188  CA  ASN A1116    19286   9335  14790  -2821    734    -24       C\\nATOM   2189  C   ASN A1116      22.464 -24.103  34.180  1.00108.33           C\\nANISOU 2189  C   ASN A1116    18027   9368  13766  -2910    776    -69       C\\nATOM   2190  O   ASN A1116      21.401 -23.993  33.560  1.00112.39           O\\nANISOU 2190  O   ASN A1116    18389  10096  14219  -3257    688   -317       O\\nATOM   2191  CB  ASN A1116      22.716 -26.227  35.496  1.00119.12           C\\nANISOU 2191  CB  ASN A1116    20066   9646  15546  -3254    712    417       C\\nATOM   2192  N   SER A1117      23.040 -23.071  34.794  1.00107.10           N\\nANISOU 2192  N   SER A1117    17599   9621  13474  -2592    871    149       N\\nATOM   2193  CA  SER A1117      22.434 -21.748  34.719  1.00102.31           C\\nANISOU 2193  CA  SER A1117    16531   9686  12658  -2613    880     85       C\\nATOM   2194  C   SER A1117      22.674 -21.101  33.361  1.00102.29           C\\nANISOU 2194  C   SER A1117    16484   9870  12513  -2343    814   -265       C\\nATOM   2195  O   SER A1117      21.756 -20.507  32.785  1.00100.23           O\\nANISOU 2195  O   SER A1117    15984   9960  12139  -2521    696   -453       O\\nATOM   2196  CB  SER A1117      22.981 -20.857  35.835  1.00 98.47           C\\nANISOU 2196  CB  SER A1117    15811   9527  12076  -2381    982    404       C\\nATOM   2197  OG  SER A1117      22.892 -21.504  37.092  1.00 97.73           O\\nANISOU 2197  OG  SER A1117    15842   9258  12035  -2624   1039    761       O\\nATOM   2198  N   LEU A1118      23.897 -21.215  32.836  1.00104.26           N\\nANISOU 2198  N   LEU A1118    16951   9904  12761  -1923    883   -351       N\\nATOM   2199  CA  LEU A1118      24.243 -20.548  31.585  1.00100.23           C\\nANISOU 2199  CA  LEU A1118    16425   9622  12038  -1690    875   -637       C\\nATOM   2200  C   LEU A1118      23.389 -21.046  30.427  1.00107.73           C\\nANISOU 2200  C   LEU A1118    17547  10492  12892  -1976    724  -1011       C\\nATOM   2201  O   LEU A1118      23.041 -20.274  29.525  1.00110.02           O\\nANISOU 2201  O   LEU A1118    17736  11135  12931  -1982    613  -1185       O\\nATOM   2202  CB  LEU A1118      25.722 -20.757  31.279  1.00 92.05           C\\nANISOU 2202  CB  LEU A1118    15569   8366  11040  -1233   1041   -692       C\\nATOM   2203  CG  LEU A1118      26.695 -19.998  32.171  1.00 86.98           C\\nANISOU 2203  CG  LEU A1118    14695   7910  10443   -907   1144   -375       C\\nATOM   2204  CD1 LEU A1118      28.100 -20.549  32.003  1.00 86.56           C\\nANISOU 2204  CD1 LEU A1118    14792   7548  10551   -488   1291   -444       C\\nATOM   2205  CD2 LEU A1118      26.654 -18.516  31.846  1.00 86.67           C\\nANISOU 2205  CD2 LEU A1118    14359   8413  10159   -835   1133   -349       C\\nATOM   2206  N   ARG A1119      23.046 -22.333  30.429  1.00104.44           N\\nANISOU 2206  N   ARG A1119    17422   9590  12668  -2232    680  -1129       N\\nATOM   2207  CA  ARG A1119      22.191 -22.858  29.372  1.00103.70           C\\nANISOU 2207  CA  ARG A1119    17500   9406  12496  -2554    498  -1514       C\\nATOM   2208  C   ARG A1119      20.795 -22.250  29.433  1.00102.63           C\\nANISOU 2208  C   ARG A1119    16991   9707  12297  -2952    292  -1490       C\\nATOM   2209  O   ARG A1119      20.133 -22.113  28.398  1.00102.11           O\\nANISOU 2209  O   ARG A1119    16930   9811  12055  -3119     75  -1792       O\\nATOM   2210  CB  ARG A1119      22.123 -24.383  29.466  1.00105.66           C\\nANISOU 2210  CB  ARG A1119    18150   8971  13026  -2774    474  -1635       C\\nATOM   2211  CG  ARG A1119      21.461 -25.066  28.282  1.00110.68           C\\nANISOU 2211  CG  ARG A1119    19053   9414  13586  -3068    283  -2116       C\\nATOM   2212  CD  ARG A1119      21.400 -26.576  28.478  1.00119.37           C\\nANISOU 2212  CD  ARG A1119    20574   9750  15030  -3303    239  -2220       C\\nATOM   2213  NE  ARG A1119      20.881 -26.936  29.795  1.00121.59           N\\nANISOU 2213  NE  ARG A1119    20741   9865  15590  -3652    240  -1772       N\\nATOM   2214  CZ  ARG A1119      21.609 -27.484  30.763  1.00120.23           C\\nANISOU 2214  CZ  ARG A1119    20757   9256  15669  -3483    350  -1432       C\\nATOM   2215  NH1 ARG A1119      22.893 -27.748  30.561  1.00119.50           N\\nANISOU 2215  NH1 ARG A1119    20917   8831  15658  -2927    455  -1524       N\\nATOM   2216  NH2 ARG A1119      21.053 -27.772  31.933  1.00120.62           N\\nANISOU 2216  NH2 ARG A1119    20732   9219  15878  -3878    351  -1000       N\\nATOM   2217  N   MET A1120      20.338 -21.863  30.627  1.00100.48           N\\nANISOU 2217  N   MET A1120    16375   9649  12155  -3093    347  -1158       N\\nATOM   2218  CA  MET A1120      19.012 -21.263  30.756  1.00103.10           C\\nANISOU 2218  CA  MET A1120    16260  10430  12486  -3427    184  -1176       C\\nATOM   2219  C   MET A1120      19.000 -19.818  30.272  1.00100.31           C\\nANISOU 2219  C   MET A1120    15604  10594  11915  -3129     66  -1209       C\\nATOM   2220  O   MET A1120      18.009 -19.365  29.686  1.00100.24           O\\nANISOU 2220  O   MET A1120    15342  10888  11857  -3303   -198  -1388       O\\nATOM   2221  CB  MET A1120      18.535 -21.349  32.203  1.00106.18           C\\nANISOU 2221  CB  MET A1120    16380  10910  13054  -3686    341   -856       C\\nATOM   2222  CG  MET A1120      18.420 -22.776  32.714  1.00117.71           C\\nANISOU 2222  CG  MET A1120    18166  11832  14725  -4073    415   -750       C\\nATOM   2223  SD  MET A1120      17.789 -22.885  34.401  1.00123.98           S\\nANISOU 2223  SD  MET A1120    18683  12804  15620  -4485    629   -335       S\\nATOM   2224  CE  MET A1120      17.761 -24.663  34.625  1.00131.09           C\\nANISOU 2224  CE  MET A1120    20134  12916  16760  -4951    624   -214       C\\nATOM   2225  N   LEU A1121      20.082 -19.075  30.519  1.00100.35           N\\nANISOU 2225  N   LEU A1121    15626  10687  11815  -2692    222  -1026       N\\nATOM   2226  CA  LEU A1121      20.236 -17.769  29.884  1.00100.41           C\\nANISOU 2226  CA  LEU A1121    15473  11071  11608  -2415     91  -1049       C\\nATOM   2227  C   LEU A1121      20.299 -17.911  28.369  1.00105.95           C\\nANISOU 2227  C   LEU A1121    16480  11732  12045  -2411    -85  -1340       C\\nATOM   2228  O   LEU A1121      19.794 -17.057  27.629  1.00108.90           O\\nANISOU 2228  O   LEU A1121    16728  12416  12235  -2399   -355  -1411       O\\nATOM   2229  CB  LEU A1121      21.498 -17.077  30.396  1.00 89.96           C\\nANISOU 2229  CB  LEU A1121    14156   9787  10238  -2005    306   -807       C\\nATOM   2230  CG  LEU A1121      21.578 -16.711  31.874  1.00 82.79           C\\nANISOU 2230  CG  LEU A1121    12972   8988   9494  -1956    454   -522       C\\nATOM   2231  CD1 LEU A1121      22.975 -16.220  32.204  1.00 72.92           C\\nANISOU 2231  CD1 LEU A1121    11799   7708   8200  -1566    625   -331       C\\nATOM   2232  CD2 LEU A1121      20.549 -15.649  32.207  1.00 85.66           C\\nANISOU 2232  CD2 LEU A1121    12882   9776   9890  -2027    296   -524       C\\nATOM   2233  N   GLN A1122      20.920 -18.991  27.892  1.00 98.13           N\\nANISOU 2233  N   GLN A1122    15913  10351  11023  -2411     46  -1520       N\\nATOM   2234  CA  GLN A1122      21.020 -19.232  26.459  1.00 98.26           C\\nANISOU 2234  CA  GLN A1122    16271  10336  10727  -2427    -75  -1857       C\\nATOM   2235  C   GLN A1122      19.667 -19.584  25.852  1.00 96.39           C\\nANISOU 2235  C   GLN A1122    15998  10161  10466  -2846   -440  -2111       C\\nATOM   2236  O   GLN A1122      19.425 -19.301  24.674  1.00 98.68           O\\nANISOU 2236  O   GLN A1122    16445  10634  10417  -2889   -682  -2330       O\\nATOM   2237  CB  GLN A1122      22.036 -20.346  26.201  1.00103.05           C\\nANISOU 2237  CB  GLN A1122    17309  10483  11362  -2283    189  -2053       C\\nATOM   2238  CG  GLN A1122      22.347 -20.616  24.747  1.00107.55           C\\nANISOU 2238  CG  GLN A1122    18269  11042  11552  -2252    165  -2458       C\\nATOM   2239  CD  GLN A1122      23.447 -21.645  24.581  1.00111.75           C\\nANISOU 2239  CD  GLN A1122    19160  11128  12172  -2017    475  -2696       C\\nATOM   2240  OE1 GLN A1122      24.039 -22.100  25.559  1.00115.12           O\\nANISOU 2240  OE1 GLN A1122    19540  11237  12962  -1840    666  -2506       O\\nATOM   2241  NE2 GLN A1122      23.726 -22.017  23.338  1.00113.25           N\\nANISOU 2241  NE2 GLN A1122    19714  11294  12023  -1998    511  -3131       N\\nATOM   2242  N   GLN A1123      18.773 -20.184  26.639  1.00102.08           N\\nANISOU 2242  N   GLN A1123    16506  10761  11521  -3189   -495  -2073       N\\nATOM   2243  CA  GLN A1123      17.459 -20.603  26.168  1.00103.74           C\\nANISOU 2243  CA  GLN A1123    16604  11025  11786  -3643   -839  -2321       C\\nATOM   2244  C   GLN A1123      16.362 -19.590  26.496  1.00108.72           C\\nANISOU 2244  C   GLN A1123    16638  12153  12517  -3742  -1093  -2203       C\\nATOM   2245  O   GLN A1123      15.179 -19.947  26.486  1.00110.87           O\\nANISOU 2245  O   GLN A1123    16643  12510  12973  -4152  -1332  -2352       O\\nATOM   2246  CB  GLN A1123      17.101 -21.971  26.754  1.00101.84           C\\nANISOU 2246  CB  GLN A1123    16492  10326  11878  -4039   -744  -2378       C\\nATOM   2247  CG  GLN A1123      17.964 -23.119  26.251  1.00 99.00           C\\nANISOU 2247  CG  GLN A1123    16739   9389  11487  -3971   -604  -2613       C\\nATOM   2248  CD  GLN A1123      17.609 -24.442  26.905  1.00109.60           C\\nANISOU 2248  CD  GLN A1123    18244  10191  13208  -4372   -553  -2607       C\\nATOM   2249  OE1 GLN A1123      17.694 -24.589  28.124  1.00109.83           O\\nANISOU 2249  OE1 GLN A1123    18131  10108  13491  -4423   -352  -2243       O\\nATOM   2250  NE2 GLN A1123      17.200 -25.410  26.095  1.00111.61           N\\nANISOU 2250  NE2 GLN A1123    18833  10095  13478  -4692   -754  -3005       N\\nATOM   2251  N   LYS A1124      16.728 -18.344  26.794  1.00101.10           N\\nANISOU 2251  N   LYS A1124    15436  11503  11475  -3376  -1053  -1965       N\\nATOM   2252  CA  LYS A1124      15.801 -17.264  27.128  1.00102.00           C\\nANISOU 2252  CA  LYS A1124    14979  12055  11722  -3354  -1290  -1880       C\\nATOM   2253  C   LYS A1124      14.956 -17.560  28.362  1.00106.14           C\\nANISOU 2253  C   LYS A1124    15026  12671  12629  -3642  -1145  -1813       C\\nATOM   2254  O   LYS A1124      13.969 -16.858  28.613  1.00108.27           O\\nANISOU 2254  O   LYS A1124    14746  13316  13075  -3688  -1344  -1851       O\\nATOM   2255  CB  LYS A1124      14.875 -16.927  25.950  1.00104.85           C\\nANISOU 2255  CB  LYS A1124    15253  12649  11937  -3482  -1823  -2115       C\\nATOM   2256  CG  LYS A1124      15.585 -16.569  24.655  1.00106.34           C\\nANISOU 2256  CG  LYS A1124    15931  12827  11648  -3267  -1994  -2170       C\\nATOM   2257  CD  LYS A1124      16.318 -15.246  24.762  1.00102.53           C\\nANISOU 2257  CD  LYS A1124    15411  12521  11026  -2834  -1939  -1876       C\\nATOM   2258  CE  LYS A1124      16.710 -14.725  23.392  1.00104.63           C\\nANISOU 2258  CE  LYS A1124    16088  12882  10786  -2721  -2205  -1897       C\\nATOM   2259  NZ  LYS A1124      15.510 -14.429  22.560  1.00109.17           N\\nANISOU 2259  NZ  LYS A1124    16517  13684  11279  -2897  -2828  -2043       N\\nATOM   2260  N   ARG A1125      15.311 -18.583  29.142  1.00109.81           N\\nANISOU 2260  N   ARG A1125    15685  12809  13228  -3839   -806  -1713       N\\nATOM   2261  CA  ARG A1125      14.563 -18.937  30.349  1.00105.46           C\\nANISOU 2261  CA  ARG A1125    14749  12354  12966  -4188   -611  -1603       C\\nATOM   2262  C   ARG A1125      15.011 -18.038  31.502  1.00105.15           C\\nANISOU 2262  C   ARG A1125    14454  12555  12943  -3878   -338  -1327       C\\nATOM   2263  O   ARG A1125      15.645 -18.469  32.467  1.00102.11           O\\nANISOU 2263  O   ARG A1125    14245  11977  12576  -3884    -12  -1083       O\\nATOM   2264  CB  ARG A1125      14.757 -20.408  30.687  1.00100.56           C\\nANISOU 2264  CB  ARG A1125    14519  11232  12456  -4562   -413  -1558       C\\nATOM   2265  CG  ARG A1125      14.118 -21.370  29.702  1.00104.76           C\\nANISOU 2265  CG  ARG A1125    15255  11516  13034  -4972   -689  -1879       C\\nATOM   2266  CD  ARG A1125      14.117 -22.790  30.251  1.00109.68           C\\nANISOU 2266  CD  ARG A1125    16197  11614  13861  -5418   -505  -1800       C\\nATOM   2267  NE  ARG A1125      15.435 -23.419  30.187  1.00111.71           N\\nANISOU 2267  NE  ARG A1125    17086  11317  14042  -5114   -333  -1714       N\\nATOM   2268  CZ  ARG A1125      15.756 -24.551  30.807  1.00114.79           C\\nANISOU 2268  CZ  ARG A1125    17840  11156  14619  -5338   -166  -1549       C\\nATOM   2269  NH1 ARG A1125      14.859 -25.182  31.553  1.00117.33           N\\nANISOU 2269  NH1 ARG A1125    17995  11419  15168  -5934   -115  -1411       N\\nATOM   2270  NH2 ARG A1125      16.978 -25.051  30.689  1.00114.27           N\\nANISOU 2270  NH2 ARG A1125    18294  10594  14529  -4971    -54  -1512       N\\nATOM   2271  N   TRP A1126      14.657 -16.753  31.387  1.00102.43           N\\nANISOU 2271  N   TRP A1126    13702  12620  12595  -3599   -520  -1377       N\\nATOM   2272  CA  TRP A1126      15.103 -15.775  32.375  1.00 99.11           C\\nANISOU 2272  CA  TRP A1126    13061  12418  12179  -3267   -310  -1183       C\\nATOM   2273  C   TRP A1126      14.567 -16.088  33.763  1.00100.00           C\\nANISOU 2273  C   TRP A1126    12842  12708  12447  -3564     17  -1092       C\\nATOM   2274  O   TRP A1126      15.235 -15.807  34.763  1.00 95.88           O\\nANISOU 2274  O   TRP A1126    12367  12211  11852  -3395    296   -877       O\\nATOM   2275  CB  TRP A1126      14.683 -14.363  31.959  1.00 98.18           C\\nANISOU 2275  CB  TRP A1126    12566  12644  12092  -2934   -622  -1293       C\\nATOM   2276  CG  TRP A1126      15.001 -14.027  30.537  1.00 99.97           C\\nANISOU 2276  CG  TRP A1126    13108  12760  12116  -2737   -990  -1360       C\\nATOM   2277  CD1 TRP A1126      14.127 -13.586  29.588  1.00102.49           C\\nANISOU 2277  CD1 TRP A1126    13224  13259  12460  -2750  -1458  -1549       C\\nATOM   2278  CD2 TRP A1126      16.280 -14.113  29.895  1.00100.88           C\\nANISOU 2278  CD2 TRP A1126    13796  12592  11940  -2519   -920  -1236       C\\nATOM   2279  NE1 TRP A1126      14.782 -13.387  28.397  1.00102.69           N\\nANISOU 2279  NE1 TRP A1126    13720  13132  12164  -2582  -1684  -1520       N\\nATOM   2280  CE2 TRP A1126      16.105 -13.705  28.559  1.00102.48           C\\nANISOU 2280  CE2 TRP A1126    14155  12841  11942  -2447  -1322  -1348       C\\nATOM   2281  CE3 TRP A1126      17.558 -14.494  30.321  1.00101.84           C\\nANISOU 2281  CE3 TRP A1126    14288  12451  11954  -2377   -563  -1048       C\\nATOM   2282  CZ2 TRP A1126      17.157 -13.666  27.646  1.00107.44           C\\nANISOU 2282  CZ2 TRP A1126    15302  13297  12222  -2277  -1308  -1288       C\\nATOM   2283  CZ3 TRP A1126      18.601 -14.457  29.411  1.00101.67           C\\nANISOU 2283  CZ3 TRP A1126    14713  12253  11664  -2171   -560  -1020       C\\nATOM   2284  CH2 TRP A1126      18.393 -14.051  28.088  1.00104.96           C\\nANISOU 2284  CH2 TRP A1126    15284  12756  11842  -2142   -895  -1146       C\\nATOM   2285  N   ASP A1127      13.370 -16.667  33.848  1.00105.05           N\\nANISOU 2285  N   ASP A1127    13142  13500  13273  -4040    -10  -1251       N\\nATOM   2286  CA  ASP A1127      12.801 -16.985  35.152  1.00105.65           C\\nANISOU 2286  CA  ASP A1127    12891  13805  13446  -4403    350  -1159       C\\nATOM   2287  C   ASP A1127      13.638 -18.034  35.873  1.00102.58           C\\nANISOU 2287  C   ASP A1127    13044  13002  12929  -4604    661   -828       C\\nATOM   2288  O   ASP A1127      14.085 -17.819  37.005  1.00 97.10           O\\nANISOU 2288  O   ASP A1127    12362  12413  12117  -4531    958   -598       O\\nATOM   2289  CB  ASP A1127      11.355 -17.458  34.988  1.00113.14           C\\nANISOU 2289  CB  ASP A1127    13346  15002  14642  -4937    260  -1403       C\\nATOM   2290  N   GLU A1128      13.877 -19.175  35.221  1.00105.05           N\\nANISOU 2290  N   GLU A1128    13834  12818  13263  -4840    560   -812       N\\nATOM   2291  CA  GLU A1128      14.589 -20.266  35.881  1.00101.37           C\\nANISOU 2291  CA  GLU A1128    13890  11878  12749  -5036    788   -497       C\\nATOM   2292  C   GLU A1128      16.064 -19.940  36.072  1.00 98.59           C\\nANISOU 2292  C   GLU A1128    13939  11292  12227  -4482    856   -278       C\\nATOM   2293  O   GLU A1128      16.652 -20.294  37.101  1.00 98.75           O\\nANISOU 2293  O   GLU A1128    14183  11164  12175  -4507   1075     48       O\\nATOM   2294  CB  GLU A1128      14.433 -21.557  35.083  1.00102.72           C\\nANISOU 2294  CB  GLU A1128    14465  11516  13047  -5400    625   -601       C\\nATOM   2295  CG  GLU A1128      13.004 -22.014  34.909  1.00109.16           C\\nANISOU 2295  CG  GLU A1128    14894  12518  14063  -6031    538   -807       C\\nATOM   2296  CD  GLU A1128      12.920 -23.465  34.496  1.00117.05           C\\nANISOU 2296  CD  GLU A1128    16374  12895  15205  -6501    444   -827       C\\nATOM   2297  OE1 GLU A1128      13.445 -24.324  35.236  1.00119.18           O\\nANISOU 2297  OE1 GLU A1128    17078  12716  15487  -6681    639   -499       O\\nATOM   2298  OE2 GLU A1128      12.343 -23.744  33.426  1.00122.20           O\\nANISOU 2298  OE2 GLU A1128    16997  13477  15956  -6685    137  -1171       O\\nATOM   2299  N   ALA A1129      16.686 -19.280  35.090  1.00106.39           N\\nANISOU 2299  N   ALA A1129    15026  12259  13140  -4007    658   -438       N\\nATOM   2300  CA  ALA A1129      18.089 -18.904  35.232  1.00 98.44           C\\nANISOU 2300  CA  ALA A1129    14315  11087  12002  -3503    734   -256       C\\nATOM   2301  C   ALA A1129      18.313 -18.065  36.481  1.00 99.96           C\\nANISOU 2301  C   ALA A1129    14247  11624  12110  -3345    925    -40       C\\nATOM   2302  O   ALA A1129      19.394 -18.111  37.080  1.00 91.71           O\\nANISOU 2302  O   ALA A1129    13458  10403  10986  -3100   1037    208       O\\nATOM   2303  CB  ALA A1129      18.562 -18.146  33.991  1.00 90.27           C\\nANISOU 2303  CB  ALA A1129    13335  10100  10864  -3097    524   -462       C\\nATOM   2304  N   ALA A1130      17.300 -17.301  36.894  1.00101.90           N\\nANISOU 2304  N   ALA A1130    13969  12366  12382  -3472    950   -165       N\\nATOM   2305  CA  ALA A1130      17.396 -16.557  38.143  1.00100.47           C\\nANISOU 2305  CA  ALA A1130    13541  12535  12097  -3370   1159    -30       C\\nATOM   2306  C   ALA A1130      17.236 -17.478  39.344  1.00 96.24           C\\nANISOU 2306  C   ALA A1130    13135  11951  11481  -3804   1437    243       C\\nATOM   2307  O   ALA A1130      17.958 -17.340  40.339  1.00 91.99           O\\nANISOU 2307  O   ALA A1130    12752  11434  10767  -3682   1586    498       O\\nATOM   2308  CB  ALA A1130      16.348 -15.446  38.172  1.00102.74           C\\nANISOU 2308  CB  ALA A1130    13205  13359  12471  -3324   1106   -319       C\\nATOM   2309  N   VAL A1131      16.303 -18.428  39.267  1.00 92.07           N\\nANISOU 2309  N   VAL A1131    12568  11350  11062  -4347   1484    213       N\\nATOM   2310  CA  VAL A1131      16.030 -19.294  40.409  1.00 92.71           C\\nANISOU 2310  CA  VAL A1131    12779  11404  11044  -4858   1755    513       C\\nATOM   2311  C   VAL A1131      17.210 -20.220  40.681  1.00 93.11           C\\nANISOU 2311  C   VAL A1131    13506  10845  11028  -4781   1726    899       C\\nATOM   2312  O   VAL A1131      17.533 -20.509  41.839  1.00 94.49           O\\nANISOU 2312  O   VAL A1131    13879  11018  11005  -4935   1900   1255       O\\nATOM   2313  CB  VAL A1131      14.728 -20.083  40.179  1.00 91.93           C\\nANISOU 2313  CB  VAL A1131    12455  11353  11120  -5514   1797    386       C\\nATOM   2314  N   ASN A1132      17.877 -20.696  39.626  1.00 98.73           N\\nANISOU 2314  N   ASN A1132    14580  11039  11893  -4528   1494    823       N\\nATOM   2315  CA  ASN A1132      19.028 -21.572  39.827  1.00 99.57           C\\nANISOU 2315  CA  ASN A1132    15279  10537  12016  -4371   1439   1132       C\\nATOM   2316  C   ASN A1132      20.208 -20.804  40.407  1.00 98.88           C\\nANISOU 2316  C   ASN A1132    15239  10564  11768  -3840   1452   1311       C\\nATOM   2317  O   ASN A1132      20.866 -21.282  41.338  1.00106.13           O\\nANISOU 2317  O   ASN A1132    16469  11262  12593  -3844   1482   1689       O\\nATOM   2318  CB  ASN A1132      19.417 -22.244  38.508  1.00100.70           C\\nANISOU 2318  CB  ASN A1132    15748  10141  12372  -4206   1226    906       C\\nATOM   2319  CG  ASN A1132      20.355 -23.432  38.702  1.00102.63           C\\nANISOU 2319  CG  ASN A1132    16592   9660  12743  -4136   1159   1173       C\\nATOM   2320  OD1 ASN A1132      21.259 -23.402  39.538  1.00 99.29           O\\nANISOU 2320  OD1 ASN A1132    16345   9141  12242  -3883   1185   1501       O\\nATOM   2321  ND2 ASN A1132      20.136 -24.489  37.929  1.00107.31           N\\nANISOU 2321  ND2 ASN A1132    17502   9719  13554  -4348   1034   1014       N\\nATOM   2322  N   LEU A1133      20.483 -19.606  39.881  1.00 85.10           N\\nANISOU 2322  N   LEU A1133    13195   9149   9988  -3405   1394   1062       N\\nATOM   2323  CA  LEU A1133      21.652 -18.849  40.317  1.00 79.83           C\\nANISOU 2323  CA  LEU A1133    12558   8566   9209  -2920   1377   1196       C\\nATOM   2324  C   LEU A1133      21.591 -18.470  41.792  1.00 85.06           C\\nANISOU 2324  C   LEU A1133    13112   9576   9629  -3048   1529   1445       C\\nATOM   2325  O   LEU A1133      22.638 -18.221  42.399  1.00 82.43           O\\nANISOU 2325  O   LEU A1133    12927   9198   9193  -2748   1484   1656       O\\nATOM   2326  CB  LEU A1133      21.813 -17.596  39.454  1.00 84.72           C\\nANISOU 2326  CB  LEU A1133    12879   9469   9842  -2527   1283    893       C\\nATOM   2327  CG  LEU A1133      22.459 -17.798  38.079  1.00 88.21           C\\nANISOU 2327  CG  LEU A1133    13529   9583  10405  -2245   1143    716       C\\nATOM   2328  CD1 LEU A1133      22.334 -16.537  37.242  1.00 90.94           C\\nANISOU 2328  CD1 LEU A1133    13587  10258  10710  -1997   1039    463       C\\nATOM   2329  CD2 LEU A1133      23.920 -18.203  38.219  1.00 83.43           C\\nANISOU 2329  CD2 LEU A1133    13242   8615   9844  -1895   1135    911       C\\nATOM   2330  N   ALA A1134      20.399 -18.433  42.386  1.00 84.49           N\\nANISOU 2330  N   ALA A1134    12774   9880   9449  -3501   1713   1404       N\\nATOM   2331  CA  ALA A1134      20.263 -18.129  43.804  1.00 83.30           C\\nANISOU 2331  CA  ALA A1134    12544  10115   8992  -3684   1912   1604       C\\nATOM   2332  C   ALA A1134      20.570 -19.322  44.697  1.00 95.28           C\\nANISOU 2332  C   ALA A1134    14547  11297  10359  -4027   1952   2087       C\\nATOM   2333  O   ALA A1134      20.536 -19.181  45.925  1.00100.46           O\\nANISOU 2333  O   ALA A1134    15234  12260  10675  -4222   2106   2315       O\\nATOM   2334  CB  ALA A1134      18.855 -17.614  44.103  1.00 88.70           C\\nANISOU 2334  CB  ALA A1134    12701  11389   9612  -4038   2147   1331       C\\nATOM   2335  N   LYS A1135      20.860 -20.486  44.116  1.00 88.10           N\\nANISOU 2335  N   LYS A1135    14044   9751   9678  -4109   1800   2243       N\\nATOM   2336  CA  LYS A1135      21.205 -21.680  44.871  1.00 87.20           C\\nANISOU 2336  CA  LYS A1135    14461   9179   9491  -4398   1755   2737       C\\nATOM   2337  C   LYS A1135      22.701 -21.967  44.852  1.00 86.32           C\\nANISOU 2337  C   LYS A1135    14744   8566   9488  -3866   1479   2966       C\\nATOM   2338  O   LYS A1135      23.109 -23.103  45.109  1.00102.38           O\\nANISOU 2338  O   LYS A1135    17270  10011  11619  -3979   1327   3328       O\\nATOM   2339  CB  LYS A1135      20.432 -22.884  44.332  1.00 91.82           C\\nANISOU 2339  CB  LYS A1135    15253   9320  10313  -4902   1752   2756       C\\nATOM   2340  N   SER A1136      23.523 -20.968  44.553  1.00 82.36           N\\nANISOU 2340  N   SER A1136    14022   8267   9005  -3296   1395   2765       N\\nATOM   2341  CA  SER A1136      24.959 -21.160  44.431  1.00 83.52           C\\nANISOU 2341  CA  SER A1136    14419   8004   9312  -2765   1149   2911       C\\nATOM   2342  C   SER A1136      25.684 -20.619  45.656  1.00 88.67           C\\nANISOU 2342  C   SER A1136    15092   8930   9667  -2607   1075   3205       C\\nATOM   2343  O   SER A1136      25.148 -19.816  46.424  1.00 92.03           O\\nANISOU 2343  O   SER A1136    15281   9935   9752  -2806   1240   3175       O\\nATOM   2344  CB  SER A1136      25.494 -20.477  43.171  1.00 79.24           C\\nANISOU 2344  CB  SER A1136    13626   7476   9007  -2270   1101   2495       C\\nATOM   2345  OG  SER A1136      25.423 -19.068  43.285  1.00 73.97           O\\nANISOU 2345  OG  SER A1136    12540   7401   8165  -2108   1183   2288       O\\nATOM   2346  N   ARG A1137      26.926 -21.078  45.832  1.00 91.39           N\\nANISOU 2346  N   ARG A1137    15712   8855  10158  -2229    806   3459       N\\nATOM   2347  CA  ARG A1137      27.767 -20.540  46.894  1.00 91.41           C\\nANISOU 2347  CA  ARG A1137    15721   9100   9909  -2019    652   3712       C\\nATOM   2348  C   ARG A1137      28.177 -19.101  46.613  1.00 85.85           C\\nANISOU 2348  C   ARG A1137    14558   8882   9179  -1656    695   3357       C\\nATOM   2349  O   ARG A1137      28.655 -18.413  47.521  1.00 85.58           O\\nANISOU 2349  O   ARG A1137    14453   9182   8883  -1561    604   3470       O\\nATOM   2350  CB  ARG A1137      29.009 -21.414  47.089  1.00 94.63           C\\nANISOU 2350  CB  ARG A1137    16484   8915  10557  -1666    293   4057       C\\nATOM   2351  N   TRP A1138      28.013 -18.639  45.372  1.00 85.61           N\\nANISOU 2351  N   TRP A1138    14253   8876   9400  -1476    803   2943       N\\nATOM   2352  CA  TRP A1138      28.240 -17.235  45.053  1.00 83.05           C\\nANISOU 2352  CA  TRP A1138    13523   8984   9049  -1214    846   2628       C\\nATOM   2353  C   TRP A1138      27.118 -16.360  45.596  1.00 83.65           C\\nANISOU 2353  C   TRP A1138    13343   9618   8821  -1522   1044   2460       C\\nATOM   2354  O   TRP A1138      27.378 -15.303  46.181  1.00 74.31           O\\nANISOU 2354  O   TRP A1138    11960   8813   7461  -1395   1022   2377       O\\nATOM   2355  CB  TRP A1138      28.387 -17.069  43.541  1.00 81.72           C\\nANISOU 2355  CB  TRP A1138    13205   8653   9191   -970    885   2291       C\\nATOM   2356  CG  TRP A1138      28.200 -15.675  43.038  1.00 80.37           C\\nANISOU 2356  CG  TRP A1138    12659   8893   8984   -845    952   1971       C\\nATOM   2357  CD1 TRP A1138      29.008 -14.601  43.270  1.00 79.75           C\\nANISOU 2357  CD1 TRP A1138    12375   9046   8880   -571    866   1931       C\\nATOM   2358  CD2 TRP A1138      27.151 -15.209  42.179  1.00 79.40           C\\nANISOU 2358  CD2 TRP A1138    12339   8950   8882   -990   1065   1659       C\\nATOM   2359  NE1 TRP A1138      28.520 -13.492  42.620  1.00 74.10           N\\nANISOU 2359  NE1 TRP A1138    11385   8600   8171   -543    925   1634       N\\nATOM   2360  CE2 TRP A1138      27.381 -13.840  41.944  1.00 77.74           C\\nANISOU 2360  CE2 TRP A1138    11841   9040   8657   -775   1031   1470       C\\nATOM   2361  CE3 TRP A1138      26.036 -15.814  41.592  1.00 70.14           C\\nANISOU 2361  CE3 TRP A1138    11201   7697   7754  -1292   1152   1527       C\\nATOM   2362  CZ2 TRP A1138      26.539 -13.069  41.149  1.00 75.61           C\\nANISOU 2362  CZ2 TRP A1138    11345   8968   8416   -815   1054   1185       C\\nATOM   2363  CZ3 TRP A1138      25.201 -15.044  40.801  1.00 72.99           C\\nANISOU 2363  CZ3 TRP A1138    11290   8307   8136  -1332   1174   1217       C\\nATOM   2364  CH2 TRP A1138      25.457 -13.689  40.588  1.00 72.54           C\\nANISOU 2364  CH2 TRP A1138    10974   8524   8064  -1078   1113   1063       C\\nATOM   2365  N   TYR A1139      25.867 -16.790  45.424  1.00 82.65           N\\nANISOU 2365  N   TYR A1139    13198   9549   8658  -1927   1233   2375       N\\nATOM   2366  CA  TYR A1139      24.743 -16.053  45.987  1.00 86.12           C\\nANISOU 2366  CA  TYR A1139    13337  10541   8845  -2219   1452   2182       C\\nATOM   2367  C   TYR A1139      24.771 -16.040  47.509  1.00 83.42           C\\nANISOU 2367  C   TYR A1139    13129  10492   8073  -2444   1516   2445       C\\nATOM   2368  O   TYR A1139      24.214 -15.122  48.120  1.00 85.20           O\\nANISOU 2368  O   TYR A1139    13075  11244   8055  -2528   1680   2223       O\\nATOM   2369  CB  TYR A1139      23.424 -16.647  45.483  1.00 93.06           C\\nANISOU 2369  CB  TYR A1139    14126  11418   9815  -2639   1632   2048       C\\nATOM   2370  CG  TYR A1139      22.187 -15.947  45.998  1.00 97.27           C\\nANISOU 2370  CG  TYR A1139    14256  12545  10156  -2931   1887   1793       C\\nATOM   2371  CD1 TYR A1139      21.714 -14.791  45.393  1.00 97.09           C\\nANISOU 2371  CD1 TYR A1139    13784  12829  10275  -2703   1891   1360       C\\nATOM   2372  CD2 TYR A1139      21.487 -16.449  47.086  1.00101.31           C\\nANISOU 2372  CD2 TYR A1139    14831  13310  10352  -3435   2125   1984       C\\nATOM   2373  CE1 TYR A1139      20.582 -14.152  45.862  1.00 98.45           C\\nANISOU 2373  CE1 TYR A1139    13534  13534  10340  -2906   2113   1072       C\\nATOM   2374  CE2 TYR A1139      20.357 -15.817  47.560  1.00102.23           C\\nANISOU 2374  CE2 TYR A1139    14515  14020  10307  -3689   2412   1691       C\\nATOM   2375  CZ  TYR A1139      19.909 -14.671  46.946  1.00 98.03           C\\nANISOU 2375  CZ  TYR A1139    13492  13774   9981  -3392   2400   1210       C\\nATOM   2376  OH  TYR A1139      18.781 -14.044  47.424  1.00 96.25           O\\nANISOU 2376  OH  TYR A1139    12784  14130   9656  -3586   2677    868       O\\nATOM   2377  N   ASN A1140      25.410 -17.028  48.134  1.00 84.98           N\\nANISOU 2377  N   ASN A1140    13766  10358   8165  -2531   1372   2902       N\\nATOM   2378  CA  ASN A1140      25.511 -17.069  49.585  1.00 81.09           C\\nANISOU 2378  CA  ASN A1140    13485  10139   7189  -2767   1384   3212       C\\nATOM   2379  C   ASN A1140      26.720 -16.316  50.123  1.00 81.14           C\\nANISOU 2379  C   ASN A1140    13495  10255   7081  -2354   1121   3259       C\\nATOM   2380  O   ASN A1140      26.732 -15.963  51.308  1.00 91.34           O\\nANISOU 2380  O   ASN A1140    14868  11933   7905  -2514   1139   3371       O\\nATOM   2381  CB  ASN A1140      25.564 -18.521  50.073  1.00 83.93           C\\nANISOU 2381  CB  ASN A1140    14351  10066   7474  -3090   1289   3738       C\\nATOM   2382  CG  ASN A1140      24.263 -19.268  49.834  1.00 88.69           C\\nANISOU 2382  CG  ASN A1140    14898  10646   8154  -3583   1553   3682       C\\nATOM   2383  OD1 ASN A1140      23.328 -19.182  50.631  1.00 94.13           O\\nANISOU 2383  OD1 ASN A1140    15427  11795   8542  -3964   1814   3633       O\\nATOM   2384  ND2 ASN A1140      24.203 -20.015  48.739  1.00 88.26           N\\nANISOU 2384  ND2 ASN A1140    14971  10056   8508  -3583   1485   3663       N\\nATOM   2385  N   GLN A1141      27.731 -16.058  49.292  1.00 79.05           N\\nANISOU 2385  N   GLN A1141    13135   9692   7209  -1861    889   3159       N\\nATOM   2386  CA  GLN A1141      28.944 -15.389  49.751  1.00 83.34           C\\nANISOU 2386  CA  GLN A1141    13640  10316   7710  -1493    612   3207       C\\nATOM   2387  C   GLN A1141      28.857 -13.872  49.622  1.00 86.83           C\\nANISOU 2387  C   GLN A1141    13669  11193   8130  -1321    691   2761       C\\nATOM   2388  O   GLN A1141      29.270 -13.148  50.534  1.00 90.33           O\\nANISOU 2388  O   GLN A1141    14085  11948   8290  -1274    578   2742       O\\nATOM   2389  CB  GLN A1141      30.158 -15.908  48.974  1.00 81.76           C\\nANISOU 2389  CB  GLN A1141    13505   9595   7966  -1066    339   3330       C\\nATOM   2390  N   THR A1142      28.341 -13.378  48.497  1.00 81.15           N\\nANISOU 2390  N   THR A1142    12660  10468   7708  -1228    841   2404       N\\nATOM   2391  CA  THR A1142      28.099 -11.952  48.276  1.00 75.62           C\\nANISOU 2391  CA  THR A1142    11594  10099   7040  -1081    896   1987       C\\nATOM   2392  C   THR A1142      26.654 -11.815  47.825  1.00 80.15           C\\nANISOU 2392  C   THR A1142    11953  10861   7638  -1313   1170   1698       C\\nATOM   2393  O   THR A1142      26.373 -11.645  46.629  1.00 76.21           O\\nANISOU 2393  O   THR A1142    11292  10208   7456  -1195   1180   1504       O\\nATOM   2394  CB  THR A1142      29.064 -11.368  47.245  1.00 71.01           C\\nANISOU 2394  CB  THR A1142    10854   9291   6836   -689    721   1873       C\\nATOM   2395  OG1 THR A1142      28.852 -12.004  45.979  1.00 61.90           O\\nANISOU 2395  OG1 THR A1142     9720   7819   5981   -656    792   1847       O\\nATOM   2396  CG2 THR A1142      30.507 -11.581  47.678  1.00 64.20           C\\nANISOU 2396  CG2 THR A1142    10120   8261   6011   -463    447   2144       C\\nATOM   2397  N   PRO A1143      25.702 -11.890  48.760  1.00 78.66           N\\nANISOU 2397  N   PRO A1143    11743  11039   7106  -1659   1396   1658       N\\nATOM   2398  CA  PRO A1143      24.288 -11.947  48.355  1.00 77.44           C\\nANISOU 2398  CA  PRO A1143    11332  11073   7019  -1917   1663   1400       C\\nATOM   2399  C   PRO A1143      23.754 -10.645  47.786  1.00 81.38           C\\nANISOU 2399  C   PRO A1143    11396  11793   7731  -1681   1672    913       C\\nATOM   2400  O   PRO A1143      22.964 -10.679  46.836  1.00 67.23           O\\nANISOU 2400  O   PRO A1143     9390   9947   6208  -1709   1715    723       O\\nATOM   2401  CB  PRO A1143      23.575 -12.337  49.655  1.00 74.02           C\\nANISOU 2401  CB  PRO A1143    10976  11033   6115  -2363   1931   1502       C\\nATOM   2402  CG  PRO A1143      24.484 -11.856  50.733  1.00 74.95           C\\nANISOU 2402  CG  PRO A1143    11275  11318   5883  -2235   1792   1614       C\\nATOM   2403  CD  PRO A1143      25.873 -12.037  50.213  1.00 80.85           C\\nANISOU 2403  CD  PRO A1143    12236  11590   6893  -1870   1423   1866       C\\nATOM   2404  N   ASN A1144      24.148  -9.498  48.346  1.00 79.84           N\\nANISOU 2404  N   ASN A1144    11080  11820   7435  -1453   1593    702       N\\nATOM   2405  CA  ASN A1144      23.656  -8.219  47.839  1.00 82.18           C\\nANISOU 2405  CA  ASN A1144    11000  12248   7977  -1203   1550    249       C\\nATOM   2406  C   ASN A1144      24.024  -8.031  46.372  1.00 83.32           C\\nANISOU 2406  C   ASN A1144    11122  12002   8536   -947   1323    262       C\\nATOM   2407  O   ASN A1144      23.168  -7.712  45.538  1.00 77.89           O\\nANISOU 2407  O   ASN A1144    10184  11322   8089   -907   1317     25       O\\nATOM   2408  CB  ASN A1144      24.209  -7.072  48.683  1.00 86.17           C\\nANISOU 2408  CB  ASN A1144    11466  12947   8328   -999   1448     44       C\\nATOM   2409  CG  ASN A1144      23.399  -6.831  49.942  1.00 91.58           C\\nANISOU 2409  CG  ASN A1144    12020  14149   8626  -1210   1730   -220       C\\nATOM   2410  OD1 ASN A1144      22.445  -6.054  49.938  1.00 89.43           O\\nANISOU 2410  OD1 ASN A1144    11378  14135   8467  -1137   1861   -680       O\\nATOM   2411  ND2 ASN A1144      23.778  -7.496  51.028  1.00 95.06           N\\nANISOU 2411  ND2 ASN A1144    12763  14756   8600  -1466   1818     62       N\\nATOM   2412  N   ARG A1145      25.302  -8.228  46.040  1.00 83.54           N\\nANISOU 2412  N   ARG A1145    11397  11711   8633   -780   1132    536       N\\nATOM   2413  CA  ARG A1145      25.740  -8.103  44.655  1.00 77.75           C\\nANISOU 2413  CA  ARG A1145    10673  10652   8215   -579    973    561       C\\nATOM   2414  C   ARG A1145      25.101  -9.167  43.774  1.00 76.82           C\\nANISOU 2414  C   ARG A1145    10624  10365   8200   -753   1062    630       C\\nATOM   2415  O   ARG A1145      24.721  -8.887  42.631  1.00 82.58           O\\nANISOU 2415  O   ARG A1145    11252  10993   9130   -675    981    488       O\\nATOM   2416  CB  ARG A1145      27.264  -8.189  44.587  1.00 73.67           C\\nANISOU 2416  CB  ARG A1145    10353   9896   7744   -393    814    816       C\\nATOM   2417  CG  ARG A1145      27.829  -8.227  43.179  1.00 69.75           C\\nANISOU 2417  CG  ARG A1145     9893   9104   7505   -234    729    865       C\\nATOM   2418  CD  ARG A1145      29.352  -8.232  43.189  1.00 73.59           C\\nANISOU 2418  CD  ARG A1145    10468   9428   8064    -50    612   1067       C\\nATOM   2419  NE  ARG A1145      29.897  -8.135  41.837  1.00 80.75           N\\nANISOU 2419  NE  ARG A1145    11375  10131   9175     79    594   1070       N\\nATOM   2420  CZ  ARG A1145      31.175  -7.901  41.556  1.00 82.83           C\\nANISOU 2420  CZ  ARG A1145    11612  10298   9561    237    528   1175       C\\nATOM   2421  NH1 ARG A1145      32.054  -7.734  42.535  1.00 82.57           N\\nANISOU 2421  NH1 ARG A1145    11535  10328   9508    307    415   1287       N\\nATOM   2422  NH2 ARG A1145      31.574  -7.829  40.293  1.00 85.74           N\\nANISOU 2422  NH2 ARG A1145    11982  10541  10053    302    578   1158       N\\nATOM   2423  N   ALA A1146      24.974 -10.393  44.287  1.00 78.38           N\\nANISOU 2423  N   ALA A1146    11025  10507   8249  -1011   1196    857       N\\nATOM   2424  CA  ALA A1146      24.412 -11.480  43.491  1.00 77.28           C\\nANISOU 2424  CA  ALA A1146    10992  10148   8224  -1212   1259    913       C\\nATOM   2425  C   ALA A1146      22.965 -11.191  43.114  1.00 83.69           C\\nANISOU 2425  C   ALA A1146    11482  11202   9113  -1389   1341    610       C\\nATOM   2426  O   ALA A1146      22.575 -11.340  41.951  1.00 81.20           O\\nANISOU 2426  O   ALA A1146    11127  10738   8988  -1380   1252    495       O\\nATOM   2427  CB  ALA A1146      24.519 -12.800  44.253  1.00 75.31           C\\nANISOU 2427  CB  ALA A1146    11049   9751   7813  -1491   1359   1239       C\\nATOM   2428  N   LYS A1147      22.154 -10.771  44.090  1.00 81.29           N\\nANISOU 2428  N   LYS A1147    10927  11303   8657  -1547   1506    451       N\\nATOM   2429  CA  LYS A1147      20.760 -10.442  43.804  1.00 80.52           C\\nANISOU 2429  CA  LYS A1147    10420  11486   8686  -1680   1585    116       C\\nATOM   2430  C   LYS A1147      20.649  -9.302  42.799  1.00 83.83           C\\nANISOU 2430  C   LYS A1147    10611  11866   9377  -1325   1329   -152       C\\nATOM   2431  O   LYS A1147      19.710  -9.273  41.995  1.00 68.30           O\\nANISOU 2431  O   LYS A1147     8403   9940   7609  -1375   1246   -350       O\\nATOM   2432  CB  LYS A1147      20.023 -10.088  45.098  1.00 67.35           C\\nANISOU 2432  CB  LYS A1147     8483  10311   6797  -1863   1853    -63       C\\nATOM   2433  N   ARG A1148      21.599  -8.365  42.815  1.00 85.54           N\\nANISOU 2433  N   ARG A1148    10910  11984   9606   -988   1167   -140       N\\nATOM   2434  CA  ARG A1148      21.574  -7.277  41.842  1.00 79.68           C\\nANISOU 2434  CA  ARG A1148    10031  11139   9107   -685    892   -317       C\\nATOM   2435  C   ARG A1148      21.891  -7.783  40.437  1.00 82.33           C\\nANISOU 2435  C   ARG A1148    10589  11152   9539   -673    733   -165       C\\nATOM   2436  O   ARG A1148      21.289  -7.330  39.457  1.00 90.33           O\\nANISOU 2436  O   ARG A1148    11469  12136  10717   -591    526   -312       O\\nATOM   2437  CB  ARG A1148      22.555  -6.182  42.261  1.00 70.66           C\\nANISOU 2437  CB  ARG A1148     8952   9944   7952   -403    768   -316       C\\nATOM   2438  CG  ARG A1148      21.892  -4.860  42.620  1.00 71.12           C\\nANISOU 2438  CG  ARG A1148     8676  10192   8155   -198    669   -688       C\\nATOM   2439  CD  ARG A1148      22.475  -4.260  43.892  1.00 73.19           C\\nANISOU 2439  CD  ARG A1148     8962  10601   8247   -122    743   -769       C\\nATOM   2440  NE  ARG A1148      23.934  -4.303  43.899  1.00 73.07           N\\nANISOU 2440  NE  ARG A1148     9271  10346   8145    -63    641   -461       N\\nATOM   2441  CZ  ARG A1148      24.686  -4.003  44.953  1.00 72.04           C\\nANISOU 2441  CZ  ARG A1148     9236  10306   7829    -40    656   -444       C\\nATOM   2442  NH1 ARG A1148      24.121  -3.632  46.093  1.00 77.77           N\\nANISOU 2442  NH1 ARG A1148     9809  11363   8378    -79    795   -729       N\\nATOM   2443  NH2 ARG A1148      26.005  -4.075  44.867  1.00 70.75           N\\nANISOU 2443  NH2 ARG A1148     9301   9933   7647     15    532   -167       N\\nATOM   2444  N   VAL A1149      22.824  -8.727  40.321  1.00 86.59           N\\nANISOU 2444  N   VAL A1149    11473  11454   9974   -742    812    112       N\\nATOM   2445  CA  VAL A1149      23.201  -9.252  39.011  1.00 82.53           C\\nANISOU 2445  CA  VAL A1149    11189  10655   9513   -723    713    200       C\\nATOM   2446  C   VAL A1149      22.160 -10.240  38.500  1.00 89.46           C\\nANISOU 2446  C   VAL A1149    12052  11515  10424  -1007    747    112       C\\nATOM   2447  O   VAL A1149      21.841 -10.260  37.304  1.00 88.71           O\\nANISOU 2447  O   VAL A1149    11995  11326  10387  -1003    583     17       O\\nATOM   2448  CB  VAL A1149      24.603  -9.881  39.089  1.00 69.15           C\\nANISOU 2448  CB  VAL A1149     9812   8710   7751   -638    790    459       C\\nATOM   2449  CG1 VAL A1149      24.961 -10.583  37.793  1.00 62.41           C\\nANISOU 2449  CG1 VAL A1149     9197   7590   6927   -632    765    483       C\\nATOM   2450  CG2 VAL A1149      25.636  -8.812  39.423  1.00 65.57           C\\nANISOU 2450  CG2 VAL A1149     9323   8286   7303   -385    710    522       C\\nATOM   2451  N   ILE A1150      21.606 -11.063  39.394  1.00 84.73           N\\nANISOU 2451  N   ILE A1150    11413  11014   9767  -1295    945    151       N\\nATOM   2452  CA  ILE A1150      20.566 -12.008  38.997  1.00 83.24           C\\nANISOU 2452  CA  ILE A1150    11179  10809   9639  -1639    980     64       C\\nATOM   2453  C   ILE A1150      19.315 -11.263  38.545  1.00 84.16           C\\nANISOU 2453  C   ILE A1150    10861  11211   9905  -1651    831   -246       C\\nATOM   2454  O   ILE A1150      18.622 -11.692  37.612  1.00 93.69           O\\nANISOU 2454  O   ILE A1150    12028  12360  11209  -1807    688   -369       O\\nATOM   2455  CB  ILE A1150      20.272 -12.986  40.152  1.00 84.83           C\\nANISOU 2455  CB  ILE A1150    11442  11060   9730  -2003   1240    225       C\\nATOM   2456  CG1 ILE A1150      21.486 -13.878  40.414  1.00 82.12           C\\nANISOU 2456  CG1 ILE A1150    11568  10333   9299  -1964   1285    553       C\\nATOM   2457  CG2 ILE A1150      19.059 -13.839  39.844  1.00 86.81           C\\nANISOU 2457  CG2 ILE A1150    11564  11344  10076  -2432   1287    113       C\\nATOM   2458  CD1 ILE A1150      21.367 -14.717  41.663  1.00 70.60           C\\nANISOU 2458  CD1 ILE A1150    10253   8891   7682  -2294   1484    806       C\\nATOM   2459  N   THR A1151      19.009 -10.131  39.188  1.00 79.62           N\\nANISOU 2459  N   THR A1151     9946  10934   9371  -1467    829   -404       N\\nATOM   2460  CA  THR A1151      17.920  -9.283  38.713  1.00 85.27           C\\nANISOU 2460  CA  THR A1151    10223  11875  10301  -1363    618   -716       C\\nATOM   2461  C   THR A1151      18.194  -8.785  37.302  1.00 88.73           C\\nANISOU 2461  C   THR A1151    10820  12078  10815  -1128    245   -709       C\\nATOM   2462  O   THR A1151      17.290  -8.744  36.460  1.00 89.80           O\\nANISOU 2462  O   THR A1151    10761  12268  11090  -1177     -2   -876       O\\nATOM   2463  CB  THR A1151      17.713  -8.098  39.655  1.00 85.11           C\\nANISOU 2463  CB  THR A1151     9861  12141  10338  -1127    668   -919       C\\nATOM   2464  OG1 THR A1151      17.364  -8.577  40.957  1.00 90.34           O\\nANISOU 2464  OG1 THR A1151    10377  13098  10849  -1398   1046   -947       O\\nATOM   2465  CG2 THR A1151      16.602  -7.194  39.144  1.00 80.06           C\\nANISOU 2465  CG2 THR A1151     8743  11680   9998   -942    398  -1262       C\\nATOM   2466  N   THR A1152      19.440  -8.402  37.023  1.00 89.05           N\\nANISOU 2466  N   THR A1152    11208  11880  10745   -898    191   -508       N\\nATOM   2467  CA  THR A1152      19.772  -7.948  35.679  1.00 88.03           C\\nANISOU 2467  CA  THR A1152    11283  11556  10607   -736   -114   -459       C\\nATOM   2468  C   THR A1152      19.666  -9.080  34.665  1.00 84.57           C\\nANISOU 2468  C   THR A1152    11105  10963  10066   -967   -143   -432       C\\nATOM   2469  O   THR A1152      19.276  -8.846  33.516  1.00 88.93           O\\nANISOU 2469  O   THR A1152    11704  11483  10603   -948   -442   -501       O\\nATOM   2470  CB  THR A1152      21.170  -7.335  35.670  1.00 84.93           C\\nANISOU 2470  CB  THR A1152    11169  10986  10115   -508    -96   -248       C\\nATOM   2471  OG1 THR A1152      21.238  -6.314  36.674  1.00 87.26           O\\nANISOU 2471  OG1 THR A1152    11240  11404  10511   -322    -88   -315       O\\nATOM   2472  CG2 THR A1152      21.473  -6.721  34.321  1.00 75.79           C\\nANISOU 2472  CG2 THR A1152    10215   9677   8903   -385   -386   -175       C\\nATOM   2473  N   PHE A1153      19.988 -10.311  35.069  1.00 80.31           N\\nANISOU 2473  N   PHE A1153    10763  10305   9447  -1189    130   -341       N\\nATOM   2474  CA  PHE A1153      19.838 -11.445  34.163  1.00 86.85           C\\nANISOU 2474  CA  PHE A1153    11850  10938  10209  -1417    102   -378       C\\nATOM   2475  C   PHE A1153      18.375 -11.753  33.876  1.00 94.28           C\\nANISOU 2475  C   PHE A1153    12493  12048  11280  -1692    -61   -605       C\\nATOM   2476  O   PHE A1153      18.051 -12.271  32.802  1.00 97.03           O\\nANISOU 2476  O   PHE A1153    13001  12289  11578  -1834   -250   -712       O\\nATOM   2477  CB  PHE A1153      20.524 -12.681  34.744  1.00 85.98           C\\nANISOU 2477  CB  PHE A1153    12033  10584  10052  -1564    394   -224       C\\nATOM   2478  CG  PHE A1153      21.973 -12.790  34.388  1.00 82.81           C\\nANISOU 2478  CG  PHE A1153    11993   9932   9541  -1323    479    -73       C\\nATOM   2479  CD1 PHE A1153      22.400 -12.549  33.096  1.00 87.89           C\\nANISOU 2479  CD1 PHE A1153    12840  10494  10062  -1196    348   -140       C\\nATOM   2480  CD2 PHE A1153      22.908 -13.132  35.345  1.00 77.41           C\\nANISOU 2480  CD2 PHE A1153    11425   9126   8862  -1234    685    132       C\\nATOM   2481  CE1 PHE A1153      23.735 -12.650  32.764  1.00 85.44           C\\nANISOU 2481  CE1 PHE A1153    12792  10012   9660   -991    485    -39       C\\nATOM   2482  CE2 PHE A1153      24.244 -13.233  35.021  1.00 77.07           C\\nANISOU 2482  CE2 PHE A1153    11625   8883   8776   -993    759    238       C\\nATOM   2483  CZ  PHE A1153      24.658 -12.992  33.729  1.00 80.39           C\\nANISOU 2483  CZ  PHE A1153    12194   9251   9099   -874    690    135       C\\nATOM   2484  N   ARG A1154      17.484 -11.446  34.817  1.00 88.53           N\\nANISOU 2484  N   ARG A1154    11311  11612  10713  -1783     15   -710       N\\nATOM   2485  CA  ARG A1154      16.070 -11.771  34.679  1.00 90.56           C\\nANISOU 2485  CA  ARG A1154    11175  12087  11146  -2076    -96   -944       C\\nATOM   2486  C   ARG A1154      15.287 -10.657  33.990  1.00 94.08           C\\nANISOU 2486  C   ARG A1154    11255  12736  11753  -1845   -507  -1151       C\\nATOM   2487  O   ARG A1154      14.589 -10.908  33.004  1.00 98.43           O\\nANISOU 2487  O   ARG A1154    11752  13292  12353  -1977   -823  -1290       O\\nATOM   2488  CB  ARG A1154      15.471 -12.072  36.056  1.00 91.66           C\\nANISOU 2488  CB  ARG A1154    10967  12492  11368  -2333    250   -973       C\\nATOM   2489  CG  ARG A1154      13.953 -12.110  36.087  1.00 98.75           C\\nANISOU 2489  CG  ARG A1154    11273  13741  12505  -2600    179  -1261       C\\nATOM   2490  CD  ARG A1154      13.450 -12.527  37.460  1.00 98.15           C\\nANISOU 2490  CD  ARG A1154    10903  13957  12432  -2937    616  -1264       C\\nATOM   2491  NE  ARG A1154      14.141 -11.809  38.526  1.00 96.23           N\\nANISOU 2491  NE  ARG A1154    10691  13830  12042  -2666    855  -1169       N\\nATOM   2492  CZ  ARG A1154      13.729 -10.656  39.043  1.00 99.35           C\\nANISOU 2492  CZ  ARG A1154    10627  14571  12550  -2384    862  -1413       C\\nATOM   2493  NH1 ARG A1154      12.618 -10.085  38.594  1.00102.81           N\\nANISOU 2493  NH1 ARG A1154    10503  15271  13290  -2299    634  -1752       N\\nATOM   2494  NH2 ARG A1154      14.426 -10.074  40.011  1.00 97.58           N\\nANISOU 2494  NH2 ARG A1154    10500  14418  12157  -2171   1067  -1343       N\\nATOM   2495  N   THR A1155      15.394  -9.425  34.492  1.00 91.70           N\\nANISOU 2495  N   THR A1155    10720  12575  11545  -1493   -553  -1180       N\\nATOM   2496  CA  THR A1155      14.626  -8.327  33.913  1.00 95.66           C\\nANISOU 2496  CA  THR A1155    10869  13211  12265  -1227   -991  -1368       C\\nATOM   2497  C   THR A1155      15.189  -7.887  32.570  1.00 97.84           C\\nANISOU 2497  C   THR A1155    11567  13229  12380  -1038  -1391  -1215       C\\nATOM   2498  O   THR A1155      14.426  -7.500  31.678  1.00103.63           O\\nANISOU 2498  O   THR A1155    12148  14011  13216   -975  -1852  -1325       O\\nATOM   2499  CB  THR A1155      14.590  -7.135  34.871  1.00 96.53           C\\nANISOU 2499  CB  THR A1155    10639  13482  12554   -890   -932  -1480       C\\nATOM   2500  OG1 THR A1155      15.865  -6.481  34.875  1.00 89.26           O\\nANISOU 2500  OG1 THR A1155    10139  12306  11469   -624   -926  -1243       O\\nATOM   2501  CG2 THR A1155      14.254  -7.597  36.282  1.00102.13           C\\nANISOU 2501  CG2 THR A1155    11038  14480  13285  -1108   -443  -1599       C\\nATOM   2502  N   GLY A1156      16.506  -7.938  32.402  1.00 98.59           N\\nANISOU 2502  N   GLY A1156    12176  13074  12209   -961  -1232   -958       N\\nATOM   2503  CA  GLY A1156      17.109  -7.426  31.192  1.00 97.17           C\\nANISOU 2503  CA  GLY A1156    12393  12702  11824   -813  -1538   -796       C\\nATOM   2504  C   GLY A1156      17.208  -5.922  31.139  1.00 94.99           C\\nANISOU 2504  C   GLY A1156    12028  12391  11674   -459  -1843   -727       C\\nATOM   2505  O   GLY A1156      17.414  -5.364  30.057  1.00 94.83           O\\nANISOU 2505  O   GLY A1156    12287  12241  11502   -370  -2199   -582       O\\nATOM   2506  N   THR A1157      17.055  -5.243  32.275  1.00 98.59           N\\nANISOU 2506  N   THR A1157    12130  12944  12386   -269  -1724   -831       N\\nATOM   2507  CA  THR A1157      17.188  -3.793  32.334  1.00 99.99           C\\nANISOU 2507  CA  THR A1157    12241  13012  12740     83  -2014   -798       C\\nATOM   2508  C   THR A1157      18.117  -3.396  33.475  1.00 95.58           C\\nANISOU 2508  C   THR A1157    11722  12408  12187    197  -1666   -741       C\\nATOM   2509  O   THR A1157      18.739  -4.258  34.103  1.00 99.83           O\\nANISOU 2509  O   THR A1157    12385  12993  12552     13  -1238   -673       O\\nATOM   2510  CB  THR A1157      15.819  -3.130  32.503  1.00100.53           C\\nANISOU 2510  CB  THR A1157    11744  13243  13210    283  -2359  -1106       C\\nATOM   2511  N   TRP A1158      18.225  -2.094  33.747  1.00 93.22           N\\nANISOU 2511  N   TRP A1158    11337  11987  12095    500  -1890   -770       N\\nATOM   2512  CA  TRP A1158      19.077  -1.577  34.810  1.00 93.29           C\\nANISOU 2512  CA  TRP A1158    11380  11944  12121    611  -1638   -757       C\\nATOM   2513  C   TRP A1158      18.284  -1.180  36.050  1.00100.83           C\\nANISOU 2513  C   TRP A1158    11839  13130  13343    767  -1520  -1143       C\\nATOM   2514  O   TRP A1158      18.687  -0.262  36.773  1.00104.41           O\\nANISOU 2514  O   TRP A1158    12262  13494  13913    976  -1523  -1234       O\\nATOM   2515  CB  TRP A1158      19.888  -0.380  34.315  1.00 93.24           C\\nANISOU 2515  CB  TRP A1158    11675  11603  12148    796  -1939   -534       C\\nATOM   2516  CG  TRP A1158      20.831  -0.689  33.202  1.00 90.86           C\\nANISOU 2516  CG  TRP A1158    11861  11134  11527    615  -1955   -159       C\\nATOM   2517  CD1 TRP A1158      20.661  -0.401  31.878  1.00 92.31           C\\nANISOU 2517  CD1 TRP A1158    12294  11175  11605    591  -2335     30       C\\nATOM   2518  CD2 TRP A1158      22.100  -1.341  33.312  1.00 84.64           C\\nANISOU 2518  CD2 TRP A1158    11359  10335  10467    435  -1569     52       C\\nATOM   2519  NE1 TRP A1158      21.746  -0.835  31.158  1.00 87.61           N\\nANISOU 2519  NE1 TRP A1158    12125  10516  10649    382  -2146    322       N\\nATOM   2520  CE2 TRP A1158      22.643  -1.417  32.015  1.00 81.33           C\\nANISOU 2520  CE2 TRP A1158    11324   9793   9787    307  -1675    322       C\\nATOM   2521  CE3 TRP A1158      22.829  -1.871  34.381  1.00 79.01           C\\nANISOU 2521  CE3 TRP A1158    10605   9715   9699    377  -1161     35       C\\nATOM   2522  CZ2 TRP A1158      23.881  -2.001  31.759  1.00 77.25           C\\nANISOU 2522  CZ2 TRP A1158    11088   9260   9004    149  -1343    521       C\\nATOM   2523  CZ3 TRP A1158      24.059  -2.452  34.124  1.00 69.87           C\\nANISOU 2523  CZ3 TRP A1158     9733   8502   8314    244   -903    268       C\\nATOM   2524  CH2 TRP A1158      24.572  -2.511  32.824  1.00 69.73           C\\nANISOU 2524  CH2 TRP A1158    10033   8375   8085    144   -972    482       C\\nATOM   2525  N   ASP A1159      17.156  -1.850  36.306  1.00 98.45           N\\nANISOU 2525  N   ASP A1159    11135  13138  13133    646  -1402  -1399       N\\nATOM   2526  CA  ASP A1159      16.331  -1.497  37.457  1.00 97.23           C\\nANISOU 2526  CA  ASP A1159    10456  13283  13205    769  -1227  -1814       C\\nATOM   2527  C   ASP A1159      17.098  -1.638  38.765  1.00 90.66           C\\nANISOU 2527  C   ASP A1159     9725  12569  12151    685   -774  -1819       C\\nATOM   2528  O   ASP A1159      16.820  -0.916  39.727  1.00 92.33           O\\nANISOU 2528  O   ASP A1159     9651  12933  12497    879   -679  -2146       O\\nATOM   2529  CB  ASP A1159      15.076  -2.368  37.498  1.00105.69           C\\nANISOU 2529  CB  ASP A1159    11073  14718  14366    540  -1095  -2046       C\\nATOM   2530  CG  ASP A1159      14.329  -2.379  36.182  1.00109.35           C\\nANISOU 2530  CG  ASP A1159    11447  15092  15007    573  -1581  -2031       C\\nATOM   2531  OD1 ASP A1159      14.839  -2.991  35.220  1.00106.95           O\\nANISOU 2531  OD1 ASP A1159    11588  14593  14457    378  -1693  -1714       O\\nATOM   2532  OD2 ASP A1159      13.231  -1.786  36.115  1.00113.68           O\\nANISOU 2532  OD2 ASP A1159    11472  15783  15940    804  -1860  -2361       O\\nATOM   2533  N   ALA A1160      18.061  -2.558  38.822  1.00 90.75           N\\nANISOU 2533  N   ALA A1160    10142  12514  11824    416   -516  -1483       N\\nATOM   2534  CA  ALA A1160      18.793  -2.777  40.062  1.00 83.07           C\\nANISOU 2534  CA  ALA A1160     9285  11661  10616    322   -147  -1445       C\\nATOM   2535  C   ALA A1160      19.805  -1.671  40.330  1.00 83.07           C\\nANISOU 2535  C   ALA A1160     9492  11427  10644    577   -301  -1398       C\\nATOM   2536  O   ALA A1160      20.159  -1.427  41.488  1.00 80.26           O\\nANISOU 2536  O   ALA A1160     9111  11213  10170    595    -98  -1520       O\\nATOM   2537  CB  ALA A1160      19.490  -4.133  40.023  1.00 69.19           C\\nANISOU 2537  CB  ALA A1160     7878   9858   8554     -5    110  -1098       C\\nATOM   2538  N   TYR A1161      20.270  -0.989  39.289  1.00 85.89           N\\nANISOU 2538  N   TYR A1161    10067  11436  11131    737   -663  -1221       N\\nATOM   2539  CA  TYR A1161      21.312   0.021  39.439  1.00 81.29           C\\nANISOU 2539  CA  TYR A1161     9712  10587  10590    902   -820  -1122       C\\nATOM   2540  C   TYR A1161      20.830   1.413  39.031  1.00 86.56           C\\nANISOU 2540  C   TYR A1161    10259  11009  11620   1221  -1257  -1309       C\\nATOM   2541  O   TYR A1161      19.780   1.882  39.473  1.00 90.75           O\\nANISOU 2541  O   TYR A1161    10405  11678  12398   1423  -1325  -1710       O\\nATOM   2542  CB  TYR A1161      22.541  -0.357  38.608  1.00 78.82           C\\nANISOU 2542  CB  TYR A1161     9822  10037  10089    757   -833   -681       C\\nATOM   2543  CG  TYR A1161      23.144  -1.708  38.932  1.00 79.07           C\\nANISOU 2543  CG  TYR A1161    10004  10209   9831    508   -467   -486       C\\nATOM   2544  CD1 TYR A1161      22.612  -2.876  38.400  1.00 78.87           C\\nANISOU 2544  CD1 TYR A1161     9993  10274   9701    320   -342   -427       C\\nATOM   2545  CD2 TYR A1161      24.263  -1.813  39.748  1.00 75.01           C\\nANISOU 2545  CD2 TYR A1161     9629   9697   9174    468   -297   -359       C\\nATOM   2546  CE1 TYR A1161      23.166  -4.110  38.683  1.00 74.50           C\\nANISOU 2546  CE1 TYR A1161     9613   9760   8934    118    -53   -248       C\\nATOM   2547  CE2 TYR A1161      24.824  -3.042  40.039  1.00 67.83           C\\nANISOU 2547  CE2 TYR A1161     8865   8860   8048    288    -30   -162       C\\nATOM   2548  CZ  TYR A1161      24.272  -4.189  39.504  1.00 71.43           C\\nANISOU 2548  CZ  TYR A1161     9359   9354   8428    123     94   -104       C\\nATOM   2549  OH  TYR A1161      24.829  -5.416  39.787  1.00 69.66           O\\nANISOU 2549  OH  TYR A1161     9313   9118   8037    -32    319     91       O\\nATOM   2550  N   SER A 364      17.508   3.047  36.367  1.00104.00           N\\nATOM   2551  CA  SER A 364      18.568   3.670  35.585  1.00104.92           C\\nATOM   2552  C   SER A 364      18.623   3.097  34.167  1.00111.72           C\\nATOM   2553  O   SER A 364      19.675   3.111  33.526  1.00111.66           O\\nATOM   2554  CB  SER A 364      19.919   3.488  36.282  1.00 97.65           C\\nATOM   2555  N   GLN A 365      17.486   2.600  33.682  1.00122.15           N\\nATOM   2556  CA  GLN A 365      17.397   1.937  32.386  1.00115.38           C\\nATOM   2557  C   GLN A 365      16.553   2.767  31.428  1.00110.61           C\\nATOM   2558  O   GLN A 365      15.419   3.137  31.753  1.00 98.43           O\\nATOM   2559  CB  GLN A 365      16.796   0.536  32.527  1.00106.22           C\\nATOM   2560  N   GLN A 366      17.101   3.039  30.246  1.00120.06           N\\nATOM   2561  CA  GLN A 366      16.385   3.791  29.223  1.00115.06           C\\nATOM   2562  C   GLN A 366      15.363   2.887  28.544  1.00110.82           C\\nATOM   2563  O   GLN A 366      15.719   1.836  27.999  1.00106.83           O\\nATOM   2564  CB  GLN A 366      17.364   4.363  28.199  1.00114.61           C\\nATOM   2565  N   LYS A 367      14.097   3.295  28.574  1.00106.95           N\\nATOM   2566  CA  LYS A 367      13.014   2.529  27.974  1.00112.85           C\\nATOM   2567  C   LYS A 367      12.771   2.895  26.516  1.00109.20           C\\nATOM   2568  O   LYS A 367      11.803   2.410  25.921  1.00103.35           O\\nATOM   2569  CB  LYS A 367      11.727   2.721  28.781  1.00115.42           C\\nATOM   2570  N   GLU A 368      13.626   3.733  25.930  1.00114.20           N\\nATOM   2571  CA  GLU A 368      13.436   4.206  24.566  1.00 99.97           C\\nATOM   2572  C   GLU A 368      14.152   3.361  23.525  1.00100.67           C\\nATOM   2573  O   GLU A 368      13.805   3.444  22.342  1.00 97.34           O\\nATOM   2574  CB  GLU A 368      13.920   5.655  24.437  1.00 81.44           C\\nATOM   2575  CG  GLU A 368      13.087   6.681  25.188  1.00 79.48           C\\nATOM   2576  CD  GLU A 368      11.923   7.216  24.368  1.00 87.69           C\\nATOM   2577  OE1 GLU A 368      11.484   6.529  23.419  1.00 87.57           O\\nATOM   2578  OE2 GLU A 368      11.451   8.332  24.674  1.00 90.78           O\\nATOM   2579  N   LYS A 369      15.139   2.557  23.932  1.00101.97           N\\nATOM   2580  CA  LYS A 369      15.965   1.842  22.963  1.00 93.96           C\\nATOM   2581  C   LYS A 369      15.123   0.959  22.051  1.00 87.89           C\\nATOM   2582  O   LYS A 369      15.377   0.886  20.844  1.00 84.82           O\\nATOM   2583  CB  LYS A 369      17.025   1.012  23.689  1.00 94.15           C\\nATOM   2584  N   LYS A 370      14.107   0.291  22.605  1.00 95.07           N\\nATOM   2585  CA  LYS A 370      13.254  -0.567  21.787  1.00 92.51           C\\nATOM   2586  C   LYS A 370      12.587   0.220  20.665  1.00 85.60           C\\nATOM   2587  O   LYS A 370      12.454  -0.280  19.541  1.00 77.93           O\\nATOM   2588  CB  LYS A 370      12.203  -1.254  22.662  1.00 85.65           C\\nATOM   2589  N   ALA A 371      12.167   1.454  20.944  1.00 85.70           N\\nATOM   2590  CA  ALA A 371      11.556   2.271  19.901  1.00 78.85           C\\nATOM   2591  C   ALA A 371      12.589   2.776  18.902  1.00 73.40           C\\nATOM   2592  O   ALA A 371      12.274   2.940  17.718  1.00 67.94           O\\nATOM   2593  CB  ALA A 371      10.805   3.440  20.520  1.00 20.00           C\\nATOM   2594  N   THR A 372      13.820   3.030  19.357  1.00 75.36           N\\nATOM   2595  CA  THR A 372      14.875   3.470  18.451  1.00 64.07           C\\nATOM   2596  C   THR A 372      15.326   2.343  17.535  1.00 71.79           C\\nATOM   2597  O   THR A 372      15.714   2.593  16.389  1.00 80.74           O\\nATOM   2598  CB  THR A 372      16.066   4.010  19.246  1.00 69.33           C\\nATOM   2599  OG1 THR A 372      15.634   5.071  20.104  1.00 74.68           O\\nATOM   2600  CG2 THR A 372      17.138   4.544  18.316  1.00 68.04           C\\nATOM   2601  N   GLN A 373      15.283   1.100  18.019  1.00 68.72           N\\nATOM   2602  CA  GLN A 373      15.663  -0.031  17.180  1.00 79.96           C\\nATOM   2603  C   GLN A 373      14.624  -0.283  16.095  1.00 79.40           C\\nATOM   2604  O   GLN A 373      14.972  -0.633  14.961  1.00 75.09           O\\nATOM   2605  CB  GLN A 373      15.857  -1.276  18.043  1.00 95.27           C\\nATOM   2606  CG  GLN A 373      17.006  -1.162  19.028  1.00107.01           C\\nATOM   2607  CD  GLN A 373      16.835  -2.074  20.228  1.00113.19           C\\nATOM   2608  OE1 GLN A 373      15.768  -2.652  20.438  1.00109.22           O\\nATOM   2609  NE2 GLN A 373      17.889  -2.204  21.025  1.00117.08           N\\nATOM   2610  N   MET A 374      13.345  -0.105  16.421  1.00 79.17           N\\nATOM   2611  CA  MET A 374      12.307  -0.277  15.413  1.00 76.40           C\\nATOM   2612  C   MET A 374      12.384   0.814  14.350  1.00 70.69           C\\nATOM   2613  O   MET A 374      12.182   0.543  13.160  1.00 68.25           O\\nATOM   2614  CB  MET A 374      10.934  -0.292  16.079  1.00 77.49           C\\nATOM   2615  CG  MET A 374       9.801  -0.689  15.153  1.00 81.14           C\\nATOM   2616  SD  MET A 374       8.219  -0.741  16.009  1.00 84.97           S\\nATOM   2617  CE  MET A 374       8.086   0.958  16.565  1.00103.28           C\\nATOM   2618  N   ALA A 375      12.684   2.052  14.756  1.00 72.85           N\\nATOM   2619  CA  ALA A 375      12.789   3.144  13.793  1.00 69.01           C\\nATOM   2620  C   ALA A 375      13.899   2.887  12.783  1.00 71.99           C\\nATOM   2621  O   ALA A 375      13.756   3.203  11.596  1.00 68.65           O\\nATOM   2622  CB  ALA A 375      13.021   4.464  14.513  1.00 20.00           C\\nATOM   2623  N   ALA A 376      15.014   2.312  13.234  1.00 72.30           N\\nATOM   2624  CA  ALA A 376      16.110   2.018  12.320  1.00 74.21           C\\nATOM   2625  C   ALA A 376      15.790   0.830  11.427  1.00 77.19           C\\nATOM   2626  O   ALA A 376      16.261   0.771  10.285  1.00 87.02           O\\nATOM   2627  CB  ALA A 376      17.398   1.765  13.104  1.00 74.32           C\\nATOM   2628  N   ILE A 377      15.001  -0.125  11.921  1.00 87.67           N\\nATOM   2629  CA  ILE A 377      14.633  -1.265  11.089  1.00 95.90           C\\nATOM   2630  C   ILE A 377      13.706  -0.839   9.957  1.00101.03           C\\nATOM   2631  O   ILE A 377      13.826  -1.331   8.830  1.00 92.85           O\\nATOM   2632  CB  ILE A 377      13.963  -2.361  11.939  1.00 20.00           C\\nATOM   2633  CG1 ILE A 377      14.964  -2.954  12.932  1.00 20.00           C\\nATOM   2634  CG2 ILE A 377      13.385  -3.448  11.046  1.00 20.00           C\\nATOM   2635  CD1 ILE A 377      14.332  -3.844  13.978  1.00 20.00           C\\nATOM   2636  N   VAL A 378      12.786   0.088  10.234  1.00 89.06           N\\nATOM   2637  CA  VAL A 378      11.896   0.596   9.192  1.00 75.68           C\\nATOM   2638  C   VAL A 378      12.683   1.387   8.156  1.00 75.18           C\\nATOM   2639  O   VAL A 378      12.445   1.268   6.948  1.00 76.19           O\\nATOM   2640  CB  VAL A 378      10.775   1.445   9.820  1.00 64.00           C\\nATOM   2641  CG1 VAL A 378       9.960   2.132   8.740  1.00 62.64           C\\nATOM   2642  CG2 VAL A 378       9.887   0.580  10.701  1.00 69.48           C\\nATOM   2643  N   ALA A 379      13.629   2.210   8.612  1.00 84.87           N\\nATOM   2644  CA  ALA A 379      14.470   2.963   7.688  1.00 87.10           C\\nATOM   2645  C   ALA A 379      15.330   2.035   6.842  1.00 88.96           C\\nATOM   2646  O   ALA A 379      15.578   2.310   5.662  1.00 81.40           O\\nATOM   2647  CB  ALA A 379      15.348   3.945   8.463  1.00 44.79           C\\nATOM   2648  N   GLY A 380      15.802   0.935   7.428  1.00 77.23           N\\nATOM   2649  CA  GLY A 380      16.620   0.001   6.670  1.00 80.45           C\\nATOM   2650  C   GLY A 380      15.818  -0.749   5.624  1.00 77.59           C\\nATOM   2651  O   GLY A 380      16.246  -0.884   4.475  1.00 69.34           O\\nATOM   2652  N   VAL A 381      14.642  -1.252   6.012  1.00 81.99           N\\nATOM   2653  CA  VAL A 381      13.758  -1.918   5.057  1.00 83.38           C\\nATOM   2654  C   VAL A 381      13.412  -0.978   3.910  1.00 77.79           C\\nATOM   2655  O   VAL A 381      13.311  -1.397   2.751  1.00 66.26           O\\nATOM   2656  CB  VAL A 381      12.494  -2.434   5.772  1.00 76.89           C\\nATOM   2657  CG1 VAL A 381      11.472  -2.937   4.769  1.00 69.18           C\\nATOM   2658  CG2 VAL A 381      12.858  -3.534   6.752  1.00 75.31           C\\nATOM   2659  N   PHE A 382      13.231   0.308   4.214  1.00 79.75           N\\nATOM   2660  CA  PHE A 382      13.014   1.298   3.166  1.00 68.40           C\\nATOM   2661  C   PHE A 382      14.165   1.294   2.171  1.00 73.80           C\\nATOM   2662  O   PHE A 382      13.953   1.186   0.958  1.00 78.38           O\\nATOM   2663  CB  PHE A 382      12.844   2.679   3.796  1.00 62.89           C\\nATOM   2664  CG  PHE A 382      12.514   3.767   2.815  1.00 69.81           C\\nATOM   2665  CD1 PHE A 382      11.203   4.013   2.452  1.00 78.17           C\\nATOM   2666  CD2 PHE A 382      13.513   4.560   2.276  1.00 67.00           C\\nATOM   2667  CE1 PHE A 382      10.895   5.021   1.557  1.00 75.89           C\\nATOM   2668  CE2 PHE A 382      13.211   5.566   1.380  1.00 62.38           C\\nATOM   2669  CZ  PHE A 382      11.900   5.797   1.021  1.00 65.04           C\\nATOM   2670  N   ILE A 383      15.399   1.395   2.672  1.00 79.94           N\\nATOM   2671  CA  ILE A 383      16.564   1.405   1.792  1.00 76.66           C\\nATOM   2672  C   ILE A 383      16.668   0.093   1.027  1.00 74.25           C\\nATOM   2673  O   ILE A 383      17.053   0.072  -0.148  1.00 81.52           O\\nATOM   2674  CB  ILE A 383      17.840   1.702   2.601  1.00 71.78           C\\nATOM   2675  CG1 ILE A 383      17.851   3.163   3.035  1.00 63.66           C\\nATOM   2676  CG2 ILE A 383      19.084   1.400   1.789  1.00 79.30           C\\nATOM   2677  CD1 ILE A 383      17.701   4.126   1.880  1.00 64.10           C\\nATOM   2678  N   ILE A 384      16.309  -1.019   1.668  1.00 77.47           N\\nANISOU 2678  N   ILE A 384    10269   8636  10532   1676   -785   -446       N\\nATOM   2679  CA  ILE A 384      16.346  -2.312   0.990  1.00 77.09           C\\nANISOU 2679  CA  ILE A 384    10626   8415  10249   1786   -743   -487       C\\nATOM   2680  C   ILE A 384      15.395  -2.323  -0.203  1.00 79.25           C\\nANISOU 2680  C   ILE A 384    11068   8660  10381   1476   -652   -397       C\\nATOM   2681  O   ILE A 384      15.699  -2.905  -1.252  1.00 79.85           O\\nANISOU 2681  O   ILE A 384    11325   8712  10302   1540   -544   -477       O\\nATOM   2682  CB  ILE A 384      16.026  -3.439   1.989  1.00 74.75           C\\nANISOU 2682  CB  ILE A 384    10740   7870   9793   1895   -906   -471       C\\nATOM   2683  CG1 ILE A 384      17.200  -3.648   2.941  1.00 77.41           C\\nANISOU 2683  CG1 ILE A 384    10961   8240  10210   2294  -1026   -570       C\\nATOM   2684  CG2 ILE A 384      15.704  -4.737   1.267  1.00 71.60           C\\nANISOU 2684  CG2 ILE A 384    10844   7191   9169   1898   -891   -497       C\\nATOM   2685  CD1 ILE A 384      18.443  -4.186   2.256  1.00 79.90           C\\nANISOU 2685  CD1 ILE A 384    11224   8571  10564   2673   -951   -738       C\\nATOM   2686  N   CYS A 385      14.245  -1.657  -0.076  1.00 75.66           N\\nANISOU 2686  N   CYS A 385    10540   8236   9971   1156   -704   -252       N\\nATOM   2687  CA  CYS A 385      13.214  -1.744  -1.106  1.00 79.40           C\\nANISOU 2687  CA  CYS A 385    11178   8693  10298    856   -690   -152       C\\nATOM   2688  C   CYS A 385      13.483  -0.807  -2.281  1.00 77.99           C\\nANISOU 2688  C   CYS A 385    10754   8710  10168    769   -575    -84       C\\nATOM   2689  O   CYS A 385      13.199  -1.160  -3.432  1.00 80.47           O\\nANISOU 2689  O   CYS A 385    11270   9043  10261    646   -531    -66       O\\nATOM   2690  CB  CYS A 385      11.842  -1.449  -0.500  1.00 80.67           C\\nANISOU 2690  CB  CYS A 385    11312   8841  10500    576   -801    -23       C\\nATOM   2691  SG  CYS A 385      11.235  -2.722   0.645  1.00 83.19           S\\nANISOU 2691  SG  CYS A 385    12017   8939  10653    532   -901    -25       S\\nATOM   2692  N   TRP A 386      14.018   0.384  -2.024  1.00 68.60           N\\nANISOU 2692  N   TRP A 386     9160   7658   9246    804   -535    -37       N\\nATOM   2693  CA  TRP A 386      14.213   1.350  -3.095  1.00 71.32           C\\nANISOU 2693  CA  TRP A 386     9293   8158   9646    667   -432     98       C\\nATOM   2694  C   TRP A 386      15.618   1.346  -3.677  1.00 73.91           C\\nANISOU 2694  C   TRP A 386     9483   8642   9959    842   -227     12       C\\nATOM   2695  O   TRP A 386      15.812   1.874  -4.776  1.00 77.41           O\\nANISOU 2695  O   TRP A 386     9849   9237  10328    705    -92    139       O\\nATOM   2696  CB  TRP A 386      13.885   2.767  -2.612  1.00 68.85           C\\nANISOU 2696  CB  TRP A 386     8631   7857   9670    543   -510    230       C\\nATOM   2697  CG  TRP A 386      12.415   3.071  -2.565  1.00 72.68           C\\nANISOU 2697  CG  TRP A 386     9161   8279  10174    338   -661    365       C\\nATOM   2698  CD1 TRP A 386      11.648   3.236  -1.448  1.00 67.00           C\\nANISOU 2698  CD1 TRP A 386     8370   7494   9594    332   -777    320       C\\nATOM   2699  CD2 TRP A 386      11.534   3.244  -3.684  1.00 78.89           C\\nANISOU 2699  CD2 TRP A 386    10042   9108  10823    121   -715    558       C\\nATOM   2700  NE1 TRP A 386      10.348   3.502  -1.801  1.00 70.95           N\\nANISOU 2700  NE1 TRP A 386     8865   8000  10093    139   -882    461       N\\nATOM   2701  CE2 TRP A 386      10.251   3.512  -3.168  1.00 76.55           C\\nANISOU 2701  CE2 TRP A 386     9677   8767  10641      9   -876    617       C\\nATOM   2702  CE3 TRP A 386      11.706   3.200  -5.072  1.00 78.88           C\\nANISOU 2702  CE3 TRP A 386    10168   9215  10586     17   -646    682       C\\nATOM   2703  CZ2 TRP A 386       9.146   3.736  -3.988  1.00 75.36           C\\nANISOU 2703  CZ2 TRP A 386     9547   8666  10419   -188  -1008    800       C\\nATOM   2704  CZ3 TRP A 386      10.606   3.421  -5.885  1.00 78.84           C\\nANISOU 2704  CZ3 TRP A 386    10240   9252  10462   -196   -791    875       C\\nATOM   2705  CH2 TRP A 386       9.343   3.684  -5.340  1.00 78.30           C\\nANISOU 2705  CH2 TRP A 386    10069   9128  10555   -289   -989    935       C\\nATOM   2706  N   LEU A 387      16.599   0.779  -2.986  1.00 71.16           N\\nANISOU 2706  N   LEU A 387     9082   8289   9666   1138   -199   -185       N\\nATOM   2707  CA  LEU A 387      17.963   0.908  -3.486  1.00 77.39           C\\nANISOU 2707  CA  LEU A 387     9613   9290  10501   1307     10   -275       C\\nATOM   2708  C   LEU A 387      18.178   0.130  -4.783  1.00 81.59           C\\nANISOU 2708  C   LEU A 387    10394   9919  10687   1358    212   -346       C\\nATOM   2709  O   LEU A 387      18.816   0.661  -5.701  1.00 86.35           O\\nANISOU 2709  O   LEU A 387    10786  10774  11250   1288    442   -288       O\\nATOM   2710  CB  LEU A 387      18.985   0.473  -2.436  1.00 76.08           C\\nANISOU 2710  CB  LEU A 387     9284   9129  10492   1656    -47   -481       C\\nATOM   2711  CG  LEU A 387      20.393   0.933  -2.792  1.00 73.95           C\\nANISOU 2711  CG  LEU A 387     8566   9145  10385   1779    152   -557       C\\nATOM   2712  CD1 LEU A 387      20.380   2.425  -3.067  1.00 70.62           C\\nANISOU 2712  CD1 LEU A 387     7792   8838  10202   1432    210   -352       C\\nATOM   2713  CD2 LEU A 387      21.363   0.599  -1.677  1.00 74.27           C\\nANISOU 2713  CD2 LEU A 387     8384   9220  10617   2125     25   -752       C\\nATOM   2714  N   PRO A 388      17.692  -1.112  -4.913  1.00 79.42           N\\nANISOU 2714  N   PRO A 388    10576   9454  10144   1463    148   -479       N\\nATOM   2715  CA  PRO A 388      17.785  -1.780  -6.223  1.00 83.37           C\\nANISOU 2715  CA  PRO A 388    11355  10040  10283   1481    328   -585       C\\nATOM   2716  C   PRO A 388      17.190  -0.967  -7.356  1.00 88.60           C\\nANISOU 2716  C   PRO A 388    12005  10889  10771   1117    400   -357       C\\nATOM   2717  O   PRO A 388      17.670  -1.054  -8.493  1.00 89.35           O\\nANISOU 2717  O   PRO A 388    12143  11216  10591   1123    637   -407       O\\nATOM   2718  CB  PRO A 388      17.015  -3.085  -5.998  1.00 78.09           C\\nANISOU 2718  CB  PRO A 388    11219   9031   9418   1534    148   -722       C\\nATOM   2719  CG  PRO A 388      17.214  -3.371  -4.563  1.00 73.10           C\\nANISOU 2719  CG  PRO A 388    10537   8200   9037   1742    -22   -758       C\\nATOM   2720  CD  PRO A 388      17.196  -2.039  -3.878  1.00 74.29           C\\nANISOU 2720  CD  PRO A 388    10229   8503   9495   1588    -73   -564       C\\nATOM   2721  N   PHE A 389      16.157  -0.168  -7.077  1.00 87.86           N\\nANISOU 2721  N   PHE A 389    11851  10717  10815    821    202   -105       N\\nATOM   2722  CA  PHE A 389      15.588   0.699  -8.103  1.00 88.83           C\\nANISOU 2722  CA  PHE A 389    11946  10997  10808    504    215    164       C\\nATOM   2723  C   PHE A 389      16.581   1.776  -8.524  1.00 87.11           C\\nANISOU 2723  C   PHE A 389    11342  11030  10726    460    445    317       C\\nATOM   2724  O   PHE A 389      16.791   2.009  -9.719  1.00 91.58           O\\nANISOU 2724  O   PHE A 389    11960  11831  11005    327    627    435       O\\nATOM   2725  CB  PHE A 389      14.287   1.323  -7.592  1.00 81.78           C\\nANISOU 2725  CB  PHE A 389    11019   9946  10106    271    -69    378       C\\nATOM   2726  CG  PHE A 389      13.670   2.319  -8.536  1.00 78.75           C\\nANISOU 2726  CG  PHE A 389    10580   9686   9656    -11   -125    698       C\\nATOM   2727  CD1 PHE A 389      12.947   1.897  -9.638  1.00 72.20           C\\nANISOU 2727  CD1 PHE A 389    10065   8946   8421   -182   -197    758       C\\nATOM   2728  CD2 PHE A 389      13.795   3.677  -8.309  1.00 74.32           C\\nANISOU 2728  CD2 PHE A 389     9675   9124   9438   -104   -142    940       C\\nATOM   2729  CE1 PHE A 389      12.374   2.812 -10.501  1.00 66.21           C\\nANISOU 2729  CE1 PHE A 389     9270   8308   7580   -418   -296   1089       C\\nATOM   2730  CE2 PHE A 389      13.221   4.593  -9.169  1.00 73.66           C\\nANISOU 2730  CE2 PHE A 389     9576   9102   9309   -336   -229   1275       C\\nATOM   2731  CZ  PHE A 389      12.508   4.160 -10.263  1.00 67.96           C\\nANISOU 2731  CZ  PHE A 389     9160   8501   8161   -483   -313   1367       C\\nATOM   2732  N   PHE A 390      17.211   2.438  -7.553  1.00 78.28           N\\nANISOU 2732  N   PHE A 390     9842   9876  10022    542    440    319       N\\nATOM   2733  CA  PHE A 390      18.154   3.503  -7.865  1.00 77.80           C\\nANISOU 2733  CA  PHE A 390     9387  10020  10154    435    640    473       C\\nATOM   2734  C   PHE A 390      19.520   2.977  -8.285  1.00 85.50           C\\nANISOU 2734  C   PHE A 390    10201  11281  11003    650    968    266       C\\nATOM   2735  O   PHE A 390      20.266   3.699  -8.955  1.00 80.65           O\\nANISOU 2735  O   PHE A 390     9313  10928  10401    495   1220    418       O\\nATOM   2736  CB  PHE A 390      18.290   4.441  -6.666  1.00 72.78           C\\nANISOU 2736  CB  PHE A 390     8403   9227  10023    409    479    515       C\\nATOM   2737  CG  PHE A 390      17.046   5.229  -6.384  1.00 71.97           C\\nANISOU 2737  CG  PHE A 390     8367   8891  10086    201    217    731       C\\nATOM   2738  CD1 PHE A 390      16.770   6.384  -7.095  1.00 73.92           C\\nANISOU 2738  CD1 PHE A 390     8531   9132  10422    -77    215   1066       C\\nATOM   2739  CD2 PHE A 390      16.146   4.810  -5.423  1.00 69.40           C\\nANISOU 2739  CD2 PHE A 390     8185   8358   9824    295    -21    611       C\\nATOM   2740  CE1 PHE A 390      15.624   7.110  -6.848  1.00 69.85           C\\nANISOU 2740  CE1 PHE A 390     8056   8392  10093   -202    -42   1247       C\\nATOM   2741  CE2 PHE A 390      14.995   5.533  -5.171  1.00 69.17           C\\nANISOU 2741  CE2 PHE A 390     8161   8162   9960    142   -234    777       C\\nATOM   2742  CZ  PHE A 390      14.735   6.685  -5.884  1.00 63.89           C\\nANISOU 2742  CZ  PHE A 390     7389   7471   9415    -78   -256   1080       C\\nATOM   2743  N   ILE A 391      19.865   1.744  -7.905  1.00 83.05           N\\nANISOU 2743  N   ILE A 391    10043  10926  10586   1005    976    -67       N\\nATOM   2744  CA  ILE A 391      21.044   1.100  -8.477  1.00 88.93           C\\nANISOU 2744  CA  ILE A 391    10677  11954  11158   1273   1299   -305       C\\nATOM   2745  C   ILE A 391      20.854   0.907  -9.975  1.00 91.28           C\\nANISOU 2745  C   ILE A 391    11243  12480  10960   1127   1541   -254       C\\nATOM   2746  O   ILE A 391      21.789   1.084 -10.766  1.00 94.74           O\\nANISOU 2746  O   ILE A 391    11451  13294  11253   1139   1904   -276       O\\nATOM   2747  CB  ILE A 391      21.321  -0.238  -7.761  1.00 85.00           C\\nANISOU 2747  CB  ILE A 391    10370  11271  10655   1728   1197   -664       C\\nATOM   2748  CG1 ILE A 391      21.803   0.004  -6.329  1.00 81.99           C\\nANISOU 2748  CG1 ILE A 391     9657  10782  10715   1901    995   -715       C\\nATOM   2749  CG2 ILE A 391      22.336  -1.068  -8.534  1.00 85.18           C\\nANISOU 2749  CG2 ILE A 391    10376  11551  10438   2063   1525   -960       C\\nATOM   2750  CD1 ILE A 391      22.006  -1.268  -5.531  1.00 79.71           C\\nANISOU 2750  CD1 ILE A 391     9598  10266  10423   2344    833   -991       C\\nATOM   2751  N   THR A 392      19.633   0.564 -10.388  1.00 91.03           N\\nANISOU 2751  N   THR A 392    11682  12262  10642    965   1345   -183       N\\nATOM   2752  CA  THR A 392      19.347   0.341 -11.801  1.00 92.03           C\\nANISOU 2752  CA  THR A 392    12124  12607  10236    813   1511   -151       C\\nATOM   2753  C   THR A 392      19.510   1.622 -12.611  1.00 96.64           C\\nANISOU 2753  C   THR A 392    12473  13487  10758    456   1684    247       C\\nATOM   2754  O   THR A 392      19.972   1.585 -13.759  1.00 99.51           O\\nANISOU 2754  O   THR A 392    12896  14212  10701    394   2002    256       O\\nATOM   2755  CB  THR A 392      17.934  -0.222 -11.949  1.00 85.65           C\\nANISOU 2755  CB  THR A 392    11821  11527   9195    670   1183   -144       C\\nATOM   2756  OG1 THR A 392      17.843  -1.462 -11.238  1.00 86.36           O\\nANISOU 2756  OG1 THR A 392    12169  11313   9330    965   1047   -489       O\\nATOM   2757  CG2 THR A 392      17.589  -0.458 -13.404  1.00 82.50           C\\nANISOU 2757  CG2 THR A 392    11776  11367   8203    498   1292   -131       C\\nATOM   2758  N   HIS A 393      19.187   2.742 -12.031  1.00 88.71           N\\nANISOU 2758  N   HIS A 393    11226  12324  10155    219   1485    579       N\\nATOM   2759  CA  HIS A 393      19.363   3.957 -12.738  1.00 88.98           C\\nANISOU 2759  CA  HIS A 393    11056  12550  10202   -130   1618   1001       C\\nATOM   2760  C   HIS A 393      20.809   4.181 -13.033  1.00 88.31           C\\nANISOU 2760  C   HIS A 393    10554  12829  10172   -105   2051    965       C\\nATOM   2761  O   HIS A 393      21.145   4.651 -14.071  1.00 90.40           O\\nANISOU 2761  O   HIS A 393    10759  13392  10197   -381   2313   1255       O\\nATOM   2762  CB  HIS A 393      18.863   5.074 -11.893  1.00 92.81           C\\nANISOU 2762  CB  HIS A 393    11357  12712  11192   -324   1304   1294       C\\nATOM   2763  CG  HIS A 393      17.412   5.334 -12.064  1.00 96.38           C\\nANISOU 2763  CG  HIS A 393    12141  12922  11557   -443    932   1454       C\\nATOM   2764  ND1 HIS A 393      16.815   5.355 -13.296  1.00101.35           N\\nANISOU 2764  ND1 HIS A 393    12985  13642  11882   -712    860   1815       N\\nATOM   2765  CD2 HIS A 393      16.440   5.591 -11.168  1.00 93.09           C\\nANISOU 2765  CD2 HIS A 393    11851  12212  11307   -333    611   1312       C\\nATOM   2766  CE1 HIS A 393      15.536   5.622 -13.155  1.00 98.51           C\\nANISOU 2766  CE1 HIS A 393    12830  13059  11540   -744    489   1868       C\\nATOM   2767  NE2 HIS A 393      15.282   5.762 -11.872  1.00 93.35           N\\nANISOU 2767  NE2 HIS A 393    12117  12180  11171   -533    357   1563       N\\nATOM   2768  N   ILE A 394      21.675   3.869 -12.094  1.00 95.53           N\\nANISOU 2768  N   ILE A 394    11157  13746  11395    209   2124    635       N\\nATOM   2769  CA  ILE A 394      23.103   4.065 -12.304  1.00100.46           C\\nANISOU 2769  CA  ILE A 394    11300  14765  12104    258   2532    556       C\\nATOM   2770  C   ILE A 394      23.590   3.234 -13.480  1.00110.00           C\\nANISOU 2770  C   ILE A 394    12669  16389  12736    410   2939    349       C\\nATOM   2771  O   ILE A 394      24.530   3.628 -14.181  1.00116.65           O\\nANISOU 2771  O   ILE A 394    13187  17679  13455    283   3367    434       O\\nATOM   2772  CB  ILE A 394      23.876   3.735 -11.014  1.00 95.87           C\\nANISOU 2772  CB  ILE A 394    10335  14092  12001    599   2436    239       C\\nATOM   2773  N   LEU A 395      22.959   2.084 -13.726  1.00109.05           N\\nANISOU 2773  N   LEU A 395    13051  16136  12246    661   2828     65       N\\nATOM   2774  CA  LEU A 395      23.384   1.213 -14.816  1.00115.80           C\\nANISOU 2774  CA  LEU A 395    14119  17349  12533    853   3195   -221       C\\nATOM   2775  C   LEU A 395      22.911   1.731 -16.169  1.00123.98           C\\nANISOU 2775  C   LEU A 395    15434  18666  13007    451   3352    106       C\\nATOM   2776  O   LEU A 395      23.622   1.591 -17.170  1.00132.70           O\\nANISOU 2776  O   LEU A 395    16488  20259  13673    459   3812     22       O\\nATOM   2777  CB  LEU A 395      22.873  -0.208 -14.578  1.00113.04           C\\nANISOU 2777  CB  LEU A 395    14254  16684  12011   1243   2983   -662       C\\nATOM   2778  CG  LEU A 395      23.285  -0.827 -13.242  1.00107.58           C\\nANISOU 2778  CG  LEU A 395    13379  15684  11813   1666   2788   -952       C\\nATOM   2779  CD1 LEU A 395      22.874  -2.287 -13.174  1.00109.94           C\\nANISOU 2779  CD1 LEU A 395    14213  15663  11896   2035   2631  -1369       C\\nATOM   2780  CD2 LEU A 395      24.782  -0.681 -13.009  1.00102.89           C\\nANISOU 2780  CD2 LEU A 395    12151  15454  11490   1927   3132  -1110       C\\nATOM   2781  N   ASN A 396      21.713   2.324 -16.219  1.00120.69           N\\nANISOU 2781  N   ASN A 396    15306  17974  12576    116   2975    478       N\\nATOM   2782  CA  ASN A 396      21.242   2.943 -17.454  1.00120.58           C\\nANISOU 2782  CA  ASN A 396    15547  18214  12053   -278   3052    871       C\\nATOM   2783  C   ASN A 396      22.194   4.031 -17.930  1.00122.42           C\\nANISOU 2783  C   ASN A 396    15355  18837  12322   -573   3455   1241       C\\nATOM   2784  O   ASN A 396      22.387   4.205 -19.139  1.00125.81           O\\nANISOU 2784  O   ASN A 396    15933  19697  12171   -784   3770   1420       O\\nATOM   2785  CB  ASN A 396      19.841   3.523 -17.251  1.00116.75           C\\nANISOU 2785  CB  ASN A 396    15328  17340  11693   -546   2527   1239       C\\nATOM   2786  CG  ASN A 396      18.760   2.676 -17.888  1.00117.94           C\\nANISOU 2786  CG  ASN A 396    16062  17433  11316   -534   2274   1087       C\\nATOM   2787  OD1 ASN A 396      18.987   1.516 -18.228  1.00121.59           O\\nANISOU 2787  OD1 ASN A 396    16780  18007  11413   -276   2424    626       O\\nATOM   2788  ND2 ASN A 396      17.576   3.253 -18.057  1.00116.24           N\\nANISOU 2788  ND2 ASN A 396    16052  17032  11079   -807   1870   1457       N\\nATOM   2789  N   ILE A 397      22.806   4.760 -16.997  1.00128.30           N\\nANISOU 2789  N   ILE A 397    15581  19448  13721   -619   3450   1356       N\\nATOM   2790  CA  ILE A 397      23.706   5.849 -17.357  1.00131.63           C\\nANISOU 2790  CA  ILE A 397    15568  20182  14265   -972   3805   1730       C\\nATOM   2791  C   ILE A 397      25.103   5.322 -17.667  1.00137.13           C\\nANISOU 2791  C   ILE A 397    15858  21427  14818   -764   4380   1392       C\\nATOM   2792  O   ILE A 397      25.789   5.839 -18.556  1.00140.52           O\\nANISOU 2792  O   ILE A 397    16093  22338  14959  -1056   4838   1642       O\\nATOM   2793  CB  ILE A 397      23.731   6.896 -16.228  1.00123.72           C\\nANISOU 2793  CB  ILE A 397    14191  18774  14042  -1149   3517   1971       C\\nATOM   2794  CG1 ILE A 397      22.331   7.473 -16.007  1.00113.56           C\\nANISOU 2794  CG1 ILE A 397    13280  16985  12883  -1327   2987   2301       C\\nATOM   2795  CG2 ILE A 397      24.735   8.002 -16.530  1.00125.40           C\\nANISOU 2795  CG2 ILE A 397    13930  19262  14453  -1557   3873   2337       C\\nATOM   2796  CD1 ILE A 397      22.251   8.459 -14.860  1.00102.21           C\\nANISOU 2796  CD1 ILE A 397    11537  15104  12195  -1449   2680   2462       C\\nATOM   2797  N   HIS A 398      25.537   4.278 -16.959  1.00136.75           N\\nANISOU 2797  N   HIS A 398    15674  21329  14958   -248   4372    832       N\\nATOM   2798  CA  HIS A 398      26.930   3.846 -17.033  1.00140.25           C\\nANISOU 2798  CA  HIS A 398    15599  22260  15431     23   4867    485       C\\nATOM   2799  C   HIS A 398      27.250   3.199 -18.376  1.00154.68           C\\nANISOU 2799  C   HIS A 398    17644  24638  16490    117   5371    293       C\\nATOM   2800  O   HIS A 398      28.121   3.674 -19.114  1.00162.37           O\\nANISOU 2800  O   HIS A 398    18256  26184  17254   -111   5901    448       O\\nATOM   2801  CB  HIS A 398      27.240   2.881 -15.886  1.00132.50           C\\nANISOU 2801  CB  HIS A 398    14462  21019  14861    602   4649    -39       C\\nATOM   2802  N   CYS A 399      26.570   2.103 -18.707  1.00157.99           N\\nANISOU 2802  N   CYS A 399    18652  24908  16468    436   5229    -65       N\\nATOM   2803  CA  CYS A 399      26.929   1.309 -19.875  1.00171.19           C\\nANISOU 2803  CA  CYS A 399    20554  27077  17414    635   5693   -403       C\\nATOM   2804  C   CYS A 399      25.915   1.388 -21.006  1.00172.38           C\\nANISOU 2804  C   CYS A 399    21379  27292  16826    306   5614   -163       C\\nATOM   2805  O   CYS A 399      26.152   0.799 -22.069  1.00171.94           O\\nANISOU 2805  O   CYS A 399    21574  27683  16070    417   5999   -433       O\\nATOM   2806  CB  CYS A 399      27.145  -0.157 -19.472  1.00177.68           C\\nANISOU 2806  CB  CYS A 399    21527  27720  18264   1324   5648  -1118       C\\nATOM   2807  SG  CYS A 399      25.689  -1.129 -18.956  1.00177.65           S\\nANISOU 2807  SG  CYS A 399    22318  26935  18245   1520   4957  -1341       S\\nATOM   2808  N   ASP A 400      24.802   2.093 -20.815  1.00169.42           N\\nANISOU 2808  N   ASP A 400    21292  26506  16572    -73   5118    313       N\\nATOM   2809  CA  ASP A 400      23.708   2.176 -21.779  1.00172.19           C\\nANISOU 2809  CA  ASP A 400    22278  26866  16282   -369   4909    565       C\\nATOM   2810  C   ASP A 400      23.130   0.810 -22.126  1.00178.49           C\\nANISOU 2810  C   ASP A 400    23661  27552  16606    -24   4760      1       C\\nATOM   2811  O   ASP A 400      22.354   0.694 -23.084  1.00180.90           O\\nANISOU 2811  O   ASP A 400    24500  27979  16254   -230   4642     91       O\\nATOM   2812  CB  ASP A 400      24.139   2.903 -23.061  1.00174.58           C\\nANISOU 2812  CB  ASP A 400    22570  27804  15958   -772   5382    965       C\\nATOM   2813  N   CYS A 401      23.494  -0.229 -21.377  1.00180.63           N\\nANISOU 2813  N   CYS A 401    23862  27575  17194    489   4738   -576       N\\nATOM   2814  CA  CYS A 401      22.923  -1.551 -21.583  1.00179.00           C\\nANISOU 2814  CA  CYS A 401    24242  27130  16641    806   4543  -1120       C\\nATOM   2815  C   CYS A 401      21.440  -1.519 -21.252  1.00170.63           C\\nANISOU 2815  C   CYS A 401    23622  25538  15671    556   3881   -897       C\\nATOM   2816  O   CYS A 401      21.063  -1.243 -20.109  1.00166.40           O\\nANISOU 2816  O   CYS A 401    22893  24541  15789    548   3513   -729       O\\nATOM   2817  CB  CYS A 401      23.624  -2.583 -20.701  1.00179.14           C\\nANISOU 2817  CB  CYS A 401    24079  26891  17096   1410   4598  -1700       C\\nATOM   2818  SG  CYS A 401      25.421  -2.457 -20.478  1.00183.37           S\\nANISOU 2818  SG  CYS A 401    23801  27930  17940   1774   5237  -1908       S\\nATOM   2819  N   ASN A 402      20.597  -1.793 -22.244  1.00163.09           N\\nANISOU 2819  N   ASN A 402    23235  24683  14049    348   3727   -908       N\\nATOM   2820  CA  ASN A 402      19.171  -1.877 -21.964  1.00152.09           C\\nANISOU 2820  CA  ASN A 402    22222  22828  12736    126   3092   -755       C\\nATOM   2821  C   ASN A 402      18.914  -3.031 -21.004  1.00144.87           C\\nANISOU 2821  C   ASN A 402    21476  21352  12215    479   2819  -1242       C\\nATOM   2822  O   ASN A 402      19.334  -4.167 -21.242  1.00148.09           O\\nANISOU 2822  O   ASN A 402    22151  21737  12380    836   2997  -1823       O\\nATOM   2823  CB  ASN A 402      18.364  -2.039 -23.255  1.00153.00           C\\nANISOU 2823  CB  ASN A 402    22907  23202  12025   -153   2955   -727       C\\nATOM   2824  CG  ASN A 402      18.644  -3.344 -23.970  1.00154.48           C\\nANISOU 2824  CG  ASN A 402    23550  23525  11619    142   3169  -1424       C\\nATOM   2825  OD1 ASN A 402      18.048  -4.376 -23.657  1.00152.23           O\\nANISOU 2825  OD1 ASN A 402    23645  22801  11394    294   2842  -1846       O\\nATOM   2826  ND2 ASN A 402      19.540  -3.303 -24.949  1.00156.47           N\\nANISOU 2826  ND2 ASN A 402    23784  24383  11285    209   3730  -1554       N\\nATOM   2827  N   ILE A 403      18.259  -2.719 -19.893  1.00137.95           N\\nANISOU 2827  N   ILE A 403    20445  20015  11956    389   2403   -999       N\\nATOM   2828  CA  ILE A 403      18.056  -3.664 -18.801  1.00126.08           C\\nANISOU 2828  CA  ILE A 403    19041  17968  10897    679   2150  -1342       C\\nATOM   2829  C   ILE A 403      16.725  -4.370 -19.025  1.00123.67           C\\nANISOU 2829  C   ILE A 403    19300  17348  10341    476   1691  -1463       C\\nATOM   2830  O   ILE A 403      15.774  -3.737 -19.506  1.00123.23           O\\nANISOU 2830  O   ILE A 403    19345  17396  10082     73   1419  -1099       O\\nATOM   2831  CB  ILE A 403      18.121  -2.936 -17.448  1.00116.57           C\\nANISOU 2831  CB  ILE A 403    17344  16498  10450    680   1990  -1029       C\\nATOM   2832  CG1 ILE A 403      19.571  -2.545 -17.154  1.00117.76           C\\nANISOU 2832  CG1 ILE A 403    16950  16923  10871    944   2430  -1064       C\\nATOM   2833  CG2 ILE A 403      17.524  -3.771 -16.324  1.00111.83           C\\nANISOU 2833  CG2 ILE A 403    16927  15326  10238    834   1619  -1235       C\\nATOM   2834  CD1 ILE A 403      19.744  -1.682 -15.938  1.00115.05           C\\nANISOU 2834  CD1 ILE A 403    16103  16396  11214    903   2293   -760       C\\nATOM   2835  N   PRO A 404      16.628  -5.671 -18.745  1.00118.90           N\\nANISOU 2835  N   PRO A 404    19074  16363   9738    731   1581  -1960       N\\nATOM   2836  CA  PRO A 404      15.360  -6.387 -18.918  1.00118.90           C\\nANISOU 2836  CA  PRO A 404    19598  16036   9542    479   1130  -2089       C\\nATOM   2837  C   PRO A 404      14.199  -5.600 -18.342  1.00114.46           C\\nANISOU 2837  C   PRO A 404    18849  15327   9312     80    700  -1589       C\\nATOM   2838  O   PRO A 404      14.149  -5.345 -17.130  1.00111.06           O\\nANISOU 2838  O   PRO A 404    18106  14611   9479    144    589  -1414       O\\nATOM   2839  CB  PRO A 404      15.590  -7.690 -18.142  1.00118.42           C\\nANISOU 2839  CB  PRO A 404    19799  15435   9759    841   1069  -2563       C\\nATOM   2840  CG  PRO A 404      17.050  -7.938 -18.305  1.00121.83           C\\nANISOU 2840  CG  PRO A 404    20054  16085  10152   1347   1569  -2883       C\\nATOM   2841  CD  PRO A 404      17.718  -6.580 -18.344  1.00119.79           C\\nANISOU 2841  CD  PRO A 404    19169  16331  10014   1271   1867  -2444       C\\nATOM   2842  N   PRO A 405      13.257  -5.175 -19.187  1.00111.48           N\\nANISOU 2842  N   PRO A 405    18639  15168   8549   -316    448  -1354       N\\nATOM   2843  CA  PRO A 405      12.126  -4.381 -18.686  1.00109.02           C\\nANISOU 2843  CA  PRO A 405    18100  14751   8571   -653     36   -886       C\\nATOM   2844  C   PRO A 405      11.320  -5.093 -17.621  1.00107.40           C\\nANISOU 2844  C   PRO A 405    17974  14039   8792   -700   -301  -1012       C\\nATOM   2845  O   PRO A 405      10.656  -4.425 -16.820  1.00106.74           O\\nANISOU 2845  O   PRO A 405    17562  13840   9155   -851   -528   -666       O\\nATOM   2846  CB  PRO A 405      11.292  -4.119 -19.948  1.00110.35           C\\nANISOU 2846  CB  PRO A 405    18539  15248   8141  -1009   -207   -731       C\\nATOM   2847  CG  PRO A 405      11.691  -5.197 -20.899  1.00113.76           C\\nANISOU 2847  CG  PRO A 405    19491  15789   7942   -900    -38  -1264       C\\nATOM   2848  CD  PRO A 405      13.141  -5.456 -20.627  1.00117.16           C\\nANISOU 2848  CD  PRO A 405    19780  16246   8490   -452    496  -1536       C\\nATOM   2849  N   VAL A 406      11.356  -6.428 -17.580  1.00111.87           N\\nANISOU 2849  N   VAL A 406    18978  14290   9236   -579   -329  -1496       N\\nATOM   2850  CA  VAL A 406      10.738  -7.139 -16.469  1.00102.56           C\\nANISOU 2850  CA  VAL A 406    17881  12600   8486   -624   -592  -1581       C\\nATOM   2851  C   VAL A 406      11.508  -6.882 -15.181  1.00104.10           C\\nANISOU 2851  C   VAL A 406    17697  12610   9246   -300   -398  -1479       C\\nATOM   2852  O   VAL A 406      10.926  -6.894 -14.090  1.00102.17           O\\nANISOU 2852  O   VAL A 406    17313  12081   9424   -395   -602  -1324       O\\nATOM   2853  CB  VAL A 406      10.640  -8.644 -16.776  1.00 94.49           C\\nANISOU 2853  CB  VAL A 406    17480  11217   7203   -584   -680  -2114       C\\nATOM   2854  N   LEU A 407      12.818  -6.639 -15.277  1.00103.82           N\\nANISOU 2854  N   LEU A 407    17468  12769   9209     74     -3  -1567       N\\nATOM   2855  CA  LEU A 407      13.592  -6.296 -14.089  1.00100.38           C\\nANISOU 2855  CA  LEU A 407    16623  12220   9296    369    146  -1462       C\\nATOM   2856  C   LEU A 407      13.390  -4.838 -13.698  1.00 94.26           C\\nANISOU 2856  C   LEU A 407    15315  11675   8824    182    114   -975       C\\nATOM   2857  O   LEU A 407      13.200  -4.533 -12.516  1.00 88.29           O\\nANISOU 2857  O   LEU A 407    14299  10718   8529    200     -8   -812       O\\nATOM   2858  CB  LEU A 407      15.077  -6.584 -14.317  1.00101.90           C\\nANISOU 2858  CB  LEU A 407    16737  12562   9418    837    561  -1755       C\\nATOM   2859  N   TYR A 408      13.370  -3.956 -14.650  1.00 94.06           N\\nANISOU 2859  N   TYR A 408    15152  12055   8531      5    218   -738       N\\nATOM   2860  CA  TYR A 408      13.143  -2.599 -14.299  1.00 92.67           C\\nANISOU 2860  CA  TYR A 408    14536  12021   8655   -189    141   -264       C\\nATOM   2861  C   TYR A 408      11.764  -2.493 -13.713  1.00 95.64           C\\nANISOU 2861  C   TYR A 408    14901  12179   9258   -462   -278    -65       C\\nATOM   2862  O   TYR A 408      11.578  -1.795 -12.766  1.00 92.85           O\\nANISOU 2862  O   TYR A 408    14175  11751   9352   -489   -366    194       O\\nATOM   2863  CB  TYR A 408      13.263  -1.746 -15.521  1.00 92.66           C\\nANISOU 2863  CB  TYR A 408    14496  12449   8263   -369    283     -7       C\\nATOM   2864  CG  TYR A 408      13.909  -0.444 -15.274  1.00 92.93           C\\nANISOU 2864  CG  TYR A 408    14043  12651   8617   -377    472    359       C\\nATOM   2865  CD1 TYR A 408      13.694   0.227 -14.129  1.00 88.51           C\\nANISOU 2865  CD1 TYR A 408    13122  11858   8651   -379    316    564       C\\nATOM   2866  CD2 TYR A 408      14.725   0.122 -16.199  1.00 98.66           C\\nANISOU 2866  CD2 TYR A 408    14681  13767   9040   -406    819    487       C\\nATOM   2867  CE1 TYR A 408      14.287   1.434 -13.904  1.00 87.26           C\\nANISOU 2867  CE1 TYR A 408    12549  11797   8809   -413    462    866       C\\nATOM   2868  CE2 TYR A 408      15.323   1.331 -15.973  1.00 98.99           C\\nANISOU 2868  CE2 TYR A 408    14288  13921   9401   -474    985    837       C\\nATOM   2869  CZ  TYR A 408      15.086   1.974 -14.814  1.00 95.40           C\\nANISOU 2869  CZ  TYR A 408    13502  13174   9570   -479    786   1014       C\\nATOM   2870  OH  TYR A 408      15.640   3.178 -14.533  1.00 98.94           O\\nANISOU 2870  OH  TYR A 408    13550  13681  10361   -572    923   1329       O\\nATOM   2871  N   SER A 409      10.781  -3.173 -14.278  1.00105.38           N\\nANISOU 2871  N   SER A 409    16521  13320  10198   -667   -536   -211       N\\nATOM   2872  CA  SER A 409       9.431  -3.119 -13.727  1.00100.18           C\\nANISOU 2872  CA  SER A 409    15802  12496   9765   -940   -916    -53       C\\nATOM   2873  C   SER A 409       9.363  -3.750 -12.341  1.00 91.59           C\\nANISOU 2873  C   SER A 409    14684  11035   9081   -825   -948   -193       C\\nATOM   2874  O   SER A 409       8.543  -3.336 -11.513  1.00 85.61           O\\nANISOU 2874  O   SER A 409    13671  10195   8661   -967  -1137      4       O\\nATOM   2875  CB  SER A 409       8.447  -3.811 -14.672  1.00102.06           C\\nANISOU 2875  CB  SER A 409    16434  12778   9567  -1245  -1202   -175       C\\nATOM   2876  OG  SER A 409       8.493  -3.239 -15.967  1.00105.65           O\\nANISOU 2876  OG  SER A 409    16956  13611   9576  -1354  -1197    -26       O\\nATOM   2877  N   ALA A 410      10.216  -4.740 -12.069  1.00 90.76           N\\nANISOU 2877  N   ALA A 410    14837  10715   8935   -552   -765   -524       N\\nATOM   2878  CA  ALA A 410      10.196  -5.405 -10.769  1.00 84.55           C\\nANISOU 2878  CA  ALA A 410    14089   9558   8478   -436   -813   -622       C\\nATOM   2879  C   ALA A 410      10.716  -4.488  -9.669  1.00 85.46           C\\nANISOU 2879  C   ALA A 410    13726   9716   9028   -244   -702   -420       C\\nATOM   2880  O   ALA A 410      10.097  -4.365  -8.607  1.00 76.26           O\\nANISOU 2880  O   ALA A 410    12411   8410   8155   -337   -841   -294       O\\nATOM   2881  CB  ALA A 410      11.018  -6.693 -10.829  1.00 79.54           C\\nANISOU 2881  CB  ALA A 410    13883   8649   7690   -141   -680  -1016       C\\nATOM   2882  N   PHE A 411      11.858  -3.837  -9.904  1.00 82.88           N\\nANISOU 2882  N   PHE A 411    13149   9606   8736      5   -442   -403       N\\nATOM   2883  CA  PHE A 411      12.446  -2.977  -8.883  1.00 81.51           C\\nANISOU 2883  CA  PHE A 411    12529   9464   8975    175   -355   -259       C\\nATOM   2884  C   PHE A 411      11.593  -1.745  -8.614  1.00 76.95           C\\nANISOU 2884  C   PHE A 411    11608   8991   8637    -75   -511     73       C\\nATOM   2885  O   PHE A 411      11.658  -1.179  -7.516  1.00 76.38           O\\nANISOU 2885  O   PHE A 411    11240   8854   8929      0   -536    155       O\\nATOM   2886  CB  PHE A 411      13.859  -2.567  -9.293  1.00 88.89           C\\nANISOU 2886  CB  PHE A 411    13244  10633   9898    438    -44   -321       C\\nATOM   2887  CG  PHE A 411      14.856  -3.688  -9.233  1.00 94.35           C\\nANISOU 2887  CG  PHE A 411    14147  11212  10488    811    121   -674       C\\nATOM   2888  CD1 PHE A 411      14.562  -4.860  -8.555  1.00 93.62           C\\nANISOU 2888  CD1 PHE A 411    14407  10746  10418    926    -36   -865       C\\nATOM   2889  CD2 PHE A 411      16.092  -3.568  -9.846  1.00 94.90           C\\nANISOU 2889  CD2 PHE A 411    14052  11548  10457   1055    438   -805       C\\nATOM   2890  CE1 PHE A 411      15.480  -5.891  -8.497  1.00 91.66           C\\nANISOU 2890  CE1 PHE A 411    14375  10339  10112   1324     82  -1184       C\\nATOM   2891  CE2 PHE A 411      17.013  -4.595  -9.790  1.00 91.21           C\\nANISOU 2891  CE2 PHE A 411    13738  10988   9931   1464    585  -1156       C\\nATOM   2892  CZ  PHE A 411      16.707  -5.757  -9.115  1.00 90.35           C\\nANISOU 2892  CZ  PHE A 411    14011  10453   9865   1623    389  -1349       C\\nATOM   2893  N   THR A 412      10.799  -1.310  -9.596  1.00 86.37           N\\nANISOU 2893  N   THR A 412    12841  10347   9628   -346   -634    251       N\\nATOM   2894  CA  THR A 412       9.854  -0.225  -9.353  1.00 83.78           C\\nANISOU 2894  CA  THR A 412    12208  10075   9551   -541   -831    553       C\\nATOM   2895  C   THR A 412       8.712  -0.693  -8.459  1.00 78.58           C\\nANISOU 2895  C   THR A 412    11565   9242   9050   -678  -1053    522       C\\nATOM   2896  O   THR A 412       8.335  -0.005  -7.503  1.00 75.36           O\\nANISOU 2896  O   THR A 412    10841   8797   8997   -662  -1111    634       O\\nATOM   2897  CB  THR A 412       9.310   0.315 -10.677  1.00 83.99           C\\nANISOU 2897  CB  THR A 412    12287  10328   9297   -765   -948    775       C\\nATOM   2898  OG1 THR A 412      10.397   0.624 -11.557  1.00 88.79           O\\nANISOU 2898  OG1 THR A 412    12926  11134   9675   -676   -690    805       O\\nATOM   2899  CG2 THR A 412       8.491   1.578 -10.436  1.00 76.49           C\\nANISOU 2899  CG2 THR A 412    10981   9411   8671   -879  -1149   1106       C\\nATOM   2900  N   TRP A 413       8.148  -1.866  -8.758  1.00 79.97           N\\nANISOU 2900  N   TRP A 413    12110   9314   8961   -831  -1168    357       N\\nATOM   2901  CA  TRP A 413       7.078  -2.406  -7.927  1.00 79.43           C\\nANISOU 2901  CA  TRP A 413    12060   9094   9024  -1024  -1347    342       C\\nATOM   2902  C   TRP A 413       7.576  -2.703  -6.520  1.00 73.46           C\\nANISOU 2902  C   TRP A 413    11258   8138   8517   -819  -1224    254       C\\nATOM   2903  O   TRP A 413       6.853  -2.491  -5.539  1.00 70.81           O\\nANISOU 2903  O   TRP A 413    10714   7782   8407   -915  -1295    340       O\\nATOM   2904  CB  TRP A 413       6.498  -3.667  -8.569  1.00 85.80           C\\nANISOU 2904  CB  TRP A 413    13317   9783   9501  -1268  -1494    166       C\\nATOM   2905  CG  TRP A 413       5.728  -3.398  -9.828  1.00 91.51           C\\nANISOU 2905  CG  TRP A 413    14070  10739   9962  -1534  -1703    261       C\\nATOM   2906  CD1 TRP A 413       5.242  -2.195 -10.250  1.00 85.59           C\\nANISOU 2906  CD1 TRP A 413    12966  10256   9299  -1598  -1823    542       C\\nATOM   2907  CD2 TRP A 413       5.358  -4.354 -10.833  1.00 96.72           C\\nANISOU 2907  CD2 TRP A 413    15160  11373  10216  -1760  -1855     72       C\\nATOM   2908  NE1 TRP A 413       4.589  -2.343 -11.449  1.00 88.41           N\\nANISOU 2908  NE1 TRP A 413    13492  10790   9309  -1846  -2056    571       N\\nATOM   2909  CE2 TRP A 413       4.646  -3.658 -11.829  1.00 95.02           C\\nANISOU 2909  CE2 TRP A 413    14808  11468   9826  -1963  -2077    265       C\\nATOM   2910  CE3 TRP A 413       5.558  -5.731 -10.985  1.00100.43           C\\nANISOU 2910  CE3 TRP A 413    16143  11559  10456  -1802  -1850   -252       C\\nATOM   2911  CZ2 TRP A 413       4.135  -4.290 -12.963  1.00 98.69           C\\nANISOU 2911  CZ2 TRP A 413    15618  12022   9858  -2226  -2299    130       C\\nATOM   2912  CZ3 TRP A 413       5.049  -6.356 -12.111  1.00103.40           C\\nANISOU 2912  CZ3 TRP A 413    16876  11980  10432  -2067  -2053   -417       C\\nATOM   2913  CH2 TRP A 413       4.347  -5.636 -13.085  1.00102.66           C\\nANISOU 2913  CH2 TRP A 413    16621  12251  10133  -2286  -2277   -233       C\\nATOM   2914  N   LEU A 414       8.817  -3.184  -6.402  1.00 75.32           N\\nANISOU 2914  N   LEU A 414    11667   8256   8695   -521  -1041     79       N\\nATOM   2915  CA  LEU A 414       9.384  -3.467  -5.087  1.00 69.21           C\\nANISOU 2915  CA  LEU A 414    10863   7310   8123   -291   -967     10       C\\nATOM   2916  C   LEU A 414       9.434  -2.210  -4.226  1.00 77.59           C\\nANISOU 2916  C   LEU A 414    11447   8517   9516   -215   -939    159       C\\nATOM   2917  O   LEU A 414       9.179  -2.265  -3.016  1.00 79.71           O\\nANISOU 2917  O   LEU A 414    11637   8710   9938   -194   -969    169       O\\nATOM   2918  CB  LEU A 414      10.778  -4.078  -5.238  1.00 67.92           C\\nANISOU 2918  CB  LEU A 414    10893   7049   7867     71   -800   -201       C\\nATOM   2919  CG  LEU A 414      11.552  -4.368  -3.947  1.00 71.97           C\\nANISOU 2919  CG  LEU A 414    11370   7408   8567    375   -760   -268       C\\nATOM   2920  CD1 LEU A 414      10.756  -5.279  -3.035  1.00 56.68           C\\nANISOU 2920  CD1 LEU A 414     9726   5197   6611    226   -906   -242       C\\nATOM   2921  CD2 LEU A 414      12.904  -4.980  -4.260  1.00 76.87           C\\nANISOU 2921  CD2 LEU A 414    12133   7966   9108    768   -617   -490       C\\nATOM   2922  N   GLY A 415       9.747  -1.065  -4.832  1.00 76.07           N\\nANISOU 2922  N   GLY A 415    10960   8524   9421   -187   -885    275       N\\nATOM   2923  CA  GLY A 415       9.745   0.179  -4.081  1.00 72.96           C\\nANISOU 2923  CA  GLY A 415    10144   8207   9369   -132   -886    390       C\\nATOM   2924  C   GLY A 415       8.357   0.581  -3.618  1.00 74.19           C\\nANISOU 2924  C   GLY A 415    10131   8394   9665   -339  -1044    507       C\\nATOM   2925  O   GLY A 415       8.180   1.043  -2.488  1.00 75.00           O\\nANISOU 2925  O   GLY A 415    10010   8487   9999   -269  -1044    489       O\\nATOM   2926  N   TYR A 416       7.355   0.423  -4.485  1.00 71.29           N\\nANISOU 2926  N   TYR A 416     9841   8097   9148   -588  -1184    609       N\\nATOM   2927  CA  TYR A 416       5.978   0.695  -4.089  1.00 65.72           C\\nANISOU 2927  CA  TYR A 416     8925   7466   8580   -782  -1337    704       C\\nATOM   2928  C   TYR A 416       5.494  -0.288  -3.030  1.00 74.23           C\\nANISOU 2928  C   TYR A 416    10136   8452   9617   -880  -1320    595       C\\nATOM   2929  O   TYR A 416       4.629   0.058  -2.215  1.00 72.94           O\\nANISOU 2929  O   TYR A 416     9706   8378   9627   -957  -1345    631       O\\nATOM   2930  CB  TYR A 416       5.065   0.646  -5.312  1.00 62.97           C\\nANISOU 2930  CB  TYR A 416     8626   7243   8059  -1034  -1533    831       C\\nATOM   2931  CG  TYR A 416       5.257   1.800  -6.266  1.00 72.57           C\\nANISOU 2931  CG  TYR A 416     9671   8573   9328   -975  -1592   1030       C\\nATOM   2932  CD1 TYR A 416       5.334   3.107  -5.802  1.00 77.77           C\\nANISOU 2932  CD1 TYR A 416     9966   9229  10353   -816  -1582   1149       C\\nATOM   2933  CD2 TYR A 416       5.362   1.584  -7.633  1.00 70.98           C\\nANISOU 2933  CD2 TYR A 416     9709   8467   8795  -1089  -1663   1103       C\\nATOM   2934  CE1 TYR A 416       5.505   4.166  -6.675  1.00 81.18           C\\nANISOU 2934  CE1 TYR A 416    10288   9707  10852   -788  -1652   1381       C\\nATOM   2935  CE2 TYR A 416       5.537   2.637  -8.513  1.00 78.84           C\\nANISOU 2935  CE2 TYR A 416    10587   9572   9796  -1063  -1716   1345       C\\nATOM   2936  CZ  TYR A 416       5.608   3.925  -8.030  1.00 78.01           C\\nANISOU 2936  CZ  TYR A 416    10131   9419  10091   -919  -1715   1507       C\\nATOM   2937  OH  TYR A 416       5.781   4.974  -8.906  1.00 66.59           O\\nANISOU 2937  OH  TYR A 416     8612   8022   8665   -917  -1783   1795       O\\nATOM   2938  N   VAL A 417       6.036  -1.510  -3.031  1.00 75.00           N\\nANISOU 2938  N   VAL A 417    10650   8367   9481   -873  -1268    468       N\\nATOM   2939  CA  VAL A 417       5.682  -2.503  -2.019  1.00 75.22           C\\nANISOU 2939  CA  VAL A 417    10882   8250   9450   -979  -1253    416       C\\nATOM   2940  C   VAL A 417       6.049  -2.017  -0.621  1.00 75.65           C\\nANISOU 2940  C   VAL A 417    10726   8332   9686   -769  -1144    400       C\\nATOM   2941  O   VAL A 417       5.383  -2.367   0.363  1.00 73.28           O\\nANISOU 2941  O   VAL A 417    10419   8044   9381   -909  -1125    429       O\\nATOM   2942  CB  VAL A 417       6.357  -3.847  -2.359  1.00 69.42           C\\nANISOU 2942  CB  VAL A 417    10679   7234   8461   -938  -1241    282       C\\nATOM   2943  CG1 VAL A 417       6.474  -4.740  -1.133  1.00 66.88           C\\nANISOU 2943  CG1 VAL A 417    10605   6693   8112   -911  -1204    262       C\\nATOM   2944  CG2 VAL A 417       5.575  -4.550  -3.446  1.00 68.97           C\\nANISOU 2944  CG2 VAL A 417    10878   7133   8193  -1268  -1387    262       C\\nATOM   2945  N   ASN A 418       7.086  -1.184  -0.510  1.00 69.14           N\\nANISOU 2945  N   ASN A 418     9719   7544   9007   -464  -1071    354       N\\nATOM   2946  CA  ASN A 418       7.506  -0.674   0.790  1.00 59.69           C\\nANISOU 2946  CA  ASN A 418     8331   6385   7962   -263  -1004    296       C\\nATOM   2947  C   ASN A 418       6.365   0.000   1.544  1.00 72.46           C\\nANISOU 2947  C   ASN A 418     9629   8176   9728   -397  -1007    338       C\\nATOM   2948  O   ASN A 418       6.372   0.033   2.780  1.00 78.40           O\\nANISOU 2948  O   ASN A 418    10330   8974  10483   -321   -946    277       O\\nATOM   2949  CB  ASN A 418       8.666   0.302   0.607  1.00 65.48           C\\nANISOU 2949  CB  ASN A 418     8842   7154   8882      6   -958    240       C\\nATOM   2950  CG  ASN A 418       9.105   0.938   1.907  1.00 70.06           C\\nANISOU 2950  CG  ASN A 418     9208   7784   9627    195   -932    141       C\\nATOM   2951  OD1 ASN A 418       9.915   0.373   2.644  1.00 72.31           O\\nANISOU 2951  OD1 ASN A 418     9648   8008   9820    376   -923     50       O\\nATOM   2952  ND2 ASN A 418       8.575   2.123   2.197  1.00 73.88           N\\nANISOU 2952  ND2 ASN A 418     9344   8372  10354    175   -946    143       N\\nATOM   2953  N   SER A 419       5.371   0.528   0.828  1.00 73.71           N\\nANISOU 2953  N   SER A 419     9563   8456   9988   -577  -1081    433       N\\nATOM   2954  CA  SER A 419       4.257   1.208   1.479  1.00 74.87           C\\nANISOU 2954  CA  SER A 419     9342   8795  10311   -653  -1075    444       C\\nATOM   2955  C   SER A 419       3.387   0.269   2.304  1.00 71.13           C\\nANISOU 2955  C   SER A 419     8963   8398   9665   -899  -1010    455       C\\nATOM   2956  O   SER A 419       2.578   0.748   3.105  1.00 79.35           O\\nANISOU 2956  O   SER A 419     9691   9646  10814   -930   -935    423       O\\nATOM   2957  CB  SER A 419       3.402   1.927   0.433  1.00 76.98           C\\nANISOU 2957  CB  SER A 419     9339   9174  10737   -757  -1215    564       C\\nATOM   2958  OG  SER A 419       4.102   3.028  -0.124  1.00 76.00           O\\nANISOU 2958  OG  SER A 419     9078   8985  10813   -542  -1256    597       O\\nATOM   2959  N   ALA A 420       3.532  -1.043   2.146  1.00 64.52           N\\nANISOU 2959  N   ALA A 420     8553   7392   8567  -1076  -1023    494       N\\nATOM   2960  CA  ALA A 420       2.711  -1.998   2.873  1.00 70.62           C\\nANISOU 2960  CA  ALA A 420     9465   8194   9173  -1382   -964    556       C\\nATOM   2961  C   ALA A 420       3.486  -2.802   3.908  1.00 76.87           C\\nANISOU 2961  C   ALA A 420    10638   8808   9762  -1279   -878    546       C\\nATOM   2962  O   ALA A 420       2.886  -3.634   4.598  1.00 79.00           O\\nANISOU 2962  O   ALA A 420    11085   9071   9862  -1550   -815    643       O\\nATOM   2963  CB  ALA A 420       2.026  -2.954   1.892  1.00 69.09           C\\nANISOU 2963  CB  ALA A 420     9496   7901   8853  -1760  -1092    637       C\\nATOM   2964  N   VAL A 421       4.793  -2.590   4.035  1.00 77.91           N\\nANISOU 2964  N   VAL A 421    10893   8806   9904   -910   -888    455       N\\nATOM   2965  CA  VAL A 421       5.579  -3.412   4.946  1.00 79.27           C\\nANISOU 2965  CA  VAL A 421    11443   8799   9879   -770   -869    464       C\\nATOM   2966  C   VAL A 421       5.680  -2.792   6.335  1.00 78.59           C\\nANISOU 2966  C   VAL A 421    11159   8929   9775   -616   -776    415       C\\nATOM   2967  O   VAL A 421       5.844  -3.521   7.319  1.00 80.37           O\\nANISOU 2967  O   VAL A 421    11677   9096   9766   -626   -753    490       O\\nATOM   2968  CB  VAL A 421       6.980  -3.686   4.367  1.00 73.59           C\\nANISOU 2968  CB  VAL A 421    10961   7841   9160   -437   -947    375       C\\nATOM   2969  CG1 VAL A 421       6.871  -4.312   2.991  1.00 71.39           C\\nANISOU 2969  CG1 VAL A 421    10910   7375   8838   -578  -1015    377       C\\nATOM   2970  CG2 VAL A 421       7.810  -2.409   4.324  1.00 65.73           C\\nANISOU 2970  CG2 VAL A 421     9584   7002   8387   -121   -934    246       C\\nATOM   2971  N   ASN A 422       5.581  -1.466   6.440  1.00 74.03           N\\nANISOU 2971  N   ASN A 422    10123   8582   9422   -475   -738    288       N\\nATOM   2972  CA  ASN A 422       5.742  -0.820   7.742  1.00 73.83           C\\nANISOU 2972  CA  ASN A 422     9929   8759   9366   -304   -662    170       C\\nATOM   2973  C   ASN A 422       4.697  -1.265   8.756  1.00 74.68           C\\nANISOU 2973  C   ASN A 422    10063   9076   9236   -564   -510    254       C\\nATOM   2974  O   ASN A 422       5.081  -1.611   9.887  1.00 76.59           O\\nANISOU 2974  O   ASN A 422    10516   9367   9218   -484   -475    261       O\\nATOM   2975  CB  ASN A 422       5.757   0.700   7.560  1.00 72.41           C\\nANISOU 2975  CB  ASN A 422     9279   8717   9517   -120   -663     -7       C\\nATOM   2976  CG  ASN A 422       7.075   1.199   7.026  1.00 70.46           C\\nANISOU 2976  CG  ASN A 422     9018   8305   9448    152   -777    -94       C\\nATOM   2977  OD1 ASN A 422       8.006   0.419   6.829  1.00 69.93           O\\nANISOU 2977  OD1 ASN A 422     9248   8068   9254    251   -842    -54       O\\nATOM   2978  ND2 ASN A 422       7.166   2.500   6.780  1.00 74.23           N\\nANISOU 2978  ND2 ASN A 422     9142   8823  10239    275   -798   -213       N\\nATOM   2979  N   PRO A 423       3.396  -1.299   8.444  1.00 74.98           N\\nANISOU 2979  N   PRO A 423     9889   9275   9326   -884   -418    332       N\\nATOM   2980  CA  PRO A 423       2.439  -1.829   9.431  1.00 79.39           C\\nANISOU 2980  CA  PRO A 423    10466  10068   9629  -1180   -229    435       C\\nATOM   2981  C   PRO A 423       2.722  -3.267   9.832  1.00 83.90           C\\nANISOU 2981  C   PRO A 423    11615  10404   9861  -1378   -249    663       C\\nATOM   2982  O   PRO A 423       2.406  -3.662  10.961  1.00 90.16           O\\nANISOU 2982  O   PRO A 423    12538  11363  10356  -1521    -99    763       O\\nATOM   2983  CB  PRO A 423       1.089  -1.697   8.713  1.00 72.48           C\\nANISOU 2983  CB  PRO A 423     9227   9375   8937  -1503   -180    488       C\\nATOM   2984  CG  PRO A 423       1.299  -0.620   7.719  1.00 68.97           C\\nANISOU 2984  CG  PRO A 423     8463   8890   8854  -1250   -321    353       C\\nATOM   2985  CD  PRO A 423       2.703  -0.792   7.246  1.00 69.67           C\\nANISOU 2985  CD  PRO A 423     8902   8634   8934   -993   -481    335       C\\nATOM   2986  N   ILE A 424       3.313  -4.062   8.939  1.00 83.26           N\\nANISOU 2986  N   ILE A 424    11907   9927   9801  -1380   -427    747       N\\nATOM   2987  CA  ILE A 424       3.682  -5.430   9.285  1.00 83.10           C\\nANISOU 2987  CA  ILE A 424    12489   9580   9504  -1500   -487    952       C\\nATOM   2988  C   ILE A 424       4.819  -5.441  10.300  1.00 81.27           C\\nANISOU 2988  C   ILE A 424    12492   9304   9083  -1119   -542    931       C\\nATOM   2989  O   ILE A 424       4.919  -6.359  11.125  1.00 80.08           O\\nANISOU 2989  O   ILE A 424    12773   9025   8629  -1213   -546   1138       O\\nATOM   2990  CB  ILE A 424       4.040  -6.206   8.002  1.00 78.55           C\\nANISOU 2990  CB  ILE A 424    12237   8582   9027  -1536   -666    971       C\\nATOM   2991  CG1 ILE A 424       2.825  -6.276   7.073  1.00 73.56           C\\nANISOU 2991  CG1 ILE A 424    11398   8028   8524  -1971   -654   1003       C\\nATOM   2992  CG2 ILE A 424       4.560  -7.600   8.325  1.00 80.22           C\\nANISOU 2992  CG2 ILE A 424    13116   8357   9008  -1567   -766   1149       C\\nATOM   2993  CD1 ILE A 424       3.095  -6.975   5.758  1.00 71.89           C\\nANISOU 2993  CD1 ILE A 424    11502   7446   8367  -2028   -834    970       C\\nATOM   2994  N   ILE A 425       5.680  -4.422  10.275  1.00 72.91           N\\nANISOU 2994  N   ILE A 425    11155   8352   8197   -705   -607    699       N\\nATOM   2995  CA  ILE A 425       6.795  -4.363  11.215  1.00 77.19           C\\nANISOU 2995  CA  ILE A 425    11857   8894   8577   -341   -708    646       C\\nATOM   2996  C   ILE A 425       6.320  -3.961  12.608  1.00 86.64           C\\nANISOU 2996  C   ILE A 425    12947  10469   9504   -403   -561    636       C\\nATOM   2997  O   ILE A 425       6.863  -4.432  13.615  1.00 84.58           O\\nANISOU 2997  O   ILE A 425    13008  10207   8921   -280   -633    733       O\\nATOM   2998  CB  ILE A 425       7.877  -3.406  10.689  1.00 71.65           C\\nANISOU 2998  CB  ILE A 425    10863   8188   8172     58   -830    392       C\\nATOM   2999  CG1 ILE A 425       8.343  -3.850   9.303  1.00 71.05           C\\nANISOU 2999  CG1 ILE A 425    10906   7796   8294    111   -926    402       C\\nATOM   3000  CG2 ILE A 425       9.062  -3.360  11.634  1.00 68.37           C\\nANISOU 3000  CG2 ILE A 425    10565   7798   7613    422   -980    318       C\\nATOM   3001  CD1 ILE A 425       9.377  -2.939   8.685  1.00 69.86           C\\nANISOU 3001  CD1 ILE A 425    10448   7667   8427    435  -1000    194       C\\nATOM   3002  N   TYR A 426       5.302  -3.102  12.695  1.00 80.85           N\\nANISOU 3002  N   TYR A 426    11769  10077   8874   -571   -359    514       N\\nATOM   3003  CA  TYR A 426       4.811  -2.668  13.999  1.00 87.40           C\\nANISOU 3003  CA  TYR A 426    12467  11316   9424   -609   -172    444       C\\nATOM   3004  C   TYR A 426       4.159  -3.813  14.767  1.00 95.75           C\\nANISOU 3004  C   TYR A 426    13906  12427  10045   -980    -30    771       C\\nATOM   3005  O   TYR A 426       4.175  -3.815  16.004  1.00 99.16           O\\nANISOU 3005  O   TYR A 426    14463  13130  10085   -961     67    794       O\\nATOM   3006  CB  TYR A 426       3.826  -1.511  13.828  1.00 86.99           C\\nANISOU 3006  CB  TYR A 426    11825  11596   9630   -664     22    214       C\\nATOM   3007  CG  TYR A 426       4.370  -0.345  13.027  1.00 85.70           C\\nANISOU 3007  CG  TYR A 426    11311  11332   9920   -350   -120    -55       C\\nATOM   3008  CD1 TYR A 426       5.706   0.027  13.118  1.00 83.30           C\\nANISOU 3008  CD1 TYR A 426    11097  10869   9684      2   -327   -201       C\\nATOM   3009  CD2 TYR A 426       3.547   0.381  12.176  1.00 83.93           C\\nANISOU 3009  CD2 TYR A 426    10656  11172  10061   -422    -61   -137       C\\nATOM   3010  CE1 TYR A 426       6.206   1.093  12.385  1.00 79.72           C\\nANISOU 3010  CE1 TYR A 426    10330  10311   9648    224   -438   -408       C\\nATOM   3011  CE2 TYR A 426       4.037   1.447  11.441  1.00 82.37           C\\nANISOU 3011  CE2 TYR A 426    10186  10845  10265   -163   -196   -323       C\\nATOM   3012  CZ  TYR A 426       5.368   1.799  11.548  1.00 77.29           C\\nANISOU 3012  CZ  TYR A 426     9656  10030   9679    135   -368   -452       C\\nATOM   3013  OH  TYR A 426       5.859   2.858  10.815  1.00 65.48           O\\nANISOU 3013  OH  TYR A 426     7898   8395   8588    330   -485   -601       O\\nATOM   3014  N   THR A 427       3.583  -4.790  14.059  1.00 94.12           N\\nANISOU 3014  N   THR A 427    13912  11967   9880  -1346    -21   1029       N\\nATOM   3015  CA  THR A 427       2.981  -5.936  14.735  1.00 94.73           C\\nANISOU 3015  CA  THR A 427    14395  12024   9574  -1766    104   1385       C\\nATOM   3016  C   THR A 427       4.036  -6.873  15.301  1.00 93.77           C\\nANISOU 3016  C   THR A 427    14923  11553   9151  -1581   -115   1608       C\\nATOM   3017  O   THR A 427       3.779  -7.565  16.293  1.00107.23           O\\nANISOU 3017  O   THR A 427    16989  13325  10429  -1808    -22   1896       O\\nATOM   3018  CB  THR A 427       2.076  -6.711  13.777  1.00 92.02           C\\nANISOU 3018  CB  THR A 427    14101  11462   9402  -2246    135   1572       C\\nATOM   3019  OG1 THR A 427       2.869  -7.267  12.722  1.00 87.69           O\\nANISOU 3019  OG1 THR A 427    13873  10378   9067  -2083   -148   1577       O\\nATOM   3020  CG2 THR A 427       1.028  -5.801  13.182  1.00 92.49           C\\nANISOU 3020  CG2 THR A 427    13488  11881   9771  -2397    298   1371       C\\nATOM   3021  N   THR A 428       5.216  -6.918  14.687  1.00 86.78           N\\nANISOU 3021  N   THR A 428    14188  10309   8477  -1167   -404   1497       N\\nATOM   3022  CA  THR A 428       6.250  -7.850  15.112  1.00 80.90           C\\nANISOU 3022  CA  THR A 428    14030   9197   7512   -924   -656   1699       C\\nATOM   3023  C   THR A 428       7.087  -7.298  16.260  1.00 88.26           C\\nANISOU 3023  C   THR A 428    14945  10410   8178   -536   -758   1595       C\\nATOM   3024  O   THR A 428       7.228  -7.954  17.297  1.00 98.04           O\\nANISOU 3024  O   THR A 428    16618  11653   8981   -567   -810   1867       O\\nATOM   3025  CB  THR A 428       7.162  -8.200  13.934  1.00 75.14           C\\nANISOU 3025  CB  THR A 428    13433   7992   7124   -626   -905   1599       C\\nATOM   3026  OG1 THR A 428       6.369  -8.438  12.764  1.00 66.95           O\\nANISOU 3026  OG1 THR A 428    12310   6784   6344   -965   -819   1592       O\\nATOM   3027  CG2 THR A 428       7.977  -9.450  14.258  1.00 74.10           C\\nANISOU 3027  CG2 THR A 428    13971   7385   6798   -439  -1156   1861       C\\nATOM   3028  N   PHE A 429       7.642  -6.097  16.092  1.00 82.80           N\\nANISOU 3028  N   PHE A 429    13778   9948   7733   -194   -807   1216       N\\nATOM   3029  CA  PHE A 429       8.628  -5.569  17.024  1.00 85.65           C\\nANISOU 3029  CA  PHE A 429    14115  10520   7909    205   -988   1057       C\\nATOM   3030  C   PHE A 429       8.031  -4.731  18.145  1.00 88.27           C\\nANISOU 3030  C   PHE A 429    14208  11398   7933    109   -780    904       C\\nATOM   3031  O   PHE A 429       8.759  -4.373  19.077  1.00 94.52           O\\nANISOU 3031  O   PHE A 429    15046  12401   8467    386   -940    780       O\\nATOM   3032  CB  PHE A 429       9.666  -4.731  16.274  1.00 81.51           C\\nANISOU 3032  CB  PHE A 429    13220   9923   7826    606  -1176    717       C\\nATOM   3033  CG  PHE A 429      10.610  -5.545  15.451  1.00 86.84           C\\nANISOU 3033  CG  PHE A 429    14151  10141   8702    848  -1415    814       C\\nATOM   3034  CD1 PHE A 429      11.723  -6.132  16.031  1.00 95.71           C\\nANISOU 3034  CD1 PHE A 429    15590  11131   9647   1208  -1714    909       C\\nATOM   3035  CD2 PHE A 429      10.383  -5.736  14.099  1.00 90.50           C\\nANISOU 3035  CD2 PHE A 429    14539  10330   9515    740  -1348    797       C\\nATOM   3036  CE1 PHE A 429      12.597  -6.891  15.275  1.00100.77           C\\nANISOU 3036  CE1 PHE A 429    16434  11359  10493   1488  -1918    962       C\\nATOM   3037  CE2 PHE A 429      11.253  -6.492  13.334  1.00 94.15           C\\nANISOU 3037  CE2 PHE A 429    15239  10395  10137    990  -1533    835       C\\nATOM   3038  CZ  PHE A 429      12.362  -7.070  13.923  1.00 99.97           C\\nANISOU 3038  CZ  PHE A 429    16261  10992  10733   1381  -1805    907       C\\nATOM   3039  N   ASN A 430       6.743  -4.409  18.090  1.00 83.72           N\\nANISOU 3039  N   ASN A 430    13363  11080   7368   -257   -438    882       N\\nATOM   3040  CA  ASN A 430       6.116  -3.571  19.103  1.00 88.98           C\\nANISOU 3040  CA  ASN A 430    13756  12293   7759   -315   -190    673       C\\nATOM   3041  C   ASN A 430       4.910  -4.295  19.678  1.00 94.26           C\\nANISOU 3041  C   ASN A 430    14603  13185   8026   -804    139    994       C\\nATOM   3042  O   ASN A 430       3.949  -4.578  18.954  1.00 90.37           O\\nANISOU 3042  O   ASN A 430    13952  12628   7755  -1162    332   1116       O\\nATOM   3043  CB  ASN A 430       5.708  -2.218  18.523  1.00 82.34           C\\nANISOU 3043  CB  ASN A 430    12274  11632   7378   -219    -60    251       C\\nATOM   3044  CG  ASN A 430       5.177  -1.278  19.577  1.00 86.94           C\\nANISOU 3044  CG  ASN A 430    12575  12746   7711   -183    175    -57       C\\nATOM   3045  OD1 ASN A 430       3.978  -1.247  19.844  1.00 86.57           O\\nANISOU 3045  OD1 ASN A 430    12339  13023   7531   -474    525    -28       O\\nATOM   3046  ND2 ASN A 430       6.069  -0.510  20.193  1.00 93.49           N\\nANISOU 3046  ND2 ASN A 430    13362  13689   8473    174    -14   -380       N\\nATOM   3047  N   ILE A 431       4.963  -4.590  20.979  1.00 96.66           N\\nANISOU 3047  N   ILE A 431    15226  13779   7721   -842    197   1137       N\\nATOM   3048  CA  ILE A 431       3.848  -5.262  21.638  1.00 92.58           C\\nANISOU 3048  CA  ILE A 431    14883  13536   6757  -1346    552   1472       C\\nATOM   3049  C   ILE A 431       2.630  -4.348  21.695  1.00 98.55           C\\nANISOU 3049  C   ILE A 431    15013  14819   7614  -1537    984   1175       C\\nATOM   3050  O   ILE A 431       1.488  -4.806  21.569  1.00 98.81           O\\nANISOU 3050  O   ILE A 431    14936  14997   7611  -2018   1303   1397       O\\nATOM   3051  CB  ILE A 431       4.263  -5.738  23.042  1.00 91.00           C\\nANISOU 3051  CB  ILE A 431    15200  13558   5818  -1318    503   1710       C\\nATOM   3052  N   GLU A 432       2.851  -3.043  21.881  1.00 96.20           N\\nANISOU 3052  N   GLU A 432    14279  14803   7470  -1163    992    657       N\\nATOM   3053  CA  GLU A 432       1.733  -2.109  21.979  1.00 93.30           C\\nANISOU 3053  CA  GLU A 432    13305  14920   7225  -1248   1385    325       C\\nATOM   3054  C   GLU A 432       1.005  -1.971  20.646  1.00 90.82           C\\nANISOU 3054  C   GLU A 432    12560  14400   7549  -1408   1437    316       C\\nATOM   3055  O   GLU A 432      -0.230  -1.927  20.610  1.00 84.30           O\\nANISOU 3055  O   GLU A 432    11363  13912   6757  -1725   1791    333       O\\nATOM   3056  CB  GLU A 432       2.229  -0.750  22.471  1.00 88.42           C\\nANISOU 3056  CB  GLU A 432    12394  14544   6659   -774   1324   -250       C\\nATOM   3057  N   PHE A 433       1.747  -1.901  19.538  1.00 90.26           N\\nANISOU 3057  N   PHE A 433    12509  13817   7970  -1197   1087    288       N\\nATOM   3058  CA  PHE A 433       1.098  -1.850  18.232  1.00 93.03           C\\nANISOU 3058  CA  PHE A 433    12520  13969   8860  -1363   1090    317       C\\nATOM   3059  C   PHE A 433       0.366  -3.155  17.929  1.00 92.59           C\\nANISOU 3059  C   PHE A 433    12717  13789   8674  -1909   1194    776       C\\nATOM   3060  O   PHE A 433      -0.768  -3.136  17.438  1.00 86.48           O\\nANISOU 3060  O   PHE A 433    11554  13195   8111  -2229   1396    805       O\\nATOM   3061  CB  PHE A 433       2.125  -1.540  17.137  1.00 94.23           C\\nANISOU 3061  CB  PHE A 433    12696  13628   9479  -1036    712    208       C\\nATOM   3062  CG  PHE A 433       2.253  -0.070  16.807  1.00 90.02           C\\nANISOU 3062  CG  PHE A 433    11657  13176   9371   -672    669   -233       C\\nATOM   3063  CD1 PHE A 433       1.220   0.604  16.178  1.00 82.18           C\\nANISOU 3063  CD1 PHE A 433    10137  12335   8753   -746    821   -367       C\\nATOM   3064  CD2 PHE A 433       3.413   0.630  17.106  1.00 88.82           C\\nANISOU 3064  CD2 PHE A 433    11559  12920   9269   -265    446   -498       C\\nATOM   3065  CE1 PHE A 433       1.331   1.949  15.867  1.00 78.56           C\\nANISOU 3065  CE1 PHE A 433     9265  11877   8709   -401    756   -738       C\\nATOM   3066  CE2 PHE A 433       3.531   1.976  16.796  1.00 82.75           C\\nANISOU 3066  CE2 PHE A 433    10368  12155   8919     24    394   -882       C\\nATOM   3067  CZ  PHE A 433       2.487   2.635  16.177  1.00 81.74           C\\nANISOU 3067  CZ  PHE A 433     9768  12128   9161    -34    550   -991       C\\nATOM   3068  N   ARG A 434       0.991  -4.296  18.232  1.00 96.08           N\\nANISOU 3068  N   ARG A 434    13805  13913   8786  -2025   1037   1134       N\\nATOM   3069  CA  ARG A 434       0.385  -5.588  17.918  1.00 91.88           C\\nANISOU 3069  CA  ARG A 434    13600  13146   8164  -2562   1089   1576       C\\nATOM   3070  C   ARG A 434      -0.930  -5.778  18.663  1.00 88.38           C\\nANISOU 3070  C   ARG A 434    12942  13229   7411  -3068   1532   1730       C\\nATOM   3071  O   ARG A 434      -1.944  -6.162  18.068  1.00 89.59           O\\nANISOU 3071  O   ARG A 434    12864  13413   7764  -3530   1674   1870       O\\nATOM   3072  CB  ARG A 434       1.360  -6.718  18.249  1.00 91.99           C\\nANISOU 3072  CB  ARG A 434    14390  12689   7871  -2520    823   1923       C\\nATOM   3073  N   LYS A 435      -0.934  -5.515  19.973  1.00 92.30           N\\nANISOU 3073  N   LYS A 435    13491  14183   7397  -3005   1759   1697       N\\nATOM   3074  CA  LYS A 435      -2.157  -5.679  20.753  1.00 95.80           C\\nANISOU 3074  CA  LYS A 435    13709  15207   7485  -3485   2243   1837       C\\nATOM   3075  C   LYS A 435      -3.199  -4.633  20.385  1.00 95.39           C\\nANISOU 3075  C   LYS A 435    12798  15636   7810  -3466   2525   1447       C\\nATOM   3076  O   LYS A 435      -4.399  -4.865  20.566  1.00100.11           O\\nANISOU 3076  O   LYS A 435    13054  16654   8329  -3942   2904   1572       O\\nATOM   3077  CB  LYS A 435      -1.843  -5.617  22.249  1.00100.45           C\\nANISOU 3077  CB  LYS A 435    14594  16206   7366  -3383   2418   1871       C\\nATOM   3078  N   ALA A 436      -2.763  -3.482  19.869  1.00 97.48           N\\nANISOU 3078  N   ALA A 436    12695  15840   8503  -2926   2339    989       N\\nATOM   3079  CA  ALA A 436      -3.711  -2.457  19.446  1.00 99.12           C\\nANISOU 3079  CA  ALA A 436    12109  16422   9131  -2835   2542    627       C\\nATOM   3080  C   ALA A 436      -4.463  -2.884  18.193  1.00 98.71           C\\nANISOU 3080  C   ALA A 436    11791  16164   9549  -3194   2456    809       C\\nATOM   3081  O   ALA A 436      -5.682  -2.702  18.103  1.00 98.79           O\\nANISOU 3081  O   ALA A 436    11222  16613   9701  -3464   2744    764       O\\nATOM   3082  CB  ALA A 436      -2.984  -1.133  19.210  1.00 94.08           C\\nANISOU 3082  CB  ALA A 436    11230  15675   8839  -2179   2321    134       C\\nATOM   3083  N   PHE A 437      -3.753  -3.456  17.217  1.00 90.64           N\\nANISOU 3083  N   PHE A 437    11168  14510   8763  -3193   2056    991       N\\nATOM   3084  CA  PHE A 437      -4.405  -3.888  15.985  1.00 89.75           C\\nANISOU 3084  CA  PHE A 437    10864  14185   9052  -3536   1925   1136       C\\nATOM   3085  C   PHE A 437      -5.403  -5.004  16.256  1.00 98.61           C\\nANISOU 3085  C   PHE A 437    12055  15479   9935  -4263   2173   1518       C\\nATOM   3086  O   PHE A 437      -6.491  -5.031  15.669  1.00 97.68           O\\nANISOU 3086  O   PHE A 437    11436  15585  10092  -4617   2265   1534       O\\nATOM   3087  CB  PHE A 437      -3.365  -4.353  14.965  1.00 85.17           C\\nANISOU 3087  CB  PHE A 437    10775  12904   8681  -3381   1477   1231       C\\nATOM   3088  CG  PHE A 437      -2.480  -3.255  14.437  1.00 86.40           C\\nANISOU 3088  CG  PHE A 437    10779  12886   9165  -2763   1230    890       C\\nATOM   3089  CD1 PHE A 437      -2.661  -1.937  14.822  1.00 90.40           C\\nANISOU 3089  CD1 PHE A 437    10767  13767   9814  -2388   1365    522       C\\nATOM   3090  CD2 PHE A 437      -1.469  -3.548  13.540  1.00 80.59           C\\nANISOU 3090  CD2 PHE A 437    10422  11598   8603  -2569    873    931       C\\nATOM   3091  CE1 PHE A 437      -1.838  -0.938  14.328  1.00 85.90           C\\nANISOU 3091  CE1 PHE A 437    10090  12981   9568  -1879   1127    241       C\\nATOM   3092  CE2 PHE A 437      -0.645  -2.555  13.044  1.00 80.08           C\\nANISOU 3092  CE2 PHE A 437    10206  11388   8833  -2065    672    655       C\\nATOM   3093  CZ  PHE A 437      -0.831  -1.248  13.438  1.00 81.28           C\\nANISOU 3093  CZ  PHE A 437     9867  11875   9140  -1744    789    329       C\\nATOM   3094  N   LEU A 438      -5.047  -5.938  17.144  1.00 97.43           N\\nANISOU 3094  N   LEU A 438    12520  15222   9276  -4511   2262   1848       N\\nATOM   3095  CA  LEU A 438      -5.930  -7.059  17.446  1.00 99.16           C\\nANISOU 3095  CA  LEU A 438    12887  15540   9250  -5265   2497   2270       C\\nATOM   3096  C   LEU A 438      -7.187  -6.605  18.176  1.00104.88           C\\nANISOU 3096  C   LEU A 438    12926  17091   9832  -5548   3020   2189       C\\nATOM   3097  O   LEU A 438      -8.233  -7.257  18.066  1.00112.28           O\\nANISOU 3097  O   LEU A 438    13646  18228  10786  -6211   3228   2440       O\\nATOM   3098  CB  LEU A 438      -5.179  -8.106  18.269  1.00101.79           C\\nANISOU 3098  CB  LEU A 438    14093  15526   9057  -5410   2445   2676       C\\nATOM   3099  N   LYS A 439      -7.108  -5.501  18.923  1.00104.77           N\\nANISOU 3099  N   LYS A 439    12553  17573   9684  -5064   3242   1817       N\\nATOM   3100  CA  LYS A 439      -8.295  -4.960  19.574  1.00111.86           C\\nANISOU 3100  CA  LYS A 439    12728  19296  10480  -5232   3763   1648       C\\nATOM   3101  C   LYS A 439      -9.200  -4.234  18.588  1.00113.57           C\\nANISOU 3101  C   LYS A 439    12089  19730  11334  -5165   3740   1359       C\\nATOM   3102  O   LYS A 439     -10.419  -4.192  18.788  1.00116.22           O\\nANISOU 3102  O   LYS A 439    11788  20658  11710  -5514   4113   1349       O\\nATOM   3103  CB  LYS A 439      -7.894  -4.019  20.711  1.00111.35           C\\nANISOU 3103  CB  LYS A 439    12602  19665  10042  -4703   3997   1288       C\\nATOM   3104  N   ILE A 440      -8.629  -3.664  17.526  1.00111.11           N\\nANISOU 3104  N   ILE A 440    11741  18958  11519  -4713   3295   1139       N\\nATOM   3105  CA  ILE A 440      -9.451  -3.036  16.502  1.00110.51           C\\nANISOU 3105  CA  ILE A 440    10923  19028  12037  -4650   3192    931       C\\nATOM   3106  C   ILE A 440     -10.182  -4.088  15.675  1.00112.85           C\\nANISOU 3106  C   ILE A 440    11191  19185  12503  -5352   3077   1285       C\\nATOM   3107  O   ILE A 440     -11.326  -3.874  15.259  1.00112.91           O\\nANISOU 3107  O   ILE A 440    10465  19613  12823  -5584   3184   1219       O\\nATOM   3108  CB  ILE A 440      -8.581  -2.115  15.629  1.00104.69           C\\nANISOU 3108  CB  ILE A 440    10219  17834  11725  -3988   2753    640       C\\nATOM   3109  CG1 ILE A 440      -7.927  -1.040  16.500  1.00107.61           C\\nANISOU 3109  CG1 ILE A 440    10580  18352  11953  -3351   2868    257       C\\nATOM   3110  CG2 ILE A 440      -9.411  -1.469  14.537  1.00101.39           C\\nANISOU 3110  CG2 ILE A 440     9088  17539  11896  -3905   2594    477       C\\nATOM   3111  CD1 ILE A 440      -7.131  -0.015  15.728  1.00100.57           C\\nANISOU 3111  CD1 ILE A 440     9658  17052  11502  -2734   2483    -35       C\\nATOM   3112  N   LEU A 441      -9.554  -5.245  15.440  1.00112.02           N\\nANISOU 3112  N   LEU A 441    11866  18490  12207  -5698   2844   1648       N\\nATOM   3113  CA  LEU A 441     -10.167  -6.342  14.697  1.00113.38           C\\nANISOU 3113  CA  LEU A 441    12136  18432  12510  -6402   2704   1969       C\\nATOM   3114  C   LEU A 441     -10.959  -7.287  15.593  1.00125.26           C\\nANISOU 3114  C   LEU A 441    13779  20090  13724  -6864   2989   2236       C\\nATOM   3115  O   LEU A 441     -11.000  -8.499  15.335  1.00130.59           O\\nANISOU 3115  O   LEU A 441    14979  20276  14364  -7284   2800   2536       O\\nATOM   3116  CB  LEU A 441      -9.096  -7.115  13.924  1.00105.56           C\\nANISOU 3116  CB  LEU A 441    11981  16582  11546  -6372   2234   2137       C\\nATOM   3117  CG  LEU A 441      -8.272  -6.304  12.915  1.00100.01           C\\nANISOU 3117  CG  LEU A 441    11276  15521  11203  -5710   1825   1833       C\\nATOM   3118  CD1 LEU A 441      -7.049  -7.083  12.435  1.00 92.92           C\\nANISOU 3118  CD1 LEU A 441    11249  13839  10218  -5600   1460   1975       C\\nATOM   3119  CD2 LEU A 441      -9.133  -5.880  11.735  1.00101.27           C\\nANISOU 3119  CD2 LEU A 441    10791  15843  11843  -5803   1635   1687       C\\nATOM   3120  N   HIS A 442     -11.587  -6.766  16.640  1.00118.20           N\\nANISOU 3120  N   HIS A 442    12431  19851  12628  -6779   3439   2114       N\\nATOM   3121  CA  HIS A 442     -12.365  -7.591  17.554  1.00126.48           C\\nANISOU 3121  CA  HIS A 442    13562  21110  13385  -7224   3754   2376       C\\nATOM   3122  C   HIS A 442     -13.375  -6.752  18.337  1.00131.96           C\\nANISOU 3122  C   HIS A 442    13462  22622  14057  -7071   4227   2114       C\\nATOM   3123  O   HIS A 442     -14.028  -5.864  17.785  1.00131.46           O\\nANISOU 3123  O   HIS A 442    12638  22887  14424  -6809   4221   1787       O\\nATOM   3124  CB  HIS A 442     -11.436  -8.335  18.515  1.00127.27           C\\nANISOU 3124  CB  HIS A 442    14545  20900  12913  -7295   3807   2692       C\\nCONECT    1    2\\nCONECT    2    1    5    3\\nCONECT    3    2    4    6\\nCONECT    4    3\\nCONECT    5    2\\nCONECT    6    7    3\\nCONECT    7    6   10    8\\nCONECT    8    7    9   11\\nCONECT    9    8\\nCONECT   10    7\\nCONECT   58   59   53\\nCONECT   59   58   62   60\\nCONECT   60   59   61   63\\nCONECT   61   60\\nCONECT   62   59\\nCONECT  194  195  185\\nCONECT  195  194  198  196\\nCONECT  196  195  197  199\\nCONECT  197  196\\nCONECT  198  195\\nCONECT  199  200  196\\nCONECT  200  199  203  201\\nCONECT  201  200  202  204\\nCONECT  202  201\\nCONECT  203  200\\nCONECT  451  452  444\\nCONECT  452  451  455  453\\nCONECT  453  452  454  456\\nCONECT  454  453\\nCONECT  455  452\\nCONECT  467  468  465\\nCONECT  468  467  471  469\\nCONECT  469  468  470  472\\nCONECT  470  469\\nCONECT  471  468\\nCONECT  486  487  474\\nCONECT  487  486  490  488\\nCONECT  488  487  489  491\\nCONECT  489  488\\nCONECT  490  487\\nCONECT  542 1057  541\\nCONECT  772  778  773  766\\nCONECT  773  772  776  774\\nCONECT  774  773  775\\nCONECT  775  774\\nCONECT  776  773  777\\nCONECT  777  776  778\\nCONECT  778  772  777\\nCONECT  779  780\\nCONECT  780  779  783  781\\nCONECT  781  780  782  784\\nCONECT  782  781\\nCONECT  783  780\\nCONECT  784  785  781\\nCONECT  785  784  788  786\\nCONECT  786  785  787  789\\nCONECT  787  786\\nCONECT  788  785\\nCONECT  801  802  791\\nCONECT  802  801  805  803\\nCONECT  803  802  804  806\\nCONECT  804  803\\nCONECT  805  802\\nCONECT  812  813  808\\nCONECT  813  812  816  814\\nCONECT  814  813  815  817\\nCONECT  815  814\\nCONECT  816  813\\nCONECT  817  818  814\\nCONECT  818  817  821  819\\nCONECT  819  818  820  822\\nCONECT  820  819\\nCONECT  821  818\\nCONECT 1018 1019 1012\\nCONECT 1019 1018 1022 1020\\nCONECT 1020 1019 1021 1023\\nCONECT 1021 1020\\nCONECT 1022 1019\\nCONECT 1028 1029 1025\\nCONECT 1029 1028 1032 1030\\nCONECT 1030 1029 1031 1033\\nCONECT 1031 1030\\nCONECT 1032 1029\\nCONECT 1033 1034 1030\\nCONECT 1034 1033 1037 1035\\nCONECT 1035 1034 1036 1038\\nCONECT 1036 1035\\nCONECT 1037 1034\\nCONECT 1038 1039 1035\\nCONECT 1039 1038 1042 1040\\nCONECT 1040 1039 1041 1043\\nCONECT 1041 1040\\nCONECT 1042 1039\\nCONECT 1057  542 1056\\nCONECT 1282 1283 1276\\nCONECT 1283 1282 1286 1284\\nCONECT 1284 1283 1285 1289\\nCONECT 1285 1284\\nCONECT 1286 1283 1287\\nCONECT 1287 1286 1288\\nCONECT 1288 1287\\nCONECT 1332 1333 1326\\nCONECT 1333 1332 1336 1334\\nCONECT 1334 1333 1335 1337\\nCONECT 1335 1334\\nCONECT 1336 1333\\nCONECT 1337 1338 1334\\nCONECT 1338 1337 1341 1339\\nCONECT 1339 1338 1340 1342\\nCONECT 1340 1339\\nCONECT 1341 1338\\nCONECT 1364 1365 1355\\nCONECT 1365 1364 1368 1366\\nCONECT 1366 1365 1367 1369\\nCONECT 1367 1366\\nCONECT 1368 1365\\nCONECT 1369 1370 1366\\nCONECT 1370 1369 1373 1371\\nCONECT 1371 1370 1372 1374\\nCONECT 1372 1371\\nCONECT 1373 1370\\nCONECT 1493 1494 1487\\nCONECT 1494 1493 1497 1495\\nCONECT 1495 1494 1496 1498\\nCONECT 1496 1495\\nCONECT 1497 1494\\nCONECT 1518 1519 1508\\nCONECT 1519 1518 1522 1520\\nCONECT 1520 1519 1521 1523\\nCONECT 1521 1520\\nCONECT 1522 1519\\nCONECT 1538 1539 1533\\nCONECT 1539 1538 1542 1540\\nCONECT 1540 1539 1541 1543\\nCONECT 1541 1540\\nCONECT 1542 1539\\nCONECT 1612 1613 1604\\nCONECT 1613 1612 1616 1614\\nCONECT 1614 1613 1615 1617\\nCONECT 1615 1614\\nCONECT 1616 1613\\nCONECT 1617 1618 1614\\nCONECT 1618 1617 1621 1619\\nCONECT 1619 1618 1620 1622\\nCONECT 1620 1619\\nCONECT 1621 1618\\nCONECT 1629 1630 1624\\nCONECT 1630 1629 1633 1631\\nCONECT 1631 1630 1632 1634\\nCONECT 1632 1631\\nCONECT 1633 1630\\nCONECT 1634 1635 1631\\nCONECT 1635 1634 1638 1636\\nCONECT 1636 1635 1637 1639\\nCONECT 1637 1636\\nCONECT 1638 1635\\nCONECT 1646 1647 1641\\nCONECT 1647 1646 1650 1648\\nCONECT 1648 1647 1649 1651\\nCONECT 1649 1648\\nCONECT 1650 1647\\nCONECT 1659 1660 1653\\nCONECT 1660 1659 1663 1661\\nCONECT 1661 1660 1662 1664\\nCONECT 1662 1661\\nCONECT 1663 1660\\nCONECT 1683 1684 1676\\nCONECT 1684 1683 1687 1685\\nCONECT 1685 1684 1686 1688\\nCONECT 1686 1685\\nCONECT 1687 1684\\nCONECT 1688 1689 1685\\nCONECT 1689 1688 1692 1690\\nCONECT 1690 1689 1691 1693\\nCONECT 1691 1690\\nCONECT 1692 1689\\nCONECT 1709 1710 1703\\nCONECT 1710 1709 1713 1711\\nCONECT 1711 1710 1712 1714\\nCONECT 1712 1711\\nCONECT 1713 1710\\nCONECT 1719 1720 1716\\nCONECT 1720 1719 1723 1721\\nCONECT 1721 1720 1722 1724\\nCONECT 1722 1721\\nCONECT 1723 1720\\nCONECT 1739 1740 1730\\nCONECT 1740 1739 1743 1741\\nCONECT 1741 1740 1742 1744\\nCONECT 1742 1741\\nCONECT 1743 1740\\nCONECT 1744 1745 1741\\nCONECT 1745 1744 1748 1746\\nCONECT 1746 1745 1747 1749\\nCONECT 1747 1746\\nCONECT 1748 1745\\nCONECT 1749 1750 1746\\nCONECT 1750 1749 1753 1751\\nCONECT 1751 1750 1752 1754\\nCONECT 1752 1751\\nCONECT 1753 1750\\nCONECT 1758 1759 1756\\nCONECT 1759 1758 1762 1760\\nCONECT 1760 1759 1761 1763\\nCONECT 1761 1760\\nCONECT 1762 1759\\nCONECT 1778 1779 1773\\nCONECT 1779 1778 1782 1780\\nCONECT 1780 1779 1781 1783\\nCONECT 1781 1780\\nCONECT 1782 1779\\nCONECT 1814 1815 1807\\nCONECT 1815 1814 1818 1816\\nCONECT 1816 1815 1817 1819\\nCONECT 1817 1816\\nCONECT 1818 1815\\nCONECT 1926 1927 1920\\nCONECT 1927 1926 1930 1928\\nCONECT 1928 1927 1929 1931\\nCONECT 1929 1928\\nCONECT 1930 1927\\nCONECT 1944 1945 1941\\nCONECT 1945 1944 1948 1946\\nCONECT 1946 1945 1947 1949\\nCONECT 1947 1946\\nCONECT 1948 1945\\nCONECT 1957 1958 1951\\nCONECT 1958 1957 1961 1959\\nCONECT 1959 1958 1960 1962\\nCONECT 1960 1959\\nCONECT 1961 1958\\nCONECT 2187 2188 2182\\nCONECT 2188 2187 2191 2189\\nCONECT 2189 2188 2190 2192\\nCONECT 2190 2189\\nCONECT 2191 2188\\nCONECT 2285 2286 2273\\nCONECT 2286 2285 2289 2287\\nCONECT 2287 2286 2288 2290\\nCONECT 2288 2287\\nCONECT 2289 2286\\nCONECT 2309 2310 2306\\nCONECT 2310 2309 2313 2311\\nCONECT 2311 2310 2312 2314\\nCONECT 2312 2311\\nCONECT 2313 2310\\nCONECT 2335 2336 2332\\nCONECT 2336 2335 2339 2337\\nCONECT 2337 2336 2338 2340\\nCONECT 2338 2337\\nCONECT 2339 2336\\nCONECT 2346 2347 2342\\nCONECT 2347 2346 2350 2348\\nCONECT 2348 2347 2349 2351\\nCONECT 2349 2348\\nCONECT 2350 2347\\nCONECT 2385 2386 2379\\nCONECT 2386 2385 2389 2387\\nCONECT 2387 2386 2388 2390\\nCONECT 2388 2387\\nCONECT 2389 2386\\nCONECT 2428 2429 2425\\nCONECT 2429 2428 2432 2430\\nCONECT 2430 2429 2431 2433\\nCONECT 2431 2430\\nCONECT 2432 2429\\nCONECT 2506 2507 2504\\nCONECT 2507 2506 2510 2508\\nCONECT 2508 2507 2509 2511\\nCONECT 2509 2508\\nCONECT 2510 2507\\nCONECT 2538 2539 2535\\nCONECT 2539 2538 2542 2540\\nCONECT 2540 2539 2541\\nCONECT 2541 2540\\nCONECT 2542 2539 2543\\nCONECT 2543 2542 2544 2545\\nCONECT 2544 2543 2546\\nCONECT 2545 2543 2547\\nCONECT 2546 2544 2548\\nCONECT 2547 2545 2548\\nCONECT 2548 2546 2547 2549\\nCONECT 2549 2548\\nCONECT 2550 2551\\nCONECT 2551 2550 2554 2552\\nCONECT 2552 2551 2553 2555\\nCONECT 2553 2552\\nCONECT 2554 2551\\nCONECT 2555 2556 2552\\nCONECT 2556 2555 2559 2557\\nCONECT 2557 2556 2558 2560\\nCONECT 2558 2557\\nCONECT 2559 2556\\nCONECT 2560 2561 2557\\nCONECT 2561 2560 2564 2562\\nCONECT 2562 2561 2563 2565\\nCONECT 2563 2562\\nCONECT 2564 2561\\nCONECT 2565 2566 2562\\nCONECT 2566 2565 2569 2567\\nCONECT 2567 2566 2568 2570\\nCONECT 2568 2567\\nCONECT 2569 2566\\nCONECT 2579 2580 2572\\nCONECT 2580 2579 2583 2581\\nCONECT 2581 2580 2582 2584\\nCONECT 2582 2581\\nCONECT 2583 2580\\nCONECT 2584 2585 2581\\nCONECT 2585 2584 2588 2586\\nCONECT 2586 2585 2587 2589\\nCONECT 2587 2586\\nCONECT 2588 2585\\nCONECT 2768 2769 2760\\nCONECT 2769 2768 2772 2770\\nCONECT 2770 2769 2771 2773\\nCONECT 2771 2770\\nCONECT 2772 2769\\nCONECT 2797 2798 2791\\nCONECT 2798 2797 2801 2799\\nCONECT 2799 2798 2800 2802\\nCONECT 2800 2799\\nCONECT 2801 2798\\nCONECT 2807 2818 2806\\nCONECT 2808 2809 2804\\nCONECT 2809 2808 2812 2810\\nCONECT 2810 2809 2811 2813\\nCONECT 2811 2810\\nCONECT 2812 2809\\nCONECT 2818 2807 2817\\nCONECT 2849 2850 2844\\nCONECT 2850 2849 2853 2851\\nCONECT 2851 2850 2852 2854\\nCONECT 2852 2851\\nCONECT 2853 2850\\nCONECT 2854 2855 2851\\nCONECT 2855 2854 2858 2856\\nCONECT 2856 2855 2857 2859\\nCONECT 2857 2856\\nCONECT 2858 2855\\nCONECT 3047 3048 3041\\nCONECT 3048 3047 3051 3049\\nCONECT 3049 3048 3050 3052\\nCONECT 3050 3049\\nCONECT 3051 3048\\nCONECT 3052 3053 3049\\nCONECT 3053 3052 3056 3054\\nCONECT 3054 3053 3055 3057\\nCONECT 3055 3054\\nCONECT 3056 3053\\nCONECT 3068 3069 3059\\nCONECT 3069 3068 3072 3070\\nCONECT 3070 3069 3071 3073\\nCONECT 3071 3070\\nCONECT 3072 3069\\nCONECT 3073 3074 3070\\nCONECT 3074 3073 3077 3075\\nCONECT 3075 3074 3076 3078\\nCONECT 3076 3075\\nCONECT 3077 3074\\nCONECT 3094 3095 3085\\nCONECT 3095 3094 3098 3096\\nCONECT 3096 3095 3097 3099\\nCONECT 3097 3096\\nCONECT 3098 3095\\nCONECT 3099 3100 3096\\nCONECT 3100 3099 3103 3101\\nCONECT 3101 3100 3102 3104\\nCONECT 3102 3101\\nCONECT 3103 3100\\nCONECT 3120 3121 3114\\nCONECT 3121 3120 3124 3122\\nCONECT 3122 3121 3123\\nCONECT 3123 3122\\nCONECT 3124 3121\\nEND\\n\",\"pdb\");\n",
       "\tviewer_1716807258097742.setStyle({\"model\": 0},{\"cartoon\": {}});\n",
       "\tviewer_1716807258097742.addSurface(null,{\"opacity\": 1, \"color\": \"lightgray\"});\n",
       "\tviewer_1716807258097742.addModels(\"HETATM    1 C94  UNL   1        8.221   2.938 -13.874  1.00  0.00           C  \\nHETATM    2 C95  UNL   1        7.345   3.829 -13.234  1.00  0.00           C  \\nHETATM    3 C96  UNL   1        6.076   3.425 -12.847  1.00  0.00           C  \\nHETATM    4 C97  UNL   1        5.649   2.155 -13.231  1.00  0.00           C  \\nHETATM    5 C98  UNL   1        6.492   1.212 -13.886  1.00  0.00           C  \\nHETATM    6 C99  UNL   1        7.829   1.594 -14.141  1.00  0.00           C  \\nHETATM    7 C100 UNL   1        5.822  -0.102 -14.294  1.00  0.00           C  \\nHETATM    8 C101 UNL   1        4.375  -0.167 -13.812  1.00  0.00           C  \\nHETATM    9 C102 UNL   1        3.493  -0.426 -14.792  1.00  0.00           C  \\nHETATM   10 C103 UNL   1        4.249  -0.613 -16.015  1.00  0.00           C  \\nHETATM   11 C104 UNL   1        5.612  -0.438 -15.769  1.00  0.00           C  \\nHETATM   12 N14  UNL   1        6.594  -0.619 -16.686  1.00  0.00           N  \\nHETATM   13 C105 UNL   1        6.156  -0.971 -17.920  1.00  0.00           C  \\nHETATM   14 C106 UNL   1        4.812  -1.144 -18.260  1.00  0.00           C  \\nHETATM   15 C107 UNL   1        3.832  -0.963 -17.283  1.00  0.00           C  \\nHETATM   16 O10  UNL   1        6.529  -1.190 -13.678  1.00  0.00           O  \\nHETATM   17 N15  UNL   1        5.169   4.344 -12.308  1.00  0.00           N  \\nHETATM   18 N16  UNL   1        8.736   0.743 -14.814  1.00  0.00           N  \\nHETATM   19 C108 UNL   1        9.633   4.281 -15.307  1.00  0.00           C  \\nHETATM   20 C109 UNL   1        9.560   3.472 -14.237  1.00  0.00           C  \\nHETATM   21 N17  UNL   1       10.596   3.098 -13.416  1.00  0.00           N  \\nHETATM   22 C110 UNL   1       10.846   4.978 -15.836  1.00  0.00           C  \\nHETATM   23 N18  UNL   1       13.744   5.012 -16.349  1.00  0.00           N  \\nHETATM   24 C111 UNL   1       12.929   4.168 -16.892  1.00  0.00           C  \\nHETATM   25 N19  UNL   1       11.599   4.020 -16.611  1.00  0.00           N  \\nHETATM   26 N20  UNL   1       15.002   4.934 -16.841  1.00  0.00           N  \\nCONECT    1    2    2    6   20\\nCONECT    2    1    1    3\\nCONECT    6    1    5    5   18\\nCONECT   20    1   19   19   21\\nCONECT    3    2    4    4   17\\nCONECT    4    3    3    5\\nCONECT   17    3\\nCONECT    5    4    6    6    7\\nCONECT    7    5    8   11   16\\nCONECT   18    6\\nCONECT    8    7    9    9\\nCONECT   11    7   10   10   12\\nCONECT   16    7\\nCONECT    9    8    8   10\\nCONECT   10    9   11   11   15\\nCONECT   15   10   14   14\\nCONECT   12   11   13   13\\nCONECT   13   12   12   14\\nCONECT   14   13   15   15\\nCONECT   19   20   20   22\\nCONECT   22   19   25\\nCONECT   21   20\\nCONECT   25   22   24\\nCONECT   23   24   24   26\\nCONECT   24   23   23   25\\nCONECT   26   23\\nEND\",\"pdb\");\n",
       "\tviewer_1716807258097742.setStyle({\"model\": 1},{\"stick\": {\"color\": \"cyan\"}});\n",
       "\tviewer_1716807258097742.zoomTo();\n",
       "viewer_1716807258097742.render();\n",
       "});\n",
       "</script>"
      ]
     },
     "metadata": {},
     "output_type": "display_data"
    }
   ],
   "source": [
    "show_ligand_and_protein(ligands[0])\n",
    "show_ligand_and_protein(ligands[1])"
   ]
  },
  {
   "cell_type": "markdown",
   "metadata": {},
   "source": [
    "Alrighty, that seems interesting all ligands are binding at the same pocket, which is nice since this is also the place where a drug named Risperidone is known to bind. The molecules are, of course, not Risperidone, however, which actually looks like this:"
   ]
  },
  {
   "cell_type": "code",
   "execution_count": 27,
   "metadata": {},
   "outputs": [
    {
     "name": "stderr",
     "output_type": "stream",
     "text": [
      "[12:56:50] SMILES Parse Error: syntax error while parsing: Risperidone\n",
      "[12:56:50] SMILES Parse Error: Failed parsing SMILES 'Risperidone' for input: 'Risperidone'\n"
     ]
    },
    {
     "data": {
      "image/png": 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",
      "text/plain": [
       "<PIL.PngImagePlugin.PngImageFile image mode=RGB size=1000x500>"
      ]
     },
     "execution_count": 27,
     "metadata": {},
     "output_type": "execute_result"
    }
   ],
   "source": [
    "risperidone = bam.molecule(\"Risperidone\")\n",
    "risperidone.chem2dview().draw()"
   ]
  },
  {
   "cell_type": "markdown",
   "metadata": {},
   "source": [
    "Still, our ligands do at least share some common structural features with Risperidone, which is encouraging given how incredibly simple our pipeline actually was and how small-scale the optimization was!"
   ]
  },
  {
   "cell_type": "markdown",
   "metadata": {},
   "source": [
    "And with that we have reached the end of this tutorial. Hopefully you now feel a little inspired for making your own molecule design pipeline with the help of BuildAMol! Thanks for checking out this tutorial and good luck with your research!"
   ]
  }
 ],
 "metadata": {
  "kernelspec": {
   "display_name": "glyco2",
   "language": "python",
   "name": "python3"
  },
  "language_info": {
   "codemirror_mode": {
    "name": "ipython",
    "version": 3
   },
   "file_extension": ".py",
   "mimetype": "text/x-python",
   "name": "python",
   "nbconvert_exporter": "python",
   "pygments_lexer": "ipython3",
   "version": "3.11.0"
  }
 },
 "nbformat": 4,
 "nbformat_minor": 2
}