CNRS Nantes University UFIP UFIP
home |  start a new run |  job status |  references&downloads |  examples |  help  

Should you encounter any unexpected behaviour,
please let us know.


***    ***

elNémo ID: 21021621200628711

Job options:

ID        	=	 21021621200628711
JOBID     	=	 
USERID    	=	 unknown
PRIVAT    	=	 0

NMODES    	=	 5
DQMIN     	=	 -100
DQMAX     	=	 100
DQSTEP    	=	 20
DOGRAPHS  	=	 on

DOPROJMODS	=	 on
DORMSD    	=	 on

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:


CRYST1   34.436   54.339   76.583  90.00  90.00  90.00 P 21 21 21
SCALE1      0.029039  0.000000  0.000000        0.00000
SCALE2      0.000000  0.018403  0.000000        0.00000
SCALE3      0.000000  0.000000  0.013058        0.00000
ATOM      1  N   MET A   0       0.149 -16.915  14.825  1.00 39.65           N
ATOM      2  CA  MET A   0       0.775 -16.993  13.508  1.00 37.18           C
ATOM      3  C   MET A   0       1.930 -16.008  13.399  1.00 32.37           C
ATOM      4  O   MET A   0       2.010 -15.041  14.154  1.00 33.30           O
ATOM      5  CB  MET A   0      -0.248 -16.712  12.414  1.00 35.93           C
ATOM      6  CG  MET A   0      -0.909 -15.370  12.596  1.00 29.38           C
ATOM      7  SD  MET A   0      -2.196 -15.043  11.389  1.00 28.66           S
ATOM      8  CE  MET A   0      -1.270 -15.166   9.860  1.00 23.66           C
ATOM      9  N   VAL A   1       2.830 -16.265  12.455  1.00 31.88           N
ATOM     10  CA  VAL A   1       3.979 -15.407  12.209  1.00 30.18           C
ATOM     11  C   VAL A   1       4.195 -15.335  10.705  1.00 26.27           C
ATOM     12  O   VAL A   1       3.824 -16.247   9.958  1.00 28.73           O
ATOM     13  CB  VAL A   1       5.266 -15.910  12.914  1.00 35.16           C
ATOM     14  CG1 VAL A   1       5.098 -15.919  14.430  1.00 36.12           C
ATOM     15  CG2 VAL A   1       5.647 -17.290  12.415  1.00 30.16           C
ATOM     16  N   LEU A   2       4.784 -14.233  10.256  1.00 16.11           N
ATOM     17  CA  LEU A   2       5.148 -14.076   8.854  1.00 16.00           C
ATOM     18  C   LEU A   2       6.656 -14.191   8.722  1.00 16.66           C
ATOM     19  O   LEU A   2       7.396 -13.738   9.600  1.00 14.11           O
ATOM     20  CB  LEU A   2       4.686 -12.733   8.287  1.00 14.60           C
ATOM     21  CG  LEU A   2       3.227 -12.640   7.843  1.00 14.78           C
ATOM     22  CD1 LEU A   2       2.312 -12.618   9.062  1.00 16.85           C
ATOM     23  CD2 LEU A   2       3.029 -11.395   6.998  1.00 13.74           C
ATOM     24  N   SER A   3       7.100 -14.807   7.629  1.00 10.94           N
ATOM     25  CA  SER A   3       8.517 -14.880   7.313  1.00 13.32           C
ATOM     26  C   SER A   3       9.003 -13.531   6.802  1.00 13.84           C
ATOM     27  O   SER A   3       8.218 -12.656   6.432  1.00 10.17           O
ATOM     28  CB  SER A   3       8.785 -15.943   6.256  1.00 13.73           C
ATOM     29  OG  SER A   3       8.216 -15.578   4.998  1.00 11.79           O
ATOM     30  N   GLU A   4      10.320 -13.379   6.748  1.00 12.72           N
ATOM     31  CA  GLU A   4      10.898 -12.162   6.184  1.00 13.18           C
ATOM     32  C   GLU A   4      10.462 -12.014   4.717  1.00 14.14           C
ATOM     33  O   GLU A   4      10.134 -10.922   4.258  1.00 11.92           O
ATOM     34  CB  GLU A   4      12.429 -12.189   6.310  1.00 16.52           C
ATOM     35  CG  GLU A   4      13.128 -10.929   5.843  1.00 22.10           C
ATOM     36  CD  GLU A   4      12.676  -9.679   6.589  1.00 17.34           C
ATOM     37  OE1 GLU A   4      12.437  -9.739   7.819  1.00 20.05           O
ATOM     38  OE2 GLU A   4      12.556  -8.625   5.936  1.00 28.18           O
HETATM   39  N   TYZ A   5      10.429 -13.132   4.001  1.00 10.98           N
HETATM   40  CA  TYZ A   5       9.942 -13.172   2.635  1.00 13.51           C
HETATM   41  C   TYZ A   5       8.540 -12.562   2.552  1.00 10.22           C
HETATM   42  O   TYZ A   5       8.280 -11.754   1.718  1.00 11.24           O
HETATM   43  CB  TYZ A   5       9.933 -14.620   2.157  1.00 12.56           C
HETATM   44  CG  TYZ A   5       9.132 -14.931   0.882  1.00 11.01           C
HETATM   45  CD1 TYZ A   5       9.455 -14.393  -0.364  1.00 14.89           C
HETATM   46  CD2 TYZ A   5       8.073 -15.819   1.002  1.00 14.01           C
HETATM   47  CE1 TYZ A   5       8.708 -14.749  -1.497  1.00 11.81           C
HETATM   48  CE2 TYZ A   5       7.339 -16.168  -0.108  1.00 13.69           C
HETATM   49  CZ  TYZ A   5       7.637 -15.634  -1.349  1.00 14.36           C
HETATM   50  OH  TYZ A   5       6.829 -16.050  -2.408  1.00 15.03           O
HETATM   51  C1  TYZ A   5       6.888 -15.355  -3.615  1.00 14.66           C
HETATM   52  C2  TYZ A   5       5.942 -16.100  -4.572  1.00 11.05           C
ATOM     53  N   GLU A   6       7.666 -12.968   3.470  1.00  9.61           N
ATOM     54  CA  GLU A   6       6.281 -12.497   3.457  1.00 11.09           C
ATOM     55  C   GLU A   6       6.205 -11.011   3.829  1.00  9.15           C
ATOM     56  O   GLU A   6       5.517 -10.229   3.157  1.00 10.22           O
ATOM     57  CB  GLU A   6       5.409 -13.352   4.397  1.00  9.16           C
ATOM     58  CG  GLU A   6       5.087 -14.737   3.802  1.00  9.45           C
ATOM     59  CD  GLU A   6       4.557 -15.727   4.827  1.00 16.19           C
ATOM     60  OE1 GLU A   6       3.840 -16.670   4.429  1.00 11.85           O
ATOM     61  OE2 GLU A   6       4.856 -15.575   6.025  1.00 17.72           O
ATOM     62  N   TRP A   7       6.933 -10.604   4.872  1.00  7.52           N
ATOM     63  CA  TRP A   7       6.919  -9.190   5.241  1.00 10.76           C
ATOM     64  C   TRP A   7       7.406  -8.320   4.091  1.00 10.65           C
ATOM     65  O   TRP A   7       6.865  -7.231   3.856  1.00 10.60           O
ATOM     66  CB  TRP A   7       7.762  -8.948   6.494  1.00 11.80           C
ATOM     67  CG  TRP A   7       7.051  -9.366   7.767  1.00 12.37           C
ATOM     68  CD1 TRP A   7       7.468 -10.293   8.676  1.00 14.35           C
ATOM     69  CD2 TRP A   7       5.799  -8.870   8.247  1.00 11.93           C
ATOM     70  NE1 TRP A   7       6.559 -10.401   9.699  1.00 12.70           N
ATOM     71  CE2 TRP A   7       5.519  -9.540   9.458  1.00 10.36           C
ATOM     72  CE3 TRP A   7       4.891  -7.919   7.776  1.00 11.85           C
ATOM     73  CZ2 TRP A   7       4.367  -9.296  10.197  1.00 12.95           C
ATOM     74  CZ3 TRP A   7       3.743  -7.676   8.512  1.00 10.50           C
ATOM     75  CH2 TRP A   7       3.495  -8.359   9.714  1.00 12.22           C
ATOM     76  N   GLN A   8       8.414  -8.793   3.350  1.00  7.60           N
ATOM     77  CA  GLN A   8       8.963  -7.994   2.257  1.00 10.51           C
ATOM     78  C   GLN A   8       7.947  -7.835   1.137  1.00 10.13           C
ATOM     79  O   GLN A   8       7.864  -6.771   0.521  1.00 10.42           O
ATOM     80  CB  GLN A   8      10.259  -8.621   1.731  1.00 14.35           C
ATOM     81  CG  GLN A   8      11.448  -8.487   2.679  1.00 18.13           C
ATOM     82  CD  GLN A   8      12.718  -9.156   2.139  1.00 22.55           C
ATOM     83  OE1 GLN A   8      13.596  -9.567   2.906  1.00 28.68           O
ATOM     84  NE2 GLN A   8      12.812  -9.267   0.820  1.00 18.02           N
ATOM     85  N   LEU A   9       7.157  -8.875   0.860  1.00  8.26           N
ATOM     86  CA  LEU A   9       6.093  -8.722  -0.131  1.00  9.87           C
ATOM     87  C   LEU A   9       5.068  -7.697   0.333  1.00  9.53           C
ATOM     88  O   LEU A   9       4.606  -6.870  -0.462  1.00  8.19           O
ATOM     89  CB  LEU A   9       5.415 -10.066  -0.404  1.00  8.72           C
ATOM     90  CG  LEU A   9       6.193 -11.176  -1.117  1.00 10.67           C
ATOM     91  CD1 LEU A   9       5.463 -12.512  -0.925  1.00 11.95           C
ATOM     92  CD2 LEU A   9       6.297 -10.832  -2.595  1.00 15.08           C
ATOM     93  N   VAL A  10       4.694  -7.745   1.616  1.00  9.75           N
ATOM     94  CA  VAL A  10       3.708  -6.815   2.164  1.00  9.90           C
ATOM     95  C   VAL A  10       4.219  -5.382   2.072  1.00  6.63           C
ATOM     96  O   VAL A  10       3.508  -4.471   1.626  1.00  8.54           O
ATOM     97  CB  VAL A  10       3.364  -7.193   3.621  1.00 10.00           C
ATOM     98  CG1 VAL A  10       2.461  -6.126   4.267  1.00  8.52           C
ATOM     99  CG2 VAL A  10       2.680  -8.557   3.692  1.00  9.99           C
ATOM    100  N   LEU A  11       5.458  -5.152   2.505  1.00  7.01           N
ATOM    101  CA  LEU A  11       5.968  -3.782   2.544  1.00  8.43           C
ATOM    102  C   LEU A  11       6.321  -3.273   1.152  1.00 10.54           C
ATOM    103  O   LEU A  11       6.279  -2.060   0.910  1.00  9.59           O
ATOM    104  CB  LEU A  11       7.167  -3.693   3.489  1.00  9.80           C
ATOM    105  CG  LEU A  11       6.773  -3.992   4.930  1.00  9.72           C
ATOM    106  CD1 LEU A  11       7.956  -3.925   5.874  1.00  8.16           C
ATOM    107  CD2 LEU A  11       5.666  -3.036   5.400  1.00 10.23           C
ATOM    108  N   HIS A  12       6.641  -4.171   0.220  1.00  8.18           N
ATOM    109  CA  HIS A  12       6.935  -3.728  -1.145  1.00 10.61           C
ATOM    110  C   HIS A  12       5.694  -3.139  -1.803  1.00 11.05           C
ATOM    111  O   HIS A  12       5.752  -2.051  -2.397  1.00 13.99           O
ATOM    112  CB  HIS A  12       7.488  -4.883  -1.980  1.00 12.29           C
ATOM    113  CG  HIS A  12       8.124  -4.457  -3.273  1.00 18.79           C
ATOM    114  ND1 HIS A  12       9.392  -3.916  -3.339  1.00 16.58           N
ATOM    115  CD2 HIS A  12       7.672  -4.511  -4.550  1.00 17.44           C
ATOM    116  CE1 HIS A  12       9.688  -3.645  -4.600  1.00 23.15           C
ATOM    117  NE2 HIS A  12       8.660  -3.993  -5.355  1.00 20.49           N
ATOM    118  N   VAL A  13       4.551  -3.823  -1.692  1.00 10.08           N
ATOM    119  CA  VAL A  13       3.342  -3.249  -2.276  1.00  8.77           C
ATOM    120  C   VAL A  13       2.890  -2.034  -1.478  1.00 11.79           C
ATOM    121  O   VAL A  13       2.337  -1.088  -2.053  1.00 11.13           O
ATOM    122  CB  VAL A  13       2.204  -4.279  -2.409  1.00  7.85           C
ATOM    123  CG1 VAL A  13       1.662  -4.677  -1.049  1.00  8.38           C
ATOM    124  CG2 VAL A  13       1.085  -3.704  -3.294  1.00 11.42           C
ATOM    125  N   TRP A  14       3.126  -2.018  -0.154  1.00 10.66           N
ATOM    126  CA  TRP A  14       2.696  -0.862   0.632  1.00 11.71           C
ATOM    127  C   TRP A  14       3.361   0.416   0.144  1.00 12.46           C
ATOM    128  O   TRP A  14       2.741   1.489   0.148  1.00 11.93           O
ATOM    129  CB  TRP A  14       2.973  -1.052   2.124  1.00 13.85           C
ATOM    130  CG  TRP A  14       2.241   0.016   2.888  1.00 11.74           C
ATOM    131  CD1 TRP A  14       2.762   1.165   3.405  1.00 14.86           C
ATOM    132  CD2 TRP A  14       0.827   0.073   3.124  1.00 11.90           C
ATOM    133  NE1 TRP A  14       1.760   1.921   3.982  1.00 13.58           N
ATOM    134  CE2 TRP A  14       0.567   1.268   3.827  1.00 12.82           C
ATOM    135  CE3 TRP A  14      -0.241  -0.784   2.829  1.00 14.81           C
ATOM    136  CZ2 TRP A  14      -0.718   1.629   4.237  1.00 14.65           C
ATOM    137  CZ3 TRP A  14      -1.516  -0.423   3.239  1.00 15.62           C
ATOM    138  CH2 TRP A  14      -1.740   0.771   3.938  1.00 14.60           C
ATOM    139  N   ALA A  15       4.627   0.325  -0.277  1.00 10.30           N
ATOM    140  CA  ALA A  15       5.312   1.493  -0.818  1.00 12.78           C
ATOM    141  C   ALA A  15       4.536   2.116  -1.977  1.00 11.54           C
ATOM    142  O   ALA A  15       4.559   3.340  -2.155  1.00 14.51           O
ATOM    143  CB  ALA A  15       6.728   1.099  -1.248  1.00 12.16           C
ATOM    144  N   LYS A  16       3.815   1.304  -2.755  1.00 11.91           N
ATOM    145  CA  LYS A  16       3.006   1.860  -3.841  1.00 12.55           C
ATOM    146  C   LYS A  16       1.837   2.688  -3.317  1.00 13.15           C
ATOM    147  O   LYS A  16       1.413   3.648  -3.977  1.00 12.11           O
ATOM    148  CB  LYS A  16       2.487   0.740  -4.750  1.00 14.62           C
ATOM    149  CG  LYS A  16       3.541  -0.268  -5.182  1.00 13.15           C
ATOM    150  CD  LYS A  16       4.737   0.387  -5.855  1.00 19.53           C
ATOM    151  CE  LYS A  16       4.308   1.260  -7.026  1.00 26.08           C
ATOM    152  NZ  LYS A  16       3.429   0.539  -7.987  1.00 33.14           N
ATOM    153  N   VAL A  17       1.283   2.321  -2.156  1.00 12.19           N
ATOM    154  CA  VAL A  17       0.219   3.114  -1.548  1.00 11.24           C
ATOM    155  C   VAL A  17       0.727   4.514  -1.217  1.00 11.67           C
ATOM    156  O   VAL A  17       0.003   5.510  -1.349  1.00 11.04           O
ATOM    157  CB  VAL A  17      -0.318   2.396  -0.292  1.00 11.97           C
ATOM    158  CG1 VAL A  17      -1.267   3.287   0.489  1.00 12.43           C
ATOM    159  CG2 VAL A  17      -0.996   1.094  -0.670  1.00 11.13           C
ATOM    160  N   GLU A  18       1.989   4.612  -0.804  1.00 11.46           N
ATOM    161  CA  GLU A  18       2.533   5.867  -0.307  1.00 11.91           C
ATOM    162  C   GLU A  18       2.716   6.907  -1.400  1.00 11.31           C
ATOM    163  O   GLU A  18       2.890   8.091  -1.073  1.00  8.93           O
ATOM    164  CB  GLU A  18       3.854   5.594   0.413  1.00 11.23           C
ATOM    165  CG  GLU A  18       3.662   4.690   1.648  1.00 11.84           C
ATOM    166  CD  GLU A  18       4.963   4.314   2.337  1.00 12.82           C
ATOM    167  OE1 GLU A  18       4.936   4.051   3.564  1.00 14.50           O
ATOM    168  OE2 GLU A  18       6.004   4.269   1.647  1.00 10.81           O
ATOM    169  N   ALA A  19       2.659   6.504  -2.675  1.00 10.93           N
ATOM    170  CA  ALA A  19       2.681   7.481  -3.761  1.00 11.06           C
ATOM    171  C   ALA A  19       1.540   8.472  -3.628  1.00 12.20           C
ATOM    172  O   ALA A  19       1.682   9.642  -4.009  1.00 11.10           O
ATOM    173  CB  ALA A  19       2.589   6.785  -5.124  1.00 14.85           C
ATOM    174  N   ASP A  20       0.403   8.015  -3.107  1.00  8.77           N
ATOM    175  CA  ASP A  20      -0.759   8.856  -2.861  1.00 11.41           C
ATOM    176  C   ASP A  20      -1.643   8.176  -1.822  1.00  8.72           C
ATOM    177  O   ASP A  20      -2.585   7.460  -2.176  1.00  8.45           O
ATOM    178  CB  ASP A  20      -1.534   9.100  -4.162  1.00 12.18           C
ATOM    179  CG  ASP A  20      -2.788   9.947  -3.954  1.00 10.68           C
ATOM    180  OD1 ASP A  20      -3.568  10.107  -4.915  1.00 13.64           O
ATOM    181  OD2 ASP A  20      -2.991  10.463  -2.840  1.00 10.60           O
ATOM    182  N   VAL A  21      -1.356   8.388  -0.537  1.00  7.93           N
ATOM    183  CA  VAL A  21      -2.145   7.717   0.500  1.00  7.47           C
ATOM    184  C   VAL A  21      -3.608   8.160   0.450  1.00  9.71           C
ATOM    185  O   VAL A  21      -4.525   7.340   0.593  1.00  8.67           O
ATOM    186  CB  VAL A  21      -1.525   7.966   1.887  1.00  9.15           C
ATOM    187  CG1 VAL A  21      -2.372   7.322   2.952  1.00  8.68           C
ATOM    188  CG2 VAL A  21      -0.102   7.400   1.948  1.00  8.53           C
ATOM    189  N   ALA A  22      -3.852   9.460   0.238  1.00  7.09           N
ATOM    190  CA  ALA A  22      -5.224   9.968   0.231  1.00  9.33           C
ATOM    191  C   ALA A  22      -6.062   9.317  -0.860  1.00  9.55           C
ATOM    192  O   ALA A  22      -7.222   8.953  -0.627  1.00  9.03           O
ATOM    193  CB  ALA A  22      -5.233  11.487   0.054  1.00  8.56           C
ATOM    194  N   GLY A  23      -5.508   9.184  -2.060  1.00  7.68           N
ATOM    195  CA  GLY A  23      -6.242   8.534  -3.132  1.00  7.71           C
ATOM    196  C   GLY A  23      -6.519   7.073  -2.832  1.00 10.80           C
ATOM    197  O   GLY A  23      -7.629   6.586  -3.055  1.00  9.55           O
ATOM    198  N   HIS A  24      -5.521   6.360  -2.298  1.00  9.38           N
ATOM    199  CA  HIS A  24      -5.750   4.962  -1.938  1.00  9.38           C
ATOM    200  C   HIS A  24      -6.778   4.838  -0.824  1.00  9.97           C
ATOM    201  O   HIS A  24      -7.617   3.935  -0.853  1.00  9.31           O
ATOM    202  CB  HIS A  24      -4.445   4.292  -1.515  1.00 11.86           C
ATOM    203  CG  HIS A  24      -3.549   3.952  -2.662  1.00 10.49           C
ATOM    204  ND1 HIS A  24      -2.763   4.891  -3.293  1.00 10.46           N
ATOM    205  CD2 HIS A  24      -3.319   2.777  -3.299  1.00 11.79           C
ATOM    206  CE1 HIS A  24      -2.082   4.310  -4.265  1.00 13.94           C
ATOM    207  NE2 HIS A  24      -2.404   3.030  -4.293  1.00 11.10           N
ATOM    208  N   GLY A  25      -6.715   5.721   0.180  1.00  8.40           N
ATOM    209  CA  GLY A  25      -7.654   5.633   1.290  1.00  8.62           C
ATOM    210  C   GLY A  25      -9.073   5.955   0.866  1.00 12.03           C
ATOM    211  O   GLY A  25     -10.036   5.361   1.365  1.00 11.47           O
ATOM    212  N   GLN A  26      -9.224   6.904  -0.057  1.00  9.13           N
ATOM    213  CA  GLN A  26     -10.544   7.175  -0.611  1.00 12.34           C
ATOM    214  C   GLN A  26     -11.120   5.927  -1.271  1.00 12.15           C
ATOM    215  O   GLN A  26     -12.279   5.567  -1.040  1.00  9.31           O
ATOM    216  CB  GLN A  26     -10.467   8.326  -1.611  1.00 12.52           C
ATOM    217  CG  GLN A  26     -11.800   8.637  -2.251  1.00 15.74           C
ATOM    218  CD  GLN A  26     -11.674   9.632  -3.368  1.00 19.08           C
ATOM    219  OE1 GLN A  26     -11.666   9.263  -4.541  1.00 22.46           O
ATOM    220  NE2 GLN A  26     -11.591  10.908  -3.016  1.00 17.28           N
ATOM    221  N   ASP A  27     -10.328   5.258  -2.116  1.00 11.27           N
ATOM    222  CA  ASP A  27     -10.818   4.044  -2.766  1.00 11.43           C
ATOM    223  C   ASP A  27     -11.184   2.982  -1.738  1.00 10.17           C
ATOM    224  O   ASP A  27     -12.163   2.251  -1.909  1.00  8.72           O
ATOM    225  CB  ASP A  27      -9.771   3.481  -3.728  1.00 13.26           C
ATOM    226  CG  ASP A  27      -9.576   4.337  -4.965  1.00 14.34           C
ATOM    227  OD1 ASP A  27     -10.233   5.385  -5.107  1.00 12.38           O
ATOM    228  OD2 ASP A  27      -8.723   3.958  -5.792  1.00 16.56           O
ATOM    229  N   ILE A  28     -10.388   2.865  -0.677  1.00  9.33           N
ATOM    230  CA  ILE A  28     -10.597   1.796   0.294  1.00  8.59           C
ATOM    231  C   ILE A  28     -11.858   2.066   1.105  1.00 10.93           C
ATOM    232  O   ILE A  28     -12.705   1.184   1.277  1.00 11.33           O
ATOM    233  CB  ILE A  28      -9.352   1.638   1.185  1.00 10.46           C
ATOM    234  CG1 ILE A  28      -8.214   0.996   0.362  1.00  5.90           C
ATOM    235  CG2 ILE A  28      -9.671   0.829   2.458  1.00 10.44           C
ATOM    236  CD1 ILE A  28      -6.860   0.966   1.049  1.00  9.73           C
ATOM    237  N   LEU A  29     -12.010   3.296   1.601  1.00  9.42           N
ATOM    238  CA  LEU A  29     -13.213   3.644   2.354  1.00  9.56           C
ATOM    239  C   LEU A  29     -14.472   3.527   1.499  1.00 10.61           C
ATOM    240  O   LEU A  29     -15.519   3.069   1.980  1.00  8.54           O
ATOM    241  CB  LEU A  29     -13.082   5.060   2.911  1.00  9.87           C
ATOM    242  CG  LEU A  29     -12.048   5.250   4.008  1.00 10.45           C
ATOM    243  CD1 LEU A  29     -12.011   6.709   4.436  1.00 14.23           C
ATOM    244  CD2 LEU A  29     -12.368   4.341   5.188  1.00 15.27           C
ATOM    245  N   ILE A  30     -14.407   3.964   0.240  1.00  8.46           N
ATOM    246  CA  ILE A  30     -15.591   3.880  -0.610  1.00  6.82           C
ATOM    247  C   ILE A  30     -15.939   2.421  -0.877  1.00  9.48           C
ATOM    248  O   ILE A  30     -17.112   2.031  -0.852  1.00 11.82           O
ATOM    249  CB  ILE A  30     -15.378   4.671  -1.915  1.00 10.35           C
ATOM    250  CG1 ILE A  30     -15.333   6.170  -1.602  1.00 11.68           C
ATOM    251  CG2 ILE A  30     -16.470   4.343  -2.933  1.00 15.62           C
ATOM    252  CD1 ILE A  30     -14.972   7.038  -2.783  1.00 15.61           C
ATOM    253  N   ARG A  31     -14.924   1.597  -1.127  1.00  8.62           N
ATOM    254  CA  ARG A  31     -15.131   0.158  -1.271  1.00 10.98           C
ATOM    255  C   ARG A  31     -15.786  -0.425  -0.025  1.00 13.19           C
ATOM    256  O   ARG A  31     -16.757  -1.188  -0.121  1.00 12.29           O
ATOM    257  CB  ARG A  31     -13.790  -0.529  -1.562  1.00 12.06           C
ATOM    258  CG  ARG A  31     -13.843  -2.065  -1.564  1.00 15.90           C
ATOM    259  CD  ARG A  31     -14.560  -2.615  -2.781  1.00 20.65           C
ATOM    260  NE  ARG A  31     -14.642  -4.076  -2.750  1.00 19.25           N
ATOM    261  CZ  ARG A  31     -15.150  -4.801  -3.735  1.00 23.15           C
ATOM    262  NH1 ARG A  31     -15.608  -4.198  -4.824  1.00 24.20           N
ATOM    263  NH2 ARG A  31     -15.198  -6.125  -3.637  1.00 24.10           N
ATOM    264  N   LEU A  32     -15.268  -0.070   1.158  1.00  9.12           N
ATOM    265  CA  LEU A  32     -15.845  -0.539   2.417  1.00  9.91           C
ATOM    266  C   LEU A  32     -17.321  -0.159   2.535  1.00 11.28           C
ATOM    267  O   LEU A  32     -18.175  -1.013   2.814  1.00 11.65           O
ATOM    268  CB  LEU A  32     -15.054   0.045   3.591  1.00  8.43           C
ATOM    269  CG  LEU A  32     -15.586  -0.265   4.991  1.00  9.79           C
ATOM    270  CD1 LEU A  32     -15.493  -1.756   5.297  1.00  9.67           C
ATOM    271  CD2 LEU A  32     -14.829   0.547   6.049  1.00 10.78           C
ATOM    272  N   PHE A  33     -17.634   1.124   2.324  1.00  8.94           N
ATOM    273  CA  PHE A  33     -18.985   1.628   2.565  1.00  9.50           C
ATOM    274  C   PHE A  33     -19.971   1.075   1.549  1.00 11.82           C
ATOM    275  O   PHE A  33     -21.129   0.807   1.881  1.00 13.82           O
ATOM    276  CB  PHE A  33     -18.994   3.156   2.518  1.00  9.40           C
ATOM    277  CG  PHE A  33     -18.171   3.806   3.598  1.00  9.74           C
ATOM    278  CD1 PHE A  33     -17.984   3.184   4.823  1.00 10.18           C
ATOM    279  CD2 PHE A  33     -17.575   5.040   3.380  1.00  9.62           C
ATOM    280  CE1 PHE A  33     -17.221   3.775   5.816  1.00 11.38           C
ATOM    281  CE2 PHE A  33     -16.814   5.645   4.371  1.00  9.23           C
ATOM    282  CZ  PHE A  33     -16.628   5.013   5.587  1.00 10.16           C
ATOM    283  N   LYS A  34     -19.534   0.899   0.306  1.00  8.71           N
ATOM    284  CA  LYS A  34     -20.434   0.365  -0.710  1.00 12.44           C
ATOM    285  C   LYS A  34     -20.602  -1.141  -0.558  1.00 14.35           C
ATOM    286  O   LYS A  34     -21.699  -1.673  -0.778  1.00 16.00           O
ATOM    287  CB  LYS A  34     -19.921   0.717  -2.107  1.00 16.69           C
ATOM    288  CG  LYS A  34     -20.016   2.188  -2.445  1.00 19.71           C
ATOM    289  CD  LYS A  34     -19.935   2.417  -3.947  1.00 28.11           C
ATOM    290  CE  LYS A  34     -18.933   1.467  -4.613  1.00 29.86           C
ATOM    291  NZ  LYS A  34     -18.640   1.837  -6.034  1.00 33.10           N
ATOM    292  N   SER A  35     -19.533  -1.846  -0.171  1.00 11.13           N
ATOM    293  CA  SER A  35     -19.646  -3.285   0.046  1.00 13.95           C
ATOM    294  C   SER A  35     -20.404  -3.602   1.323  1.00 13.74           C
ATOM    295  O   SER A  35     -21.068  -4.641   1.403  1.00 14.76           O
ATOM    296  CB  SER A  35     -18.260  -3.930   0.101  1.00 14.02           C
ATOM    297  OG  SER A  35     -17.678  -3.987  -1.186  1.00 19.04           O
ATOM    298  N   HIS A  36     -20.310  -2.732   2.331  1.00 12.61           N
ATOM    299  CA  HIS A  36     -20.890  -2.983   3.652  1.00 12.22           C
ATOM    300  C   HIS A  36     -21.473  -1.685   4.185  1.00 11.47           C
ATOM    301  O   HIS A  36     -20.862  -0.994   5.009  1.00  9.28           O
ATOM    302  CB  HIS A  36     -19.843  -3.567   4.601  1.00 11.54           C
ATOM    303  CG  HIS A  36     -19.132  -4.754   4.032  1.00 14.08           C
ATOM    304  ND1 HIS A  36     -19.621  -6.038   4.135  1.00 19.17           N
ATOM    305  CD2 HIS A  36     -17.988  -4.844   3.313  1.00 15.27           C
ATOM    306  CE1 HIS A  36     -18.798  -6.871   3.523  1.00 19.70           C
ATOM    307  NE2 HIS A  36     -17.800  -6.171   3.013  1.00 17.95           N
ATOM    308  N   PRO A  37     -22.669  -1.311   3.728  1.00  9.47           N
ATOM    309  CA  PRO A  37     -23.228  -0.004   4.110  1.00 10.91           C
ATOM    310  C   PRO A  37     -23.344   0.204   5.607  1.00  9.32           C
ATOM    311  O   PRO A  37     -23.346   1.350   6.072  1.00 14.06           O
ATOM    312  CB  PRO A  37     -24.606  -0.015   3.439  1.00 10.06           C
ATOM    313  CG  PRO A  37     -24.408  -0.895   2.241  1.00 13.99           C
ATOM    314  CD  PRO A  37     -23.499  -1.994   2.718  1.00 14.50           C
ATOM    315  N   GLU A  38     -23.457  -0.870   6.383  1.00  9.55           N
ATOM    316  CA  GLU A  38     -23.575  -0.712   7.830  1.00 10.34           C
ATOM    317  C   GLU A  38     -22.324  -0.088   8.434  1.00 14.00           C
ATOM    318  O   GLU A  38     -22.405   0.572   9.481  1.00 12.58           O
ATOM    319  CB  GLU A  38     -23.873  -2.062   8.489  1.00 12.06           C
ATOM    320  CG  GLU A  38     -22.728  -3.082   8.462  1.00 10.12           C
ATOM    321  CD  GLU A  38     -22.681  -3.917   7.184  1.00 12.90           C
ATOM    322  OE1 GLU A  38     -22.188  -5.061   7.240  1.00 13.95           O
ATOM    323  OE2 GLU A  38     -23.117  -3.427   6.125  1.00  8.90           O
ATOM    324  N   THR A  39     -21.166  -0.265   7.788  1.00  8.01           N
ATOM    325  CA  THR A  39     -19.937   0.311   8.328  1.00 10.47           C
ATOM    326  C   THR A  39     -19.979   1.831   8.319  1.00 11.39           C
ATOM    327  O   THR A  39     -19.396   2.470   9.207  1.00 11.62           O
ATOM    328  CB  THR A  39     -18.711  -0.180   7.553  1.00 12.66           C
ATOM    329  OG1 THR A  39     -18.800   0.220   6.177  1.00 13.14           O
ATOM    330  CG2 THR A  39     -18.587  -1.709   7.653  1.00 11.55           C
ATOM    331  N   LEU A  40     -20.665   2.434   7.337  1.00  7.30           N
ATOM    332  CA  LEU A  40     -20.728   3.897   7.291  1.00 10.38           C
ATOM    333  C   LEU A  40     -21.438   4.459   8.517  1.00 10.66           C
ATOM    334  O   LEU A  40     -21.141   5.582   8.955  1.00 12.91           O
ATOM    335  CB  LEU A  40     -21.425   4.356   6.004  1.00  7.80           C
ATOM    336  CG  LEU A  40     -21.522   5.874   5.752  1.00  9.58           C
ATOM    337  CD1 LEU A  40     -20.137   6.483   5.680  1.00 11.17           C
ATOM    338  CD2 LEU A  40     -22.279   6.161   4.468  1.00 10.17           C
ATOM    339  N   GLU A  41     -22.363   3.685   9.096  1.00 11.12           N
ATOM    340  CA  GLU A  41     -23.109   4.132  10.272  1.00 14.05           C
ATOM    341  C   GLU A  41     -22.208   4.415  11.464  1.00 15.25           C
ATOM    342  O   GLU A  41     -22.620   5.134  12.383  1.00 10.53           O
ATOM    343  CB  GLU A  41     -24.146   3.077  10.664  1.00 13.19           C
ATOM    344  CG  GLU A  41     -25.270   2.916   9.668  1.00 13.86           C
ATOM    345  CD  GLU A  41     -26.319   4.007   9.805  1.00 19.76           C
ATOM    346  OE1 GLU A  41     -27.330   3.793  10.517  1.00 19.70           O
ATOM    347  OE2 GLU A  41     -26.125   5.084   9.208  1.00 19.22           O
ATOM    348  N   LYS A  42     -20.990   3.876  11.476  1.00 12.39           N
ATOM    349  CA  LYS A  42     -20.088   4.079  12.603  1.00 14.12           C
ATOM    350  C   LYS A  42     -19.393   5.433  12.567  1.00 15.75           C
ATOM    351  O   LYS A  42     -18.817   5.851  13.579  1.00 15.10           O
ATOM    352  CB  LYS A  42     -19.042   2.965  12.630  1.00 13.54           C
ATOM    353  CG  LYS A  42     -19.609   1.572  12.973  1.00 12.27           C
ATOM    354  CD  LYS A  42     -20.028   1.491  14.435  1.00 17.34           C
ATOM    355  CE  LYS A  42     -20.693   0.154  14.763  1.00 20.22           C
ATOM    356  NZ  LYS A  42     -21.048   0.080  16.220  1.00 21.41           N
ATOM    357  N   PHE A  43     -19.417   6.115  11.428  1.00 13.84           N
ATOM    358  CA  PHE A  43     -18.740   7.394  11.251  1.00 15.61           C
ATOM    359  C   PHE A  43     -19.783   8.488  11.461  1.00 17.19           C
ATOM    360  O   PHE A  43     -20.470   8.906  10.529  1.00 15.23           O
ATOM    361  CB  PHE A  43     -18.102   7.457   9.867  1.00 13.65           C
ATOM    362  CG  PHE A  43     -16.935   6.527   9.697  1.00 11.09           C
ATOM    363  CD1 PHE A  43     -15.638   6.983   9.896  1.00 13.02           C
ATOM    364  CD2 PHE A  43     -17.128   5.196   9.344  1.00 11.99           C
ATOM    365  CE1 PHE A  43     -14.544   6.133   9.754  1.00 14.70           C
ATOM    366  CE2 PHE A  43     -16.043   4.339   9.199  1.00 15.56           C
ATOM    367  CZ  PHE A  43     -14.746   4.810   9.405  1.00 14.07           C
ATOM    368  N   ASP A  44     -19.898   8.956  12.704  1.00 17.36           N
ATOM    369  CA  ASP A  44     -20.911   9.959  13.017  1.00 17.39           C
ATOM    370  C   ASP A  44     -20.748  11.211  12.164  1.00 16.83           C
ATOM    371  O   ASP A  44     -21.744  11.819  11.764  1.00 19.77           O
ATOM    372  CB  ASP A  44     -20.859  10.312  14.505  1.00 23.43           C
ATOM    373  N   ARG A  45     -19.510  11.593  11.846  1.00 15.61           N
ATOM    374  CA  ARG A  45     -19.300  12.772  11.013  1.00 15.89           C
ATOM    375  C   ARG A  45     -19.708  12.558   9.560  1.00 18.71           C
ATOM    376  O   ARG A  45     -19.966  13.542   8.857  1.00 14.73           O
ATOM    377  CB  ARG A  45     -17.833  13.197  11.049  1.00 20.59           C
ATOM    378  CG  ARG A  45     -17.354  13.758  12.367  1.00 27.32           C
ATOM    379  CD  ARG A  45     -16.138  14.645  12.131  1.00 30.67           C
ATOM    380  NE  ARG A  45     -14.935  13.879  11.824  1.00 29.00           N
ATOM    381  CZ  ARG A  45     -13.885  14.379  11.183  1.00 30.09           C
ATOM    382  NH1 ARG A  45     -13.903  15.640  10.763  1.00 29.44           N
ATOM    383  NH2 ARG A  45     -12.821  13.619  10.954  1.00 26.50           N
ATOM    384  N   PHE A  46     -19.765  11.311   9.084  1.00 13.70           N
ATOM    385  CA  PHE A  46     -19.874  11.062   7.655  1.00 12.62           C
ATOM    386  C   PHE A  46     -21.032  10.166   7.248  1.00 13.91           C
ATOM    387  O   PHE A  46     -21.164   9.871   6.055  1.00 12.45           O
ATOM    388  CB  PHE A  46     -18.568  10.452   7.127  1.00 14.47           C
ATOM    389  CG  PHE A  46     -17.352  11.254   7.478  1.00 15.36           C
ATOM    390  CD1 PHE A  46     -16.472  10.810   8.453  1.00 17.14           C
ATOM    391  CD2 PHE A  46     -17.109  12.472   6.865  1.00 12.98           C
ATOM    392  CE1 PHE A  46     -15.363  11.556   8.792  1.00 17.79           C
ATOM    393  CE2 PHE A  46     -15.994  13.224   7.198  1.00 17.31           C
ATOM    394  CZ  PHE A  46     -15.123  12.765   8.163  1.00 18.62           C
ATOM    395  N   LYS A  47     -21.885   9.738   8.183  1.00 11.99           N
ATOM    396  CA  LYS A  47     -22.896   8.740   7.847  1.00 11.97           C
ATOM    397  C   LYS A  47     -23.975   9.264   6.907  1.00 12.25           C
ATOM    398  O   LYS A  47     -24.748   8.461   6.375  1.00 11.12           O
ATOM    399  CB  LYS A  47     -23.533   8.185   9.125  1.00 15.23           C
ATOM    400  CG  LYS A  47     -24.187   9.214  10.019  1.00 17.30           C
ATOM    401  CD  LYS A  47     -24.537   8.588  11.376  1.00 24.29           C
ATOM    402  CE  LYS A  47     -24.956   9.650  12.387  1.00 26.25           C
ATOM    403  NZ  LYS A  47     -24.665   9.235  13.797  1.00 40.96           N
ATOM    404  N   HIS A  48     -24.036  10.572   6.676  1.00 11.42           N
ATOM    405  CA  HIS A  48     -24.938  11.134   5.680  1.00 15.50           C
ATOM    406  C   HIS A  48     -24.409  11.001   4.256  1.00 13.47           C
ATOM    407  O   HIS A  48     -25.164  11.241   3.305  1.00 11.12           O
ATOM    408  CB  HIS A  48     -25.197  12.619   5.992  1.00 14.39           C
ATOM    409  CG  HIS A  48     -23.971  13.484   5.900  1.00 15.86           C
ATOM    410  ND1 HIS A  48     -22.904  13.370   6.772  1.00 16.34           N
ATOM    411  CD2 HIS A  48     -23.644  14.476   5.032  1.00 13.97           C
ATOM    412  CE1 HIS A  48     -21.982  14.266   6.452  1.00 17.90           C
ATOM    413  NE2 HIS A  48     -22.405  14.948   5.399  1.00 14.02           N
ATOM    414  N   LEU A  49     -23.136  10.635   4.084  1.00  9.70           N
ATOM    415  CA  LEU A  49     -22.500  10.601   2.765  1.00 11.18           C
ATOM    416  C   LEU A  49     -22.709   9.220   2.141  1.00 12.43           C
ATOM    417  O   LEU A  49     -21.792   8.409   2.028  1.00 13.06           O
ATOM    418  CB  LEU A  49     -21.018  10.936   2.886  1.00 10.05           C
ATOM    419  CG  LEU A  49     -20.662  12.292   3.481  1.00 11.14           C
ATOM    420  CD1 LEU A  49     -19.141  12.410   3.593  1.00  7.92           C
ATOM    421  CD2 LEU A  49     -21.231  13.388   2.587  1.00 11.00           C
ATOM    422  N   LYS A  50     -23.954   8.962   1.728  1.00  9.17           N
ATOM    423  CA  LYS A  50     -24.388   7.601   1.435  1.00 13.65           C
ATOM    424  C   LYS A  50     -24.157   7.162  -0.011  1.00 16.87           C
ATOM    425  O   LYS A  50     -24.600   6.069  -0.380  1.00 15.11           O
ATOM    426  CB  LYS A  50     -25.866   7.428   1.808  1.00 10.92           C
ATOM    427  CG  LYS A  50     -26.099   7.475   3.328  1.00 13.44           C
ATOM    428  CD  LYS A  50     -27.559   7.234   3.683  1.00 13.27           C
ATOM    429  CE  LYS A  50     -27.734   6.954   5.162  1.00 19.17           C
ATOM    430  NZ  LYS A  50     -27.494   8.164   5.995  1.00 15.85           N
ATOM    431  N   THR A  51     -23.474   7.960  -0.834  1.00 10.15           N
ATOM    432  CA  THR A  51     -23.094   7.520  -2.169  1.00 11.48           C
ATOM    433  C   THR A  51     -21.625   7.828  -2.427  1.00 12.25           C
ATOM    434  O   THR A  51     -21.034   8.720  -1.810  1.00 11.83           O
ATOM    435  CB  THR A  51     -23.926   8.189  -3.264  1.00 12.99           C
ATOM    436  OG1 THR A  51     -23.709   9.602  -3.209  1.00 14.40           O
ATOM    437  CG2 THR A  51     -25.423   7.876  -3.095  1.00 15.70           C
ATOM    438  N   GLU A  52     -21.054   7.103  -3.391  1.00 11.48           N
ATOM    439  CA  GLU A  52     -19.654   7.322  -3.752  1.00 10.58           C
ATOM    440  C   GLU A  52     -19.400   8.773  -4.161  1.00 12.84           C
ATOM    441  O   GLU A  52     -18.383   9.364  -3.776  1.00 13.10           O
ATOM    442  CB  GLU A  52     -19.243   6.366  -4.875  1.00 17.98           C
ATOM    443  CG  GLU A  52     -17.852   6.640  -5.416  1.00 17.02           C
ATOM    444  CD  GLU A  52     -17.421   5.646  -6.467  1.00 25.15           C
ATOM    445  OE1 GLU A  52     -16.329   5.827  -7.046  1.00 30.91           O
ATOM    446  OE2 GLU A  52     -18.172   4.684  -6.715  1.00 20.86           O
ATOM    447  N   ALA A  53     -20.312   9.364  -4.939  1.00 13.18           N
ATOM    448  CA  ALA A  53     -20.137  10.754  -5.366  1.00 13.36           C
ATOM    449  C   ALA A  53     -20.048  11.697  -4.174  1.00 12.75           C
ATOM    450  O   ALA A  53     -19.228  12.625  -4.166  1.00 12.48           O
ATOM    451  CB  ALA A  53     -21.283  11.172  -6.287  1.00 17.03           C
ATOM    452  N   GLU A  54     -20.883  11.477  -3.153  1.00 10.01           N
ATOM    453  CA  GLU A  54     -20.815  12.314  -1.959  1.00 10.23           C
ATOM    454  C   GLU A  54     -19.554  12.030  -1.150  1.00  8.98           C
ATOM    455  O   GLU A  54     -18.943  12.953  -0.599  1.00  8.91           O
ATOM    456  CB  GLU A  54     -22.057  12.104  -1.099  1.00 10.70           C
ATOM    457  CG  GLU A  54     -23.366  12.502  -1.757  1.00 10.47           C
ATOM    458  CD  GLU A  54     -24.545  12.066  -0.924  1.00 13.18           C
ATOM    459  OE1 GLU A  54     -25.205  11.075  -1.299  1.00 12.94           O
ATOM    460  OE2 GLU A  54     -24.787  12.686   0.130  1.00 15.33           O
ATOM    461  N   MET A  55     -19.159  10.758  -1.047  1.00  9.65           N
ATOM    462  CA  MET A  55     -17.954  10.420  -0.293  1.00  9.62           C
ATOM    463  C   MET A  55     -16.730  11.103  -0.889  1.00 10.63           C
ATOM    464  O   MET A  55     -15.899  11.669  -0.160  1.00 10.88           O
ATOM    465  CB  MET A  55     -17.757   8.903  -0.276  1.00 10.34           C
ATOM    466  CG  MET A  55     -18.821   8.129   0.501  1.00  9.50           C
ATOM    467  SD  MET A  55     -18.837   6.396  -0.014  1.00 13.01           S
ATOM    468  CE  MET A  55     -20.385   5.887   0.745  1.00 11.56           C
ATOM    469  N   LYS A  56     -16.600  11.047  -2.223  1.00 10.28           N
ATOM    470  CA  LYS A  56     -15.441  11.616  -2.911  1.00 14.00           C
ATOM    471  C   LYS A  56     -15.322  13.117  -2.697  1.00 12.99           C
ATOM    472  O   LYS A  56     -14.232  13.675  -2.849  1.00 12.49           O
ATOM    473  CB  LYS A  56     -15.526  11.372  -4.427  1.00 15.14           C
ATOM    474  CG  LYS A  56     -15.348   9.955  -4.912  1.00 22.08           C
ATOM    475  CD  LYS A  56     -15.144   9.992  -6.428  1.00 26.38           C
ATOM    476  CE  LYS A  56     -15.907   8.901  -7.143  1.00 30.63           C
ATOM    477  NZ  LYS A  56     -15.791   8.973  -8.632  1.00 33.23           N
ATOM    478  N   ALA A  57     -16.419  13.789  -2.377  1.00 10.15           N
ATOM    479  CA  ALA A  57     -16.438  15.238  -2.328  1.00 10.15           C
ATOM    480  C   ALA A  57     -16.238  15.777  -0.918  1.00 11.65           C
ATOM    481  O   ALA A  57     -16.448  16.973  -0.687  1.00 12.17           O
ATOM    482  CB  ALA A  57     -17.750  15.762  -2.931  1.00 10.95           C
ATOM    483  N   SER A  58     -15.840  14.929   0.028  1.00 10.92           N
ATOM    484  CA  SER A  58     -15.545  15.339   1.397  1.00 10.00           C
ATOM    485  C   SER A  58     -14.045  15.228   1.631  1.00 10.49           C
ATOM    486  O   SER A  58     -13.509  14.116   1.739  1.00 11.38           O
ATOM    487  CB  SER A  58     -16.300  14.478   2.403  1.00 10.87           C
ATOM    488  OG  SER A  58     -15.901  14.771   3.734  1.00  9.32           O
ATOM    489  N   GLU A  59     -13.365  16.374   1.723  1.00 11.26           N
ATOM    490  CA  GLU A  59     -11.955  16.307   2.096  1.00 10.21           C
ATOM    491  C   GLU A  59     -11.798  15.792   3.518  1.00 11.14           C
ATOM    492  O   GLU A  59     -10.785  15.155   3.829  1.00 10.83           O
ATOM    493  CB  GLU A  59     -11.265  17.670   1.958  1.00 11.60           C
ATOM    494  CG  GLU A  59     -11.351  18.300   0.577  1.00 10.65           C
ATOM    495  CD  GLU A  59     -10.909  17.375  -0.543  1.00 15.76           C
ATOM    496  OE1 GLU A  59      -9.856  16.708  -0.410  1.00 13.44           O
ATOM    497  OE2 GLU A  59     -11.624  17.310  -1.565  1.00 13.34           O
ATOM    498  N   ASP A  60     -12.781  16.046   4.394  1.00  8.63           N
ATOM    499  CA  ASP A  60     -12.669  15.551   5.762  1.00 10.73           C
ATOM    500  C   ASP A  60     -12.675  14.030   5.786  1.00 12.28           C
ATOM    501  O   ASP A  60     -11.921  13.414   6.548  1.00  9.70           O
ATOM    502  CB  ASP A  60     -13.787  16.105   6.645  1.00 14.23           C
ATOM    503  CG  ASP A  60     -13.476  17.494   7.170  1.00 16.53           C
ATOM    504  OD1 ASP A  60     -14.330  18.067   7.871  1.00 14.28           O
ATOM    505  OD2 ASP A  60     -12.383  18.021   6.869  1.00 16.80           O
ATOM    506  N   LEU A  61     -13.506  13.408   4.944  1.00 10.39           N
ATOM    507  CA  LEU A  61     -13.506  11.949   4.871  1.00 12.89           C
ATOM    508  C   LEU A  61     -12.191  11.427   4.309  1.00 13.71           C
ATOM    509  O   LEU A  61     -11.653  10.423   4.795  1.00 11.72           O
ATOM    510  CB  LEU A  61     -14.678  11.462   4.022  1.00 13.94           C
ATOM    511  CG  LEU A  61     -14.770   9.938   3.892  1.00 14.40           C
ATOM    512  CD1 LEU A  61     -14.835   9.248   5.268  1.00 16.60           C
ATOM    513  CD2 LEU A  61     -15.973   9.555   3.056  1.00 13.44           C
ATOM    514  N   LYS A  62     -11.648  12.101   3.297  1.00 10.10           N
ATOM    515  CA  LYS A  62     -10.350  11.697   2.760  1.00 10.61           C
ATOM    516  C   LYS A  62      -9.235  11.836   3.799  1.00 11.65           C
ATOM    517  O   LYS A  62      -8.297  11.031   3.813  1.00 10.13           O
ATOM    518  CB  LYS A  62     -10.050  12.510   1.495  1.00 14.83           C
ATOM    519  CG  LYS A  62     -11.020  12.195   0.326  1.00 14.20           C
ATOM    520  CD  LYS A  62     -11.248  13.395  -0.609  1.00 16.48           C
ATOM    521  CE  LYS A  62     -10.081  13.606  -1.564  1.00 19.87           C
ATOM    522  NZ  LYS A  62     -10.316  14.729  -2.528  1.00 17.24           N
ATOM    523  N   LYS A  63      -9.325  12.831   4.690  1.00  8.99           N
ATOM    524  CA  LYS A  63      -8.342  12.939   5.770  1.00 10.38           C
ATOM    525  C   LYS A  63      -8.460  11.780   6.759  1.00 12.48           C
ATOM    526  O   LYS A  63      -7.443  11.302   7.286  1.00 12.58           O
ATOM    527  CB  LYS A  63      -8.490  14.284   6.480  1.00 12.23           C
ATOM    528  CG  LYS A  63      -7.988  15.458   5.630  1.00 11.49           C
ATOM    529  CD  LYS A  63      -7.698  16.696   6.479  1.00 18.78           C
ATOM    530  CE  LYS A  63      -8.953  17.263   7.098  1.00 21.72           C
ATOM    531  NZ  LYS A  63      -8.657  18.580   7.737  1.00 22.32           N
ATOM    532  N   VAL A  64      -9.686  11.319   7.032  1.00 12.25           N
ATOM    533  CA  VAL A  64      -9.866  10.117   7.846  1.00 11.25           C
ATOM    534  C   VAL A  64      -9.172   8.924   7.198  1.00 11.78           C
ATOM    535  O   VAL A  64      -8.506   8.129   7.876  1.00 11.56           O
ATOM    536  CB  VAL A  64     -11.367   9.843   8.071  1.00 10.45           C
ATOM    537  CG1 VAL A  64     -11.600   8.411   8.586  1.00 17.19           C
ATOM    538  CG2 VAL A  64     -11.946  10.842   9.058  1.00 17.26           C
ATOM    539  N   GLY A  65      -9.330   8.772   5.876  1.00 11.88           N
ATOM    540  CA  GLY A  65      -8.646   7.696   5.171  1.00  9.64           C
ATOM    541  C   GLY A  65      -7.135   7.782   5.295  1.00 10.02           C
ATOM    542  O   GLY A  65      -6.453   6.761   5.464  1.00 10.05           O
ATOM    543  N   VAL A  66      -6.591   8.998   5.212  1.00  8.06           N
ATOM    544  CA  VAL A  66      -5.145   9.178   5.350  1.00  9.37           C
ATOM    545  C   VAL A  66      -4.698   8.740   6.732  1.00 10.35           C
ATOM    546  O   VAL A  66      -3.682   8.049   6.890  1.00  9.94           O
ATOM    547  CB  VAL A  66      -4.743  10.638   5.084  1.00  9.89           C
ATOM    548  CG1 VAL A  66      -3.281  10.856   5.441  1.00 13.89           C
ATOM    549  CG2 VAL A  66      -4.993  11.002   3.629  1.00  7.88           C
ATOM    550  N   THR A  67      -5.436   9.173   7.756  1.00 10.20           N
ATOM    551  CA  THR A  67      -5.097   8.833   9.132  1.00 10.07           C
ATOM    552  C   THR A  67      -5.087   7.325   9.338  1.00  8.86           C
ATOM    553  O   THR A  67      -4.177   6.777   9.972  1.00 10.46           O
ATOM    554  CB  THR A  67      -6.085   9.515  10.082  1.00 13.52           C
ATOM    555  OG1 THR A  67      -5.889  10.936  10.009  1.00 15.32           O
ATOM    556  CG2 THR A  67      -5.883   9.038  11.519  1.00 16.81           C
ATOM    557  N   ALA A  68      -6.111   6.635   8.829  1.00  7.66           N
ATOM    558  CA  ALA A  68      -6.179   5.185   8.994  1.00  9.09           C
ATOM    559  C   ALA A  68      -5.019   4.489   8.289  1.00  8.24           C
ATOM    560  O   ALA A  68      -4.357   3.622   8.866  1.00 11.00           O
ATOM    561  CB  ALA A  68      -7.514   4.663   8.469  1.00  7.51           C
ATOM    562  N   LEU A  69      -4.762   4.848   7.028  1.00 10.23           N
ATOM    563  CA  LEU A  69      -3.722   4.156   6.270  1.00 10.88           C
ATOM    564  C   LEU A  69      -2.317   4.486   6.772  1.00 12.54           C
ATOM    565  O   LEU A  69      -1.437   3.619   6.754  1.00 10.21           O
ATOM    566  CB  LEU A  69      -3.836   4.483   4.780  1.00 10.98           C
ATOM    567  CG  LEU A  69      -5.051   3.962   3.999  1.00 12.42           C
ATOM    568  CD1 LEU A  69      -4.788   4.105   2.503  1.00 11.53           C
ATOM    569  CD2 LEU A  69      -5.386   2.525   4.352  1.00 13.47           C
ATOM    570  N   THR A  70      -2.075   5.724   7.210  1.00 10.16           N
ATOM    571  CA  THR A  70      -0.777   6.047   7.798  1.00 10.14           C
ATOM    572  C   THR A  70      -0.504   5.189   9.029  1.00 10.39           C
ATOM    573  O   THR A  70       0.592   4.627   9.183  1.00  9.86           O
ATOM    574  CB  THR A  70      -0.728   7.534   8.148  1.00 14.42           C
ATOM    575  OG1 THR A  70      -0.938   8.302   6.953  1.00 14.00           O
ATOM    576  CG2 THR A  70       0.624   7.904   8.725  1.00 17.47           C
ATOM    577  N   ALA A  71      -1.497   5.069   9.915  1.00 11.48           N
ATOM    578  CA  ALA A  71      -1.370   4.199  11.086  1.00  9.18           C
ATOM    579  C   ALA A  71      -1.147   2.743  10.682  1.00  7.98           C
ATOM    580  O   ALA A  71      -0.293   2.054  11.260  1.00  7.96           O
ATOM    581  CB  ALA A  71      -2.618   4.321  11.962  1.00 13.16           C
ATOM    582  N   LEU A  72      -1.894   2.262   9.685  1.00  8.32           N
ATOM    583  CA  LEU A  72      -1.718   0.888   9.224  1.00  8.93           C
ATOM    584  C   LEU A  72      -0.325   0.681   8.647  1.00  9.67           C
ATOM    585  O   LEU A  72       0.323  -0.343   8.917  1.00  9.56           O
ATOM    586  CB  LEU A  72      -2.785   0.532   8.190  1.00  8.53           C
ATOM    587  CG  LEU A  72      -2.643  -0.917   7.692  1.00  8.76           C
ATOM    588  CD1 LEU A  72      -2.656  -1.935   8.852  1.00  9.42           C
ATOM    589  CD2 LEU A  72      -3.719  -1.229   6.650  1.00 12.10           C
ATOM    590  N   GLY A  73       0.153   1.640   7.851  1.00  8.30           N
ATOM    591  CA  GLY A  73       1.509   1.542   7.328  1.00 10.33           C
ATOM    592  C   GLY A  73       2.552   1.427   8.426  1.00 11.86           C
ATOM    593  O   GLY A  73       3.463   0.597   8.347  1.00 10.17           O
ATOM    594  N   ALA A  74       2.418   2.241   9.478  1.00  9.56           N
ATOM    595  CA  ALA A  74       3.339   2.160  10.612  1.00 11.10           C
ATOM    596  C   ALA A  74       3.259   0.801  11.299  1.00 12.52           C
ATOM    597  O   ALA A  74       4.280   0.251  11.729  1.00 13.15           O
ATOM    598  CB  ALA A  74       3.044   3.277  11.618  1.00 12.96           C
ATOM    599  N   ILE A  75       2.053   0.242  11.404  1.00 10.26           N
ATOM    600  CA  ILE A  75       1.875  -1.055  12.051  1.00 12.08           C
ATOM    601  C   ILE A  75       2.512  -2.161  11.217  1.00 13.15           C
ATOM    602  O   ILE A  75       3.232  -3.020  11.741  1.00 10.91           O
ATOM    603  CB  ILE A  75       0.377  -1.316  12.297  1.00 12.70           C
ATOM    604  CG1 ILE A  75      -0.117  -0.416  13.434  1.00 13.25           C
ATOM    605  CG2 ILE A  75       0.126  -2.786  12.592  1.00 13.98           C
ATOM    606  CD1 ILE A  75      -1.638  -0.317  13.538  1.00 17.58           C
ATOM    607  N   LEU A  76       2.267  -2.155   9.904  1.00  8.98           N
ATOM    608  CA  LEU A  76       2.858  -3.184   9.052  1.00  9.00           C
ATOM    609  C   LEU A  76       4.382  -3.143   9.105  1.00 10.66           C
ATOM    610  O   LEU A  76       5.037  -4.193   9.105  1.00 10.85           O
ATOM    611  CB  LEU A  76       2.353  -3.024   7.615  1.00  7.53           C
ATOM    612  CG  LEU A  76       0.840  -3.229   7.382  1.00  7.74           C
ATOM    613  CD1 LEU A  76       0.492  -2.901   5.924  1.00  6.67           C
ATOM    614  CD2 LEU A  76       0.423  -4.658   7.700  1.00  8.89           C
ATOM    615  N   LYS A  77       4.964  -1.946   9.182  1.00  8.88           N
ATOM    616  CA  LYS A  77       6.420  -1.831   9.240  1.00  9.04           C
ATOM    617  C   LYS A  77       7.007  -2.317  10.562  1.00 13.16           C
ATOM    618  O   LYS A  77       8.225  -2.518  10.633  1.00 13.91           O
ATOM    619  CB  LYS A  77       6.842  -0.385   8.952  1.00 10.67           C
ATOM    620  CG  LYS A  77       6.645  -0.036   7.475  1.00 10.46           C
ATOM    621  CD  LYS A  77       6.815   1.448   7.207  1.00  8.91           C
ATOM    622  CE  LYS A  77       6.406   1.765   5.761  1.00 11.63           C
ATOM    623  NZ  LYS A  77       6.652   3.193   5.407  1.00 12.14           N
ATOM    624  N   LYS A  78       6.184  -2.538  11.594  1.00 12.75           N
ATOM    625  CA  LYS A  78       6.646  -3.214  12.801  1.00 13.72           C
ATOM    626  C   LYS A  78       6.748  -4.726  12.628  1.00 15.00           C
ATOM    627  O   LYS A  78       7.274  -5.401  13.522  1.00 15.09           O
ATOM    628  CB  LYS A  78       5.713  -2.912  13.979  1.00 15.81           C
ATOM    629  CG  LYS A  78       5.522  -1.433  14.273  1.00 20.76           C
ATOM    630  CD  LYS A  78       6.840  -0.722  14.458  1.00 25.09           C
ATOM    631  CE  LYS A  78       7.462  -1.013  15.812  1.00 37.23           C
ATOM    632  NZ  LYS A  78       8.328   0.126  16.257  1.00 39.73           N
ATOM    633  N   LYS A  79       6.229  -5.269  11.525  1.00  7.67           N
ATOM    634  CA  LYS A  79       6.404  -6.675  11.161  1.00 14.18           C
ATOM    635  C   LYS A  79       6.038  -7.597  12.320  1.00 16.87           C
ATOM    636  O   LYS A  79       6.766  -8.528  12.668  1.00 13.98           O
ATOM    637  CB  LYS A  79       7.830  -6.939  10.670  1.00 10.41           C
ATOM    638  CG  LYS A  79       8.212  -6.078   9.450  1.00 13.61           C
ATOM    639  CD  LYS A  79       9.530  -6.513   8.816  1.00 14.10           C
ATOM    640  CE  LYS A  79      10.640  -6.652   9.826  1.00 21.74           C
ATOM    641  NZ  LYS A  79      11.899  -7.073   9.144  1.00 11.83           N
ATOM    642  N   GLY A  80       4.882  -7.337  12.921  1.00 11.55           N
ATOM    643  CA  GLY A  80       4.382  -8.200  13.975  1.00 19.12           C
ATOM    644  C   GLY A  80       4.834  -7.842  15.376  1.00 24.59           C
ATOM    645  O   GLY A  80       4.199  -8.279  16.347  1.00 25.94           O
ATOM    646  N   HIS A  81       5.919  -7.076  15.513  1.00 19.21           N
ATOM    647  CA  HIS A  81       6.308  -6.488  16.794  1.00 23.03           C
ATOM    648  C   HIS A  81       5.537  -5.192  17.032  1.00 26.66           C
ATOM    649  O   HIS A  81       6.136  -4.152  17.327  1.00 31.85           O
ATOM    650  CB  HIS A  81       7.812  -6.188  16.831  1.00 24.56           C
ATOM    651  CG  HIS A  81       8.673  -7.317  16.359  1.00 32.04           C
ATOM    652  ND1 HIS A  81       9.090  -8.333  17.192  1.00 32.96           N
ATOM    653  CD2 HIS A  81       9.227  -7.570  15.149  1.00 30.31           C
ATOM    654  CE1 HIS A  81       9.850  -9.173  16.512  1.00 35.61           C
ATOM    655  NE2 HIS A  81       9.950  -8.733  15.269  1.00 36.59           N
ATOM    656  N   HIS A  82       4.216  -5.230  16.895  1.00 22.53           N
ATOM    657  CA  HIS A  82       3.412  -4.020  16.769  1.00 31.13           C
ATOM    658  C   HIS A  82       2.545  -3.736  18.000  1.00 37.24           C
ATOM    659  O   HIS A  82       1.518  -3.059  17.891  1.00 35.40           O
ATOM    660  CB  HIS A  82       2.542  -4.108  15.510  1.00 27.24           C
ATOM    661  CG  HIS A  82       1.660  -5.321  15.453  1.00 25.85           C
ATOM    662  ND1 HIS A  82       1.064  -5.747  14.285  1.00 26.55           N
ATOM    663  CD2 HIS A  82       1.253  -6.185  16.417  1.00 24.66           C
ATOM    664  CE1 HIS A  82       0.333  -6.821  14.527  1.00 21.55           C
ATOM    665  NE2 HIS A  82       0.436  -7.113  15.813  1.00 27.79           N
ATOM    666  N   GLU A  83       2.953  -4.221  19.180  1.00 36.26           N
ATOM    667  CA  GLU A  83       2.072  -4.151  20.347  1.00 37.99           C
ATOM    668  C   GLU A  83       1.867  -2.714  20.815  1.00 38.09           C
ATOM    669  O   GLU A  83       0.764  -2.346  21.238  1.00 36.64           O
ATOM    670  CB AGLU A  83       2.632  -5.008  21.481  0.47 35.76           C
ATOM    671  CB BGLU A  83       2.632  -5.008  21.482  0.53 35.77           C
ATOM    672  N   ALA A  84       2.916  -1.890  20.753  1.00 39.02           N
ATOM    673  CA  ALA A  84       2.796  -0.503  21.193  1.00 37.97           C
ATOM    674  C   ALA A  84       1.768   0.252  20.365  1.00 41.36           C
ATOM    675  O   ALA A  84       1.020   1.085  20.894  1.00 40.65           O
ATOM    676  CB  ALA A  84       4.155   0.192  21.117  1.00 34.34           C
ATOM    677  N   GLU A  85       1.709  -0.034  19.064  1.00 43.18           N
ATOM    678  CA  GLU A  85       0.802   0.675  18.168  1.00 39.38           C
ATOM    679  C   GLU A  85      -0.653   0.261  18.352  1.00 36.55           C
ATOM    680  O   GLU A  85      -1.552   1.024  17.978  1.00 33.84           O
ATOM    681  CB  GLU A  85       1.224   0.449  16.713  1.00 34.76           C
ATOM    682  CG  GLU A  85       2.529   1.136  16.320  1.00 41.19           C
ATOM    683  CD  GLU A  85       3.754   0.487  16.940  1.00 45.19           C
ATOM    684  OE1 GLU A  85       3.706  -0.734  17.206  1.00 43.97           O
ATOM    685  OE2 GLU A  85       4.760   1.200  17.169  1.00 47.31           O
ATOM    686  N   LEU A  86      -0.907  -0.914  18.929  1.00 35.23           N
ATOM    687  CA  LEU A  86      -2.251  -1.476  18.950  1.00 26.11           C
ATOM    688  C   LEU A  86      -3.048  -1.138  20.199  1.00 24.19           C
ATOM    689  O   LEU A  86      -4.276  -1.050  20.118  1.00 25.26           O
ATOM    690  CB  LEU A  86      -2.194  -2.995  18.805  1.00 25.59           C
ATOM    691  CG  LEU A  86      -1.553  -3.495  17.514  1.00 28.69           C
ATOM    692  CD1 LEU A  86      -1.873  -4.958  17.310  1.00 23.84           C
ATOM    693  CD2 LEU A  86      -2.012  -2.662  16.330  1.00 30.25           C
ATOM    694  N   LYS A  87      -2.397  -0.966  21.352  1.00 25.89           N
ATOM    695  CA  LYS A  87      -3.145  -0.703  22.581  1.00 23.73           C
ATOM    696  C   LYS A  87      -4.029   0.534  22.465  1.00 21.17           C
ATOM    697  O   LYS A  87      -5.252   0.415  22.657  1.00 21.25           O
ATOM    698  CB  LYS A  87      -2.177  -0.625  23.766  1.00 31.54           C
ATOM    699  N   PRO A  88      -3.513   1.724  22.126  1.00 23.39           N
ATOM    700  CA  PRO A  88      -4.429   2.869  21.979  1.00 24.28           C
ATOM    701  C   PRO A  88      -5.404   2.717  20.821  1.00 20.13           C
ATOM    702  O   PRO A  88      -6.556   3.160  20.934  1.00 19.82           O
ATOM    703  CB  PRO A  88      -3.474   4.055  21.772  1.00 27.44           C
ATOM    704  CG  PRO A  88      -2.275   3.456  21.163  1.00 31.55           C
ATOM    705  CD  PRO A  88      -2.123   2.105  21.806  1.00 28.12           C
ATOM    706  N   LEU A  89      -4.978   2.098  19.711  1.00 16.73           N
ATOM    707  CA  LEU A  89      -5.880   1.893  18.578  1.00 18.60           C
ATOM    708  C   LEU A  89      -7.029   0.967  18.956  1.00 16.95           C
ATOM    709  O   LEU A  89      -8.195   1.263  18.670  1.00 17.77           O
ATOM    710  CB  LEU A  89      -5.105   1.334  17.381  1.00 20.39           C
ATOM    711  CG  LEU A  89      -5.850   1.212  16.052  1.00 18.26           C
ATOM    712  CD1 LEU A  89      -6.129   2.596  15.507  1.00 16.92           C
ATOM    713  CD2 LEU A  89      -5.039   0.406  15.048  1.00 19.73           C
ATOM    714  N   ALA A  90      -6.725  -0.147  19.620  1.00 15.54           N
ATOM    715  CA  ALA A  90      -7.776  -1.046  20.099  1.00 16.83           C
ATOM    716  C   ALA A  90      -8.711  -0.340  21.078  1.00 16.04           C
ATOM    717  O   ALA A  90      -9.938  -0.477  20.988  1.00 18.62           O
ATOM    718  CB  ALA A  90      -7.151  -2.276  20.759  1.00 19.71           C
ATOM    719  N   GLN A  91      -8.148   0.420  22.027  1.00 18.64           N
ATOM    720  CA  GLN A  91      -8.981   1.100  23.019  1.00 17.32           C
ATOM    721  C   GLN A  91      -9.965   2.051  22.353  1.00 17.34           C
ATOM    722  O   GLN A  91     -11.143   2.092  22.723  1.00 19.71           O
ATOM    723  CB  GLN A  91      -8.105   1.851  24.032  1.00 22.87           C
ATOM    724  CG  GLN A  91      -8.831   2.350  25.313  1.00 19.20           C
ATOM    725  CD  GLN A  91      -9.612   3.646  25.117  1.00 26.15           C
ATOM    726  OE1 GLN A  91     -10.580   3.919  25.838  1.00 24.94           O
ATOM    727  NE2 GLN A  91      -9.187   4.458  24.150  1.00 27.79           N
ATOM    728  N   SER A  92      -9.509   2.832  21.373  1.00 15.34           N
ATOM    729  CA  SER A  92     -10.436   3.756  20.733  1.00 14.42           C
ATOM    730  C   SER A  92     -11.453   3.005  19.884  1.00 15.27           C
ATOM    731  O   SER A  92     -12.636   3.358  19.872  1.00 16.70           O
ATOM    732  CB  SER A  92      -9.687   4.782  19.881  1.00 18.55           C
ATOM    733  OG  SER A  92      -9.066   4.164  18.771  1.00 20.53           O
ATOM    734  N   HIS A  93     -11.023   1.964  19.165  1.00 12.43           N
ATOM    735  CA  HIS A  93     -11.998   1.297  18.307  1.00 14.49           C
ATOM    736  C   HIS A  93     -12.940   0.395  19.082  1.00 14.70           C
ATOM    737  O   HIS A  93     -14.110   0.293  18.714  1.00 13.93           O
ATOM    738  CB  HIS A  93     -11.288   0.536  17.196  1.00 13.25           C
ATOM    739  CG  HIS A  93     -10.697   1.454  16.190  1.00 14.64           C
ATOM    740  ND1 HIS A  93      -9.717   2.365  16.522  1.00 17.24           N
ATOM    741  CD2 HIS A  93     -11.010   1.686  14.896  1.00 13.11           C
ATOM    742  CE1 HIS A  93      -9.420   3.091  15.461  1.00 17.64           C
ATOM    743  NE2 HIS A  93     -10.193   2.700  14.465  1.00 13.79           N
ATOM    744  N   ALA A  94     -12.479  -0.238  20.161  1.00 12.49           N
ATOM    745  CA  ALA A  94     -13.392  -1.040  20.972  1.00 14.26           C
ATOM    746  C   ALA A  94     -14.377  -0.164  21.738  1.00 18.73           C
ATOM    747  O   ALA A  94     -15.586  -0.419  21.727  1.00 20.55           O
ATOM    748  CB  ALA A  94     -12.611  -1.919  21.949  1.00 14.90           C
ATOM    749  N   THR A  95     -13.883   0.871  22.412  1.00 17.97           N
ATOM    750  CA  THR A  95     -14.683   1.551  23.426  1.00 20.81           C
ATOM    751  C   THR A  95     -15.302   2.862  22.967  1.00 23.39           C
ATOM    752  O   THR A  95     -16.332   3.271  23.520  1.00 16.71           O
ATOM    753  CB  THR A  95     -13.826   1.813  24.667  1.00 18.46           C
ATOM    754  OG1 THR A  95     -12.899   2.867  24.393  1.00 19.45           O
ATOM    755  CG2 THR A  95     -13.050   0.549  25.039  1.00 18.76           C
ATOM    756  N   LYS A  96     -14.706   3.547  21.991  1.00 19.26           N
ATOM    757  CA  LYS A  96     -15.235   4.826  21.532  1.00 17.48           C
ATOM    758  C   LYS A  96     -15.945   4.691  20.191  1.00 20.26           C
ATOM    759  O   LYS A  96     -17.129   5.019  20.075  1.00 24.54           O
ATOM    760  CB  LYS A  96     -14.114   5.866  21.442  1.00 20.97           C
ATOM    761  N   HIS A  97     -15.240   4.200  19.169  1.00 17.47           N
ATOM    762  CA  HIS A  97     -15.856   4.033  17.857  1.00 17.87           C
ATOM    763  C   HIS A  97     -16.782   2.823  17.794  1.00 18.36           C
ATOM    764  O   HIS A  97     -17.659   2.788  16.927  1.00 17.11           O
ATOM    765  CB  HIS A  97     -14.763   3.941  16.786  1.00 15.68           C
ATOM    766  CG  HIS A  97     -13.772   5.062  16.858  1.00 17.32           C
ATOM    767  ND1 HIS A  97     -14.153   6.375  17.051  1.00 18.71           N
ATOM    768  CD2 HIS A  97     -12.419   5.065  16.814  1.00 17.09           C
ATOM    769  CE1 HIS A  97     -13.076   7.140  17.109  1.00 19.11           C
ATOM    770  NE2 HIS A  97     -12.011   6.370  16.964  1.00 15.22           N
ATOM    771  N   LYS A  98     -16.614   1.844  18.687  1.00 16.46           N
ATOM    772  CA  LYS A  98     -17.450   0.639  18.733  1.00 16.64           C
ATOM    773  C   LYS A  98     -17.410  -0.142  17.414  1.00 17.79           C
ATOM    774  O   LYS A  98     -18.437  -0.402  16.786  1.00 18.09           O
ATOM    775  CB  LYS A  98     -18.892   0.998  19.095  1.00 21.34           C
ATOM    776  CG  LYS A  98     -19.490   0.155  20.193  1.00 35.07           C
ATOM    777  CD  LYS A  98     -19.100   0.706  21.551  1.00 31.58           C
ATOM    778  CE  LYS A  98     -19.437   2.187  21.639  1.00 32.74           C
ATOM    779  NZ  LYS A  98     -20.852   2.467  21.270  1.00 40.04           N
ATOM    780  N   ILE A  99     -16.206  -0.532  17.004  1.00 15.02           N
ATOM    781  CA  ILE A  99     -15.993  -1.217  15.733  1.00 14.18           C
ATOM    782  C   ILE A  99     -15.853  -2.714  16.016  1.00 19.25           C
ATOM    783  O   ILE A  99     -14.852  -3.123  16.623  1.00 18.26           O
ATOM    784  CB  ILE A  99     -14.750  -0.686  15.008  1.00 15.67           C
ATOM    785  CG1 ILE A  99     -14.834   0.832  14.820  1.00 14.74           C
ATOM    786  CG2 ILE A  99     -14.563  -1.401  13.675  1.00 14.81           C
ATOM    787  CD1 ILE A  99     -16.187   1.332  14.318  1.00 14.30           C
ATOM    788  N   PRO A 100     -16.795  -3.552  15.583  1.00 16.73           N
ATOM    789  CA  PRO A 100     -16.598  -5.000  15.732  1.00 16.05           C
ATOM    790  C   PRO A 100     -15.433  -5.487  14.888  1.00 16.24           C
ATOM    791  O   PRO A 100     -15.123  -4.932  13.831  1.00 15.57           O
ATOM    792  CB  PRO A 100     -17.923  -5.603  15.248  1.00 17.78           C
ATOM    793  CG  PRO A 100     -18.669  -4.495  14.585  1.00 14.91           C
ATOM    794  CD  PRO A 100     -18.153  -3.209  15.129  1.00 18.48           C
ATOM    795  N   ILE A 101     -14.792  -6.558  15.364  1.00 18.13           N
ATOM    796  CA  ILE A 101     -13.681  -7.147  14.621  1.00 16.34           C
ATOM    797  C   ILE A 101     -14.087  -7.464  13.191  1.00 15.15           C
ATOM    798  O   ILE A 101     -13.285  -7.311  12.262  1.00 16.57           O
ATOM    799  CB  ILE A 101     -13.157  -8.405  15.345  1.00 18.15           C
ATOM    800  CG1 ILE A 101     -12.587  -8.019  16.708  1.00 18.85           C
ATOM    801  CG2 ILE A 101     -12.081  -9.088  14.510  1.00 20.60           C
ATOM    802  CD1 ILE A 101     -11.341  -7.136  16.617  1.00 17.62           C
ATOM    803  N   LYS A 102     -15.337  -7.895  12.985  1.00 14.10           N
ATOM    804  CA  LYS A 102     -15.811  -8.212  11.640  1.00 13.90           C
ATOM    805  C   LYS A 102     -15.651  -7.030  10.689  1.00 13.45           C
ATOM    806  O   LYS A 102     -15.358  -7.216   9.500  1.00 11.16           O
ATOM    807  CB  LYS A 102     -17.271  -8.661  11.691  1.00 16.19           C
ATOM    808  CG  LYS A 102     -17.814  -9.104  10.342  1.00 20.31           C
ATOM    809  CD  LYS A 102     -19.283  -9.469  10.420  1.00 24.70           C
ATOM    810  CE  LYS A 102     -19.501 -10.782  11.154  1.00 28.01           C
ATOM    811  NZ  LYS A 102     -20.896 -11.281  10.922  1.00 28.94           N
ATOM    812  N   TYR A 103     -15.865  -5.808  11.179  1.00 11.34           N
ATOM    813  CA  TYR A 103     -15.634  -4.641  10.327  1.00 10.67           C
ATOM    814  C   TYR A 103     -14.158  -4.500   9.970  1.00 11.78           C
ATOM    815  O   TYR A 103     -13.829  -3.968   8.905  1.00 11.25           O
ATOM    816  CB  TYR A 103     -16.123  -3.353  11.004  1.00  9.04           C
ATOM    817  CG  TYR A 103     -17.626  -3.195  11.151  1.00 13.35           C
ATOM    818  CD1 TYR A 103     -18.179  -1.947  11.433  1.00 13.24           C
ATOM    819  CD2 TYR A 103     -18.494  -4.284  11.030  1.00 12.83           C
ATOM    820  CE1 TYR A 103     -19.547  -1.786  11.591  1.00 13.49           C
ATOM    821  CE2 TYR A 103     -19.878  -4.126  11.194  1.00 16.43           C
ATOM    822  CZ  TYR A 103     -20.390  -2.873  11.475  1.00 15.05           C
ATOM    823  OH  TYR A 103     -21.753  -2.694  11.635  1.00 16.12           O
ATOM    824  N   LEU A 104     -13.252  -4.962  10.836  1.00 11.24           N
ATOM    825  CA  LEU A 104     -11.849  -4.994  10.426  1.00 10.70           C
ATOM    826  C   LEU A 104     -11.614  -6.039   9.336  1.00 11.94           C
ATOM    827  O   LEU A 104     -10.752  -5.848   8.464  1.00 11.67           O
ATOM    828  CB  LEU A 104     -10.949  -5.241  11.634  1.00  9.70           C
ATOM    829  CG  LEU A 104     -11.067  -4.196  12.754  1.00 12.48           C
ATOM    830  CD1 LEU A 104     -10.062  -4.452  13.874  1.00 13.92           C
ATOM    831  CD2 LEU A 104     -10.930  -2.778  12.216  1.00 12.84           C
ATOM    832  N   GLU A 105     -12.376  -7.133   9.355  1.00  8.75           N
ATOM    833  C   GLU A 105     -12.830  -7.430   6.961  1.00  9.90           C
ATOM    834  O   GLU A 105     -12.227  -7.603   5.892  1.00  9.21           O
ATOM    835  CA AGLU A 105     -12.323  -8.081   8.244  0.59 11.93           C
ATOM    836  CB AGLU A 105     -13.127  -9.344   8.580  0.59 11.52           C
ATOM    837  CG AGLU A 105     -12.791 -10.546   7.685  0.59 12.57           C
ATOM    838  CD AGLU A 105     -13.593 -11.792   8.015  0.59 15.25           C
ATOM    839  OE1AGLU A 105     -13.686 -12.704   7.156  0.59 12.79           O
ATOM    840  OE2AGLU A 105     -14.147 -11.853   9.131  0.59 16.93           O
ATOM    841  CA BGLU A 105     -12.330  -8.080   8.244  0.41 11.76           C
ATOM    842  CB BGLU A 105     -13.155  -9.321   8.583  0.41 11.52           C
ATOM    843  CG BGLU A 105     -12.604 -10.103   9.751  0.41 12.81           C
ATOM    844  CD BGLU A 105     -13.533 -11.208  10.211  0.41 16.15           C
ATOM    845  OE1BGLU A 105     -14.471 -11.557   9.455  0.41 16.41           O
ATOM    846  OE2BGLU A 105     -13.328 -11.721  11.335  0.41 16.02           O
ATOM    847  N   PHE A 106     -13.920  -6.665   7.053  1.00  8.47           N
ATOM    848  CA  PHE A 106     -14.422  -5.924   5.894  1.00 11.91           C
ATOM    849  C   PHE A 106     -13.365  -4.980   5.321  1.00  9.41           C
ATOM    850  O   PHE A 106     -13.191  -4.904   4.100  1.00  9.50           O
ATOM    851  CB  PHE A 106     -15.673  -5.114   6.253  1.00 13.85           C
ATOM    852  CG  PHE A 106     -16.859  -5.932   6.685  1.00 12.27           C
ATOM    853  CD1 PHE A 106     -17.890  -5.325   7.394  1.00 15.18           C
ATOM    854  CD2 PHE A 106     -16.961  -7.274   6.380  1.00 16.17           C
ATOM    855  CE1 PHE A 106     -18.995  -6.051   7.799  1.00 15.40           C
ATOM    856  CE2 PHE A 106     -18.063  -8.005   6.784  1.00 19.66           C
ATOM    857  CZ  PHE A 106     -19.082  -7.392   7.493  1.00 16.81           C
ATOM    858  N   ILE A 107     -12.707  -4.178   6.171  1.00  9.17           N
ATOM    859  CA  ILE A 107     -11.752  -3.221   5.604  1.00  8.46           C
ATOM    860  C   ILE A 107     -10.513  -3.948   5.092  1.00  9.03           C
ATOM    861  O   ILE A 107      -9.882  -3.498   4.133  1.00  9.43           O
ATOM    862  CB  ILE A 107     -11.391  -2.107   6.609  1.00  8.07           C
ATOM    863  CG1 ILE A 107     -10.832  -0.879   5.880  1.00 11.13           C
ATOM    864  CG2 ILE A 107     -10.406  -2.615   7.658  1.00  8.51           C
ATOM    865  CD1 ILE A 107     -10.710   0.364   6.765  1.00 11.36           C
ATOM    866  N   SER A 108     -10.159  -5.087   5.691  1.00  8.38           N
ATOM    867  CA  SER A 108      -9.086  -5.910   5.129  1.00  7.82           C
ATOM    868  C   SER A 108      -9.422  -6.344   3.708  1.00 10.38           C
ATOM    869  O   SER A 108      -8.570  -6.301   2.810  1.00  9.71           O
ATOM    870  CB  SER A 108      -8.846  -7.139   6.005  1.00  7.44           C
ATOM    871  OG  SER A 108      -8.312  -6.758   7.258  1.00 10.24           O
ATOM    872  N   GLU A 109     -10.667  -6.787   3.501  1.00  8.47           N
ATOM    873  CA  GLU A 109     -11.158  -7.137   2.168  1.00  9.80           C
ATOM    874  C   GLU A 109     -11.031  -5.955   1.207  1.00  9.99           C
ATOM    875  O   GLU A 109     -10.536  -6.100   0.076  1.00 10.46           O
ATOM    876  CB AGLU A 109     -12.612  -7.613   2.249  0.33 13.73           C
ATOM    877  CG AGLU A 109     -13.156  -8.273   0.975  0.33 15.08           C
ATOM    878  CD AGLU A 109     -13.447  -7.281  -0.144  0.33 15.11           C
ATOM    879  OE1AGLU A 109     -13.290  -7.646  -1.330  0.33 16.47           O
ATOM    880  OE2AGLU A 109     -13.828  -6.130   0.160  0.33 14.71           O
ATOM    881  CB BGLU A 109     -12.611  -7.599   2.300  0.67 13.90           C
ATOM    882  CG BGLU A 109     -13.380  -7.865   1.037  0.67 15.17           C
ATOM    883  CD BGLU A 109     -14.849  -8.140   1.339  0.67 16.54           C
ATOM    884  OE1BGLU A 109     -15.553  -7.213   1.796  0.67 15.41           O
ATOM    885  OE2BGLU A 109     -15.299  -9.286   1.139  0.67 19.33           O
ATOM    886  N   ALA A 110     -11.476  -4.771   1.644  1.00  8.42           N
ATOM    887  CA  ALA A 110     -11.405  -3.578   0.804  1.00  7.76           C
ATOM    888  C   ALA A 110      -9.965  -3.216   0.458  1.00  9.50           C
ATOM    889  O   ALA A 110      -9.676  -2.810  -0.673  1.00  8.44           O
ATOM    890  CB  ALA A 110     -12.086  -2.401   1.512  1.00  8.93           C
ATOM    891  N   ILE A 111      -9.059  -3.317   1.435  1.00  6.80           N
ATOM    892  CA  ILE A 111      -7.642  -3.026   1.201  1.00  7.14           C
ATOM    893  C   ILE A 111      -7.084  -3.952   0.131  1.00  8.03           C
ATOM    894  O   ILE A 111      -6.406  -3.513  -0.808  1.00 10.49           O
ATOM    895  CB  ILE A 111      -6.841  -3.154   2.514  1.00  6.39           C
ATOM    896  CG1 ILE A 111      -7.189  -2.041   3.506  1.00  9.68           C
ATOM    897  CG2 ILE A 111      -5.331  -3.164   2.228  1.00  6.02           C
ATOM    898  CD1 ILE A 111      -6.688  -2.355   4.933  1.00  9.98           C
ATOM    899  N   ILE A 112      -7.345  -5.255   0.268  1.00  7.20           N
ATOM    900  CA  ILE A 112      -6.845  -6.203  -0.719  1.00  9.20           C
ATOM    901  C   ILE A 112      -7.448  -5.914  -2.086  1.00  8.63           C
ATOM    902  O   ILE A 112      -6.745  -5.939  -3.106  1.00 11.81           O
ATOM    903  CB  ILE A 112      -7.105  -7.651  -0.265  1.00  9.57           C
ATOM    904  CG1 ILE A 112      -6.264  -7.945   0.993  1.00 10.50           C
ATOM    905  CG2 ILE A 112      -6.742  -8.629  -1.385  1.00  7.31           C
ATOM    906  CD1 ILE A 112      -6.656  -9.199   1.730  1.00 10.56           C
ATOM    907  N   HIS A 113      -8.748  -5.610  -2.129  1.00  7.94           N
ATOM    908  CA  HIS A 113      -9.395  -5.321  -3.404  1.00  9.34           C
ATOM    909  C   HIS A 113      -8.749  -4.124  -4.098  1.00  9.81           C
ATOM    910  O   HIS A 113      -8.458  -4.169  -5.302  1.00 12.39           O
ATOM    911  CB  HIS A 113     -10.879  -5.064  -3.189  1.00  9.60           C
ATOM    912  CG  HIS A 113     -11.628  -4.816  -4.463  1.00 16.67           C
ATOM    913  ND1 HIS A 113     -11.845  -3.552  -4.972  1.00 17.48           N
ATOM    914  CD2 HIS A 113     -12.187  -5.678  -5.343  1.00 17.85           C
ATOM    915  CE1 HIS A 113     -12.525  -3.646  -6.101  1.00 14.68           C
ATOM    916  NE2 HIS A 113     -12.746  -4.925  -6.348  1.00 21.07           N
ATOM    917  N   VAL A 114      -8.532  -3.038  -3.357  1.00  7.69           N
ATOM    918  CA  VAL A 114      -7.991  -1.822  -3.967  1.00 10.33           C
ATOM    919  C   VAL A 114      -6.554  -2.046  -4.427  1.00  9.15           C
ATOM    920  O   VAL A 114      -6.156  -1.605  -5.516  1.00  8.82           O
ATOM    921  CB  VAL A 114      -8.116  -0.635  -2.989  1.00  9.14           C
ATOM    922  CG1 VAL A 114      -7.268   0.558  -3.455  1.00  8.84           C
ATOM    923  CG2 VAL A 114      -9.605  -0.227  -2.849  1.00  6.82           C
ATOM    924  N   LEU A 115      -5.766  -2.775  -3.634  1.00  7.09           N
ATOM    925  CA  LEU A 115      -4.405  -3.097  -4.049  1.00 11.30           C
ATOM    926  C   LEU A 115      -4.408  -3.967  -5.301  1.00 10.16           C
ATOM    927  O   LEU A 115      -3.561  -3.794  -6.189  1.00 11.44           O
ATOM    928  CB  LEU A 115      -3.660  -3.787  -2.906  1.00  9.29           C
ATOM    929  CG  LEU A 115      -3.294  -2.904  -1.711  1.00 11.80           C
ATOM    930  CD1 LEU A 115      -2.563  -3.707  -0.656  1.00  9.56           C
ATOM    931  CD2 LEU A 115      -2.435  -1.769  -2.173  1.00 12.08           C
ATOM    932  N   HIS A 116      -5.368  -4.900  -5.397  1.00 10.31           N
ATOM    933  CA  HIS A 116      -5.488  -5.723  -6.600  1.00  8.99           C
ATOM    934  C   HIS A 116      -5.864  -4.874  -7.813  1.00 12.12           C
ATOM    935  O   HIS A 116      -5.312  -5.065  -8.904  1.00 12.77           O
ATOM    936  CB  HIS A 116      -6.511  -6.838  -6.360  1.00 10.22           C
ATOM    937  CG  HIS A 116      -6.702  -7.762  -7.528  1.00 12.69           C
ATOM    938  ND1 HIS A 116      -7.823  -7.726  -8.330  1.00 18.07           N
ATOM    939  CD2 HIS A 116      -5.922  -8.753  -8.018  1.00 13.33           C
ATOM    940  CE1 HIS A 116      -7.726  -8.657  -9.264  1.00 16.54           C
ATOM    941  NE2 HIS A 116      -6.577  -9.290  -9.102  1.00 18.30           N
ATOM    942  N   SER A 117      -6.782  -3.915  -7.638  1.00 10.78           N
ATOM    943  CA  SER A 117      -7.179  -3.048  -8.747  1.00 10.86           C
ATOM    944  C   SER A 117      -6.017  -2.181  -9.225  1.00 14.28           C
ATOM    945  O   SER A 117      -5.765  -2.070 -10.431  1.00 12.94           O
ATOM    946  CB ASER A 117      -8.362  -2.174  -8.329  0.41 13.79           C
ATOM    947  OG ASER A 117      -8.769  -1.328  -9.390  0.41 15.53           O
ATOM    948  CB CSER A 117      -8.359  -2.168  -8.330  0.59 14.38           C
ATOM    949  OG CSER A 117      -9.514  -2.940  -8.057  0.59 15.62           O
ATOM    950  N   ARG A 118      -5.298  -1.554  -8.297  1.00 10.51           N
ATOM    951  CA  ARG A 118      -4.332  -0.521  -8.657  1.00 11.08           C
ATOM    952  C   ARG A 118      -2.919  -1.042  -8.931  1.00 11.66           C
ATOM    953  O   ARG A 118      -2.186  -0.408  -9.699  1.00 12.05           O
ATOM    954  CB AARG A 118      -4.291   0.552  -7.562  0.38 13.02           C
ATOM    955  CG AARG A 118      -5.606   1.320  -7.439  0.38 14.28           C
ATOM    956  CD AARG A 118      -5.557   2.426  -6.388  0.38 14.04           C
ATOM    957  NE AARG A 118      -4.637   3.511  -6.725  0.38 14.16           N
ATOM    958  CZ AARG A 118      -4.756   4.754  -6.265  0.38 15.21           C
ATOM    959  NH1AARG A 118      -3.874   5.685  -6.609  0.38 16.28           N
ATOM    960  NH2AARG A 118      -5.765   5.069  -5.466  0.38 14.12           N
ATOM    961  CB BARG A 118      -4.235   0.526  -7.536  0.62 13.35           C
ATOM    962  CG BARG A 118      -5.369   1.551  -7.450  0.62 14.66           C
ATOM    963  CD BARG A 118      -5.138   2.463  -6.240  0.62 13.90           C
ATOM    964  NE BARG A 118      -6.072   3.585  -6.145  0.62 15.06           N
ATOM    965  CZ BARG A 118      -5.760   4.850  -6.416  0.62 13.61           C
ATOM    966  NH1BARG A 118      -6.674   5.798  -6.294  0.62 14.99           N
ATOM    967  NH2BARG A 118      -4.539   5.169  -6.810  0.62 16.03           N
ATOM    968  N   HIS A 119      -2.493  -2.155  -8.322  1.00 12.10           N
ATOM    969  CA  HIS A 119      -1.080  -2.552  -8.347  1.00 12.50           C
ATOM    970  C   HIS A 119      -0.895  -4.042  -8.641  1.00 10.86           C
ATOM    971  O   HIS A 119      -0.190  -4.745  -7.914  1.00 11.89           O
ATOM    972  CB  HIS A 119      -0.416  -2.179  -7.022  1.00 12.64           C
ATOM    973  CG  HIS A 119      -0.561  -0.729  -6.677  1.00 14.77           C
ATOM    974  ND1 HIS A 119      -0.024   0.270  -7.455  1.00 11.24           N
ATOM    975  CD2 HIS A 119      -1.208  -0.109  -5.662  1.00 11.96           C
ATOM    976  CE1 HIS A 119      -0.319   1.447  -6.929  1.00 14.28           C
ATOM    977  NE2 HIS A 119      -1.041   1.246  -5.841  1.00 11.28           N
ATOM    978  N   PRO A 120      -1.444  -4.539  -9.754  1.00 10.88           N
ATOM    979  CA  PRO A 120      -1.271  -5.976 -10.059  1.00 16.04           C
ATOM    980  C   PRO A 120       0.179  -6.397 -10.246  1.00 16.34           C
ATOM    981  O   PRO A 120       0.529  -7.550  -9.950  1.00 15.38           O
ATOM    982  CB  PRO A 120      -2.083  -6.155 -11.350  1.00 20.25           C
ATOM    983  CG  PRO A 120      -2.092  -4.804 -11.973  1.00 17.67           C
ATOM    984  CD  PRO A 120      -2.176  -3.839 -10.825  1.00 14.16           C
ATOM    985  N   GLY A 121       1.043  -5.489 -10.703  1.00 15.25           N
ATOM    986  CA  GLY A 121       2.443  -5.825 -10.907  1.00 18.43           C
ATOM    987  C   GLY A 121       3.196  -6.121  -9.631  1.00 19.67           C
ATOM    988  O   GLY A 121       4.215  -6.818  -9.671  1.00 20.79           O
ATOM    989  N   ASN A 122       2.727  -5.601  -8.499  1.00 12.37           N
ATOM    990  CA  ASN A 122       3.347  -5.880  -7.213  1.00 15.48           C
ATOM    991  C   ASN A 122       2.385  -6.549  -6.248  1.00 12.99           C
ATOM    992  O   ASN A 122       2.702  -6.679  -5.065  1.00 12.55           O
ATOM    993  CB  ASN A 122       3.912  -4.592  -6.613  1.00 14.22           C
ATOM    994  CG  ASN A 122       5.130  -4.102  -7.378  1.00 17.59           C
ATOM    995  OD1 ASN A 122       6.215  -4.669  -7.249  1.00 21.17           O
ATOM    996  ND2 ASN A 122       4.948  -3.077  -8.210  1.00 20.56           N
ATOM    997  N   PHE A 123       1.230  -6.989  -6.726  1.00  8.55           N
ATOM    998  CA  PHE A 123       0.229  -7.659  -5.899  1.00  9.22           C
ATOM    999  C   PHE A 123      -0.240  -8.930  -6.591  1.00 11.72           C
ATOM   1000  O   PHE A 123      -1.437  -9.169  -6.775  1.00 12.02           O
ATOM   1001  CB  PHE A 123      -0.935  -6.709  -5.592  1.00  9.17           C
ATOM   1002  CG  PHE A 123      -1.648  -7.002  -4.301  1.00  8.78           C
ATOM   1003  CD1 PHE A 123      -0.933  -7.125  -3.111  1.00 11.40           C
ATOM   1004  CD2 PHE A 123      -3.022  -7.121  -4.267  1.00 10.45           C
ATOM   1005  CE1 PHE A 123      -1.586  -7.392  -1.910  1.00  9.98           C
ATOM   1006  CE2 PHE A 123      -3.699  -7.375  -3.060  1.00 11.22           C
ATOM   1007  CZ  PHE A 123      -2.982  -7.512  -1.883  1.00 10.03           C
ATOM   1008  N   GLY A 124       0.724  -9.757  -7.003  1.00 10.42           N
ATOM   1009  CA  GLY A 124       0.444 -11.069  -7.543  1.00 12.77           C
ATOM   1010  C   GLY A 124       0.094 -12.047  -6.445  1.00 12.43           C
ATOM   1011  O   GLY A 124      -0.180 -11.668  -5.303  1.00 10.01           O
ATOM   1012  N   ALA A 125       0.138 -13.336  -6.798  1.00 11.37           N
ATOM   1013  CA  ALA A 125      -0.372 -14.374  -5.898  1.00 15.41           C
ATOM   1014  C   ALA A 125       0.361 -14.390  -4.559  1.00 14.05           C
ATOM   1015  O   ALA A 125      -0.275 -14.398  -3.498  1.00  9.67           O
ATOM   1016  CB  ALA A 125      -0.278 -15.751  -6.558  1.00 17.54           C
ATOM   1017  N   CYS A 126       1.702 -14.429  -4.579  1.00 11.21           N
ATOM   1018  CA  CYS A 126       2.427 -14.490  -3.313  1.00 10.95           C
ATOM   1019  C   CYS A 126       2.177 -13.245  -2.472  1.00 12.36           C
ATOM   1020  O   CYS A 126       1.953 -13.345  -1.258  1.00 10.12           O
ATOM   1021  CB  CYS A 126       3.921 -14.693  -3.557  1.00 11.73           C
ATOM   1022  SG  CYS A 126       4.264 -16.384  -4.095  1.00 13.76           S
ATOM   1023  N   ALA A 127       2.191 -12.067  -3.101  1.00 11.39           N
ATOM   1024  CA  ALA A 127       1.965 -10.829  -2.358  1.00  9.58           C
ATOM   1025  C   ALA A 127       0.555 -10.775  -1.769  1.00 10.38           C
ATOM   1026  O   ALA A 127       0.358 -10.268  -0.658  1.00  9.30           O
ATOM   1027  CB  ALA A 127       2.213  -9.627  -3.266  1.00 11.84           C
ATOM   1028  N   GLN A 128      -0.438 -11.290  -2.497  1.00  6.41           N
ATOM   1029  CA  GLN A 128      -1.800 -11.320  -1.971  1.00  8.31           C
ATOM   1030  C   GLN A 128      -1.910 -12.230  -0.752  1.00  8.21           C
ATOM   1031  O   GLN A 128      -2.558 -11.875   0.239  1.00 11.13           O
ATOM   1032  CB  GLN A 128      -2.773 -11.776  -3.055  1.00  9.24           C
ATOM   1033  CG  GLN A 128      -3.080 -10.714  -4.083  1.00  8.26           C
ATOM   1034  CD  GLN A 128      -3.921 -11.242  -5.229  1.00  9.38           C
ATOM   1035  OE1 GLN A 128      -3.538 -11.136  -6.403  1.00 13.12           O
ATOM   1036  NE2 GLN A 128      -5.062 -11.828  -4.897  1.00  8.31           N
ATOM   1037  N   GLY A 129      -1.286 -13.409  -0.807  1.00  7.96           N
ATOM   1038  CA  GLY A 129      -1.287 -14.283   0.357  1.00 11.13           C
ATOM   1039  C   GLY A 129      -0.603 -13.654   1.554  1.00 12.09           C
ATOM   1040  O   GLY A 129      -1.107 -13.729   2.676  1.00 10.17           O
ATOM   1041  N   ALA A 130       0.551 -13.022   1.330  1.00  9.35           N
ATOM   1042  CA  ALA A 130       1.290 -12.383   2.415  1.00 10.67           C
ATOM   1043  C   ALA A 130       0.498 -11.236   3.034  1.00 10.06           C
ATOM   1044  O   ALA A 130       0.488 -11.066   4.262  1.00  9.22           O
ATOM   1045  CB  ALA A 130       2.642 -11.890   1.893  1.00  7.75           C
ATOM   1046  N   MET A 131      -0.187 -10.445   2.205  1.00  8.53           N
ATOM   1047  CA  MET A 131      -0.977  -9.340   2.745  1.00 10.39           C
ATOM   1048  C   MET A 131      -2.183  -9.855   3.521  1.00  6.92           C
ATOM   1049  O   MET A 131      -2.519  -9.318   4.579  1.00  7.64           O
ATOM   1050  CB  MET A 131      -1.426  -8.395   1.628  1.00  8.43           C
ATOM   1051  CG  MET A 131      -2.279  -7.203   2.126  1.00  5.88           C
ATOM   1052  SD  MET A 131      -1.373  -6.068   3.208  1.00  9.20           S
ATOM   1053  CE  MET A 131      -0.310  -5.243   2.026  1.00 10.82           C
ATOM   1054  N   ASN A 132      -2.838 -10.903   3.017  1.00  8.09           N
ATOM   1055  CA  ASN A 132      -3.903 -11.544   3.780  1.00  8.59           C
ATOM   1056  C   ASN A 132      -3.419 -11.932   5.172  1.00 11.17           C
ATOM   1057  O   ASN A 132      -4.075 -11.640   6.178  1.00  9.59           O
ATOM   1058  CB  ASN A 132      -4.402 -12.781   3.040  1.00 10.67           C
ATOM   1059  CG  ASN A 132      -5.535 -13.460   3.774  1.00 14.78           C
ATOM   1060  OD1 ASN A 132      -6.488 -12.805   4.168  1.00  9.51           O
ATOM   1061  ND2 ASN A 132      -5.419 -14.767   3.987  1.00 17.97           N
ATOM   1062  N   LYS A 133      -2.247 -12.565   5.244  1.00 10.63           N
ATOM   1063  CA  LYS A 133      -1.717 -13.003   6.531  1.00  9.71           C
ATOM   1064  C   LYS A 133      -1.379 -11.819   7.431  1.00 12.51           C
ATOM   1065  O   LYS A 133      -1.672 -11.849   8.633  1.00 11.67           O
ATOM   1066  CB  LYS A 133      -0.475 -13.881   6.325  1.00  9.83           C
ATOM   1067  CG  LYS A 133      -0.750 -15.331   5.990  1.00 15.96           C
ATOM   1068  CD  LYS A 133       0.566 -16.131   5.872  1.00 19.40           C
ATOM   1069  CE  LYS A 133       1.370 -16.074   7.163  1.00 22.80           C
ATOM   1070  NZ  LYS A 133       2.500 -17.057   7.194  1.00 27.09           N
ATOM   1071  N   ALA A 134      -0.753 -10.775   6.875  1.00  9.93           N
ATOM   1072  CA  ALA A 134      -0.390  -9.605   7.676  1.00  9.77           C
ATOM   1073  C   ALA A 134      -1.624  -8.932   8.261  1.00 11.47           C
ATOM   1074  O   ALA A 134      -1.638  -8.551   9.439  1.00  8.83           O
ATOM   1075  CB  ALA A 134       0.400  -8.595   6.830  1.00 10.20           C
ATOM   1076  N   LEU A 135      -2.669  -8.766   7.446  1.00  8.79           N
ATOM   1077  CA  LEU A 135      -3.904  -8.174   7.949  1.00  9.59           C
ATOM   1078  C   LEU A 135      -4.625  -9.121   8.896  1.00 12.08           C
ATOM   1079  O   LEU A 135      -5.228  -8.668   9.876  1.00 13.00           O
ATOM   1080  CB  LEU A 135      -4.804  -7.768   6.781  1.00 10.01           C
ATOM   1081  CG  LEU A 135      -4.161  -6.673   5.913  1.00 11.21           C
ATOM   1082  CD1 LEU A 135      -5.053  -6.389   4.715  1.00  8.29           C
ATOM   1083  CD2 LEU A 135      -3.849  -5.388   6.725  1.00  9.25           C
ATOM   1084  N   GLU A 136      -4.549 -10.434   8.653  1.00 11.42           N
ATOM   1085  CA  GLU A 136      -5.127 -11.371   9.609  1.00 12.86           C
ATOM   1086  C   GLU A 136      -4.415 -11.283  10.956  1.00 12.70           C
ATOM   1087  O   GLU A 136      -5.060 -11.303  12.011  1.00 11.46           O
ATOM   1088  CB  GLU A 136      -5.064 -12.793   9.057  1.00 12.47           C
ATOM   1089  CG  GLU A 136      -5.602 -13.841  10.002  1.00 18.99           C
ATOM   1090  CD  GLU A 136      -5.415 -15.243   9.464  1.00 23.06           C
ATOM   1091  OE1 GLU A 136      -4.777 -15.380   8.396  1.00 23.71           O
ATOM   1092  OE2 GLU A 136      -5.902 -16.195  10.110  1.00 23.61           O
ATOM   1093  N   LEU A 137      -3.083 -11.180  10.940  1.00 13.06           N
ATOM   1094  CA  LEU A 137      -2.340 -11.034  12.189  1.00 10.43           C
ATOM   1095  C   LEU A 137      -2.728  -9.749  12.914  1.00 11.26           C
ATOM   1096  O   LEU A 137      -2.872  -9.729  14.146  1.00 11.86           O
ATOM   1097  CB  LEU A 137      -0.840 -11.041  11.899  1.00 11.70           C
ATOM   1098  CG  LEU A 137       0.061 -10.744  13.102  1.00 14.05           C
ATOM   1099  CD1 LEU A 137      -0.148 -11.780  14.193  1.00 15.56           C
ATOM   1100  CD2 LEU A 137       1.521 -10.718  12.647  1.00 11.03           C
ATOM   1101  N   PHE A 138      -2.874  -8.658  12.163  1.00 11.45           N
ATOM   1102  CA  PHE A 138      -3.330  -7.398  12.743  1.00 12.74           C
ATOM   1103  C   PHE A 138      -4.691  -7.564  13.421  1.00 10.26           C
ATOM   1104  O   PHE A 138      -4.898  -7.102  14.554  1.00 10.48           O
ATOM   1105  CB  PHE A 138      -3.373  -6.342  11.637  1.00 10.71           C
ATOM   1106  CG  PHE A 138      -4.205  -5.132  11.962  1.00 12.97           C
ATOM   1107  CD1 PHE A 138      -5.440  -4.941  11.352  1.00 13.90           C
ATOM   1108  CD2 PHE A 138      -3.736  -4.174  12.848  1.00 14.90           C
ATOM   1109  CE1 PHE A 138      -6.206  -3.814  11.637  1.00 13.91           C
ATOM   1110  CE2 PHE A 138      -4.486  -3.041  13.138  1.00 16.74           C
ATOM   1111  CZ  PHE A 138      -5.725  -2.862  12.535  1.00 15.04           C
ATOM   1112  N   ARG A 139      -5.634  -8.230  12.744  1.00  8.15           N
ATOM   1113  CA  ARG A 139      -6.968  -8.415  13.313  1.00 10.47           C
ATOM   1114  C   ARG A 139      -6.927  -9.297  14.547  1.00 10.99           C
ATOM   1115  O   ARG A 139      -7.638  -9.039  15.523  1.00 12.39           O
ATOM   1116  CB  ARG A 139      -7.920  -9.019  12.282  1.00 14.74           C
ATOM   1117  CG  ARG A 139      -8.175  -8.142  11.073  1.00  9.84           C
ATOM   1118  CD  ARG A 139      -9.398  -8.636  10.305  1.00 10.09           C
ATOM   1119  NE  ARG A 139      -9.343 -10.055   9.955  1.00  9.48           N
ATOM   1120  CZ  ARG A 139      -8.787 -10.525   8.841  1.00 12.74           C
ATOM   1121  NH1 ARG A 139      -8.785 -11.829   8.593  1.00 13.33           N
ATOM   1122  NH2 ARG A 139      -8.232  -9.682   7.966  1.00 10.86           N
ATOM   1123  N   LYS A 140      -6.115 -10.354  14.517  1.00 11.17           N
ATOM   1124  CA  LYS A 140      -6.014 -11.237  15.675  1.00 13.35           C
ATOM   1125  C   LYS A 140      -5.418 -10.507  16.869  1.00 14.31           C
ATOM   1126  O   LYS A 140      -5.902 -10.650  18.000  1.00 14.17           O
ATOM   1127  CB  LYS A 140      -5.186 -12.471  15.317  1.00 13.82           C
ATOM   1128  CG  LYS A 140      -5.948 -13.485  14.461  1.00 17.95           C
ATOM   1129  CD  LYS A 140      -5.088 -14.679  14.078  1.00 21.25           C
ATOM   1130  CE  LYS A 140      -5.918 -15.689  13.305  1.00 25.07           C
ATOM   1131  NZ  LYS A 140      -5.155 -16.922  12.959  1.00 34.49           N
ATOM   1132  N   ASP A 141      -4.385  -9.691  16.639  1.00 14.61           N
ATOM   1133  CA  ASP A 141      -3.769  -8.983  17.757  1.00 14.33           C
ATOM   1134  C   ASP A 141      -4.697  -7.902  18.313  1.00 16.21           C
ATOM   1135  O   ASP A 141      -4.773  -7.712  19.533  1.00 16.91           O
ATOM   1136  CB  ASP A 141      -2.427  -8.390  17.328  1.00 16.53           C
ATOM   1137  CG  ASP A 141      -1.334  -9.440  17.197  1.00 17.86           C
ATOM   1138  OD1 ASP A 141      -1.521 -10.574  17.701  1.00 20.70           O
ATOM   1139  OD2 ASP A 141      -0.289  -9.125  16.587  1.00 21.29           O
ATOM   1140  N   ILE A 142      -5.422  -7.194  17.439  1.00 12.44           N
ATOM   1141  CA  ILE A 142      -6.439  -6.246  17.894  1.00 13.60           C
ATOM   1142  C   ILE A 142      -7.518  -6.958  18.700  1.00 15.17           C
ATOM   1143  O   ILE A 142      -7.970  -6.459  19.741  1.00 14.94           O
ATOM   1144  CB  ILE A 142      -7.049  -5.498  16.691  1.00 11.70           C
ATOM   1145  CG1 ILE A 142      -6.062  -4.484  16.130  1.00 15.60           C
ATOM   1146  CG2 ILE A 142      -8.359  -4.810  17.086  1.00 18.32           C
ATOM   1147  CD1 ILE A 142      -5.847  -3.287  17.026  1.00 20.95           C
ATOM   1148  N   ALA A 143      -7.965  -8.122  18.224  1.00 13.00           N
ATOM   1149  CA  ALA A 143      -9.015  -8.862  18.923  1.00 13.53           C
ATOM   1150  C   ALA A 143      -8.583  -9.242  20.335  1.00 15.30           C
ATOM   1151  O   ALA A 143      -9.391  -9.200  21.275  1.00 16.57           O
ATOM   1152  CB  ALA A 143      -9.391 -10.111  18.132  1.00 15.69           C
ATOM   1153  N   ALA A 144      -7.314  -9.622  20.500  1.00 13.90           N
ATOM   1154  CA  ALA A 144      -6.785  -9.887  21.833  1.00 17.83           C
ATOM   1155  C   ALA A 144      -6.877  -8.647  22.721  1.00 20.05           C
ATOM   1156  O   ALA A 144      -7.272  -8.740  23.891  1.00 19.72           O
ATOM   1157  CB  ALA A 144      -5.337 -10.374  21.733  1.00 16.44           C
ATOM   1158  N   LYS A 145      -6.521  -7.475  22.187  1.00 14.31           N
ATOM   1159  CA  LYS A 145      -6.603  -6.261  22.992  1.00 16.28           C
ATOM   1160  C   LYS A 145      -8.050  -5.882  23.291  1.00 17.40           C
ATOM   1161  O   LYS A 145      -8.341  -5.359  24.377  1.00 16.77           O
ATOM   1162  CB  LYS A 145      -5.875  -5.113  22.293  1.00 15.53           C
ATOM   1163  N   TYR A 146      -8.961  -6.138  22.350  1.00 12.97           N
ATOM   1164  CA  TYR A 146     -10.391  -6.021  22.627  1.00 16.56           C
ATOM   1165  C   TYR A 146     -10.782  -6.835  23.853  1.00 20.02           C
ATOM   1166  O   TYR A 146     -11.475  -6.342  24.751  1.00 18.28           O
ATOM   1167  CB  TYR A 146     -11.196  -6.507  21.420  1.00 19.73           C
ATOM   1168  CG  TYR A 146     -11.564  -5.457  20.399  1.00 15.71           C
ATOM   1169  CD1 TYR A 146     -12.845  -5.420  19.860  1.00 18.48           C
ATOM   1170  CD2 TYR A 146     -10.633  -4.518  19.954  1.00 14.98           C
ATOM   1171  CE1 TYR A 146     -13.198  -4.468  18.913  1.00 17.99           C
ATOM   1172  CE2 TYR A 146     -10.981  -3.548  19.000  1.00 13.71           C
ATOM   1173  CZ  TYR A 146     -12.260  -3.534  18.486  1.00 18.62           C
ATOM   1174  OH  TYR A 146     -12.621  -2.585  17.548  1.00 18.85           O
ATOM   1175  N   LYS A 147     -10.374  -8.111  23.879  1.00 15.00           N
ATOM   1176  CA  LYS A 147     -10.700  -8.988  25.001  1.00 17.72           C
ATOM   1177  C   LYS A 147     -10.128  -8.458  26.314  1.00 20.91           C
ATOM   1178  O   LYS A 147     -10.792  -8.520  27.355  1.00 20.19           O
ATOM   1179  CB  LYS A 147     -10.185 -10.400  24.722  1.00 18.57           C
ATOM   1180  CG  LYS A 147     -10.903 -11.105  23.584  1.00 21.43           C
ATOM   1181  CD  LYS A 147     -10.272 -12.467  23.296  1.00 26.83           C
ATOM   1182  CE  LYS A 147     -10.934 -13.137  22.101  1.00 34.73           C
ATOM   1183  NZ  LYS A 147     -10.227 -14.383  21.679  1.00 34.79           N
ATOM   1184  N   GLU A 148      -8.896  -7.936  26.288  1.00 18.07           N
ATOM   1185  CA  GLU A 148      -8.318  -7.348  27.495  1.00 19.11           C
ATOM   1186  C   GLU A 148      -9.136  -6.169  28.002  1.00 22.48           C
ATOM   1187  O   GLU A 148      -9.140  -5.893  29.204  1.00 22.53           O
ATOM   1188  CB  GLU A 148      -6.881  -6.902  27.244  1.00 20.17           C
ATOM   1189  CG  GLU A 148      -5.870  -8.037  27.302  1.00 24.53           C
ATOM   1190  CD  GLU A 148      -4.480  -7.600  26.901  1.00 33.99           C
ATOM   1191  OE1 GLU A 148      -3.707  -8.451  26.409  1.00 45.85           O
ATOM   1192  OE2 GLU A 148      -4.161  -6.405  27.069  1.00 41.08           O
ATOM   1193  N   LEU A 149      -9.823  -5.460  27.115  1.00 19.72           N
ATOM   1194  CA  LEU A 149     -10.676  -4.345  27.513  1.00 17.99           C
ATOM   1195  C   LEU A 149     -12.095  -4.782  27.850  1.00 19.31           C
ATOM   1196  O   LEU A 149     -12.941  -3.931  28.143  1.00 19.65           O
ATOM   1197  CB  LEU A 149     -10.707  -3.287  26.400  1.00 18.74           C
ATOM   1198  CG  LEU A 149      -9.373  -2.594  26.120  1.00 17.72           C
ATOM   1199  CD1 LEU A 149      -9.363  -2.014  24.716  1.00 17.86           C
ATOM   1200  CD2 LEU A 149      -9.112  -1.493  27.143  1.00 17.11           C
ATOM   1201  N   GLY A 150     -12.379  -6.076  27.805  1.00 21.65           N
ATOM   1202  CA  GLY A 150     -13.698  -6.570  28.138  1.00 23.05           C
ATOM   1203  C   GLY A 150     -14.697  -6.548  27.008  1.00 24.86           C
ATOM   1204  O   GLY A 150     -15.903  -6.607  27.266  1.00 25.87           O
ATOM   1205  N   TYR A 151     -14.244  -6.444  25.764  1.00 26.17           N
ATOM   1206  CA  TYR A 151     -15.123  -6.473  24.604  1.00 27.65           C
ATOM   1207  C   TYR A 151     -14.852  -7.740  23.807  1.00 30.59           C
ATOM   1208  O   TYR A 151     -13.694  -8.140  23.630  1.00 28.64           O
ATOM   1209  CB  TYR A 151     -14.930  -5.234  23.725  1.00 27.84           C
ATOM   1210  CG  TYR A 151     -15.387  -3.954  24.387  1.00 26.78           C
ATOM   1211  CD1 TYR A 151     -16.569  -3.325  23.996  1.00 30.02           C
ATOM   1212  CD2 TYR A 151     -14.644  -3.381  25.414  1.00 25.96           C
ATOM   1213  CE1 TYR A 151     -16.995  -2.154  24.605  1.00 29.82           C
ATOM   1214  CE2 TYR A 151     -15.062  -2.213  26.038  1.00 26.26           C
ATOM   1215  CZ  TYR A 151     -16.236  -1.604  25.629  1.00 30.76           C
ATOM   1216  OH  TYR A 151     -16.641  -0.442  26.249  1.00 30.47           O
ATOM   1217  N   GLN A 152     -15.925  -8.387  23.354  1.00 33.94           N
ATOM   1218  CA  GLN A 152     -15.764  -9.578  22.528  1.00 39.44           C
ATOM   1219  C   GLN A 152     -15.203  -9.210  21.163  1.00 37.80           C
ATOM   1220  O   GLN A 152     -14.263  -9.848  20.673  1.00 36.49           O
ATOM   1221  CB  GLN A 152     -17.101 -10.305  22.384  1.00 45.80           C
ATOM   1222  N   GLY A 153     -15.756  -8.168  20.549  1.00 34.30           N
ATOM   1223  CA  GLY A 153     -15.374  -7.752  19.212  1.00 34.56           C
ATOM   1224  C   GLY A 153     -16.362  -8.209  18.156  1.00 35.86           C
ATOM   1225  O   GLY A 153     -17.415  -8.772  18.464  1.00 43.19           O
ATOM   1226  OXT GLY A 153     -16.135  -8.036  16.961  1.00 28.87           O
TER
HETATM 1227  NB  HEM C   1      -8.962   2.477  11.725  1.00 12.67           N
HETATM 1228  ND  HEM C   1     -11.856   5.045  13.065  1.00 12.37           N
HETATM 1229  C1A HEM C   1      -9.199   6.325  13.567  1.00 12.93           C
HETATM 1230  C1B HEM C   1      -7.599   2.676  11.823  1.00  9.87           C
HETATM 1231  C1C HEM C   1     -11.642   1.265  11.095  1.00 12.65           C
HETATM 1232  C1D HEM C   1     -13.216   4.856  12.915  1.00 13.10           C
HETATM 1233  C2A HEM C   1      -7.908   6.838  13.971  1.00 12.11           C
HETATM 1234  C2B HEM C   1      -6.931   1.541  11.221  1.00 10.84           C
HETATM 1235  C2C HEM C   1     -12.935   0.758  10.662  1.00 12.30           C
HETATM 1236  C2D HEM C   1     -13.886   6.087  13.279  1.00 15.16           C
HETATM 1237  C3A HEM C   1      -6.971   5.971  13.569  1.00 12.84           C
HETATM 1238  C3B HEM C   1      -7.880   0.668  10.815  1.00  8.17           C
HETATM 1239  C3C HEM C   1     -13.886   1.598  11.123  1.00 10.30           C
HETATM 1240  C3D HEM C   1     -12.945   6.973  13.644  1.00 13.47           C
HETATM 1241  C4A HEM C   1      -7.630   4.867  12.916  1.00 12.41           C
HETATM 1242  C4B HEM C   1      -9.173   1.260  11.106  1.00  9.02           C
HETATM 1243  C4C HEM C   1     -13.215   2.656  11.855  1.00 10.15           C
HETATM 1244  C4D HEM C   1     -11.648   6.339  13.509  1.00 14.99           C
HETATM 1245  CAA HEM C   1      -7.663   8.157  14.728  1.00 16.12           C
HETATM 1246  CAB HEM C   1      -7.745  -0.693  10.079  1.00 11.80           C
HETATM 1247  CAC HEM C   1     -15.426   1.565  10.973  1.00 10.75           C
HETATM 1248  CAD HEM C   1     -13.178   8.433  14.072  1.00 16.03           C
HETATM 1249  CBA HEM C   1      -7.323   7.850  16.196  1.00 13.89           C
HETATM 1250  CBB HEM C   1      -6.763  -0.920   9.197  1.00 13.72           C
HETATM 1251  CBC HEM C   1     -16.113   0.667  10.254  1.00  9.72           C
HETATM 1252  CBD HEM C   1     -13.252   9.161  12.722  1.00 16.15           C
HETATM 1253  CGA HEM C   1      -8.397   6.996  16.832  1.00 18.18           C
HETATM 1254  CGD HEM C   1     -13.459  10.642  12.887  1.00 22.24           C
HETATM 1255  CHA HEM C   1     -10.426   6.912  13.784  1.00 13.78           C
HETATM 1256  CHB HEM C   1      -6.992   3.776  12.374  1.00  9.99           C
HETATM 1257  CHC HEM C   1     -10.410   0.696  10.831  1.00 13.23           C
HETATM 1258  CHD HEM C   1     -13.836   3.706  12.485  1.00 12.14           C
HETATM 1259  CMA HEM C   1      -5.446   6.079  13.771  1.00 16.28           C
HETATM 1260  CMB HEM C   1      -5.393   1.412  11.158  1.00  8.84           C
HETATM 1261  CMC HEM C   1     -13.108  -0.538   9.832  1.00  9.25           C
HETATM 1262  CMD HEM C   1     -15.414   6.309  13.261  1.00 13.53           C
HETATM 1263  NA  HEM C   1      -8.988   5.113  12.935  1.00 11.49           N
HETATM 1264  NC  HEM C   1     -11.857   2.429  11.815  1.00 11.07           N
HETATM 1265  O1A HEM C   1      -9.547   7.488  16.995  1.00 17.44           O
HETATM 1266  O1D HEM C   1     -12.525  11.320  13.381  1.00 20.50           O
HETATM 1267  O2A HEM C   1      -8.102   5.825  17.193  1.00 18.97           O
HETATM 1268  O2D HEM C   1     -14.550  11.143  12.509  1.00 20.94           O
HETATM 1269 FE   HEM C   1     -10.429   3.714  12.492  1.00 13.64          FE
TER
HETATM 1270  O1  SO4 D   1      11.826 -15.033   8.382  1.00 15.36           O
HETATM 1271  O2  SO4 D   1      11.620 -15.872  10.613  1.00 21.16           O
HETATM 1272  O3  SO4 D   1      13.743 -15.149   9.805  1.00 25.43           O
HETATM 1273  O4  SO4 D   1      12.038 -13.537  10.248  1.00 22.92           O
HETATM 1274  S   SO4 D   1      12.304 -14.894   9.765  1.00 20.45           S
HETATM 1275  O1  SO4 D   2       3.448  -1.602 -10.589  1.00 18.79           O
HETATM 1276  O2  SO4 D   2       1.305  -2.588 -10.867  1.00 20.47           O
HETATM 1277  O3  SO4 D   2       2.293  -2.550  -8.706  1.00 20.06           O
HETATM 1278  O4  SO4 D   2       1.521  -0.492  -9.712  1.00 26.37           O
HETATM 1279  S   SO4 D   2       2.144  -1.800  -9.959  1.00 23.85           S
HETATM 1280  O1  SO4 D   3     -22.523   5.564  -7.531  1.00 31.84           O
HETATM 1281  O2  SO4 D   3     -24.411   6.417  -6.317  1.00 29.45           O
HETATM 1282  O3  SO4 D   3     -22.491   5.565  -5.181  1.00 27.55           O
HETATM 1283  O4  SO4 D   3     -22.359   7.670  -6.430  1.00 22.15           O
HETATM 1284  S   SO4 D   3     -22.942   6.320  -6.354  1.00 32.52           S
HETATM 1285  O1  SO4 D   4       1.588 -19.582   6.353  1.00 35.76           O
HETATM 1286  O2  SO4 D   4      -0.654 -20.382   6.435  1.00 47.38           O
HETATM 1287  O3  SO4 D   4       1.073 -21.587   7.564  1.00 41.96           O
HETATM 1288  O4  SO4 D   4       0.363 -19.484   8.412  1.00 43.94           O
HETATM 1289  S   SO4 D   4       0.592 -20.258   7.189  1.00 48.74           S
TER
HETATM 1290  O   HOH S   1     -10.531   4.887  10.446  1.00 16.18           O
HETATM 1291  O   HOH S   2      -1.884  11.570  -0.507  1.00  9.03           O
HETATM 1292  O   HOH S   3      -6.633 -10.556   5.800  1.00 12.54           O
HETATM 1293  O   HOH S   4       7.762 -18.063   4.085  1.00 12.10           O
HETATM 1294  O   HOH S   5       9.375   3.425   5.260  1.00 10.63           O
HETATM 1295  O   HOH S   6     -18.178  13.532  -6.557  1.00 13.69           O
HETATM 1296  O   HOH S   7       6.393   0.147   2.816  1.00  9.92           O
HETATM 1297  O   HOH S   8      -8.306   8.821   2.045  1.00 12.52           O
HETATM 1298  O   HOH S   9       2.663  -5.713  12.001  1.00 13.96           O
HETATM 1299  O   HOH S  10       4.930  -7.052  -3.247  1.00 10.62           O
HETATM 1300  O   HOH S  11     -13.928  18.280  -1.996  1.00 12.98           O
HETATM 1301  O   HOH S  12     -10.828  -8.401  -1.690  1.00 14.92           O
HETATM 1302  O   HOH S  13       3.269 -11.735  -5.865  1.00 14.54           O
HETATM 1303  O   HOH S  14     -13.351   1.949  -4.391  1.00 15.11           O
HETATM 1304  O   HOH S  15      -9.022   7.208  10.466  1.00 15.33           O
HETATM 1305  O   HOH S  16       7.837   2.418   2.250  1.00 19.14           O
HETATM 1306  O   HOH S  17     -27.728   1.684  12.094  1.00 17.04           O
HETATM 1307  O   HOH S  18       2.863   5.276   7.690  1.00 15.77           O
HETATM 1308  O   HOH S  19     -23.803  -5.304   3.840  1.00 13.23           O
HETATM 1309  O   HOH S  20     -27.243   5.232  -0.768  1.00 15.12           O
HETATM 1310  O   HOH S  21      -5.368  13.218   7.920  1.00 14.58           O
HETATM 1311  O   HOH S  22     -10.652 -11.624  11.984  1.00 19.24           O
HETATM 1312  O   HOH S  23      10.670  -3.537  -1.006  1.00 16.80           O
HETATM 1313  O   HOH S  24     -16.966   9.984  12.163  1.00 16.90           O
HETATM 1314  O   HOH S  25     -10.530   9.718  16.739  1.00 21.53           O
HETATM 1315  O   HOH S  26     -24.896   5.694   6.887  1.00 15.45           O
HETATM 1316  O   HOH S  27      -8.326 -13.483   6.129  1.00 20.47           O
HETATM 1317  O   HOH S  28       3.796  -9.620  -7.094  1.00 17.21           O
HETATM 1318  O   HOH S  29     -18.761   5.201  16.157  1.00 20.29           O
HETATM 1319  O   HOH S  30       0.279  -7.165  11.403  1.00 16.60           O
HETATM 1320  O   HOH S  31       2.775   4.891   5.104  1.00 15.71           O
HETATM 1321  O   HOH S  32      -3.172 -15.888   2.655  1.00 19.00           O
HETATM 1322  O   HOH S  33     -16.639   7.436  16.858  1.00 22.60           O
HETATM 1323  O   HOH S  34      -2.338   3.662  -7.896  1.00 20.15           O
HETATM 1324  O   HOH S  35      -4.338   8.420  -6.910  1.00 22.61           O
HETATM 1325  O   HOH S  36       1.876   3.709  -6.710  1.00 19.37           O
HETATM 1326  O   HOH S  37      16.323 -10.051   2.668  1.00 20.25           O
HETATM 1327  O   HOH S  38     -11.373  14.758   9.184  1.00 25.18           O
HETATM 1328  O   HOH S  39     -16.476 -13.195   9.538  1.00 21.92           O
HETATM 1329  O   HOH S  40       9.949 -11.012  -0.684  1.00 17.43           O
HETATM 1330  O   HOH S  41      12.295  -6.675   5.233  1.00 19.17           O
HETATM 1331  O   HOH S  42     -14.154  -1.377  -7.857  1.00 27.36           O
HETATM 1332  O   HOH S  43       7.686  -0.855  -4.078  1.00 17.66           O
HETATM 1333  O   HOH S  44     -10.368  10.628  13.987  1.00 23.48           O
HETATM 1334  O   HOH S  45     -14.031  20.384   8.844  1.00 23.57           O
HETATM 1335  O   HOH S  46       2.802   7.793   4.235  1.00 21.33           O
HETATM 1336  O   HOH S  47      -5.303   5.563  17.946  1.00 22.46           O
HETATM 1337  O   HOH S  48      -9.798   7.216  -7.059  1.00 21.36           O
HETATM 1338  O   HOH S  49      -9.806  -5.591  -7.827  1.00 17.97           O
HETATM 1339  O   HOH S  50     -13.127  -9.758  -1.597  1.00 24.20           O
HETATM 1340  O   HOH S  51     -15.110  -4.773   1.979  1.00 17.81           O
HETATM 1341  O   HOH S  52      -8.217  11.905  10.831  1.00 19.73           O
HETATM 1342  O   HOH S  53      -2.159   8.092  11.797  1.00 19.09           O
HETATM 1343  O   HOH S  54       9.979  -4.727   0.985  1.00 17.28           O
HETATM 1344  O   HOH S  55       5.472   4.764   7.724  1.00 20.63           O
HETATM 1345  O   HOH S  56      -9.439   9.524  11.746  1.00 17.61           O
HETATM 1346  O   HOH S  57       6.436 -12.173  12.133  1.00 25.21           O
HETATM 1347  O   HOH S  58     -22.927  -0.163  11.889  1.00 18.81           O
HETATM 1348  O   HOH S  59     -17.002  -9.206  15.017  1.00 23.08           O
HETATM 1349  O   HOH S  60      12.611 -11.157  -0.477  1.00 21.60           O
HETATM 1350  O   HOH S  61       5.812   5.844  -2.888  1.00 19.39           O
HETATM 1351  O   HOH S  62     -22.647   2.368  16.920  1.00 31.42           O
HETATM 1352  O   HOH S  63      -7.010 -13.077  18.790  1.00 21.84           O
HETATM 1353  O   HOH S  64     -14.665 -11.374  -0.108  1.00 18.08           O
HETATM 1354  O   HOH S  65     -22.848   2.906   0.659  1.00 22.89           O
HETATM 1355  O   HOH S  66       2.193 -10.149  16.769  1.00 25.67           O
HETATM 1356  O   HOH S  67     -11.082  19.690   5.194  1.00 20.69           O
HETATM 1357  O   HOH S  68       9.532 -12.217  10.503  1.00 31.39           O
HETATM 1358  O   HOH S  69       6.137  -8.276  -5.537  1.00 24.03           O
HETATM 1359  O   HOH S  70     -17.602   9.109  14.692  1.00 22.42           O
HETATM 1360  O   HOH S  71       0.151 -13.092  17.291  1.00 28.71           O
HETATM 1361  O   HOH S  72      -6.872   5.003  22.740  1.00 27.13           O
HETATM 1362  O   HOH S  73     -30.303   8.375   6.750  1.00 28.73           O
HETATM 1363  O   HOH S  74      -1.442  10.741  10.039  1.00 26.39           O
HETATM 1364  O   HOH S  75      -2.726  12.694   8.468  1.00 26.10           O
HETATM 1365  O   HOH S  76     -15.916  15.363  -6.376  1.00 26.21           O
HETATM 1366  O   HOH S  77     -16.220  -1.015  -5.725  1.00 39.06           O
HETATM 1367  O   HOH S  78       2.727 -20.406   8.948  1.00 39.88           O
HETATM 1368  O   HOH S  79     -16.685  11.532  15.990  1.00 35.93           O
HETATM 1369  O   HOH S  80      -6.830   8.505  -7.223  1.00 25.49           O
HETATM 1370  O   HOH S  81      13.448  -7.008  -0.061  1.00 24.76           O
HETATM 1371  O   HOH S  82     -18.050  16.675   7.772  1.00 35.44           O
HETATM 1372  O   HOH S  83      -8.957  14.604  10.690  1.00 32.18           O
HETATM 1373  O   HOH S  84     -23.398  12.865   9.494  1.00 28.64           O
HETATM 1374  O   HOH S  85      -9.524 -13.747  10.266  1.00 22.46           O
HETATM 1375  O   HOH S  86      -5.959  15.086   9.757  1.00 25.40           O
HETATM 1376  O   HOH S  87     -28.191   5.866  11.962  1.00 33.27           O
HETATM 1377  O   HOH S  88      -8.047 -13.365  21.255  1.00 29.22           O
HETATM 1378  O   HOH S  89      -8.235  12.520  13.635  1.00 31.60           O
HETATM 1379  O   HOH S  90     -24.383   3.551   2.277  1.00 29.38           O
HETATM 1380  O   HOH S  91      -3.732  12.180  11.270  1.00 26.44           O
HETATM 1381  O   HOH S  92     -16.904   2.108  -7.216  1.00 31.66           O
HETATM 1382  O   HOH S  93      -6.083  -6.554 -11.311  1.00 25.88           O
HETATM 1383  O   HOH S  94       6.576 -10.041  16.466  1.00 42.49           O
HETATM 1384  O   HOH S  95     -28.804  10.381   5.233  1.00 29.08           O
HETATM 1385  O   HOH S  96     -20.274   7.941  -8.669  1.00 27.68           O
HETATM 1386  O   HOH S  97      -0.639 -17.145   2.485  1.00 25.87           O
HETATM 1387  O   HOH S  98       2.909 -17.643  16.273  1.00 41.82           O
HETATM 1388  O   HOH S  99      -0.315   5.411  -7.590  1.00 27.51           O
HETATM 1389  O   HOH S 100      -0.232   7.423  12.728  1.00 30.52           O
HETATM 1390  O   HOH S 101       2.517   1.857 -10.475  1.00 34.29           O
HETATM 1391  O   HOH S 102     -16.919  16.925   9.209  1.00 34.34           O
HETATM 1392  O   HOH S 103     -16.043   0.818  -4.675  1.00 29.09           O
HETATM 1393  O   HOH S 104      14.491 -17.831   9.748  1.00 28.84           O
HETATM 1394  O   HOH S 105       0.504   3.104  14.018  1.00 23.38           O
HETATM 1395  O   HOH S 106      -1.019   7.269  -6.873  1.00 34.47           O
HETATM 1396  O   HOH S 107     -11.783  -0.062  -5.965  1.00 30.00           O
HETATM 1397  O   HOH S 108     -13.068   3.909  -6.289  1.00 30.61           O
HETATM 1398  O   HOH S 109     -12.982   6.081  -5.312  1.00 32.50           O
HETATM 1399  O   HOH S 110       6.469   7.580   8.783  1.00 27.11           O
HETATM 1400  O   HOH S 111      -7.712 -15.938   5.366  1.00 29.09           O
HETATM 1401  O   HOH S 112     -11.964  13.262  -4.344  1.00 28.07           O
HETATM 1402  O   HOH S 113     -22.444  -2.461  16.532  1.00 39.25           O
HETATM 1403  O   HOH S 114     -17.083  -4.464  20.064  1.00 34.28           O
HETATM 1404  O   HOH S 115       9.450  -8.596  -2.400  1.00 31.23           O
HETATM 1405  O   HOH S 116      -6.486 -11.121  25.312  1.00 28.12           O
HETATM 1406  O   HOH S 117      -9.373   1.204  -6.860  1.00 27.53           O
HETATM 1407  O   HOH S 118     -18.908   9.665  -8.364  1.00 29.48           O
HETATM 1408  O   HOH S 119      -3.077   5.015  16.303  1.00 28.96           O
HETATM 1409  O   HOH S 120      -8.282  10.219  -7.283  1.00 35.60           O
HETATM 1410  O   HOH S 121     -18.847  -3.775  19.081  1.00 37.33           O
HETATM 1411  O   HOH S 122     -25.181   0.361  12.614  1.00 34.12           O
HETATM 1412  O   HOH S 123     -16.375  17.775  -5.148  1.00 30.54           O
HETATM 1413  O   HOH S 124     -13.128  10.660  17.449  1.00 32.72           O
HETATM 1414  O   HOH S 125       5.614 -18.361   5.569  1.00 30.53           O
HETATM 1415  O   HOH S 126     -17.424  -2.353  20.622  1.00 32.25           O
HETATM 1416  O   HOH S 127     -16.362 -15.111  11.095  1.00 35.37           O
HETATM 1417  O   HOH S 128     -23.971  -0.339  -1.742  1.00 33.23           O
HETATM 1418  O   HOH S 129     -14.772 -13.403  12.864  1.00 30.92           O
HETATM 1419  O   HOH S 130      10.967 -10.471   9.774  1.00 35.67           O
HETATM 1420  O   HOH S 131      -9.856 -12.480  13.909  1.00 38.10           O
HETATM 1421  O   HOH S 132     -28.293   3.725  14.364  1.00 35.49           O
HETATM 1422  O   HOH S 133       2.302  -9.603 -10.826  1.00 39.69           O
HETATM 1423  O   HOH S 134     -26.122   4.979  -5.851  1.00 42.77           O
HETATM 1424  O   HOH S 135     -24.144  -3.906  12.288  1.00 42.73           O
HETATM 1425  O   HOH S 136      18.288  -9.326   4.315  1.00 34.77           O
HETATM 1426  O   HOH S 137       1.992   7.303  12.569  1.00 37.15           O
HETATM 1427  O   HOH S 138     -27.726  10.881   8.083  1.00 33.56           O
HETATM 1428  O   HOH S 139       3.205 -20.028  14.617  1.00 41.79           O
HETATM 1429  O   HOH S 140       4.536 -10.205  -9.335  1.00 40.61           O
HETATM 1430  O   HOH S 141     -11.843 -14.724   9.468  1.00 42.66           O
HETATM 1431  O   HOH S 142     -25.117   3.330  15.906  1.00 42.45           O
TER
END


A second structure was input as follows:


REMARK Date 2020-12-03 Time 11:32:54 EST -0500 (1607013174.51 s)
REMARK PHENIX refinement
REMARK 
REMARK ****************** INPUT FILES AND LABELS ******************************
REMARK Reflections:
REMARK   file name      : /Users/johnbacik/Desktop/SSRL_9_2_20201113/local_processing/A2_t2/A2_t2_aimless117.mtz
REMARK   labels         : ['IMEAN_XDSdataset,SIGIMEAN_XDSdataset']
REMARK R-free flags:
REMARK   file name      : /Users/johnbacik/Desktop/SSRL_9_2_20201113/local_processing/A2_t2/A2_t2_aimless117.mtz
REMARK   label          : FreeR_flag
REMARK   test_flag_value: 0
REMARK Model file name(s): 
REMARK   /Users/johnbacik/Desktop/SSRL_9_2_20201113/local_processing/A2_t2/A2_t2_refine_8-coot-1.pdb
REMARK 
REMARK ******************** REFINEMENT SUMMARY: QUICK FACTS *******************
REMARK Start: r_work = 0.1474 r_free = 0.1726 bonds = 0.011 angles = 1.194
REMARK Final: r_work = 0.1469 r_free = 0.1721 bonds = 0.011 angles = 1.194
REMARK ************************************************************************
REMARK 
REMARK ****************** REFINEMENT STATISTICS STEP BY STEP ******************
REMARK leading digit, like 1_, means number of macro-cycle                     
REMARK 0    : statistics at the very beginning when nothing is done yet        
REMARK 1_bss: bulk solvent correction and/or (anisotropic) scaling             
REMARK 1_adp: refinement of ADPs (Atomic Displacement Parameters)              
REMARK 1_occ: refinement of occupancies                                        
REMARK ------------------------------------------------------------------------
REMARK  stage       r-work r-free bonds angles b_min b_max b_ave n_water shift
REMARK       0    : 0.2427 0.2278 0.011  1.19   9.9  71.2  18.2 111      0.000
REMARK       1_bss: 0.1474 0.1726 0.011  1.19   9.9  71.2  18.2 111      0.000
REMARK 1_settarget: 0.1474 0.1726 0.011  1.19   9.9  71.2  18.2 111      0.000
REMARK    1_weight: 0.1474 0.1726 0.011  1.19   9.9  71.2  18.2 111      0.000
REMARK       1_adp: 0.1498 0.1816 0.011  1.19   9.4  71.8  18.3 111      0.000
REMARK       1_occ: 0.1498 0.1817 0.011  1.19   9.4  71.8  18.3 111      0.000
REMARK       2_bss: 0.1496 0.1821 0.011  1.19   9.4  71.8  18.3 111      0.000
REMARK 2_settarget: 0.1496 0.1821 0.011  1.19   9.4  71.8  18.3 111      0.000
REMARK    2_weight: 0.1496 0.1821 0.011  1.19   9.4  71.8  18.3 111      0.000
REMARK       2_adp: 0.1471 0.1731 0.011  1.19   9.7  71.6  18.2 111      0.000
REMARK       2_occ: 0.1471 0.1729 0.011  1.19   9.7  71.6  18.2 111      0.000
REMARK       3_bss: 0.1468 0.1723 0.011  1.19   9.7  71.6  18.2 111      0.000
REMARK 3_settarget: 0.1468 0.1723 0.011  1.19   9.7  71.6  18.2 111      0.000
REMARK    3_weight: 0.1468 0.1723 0.011  1.19   9.7  71.6  18.2 111      0.000
REMARK       3_adp: 0.1469 0.1722 0.011  1.19   9.7  71.5  18.0 111      0.000
REMARK       3_occ: 0.1469 0.1722 0.011  1.19   9.7  71.5  18.0 111      0.000
REMARK         end: 0.1469 0.1721 0.011  1.19   9.7  71.5  18.0 111      0.000
REMARK ------------------------------------------------------------------------
REMARK MODEL CONTENT.
REMARK  ELEMENT        ATOM RECORD COUNT   OCCUPANCY SUM
REMARK        S                        9            9.00
REMARK        C                      835          820.00
REMARK       Fe                        1            1.00
REMARK        O                      352          351.00
REMARK        N                      222          219.00
REMARK    TOTAL                     1419         1400.00

REMARK -----------------------------------------------------------------------
REMARK r_free_flags.md5.hexdigest 05d565b6dcd239209ff13f3aaf07814b
REMARK 
REMARK IF THIS FILE IS FOR PDB DEPOSITION: REMOVE ALL FROM THIS LINE UP.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : PHENIX (1.13_2998: ???)
REMARK   3   AUTHORS     : Adams,Afonine,Bunkoczi,Burnley,Chen,Dar,Davis,
REMARK   3               : Draizen,Echols,Gildea,Gros,Grosse-Kunstleve,Headd,
REMARK   3               : Hintze,Hung,Ioerger,Liebschner,McCoy,McKee,Moriarty,
REMARK   3               : Oeffner,Poon,Read,Richardson,Richardson,Sacchettini,
REMARK   3               : Sauter,Sobolev,Storoni,Terwilliger,Williams,Zwart
REMARK   3
REMARK   3  X-RAY DATA.
REMARK   3  
REMARK   3  REFINEMENT TARGET : ML
REMARK   3  
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.170   
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 35.655  
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.34  
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.69 
REMARK   3   NUMBER OF REFLECTIONS             : 52931     
REMARK   3   NUMBER OF REFLECTIONS (NON-ANOMALOUS) : 52931     
REMARK   3  
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.1482
REMARK   3   R VALUE            (WORKING SET) : 0.1469
REMARK   3   FREE R VALUE                     : 0.1721
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.93  
REMARK   3   FREE R VALUE TEST SET COUNT      : 2607      
REMARK   3  
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE  CCWORK CCFREE
REMARK   3     1 35.6713 -  3.1214    1.00     2859   175  0.1679 0.2005   0.934  0.919
REMARK   3     2  3.1214 -  2.4777    1.00     2730   149  0.1645 0.1744   0.931  0.921
REMARK   3     3  2.4777 -  2.1646    1.00     2709   148  0.1450 0.1455   0.948  0.948
REMARK   3     4  2.1646 -  1.9667    1.00     2685   165  0.1320 0.1635   0.955  0.934
REMARK   3     5  1.9667 -  1.8257    1.00     2677   139  0.1352 0.1477   0.953  0.943
REMARK   3     6  1.8257 -  1.7181    1.00     2705   122  0.1318 0.1599   0.957  0.935
REMARK   3     7  1.7181 -  1.6320    1.00     2641   145  0.1192 0.1477   0.963  0.944
REMARK   3     8  1.6320 -  1.5610    0.99     2672   142  0.1107 0.1369   0.970  0.960
REMARK   3     9  1.5610 -  1.5009    1.00     2648   146  0.1085 0.1593   0.970  0.957
REMARK   3    10  1.5009 -  1.4491    1.00     2695   114  0.1070 0.1183   0.970  0.962
REMARK   3    11  1.4491 -  1.4038    1.00     2655   124  0.1144 0.1569   0.965  0.924
REMARK   3    12  1.4038 -  1.3637    1.00     2680   126  0.1240 0.1593   0.958  0.936
REMARK   3    13  1.3637 -  1.3278    0.99     2610   116  0.1291 0.1928   0.956  0.905
REMARK   3    14  1.3278 -  1.2954    1.00     2674   153  0.1344 0.1843   0.950  0.926
REMARK   3    15  1.2954 -  1.2659    1.00     2659   123  0.1426 0.1624   0.946  0.940
REMARK   3    16  1.2659 -  1.2390    1.00     2634   145  0.1573 0.1606   0.932  0.922
REMARK   3    17  1.2390 -  1.2142    1.00     2628   129  0.1666 0.2217   0.922  0.874
REMARK   3    18  1.2142 -  1.1913    0.93     2466   124  0.1967 0.2615   0.889  0.813
REMARK   3    19  1.1913 -  1.1700    0.87     2297   122  0.2202 0.2434   0.845  0.806
REMARK   3  
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL
REMARK   3   SOLVENT RADIUS     : 1.11    
REMARK   3   SHRINKAGE RADIUS   : 0.90    
REMARK   3   GRID STEP FACTOR   : 4.00    
REMARK   3  
REMARK   3  ERROR ESTIMATES.
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.08    
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 15.63   
REMARK   3  
REMARK   3  STRUCTURE FACTORS CALCULATION ALGORITHM : FFT
REMARK   3  
REMARK   3  
REMARK   3  DEVIATIONS FROM IDEAL VALUES.
REMARK   3    BOND      :  0.011   0.067   1339
REMARK   3    ANGLE     :  1.194   7.963   1817
REMARK   3    CHIRALITY :  0.075   0.244    188
REMARK   3    PLANARITY :  0.009   0.057    218
REMARK   3    DIHEDRAL  : 26.176 179.950    485
REMARK   3    MIN NONBONDED DISTANCE : 2.206 
REMARK   3  REMARK   3  
REMARK   3  MOLPROBITY STATISTICS.
REMARK   3    ALL-ATOM CLASHSCORE : 1.53
REMARK   3    RAMACHANDRAN PLOT:
REMARK   3      OUTLIERS : 0.00  %
REMARK   3      ALLOWED  : 2.72  %
REMARK   3      FAVORED  : 97.28 %
REMARK   3    ROTAMER OUTLIERS : 0.00 %
REMARK   3    CBETA DEVIATIONS : 0
REMARK   3    PEPTIDE PLANE:
REMARK   3      CIS-PROLINE     : 0.0
REMARK   3      CIS-GENERAL     : 0.0
REMARK   3      TWISTED PROLINE : 0.0
REMARK   3      TWISTED GENERAL : 0.0
REMARK   3  
REMARK   3  ATOMIC DISPLACEMENT PARAMETERS.
REMARK   3   WILSON B : 13.08
REMARK   3   RMS(B_ISO_OR_EQUIVALENT_BONDED) : 1.46
REMARK   3   ATOMS          NUMBER OF ATOMS
REMARK   3                    ISO.  ANISO. 
REMARK   3    ALL         :      3    1416
REMARK   3    ALL (NO H)  :      3    1416
REMARK   3    SOLVENT     :      3     108
REMARK   3    NON-SOLVENT :      0    1308
REMARK   3    HYDROGENS   :      0       0
REMARK   3  
REMARK   3
LINK        FE   HEM C   1                 NE2 HIS A  93 
LINK        FE   HEM C   1                 O2  OXY C 101 
LINK         C2  PYZ A   5                 SG  CYS A 126 
CRYST1   42.408   55.985   65.855  90.00  90.00  90.00 P 21 21 21
SCALE1      0.023580  0.000000  0.000000        0.00000
SCALE2      0.000000  0.017862  0.000000        0.00000
SCALE3      0.000000  0.000000  0.015185        0.00000
ATOM      1  N   MET A   0     -31.977  -8.393   5.800  1.00 32.18           N
ANISOU    1  N   MET A   0     3998   4360   3869   -159   -525    702       N
ATOM      2  CA  MET A   0     -31.487  -9.383   6.752  1.00 31.04           C
ANISOU    2  CA  MET A   0     3732   4260   3802   -183   -513    637       C
ATOM      3  C   MET A   0     -31.475  -8.790   8.150  1.00 29.52           C
ANISOU    3  C   MET A   0     3381   4123   3712   -175   -574    718       C
ATOM      4  O   MET A   0     -31.493  -7.567   8.331  1.00 29.36           O
ANISOU    4  O   MET A   0     3244   4177   3734    -49   -740    925       O
ATOM      5  CB  MET A   0     -30.074  -9.841   6.386  1.00 30.74           C
ANISOU    5  CB  MET A   0     3822   4121   3738   -258   -449    540       C
ATOM      6  CG  MET A   0     -29.056  -8.761   6.594  1.00 28.97           C
ANISOU    6  CG  MET A   0     3615   3813   3578   -469   -434    409       C
ATOM      7  SD  MET A   0     -27.394  -9.169   6.066  1.00 26.72           S
ANISOU    7  SD  MET A   0     3350   3461   3344   -554   -474    334       S
ATOM      8  CE  MET A   0     -26.849 -10.286   7.357  1.00 27.27           C
ANISOU    8  CE  MET A   0     3477   3613   3273   -480   -714    382       C
ATOM      9  N   VAL A   1     -31.453  -9.671   9.144  1.00 27.64           N
ANISOU    9  N   VAL A   1     3166   3832   3505   -208   -550    642       N
ATOM     10  CA  VAL A   1     -31.410  -9.274  10.545  1.00 25.47           C
ANISOU   10  CA  VAL A   1     2951   3448   3278    -47   -461    556       C
ATOM     11  C   VAL A   1     -30.418 -10.179  11.265  1.00 23.16           C
ANISOU   11  C   VAL A   1     2870   2958   2971     80   -538    323       C
ATOM     12  O   VAL A   1     -30.193 -11.328  10.869  1.00 25.62           O
ANISOU   12  O   VAL A   1     3610   3105   3020    115   -757      3       O
ATOM     13  CB  VAL A   1     -32.790  -9.352  11.228  1.00 27.02           C
ANISOU   13  CB  VAL A   1     3136   3599   3533     12   -288    593       C
ATOM     14  CG1 VAL A   1     -33.788  -8.430  10.550  1.00 27.89           C
ANISOU   14  CG1 VAL A   1     3265   3706   3626    106   -218    596       C
ATOM     15  CG2 VAL A   1     -33.275 -10.790  11.245  1.00 27.80           C
ANISOU   15  CG2 VAL A   1     3267   3675   3620    -78   -150    533       C
ATOM     16  N   LEU A   2     -29.797  -9.658  12.313  1.00 18.59           N
ANISOU   16  N   LEU A   2     1923   2549   2591    -73   -350    365       N
ATOM     17  CA  LEU A   2     -29.002 -10.485  13.207  1.00 16.61           C
ANISOU   17  CA  LEU A   2     1773   2150   2387   -115    -29    240       C
ATOM     18  C   LEU A   2     -29.864 -10.848  14.410  1.00 16.18           C
ANISOU   18  C   LEU A   2     1594   2124   2429   -135     95    217       C
ATOM     19  O   LEU A   2     -30.721 -10.073  14.826  1.00 17.57           O
ANISOU   19  O   LEU A   2     1873   2272   2530    -25    181    346       O
ATOM     20  CB  LEU A   2     -27.743  -9.748  13.694  1.00 15.27           C
ANISOU   20  CB  LEU A   2     1701   1880   2221   -210    192    117       C
ATOM     21  CG  LEU A   2     -26.521  -9.785  12.751  1.00 15.14           C
ANISOU   21  CG  LEU A   2     1837   1819   2096   -170    172    139       C
ATOM     22  CD1 LEU A   2     -26.796  -8.988  11.465  1.00 16.75           C
ANISOU   22  CD1 LEU A   2     2222   2082   2058    -65    285    182       C
ATOM     23  CD2 LEU A   2     -25.300  -9.226  13.444  1.00 15.55           C
ANISOU   23  CD2 LEU A   2     1941   1777   2192   -267    138      3       C
ATOM     24  N   SER A   3     -29.623 -12.022  14.972  1.00 15.32           N
ANISOU   24  N   SER A   3     1492   1901   2430   -274     28    194       N
ATOM     25  CA  SER A   3     -30.259 -12.370  16.229  1.00 15.87           C
ANISOU   25  CA  SER A   3     1651   1805   2574   -283     36    239       C
ATOM     26  C   SER A   3     -29.601 -11.616  17.393  1.00 15.19           C
ANISOU   26  C   SER A   3     1590   1718   2463    -41    222    199       C
ATOM     27  O   SER A   3     -28.481 -11.085  17.292  1.00 14.50           O
ANISOU   27  O   SER A   3     1567   1612   2331   -176    232    157       O
ATOM     28  CB  SER A   3     -30.134 -13.884  16.457  1.00 16.44           C
ANISOU   28  CB  SER A   3     1765   1797   2684   -292    -50    157       C
ATOM     29  OG  SER A   3     -28.770 -14.220  16.703  1.00 16.38           O
ANISOU   29  OG  SER A   3     1842   1669   2713   -380    -68     27       O
ATOM     30  N   GLU A   4     -30.306 -11.579  18.522  1.00 15.42           N
ANISOU   30  N   GLU A   4     1550   1800   2511    -51    334    217       N
ATOM     31  CA  GLU A   4     -29.707 -11.013  19.724  1.00 16.09           C
ANISOU   31  CA  GLU A   4     1787   1888   2440    104    514    135       C
ATOM     32  C   GLU A   4     -28.398 -11.688  20.098  1.00 14.62           C
ANISOU   32  C   GLU A   4     1794   1606   2156    -34    409    228       C
ATOM     33  O   GLU A   4     -27.466 -11.020  20.478  1.00 14.58           O
ANISOU   33  O   GLU A   4     1918   1612   2010   -242    393    132       O
ATOM     34  CB  GLU A   4     -30.701 -11.043  20.891  1.00 20.18           C
ANISOU   34  CB  GLU A   4     2454   2353   2862    164    572     12       C
ATOM     35  CG  GLU A   4     -30.209 -10.336  22.148  1.00 25.38           C
ANISOU   35  CG  GLU A   4     3426   2823   3396    209    432    -63       C
ATOM     36  CD  GLU A   4     -29.816  -8.878  21.913  1.00 29.68           C
ANISOU   36  CD  GLU A   4     4268   3183   3825    114    176    -98       C
ATOM     37  OE1 GLU A   4     -30.453  -8.172  21.085  1.00 30.57           O
ANISOU   37  OE1 GLU A   4     4504   3212   3900    218    223   -113       O
ATOM     38  OE2 GLU A   4     -28.836  -8.450  22.558  1.00 31.79           O
ANISOU   38  OE2 GLU A   4     4663   3353   4064    -58    -33    -37       O
HETATM   39  N   PYZ A   5     -28.333 -13.013  19.979  1.00 13.25           N
ANISOU   39  N   PYZ A   5     1563   1392   2077     47    392    294       N
HETATM   40  CA  PYZ A   5     -27.084 -13.737  20.268  1.00 13.12           C
ANISOU   40  CA  PYZ A   5     1671   1299   2014   -140    386    259       C
HETATM   41  C   PYZ A   5     -25.970 -13.261  19.329  1.00 12.49           C
ANISOU   41  C   PYZ A   5     1709   1281   1757   -254    244    189       C
HETATM   42  O   PYZ A   5     -24.849 -13.030  19.770  1.00 12.73           O
ANISOU   42  O   PYZ A   5     1749   1343   1743   -286    159    263       O
HETATM   43  CB  PYZ A   5     -27.379 -15.248  20.055  1.00 13.74           C
ANISOU   43  CB  PYZ A   5     1874   1258   2087     -6    305    238       C
HETATM   44  CG  PYZ A   5     -26.191 -16.143  20.028  1.00 13.19           C
ANISOU   44  CG  PYZ A   5     1873   1262   1877   -153    299    319       C
HETATM   45  CD1 PYZ A   5     -25.176 -16.082  21.008  1.00 13.71           C
ANISOU   45  CD1 PYZ A   5     2100   1412   1698   -166    315    276       C
HETATM   46  CD2 PYZ A   5     -26.065 -17.105  19.033  1.00 13.42           C
ANISOU   46  CD2 PYZ A   5     1757   1413   1928   -299    326    148       C
HETATM   47  CE1 PYZ A   5     -24.079 -16.924  20.976  1.00 13.00           C
ANISOU   47  CE1 PYZ A   5     2008   1342   1588   -192    334    266       C
HETATM   48  CE2 PYZ A   5     -24.958 -17.967  18.992  1.00 13.99           C
ANISOU   48  CE2 PYZ A   5     1877   1529   1907   -303    253     57       C
HETATM   49  CZ  PYZ A   5     -23.960 -17.892  19.982  1.00 13.31           C
ANISOU   49  CZ  PYZ A   5     1840   1411   1806   -316    274     98       C
HETATM   50  NZ  PYZ A   5     -22.800 -18.709  19.991  1.00 13.43           N
ANISOU   50  NZ  PYZ A   5     1717   1390   1994   -335    317     17       N
HETATM   51  OZ  PYZ A   5     -22.976 -19.708  17.932  1.00 14.16           O
ANISOU   51  OZ  PYZ A   5     2004   1472   1902   -100     97    -30       O
HETATM   52  C1  PYZ A   5     -22.362 -19.503  18.987  1.00 13.56           C
ANISOU   52  C1  PYZ A   5     1817   1420   1915   -270    245    188       C
HETATM   53  C2  PYZ A   5     -21.041 -20.217  19.236  1.00 14.03           C
ANISOU   53  C2  PYZ A   5     1827   1499   2003   -188    231    271       C
ATOM     54  N   GLU A   6     -26.260 -13.130  18.033  1.00 12.39           N
ANISOU   54  N   GLU A   6     1641   1356   1710   -208    287    226       N
ATOM     55  CA  GLU A   6     -25.244 -12.601  17.125  1.00 12.42           C
ANISOU   55  CA  GLU A   6     1720   1375   1625   -273    147     72       C
ATOM     56  C   GLU A   6     -24.818 -11.184  17.517  1.00 11.67           C
ANISOU   56  C   GLU A   6     1461   1391   1583   -206    151    167       C
ATOM     57  O   GLU A   6     -23.613 -10.892  17.510  1.00 11.76           O
ANISOU   57  O   GLU A   6     1439   1426   1605   -205     67    103       O
ATOM     58  CB  GLU A   6     -25.779 -12.634  15.685  1.00 13.42           C
ANISOU   58  CB  GLU A   6     1848   1482   1769    -63    -33     19       C
ATOM     59  CG  GLU A   6     -25.806 -14.056  15.148  1.00 14.42           C
ANISOU   59  CG  GLU A   6     1958   1552   1970    -92     18    -88       C
ATOM     60  CD  GLU A   6     -26.614 -14.268  13.873  1.00 15.36           C
ANISOU   60  CD  GLU A   6     1966   1740   2131      6    -68   -252       C
ATOM     61  OE1 GLU A   6     -26.298 -15.224  13.109  1.00 17.09           O
ANISOU   61  OE1 GLU A   6     2446   1980   2069   -134    -76   -316       O
ATOM     62  OE2 GLU A   6     -27.520 -13.455  13.598  1.00 16.28           O
ANISOU   62  OE2 GLU A   6     1947   1980   2258     23   -114   -271       O
ATOM     63  N   TRP A   7     -25.750 -10.317  17.908  1.00 11.81           N
ANISOU   63  N   TRP A   7     1497   1357   1634   -143    189      1       N
ATOM     64  CA  TRP A   7     -25.343  -8.985  18.348  1.00 12.25           C
ANISOU   64  CA  TRP A   7     1619   1342   1692   -114     82     32       C
ATOM     65  C   TRP A   7     -24.465  -9.054  19.589  1.00 12.16           C
ANISOU   65  C   TRP A   7     1697   1411   1514   -139    219     34       C
ATOM     66  O   TRP A   7     -23.529  -8.264  19.732  1.00 12.83           O
ANISOU   66  O   TRP A   7     1868   1368   1640   -240    136     35       O
ATOM     67  CB  TRP A   7     -26.519  -8.049  18.587  1.00 12.77           C
ANISOU   67  CB  TRP A   7     1531   1447   1872    -80    176    196       C
ATOM     68  CG  TRP A   7     -27.155  -7.572  17.323  1.00 12.84           C
ANISOU   68  CG  TRP A   7     1506   1438   1936    -77    185    158       C
ATOM     69  CD1 TRP A   7     -28.438  -7.779  16.906  1.00 13.62           C
ANISOU   69  CD1 TRP A   7     1605   1526   2042    -99    -72    195       C
ATOM     70  CD2 TRP A   7     -26.540  -6.768  16.295  1.00 12.81           C
ANISOU   70  CD2 TRP A   7     1509   1372   1986    -25     69    184       C
ATOM     71  NE1 TRP A   7     -28.669  -7.170  15.710  1.00 14.03           N
ANISOU   71  NE1 TRP A   7     1608   1562   2161   -122    -71    186       N
ATOM     72  CE2 TRP A   7     -27.515  -6.557  15.292  1.00 13.41           C
ANISOU   72  CE2 TRP A   7     1527   1488   2080    -36     79    124       C
ATOM     73  CE3 TRP A   7     -25.266  -6.203  16.132  1.00 13.50           C
ANISOU   73  CE3 TRP A   7     1700   1397   2032   -109    207    252       C
ATOM     74  CZ2 TRP A   7     -27.255  -5.812  14.142  1.00 14.29           C
ANISOU   74  CZ2 TRP A   7     1763   1576   2089     49    140    183       C
ATOM     75  CZ3 TRP A   7     -25.017  -5.463  14.999  1.00 13.89           C
ANISOU   75  CZ3 TRP A   7     1810   1497   1968    -88    178    324       C
ATOM     76  CH2 TRP A   7     -26.003  -5.289  14.000  1.00 14.55           C
ANISOU   76  CH2 TRP A   7     1966   1582   1982    -22     91    233       C
ATOM     77  N   GLN A   8     -24.778  -9.974  20.504  1.00 12.71           N
ANISOU   77  N   GLN A   8     1898   1431   1500   -108    297    129       N
ATOM     78  CA  GLN A   8     -23.960 -10.110  21.737  1.00 13.90           C
ANISOU   78  CA  GLN A   8     2098   1612   1572   -299    332    163       C
ATOM     79  C   GLN A   8     -22.522 -10.436  21.336  1.00 12.90           C
ANISOU   79  C   GLN A   8     2046   1442   1413   -297    216    280       C
ATOM     80  O   GLN A   8     -21.600  -9.825  21.888  1.00 13.84           O
ANISOU   80  O   GLN A   8     2126   1616   1518   -356    -20    295       O
ATOM     81  CB  GLN A   8     -24.482 -11.250  22.613  1.00 16.49           C
ANISOU   81  CB  GLN A   8     2418   2027   1821   -231    585    108       C
ATOM     82  CG  GLN A   8     -25.748 -10.909  23.376  1.00 19.72           C
ANISOU   82  CG  GLN A   8     3040   2416   2037   -346    706    193       C
ATOM     83  CD  GLN A   8     -26.270 -12.125  24.101  1.00 23.64           C
ANISOU   83  CD  GLN A   8     3834   2748   2402   -531    835    157       C
ATOM     84  OE1 GLN A   8     -26.538 -13.166  23.507  1.00 25.91           O
ANISOU   84  OE1 GLN A   8     4394   2816   2633   -568    771    143       O
ATOM     85  NE2 GLN A   8     -26.409 -12.001  25.405  1.00 25.85           N
ANISOU   85  NE2 GLN A   8     4309   2989   2524   -452    747    282       N
ATOM     86  N   LEU A   9     -22.355 -11.381  20.415  1.00 12.53           N
ANISOU   86  N   LEU A   9     1840   1494   1429   -195    179    292       N
ATOM     87  CA  LEU A   9     -21.009 -11.747  19.992  1.00 12.92           C
ANISOU   87  CA  LEU A   9     1834   1556   1519   -226    129    355       C
ATOM     88  C   LEU A   9     -20.294 -10.553  19.372  1.00 12.44           C
ANISOU   88  C   LEU A   9     1672   1632   1423   -324    -70    279       C
ATOM     89  O   LEU A   9     -19.102 -10.316  19.646  1.00 13.35           O
ANISOU   89  O   LEU A   9     1807   1806   1458   -314    -89    258       O
ATOM     90  CB  LEU A   9     -21.091 -12.902  18.994  1.00 13.35           C
ANISOU   90  CB  LEU A   9     1972   1460   1639   -219    229    430       C
ATOM     91  CG  LEU A   9     -21.495 -14.238  19.607  1.00 14.45           C
ANISOU   91  CG  LEU A   9     2105   1566   1820     35    204    431       C
ATOM     92  CD1 LEU A   9     -21.955 -15.161  18.453  1.00 15.11           C
ANISOU   92  CD1 LEU A   9     2260   1496   1986   -176    325    179       C
ATOM     93  CD2 LEU A   9     -20.368 -14.862  20.408  1.00 16.75           C
ANISOU   93  CD2 LEU A   9     2439   1786   2138    142    -84    598       C
ATOM     94  N   VAL A  10     -20.992  -9.823  18.490  1.00 11.64           N
ANISOU   94  N   VAL A  10     1703   1433   1285   -240     18    230       N
ATOM     95  CA  VAL A  10     -20.402  -8.663  17.825  1.00 11.31           C
ANISOU   95  CA  VAL A  10     1644   1452   1203   -321     -9    154       C
ATOM     96  C   VAL A  10     -19.931  -7.638  18.853  1.00 11.42           C
ANISOU   96  C   VAL A  10     1569   1500   1271   -355      7    161       C
ATOM     97  O   VAL A  10     -18.832  -7.096  18.745  1.00 11.95           O
ANISOU   97  O   VAL A  10     1623   1599   1319   -419    -81    135       O
ATOM     98  CB  VAL A  10     -21.436  -8.067  16.851  1.00 11.78           C
ANISOU   98  CB  VAL A  10     1702   1504   1268   -416   -198    115       C
ATOM     99  CG1 VAL A  10     -21.027  -6.653  16.348  1.00 12.34           C
ANISOU   99  CG1 VAL A  10     1798   1489   1400   -430     20    210       C
ATOM    100  CG2 VAL A  10     -21.627  -9.010  15.697  1.00 13.00           C
ANISOU  100  CG2 VAL A  10     1954   1698   1288   -540   -162    198       C
ATOM    101  N   LEU A  11     -20.791  -7.318  19.820  1.00 11.70           N
ANISOU  101  N   LEU A  11     1733   1509   1203   -185    -79    136       N
ATOM    102  CA  LEU A  11     -20.492  -6.219  20.730  1.00 12.31           C
ANISOU  102  CA  LEU A  11     1789   1566   1324   -158    -34    139       C
ATOM    103  C   LEU A  11     -19.487  -6.608  21.789  1.00 11.97           C
ANISOU  103  C   LEU A  11     1644   1647   1256   -291    -80    226       C
ATOM    104  O   LEU A  11     -18.755  -5.729  22.256  1.00 12.95           O
ANISOU  104  O   LEU A  11     1850   1680   1389   -371   -125    134       O
ATOM    105  CB  LEU A  11     -21.778  -5.654  21.331  1.00 13.65           C
ANISOU  105  CB  LEU A  11     1991   1639   1557   -139     14    233       C
ATOM    106  CG  LEU A  11     -22.663  -5.038  20.242  1.00 15.94           C
ANISOU  106  CG  LEU A  11     2358   1785   1912      2    -19    158       C
ATOM    107  CD1 LEU A  11     -23.938  -4.574  20.826  1.00 17.70           C
ANISOU  107  CD1 LEU A  11     2438   2021   2266    -36    108     57       C
ATOM    108  CD2 LEU A  11     -21.961  -3.867  19.499  1.00 17.20           C
ANISOU  108  CD2 LEU A  11     2656   1846   2031    -10    -18    239       C
ATOM    109  N   HIS A  12     -19.406  -7.893  22.176  1.00 12.43           N
ANISOU  109  N   HIS A  12     1798   1762   1164   -261      9    261       N
ATOM    110  CA  HIS A  12     -18.303  -8.285  23.048  1.00 13.56           C
ANISOU  110  CA  HIS A  12     2045   1793   1315   -317   -106    343       C
ATOM    111  C   HIS A  12     -16.975  -8.149  22.317  1.00 13.92           C
ANISOU  111  C   HIS A  12     2052   1878   1360   -375   -154    271       C
ATOM    112  O   HIS A  12     -16.004  -7.648  22.887  1.00 14.85           O
ANISOU  112  O   HIS A  12     1950   2173   1520   -367   -288    211       O
ATOM    113  CB  HIS A  12     -18.517  -9.686  23.603  1.00 15.35           C
ANISOU  113  CB  HIS A  12     2167   2130   1537   -476    -90    378       C
ATOM    114  CG  HIS A  12     -19.559  -9.741  24.687  1.00 17.63           C
ANISOU  114  CG  HIS A  12     2398   2709   1590   -658   -206    406       C
ATOM    115  ND1 HIS A  12     -19.403  -9.096  25.894  1.00 19.03           N
ANISOU  115  ND1 HIS A  12     2559   3076   1595   -878   -180    342       N
ATOM    116  CD2 HIS A  12     -20.759 -10.365  24.749  1.00 20.14           C
ANISOU  116  CD2 HIS A  12     2776   3124   1752   -888     48    404       C
ATOM    117  CE1 HIS A  12     -20.455  -9.333  26.655  1.00 20.53           C
ANISOU  117  CE1 HIS A  12     2856   3251   1695  -1048   -129    349       C
ATOM    118  NE2 HIS A  12     -21.298 -10.087  25.979  1.00 21.28           N
ANISOU  118  NE2 HIS A  12     2912   3342   1831  -1053      3    367       N
ATOM    119  N   VAL A  13     -16.910  -8.609  21.063  1.00 13.87           N
ANISOU  119  N   VAL A  13     1974   1826   1469   -315     29    131       N
ATOM    120  CA  VAL A  13     -15.717  -8.393  20.269  1.00 14.14           C
ANISOU  120  CA  VAL A  13     2020   1783   1569   -383    123     62       C
ATOM    121  C   VAL A  13     -15.389  -6.922  20.178  1.00 12.92           C
ANISOU  121  C   VAL A  13     1753   1737   1417   -361    -91     82       C
ATOM    122  O   VAL A  13     -14.221  -6.521  20.308  1.00 12.93           O
ANISOU  122  O   VAL A  13     1739   1670   1503   -182   -191    114       O
ATOM    123  CB  VAL A  13     -15.867  -9.026  18.877  1.00 15.87           C
ANISOU  123  CB  VAL A  13     2332   1800   1897   -465    429   -221       C
ATOM    124  CG1 VAL A  13     -14.727  -8.563  17.970  1.00 16.53           C
ANISOU  124  CG1 VAL A  13     2353   2064   1862   -329    502   -239       C
ATOM    125  CG2 VAL A  13     -15.901 -10.518  19.011  1.00 17.41           C
ANISOU  125  CG2 VAL A  13     2606   1806   2203   -300    488   -337       C
ATOM    126  N   TRP A  14     -16.384  -6.097  19.896  1.00 12.67           N
ANISOU  126  N   TRP A  14     1751   1733   1329   -262    -69    107       N
ATOM    127  CA  TRP A  14     -16.070  -4.682  19.708  1.00 12.25           C
ANISOU  127  CA  TRP A  14     1528   1741   1385   -210   -267    243       C
ATOM    128  C   TRP A  14     -15.530  -4.048  20.985  1.00 12.36           C
ANISOU  128  C   TRP A  14     1562   1794   1341   -189   -229    270       C
ATOM    129  O   TRP A  14     -14.642  -3.174  20.947  1.00 13.03           O
ANISOU  129  O   TRP A  14     1653   1849   1450   -385   -253    258       O
ATOM    130  CB  TRP A  14     -17.279  -3.899  19.187  1.00 13.52           C
ANISOU  130  CB  TRP A  14     1647   1828   1662   -157   -398    231       C
ATOM    131  CG  TRP A  14     -16.731  -2.706  18.410  1.00 15.51           C
ANISOU  131  CG  TRP A  14     1823   1880   2190    -77   -561    231       C
ATOM    132  CD1 TRP A  14     -16.599  -1.379  18.815  1.00 17.45           C
ANISOU  132  CD1 TRP A  14     1877   2230   2522     12   -679    143       C
ATOM    133  CD2 TRP A  14     -16.095  -2.790  17.130  1.00 15.96           C
ANISOU  133  CD2 TRP A  14     1975   1875   2213   -333   -404    706       C
ATOM    134  NE1 TRP A  14     -15.949  -0.682  17.839  1.00 17.03           N
ANISOU  134  NE1 TRP A  14     1809   2112   2549    -72   -786    151       N
ATOM    135  CE2 TRP A  14     -15.627  -1.508  16.800  1.00 17.97           C
ANISOU  135  CE2 TRP A  14     2115   2250   2465   -250   -392    513       C
ATOM    136  CE3 TRP A  14     -15.858  -3.854  16.241  1.00 17.93           C
ANISOU  136  CE3 TRP A  14     2360   2379   2075   -224   -285    747       C
ATOM    137  CZ2 TRP A  14     -14.975  -1.252  15.617  1.00 18.67           C
ANISOU  137  CZ2 TRP A  14     2236   2508   2349   -170   -256    597       C
ATOM    138  CZ3 TRP A  14     -15.205  -3.598  15.068  1.00 19.96           C
ANISOU  138  CZ3 TRP A  14     2586   2744   2255   -209   -168    660       C
ATOM    139  CH2 TRP A  14     -14.788  -2.315  14.764  1.00 20.09           C
ANISOU  139  CH2 TRP A  14     2571   2666   2395   -138   -226    663       C
ATOM    140  N   ALA A  15     -16.068  -4.452  22.136  1.00 12.32           N
ANISOU  140  N   ALA A  15     1700   1756   1224   -178   -220    143       N
ATOM    141  CA  ALA A  15     -15.546  -3.928  23.402  1.00 13.19           C
ANISOU  141  CA  ALA A  15     1908   1836   1267   -129   -242     89       C
ATOM    142  C   ALA A  15     -14.077  -4.310  23.586  1.00 13.24           C
ANISOU  142  C   ALA A  15     1871   1742   1418    -64   -427     90       C
ATOM    143  O   ALA A  15     -13.311  -3.543  24.177  1.00 14.28           O
ANISOU  143  O   ALA A  15     2124   1887   1416   -225   -533     26       O
ATOM    144  CB  ALA A  15     -16.412  -4.400  24.571  1.00 14.46           C
ANISOU  144  CB  ALA A  15     2203   1997   1294   -318    -25    -14       C
ATOM    145  N   LYS A  16     -13.663  -5.480  23.081  1.00 14.25           N
ANISOU  145  N   LYS A  16     1899   1769   1745    213   -413     -5       N
ATOM    146  CA  LYS A  16     -12.244  -5.831  23.085  1.00 15.21           C
ANISOU  146  CA  LYS A  16     2001   1727   2050    154   -466   -185       C
ATOM    147  C   LYS A  16     -11.444  -4.929  22.151  1.00 15.26           C
ANISOU  147  C   LYS A  16     1839   1910   2050     58   -566   -273       C
ATOM    148  O   LYS A  16     -10.339  -4.491  22.510  1.00 16.40           O
ANISOU  148  O   LYS A  16     1972   2005   2253     66   -610   -254       O
ATOM    149  CB  LYS A  16     -12.055  -7.295  22.729  1.00 16.41           C
ANISOU  149  CB  LYS A  16     2303   1628   2303    135   -397     -8       C
ATOM    150  CG  LYS A  16     -12.646  -8.235  23.765  1.00 18.96           C
ANISOU  150  CG  LYS A  16     2717   1821   2664     28   -250    109       C
ATOM    151  CD  LYS A  16     -12.264  -9.711  23.453  1.00 22.30           C
ANISOU  151  CD  LYS A  16     3310   2122   3041   -121   -196    263       C
ATOM    152  CE  LYS A  16     -12.568 -10.654  24.611  1.00 24.75           C
ANISOU  152  CE  LYS A  16     3581   2420   3402   -352   -163    295       C
ATOM    153  NZ  LYS A  16     -14.036 -10.865  24.822  1.00 26.11           N
ANISOU  153  NZ  LYS A  16     3737   2537   3648   -446    -47    242       N
ATOM    154  N   VAL A  17     -11.996  -4.605  20.971  1.00 14.37           N
ANISOU  154  N   VAL A  17     1747   1881   1833    101   -286   -209       N
ATOM    155  CA  VAL A  17     -11.331  -3.667  20.060  1.00 13.94           C
ANISOU  155  CA  VAL A  17     1684   2011   1600    -10   -298   -320       C
ATOM    156  C   VAL A  17     -11.080  -2.324  20.752  1.00 13.22           C
ANISOU  156  C   VAL A  17     1529   1984   1510   -130   -209   -326       C
ATOM    157  O   VAL A  17     -10.031  -1.668  20.551  1.00 13.85           O
ANISOU  157  O   VAL A  17     1606   2200   1457   -282   -168   -236       O
ATOM    158  CB  VAL A  17     -12.199  -3.482  18.792  1.00 14.93           C
ANISOU  158  CB  VAL A  17     1943   2199   1529   -154   -185   -391       C
ATOM    159  CG1 VAL A  17     -11.701  -2.322  17.937  1.00 15.33           C
ANISOU  159  CG1 VAL A  17     2152   2258   1415   -134    -98   -264       C
ATOM    160  CG2 VAL A  17     -12.281  -4.756  18.012  1.00 16.06           C
ANISOU  160  CG2 VAL A  17     2170   2281   1650   -235   -143   -468       C
ATOM    161  N   GLU A  18     -12.046  -1.893  21.571  1.00 12.60           N
ANISOU  161  N   GLU A  18     1659   1791   1339     -7    -83   -151       N
ATOM    162  CA  GLU A  18     -11.945  -0.603  22.241  1.00 12.70           C
ANISOU  162  CA  GLU A  18     1718   1824   1283     -1   -116   -131       C
ATOM    163  C   GLU A  18     -10.809  -0.510  23.250  1.00 12.96           C
ANISOU  163  C   GLU A  18     1797   1815   1311   -186   -152    -44       C
ATOM    164  O   GLU A  18     -10.502   0.596  23.691  1.00 13.70           O
ANISOU  164  O   GLU A  18     1783   1898   1524   -233    -64     43       O
ATOM    165  CB  GLU A  18     -13.278  -0.240  22.891  1.00 13.61           C
ANISOU  165  CB  GLU A  18     1574   2150   1447     88    -84     38       C
ATOM    166  CG  GLU A  18     -14.295   0.092  21.797  1.00 15.35           C
ANISOU  166  CG  GLU A  18     1760   2386   1688    231   -149      3       C
ATOM    167  CD  GLU A  18     -15.681   0.321  22.307  1.00 17.74           C
ANISOU  167  CD  GLU A  18     2065   2782   1894    226   -328     99       C
ATOM    168  OE1 GLU A  18     -16.473   0.944  21.585  1.00 18.04           O
ANISOU  168  OE1 GLU A  18     2002   2665   2186    185   -269    121       O
ATOM    169  OE2 GLU A  18     -15.988  -0.122  23.429  1.00 20.30           O
ANISOU  169  OE2 GLU A  18     2323   3380   2009    150   -204    248       O
ATOM    170  N   ALA A  19     -10.153  -1.620  23.600  1.00 12.77           N
ANISOU  170  N   ALA A  19     1716   1830   1307   -228   -172     94       N
ATOM    171  CA  ALA A  19      -8.968  -1.553  24.444  1.00 13.07           C
ANISOU  171  CA  ALA A  19     1803   1782   1382   -232   -147    143       C
ATOM    172  C   ALA A  19      -7.775  -0.989  23.680  1.00 13.13           C
ANISOU  172  C   ALA A  19     1659   2052   1276   -220   -152     92       C
ATOM    173  O   ALA A  19      -6.815  -0.546  24.304  1.00 15.28           O
ANISOU  173  O   ALA A  19     1795   2537   1473   -422   -284    180       O
ATOM    174  CB  ALA A  19      -8.634  -2.928  24.996  1.00 13.86           C
ANISOU  174  CB  ALA A  19     2148   1576   1541   -149   -139    147       C
ATOM    175  N   ASP A  20      -7.808  -1.013  22.346  1.00 13.31           N
ANISOU  175  N   ASP A  20     1765   2036   1257   -107    -29    157       N
ATOM    176  CA  ASP A  20      -6.697  -0.468  21.546  1.00 13.95           C
ANISOU  176  CA  ASP A  20     1616   2318   1365     29    -81    152       C
ATOM    177  C   ASP A  20      -7.233  -0.071  20.173  1.00 13.14           C
ANISOU  177  C   ASP A  20     1543   2050   1399    -63    -49    155       C
ATOM    178  O   ASP A  20      -6.978  -0.729  19.160  1.00 13.15           O
ANISOU  178  O   ASP A  20     1616   2017   1363   -118     -9    125       O
ATOM    179  CB  ASP A  20      -5.536  -1.442  21.371  1.00 16.41           C
ANISOU  179  CB  ASP A  20     1821   2837   1579    159    -76    192       C
ATOM    180  CG  ASP A  20      -4.365  -0.802  20.611  1.00 18.17           C
ANISOU  180  CG  ASP A  20     1978   3083   1844    288   -181    174       C
ATOM    181  OD1 ASP A  20      -3.422  -1.561  20.364  1.00 21.50           O
ANISOU  181  OD1 ASP A  20     2317   3415   2439    306     75     47       O
ATOM    182  OD2 ASP A  20      -4.383   0.431  20.295  1.00 17.89           O
ANISOU  182  OD2 ASP A  20     2039   3191   1567     47   -287    154       O
ATOM    183  N   VAL A  21      -7.976   1.030  20.128  1.00 13.29           N
ANISOU  183  N   VAL A  21     1624   1969   1454    -33    -50    251       N
ATOM    184  CA  VAL A  21      -8.627   1.420  18.890  1.00 13.47           C
ANISOU  184  CA  VAL A  21     1604   2076   1437     24    110    313       C
ATOM    185  C   VAL A  21      -7.596   1.807  17.839  1.00 13.05           C
ANISOU  185  C   VAL A  21     1670   1977   1310   -108     90    169       C
ATOM    186  O   VAL A  21      -7.701   1.403  16.670  1.00 12.74           O
ANISOU  186  O   VAL A  21     1626   2043   1171    -68     69     65       O
ATOM    187  CB  VAL A  21      -9.619   2.574  19.137  1.00 15.16           C
ANISOU  187  CB  VAL A  21     1843   2252   1667    208    185    379       C
ATOM    188  CG1 VAL A  21     -10.274   2.993  17.809  1.00 16.10           C
ANISOU  188  CG1 VAL A  21     1983   2338   1796    335    139    500       C
ATOM    189  CG2 VAL A  21     -10.664   2.182  20.180  1.00 16.61           C
ANISOU  189  CG2 VAL A  21     2144   2368   1798    206    385    374       C
ATOM    190  N   ALA A  22      -6.594   2.593  18.237  1.00 13.63           N
ANISOU  190  N   ALA A  22     1851   2021   1305   -261     16    125       N
ATOM    191  CA  ALA A  22      -5.616   3.091  17.280  1.00 14.25           C
ANISOU  191  CA  ALA A  22     1859   2122   1434   -343    120     71       C
ATOM    192  C   ALA A  22      -4.841   1.949  16.643  1.00 13.25           C
ANISOU  192  C   ALA A  22     1593   2074   1368   -284     33    132       C
ATOM    193  O   ALA A  22      -4.577   1.967  15.432  1.00 13.71           O
ANISOU  193  O   ALA A  22     1679   2153   1379   -193     12    124       O
ATOM    194  CB  ALA A  22      -4.694   4.111  17.963  1.00 15.87           C
ANISOU  194  CB  ALA A  22     2109   2334   1589   -411    111     40       C
ATOM    195  N   GLY A  23      -4.439   0.959  17.447  1.00 13.37           N
ANISOU  195  N   GLY A  23     1546   2138   1394   -204    -98    119       N
ATOM    196  CA  GLY A  23      -3.680  -0.153  16.914  1.00 13.51           C
ANISOU  196  CA  GLY A  23     1581   2165   1387   -213    -26     64       C
ATOM    197  C   GLY A  23      -4.494  -1.001  15.962  1.00 12.50           C
ANISOU  197  C   GLY A  23     1416   2005   1329   -122    -89    213       C
ATOM    198  O   GLY A  23      -3.999  -1.403  14.904  1.00 12.91           O
ANISOU  198  O   GLY A  23     1446   2038   1421     18    -55    231       O
ATOM    199  N   HIS A  24      -5.764  -1.279  16.301  1.00 12.23           N
ANISOU  199  N   HIS A  24     1432   1908   1308    -95    -52    273       N
ATOM    200  CA  HIS A  24      -6.631  -1.979  15.361  1.00 12.02           C
ANISOU  200  CA  HIS A  24     1441   1844   1283   -107    -83    245       C
ATOM    201  C   HIS A  24      -6.791  -1.183  14.073  1.00 12.17           C
ANISOU  201  C   HIS A  24     1473   1829   1322    -48     -3    286       C
ATOM    202  O   HIS A  24      -6.770  -1.752  12.977  1.00 12.25           O
ANISOU  202  O   HIS A  24     1525   1861   1270   -144     22    216       O
ATOM    203  CB  HIS A  24      -8.011  -2.246  15.985  1.00 12.08           C
ANISOU  203  CB  HIS A  24     1395   1822   1374   -135     83    216       C
ATOM    204  CG  HIS A  24      -8.039  -3.397  16.948  1.00 12.58           C
ANISOU  204  CG  HIS A  24     1526   1727   1526     42    103    196       C
ATOM    205  ND1 HIS A  24      -7.674  -3.271  18.271  1.00 13.41           N
ANISOU  205  ND1 HIS A  24     1762   1820   1515    -66     99    335       N
ATOM    206  CD2 HIS A  24      -8.450  -4.690  16.805  1.00 13.76           C
ANISOU  206  CD2 HIS A  24     1822   1750   1656     20    120    233       C
ATOM    207  CE1 HIS A  24      -7.827  -4.439  18.889  1.00 13.96           C
ANISOU  207  CE1 HIS A  24     1758   1858   1688   -121    219    317       C
ATOM    208  NE2 HIS A  24      -8.292  -5.324  18.025  1.00 14.38           N
ANISOU  208  NE2 HIS A  24     1886   1797   1780     -2    240    276       N
ATOM    209  N   GLY A  25      -7.013   0.133  14.195  1.00 11.90           N
ANISOU  209  N   GLY A  25     1366   1779   1377   -109     22    421       N
ATOM    210  CA  GLY A  25      -7.238   0.947  13.010  1.00 12.85           C
ANISOU  210  CA  GLY A  25     1629   1886   1366   -183    -65    441       C
ATOM    211  C   GLY A  25      -6.038   0.965  12.081  1.00 12.21           C
ANISOU  211  C   GLY A  25     1484   1871   1283   -177   -181    329       C
ATOM    212  O   GLY A  25      -6.181   0.892  10.855  1.00 12.75           O
ANISOU  212  O   GLY A  25     1607   1968   1268   -231   -102    214       O
ATOM    213  N   GLN A  26      -4.846   1.089  12.650  1.00 12.23           N
ANISOU  213  N   GLN A  26     1488   1889   1271   -316    -52    248       N
ATOM    214  CA  GLN A  26      -3.624   1.047  11.861  1.00 13.18           C
ANISOU  214  CA  GLN A  26     1530   2048   1431   -415    -59    181       C
ATOM    215  C   GLN A  26      -3.500  -0.281  11.141  1.00 12.70           C
ANISOU  215  C   GLN A  26     1388   1975   1462   -394      5    111       C
ATOM    216  O   GLN A  26      -3.190  -0.334   9.943  1.00 13.34           O
ANISOU  216  O   GLN A  26     1551   2087   1431   -346     77     42       O
ATOM    217  CB  GLN A  26      -2.417   1.235  12.770  1.00 15.22           C
ANISOU  217  CB  GLN A  26     1688   2417   1679   -607   -249    215       C
ATOM    218  CG  GLN A  26      -2.187   2.630  13.213  1.00 18.44           C
ANISOU  218  CG  GLN A  26     2257   2844   1904   -727   -338    306       C
ATOM    219  CD  GLN A  26      -0.967   2.725  14.111  1.00 20.83           C
ANISOU  219  CD  GLN A  26     2580   3225   2111   -932   -591    475       C
ATOM    220  OE1 GLN A  26       0.013   3.466  13.833  1.00 22.31           O
ANISOU  220  OE1 GLN A  26     2564   3450   2461  -1013   -640    469       O
ATOM    221  NE2 GLN A  26      -0.987   1.960  15.180  1.00 21.45           N
ANISOU  221  NE2 GLN A  26     2752   3353   2045   -985   -678    530       N
ATOM    222  N   ASP A  27      -3.709  -1.373  11.872  1.00 12.80           N
ANISOU  222  N   ASP A  27     1364   1926   1573   -220    -23    274       N
ATOM    223  CA  ASP A  27      -3.545  -2.683  11.268  1.00 12.98           C
ANISOU  223  CA  ASP A  27     1461   1871   1600     48    -49    335       C
ATOM    224  C   ASP A  27      -4.564  -2.901  10.151  1.00 12.16           C
ANISOU  224  C   ASP A  27     1338   1843   1438    -48     53    217       C
ATOM    225  O   ASP A  27      -4.242  -3.523   9.122  1.00 12.54           O
ANISOU  225  O   ASP A  27     1406   1902   1456     80     -3    167       O
ATOM    226  CB  ASP A  27      -3.707  -3.785  12.319  1.00 15.12           C
ANISOU  226  CB  ASP A  27     1655   2238   1852    140   -265    356       C
ATOM    227  CG  ASP A  27      -2.528  -3.882  13.274  1.00 18.18           C
ANISOU  227  CG  ASP A  27     2065   2787   2058     52   -267    360       C
ATOM    228  OD1 ASP A  27      -1.481  -3.230  13.052  1.00 19.98           O
ANISOU  228  OD1 ASP A  27     2121   3148   2321     59   -317    263       O
ATOM    229  OD2 ASP A  27      -2.651  -4.653  14.247  1.00 19.59           O
ANISOU  229  OD2 ASP A  27     2363   3011   2068    286   -373    461       O
ATOM    230  N   ILE A  28      -5.817  -2.443  10.363  1.00 11.58           N
ANISOU  230  N   ILE A  28     1381   1762   1258    -65    -51    166       N
ATOM    231  CA  ILE A  28      -6.853  -2.626   9.355  1.00 10.93           C
ANISOU  231  CA  ILE A  28     1271   1587   1294    -82    -51    156       C
ATOM    232  C   ILE A  28      -6.515  -1.855   8.090  1.00 11.33           C
ANISOU  232  C   ILE A  28     1340   1647   1318   -120    107    169       C
ATOM    233  O   ILE A  28      -6.610  -2.409   6.982  1.00 12.14           O
ANISOU  233  O   ILE A  28     1501   1718   1394    -50     41     15       O
ATOM    234  CB  ILE A  28      -8.226  -2.247   9.937  1.00 11.01           C
ANISOU  234  CB  ILE A  28     1288   1502   1393    -51    -15     41       C
ATOM    235  CG1 ILE A  28      -8.687  -3.332  10.924  1.00 11.78           C
ANISOU  235  CG1 ILE A  28     1475   1532   1469    -18     91     19       C
ATOM    236  CG2 ILE A  28      -9.259  -2.065   8.835  1.00 11.58           C
ANISOU  236  CG2 ILE A  28     1347   1598   1455     25    -61    155       C
ATOM    237  CD1 ILE A  28      -9.732  -2.904  11.913  1.00 12.26           C
ANISOU  237  CD1 ILE A  28     1460   1664   1532    -40    195     61       C
ATOM    238  N   LEU A  29      -6.133  -0.580   8.229  1.00 11.57           N
ANISOU  238  N   LEU A  29     1324   1724   1347   -147      8    184       N
ATOM    239  CA  LEU A  29      -5.832   0.191   7.024  1.00 11.98           C
ANISOU  239  CA  LEU A  29     1489   1733   1328   -170    108    114       C
ATOM    240  C   LEU A  29      -4.589  -0.323   6.327  1.00 12.20           C
ANISOU  240  C   LEU A  29     1533   1834   1268    -78     66    129       C
ATOM    241  O   LEU A  29      -4.554  -0.372   5.095  1.00 12.86           O
ANISOU  241  O   LEU A  29     1688   1922   1277   -106    123     73       O
ATOM    242  CB  LEU A  29      -5.689   1.686   7.346  1.00 12.42           C
ANISOU  242  CB  LEU A  29     1455   1681   1582   -173    136     42       C
ATOM    243  CG  LEU A  29      -6.983   2.401   7.738  1.00 13.72           C
ANISOU  243  CG  LEU A  29     1575   1855   1784    -95    119    -39       C
ATOM    244  CD1 LEU A  29      -6.706   3.872   8.040  1.00 14.38           C
ANISOU  244  CD1 LEU A  29     1828   1721   1916   -117    198   -115       C
ATOM    245  CD2 LEU A  29      -8.090   2.236   6.686  1.00 15.57           C
ANISOU  245  CD2 LEU A  29     1870   2090   1956    102   -257   -105       C
ATOM    246  N   ILE A  30      -3.560  -0.720   7.086  1.00 12.48           N
ANISOU  246  N   ILE A  30     1494   1933   1314    -23     97    178       N
ATOM    247  CA  ILE A  30      -2.364  -1.254   6.437  1.00 13.70           C
ANISOU  247  CA  ILE A  30     1480   2239   1486      0     68    112       C
ATOM    248  C   ILE A  30      -2.693  -2.541   5.685  1.00 12.99           C
ANISOU  248  C   ILE A  30     1462   2106   1370     57     42    190       C
ATOM    249  O   ILE A  30      -2.232  -2.739   4.557  1.00 13.87           O
ANISOU  249  O   ILE A  30     1511   2314   1445    -18     63     51       O
ATOM    250  CB  ILE A  30      -1.236  -1.433   7.459  1.00 14.63           C
ANISOU  250  CB  ILE A  30     1567   2477   1515   -121     65     58       C
ATOM    251  CG1 ILE A  30      -0.784  -0.054   7.921  1.00 15.80           C
ANISOU  251  CG1 ILE A  30     1767   2678   1557   -453     -3    -67       C
ATOM    252  CG2 ILE A  30      -0.096  -2.248   6.865  1.00 16.02           C
ANISOU  252  CG2 ILE A  30     1623   2748   1715     62     95     -6       C
ATOM    253  CD1 ILE A  30       0.209  -0.093   9.065  1.00 17.58           C
ANISOU  253  CD1 ILE A  30     1861   2988   1828   -288   -251   -316       C
ATOM    254  N   ARG A  31      -3.506  -3.416   6.287  1.00 12.71           N
ANISOU  254  N   ARG A  31     1512   1924   1393    146      3    160       N
ATOM    255  CA  ARG A  31      -3.906  -4.637   5.600  1.00 13.60           C
ANISOU  255  CA  ARG A  31     1626   2056   1483     52     25     67       C
ATOM    256  C   ARG A  31      -4.688  -4.295   4.331  1.00 13.37           C
ANISOU  256  C   ARG A  31     1569   2013   1498    138     51     33       C
ATOM    257  O   ARG A  31      -4.481  -4.902   3.274  1.00 14.65           O
ANISOU  257  O   ARG A  31     1763   2215   1589    269    203   -114       O
ATOM    258  CB  ARG A  31      -4.760  -5.493   6.534  1.00 14.69           C
ANISOU  258  CB  ARG A  31     1797   2058   1726     50    -44      2       C
ATOM    259  CG  ARG A  31      -5.377  -6.717   5.891  1.00 18.16           C
ANISOU  259  CG  ARG A  31     2420   2194   2284    114     -2   -136       C
ATOM    260  CD  ARG A  31      -4.331  -7.750   5.590  1.00 21.78           C
ANISOU  260  CD  ARG A  31     3236   2380   2660    138     99   -193       C
ATOM    261  NE  ARG A  31      -4.941  -8.946   5.025  1.00 25.48           N
ANISOU  261  NE  ARG A  31     4098   2591   2992    160    105   -282       N
ATOM    262  CZ  ARG A  31      -4.262 -10.048   4.721  1.00 28.57           C
ANISOU  262  CZ  ARG A  31     4741   2790   3325    188      6   -392       C
ATOM    263  NH1 ARG A  31      -2.949 -10.091   4.911  1.00 29.92           N
ANISOU  263  NH1 ARG A  31     4929   2960   3480    249     16   -369       N
ATOM    264  NH2 ARG A  31      -4.893 -11.092   4.193  1.00 30.00           N
ANISOU  264  NH2 ARG A  31     5113   2879   3408     86    -32   -485       N
ATOM    265  N   LEU A  32      -5.609  -3.336   4.417  1.00 12.66           N
ANISOU  265  N   LEU A  32     1466   1966   1379    134     43    137       N
ATOM    266  CA  LEU A  32      -6.370  -2.901   3.249  1.00 12.56           C
ANISOU  266  CA  LEU A  32     1412   2083   1278    250     72    105       C
ATOM    267  C   LEU A  32      -5.447  -2.406   2.138  1.00 13.16           C
ANISOU  267  C   LEU A  32     1381   2305   1316    196    110    -48       C
ATOM    268  O   LEU A  32      -5.601  -2.790   0.969  1.00 14.22           O
ANISOU  268  O   LEU A  32     1563   2391   1449    199    131   -111       O
ATOM    269  CB  LEU A  32      -7.323  -1.776   3.690  1.00 12.04           C
ANISOU  269  CB  LEU A  32     1304   1966   1305    196     -3     65       C
ATOM    270  CG  LEU A  32      -8.157  -1.174   2.564  1.00 11.84           C
ANISOU  270  CG  LEU A  32     1260   1863   1375     82     63     68       C
ATOM    271  CD1 LEU A  32      -9.115  -2.185   1.924  1.00 12.64           C
ANISOU  271  CD1 LEU A  32     1304   2057   1441     15    -12    110       C
ATOM    272  CD2 LEU A  32      -8.868   0.069   3.039  1.00 12.74           C
ANISOU  272  CD2 LEU A  32     1498   1878   1463     17    157    136       C
ATOM    273  N   PHE A  33      -4.493  -1.534   2.484  1.00 13.51           N
ANISOU  273  N   PHE A  33     1298   2547   1290    133    169    129       N
ATOM    274  CA  PHE A  33      -3.629  -0.937   1.468  1.00 14.70           C
ANISOU  274  CA  PHE A  33     1313   2848   1426    135    256    182       C
ATOM    275  C   PHE A  33      -2.628  -1.928   0.901  1.00 16.77           C
ANISOU  275  C   PHE A  33     1499   3288   1585    284    237    123       C
ATOM    276  O   PHE A  33      -2.269  -1.825  -0.274  1.00 18.47           O
ANISOU  276  O   PHE A  33     1771   3596   1652    248    330    166       O
ATOM    277  CB  PHE A  33      -2.900   0.269   2.050  1.00 14.79           C
ANISOU  277  CB  PHE A  33     1380   2694   1545   -117     73    264       C
ATOM    278  CG  PHE A  33      -3.805   1.374   2.513  1.00 14.16           C
ANISOU  278  CG  PHE A  33     1346   2540   1496   -182     44    332       C
ATOM    279  CD1 PHE A  33      -5.015   1.625   1.909  1.00 14.15           C
ANISOU  279  CD1 PHE A  33     1364   2450   1562   -192     12    325       C
ATOM    280  CD2 PHE A  33      -3.442   2.170   3.595  1.00 14.74           C
ANISOU  280  CD2 PHE A  33     1543   2560   1498   -284    -60    403       C
ATOM    281  CE1 PHE A  33      -5.836   2.630   2.367  1.00 14.87           C
ANISOU  281  CE1 PHE A  33     1622   2487   1540   -383     10    283       C
ATOM    282  CE2 PHE A  33      -4.246   3.196   4.053  1.00 14.81           C
ANISOU  282  CE2 PHE A  33     1591   2536   1501   -308    -40    446       C
ATOM    283  CZ  PHE A  33      -5.457   3.420   3.448  1.00 15.06           C
ANISOU  283  CZ  PHE A  33     1705   2504   1512   -473   -130    363       C
ATOM    284  N   LYS A  34      -2.175  -2.891   1.695  1.00 17.68           N
ANISOU  284  N   LYS A  34     1553   3419   1744    553    269     43       N
ATOM    285  CA  LYS A  34      -1.265  -3.903   1.167  1.00 19.82           C
ANISOU  285  CA  LYS A  34     1905   3663   1963    827    -21     -7       C
ATOM    286  C   LYS A  34      -1.994  -4.904   0.286  1.00 19.13           C
ANISOU  286  C   LYS A  34     2028   3415   1827    996     68   -112       C
ATOM    287  O   LYS A  34      -1.470  -5.317  -0.758  1.00 21.00           O
ANISOU  287  O   LYS A  34     2379   3580   2021   1042    299   -311       O
ATOM    288  CB  LYS A  34      -0.537  -4.588   2.325  1.00 23.00           C
ANISOU  288  CB  LYS A  34     2214   4139   2386    699   -155     21       C
ATOM    289  CG  LYS A  34       0.497  -3.636   2.959  1.00 26.99           C
ANISOU  289  CG  LYS A  34     2820   4656   2780    302    -31     49       C
ATOM    290  CD  LYS A  34       1.481  -3.133   1.896  1.00 30.53           C
ANISOU  290  CD  LYS A  34     3454   4996   3148    -67     60     80       C
ATOM    291  CE  LYS A  34       2.243  -1.907   2.364  1.00 32.70           C
ANISOU  291  CE  LYS A  34     3839   5221   3364   -304    215    135       C
ATOM    292  NZ  LYS A  34       3.173  -1.448   1.302  1.00 34.05           N
ANISOU  292  NZ  LYS A  34     4101   5349   3485   -458    224    183       N
ATOM    293  N   SER A  35      -3.207  -5.296   0.686  1.00 17.99           N
ANISOU  293  N   SER A  35     2039   3041   1756    976    -84     35       N
ATOM    294  CA  SER A  35      -3.963  -6.282  -0.078  1.00 18.29           C
ANISOU  294  CA  SER A  35     2369   2839   1741    942     27     -3       C
ATOM    295  C   SER A  35      -4.595  -5.690  -1.328  1.00 17.50           C
ANISOU  295  C   SER A  35     2350   2669   1630    827     56   -173       C
ATOM    296  O   SER A  35      -4.809  -6.406  -2.311  1.00 18.21           O
ANISOU  296  O   SER A  35     2488   2664   1767    952    -56   -294       O
ATOM    297  CB  SER A  35      -5.065  -6.909   0.773  1.00 20.73           C
ANISOU  297  CB  SER A  35     2924   2965   1989    809      5    208       C
ATOM    298  OG  SER A  35      -4.502  -7.607   1.858  1.00 23.52           O
ANISOU  298  OG  SER A  35     3451   3220   2265    698     52    393       O
ATOM    299  N   HIS A  36      -4.944  -4.412  -1.288  1.00 15.99           N
ANISOU  299  N   HIS A  36     2013   2470   1592    818     90    -48       N
ATOM    300  CA  HIS A  36      -5.704  -3.749  -2.347  1.00 15.06           C
ANISOU  300  CA  HIS A  36     1886   2353   1481    641     22    -70       C
ATOM    301  C   HIS A  36      -5.154  -2.351  -2.541  1.00 15.17           C
ANISOU  301  C   HIS A  36     1995   2356   1414    469     30   -132       C
ATOM    302  O   HIS A  36      -5.774  -1.366  -2.136  1.00 14.42           O
ANISOU  302  O   HIS A  36     1946   2221   1314    425     51    -40       O
ATOM    303  CB  HIS A  36      -7.196  -3.724  -2.018  1.00 15.70           C
ANISOU  303  CB  HIS A  36     1934   2315   1716    584     96     35       C
ATOM    304  CG  HIS A  36      -7.745  -5.066  -1.672  1.00 16.81           C
ANISOU  304  CG  HIS A  36     2047   2387   1951    608    218    219       C
ATOM    305  ND1 HIS A  36      -8.073  -6.015  -2.619  1.00 18.45           N
ANISOU  305  ND1 HIS A  36     2405   2380   2224    550     88    231       N
ATOM    306  CD2 HIS A  36      -8.016  -5.627  -0.469  1.00 18.37           C
ANISOU  306  CD2 HIS A  36     2258   2541   2182    687    336    315       C
ATOM    307  CE1 HIS A  36      -8.503  -7.112  -2.010  1.00 19.38           C
ANISOU  307  CE1 HIS A  36     2525   2487   2350    545    204    207       C
ATOM    308  NE2 HIS A  36      -8.474  -6.902  -0.706  1.00 19.66           N
ANISOU  308  NE2 HIS A  36     2439   2653   2377    611    273    260       N
ATOM    309  N   PRO A  37      -3.965  -2.230  -3.155  1.00 15.57           N
ANISOU  309  N   PRO A  37     1773   2500   1644    534    169    -32       N
ATOM    310  CA  PRO A  37      -3.281  -0.926  -3.178  1.00 15.80           C
ANISOU  310  CA  PRO A  37     1623   2623   1756    389    256     -6       C
ATOM    311  C   PRO A  37      -4.039   0.200  -3.838  1.00 14.71           C
ANISOU  311  C   PRO A  37     1657   2473   1461    343    324    -97       C
ATOM    312  O   PRO A  37      -3.847   1.366  -3.455  1.00 15.33           O
ANISOU  312  O   PRO A  37     1748   2540   1537    319    178   -114       O
ATOM    313  CB  PRO A  37      -1.950  -1.225  -3.884  1.00 18.49           C
ANISOU  313  CB  PRO A  37     2015   2830   2181    440    364     36       C
ATOM    314  CG  PRO A  37      -1.772  -2.679  -3.794  1.00 19.76           C
ANISOU  314  CG  PRO A  37     2301   2894   2314    324    512     16       C
ATOM    315  CD  PRO A  37      -3.122  -3.314  -3.698  1.00 17.38           C
ANISOU  315  CD  PRO A  37     1928   2675   2001    505    315     34       C
ATOM    316  N   GLU A  38      -4.961  -0.123  -4.752  1.00 14.80           N
ANISOU  316  N   GLU A  38     1828   2560   1235    268    180    -96       N
ATOM    317  CA  GLU A  38      -5.747   0.916  -5.412  1.00 14.48           C
ANISOU  317  CA  GLU A  38     1908   2357   1238    198     61    -93       C
ATOM    318  C   GLU A  38      -6.580   1.705  -4.397  1.00 12.90           C
ANISOU  318  C   GLU A  38     1631   2104   1166     97      2    -38       C
ATOM    319  O   GLU A  38      -6.933   2.862  -4.645  1.00 13.48           O
ANISOU  319  O   GLU A  38     1812   1987   1323     36      3     41       O
ATOM    320  CB  GLU A  38      -6.640   0.302  -6.507  1.00 15.08           C
ANISOU  320  CB  GLU A  38     2104   2304   1320    180     97   -248       C
ATOM    321  CG  GLU A  38      -7.705  -0.710  -6.039  1.00 15.55           C
ANISOU  321  CG  GLU A  38     2158   2238   1513    167     72   -233       C
ATOM    322  CD  GLU A  38      -7.260  -2.147  -5.835  1.00 16.78           C
ANISOU  322  CD  GLU A  38     2302   2300   1773    108     45   -101       C
ATOM    323  OE1 GLU A  38      -8.148  -3.012  -5.885  1.00 17.95           O
ANISOU  323  OE1 GLU A  38     2601   2189   2029    130     35    -30       O
ATOM    324  OE2 GLU A  38      -6.059  -2.409  -5.642  1.00 17.42           O
ANISOU  324  OE2 GLU A  38     2447   2357   1814    265   -100    -18       O
ATOM    325  N   THR A  39      -6.908   1.099  -3.240  1.00 12.26           N
ANISOU  325  N   THR A  39     1548   2016   1096     -4    120    -35       N
ATOM    326  CA  THR A  39      -7.727   1.795  -2.250  1.00 12.08           C
ANISOU  326  CA  THR A  39     1533   1857   1201     96    124    -65       C
ATOM    327  C   THR A  39      -7.028   3.007  -1.673  1.00 12.23           C
ANISOU  327  C   THR A  39     1472   1920   1255     43    -38   -134       C
ATOM    328  O   THR A  39      -7.702   3.968  -1.278  1.00 12.79           O
ANISOU  328  O   THR A  39     1544   1962   1354    -34     79   -200       O
ATOM    329  CB  THR A  39      -8.168   0.844  -1.129  1.00 12.19           C
ANISOU  329  CB  THR A  39     1548   1899   1187    178     71     70       C
ATOM    330  OG1 THR A  39      -7.037   0.349  -0.418  1.00 12.46           O
ANISOU  330  OG1 THR A  39     1589   1986   1159    220    -32     75       O
ATOM    331  CG2 THR A  39      -9.058  -0.282  -1.634  1.00 12.73           C
ANISOU  331  CG2 THR A  39     1692   1876   1268    -59    -14     56       C
ATOM    332  N   LEU A  40      -5.695   2.992  -1.652  1.00 12.94           N
ANISOU  332  N   LEU A  40     1442   2162   1314   -106    -26   -136       N
ATOM    333  CA  LEU A  40      -4.964   4.097  -1.055  1.00 13.19           C
ANISOU  333  CA  LEU A  40     1421   2192   1399   -150     45   -175       C
ATOM    334  C   LEU A  40      -5.175   5.402  -1.832  1.00 13.15           C
ANISOU  334  C   LEU A  40     1518   2090   1389   -187    199   -181       C
ATOM    335  O   LEU A  40      -5.128   6.489  -1.248  1.00 13.59           O
ANISOU  335  O   LEU A  40     1513   2199   1451   -151    103   -224       O
ATOM    336  CB  LEU A  40      -3.492   3.699  -0.988  1.00 15.00           C
ANISOU  336  CB  LEU A  40     1663   2411   1627    -87      7   -304       C
ATOM    337  CG  LEU A  40      -2.542   4.718  -0.391  1.00 15.55           C
ANISOU  337  CG  LEU A  40     1521   2632   1757   -172     44   -138       C
ATOM    338  CD1 LEU A  40      -2.930   5.108   1.040  1.00 15.27           C
ANISOU  338  CD1 LEU A  40     1796   2457   1551   -332     29    -92       C
ATOM    339  CD2 LEU A  40      -1.127   4.148  -0.403  1.00 17.29           C
ANISOU  339  CD2 LEU A  40     1529   2952   2089    -66     83      7       C
ATOM    340  N   GLU A  41      -5.472   5.304  -3.128  1.00 13.12           N
ANISOU  340  N   GLU A  41     1622   2069   1294    -60    230    -52       N
ATOM    341  CA  GLU A  41      -5.702   6.480  -3.952  1.00 13.14           C
ANISOU  341  CA  GLU A  41     1735   1976   1282    -67    159    -85       C
ATOM    342  C   GLU A  41      -6.848   7.327  -3.448  1.00 12.94           C
ANISOU  342  C   GLU A  41     1697   1840   1378   -108     99    -43       C
ATOM    343  O   GLU A  41      -6.901   8.531  -3.729  1.00 14.37           O
ANISOU  343  O   GLU A  41     2007   1937   1518    -64    270    -19       O
ATOM    344  CB  GLU A  41      -5.959   6.055  -5.410  1.00 14.36           C
ANISOU  344  CB  GLU A  41     1922   2134   1402    -13     87     52       C
ATOM    345  CG  GLU A  41      -6.209   7.185  -6.370  1.00 15.98           C
ANISOU  345  CG  GLU A  41     2140   2333   1600    -73    128     59       C
ATOM    346  CD  GLU A  41      -5.022   8.105  -6.560  1.00 17.28           C
ANISOU  346  CD  GLU A  41     2371   2477   1719   -155    158     88       C
ATOM    347  OE1 GLU A  41      -3.867   7.648  -6.349  1.00 18.53           O
ANISOU  347  OE1 GLU A  41     2374   2680   1985   -146    382     92       O
ATOM    348  OE2 GLU A  41      -5.226   9.266  -6.947  1.00 18.17           O
ANISOU  348  OE2 GLU A  41     2609   2515   1781   -353    179     86       O
ATOM    349  N   LYS A  42      -7.809   6.716  -2.758  1.00 12.64           N
ANISOU  349  N   LYS A  42     1459   2051   1293   -127    134      7       N
ATOM    350  CA  LYS A  42      -8.966   7.461  -2.274  1.00 12.53           C
ANISOU  350  CA  LYS A  42     1431   1980   1348    -69    134    -42       C
ATOM    351  C   LYS A  42      -8.613   8.391  -1.116  1.00 12.38           C
ANISOU  351  C   LYS A  42     1527   1903   1275    -28     94     -4       C
ATOM    352  O   LYS A  42      -9.414   9.260  -0.771  1.00 12.73           O
ANISOU  352  O   LYS A  42     1668   1836   1334     56    106     36       O
ATOM    353  CB  LYS A  42     -10.068   6.482  -1.883  1.00 12.36           C
ANISOU  353  CB  LYS A  42     1337   1931   1429   -120     58   -106       C
ATOM    354  CG  LYS A  42     -10.657   5.711  -3.044  1.00 12.75           C
ANISOU  354  CG  LYS A  42     1466   1937   1439    -86    -51   -140       C
ATOM    355  CD  LYS A  42     -11.458   6.601  -3.992  1.00 13.33           C
ANISOU  355  CD  LYS A  42     1542   2049   1474     -1   -167   -148       C
ATOM    356  CE  LYS A  42     -11.933   5.843  -5.233  1.00 14.23           C
ANISOU  356  CE  LYS A  42     1662   2215   1528    156   -174    -23       C
ATOM    357  NZ  LYS A  42     -12.818   6.713  -6.020  1.00 14.26           N
ANISOU  357  NZ  LYS A  42     1757   2236   1423    106   -146     86       N
ATOM    358  N   PHE A  43      -7.448   8.225  -0.503  1.00 12.60           N
ANISOU  358  N   PHE A  43     1465   2062   1261   -168     66    -78       N
ATOM    359  CA  PHE A  43      -7.063   8.987   0.692  1.00 13.13           C
ANISOU  359  CA  PHE A  43     1449   2125   1416   -118     -3   -121       C
ATOM    360  C   PHE A  43      -6.177  10.146   0.293  1.00 14.46           C
ANISOU  360  C   PHE A  43     1483   2283   1730   -256    165    -57       C
ATOM    361  O   PHE A  43      -4.951  10.042   0.317  1.00 15.83           O
ANISOU  361  O   PHE A  43     1631   2451   1932   -355    260   -292       O
ATOM    362  CB  PHE A  43      -6.407   8.095   1.740  1.00 13.41           C
ANISOU  362  CB  PHE A  43     1610   2129   1357     36     64    -67       C
ATOM    363  CG  PHE A  43      -7.355   7.085   2.320  1.00 13.05           C
ANISOU  363  CG  PHE A  43     1576   1972   1412     55    -81   -167       C
ATOM    364  CD1 PHE A  43      -7.997   7.355   3.499  1.00 13.16           C
ANISOU  364  CD1 PHE A  43     1587   2030   1385     52   -111    -19       C
ATOM    365  CD2 PHE A  43      -7.604   5.885   1.664  1.00 13.67           C
ANISOU  365  CD2 PHE A  43     1495   1999   1699    -93   -198   -249       C
ATOM    366  CE1 PHE A  43      -8.908   6.468   4.024  1.00 14.32           C
ANISOU  366  CE1 PHE A  43     1687   2163   1590    -80   -318   -115       C
ATOM    367  CE2 PHE A  43      -8.500   4.997   2.151  1.00 14.18           C
ANISOU  367  CE2 PHE A  43     1632   2003   1754     41   -147   -141       C
ATOM    368  CZ  PHE A  43      -9.160   5.263   3.351  1.00 14.15           C
ANISOU  368  CZ  PHE A  43     1525   2095   1757      6   -399    -74       C
ATOM    369  N   ASP A  44      -6.800  11.278  -0.036  1.00 15.45           N
ANISOU  369  N   ASP A  44     1741   2393   1735   -482     21    267       N
ATOM    370  CA  ASP A  44      -6.010  12.438  -0.422  1.00 18.19           C
ANISOU  370  CA  ASP A  44     2162   2671   2076   -767    -70    545       C
ATOM    371  C   ASP A  44      -5.037  12.886   0.649  1.00 17.41           C
ANISOU  371  C   ASP A  44     2019   2493   2104   -841    126    551       C
ATOM    372  O   ASP A  44      -4.035  13.529   0.326  1.00 20.47           O
ANISOU  372  O   ASP A  44     2395   3097   2286  -1119     44    785       O
ATOM    373  CB  ASP A  44      -6.934  13.549  -0.837  1.00 21.86           C
ANISOU  373  CB  ASP A  44     2762   3056   2486   -918   -220    698       C
ATOM    374  CG  ASP A  44      -7.613  13.222  -2.149  1.00 25.81           C
ANISOU  374  CG  ASP A  44     3546   3479   2783   -755   -308    662       C
ATOM    375  OD1 ASP A  44      -6.942  12.602  -3.019  1.00 27.31           O
ANISOU  375  OD1 ASP A  44     3946   3630   2801   -724   -667    636       O
ATOM    376  OD2 ASP A  44      -8.758  13.604  -2.346  1.00 27.92           O
ANISOU  376  OD2 ASP A  44     3760   3748   3100   -831   -234    588       O
ATOM    377  N   ARG A  45      -5.298  12.566   1.903  1.00 15.31           N
ANISOU  377  N   ARG A  45     1917   2006   1895   -530     46    213       N
ATOM    378  CA  ARG A  45      -4.422  13.023   2.962  1.00 15.78           C
ANISOU  378  CA  ARG A  45     1939   2124   1934   -502    -21    104       C
ATOM    379  C   ARG A  45      -3.083  12.292   2.978  1.00 15.63           C
ANISOU  379  C   ARG A  45     1841   2132   1965   -573      3     40       C
ATOM    380  O   ARG A  45      -2.111  12.829   3.514  1.00 16.84           O
ANISOU  380  O   ARG A  45     1959   2238   2202   -627   -141    136       O
ATOM    381  CB  ARG A  45      -5.168  12.852   4.289  1.00 16.15           C
ANISOU  381  CB  ARG A  45     1950   2198   1988   -340     74    -44       C
ATOM    382  CG  ARG A  45      -4.504  13.516   5.494  1.00 16.85           C
ANISOU  382  CG  ARG A  45     2224   2099   2081   -433     -7   -149       C
ATOM    383  CD  ARG A  45      -5.308  13.309   6.751  1.00 16.86           C
ANISOU  383  CD  ARG A  45     2149   2069   2187   -264    -13   -101       C
ATOM    384  NE  ARG A  45      -6.688  13.731   6.631  1.00 16.70           N
ANISOU  384  NE  ARG A  45     2137   2038   2168   -342    -78   -220       N
ATOM    385  CZ  ARG A  45      -7.115  14.985   6.767  1.00 17.33           C
ANISOU  385  CZ  ARG A  45     2306   2050   2228   -316   -160   -150       C
ATOM    386  NH1 ARG A  45      -6.263  15.989   7.075  1.00 18.38           N
ANISOU  386  NH1 ARG A  45     2770   2002   2213   -393   -214   -104       N
ATOM    387  NH2 ARG A  45      -8.422  15.215   6.630  1.00 18.41           N
ANISOU  387  NH2 ARG A  45     2380   2232   2383    -44    -32   -132       N
ATOM    388  N   PHE A  46      -3.004  11.046   2.466  1.00 14.68           N
ANISOU  388  N   PHE A  46     1668   2098   1812   -256    283     48       N
ATOM    389  CA  PHE A  46      -1.777  10.268   2.643  1.00 15.51           C
ANISOU  389  CA  PHE A  46     1782   2294   1818   -317    286    -22       C
ATOM    390  C   PHE A  46      -1.562   9.244   1.531  1.00 15.49           C
ANISOU  390  C   PHE A  46     1714   2303   1869   -285    300    -60       C
ATOM    391  O   PHE A  46      -0.875   8.242   1.746  1.00 16.02           O
ANISOU  391  O   PHE A  46     1881   2229   1975   -250    501    104       O
ATOM    392  CB  PHE A  46      -1.640   9.641   4.048  1.00 15.94           C
ANISOU  392  CB  PHE A  46     1886   2363   1807   -301    155    106       C
ATOM    393  CG  PHE A  46      -2.869   8.917   4.524  1.00 15.90           C
ANISOU  393  CG  PHE A  46     1763   2534   1743    -11    204    320       C
ATOM    394  CD1 PHE A  46      -3.657   9.437   5.534  1.00 17.45           C
ANISOU  394  CD1 PHE A  46     2098   2697   1838    155    348    393       C
ATOM    395  CD2 PHE A  46      -3.208   7.691   3.999  1.00 16.61           C
ANISOU  395  CD2 PHE A  46     1803   2798   1711   -184     95    312       C
ATOM    396  CE1 PHE A  46      -4.776   8.779   5.989  1.00 18.24           C
ANISOU  396  CE1 PHE A  46     2142   2889   1899    206    378    558       C
ATOM    397  CE2 PHE A  46      -4.332   7.014   4.469  1.00 17.25           C
ANISOU  397  CE2 PHE A  46     1860   2992   1701   -224    -14    482       C
ATOM    398  CZ  PHE A  46      -5.108   7.576   5.449  1.00 17.63           C
ANISOU  398  CZ  PHE A  46     1913   3019   1769   -129     99    635       C
ATOM    399  N   LYS A  47      -2.051   9.523   0.313  1.00 15.95           N
ANISOU  399  N   LYS A  47     1710   2439   1912   -156    253   -208       N
ATOM    400  CA  LYS A  47      -1.901   8.562  -0.770  1.00 17.43           C
ANISOU  400  CA  LYS A  47     1856   2560   2205   -196    263   -297       C
ATOM    401  C   LYS A  47      -0.462   8.441  -1.264  1.00 17.54           C
ANISOU  401  C   LYS A  47     1885   2553   2226   -158    490   -245       C
ATOM    402  O   LYS A  47      -0.173   7.535  -2.051  1.00 20.57           O
ANISOU  402  O   LYS A  47     2469   2813   2533   -150    573   -405       O
ATOM    403  CB  LYS A  47      -2.840   8.861  -1.935  1.00 19.27           C
ANISOU  403  CB  LYS A  47     2149   2841   2331   -210     11   -350       C
ATOM    404  CG  LYS A  47      -2.653  10.201  -2.578  1.00 22.35           C
ANISOU  404  CG  LYS A  47     2687   3340   2465    -21   -248   -225       C
ATOM    405  CD  LYS A  47      -3.629  10.347  -3.734  1.00 25.64           C
ANISOU  405  CD  LYS A  47     3241   3805   2697    107   -526   -209       C
ATOM    406  CE  LYS A  47      -3.874  11.785  -4.077  1.00 28.82           C
ANISOU  406  CE  LYS A  47     3816   4218   2918    160   -697    -24       C
ATOM    407  NZ  LYS A  47      -4.953  11.870  -5.102  1.00 30.77           N
ANISOU  407  NZ  LYS A  47     4148   4418   3125    174   -706     69       N
ATOM    408  N   HIS A  48       0.453   9.284  -0.798  1.00 16.10           N
ANISOU  408  N   HIS A  48     1562   2340   2216   -182    393    110       N
ATOM    409  CA  HIS A  48       1.851   9.153  -1.176  1.00 17.54           C
ANISOU  409  CA  HIS A  48     1779   2404   2481   -119    381    266       C
ATOM    410  C   HIS A  48       2.588   8.095  -0.370  1.00 17.19           C
ANISOU  410  C   HIS A  48     1667   2492   2373    -64    380    348       C
ATOM    411  O   HIS A  48       3.745   7.796  -0.686  1.00 18.43           O
ANISOU  411  O   HIS A  48     1768   2739   2494   -102    430    398       O
ATOM    412  CB  HIS A  48       2.553  10.478  -0.930  1.00 19.16           C
ANISOU  412  CB  HIS A  48     2060   2399   2820   -189    397    225       C
ATOM    413  CG  HIS A  48       2.528  10.909   0.503  1.00 19.67           C
ANISOU  413  CG  HIS A  48     2049   2299   3127   -358    350    101       C
ATOM    414  ND1 HIS A  48       1.402  11.448   1.079  1.00 20.78           N
ANISOU  414  ND1 HIS A  48     2216   2375   3307   -223    310     50       N
ATOM    415  CD2 HIS A  48       3.455  10.852   1.488  1.00 20.41           C
ANISOU  415  CD2 HIS A  48     2173   2335   3245   -394    254    120       C
ATOM    416  CE1 HIS A  48       1.634  11.716   2.351  1.00 21.03           C
ANISOU  416  CE1 HIS A  48     2274   2337   3378   -341    140     14       C
ATOM    417  NE2 HIS A  48       2.883  11.378   2.621  1.00 21.06           N
ANISOU  417  NE2 HIS A  48     2306   2303   3391   -281    120     58       N
ATOM    418  N   LEU A  49       1.987   7.525   0.677  1.00 16.65           N
ANISOU  418  N   LEU A  49     1763   2347   2215    -10    204    362       N
ATOM    419  CA  LEU A  49       2.679   6.505   1.470  1.00 16.93           C
ANISOU  419  CA  LEU A  49     1887   2298   2249     67    186    197       C
ATOM    420  C   LEU A  49       2.943   5.254   0.628  1.00 17.94           C
ANISOU  420  C   LEU A  49     1932   2472   2413     73    -64    -61       C
ATOM    421  O   LEU A  49       2.100   4.839  -0.161  1.00 18.78           O
ANISOU  421  O   LEU A  49     2006   2598   2531     -9    -21   -160       O
ATOM    422  CB  LEU A  49       1.839   6.141   2.710  1.00 17.18           C
ANISOU  422  CB  LEU A  49     2020   2322   2184    143    297    262       C
ATOM    423  CG  LEU A  49       1.566   7.289   3.688  1.00 17.68           C
ANISOU  423  CG  LEU A  49     2051   2550   2115    110    188    270       C
ATOM    424  CD1 LEU A  49       0.538   6.844   4.763  1.00 18.53           C
ANISOU  424  CD1 LEU A  49     2399   2624   2017    -71    269    409       C
ATOM    425  CD2 LEU A  49       2.860   7.759   4.343  1.00 19.78           C
ANISOU  425  CD2 LEU A  49     2265   2916   2337    170     64     75       C
ATOM    426  N   LYS A  50       4.122   4.655   0.789  1.00 18.79           N
ANISOU  426  N   LYS A  50     2138   2503   2500    273   -170   -135       N
ATOM    427  CA  LYS A  50       4.520   3.522  -0.040  1.00 20.25           C
ANISOU  427  CA  LYS A  50     2427   2622   2647    178   -374   -105       C
ATOM    428  C   LYS A  50       4.779   2.266   0.766  1.00 20.64           C
ANISOU  428  C   LYS A  50     2514   2627   2701     69   -515   -122       C
ATOM    429  O   LYS A  50       4.315   1.189   0.393  1.00 23.99           O
ANISOU  429  O   LYS A  50     3291   2777   3046     26   -809   -195       O
ATOM    430  CB  LYS A  50       5.765   3.856  -0.875  1.00 23.39           C
ANISOU  430  CB  LYS A  50     3077   2914   2897    190   -202      7       C
ATOM    431  CG  LYS A  50       5.596   5.042  -1.805  1.00 27.00           C
ANISOU  431  CG  LYS A  50     3854   3226   3178    169   -132     68       C
ATOM    432  CD  LYS A  50       4.726   4.700  -2.971  1.00 30.06           C
ANISOU  432  CD  LYS A  50     4488   3509   3425      9   -163    169       C
ATOM    433  CE  LYS A  50       4.334   5.952  -3.762  1.00 32.57           C
ANISOU  433  CE  LYS A  50     5035   3743   3598   -136   -227    258       C
ATOM    434  NZ  LYS A  50       5.253   7.094  -3.513  1.00 34.12           N
ANISOU  434  NZ  LYS A  50     5340   3942   3684   -242   -284    330       N
ATOM    435  N   THR A  51       5.440   2.362   1.906  1.00 18.05           N
ANISOU  435  N   THR A  51     1900   2550   2410    133   -188    108       N
ATOM    436  CA  THR A  51       5.875   1.183   2.633  1.00 17.50           C
ANISOU  436  CA  THR A  51     1599   2541   2510     84    -60    203       C
ATOM    437  C   THR A  51       5.060   1.032   3.907  1.00 17.11           C
ANISOU  437  C   THR A  51     1502   2466   2533      0   -198    169       C
ATOM    438  O   THR A  51       4.477   1.990   4.429  1.00 16.72           O
ANISOU  438  O   THR A  51     1467   2462   2422    -11   -145     96       O
ATOM    439  CB  THR A  51       7.355   1.279   3.026  1.00 18.24           C
ANISOU  439  CB  THR A  51     1601   2727   2602    -20     27    168       C
ATOM    440  OG1 THR A  51       7.500   2.341   3.963  1.00 18.14           O
ANISOU  440  OG1 THR A  51     1554   2802   2535   -145     42    147       O
ATOM    441  CG2 THR A  51       8.263   1.566   1.790  1.00 18.97           C
ANISOU  441  CG2 THR A  51     1703   2865   2641    196     93    216       C
ATOM    442  N   GLU A  52       5.077  -0.189   4.439  1.00 18.35           N
ANISOU  442  N   GLU A  52     1823   2450   2700    -22   -248    330       N
ATOM    443  CA  GLU A  52       4.430  -0.426   5.732  1.00 19.69           C
ANISOU  443  CA  GLU A  52     2046   2522   2913    -93   -232    551       C
ATOM    444  C   GLU A  52       5.041   0.435   6.830  1.00 18.72           C
ANISOU  444  C   GLU A  52     1799   2640   2674      9   -304    587       C
ATOM    445  O   GLU A  52       4.320   0.954   7.680  1.00 18.39           O
ANISOU  445  O   GLU A  52     1785   2629   2572    -57   -179    653       O
ATOM    446  CB  GLU A  52       4.497  -1.904   6.100  1.00 22.94           C
ANISOU  446  CB  GLU A  52     2678   2636   3403     89   -205    628       C
ATOM    447  CG  GLU A  52       3.813  -2.230   7.402  1.00 26.86           C
ANISOU  447  CG  GLU A  52     3450   2935   3821     12    -37    708       C
ATOM    448  CD  GLU A  52       3.630  -3.720   7.620  1.00 30.84           C
ANISOU  448  CD  GLU A  52     4269   3277   4171    -46     80    771       C
ATOM    449  OE1 GLU A  52       3.834  -4.515   6.676  1.00 32.13           O
ANISOU  449  OE1 GLU A  52     4550   3336   4322    -73     84    824       O
ATOM    450  OE2 GLU A  52       3.276  -4.084   8.741  1.00 33.10           O
ANISOU  450  OE2 GLU A  52     4693   3528   4354   -136    172    793       O
ATOM    451  N   ALA A  53       6.366   0.620   6.811  1.00 18.60           N
ANISOU  451  N   ALA A  53     1690   2740   2637   -118   -351    426       N
ATOM    452  CA  ALA A  53       7.002   1.440   7.835  1.00 18.17           C
ANISOU  452  CA  ALA A  53     1528   2782   2596   -174   -473    333       C
ATOM    453  C   ALA A  53       6.532   2.885   7.752  1.00 17.50           C
ANISOU  453  C   ALA A  53     1490   2782   2379   -265   -286    344       C
ATOM    454  O   ALA A  53       6.312   3.533   8.786  1.00 18.10           O
ANISOU  454  O   ALA A  53     1721   2880   2278   -227   -254    447       O
ATOM    455  CB  ALA A  53       8.516   1.372   7.680  1.00 19.60           C
ANISOU  455  CB  ALA A  53     1791   2859   2797    -91   -567    215       C
ATOM    456  N   GLU A  54       6.379   3.424   6.530  1.00 16.26           N
ANISOU  456  N   GLU A  54     1324   2695   2161   -228   -117    360       N
ATOM    457  CA  GLU A  54       5.843   4.781   6.399  1.00 16.40           C
ANISOU  457  CA  GLU A  54     1509   2741   1979    -98     -7    376       C
ATOM    458  C   GLU A  54       4.414   4.848   6.904  1.00 15.76           C
ANISOU  458  C   GLU A  54     1499   2641   1847   -188    -39    271       C
ATOM    459  O   GLU A  54       4.006   5.828   7.552  1.00 15.69           O
ANISOU  459  O   GLU A  54     1626   2608   1729   -251     11    100       O
ATOM    460  CB  GLU A  54       5.889   5.224   4.936  1.00 16.37           C
ANISOU  460  CB  GLU A  54     1394   2926   1899   -176    118    417       C
ATOM    461  CG  GLU A  54       7.314   5.458   4.473  1.00 17.51           C
ANISOU  461  CG  GLU A  54     1428   3131   2094    -95    228    376       C
ATOM    462  CD  GLU A  54       7.472   5.406   2.965  1.00 18.60           C
ANISOU  462  CD  GLU A  54     1454   3361   2252   -316     41    285       C
ATOM    463  OE1 GLU A  54       6.481   5.273   2.209  1.00 19.81           O
ANISOU  463  OE1 GLU A  54     1660   3573   2293   -217    -40    335       O
ATOM    464  OE2 GLU A  54       8.629   5.461   2.540  1.00 19.80           O
ANISOU  464  OE2 GLU A  54     1617   3590   2315   -439     86     68       O
ATOM    465  N   MET A  55       3.629   3.815   6.614  1.00 15.22           N
ANISOU  465  N   MET A  55     1437   2550   1794   -297   -143    382       N
ATOM    466  CA  MET A  55       2.248   3.823   7.072  1.00 15.25           C
ANISOU  466  CA  MET A  55     1384   2638   1772   -337    -81    245       C
ATOM    467  C   MET A  55       2.176   3.786   8.586  1.00 15.59           C
ANISOU  467  C   MET A  55     1364   2771   1788   -254    -86    328       C
ATOM    468  O   MET A  55       1.325   4.449   9.184  1.00 16.36           O
ANISOU  468  O   MET A  55     1630   2862   1724   -195     89    406       O
ATOM    469  CB  MET A  55       1.497   2.638   6.474  1.00 15.86           C
ANISOU  469  CB  MET A  55     1679   2579   1768   -376   -110    245       C
ATOM    470  CG  MET A  55       1.313   2.782   4.971  1.00 16.12           C
ANISOU  470  CG  MET A  55     1628   2678   1819   -331   -177    144       C
ATOM    471  SD  MET A  55       0.584   1.301   4.275  1.00 17.36           S
ANISOU  471  SD  MET A  55     1774   2849   1974   -282    -43     53       S
ATOM    472  CE  MET A  55       0.644   1.679   2.557  1.00 19.95           C
ANISOU  472  CE  MET A  55     2328   3129   2121   -396     -8    -41       C
ATOM    473  N   LYS A  56       3.055   2.993   9.225  1.00 16.58           N
ANISOU  473  N   LYS A  56     1562   2836   1901   -173   -206    501       N
ATOM    474  CA  LYS A  56       3.038   2.894  10.683  1.00 19.12           C
ANISOU  474  CA  LYS A  56     1949   3095   2220   -251   -154    540       C
ATOM    475  C   LYS A  56       3.494   4.188  11.341  1.00 18.96           C
ANISOU  475  C   LYS A  56     1844   3230   2131   -325   -200    389       C
ATOM    476  O   LYS A  56       3.103   4.474  12.480  1.00 20.93           O
ANISOU  476  O   LYS A  56     2315   3454   2184   -214     78    394       O
ATOM    477  CB  LYS A  56       3.897   1.712  11.150  1.00 21.91           C
ANISOU  477  CB  LYS A  56     2395   3243   2686   -218   -269    676       C
ATOM    478  CG  LYS A  56       3.244   0.358  10.934  1.00 24.74           C
ANISOU  478  CG  LYS A  56     2795   3399   3207    -55   -364    743       C
ATOM    479  CD  LYS A  56       4.198  -0.784  11.191  1.00 28.51           C
ANISOU  479  CD  LYS A  56     3451   3653   3730     16   -287    670       C
ATOM    480  CE  LYS A  56       3.453  -2.095  11.195  1.00 30.74           C
ANISOU  480  CE  LYS A  56     3806   3807   4070    102   -216    657       C
ATOM    481  NZ  LYS A  56       4.385  -3.261  11.094  1.00 32.06           N
ANISOU  481  NZ  LYS A  56     3971   3965   4247    172   -208    604       N
ATOM    482  N   ALA A  57       4.337   4.959  10.673  1.00 17.94           N
ANISOU  482  N   ALA A  57     1610   3061   2143   -170   -332    247       N
ATOM    483  CA  ALA A  57       4.821   6.214  11.217  1.00 18.51           C
ANISOU  483  CA  ALA A  57     1647   3127   2257   -326   -257     92       C
ATOM    484  C   ALA A  57       3.865   7.373  10.967  1.00 18.46           C
ANISOU  484  C   ALA A  57     1736   3072   2205   -536   -271     35       C
ATOM    485  O   ALA A  57       4.127   8.472  11.482  1.00 21.02           O
ANISOU  485  O   ALA A  57     2104   3308   2576   -467   -516    -83       O
ATOM    486  CB  ALA A  57       6.173   6.504  10.581  1.00 19.51           C
ANISOU  486  CB  ALA A  57     1731   3272   2412   -287   -270     97       C
ATOM    487  N   SER A  58       2.781   7.174  10.191  1.00 16.76           N
ANISOU  487  N   SER A  58     1508   2889   1972   -422    -98    150       N
ATOM    488  CA  SER A  58       1.892   8.269   9.828  1.00 16.83           C
ANISOU  488  CA  SER A  58     1691   2708   1997   -482     36    123       C
ATOM    489  C   SER A  58       0.863   8.501  10.935  1.00 16.85           C
ANISOU  489  C   SER A  58     1696   2668   2038   -562      1     41       C
ATOM    490  O   SER A  58      -0.049   7.681  11.147  1.00 16.83           O
ANISOU  490  O   SER A  58     1809   2596   1989   -527    122    173       O
ATOM    491  CB  SER A  58       1.184   7.923   8.526  1.00 16.69           C
ANISOU  491  CB  SER A  58     1780   2561   2000   -418     43    231       C
ATOM    492  OG  SER A  58       0.175   8.882   8.269  1.00 16.89           O
ANISOU  492  OG  SER A  58     1759   2553   2103   -425     -2    213       O
ATOM    493  N   GLU A  59       0.924   9.676  11.552  1.00 17.39           N
ANISOU  493  N   GLU A  59     1625   2763   2221   -679    -14   -105       N
ATOM    494  CA  GLU A  59      -0.100  10.019  12.523  1.00 19.00           C
ANISOU  494  CA  GLU A  59     1917   2936   2368   -745    -68   -337       C
ATOM    495  C   GLU A  59      -1.450  10.226  11.861  1.00 17.54           C
ANISOU  495  C   GLU A  59     1737   2686   2243   -635    -89   -166       C
ATOM    496  O   GLU A  59      -2.481   9.878  12.448  1.00 17.56           O
ANISOU  496  O   GLU A  59     1828   2668   2178   -684    -54   -152       O
ATOM    497  CB  GLU A  59       0.329  11.272  13.291  1.00 23.78           C
ANISOU  497  CB  GLU A  59     2816   3483   2736   -744    -93   -598       C
ATOM    498  CG  GLU A  59      -0.505  11.584  14.525  1.00 29.39           C
ANISOU  498  CG  GLU A  59     3919   4082   3165   -603     53   -714       C
ATOM    499  CD  GLU A  59      -0.147  10.704  15.731  1.00 34.47           C
ANISOU  499  CD  GLU A  59     4932   4638   3526   -445    166   -779       C
ATOM    500  OE1 GLU A  59       0.761   9.845  15.621  1.00 36.36           O
ANISOU  500  OE1 GLU A  59     5326   4829   3659   -406     59   -801       O
ATOM    501  OE2 GLU A  59      -0.759  10.889  16.803  1.00 37.03           O
ANISOU  501  OE2 GLU A  59     5387   4906   3777   -450    213   -704       O
ATOM    502  N   ASP A  60      -1.454  10.733  10.624  1.00 17.31           N
ANISOU  502  N   ASP A  60     1810   2482   2284   -674    -76    -20       N
ATOM    503  CA  ASP A  60      -2.711  10.944   9.915  1.00 17.04           C
ANISOU  503  CA  ASP A  60     1924   2259   2293   -637    -28    166       C
ATOM    504  C   ASP A  60      -3.415   9.634   9.615  1.00 15.43           C
ANISOU  504  C   ASP A  60     1706   2083   2075   -422     83    191       C
ATOM    505  O   ASP A  60      -4.639   9.556   9.749  1.00 15.40           O
ANISOU  505  O   ASP A  60     1672   2084   2096   -334    -53    182       O
ATOM    506  CB  ASP A  60      -2.444  11.694   8.615  1.00 19.32           C
ANISOU  506  CB  ASP A  60     2532   2305   2503   -644    -84    265       C
ATOM    507  CG  ASP A  60      -2.269  13.200   8.831  1.00 21.78           C
ANISOU  507  CG  ASP A  60     2959   2475   2842   -641   -173    176       C
ATOM    508  OD1 ASP A  60      -2.573  13.703   9.941  1.00 23.74           O
ANISOU  508  OD1 ASP A  60     3349   2549   3120   -521   -204      2       O
ATOM    509  OD2 ASP A  60      -1.847  13.869   7.869  1.00 23.13           O
ANISOU  509  OD2 ASP A  60     3148   2551   3089   -745   -281    188       O
ATOM    510  N   LEU A  61      -2.676   8.618   9.155  1.00 14.24           N
ANISOU  510  N   LEU A  61     1505   1958   1948   -403    -12    301       N
ATOM    511  CA  LEU A  61      -3.292   7.326   8.914  1.00 13.60           C
ANISOU  511  CA  LEU A  61     1491   1984   1692   -365     70    284       C
ATOM    512  C   LEU A  61      -3.891   6.771  10.207  1.00 12.86           C
ANISOU  512  C   LEU A  61     1363   1996   1526   -170     39    152       C
ATOM    513  O   LEU A  61      -5.025   6.273  10.218  1.00 12.98           O
ANISOU  513  O   LEU A  61     1381   2026   1524   -170     99    140       O
ATOM    514  CB  LEU A  61      -2.247   6.389   8.301  1.00 13.80           C
ANISOU  514  CB  LEU A  61     1483   2080   1680   -435     79    165       C
ATOM    515  CG  LEU A  61      -2.733   5.004   7.909  1.00 14.27           C
ANISOU  515  CG  LEU A  61     1659   2202   1563   -259     78     90       C
ATOM    516  CD1 LEU A  61      -1.813   4.482   6.822  1.00 14.91           C
ANISOU  516  CD1 LEU A  61     1631   2457   1578   -176    152    -14       C
ATOM    517  CD2 LEU A  61      -2.792   3.996   9.080  1.00 15.17           C
ANISOU  517  CD2 LEU A  61     1760   2336   1668   -211     71    158       C
ATOM    518  N   LYS A  62      -3.162   6.895  11.321  1.00 13.54           N
ANISOU  518  N   LYS A  62     1507   2125   1514   -309    -20    101       N
ATOM    519  CA  LYS A  62      -3.686   6.424  12.599  1.00 13.97           C
ANISOU  519  CA  LYS A  62     1517   2239   1553   -296   -114     48       C
ATOM    520  C   LYS A  62      -4.975   7.150  12.975  1.00 13.41           C
ANISOU  520  C   LYS A  62     1522   1993   1580   -232    -83     17       C
ATOM    521  O   LYS A  62      -5.953   6.522  13.404  1.00 13.55           O
ANISOU  521  O   LYS A  62     1571   1925   1651   -220    -73    197       O
ATOM    522  CB  LYS A  62      -2.610   6.647  13.679  1.00 15.97           C
ANISOU  522  CB  LYS A  62     1841   2641   1587   -314   -265    187       C
ATOM    523  CG  LYS A  62      -3.034   6.155  15.044  1.00 18.40           C
ANISOU  523  CG  LYS A  62     2146   3085   1759   -279   -520    322       C
ATOM    524  CD  LYS A  62      -2.087   6.593  16.157  1.00 23.39           C
ANISOU  524  CD  LYS A  62     2976   3652   2258   -229   -552    224       C
ATOM    525  CE  LYS A  62      -0.682   6.220  15.868  1.00 27.41           C
ANISOU  525  CE  LYS A  62     3737   4009   2670   -217   -817    174       C
ATOM    526  NZ  LYS A  62       0.249   6.852  16.859  1.00 29.22           N
ANISOU  526  NZ  LYS A  62     4013   4193   2895   -401  -1000    160       N
ATOM    527  N   LYS A  63      -5.017   8.475  12.811  1.00 13.72           N
ANISOU  527  N   LYS A  63     1551   1966   1697   -317   -173    -62       N
ATOM    528  CA  LYS A  63      -6.218   9.224  13.177  1.00 14.16           C
ANISOU  528  CA  LYS A  63     1745   1857   1780   -345     -2   -180       C
ATOM    529  C   LYS A  63      -7.403   8.843  12.294  1.00 12.60           C
ANISOU  529  C   LYS A  63     1522   1748   1519   -293     57    -67       C
ATOM    530  O   LYS A  63      -8.531   8.712  12.787  1.00 13.05           O
ANISOU  530  O   LYS A  63     1658   1773   1526   -116    193    -65       O
ATOM    531  CB  LYS A  63      -5.957  10.723  13.088  1.00 17.38           C
ANISOU  531  CB  LYS A  63     2345   2039   2219   -480   -164   -345       C
ATOM    532  CG  LYS A  63      -4.995  11.215  14.143  1.00 21.24           C
ANISOU  532  CG  LYS A  63     3060   2247   2765   -705   -292   -346       C
ATOM    533  CD  LYS A  63      -5.100  12.753  14.289  1.00 26.63           C
ANISOU  533  CD  LYS A  63     4109   2681   3329   -639   -305   -244       C
ATOM    534  CE  LYS A  63      -4.002  13.487  13.595  1.00 31.20           C
ANISOU  534  CE  LYS A  63     4988   3132   3735   -388   -211   -150       C
ATOM    535  NZ  LYS A  63      -4.277  14.959  13.597  1.00 33.08           N
ANISOU  535  NZ  LYS A  63     5382   3286   3902   -498   -170   -172       N
ATOM    536  N   VAL A  64      -7.167   8.641  10.991  1.00 12.20           N
ANISOU  536  N   VAL A  64     1517   1620   1498   -194     -4     -2       N
ATOM    537  CA  VAL A  64      -8.243   8.241  10.086  1.00 11.96           C
ANISOU  537  CA  VAL A  64     1460   1675   1409   -261     43    120       C
ATOM    538  C   VAL A  64      -8.763   6.860  10.458  1.00 11.34           C
ANISOU  538  C   VAL A  64     1365   1495   1449    -24    110     64       C
ATOM    539  O   VAL A  64      -9.976   6.623  10.456  1.00 12.03           O
ANISOU  539  O   VAL A  64     1417   1634   1519   -120     66    102       O
ATOM    540  CB  VAL A  64      -7.730   8.348   8.639  1.00 12.62           C
ANISOU  540  CB  VAL A  64     1589   1809   1399    -94     97    165       C
ATOM    541  CG1 VAL A  64      -8.673   7.642   7.684  1.00 13.64           C
ANISOU  541  CG1 VAL A  64     1730   2030   1424    -33    -32     54       C
ATOM    542  CG2 VAL A  64      -7.629   9.826   8.278  1.00 14.02           C
ANISOU  542  CG2 VAL A  64     1941   1906   1479    -66     97    335       C
ATOM    543  N   GLY A  65      -7.874   5.949  10.854  1.00 11.54           N
ANISOU  543  N   GLY A  65     1404   1485   1495    -89     72    100       N
ATOM    544  CA  GLY A  65      -8.328   4.644  11.312  1.00 11.88           C
ANISOU  544  CA  GLY A  65     1476   1511   1526    -50    122    197       C
ATOM    545  C   GLY A  65      -9.157   4.733  12.584  1.00 11.71           C
ANISOU  545  C   GLY A  65     1317   1626   1504    -23     50    220       C
ATOM    546  O   GLY A  65     -10.177   4.043  12.725  1.00 12.06           O
ANISOU  546  O   GLY A  65     1298   1597   1688    -29     98    163       O
ATOM    547  N   VAL A  66      -8.743   5.578  13.531  1.00 12.26           N
ANISOU  547  N   VAL A  66     1540   1737   1382    -70     45    145       N
ATOM    548  CA  VAL A  66      -9.515   5.739  14.769  1.00 12.21           C
ANISOU  548  CA  VAL A  66     1504   1776   1361   -201   -118     86       C
ATOM    549  C   VAL A  66     -10.904   6.276  14.463  1.00 11.68           C
ANISOU  549  C   VAL A  66     1462   1601   1377   -149     13    173       C
ATOM    550  O   VAL A  66     -11.894   5.804  15.028  1.00 12.22           O
ANISOU  550  O   VAL A  66     1485   1706   1452   -147     65     30       O
ATOM    551  CB  VAL A  66      -8.764   6.637  15.770  1.00 13.78           C
ANISOU  551  CB  VAL A  66     1682   2110   1442   -272   -187     29       C
ATOM    552  CG1 VAL A  66      -9.698   7.089  16.908  1.00 15.36           C
ANISOU  552  CG1 VAL A  66     1887   2373   1577   -143    -29   -112       C
ATOM    553  CG2 VAL A  66      -7.519   5.918  16.292  1.00 15.01           C
ANISOU  553  CG2 VAL A  66     1771   2321   1611   -196   -295    235       C
ATOM    554  N   THR A  67     -11.009   7.266  13.571  1.00 11.70           N
ANISOU  554  N   THR A  67     1480   1607   1360    -57    -17    110       N
ATOM    555  CA  THR A  67     -12.309   7.823  13.262  1.00 11.92           C
ANISOU  555  CA  THR A  67     1510   1512   1507    -68   -161    154       C
ATOM    556  C   THR A  67     -13.212   6.768  12.640  1.00 11.08           C
ANISOU  556  C   THR A  67     1451   1399   1360    -35    -70    176       C
ATOM    557  O   THR A  67     -14.388   6.641  13.024  1.00 11.28           O
ANISOU  557  O   THR A  67     1409   1458   1418      9    113    103       O
ATOM    558  CB  THR A  67     -12.103   8.989  12.302  1.00 12.82           C
ANISOU  558  CB  THR A  67     1791   1374   1708    -42   -131    118       C
ATOM    559  OG1 THR A  67     -11.403  10.011  13.024  1.00 15.88           O
ANISOU  559  OG1 THR A  67     2352   1674   2008   -323   -323     56       O
ATOM    560  CG2 THR A  67     -13.425   9.494  11.737  1.00 12.93           C
ANISOU  560  CG2 THR A  67     1762   1423   1728    205      9     79       C
ATOM    561  N   ALA A  68     -12.689   5.964  11.707  1.00 11.19           N
ANISOU  561  N   ALA A  68     1570   1419   1262    -25    -24     48       N
ATOM    562  CA  ALA A  68     -13.526   4.937  11.083  1.00 11.16           C
ANISOU  562  CA  ALA A  68     1585   1457   1200     -9    140    -11       C
ATOM    563  C   ALA A  68     -14.023   3.928  12.109  1.00 10.44           C
ANISOU  563  C   ALA A  68     1307   1466   1193    112     69     -9       C
ATOM    564  O   ALA A  68     -15.207   3.553  12.120  1.00 10.70           O
ANISOU  564  O   ALA A  68     1307   1539   1220      8     63     40       O
ATOM    565  CB  ALA A  68     -12.765   4.233   9.966  1.00 12.15           C
ANISOU  565  CB  ALA A  68     1821   1631   1166    -22    276     42       C
ATOM    566  N   LEU A  69     -13.110   3.443  12.959  1.00 10.29           N
ANISOU  566  N   LEU A  69     1355   1360   1195      2    -63     64       N
ATOM    567  CA  LEU A  69     -13.523   2.445  13.942  1.00 10.78           C
ANISOU  567  CA  LEU A  69     1390   1470   1237     20    -38    103       C
ATOM    568  C   LEU A  69     -14.494   3.025  14.956  1.00 10.83           C
ANISOU  568  C   LEU A  69     1227   1670   1217   -132     40    -24       C
ATOM    569  O   LEU A  69     -15.386   2.318  15.442  1.00 11.77           O
ANISOU  569  O   LEU A  69     1430   1665   1376   -128     71     68       O
ATOM    570  CB  LEU A  69     -12.327   1.811  14.640  1.00 11.70           C
ANISOU  570  CB  LEU A  69     1426   1596   1421    153    -22     48       C
ATOM    571  CG  LEU A  69     -11.453   0.948  13.735  1.00 13.49           C
ANISOU  571  CG  LEU A  69     1561   1728   1836    127    -82    -63       C
ATOM    572  CD1 LEU A  69     -10.433   0.205  14.568  1.00 14.31           C
ANISOU  572  CD1 LEU A  69     1579   1834   2024    208   -126     -4       C
ATOM    573  CD2 LEU A  69     -12.239  -0.041  12.834  1.00 15.82           C
ANISOU  573  CD2 LEU A  69     2008   1910   2092     86    -74   -186       C
ATOM    574  N   THR A  70     -14.324   4.299  15.309  1.00 11.17           N
ANISOU  574  N   THR A  70     1318   1691   1235   -139     11   -167       N
ATOM    575  CA  THR A  70     -15.254   4.952  16.230  1.00 12.07           C
ANISOU  575  CA  THR A  70     1393   1800   1394   -126     41   -251       C
ATOM    576  C   THR A  70     -16.653   4.978  15.640  1.00 10.86           C
ANISOU  576  C   THR A  70     1349   1486   1290    -24     91   -171       C
ATOM    577  O   THR A  70     -17.626   4.653  16.327  1.00 11.24           O
ANISOU  577  O   THR A  70     1435   1510   1326     12     72     22       O
ATOM    578  CB  THR A  70     -14.749   6.363  16.554  1.00 14.33           C
ANISOU  578  CB  THR A  70     1584   2193   1668   -208     89   -693       C
ATOM    579  OG1 THR A  70     -13.488   6.237  17.208  1.00 16.17           O
ANISOU  579  OG1 THR A  70     1782   2640   1721   -482     58   -646       O
ATOM    580  CG2 THR A  70     -15.697   7.087  17.481  1.00 16.44           C
ANISOU  580  CG2 THR A  70     1979   2337   1930   -208    286   -759       C
ATOM    581  N   ALA A  71     -16.772   5.378  14.376  1.00 10.45           N
ANISOU  581  N   ALA A  71     1447   1267   1257     60     27      4       N
ATOM    582  CA  ALA A  71     -18.074   5.419  13.737  1.00 10.17           C
ANISOU  582  CA  ALA A  71     1306   1259   1301     19     43     48       C
ATOM    583  C   ALA A  71     -18.660   4.019  13.598  1.00 10.25           C
ANISOU  583  C   ALA A  71     1357   1243   1295     46     73     36       C
ATOM    584  O   ALA A  71     -19.870   3.822  13.824  1.00 11.09           O
ANISOU  584  O   ALA A  71     1423   1319   1472    -10    158    129       O
ATOM    585  CB  ALA A  71     -17.976   6.113  12.394  1.00 11.14           C
ANISOU  585  CB  ALA A  71     1495   1376   1360     31     28    192       C
ATOM    586  N   LEU A  72     -17.840   3.041  13.199  1.00 10.10           N
ANISOU  586  N   LEU A  72     1468   1166   1202    -49     21     70       N
ATOM    587  CA  LEU A  72     -18.351   1.686  13.058  1.00 10.75           C
ANISOU  587  CA  LEU A  72     1566   1192   1327    -35    174      1       C
ATOM    588  C   LEU A  72     -18.871   1.167  14.395  1.00 10.70           C
ANISOU  588  C   LEU A  72     1514   1215   1336    -32    137     48       C
ATOM    589  O   LEU A  72     -19.953   0.571  14.470  1.00 11.20           O
ANISOU  589  O   LEU A  72     1487   1292   1477    -79    199     25       O
ATOM    590  CB  LEU A  72     -17.254   0.765  12.495  1.00 11.05           C
ANISOU  590  CB  LEU A  72     1672   1179   1347    -21    223    -42       C
ATOM    591  CG  LEU A  72     -17.690  -0.689  12.309  1.00 12.32           C
ANISOU  591  CG  LEU A  72     1892   1320   1470    -84    134     50       C
ATOM    592  CD1 LEU A  72     -18.911  -0.823  11.421  1.00 13.94           C
ANISOU  592  CD1 LEU A  72     1985   1694   1618   -305     -5   -107       C
ATOM    593  CD2 LEU A  72     -16.513  -1.490  11.747  1.00 13.29           C
ANISOU  593  CD2 LEU A  72     2226   1389   1437    257    294     30       C
ATOM    594  N   GLY A  73     -18.118   1.400  15.471  1.00 10.67           N
ANISOU  594  N   GLY A  73     1544   1332   1179     -3     73    167       N
ATOM    595  CA  GLY A  73     -18.572   0.971  16.786  1.00 11.13           C
ANISOU  595  CA  GLY A  73     1544   1455   1230    -27    164    205       C
ATOM    596  C   GLY A  73     -19.898   1.599  17.176  1.00 11.18           C
ANISOU  596  C   GLY A  73     1571   1511   1166    -13    191    130       C
ATOM    597  O   GLY A  73     -20.781   0.921  17.718  1.00 11.86           O
ANISOU  597  O   GLY A  73     1634   1614   1259    -90    123    158       O
ATOM    598  N   ALA A  74     -20.056   2.902  16.928  1.00 11.04           N
ANISOU  598  N   ALA A  74     1526   1358   1311    132    106     40       N
ATOM    599  CA  ALA A  74     -21.310   3.562  17.268  1.00 11.76           C
ANISOU  599  CA  ALA A  74     1513   1405   1549    122     90      6       C
ATOM    600  C   ALA A  74     -22.466   2.944  16.502  1.00 11.33           C
ANISOU  600  C   ALA A  74     1437   1380   1486     72    221     68       C
ATOM    601  O   ALA A  74     -23.573   2.764  17.041  1.00 12.39           O
ANISOU  601  O   ALA A  74     1629   1572   1506     38    246     90       O
ATOM    602  CB  ALA A  74     -21.197   5.068  16.991  1.00 12.95           C
ANISOU  602  CB  ALA A  74     1752   1453   1716    186    176     34       C
ATOM    603  N   ILE A  75     -22.237   2.625  15.232  1.00 11.17           N
ANISOU  603  N   ILE A  75     1433   1285   1526    -96    145    -38       N
ATOM    604  CA  ILE A  75     -23.266   2.009  14.415  1.00 11.26           C
ANISOU  604  CA  ILE A  75     1401   1452   1427   -152    124     49       C
ATOM    605  C   ILE A  75     -23.576   0.596  14.901  1.00 11.21           C
ANISOU  605  C   ILE A  75     1366   1461   1430   -152    109    105       C
ATOM    606  O   ILE A  75     -24.741   0.212  15.034  1.00 12.06           O
ANISOU  606  O   ILE A  75     1524   1533   1525   -209     25    117       O
ATOM    607  CB  ILE A  75     -22.854   2.069  12.937  1.00 12.16           C
ANISOU  607  CB  ILE A  75     1515   1631   1475   -119    130    151       C
ATOM    608  CG1 ILE A  75     -22.961   3.534  12.453  1.00 13.91           C
ANISOU  608  CG1 ILE A  75     1835   1707   1741    -61     81    446       C
ATOM    609  CG2 ILE A  75     -23.679   1.118  12.077  1.00 12.97           C
ANISOU  609  CG2 ILE A  75     1672   1846   1410   -228    -86     35       C
ATOM    610  CD1 ILE A  75     -22.226   3.815  11.167  1.00 15.49           C
ANISOU  610  CD1 ILE A  75     2112   1887   1888    -31     82    510       C
ATOM    611  N   LEU A  76     -22.555  -0.215  15.165  1.00 10.71           N
ANISOU  611  N   LEU A  76     1418   1267   1384   -152     26     77       N
ATOM    612  CA  LEU A  76     -22.788  -1.592  15.630  1.00 11.75           C
ANISOU  612  CA  LEU A  76     1582   1395   1488    -71     63    136       C
ATOM    613  C   LEU A  76     -23.575  -1.601  16.933  1.00 11.59           C
ANISOU  613  C   LEU A  76     1543   1387   1475    -82    195    220       C
ATOM    614  O   LEU A  76     -24.433  -2.465  17.146  1.00 12.45           O
ANISOU  614  O   LEU A  76     1735   1419   1578   -171    181    159       O
ATOM    615  CB  LEU A  76     -21.453  -2.314  15.812  1.00 12.21           C
ANISOU  615  CB  LEU A  76     1686   1421   1534     46    192    111       C
ATOM    616  CG  LEU A  76     -20.655  -2.605  14.545  1.00 13.23           C
ANISOU  616  CG  LEU A  76     1745   1540   1743   -112    312     11       C
ATOM    617  CD1 LEU A  76     -19.300  -3.223  14.918  1.00 14.10           C
ANISOU  617  CD1 LEU A  76     1802   1564   1993    -48    269      2       C
ATOM    618  CD2 LEU A  76     -21.439  -3.498  13.579  1.00 14.73           C
ANISOU  618  CD2 LEU A  76     2082   1652   1863   -357    271    -54       C
ATOM    619  N   LYS A  77     -23.326  -0.642  17.824  1.00 11.54           N
ANISOU  619  N   LYS A  77     1523   1526   1336     75    140    176       N
ATOM    620  CA  LYS A  77     -24.040  -0.620  19.102  1.00 12.42           C
ANISOU  620  CA  LYS A  77     1649   1616   1452    -50     52    161       C
ATOM    621  C   LYS A  77     -25.527  -0.341  18.932  1.00 12.68           C
ANISOU  621  C   LYS A  77     1687   1590   1540     15     54    165       C
ATOM    622  O   LYS A  77     -26.290  -0.626  19.858  1.00 14.12           O
ANISOU  622  O   LYS A  77     1782   1995   1586   -118    215    128       O
ATOM    623  CB  LYS A  77     -23.403   0.401  20.019  1.00 13.01           C
ANISOU  623  CB  LYS A  77     1685   1720   1539    -64     38     29       C
ATOM    624  CG  LYS A  77     -22.018  -0.050  20.488  1.00 13.59           C
ANISOU  624  CG  LYS A  77     1756   1788   1618      2    -45     65       C
ATOM    625  CD  LYS A  77     -21.266   1.061  21.196  1.00 15.01           C
ANISOU  625  CD  LYS A  77     1912   2105   1687     45   -173    -24       C
ATOM    626  CE  LYS A  77     -19.815   0.664  21.372  1.00 15.70           C
ANISOU  626  CE  LYS A  77     1928   2234   1805    -90   -232    -40       C
ATOM    627  NZ  LYS A  77     -19.088   1.664  22.153  1.00 16.77           N
ANISOU  627  NZ  LYS A  77     2060   2505   1807   -120   -321    -86       N
ATOM    628  N   LYS A  78     -25.965   0.161  17.761  1.00 12.58           N
ANISOU  628  N   LYS A  78     1568   1548   1663     -9    -35     62       N
ATOM    629  CA  LYS A  78     -27.384   0.313  17.473  1.00 12.95           C
ANISOU  629  CA  LYS A  78     1508   1551   1863    -81     67    119       C
ATOM    630  C   LYS A  78     -28.051  -0.987  17.083  1.00 13.69           C
ANISOU  630  C   LYS A  78     1551   1553   2097   -106     90     95       C
ATOM    631  O   LYS A  78     -29.280  -1.021  16.990  1.00 15.02           O
ANISOU  631  O   LYS A  78     1627   1706   2374   -139     35     47       O
ATOM    632  CB  LYS A  78     -27.610   1.326  16.373  1.00 13.73           C
ANISOU  632  CB  LYS A  78     1783   1517   1919     90    -34    125       C
ATOM    633  CG  LYS A  78     -27.062   2.725  16.636  1.00 15.46           C
ANISOU  633  CG  LYS A  78     2024   1646   2205     15   -136    178       C
ATOM    634  CD  LYS A  78     -27.521   3.343  17.913  1.00 17.05           C
ANISOU  634  CD  LYS A  78     2265   1809   2405    138    -63     40       C
ATOM    635  CE  LYS A  78     -29.011   3.468  18.052  1.00 17.88           C
ANISOU  635  CE  LYS A  78     2310   2053   2430    -35    203    -22       C
ATOM    636  NZ  LYS A  78     -29.672   4.351  17.046  1.00 19.03           N
ANISOU  636  NZ  LYS A  78     2453   2233   2546    -12    205     -4       N
ATOM    637  N   LYS A  79     -27.292  -2.070  16.912  1.00 14.16           N
ANISOU  637  N   LYS A  79     1763   1474   2142   -162     49     65       N
ATOM    638  CA  LYS A  79     -27.856  -3.408  16.653  1.00 15.47           C
ANISOU  638  CA  LYS A  79     1904   1673   2302   -271   -192     65       C
ATOM    639  C   LYS A  79     -28.839  -3.373  15.489  1.00 16.25           C
ANISOU  639  C   LYS A  79     1948   1706   2519   -322   -276    -61       C
ATOM    640  O   LYS A  79     -29.949  -3.913  15.560  1.00 17.25           O
ANISOU  640  O   LYS A  79     1928   1846   2779   -332   -316   -147       O
ATOM    641  CB  LYS A  79     -28.475  -4.037  17.910  1.00 16.67           C
ANISOU  641  CB  LYS A  79     2025   1991   2317   -189     89    166       C
ATOM    642  CG  LYS A  79     -27.443  -4.203  19.009  1.00 18.04           C
ANISOU  642  CG  LYS A  79     2263   2220   2372   -361    331    239       C
ATOM    643  CD  LYS A  79     -27.946  -5.005  20.191  1.00 21.80           C
ANISOU  643  CD  LYS A  79     2910   2772   2600   -201    445    220       C
ATOM    644  CE  LYS A  79     -29.054  -4.351  20.910  1.00 25.35           C
ANISOU  644  CE  LYS A  79     3621   3196   2814    -66    523    114       C
ATOM    645  NZ  LYS A  79     -29.483  -5.317  21.974  1.00 26.69           N
ANISOU  645  NZ  LYS A  79     3847   3443   2851      2    706    124       N
ATOM    646  N   GLY A  80     -28.442  -2.712  14.403  1.00 16.37           N
ANISOU  646  N   GLY A  80     2044   1693   2484     49   -428    -39       N
ATOM    647  CA  GLY A  80     -29.281  -2.711  13.233  1.00 16.87           C
ANISOU  647  CA  GLY A  80     1988   1924   2498    -69   -303     53       C
ATOM    648  C   GLY A  80     -30.196  -1.524  13.127  1.00 17.04           C
ANISOU  648  C   GLY A  80     1806   2151   2515    -84   -192    243       C
ATOM    649  O   GLY A  80     -30.643  -1.215  12.013  1.00 19.17           O
ANISOU  649  O   GLY A  80     2256   2416   2613     76   -314    413       O
ATOM    650  N   HIS A  81     -30.507  -0.841  14.240  1.00 16.88           N
ANISOU  650  N   HIS A  81     1780   2121   2511     71    167    295       N
ATOM    651  CA  HIS A  81     -31.399   0.328  14.226  1.00 17.05           C
ANISOU  651  CA  HIS A  81     1644   2275   2558     25    381    423       C
ATOM    652  C   HIS A  81     -30.556   1.587  14.079  1.00 14.70           C
ANISOU  652  C   HIS A  81     1387   2058   2141     67    129    139       C
ATOM    653  O   HIS A  81     -30.443   2.422  14.983  1.00 15.85           O
ANISOU  653  O   HIS A  81     1593   2308   2122     64    141   -171       O
ATOM    654  CB  HIS A  81     -32.222   0.390  15.505  1.00 21.98           C
ANISOU  654  CB  HIS A  81     2403   2742   3206   -120    634    625       C
ATOM    655  CG  HIS A  81     -33.015  -0.840  15.763  1.00 26.71           C
ANISOU  655  CG  HIS A  81     2986   3323   3840   -274    574    768       C
ATOM    656  ND1 HIS A  81     -34.299  -1.002  15.291  1.00 29.58           N
ANISOU  656  ND1 HIS A  81     3425   3637   4177   -397    391    813       N
ATOM    657  CD2 HIS A  81     -32.718  -1.964  16.452  1.00 28.95           C
ANISOU  657  CD2 HIS A  81     3373   3541   4085   -451    515    829       C
ATOM    658  CE1 HIS A  81     -34.761  -2.176  15.679  1.00 30.63           C
ANISOU  658  CE1 HIS A  81     3667   3735   4235   -473    450    937       C
ATOM    659  NE2 HIS A  81     -33.823  -2.779  16.387  1.00 30.50           N
ANISOU  659  NE2 HIS A  81     3585   3766   4239   -504    482    865       N
ATOM    660  N   HIS A  82     -29.891   1.674  12.925  1.00 13.89           N
ANISOU  660  N   HIS A  82     1517   1915   1845   -202    117     70       N
ATOM    661  CA  HIS A  82     -28.804   2.622  12.718  1.00 13.39           C
ANISOU  661  CA  HIS A  82     1528   1848   1714   -143     46    -86       C
ATOM    662  C   HIS A  82     -29.103   3.599  11.592  1.00 12.83           C
ANISOU  662  C   HIS A  82     1380   1772   1723     -3     21   -155       C
ATOM    663  O   HIS A  82     -28.164   4.187  11.043  1.00 13.12           O
ANISOU  663  O   HIS A  82     1366   1750   1869   -123    188   -198       O
ATOM    664  CB  HIS A  82     -27.480   1.898  12.461  1.00 13.28           C
ANISOU  664  CB  HIS A  82     1555   1788   1704     29     -6   -172       C
ATOM    665  CG  HIS A  82     -27.534   0.904  11.350  1.00 13.18           C
ANISOU  665  CG  HIS A  82     1562   1729   1716    -33     11    -28       C
ATOM    666  ND1 HIS A  82     -26.967  -0.349  11.448  1.00 14.95           N
ANISOU  666  ND1 HIS A  82     2061   1895   1722    -72    -83     74       N
ATOM    667  CD2 HIS A  82     -28.108   0.966  10.125  1.00 13.35           C
ANISOU  667  CD2 HIS A  82     1684   1722   1665    -68    124   -179       C
ATOM    668  CE1 HIS A  82     -27.177  -1.012  10.320  1.00 14.46           C
ANISOU  668  CE1 HIS A  82     2059   1802   1634   -286   -196     13       C
ATOM    669  NE2 HIS A  82     -27.899  -0.248   9.512  1.00 13.83           N
ANISOU  669  NE2 HIS A  82     1853   1755   1649   -294    -21    -57       N
ATOM    670  N   GLU A  83     -30.382   3.815  11.239  1.00 13.43           N
ANISOU  670  N   GLU A  83     1506   1835   1763    -57    -81    -82       N
ATOM    671  CA  GLU A  83     -30.671   4.688  10.104  1.00 13.96           C
ANISOU  671  CA  GLU A  83     1462   2019   1824   -100    -71    -84       C
ATOM    672  C   GLU A  83     -30.044   6.081  10.261  1.00 13.40           C
ANISOU  672  C   GLU A  83     1536   1859   1696    -71     99   -145       C
ATOM    673  O   GLU A  83     -29.412   6.590   9.325  1.00 13.71           O
ANISOU  673  O   GLU A  83     1708   1871   1630    -22     98    -92       O
ATOM    674  CB  GLU A  83     -32.175   4.794   9.925  1.00 15.90           C
ANISOU  674  CB  GLU A  83     1484   2520   2038     99   -133      6       C
ATOM    675  CG  GLU A  83     -32.623   5.779   8.894  1.00 17.44           C
ANISOU  675  CG  GLU A  83     1592   2861   2174    155    -63     76       C
ATOM    676  CD  GLU A  83     -32.321   5.357   7.454  1.00 19.22           C
ANISOU  676  CD  GLU A  83     1757   3296   2248    190    -50    207       C
ATOM    677  OE1 GLU A  83     -31.900   4.213   7.170  1.00 19.63           O
ANISOU  677  OE1 GLU A  83     1889   3419   2152     87   -154     93       O
ATOM    678  OE2 GLU A  83     -32.502   6.211   6.600  1.00 20.72           O
ANISOU  678  OE2 GLU A  83     2038   3484   2350    394    125    276       O
ATOM    679  N   ALA A  84     -30.266   6.744  11.392  1.00 13.74           N
ANISOU  679  N   ALA A  84     1557   1993   1672    -21     21   -240       N
ATOM    680  CA  ALA A  84     -29.762   8.109  11.551  1.00 13.71           C
ANISOU  680  CA  ALA A  84     1677   1924   1607    -41    196   -246       C
ATOM    681  C   ALA A  84     -28.248   8.151  11.552  1.00 13.55           C
ANISOU  681  C   ALA A  84     1691   1770   1689   -110    218   -266       C
ATOM    682  O   ALA A  84     -27.641   9.094  11.037  1.00 14.86           O
ANISOU  682  O   ALA A  84     1980   1723   1944     27    347   -206       O
ATOM    683  CB  ALA A  84     -30.306   8.733  12.842  1.00 14.23           C
ANISOU  683  CB  ALA A  84     1726   2029   1651    236     66   -159       C
ATOM    684  N   GLU A  85     -27.617   7.144  12.138  1.00 12.81           N
ANISOU  684  N   GLU A  85     1429   1734   1706   -100     65   -332       N
ATOM    685  CA  GLU A  85     -26.169   7.129  12.255  1.00 13.73           C
ANISOU  685  CA  GLU A  85     1668   1712   1835    -82    154   -335       C
ATOM    686  C   GLU A  85     -25.502   6.781  10.935  1.00 13.60           C
ANISOU  686  C   GLU A  85     1553   1686   1929   -312    216   -448       C
ATOM    687  O   GLU A  85     -24.440   7.327  10.603  1.00 15.31           O
ANISOU  687  O   GLU A  85     1792   1814   2210   -338    373   -629       O
ATOM    688  CB  GLU A  85     -25.758   6.121  13.327  1.00 14.04           C
ANISOU  688  CB  GLU A  85     1745   1738   1852     60    -74   -420       C
ATOM    689  CG  GLU A  85     -26.208   6.461  14.737  1.00 14.40           C
ANISOU  689  CG  GLU A  85     1743   1873   1854   -109     -9   -392       C
ATOM    690  CD  GLU A  85     -27.629   6.076  15.059  1.00 13.77           C
ANISOU  690  CD  GLU A  85     1834   1614   1785   -195    -52   -194       C
ATOM    691  OE1 GLU A  85     -28.064   6.395  16.187  1.00 14.64           O
ANISOU  691  OE1 GLU A  85     2182   1601   1779   -159     35   -143       O
ATOM    692  OE2 GLU A  85     -28.312   5.416  14.256  1.00 14.32           O
ANISOU  692  OE2 GLU A  85     1823   1814   1804   -197    -87   -287       O
ATOM    693  N   LEU A  86     -26.093   5.875  10.175  1.00 13.33           N
ANISOU  693  N   LEU A  86     1623   1634   1806   -147    260   -443       N
ATOM    694  C   LEU A  86     -25.712   6.297   7.774  1.00 13.64           C
ANISOU  694  C   LEU A  86     1546   1830   1806    -34    236   -249       C
ATOM    695  O   LEU A  86     -24.845   6.414   6.895  1.00 14.32           O
ANISOU  695  O   LEU A  86     1619   1977   1844   -202    453   -179       O
ATOM    696  CA ALEU A  86     -25.457   5.382   8.964  0.33 13.69           C
ANISOU  696  CA ALEU A  86     1727   1707   1766   -222    267   -360       C
ATOM    697  CB ALEU A  86     -25.961   3.964   8.669  0.33 14.39           C
ANISOU  697  CB ALEU A  86     1970   1758   1739   -396    312   -400       C
ATOM    698  CG ALEU A  86     -25.296   3.244   7.497  0.33 15.28           C
ANISOU  698  CG ALEU A  86     2223   1842   1740   -437    234   -422       C
ATOM    699  CD1ALEU A  86     -23.797   3.278   7.644  0.33 15.72           C
ANISOU  699  CD1ALEU A  86     2330   1901   1744   -464    228   -373       C
ATOM    700  CD2ALEU A  86     -25.790   1.798   7.373  0.33 15.89           C
ANISOU  700  CD2ALEU A  86     2378   1900   1761   -525    111   -487       C
ATOM    701  CA BLEU A  86     -25.453   5.380   8.964  0.67 13.57           C
ANISOU  701  CA BLEU A  86     1698   1697   1762   -148    274   -318       C
ATOM    702  CB BLEU A  86     -25.973   3.960   8.680  0.67 14.14           C
ANISOU  702  CB BLEU A  86     1785   1798   1790   -150    356   -279       C
ATOM    703  CG BLEU A  86     -25.464   3.213   7.443  0.67 14.97           C
ANISOU  703  CG BLEU A  86     1850   1930   1908     37    178   -162       C
ATOM    704  CD1BLEU A  86     -25.222   1.712   7.759  0.67 15.91           C
ANISOU  704  CD1BLEU A  86     2041   1985   2021     66     76   -120       C
ATOM    705  CD2BLEU A  86     -26.447   3.387   6.242  0.67 15.69           C
ANISOU  705  CD2BLEU A  86     1952   2044   1968    -33    -24    -87       C
ATOM    706  N   LYS A  87     -26.881   6.951   7.712  1.00 14.44           N
ANISOU  706  N   LYS A  87     1487   2190   1808    107     39    -67       N
ATOM    707  CA  LYS A  87     -27.197   7.757   6.538  1.00 16.27           C
ANISOU  707  CA  LYS A  87     1748   2528   1908    214    186     10       C
ATOM    708  C   LYS A  87     -26.117   8.781   6.166  1.00 15.05           C
ANISOU  708  C   LYS A  87     1828   2201   1689    387    357    -68       C
ATOM    709  O   LYS A  87     -25.727   8.823   4.986  1.00 14.82           O
ANISOU  709  O   LYS A  87     1730   2224   1677    304    323     -1       O
ATOM    710  CB  LYS A  87     -28.589   8.382   6.723  1.00 19.14           C
ANISOU  710  CB  LYS A  87     2066   3084   2122    397      5     67       C
ATOM    711  CG  LYS A  87     -28.942   9.347   5.592  1.00 21.97           C
ANISOU  711  CG  LYS A  87     2392   3461   2496    689    -39    -65       C
ATOM    712  CD  LYS A  87     -30.343   9.910   5.739  1.00 25.05           C
ANISOU  712  CD  LYS A  87     2799   3862   2857    934    -30   -205       C
ATOM    713  CE  LYS A  87     -30.637  10.403   7.147  1.00 27.30           C
ANISOU  713  CE  LYS A  87     3081   4159   3133   1148    -74   -429       C
ATOM    714  NZ  LYS A  87     -32.116  10.725   7.340  1.00 28.86           N
ANISOU  714  NZ  LYS A  87     3289   4368   3309   1200   -184   -554       N
ATOM    715  N   PRO A  88     -25.598   9.610   7.093  1.00 14.96           N
ANISOU  715  N   PRO A  88     1937   2050   1696    278    369   -199       N
ATOM    716  CA  PRO A  88     -24.603  10.622   6.690  1.00 15.30           C
ANISOU  716  CA  PRO A  88     2046   1950   1819    233    352   -241       C
ATOM    717  C   PRO A  88     -23.311  10.013   6.204  1.00 13.70           C
ANISOU  717  C   PRO A  88     1788   1802   1616    189    121   -155       C
ATOM    718  O   PRO A  88     -22.641  10.576   5.339  1.00 13.58           O
ANISOU  718  O   PRO A  88     1770   1734   1657    162    243    -18       O
ATOM    719  CB  PRO A  88     -24.369  11.450   7.976  1.00 17.73           C
ANISOU  719  CB  PRO A  88     2605   2125   2005    123    510   -256       C
ATOM    720  CG  PRO A  88     -25.441  11.044   8.928  1.00 17.78           C
ANISOU  720  CG  PRO A  88     2543   2238   1976    -27    406   -149       C
ATOM    721  CD  PRO A  88     -25.982   9.739   8.518  1.00 16.35           C
ANISOU  721  CD  PRO A  88     2305   2161   1748    239    527   -263       C
ATOM    722  N   LEU A  89     -22.937   8.901   6.796  1.00 13.28           N
ANISOU  722  N   LEU A  89     1829   1647   1569     53   -111   -148       N
ATOM    723  C   LEU A  89     -21.892   7.616   4.993  1.00 11.49           C
ANISOU  723  C   LEU A  89     1362   1512   1492    174    -39    -22       C
ATOM    724  O   LEU A  89     -20.977   7.710   4.156  1.00 11.88           O
ANISOU  724  O   LEU A  89     1368   1639   1507    149     -2    142       O
ATOM    725  CA ALEU A  89     -21.746   8.180   6.397  0.52 12.82           C
ANISOU  725  CA ALEU A  89     1654   1616   1600     57    -77    -37       C
ATOM    726  CB ALEU A  89     -21.560   7.052   7.408  0.52 14.46           C
ANISOU  726  CB ALEU A  89     1835   1798   1859   -133     28    123       C
ATOM    727  CG ALEU A  89     -20.247   6.303   7.319  0.52 15.53           C
ANISOU  727  CG ALEU A  89     1985   1867   2048    -77    -24    211       C
ATOM    728  CD1ALEU A  89     -19.119   7.210   7.813  0.52 15.52           C
ANISOU  728  CD1ALEU A  89     1822   2005   2071    -36    -84    173       C
ATOM    729  CD2ALEU A  89     -20.288   4.990   8.157  0.52 16.14           C
ANISOU  729  CD2ALEU A  89     2191   1801   2142    -64    -51    255       C
ATOM    730  CA BLEU A  89     -21.741   8.191   6.391  0.48 13.00           C
ANISOU  730  CA BLEU A  89     1722   1669   1550    153   -138   -100       C
ATOM    731  CB BLEU A  89     -21.516   7.077   7.410  0.48 14.94           C
ANISOU  731  CB BLEU A  89     2024   1934   1718    120   -150    -55       C
ATOM    732  CG BLEU A  89     -20.177   6.361   7.411  0.48 16.07           C
ANISOU  732  CG BLEU A  89     2211   2053   1843    241   -231    -17       C
ATOM    733  CD1BLEU A  89     -19.949   5.791   8.812  0.48 15.79           C
ANISOU  733  CD1BLEU A  89     2124   2081   1794    330   -445     58       C
ATOM    734  CD2BLEU A  89     -20.079   5.246   6.367  0.48 16.69           C
ANISOU  734  CD2BLEU A  89     2329   2102   1910    313   -208   -107       C
ATOM    735  N   ALA A  90     -23.038   7.011   4.706  1.00 11.82           N
ANISOU  735  N   ALA A  90     1423   1549   1520     45    -45    -92       N
ATOM    736  CA  ALA A  90     -23.269   6.498   3.370  1.00 12.52           C
ANISOU  736  CA  ALA A  90     1393   1760   1603     72    -94   -206       C
ATOM    737  C   ALA A  90     -23.220   7.631   2.357  1.00 12.58           C
ANISOU  737  C   ALA A  90     1302   1933   1543    144     45   -118       C
ATOM    738  O   ALA A  90     -22.635   7.490   1.272  1.00 13.99           O
ANISOU  738  O   ALA A  90     1590   2201   1525    168     27   -166       O
ATOM    739  CB  ALA A  90     -24.635   5.786   3.319  1.00 13.84           C
ANISOU  739  CB  ALA A  90     1546   1900   1812   -139   -100   -298       C
ATOM    740  N   GLN A  91     -23.844   8.765   2.692  1.00 13.13           N
ANISOU  740  N   GLN A  91     1503   1936   1549    299      3     16       N
ATOM    741  CA  GLN A  91     -23.850   9.907   1.774  1.00 14.07           C
ANISOU  741  CA  GLN A  91     1519   2091   1738    464    109    202       C
ATOM    742  C   GLN A  91     -22.444  10.428   1.518  1.00 12.98           C
ANISOU  742  C   GLN A  91     1484   1881   1568    425     58    201       C
ATOM    743  O   GLN A  91     -22.079  10.680   0.364  1.00 14.20           O
ANISOU  743  O   GLN A  91     1730   2183   1483    466     86    186       O
ATOM    744  CB  GLN A  91     -24.719  11.030   2.338  1.00 16.57           C
ANISOU  744  CB  GLN A  91     1728   2449   2118    648    204    373       C
ATOM    745  CG  GLN A  91     -26.166  10.657   2.417  1.00 19.23           C
ANISOU  745  CG  GLN A  91     2038   2810   2460    736    235    434       C
ATOM    746  CD  GLN A  91     -27.004  11.644   3.218  1.00 21.02           C
ANISOU  746  CD  GLN A  91     2266   3045   2677    774    328    375       C
ATOM    747  OE1 GLN A  91     -26.477  12.504   3.956  1.00 23.34           O
ANISOU  747  OE1 GLN A  91     2632   3269   2968    807    313    334       O
ATOM    748  NE2 GLN A  91     -28.307  11.497   3.118  1.00 21.13           N
ANISOU  748  NE2 GLN A  91     2283   3122   2622    863    369    445       N
ATOM    749  N   SER A  92     -21.632  10.596   2.560  1.00 12.33           N
ANISOU  749  N   SER A  92     1558   1605   1522    315     -7    173       N
ATOM    750  CA  SER A  92     -20.285  11.123   2.342  1.00 12.35           C
ANISOU  750  CA  SER A  92     1746   1513   1435    221     75     89       C
ATOM    751  C   SER A  92     -19.445  10.152   1.542  1.00 11.59           C
ANISOU  751  C   SER A  92     1676   1426   1302     67    -20    116       C
ATOM    752  O   SER A  92     -18.631  10.570   0.707  1.00 11.96           O
ANISOU  752  O   SER A  92     1662   1481   1403     97     84    230       O
ATOM    753  CB  SER A  92     -19.579  11.449   3.645  1.00 13.75           C
ANISOU  753  CB  SER A  92     2166   1516   1542    238      1    131       C
ATOM    754  OG  SER A  92     -19.254  10.278   4.350  1.00 13.59           O
ANISOU  754  OG  SER A  92     1866   1598   1702     87    -20     14       O
ATOM    755  N   HIS A  93     -19.605   8.853   1.788  1.00 11.09           N
ANISOU  755  N   HIS A  93     1489   1372   1351    122     96     46       N
ATOM    756  CA  HIS A  93     -18.790   7.880   1.071  1.00 10.80           C
ANISOU  756  CA  HIS A  93     1530   1278   1296    218    -13     56       C
ATOM    757  C   HIS A  93     -19.215   7.762  -0.389  1.00 11.32           C
ANISOU  757  C   HIS A  93     1500   1442   1359    180     98     57       C
ATOM    758  O   HIS A  93     -18.372   7.499  -1.251  1.00 12.69           O
ANISOU  758  O   HIS A  93     1749   1699   1375    370    158    172       O
ATOM    759  CB  HIS A  93     -18.732   6.560   1.843  1.00 11.32           C
ANISOU  759  CB  HIS A  93     1633   1375   1292    134    -36     72       C
ATOM    760  CG  HIS A  93     -17.824   6.645   3.044  1.00 10.91           C
ANISOU  760  CG  HIS A  93     1525   1361   1258     57     19    -39       C
ATOM    761  ND1 HIS A  93     -18.063   7.500   4.098  1.00 11.50           N
ANISOU  761  ND1 HIS A  93     1543   1569   1259    104     74   -133       N
ATOM    762  CD2 HIS A  93     -16.622   6.059   3.312  1.00 10.71           C
ANISOU  762  CD2 HIS A  93     1509   1358   1202     50     42     75       C
ATOM    763  CE1 HIS A  93     -17.053   7.422   4.961  1.00 10.88           C
ANISOU  763  CE1 HIS A  93     1325   1517   1292    133    -67    -57       C
ATOM    764  NE2 HIS A  93     -16.165   6.549   4.510  1.00  9.86           N
ANISOU  764  NE2 HIS A  93     1366   1242   1140    114    126     -5       N
ATOM    765  N   ALA A  94     -20.489   7.999  -0.697  1.00 11.64           N
ANISOU  765  N   ALA A  94     1560   1495   1367    137    -54     31       N
ATOM    766  CA  ALA A  94     -20.932   8.000  -2.087  1.00 12.77           C
ANISOU  766  CA  ALA A  94     1780   1631   1443     56   -133    205       C
ATOM    767  C   ALA A  94     -20.467   9.236  -2.842  1.00 12.90           C
ANISOU  767  C   ALA A  94     1850   1665   1387    258    -58    142       C
ATOM    768  O   ALA A  94     -20.043   9.142  -3.993  1.00 16.74           O
ANISOU  768  O   ALA A  94     2760   2041   1560    223    220    128       O
ATOM    769  CB  ALA A  94     -22.449   7.943  -2.146  1.00 13.73           C
ANISOU  769  CB  ALA A  94     1820   1808   1589     38   -299    237       C
ATOM    770  N   THR A  95     -20.518  10.405  -2.218  1.00 12.66           N
ANISOU  770  N   THR A  95     1798   1451   1560    201   -168    138       N
ATOM    771  CA  THR A  95     -20.448  11.681  -2.922  1.00 14.27           C
ANISOU  771  CA  THR A  95     1900   1624   1897    179   -250    385       C
ATOM    772  C   THR A  95     -19.148  12.418  -2.712  1.00 14.77           C
ANISOU  772  C   THR A  95     2028   1764   1821    -54     79    294       C
ATOM    773  O   THR A  95     -18.720  13.157  -3.587  1.00 17.66           O
ANISOU  773  O   THR A  95     2612   2285   1815   -295    120    469       O
ATOM    774  CB  THR A  95     -21.631  12.626  -2.522  1.00 16.59           C
ANISOU  774  CB  THR A  95     2061   1885   2360    262   -308    535       C
ATOM    775  OG1 THR A  95     -21.536  12.966  -1.134  1.00 19.00           O
ANISOU  775  OG1 THR A  95     2550   2061   2610    422    179    195       O
ATOM    776  CG2 THR A  95     -23.003  11.991  -2.791  1.00 18.47           C
ANISOU  776  CG2 THR A  95     2235   2081   2702    193   -259    651       C
ATOM    777  N   LYS A  96     -18.593  12.382  -1.527  1.00 13.87           N
ANISOU  777  N   LYS A  96     1712   1725   1832     11    -67    219       N
ATOM    778  CA  LYS A  96     -17.355  13.082  -1.218  1.00 13.81           C
ANISOU  778  CA  LYS A  96     1740   1617   1890     67   -141    206       C
ATOM    779  C   LYS A  96     -16.158  12.181  -1.457  1.00 12.91           C
ANISOU  779  C   LYS A  96     1597   1590   1717     45    -15    289       C
ATOM    780  O   LYS A  96     -15.220  12.543  -2.174  1.00 15.53           O
ANISOU  780  O   LYS A  96     1878   1915   2106     13    132    526       O
ATOM    781  CB  LYS A  96     -17.396  13.596   0.230  1.00 15.10           C
ANISOU  781  CB  LYS A  96     1938   1679   2120     81   -283    -37       C
ATOM    782  CG  LYS A  96     -16.177  14.379   0.669  1.00 17.05           C
ANISOU  782  CG  LYS A  96     2384   1761   2333     73   -153   -149       C
ATOM    783  CD  LYS A  96     -16.261  14.760   2.135  1.00 17.93           C
ANISOU  783  CD  LYS A  96     2568   1882   2361     31   -289   -343       C
ATOM    784  CE  LYS A  96     -15.039  15.579   2.539  1.00 19.50           C
ANISOU  784  CE  LYS A  96     2982   2138   2289   -182   -341   -237       C
ATOM    785  NZ  LYS A  96     -15.094  15.896   3.956  1.00 21.33           N
ANISOU  785  NZ  LYS A  96     3403   2314   2388   -103   -173   -201       N
ATOM    786  N   HIS A  97     -16.155  11.000  -0.844  1.00 11.92           N
ANISOU  786  N   HIS A  97     1697   1297   1534    119     83    140       N
ATOM    787  CA  HIS A  97     -14.980  10.140  -0.933  1.00 11.77           C
ANISOU  787  CA  HIS A  97     1566   1394   1512    183    128     67       C
ATOM    788  C   HIS A  97     -15.013   9.205  -2.143  1.00 11.72           C
ANISOU  788  C   HIS A  97     1598   1483   1373    119    151    110       C
ATOM    789  O   HIS A  97     -13.953   8.759  -2.598  1.00 12.81           O
ANISOU  789  O   HIS A  97     1628   1658   1581     61    170      7       O
ATOM    790  CB  HIS A  97     -14.821   9.309   0.357  1.00 12.21           C
ANISOU  790  CB  HIS A  97     1818   1353   1469    144    153     43       C
ATOM    791  CG  HIS A  97     -14.909  10.144   1.578  1.00 11.78           C
ANISOU  791  CG  HIS A  97     1602   1414   1459    101     63    122       C
ATOM    792  ND1 HIS A  97     -14.131  11.270   1.780  1.00 12.21           N
ANISOU  792  ND1 HIS A  97     1661   1411   1565     56    -33    144       N
ATOM    793  CD2 HIS A  97     -15.725  10.021   2.653  1.00 12.16           C
ANISOU  793  CD2 HIS A  97     1697   1584   1339     72    -28    204       C
ATOM    794  CE1 HIS A  97     -14.459  11.781   2.956  1.00 11.96           C
ANISOU  794  CE1 HIS A  97     1731   1362   1452     36   -100     99       C
ATOM    795  NE2 HIS A  97     -15.416  11.049   3.507  1.00 12.41           N
ANISOU  795  NE2 HIS A  97     1823   1463   1430    130    -71    111       N
ATOM    796  N   LYS A  98     -16.200   8.887  -2.653  1.00 12.35           N
ANISOU  796  N   LYS A  98     1860   1573   1258     87     51      3       N
ATOM    797  CA  LYS A  98     -16.400   8.059  -3.845  1.00 13.59           C
ANISOU  797  CA  LYS A  98     2177   1590   1397    226    -53    138       C
ATOM    798  C   LYS A  98     -15.858   6.650  -3.640  1.00 12.01           C
ANISOU  798  C   LYS A  98     1703   1555   1306    106    -83     93       C
ATOM    799  O   LYS A  98     -14.977   6.184  -4.377  1.00 12.55           O
ANISOU  799  O   LYS A  98     1683   1705   1380     48     72     54       O
ATOM    800  CB  LYS A  98     -15.840   8.717  -5.104  1.00 17.33           C
ANISOU  800  CB  LYS A  98     3057   1834   1693    533    -82    305       C
ATOM    801  CG  LYS A  98     -16.544  10.044  -5.335  1.00 23.50           C
ANISOU  801  CG  LYS A  98     4314   2466   2150    686   -102    546       C
ATOM    802  CD  LYS A  98     -15.843  10.916  -6.361  1.00 28.63           C
ANISOU  802  CD  LYS A  98     5182   3096   2600    904   -161    589       C
ATOM    803  CE  LYS A  98     -16.483  12.263  -6.474  1.00 32.66           C
ANISOU  803  CE  LYS A  98     5779   3600   3030    914   -292    494       C
ATOM    804  NZ  LYS A  98     -17.924  12.120  -6.815  1.00 34.98           N
ANISOU  804  NZ  LYS A  98     6124   3891   3276    935   -347    424       N
ATOM    805  N   ILE A  99     -16.414   5.947  -2.651  1.00 11.63           N
ANISOU  805  N   ILE A  99     1564   1518   1336    225    -71    179       N
ATOM    806  CA  ILE A  99     -15.917   4.633  -2.248  1.00 11.61           C
ANISOU  806  CA  ILE A  99     1503   1568   1342    251    -47    107       C
ATOM    807  C   ILE A  99     -16.871   3.573  -2.803  1.00 12.33           C
ANISOU  807  C   ILE A  99     1468   1769   1448    198     71     11       C
ATOM    808  O   ILE A  99     -18.008   3.460  -2.317  1.00 13.54           O
ANISOU  808  O   ILE A  99     1484   1907   1755    115    -32   -137       O
ATOM    809  CB  ILE A  99     -15.823   4.535  -0.721  1.00 11.27           C
ANISOU  809  CB  ILE A  99     1481   1457   1344    200     70     -8       C
ATOM    810  CG1 ILE A  99     -14.967   5.678  -0.136  1.00 11.76           C
ANISOU  810  CG1 ILE A  99     1582   1551   1337     80     74     55       C
ATOM    811  CG2 ILE A  99     -15.290   3.150  -0.310  1.00 11.84           C
ANISOU  811  CG2 ILE A  99     1541   1468   1490    139     94    -29       C
ATOM    812  CD1 ILE A  99     -13.636   5.855  -0.797  1.00 11.74           C
ANISOU  812  CD1 ILE A  99     1522   1631   1307   -102     99     82       C
ATOM    813  N   PRO A 100     -16.459   2.767  -3.779  1.00 11.96           N
ANISOU  813  N   PRO A 100     1517   1616   1410    166     28    -44       N
ATOM    814  CA  PRO A 100     -17.377   1.738  -4.289  1.00 12.51           C
ANISOU  814  CA  PRO A 100     1720   1648   1384      8   -120    -47       C
ATOM    815  C   PRO A 100     -17.634   0.678  -3.222  1.00 11.94           C
ANISOU  815  C   PRO A 100     1455   1663   1418     61   -100      8       C
ATOM    816  O   PRO A 100     -16.831   0.431  -2.317  1.00 12.31           O
ANISOU  816  O   PRO A 100     1566   1621   1489     82   -282    -14       O
ATOM    817  CB  PRO A 100     -16.630   1.144  -5.492  1.00 14.08           C
ANISOU  817  CB  PRO A 100     2017   1890   1445     55      1   -133       C
ATOM    818  CG  PRO A 100     -15.168   1.415  -5.192  1.00 14.38           C
ANISOU  818  CG  PRO A 100     2048   1852   1562    -99    202   -160       C
ATOM    819  CD  PRO A 100     -15.156   2.754  -4.459  1.00 12.27           C
ANISOU  819  CD  PRO A 100     1656   1631   1375     66    150   -145       C
ATOM    820  N   ILE A 101     -18.752  -0.027  -3.395  1.00 13.10           N
ANISOU  820  N   ILE A 101     1544   1862   1571    -61   -186    120       N
ATOM    821  CA  ILE A 101     -19.085  -1.117  -2.478  1.00 14.17           C
ANISOU  821  CA  ILE A 101     1632   2044   1706   -160   -307    196       C
ATOM    822  C   ILE A 101     -17.963  -2.137  -2.424  1.00 12.84           C
ANISOU  822  C   ILE A 101     1464   1882   1534   -101   -232     85       C
ATOM    823  O   ILE A 101     -17.678  -2.694  -1.362  1.00 12.44           O
ANISOU  823  O   ILE A 101     1530   1763   1432   -120   -263    175       O
ATOM    824  CB  ILE A 101     -20.437  -1.760  -2.844  1.00 16.20           C
ANISOU  824  CB  ILE A 101     1660   2347   2149   -161   -364    343       C
ATOM    825  CG1 ILE A 101     -21.580  -0.741  -2.669  1.00 17.52           C
ANISOU  825  CG1 ILE A 101     1731   2602   2325    -93   -462    127       C
ATOM    826  CG2 ILE A 101     -20.672  -3.078  -2.085  1.00 17.53           C
ANISOU  826  CG2 ILE A 101     1936   2412   2312   -473   -205    582       C
ATOM    827  CD1 ILE A 101     -21.805  -0.284  -1.238  1.00 19.50           C
ANISOU  827  CD1 ILE A 101     2001   2925   2483    152   -266    -45       C
ATOM    828  N   LYS A 102     -17.282  -2.403  -3.542  1.00 12.99           N
ANISOU  828  N   LYS A 102     1557   1842   1537    -29   -192     33       N
ATOM    829  CA  LYS A 102     -16.214  -3.398  -3.484  1.00 14.26           C
ANISOU  829  CA  LYS A 102     1876   2014   1527    -77   -157   -119       C
ATOM    830  C   LYS A 102     -15.136  -2.999  -2.488  1.00 11.85           C
ANISOU  830  C   LYS A 102     1605   1621   1277    -51    -91     26       C
ATOM    831  O   LYS A 102     -14.529  -3.882  -1.867  1.00 11.95           O
ANISOU  831  O   LYS A 102     1746   1476   1317     64    -64     25       O
ATOM    832  CB  LYS A 102     -15.634  -3.694  -4.858  1.00 17.61           C
ANISOU  832  CB  LYS A 102     2496   2531   1664    -79   -145   -228       C
ATOM    833  CG  LYS A 102     -14.837  -2.609  -5.482  1.00 19.87           C
ANISOU  833  CG  LYS A 102     2878   2876   1796   -214   -111   -269       C
ATOM    834  CD  LYS A 102     -14.039  -3.184  -6.680  1.00 22.32           C
ANISOU  834  CD  LYS A 102     3322   3162   1995   -510     96   -313       C
ATOM    835  CE  LYS A 102     -13.164  -2.146  -7.236  1.00 23.75           C
ANISOU  835  CE  LYS A 102     3685   3206   2132   -744    243   -332       C
ATOM    836  NZ  LYS A 102     -12.271  -2.635  -8.341  1.00 23.41           N
ANISOU  836  NZ  LYS A 102     3683   3139   2074   -789    344   -221       N
ATOM    837  N   TYR A 103     -14.862  -1.695  -2.325  1.00 11.28           N
ANISOU  837  N   TYR A 103     1591   1494   1202   -140    -45    -49       N
ATOM    838  CA  TYR A 103     -13.856  -1.291  -1.334  1.00 10.58           C
ANISOU  838  CA  TYR A 103     1409   1450   1163    -68      0     20       C
ATOM    839  C   TYR A 103     -14.365  -1.488   0.094  1.00  9.99           C
ANISOU  839  C   TYR A 103     1303   1310   1182    -16    -27     28       C
ATOM    840  O   TYR A 103     -13.568  -1.754   1.003  1.00 10.54           O
ANISOU  840  O   TYR A 103     1447   1381   1176     -2     -8     75       O
ATOM    841  CB  TYR A 103     -13.456   0.171  -1.546  1.00 11.08           C
ANISOU  841  CB  TYR A 103     1549   1538   1122     -2    179     57       C
ATOM    842  CG  TYR A 103     -12.569   0.439  -2.763  1.00 10.77           C
ANISOU  842  CG  TYR A 103     1457   1549   1087     -5      0    -31       C
ATOM    843  CD1 TYR A 103     -12.072   1.707  -2.965  1.00 11.03           C
ANISOU  843  CD1 TYR A 103     1377   1620   1196   -117     30    122       C
ATOM    844  CD2 TYR A 103     -12.228  -0.556  -3.683  1.00 11.96           C
ANISOU  844  CD2 TYR A 103     1733   1687   1124    -81    120    -47       C
ATOM    845  CE1 TYR A 103     -11.263   2.030  -4.053  1.00 11.16           C
ANISOU  845  CE1 TYR A 103     1410   1691   1141    -18      6    166       C
ATOM    846  CE2 TYR A 103     -11.404  -0.275  -4.778  1.00 12.48           C
ANISOU  846  CE2 TYR A 103     1795   1726   1222   -112     78    -64       C
ATOM    847  CZ  TYR A 103     -10.947   1.026  -4.972  1.00 12.14           C
ANISOU  847  CZ  TYR A 103     1626   1814   1171     32    191    100       C
ATOM    848  OH  TYR A 103     -10.142   1.290  -6.064  1.00 13.28           O
ANISOU  848  OH  TYR A 103     1866   2039   1141    128    212     87       O
ATOM    849  N   LEU A 104     -15.675  -1.324   0.327  1.00 10.31           N
ANISOU  849  N   LEU A 104     1333   1352   1232     41     98     -7       N
ATOM    850  CA  LEU A 104     -16.239  -1.677   1.632  1.00 10.65           C
ANISOU  850  CA  LEU A 104     1338   1378   1331     12    192     82       C
ATOM    851  C   LEU A 104     -16.171  -3.179   1.889  1.00 10.22           C
ANISOU  851  C   LEU A 104     1265   1367   1251    -56     -3     11       C
ATOM    852  O   LEU A 104     -15.975  -3.604   3.044  1.00 10.86           O
ANISOU  852  O   LEU A 104     1448   1457   1220    -64     55     70       O
ATOM    853  CB  LEU A 104     -17.684  -1.193   1.714  1.00 11.90           C
ANISOU  853  CB  LEU A 104     1345   1640   1538     92    188    121       C
ATOM    854  CG  LEU A 104     -17.871   0.340   1.604  1.00 13.61           C
ANISOU  854  CG  LEU A 104     1499   1746   1925    262    208    119       C
ATOM    855  CD1 LEU A 104     -19.336   0.652   1.680  1.00 16.17           C
ANISOU  855  CD1 LEU A 104     1686   2111   2347    437     61    -63       C
ATOM    856  CD2 LEU A 104     -17.125   1.081   2.674  1.00 15.72           C
ANISOU  856  CD2 LEU A 104     2089   1762   2124    146     43     34       C
ATOM    857  N   GLU A 105     -16.284  -4.005   0.849  1.00 10.53           N
ANISOU  857  N   GLU A 105     1376   1343   1282    -78     26    -47       N
ATOM    858  CA  GLU A 105     -16.031  -5.431   1.011  1.00 11.24           C
ANISOU  858  CA  GLU A 105     1555   1377   1338     25    -49   -141       C
ATOM    859  C   GLU A 105     -14.570  -5.679   1.375  1.00 11.20           C
ANISOU  859  C   GLU A 105     1598   1405   1252     48    -70    -42       C
ATOM    860  O   GLU A 105     -14.270  -6.477   2.284  1.00 12.24           O
ANISOU  860  O   GLU A 105     1710   1473   1468     87     16     94       O
ATOM    861  CB  GLU A 105     -16.412  -6.149  -0.299  1.00 12.28           C
ANISOU  861  CB  GLU A 105     1668   1594   1403    -36   -115   -180       C
ATOM    862  CG  GLU A 105     -17.917  -6.123  -0.540  1.00 13.65           C
ANISOU  862  CG  GLU A 105     1761   1873   1552   -160    -56   -270       C
ATOM    863  CD  GLU A 105     -18.385  -6.557  -1.891  1.00 17.11           C
ANISOU  863  CD  GLU A 105     2118   2464   1918   -192   -179   -319       C
ATOM    864  OE1 GLU A 105     -17.556  -6.785  -2.804  1.00 18.69           O
ANISOU  864  OE1 GLU A 105     2360   2758   1986   -298   -280   -345       O
ATOM    865  OE2 GLU A 105     -19.626  -6.648  -2.034  1.00 18.54           O
ANISOU  865  OE2 GLU A 105     2186   2794   2066   -261   -309   -362       O
ATOM    866  N   PHE A 106     -13.639  -4.992   0.704  1.00 11.20           N
ANISOU  866  N   PHE A 106     1496   1482   1277     65     42      7       N
ATOM    867  CA  PHE A 106     -12.231  -5.179   1.032  1.00 11.02           C
ANISOU  867  CA  PHE A 106     1435   1518   1235    159     27    -38       C
ATOM    868  C   PHE A 106     -11.937  -4.792   2.478  1.00 10.80           C
ANISOU  868  C   PHE A 106     1347   1472   1284    112     62   -102       C
ATOM    869  O   PHE A 106     -11.204  -5.501   3.170  1.00 11.66           O
ANISOU  869  O   PHE A 106     1545   1548   1339    180      5     67       O
ATOM    870  CB  PHE A 106     -11.354  -4.331   0.105  1.00 11.48           C
ANISOU  870  CB  PHE A 106     1580   1514   1267    -33     81   -129       C
ATOM    871  CG  PHE A 106     -11.389  -4.669  -1.366  1.00 12.52           C
ANISOU  871  CG  PHE A 106     1752   1642   1365    115    124   -141       C
ATOM    872  CD1 PHE A 106     -10.897  -3.731  -2.274  1.00 13.31           C
ANISOU  872  CD1 PHE A 106     1822   1861   1376    347    125    -33       C
ATOM    873  CD2 PHE A 106     -11.781  -5.928  -1.830  1.00 14.61           C
ANISOU  873  CD2 PHE A 106     2256   1854   1440    189    121   -325       C
ATOM    874  CE1 PHE A 106     -10.861  -4.020  -3.627  1.00 14.92           C
ANISOU  874  CE1 PHE A 106     2228   1949   1490    397     86   -159       C
ATOM    875  CE2 PHE A 106     -11.754  -6.216  -3.204  1.00 16.51           C
ANISOU  875  CE2 PHE A 106     2645   2052   1576    219    104   -256       C
ATOM    876  CZ  PHE A 106     -11.295  -5.251  -4.081  1.00 15.89           C
ANISOU  876  CZ  PHE A 106     2513   2014   1512    345     38   -218       C
ATOM    877  N   ILE A 107     -12.488  -3.669   2.958  1.00 10.28           N
ANISOU  877  N   ILE A 107     1280   1385   1240      1     40    -58       N
ATOM    878  CA  ILE A 107     -12.182  -3.289   4.342  1.00 10.38           C
ANISOU  878  CA  ILE A 107     1365   1363   1216     45     94      7       C
ATOM    879  C   ILE A 107     -12.835  -4.252   5.306  1.00 10.38           C
ANISOU  879  C   ILE A 107     1352   1309   1282     94     34    117       C
ATOM    880  O   ILE A 107     -12.305  -4.492   6.395  1.00 10.80           O
ANISOU  880  O   ILE A 107     1496   1321   1285    114     29    119       O
ATOM    881  CB  ILE A 107     -12.483  -1.813   4.658  1.00 10.52           C
ANISOU  881  CB  ILE A 107     1367   1298   1332     20    -81    -49       C
ATOM    882  CG1 ILE A 107     -11.615  -1.376   5.847  1.00 11.06           C
ANISOU  882  CG1 ILE A 107     1420   1382   1400     11    -74    -31       C
ATOM    883  CG2 ILE A 107     -13.974  -1.572   4.937  1.00 10.77           C
ANISOU  883  CG2 ILE A 107     1275   1380   1439     82     46     98       C
ATOM    884  CD1 ILE A 107     -11.732   0.124   6.185  1.00 12.33           C
ANISOU  884  CD1 ILE A 107     1656   1388   1642     56    -49    -67       C
ATOM    885  N   SER A 108     -13.980  -4.831   4.938  1.00 10.17           N
ANISOU  885  N   SER A 108     1337   1307   1221     -2     81     89       N
ATOM    886  CA  SER A 108     -14.607  -5.809   5.820  1.00 10.90           C
ANISOU  886  CA  SER A 108     1358   1375   1409    -78      3    115       C
ATOM    887  C   SER A 108     -13.709  -7.032   5.979  1.00 10.93           C
ANISOU  887  C   SER A 108     1408   1381   1365    -48    -55     40       C
ATOM    888  O   SER A 108     -13.559  -7.572   7.091  1.00 11.78           O
ANISOU  888  O   SER A 108     1579   1476   1421     11   -147    190       O
ATOM    889  CB  SER A 108     -15.952  -6.227   5.220  1.00 11.46           C
ANISOU  889  CB  SER A 108     1376   1489   1489     37    -84    123       C
ATOM    890  OG  SER A 108     -16.887  -5.154   5.233  1.00 12.38           O
ANISOU  890  OG  SER A 108     1511   1604   1588   -110    -33    209       O
ATOM    891  N   GLU A 109     -13.097  -7.477   4.876  1.00 11.84           N
ANISOU  891  N   GLU A 109     1633   1401   1463     72    -26    -26       N
ATOM    892  CA  GLU A 109     -12.148  -8.576   4.941  1.00 12.83           C
ANISOU  892  CA  GLU A 109     1892   1514   1467    204    -45    -73       C
ATOM    893  C   GLU A 109     -10.964  -8.208   5.821  1.00 12.05           C
ANISOU  893  C   GLU A 109     1687   1539   1351    169    -18    -42       C
ATOM    894  O   GLU A 109     -10.489  -9.037   6.597  1.00 12.26           O
ANISOU  894  O   GLU A 109     1779   1427   1451     95    -16     33       O
ATOM    895  CB  GLU A 109     -11.673  -8.932   3.532  1.00 16.61           C
ANISOU  895  CB  GLU A 109     2863   1745   1702    274    -49   -138       C
ATOM    896  CG  GLU A 109     -12.778  -9.471   2.616  1.00 23.56           C
ANISOU  896  CG  GLU A 109     4345   2404   2204     57     13   -385       C
ATOM    897  CD  GLU A 109     -12.347  -9.606   1.160  1.00 30.19           C
ANISOU  897  CD  GLU A 109     5632   3103   2737   -232     57   -489       C
ATOM    898  OE1 GLU A 109     -11.339  -8.989   0.749  1.00 32.12           O
ANISOU  898  OE1 GLU A 109     6139   3225   2841   -246    270   -369       O
ATOM    899  OE2 GLU A 109     -13.031 -10.345   0.427  1.00 33.71           O
ANISOU  899  OE2 GLU A 109     6182   3511   3116   -344    -21   -474       O
ATOM    900  N   ALA A 110     -10.460  -6.986   5.701  1.00 11.40           N
ANISOU  900  N   ALA A 110     1503   1534   1295    122    101     42       N
ATOM    901  CA  ALA A 110      -9.347  -6.551   6.533  1.00 11.73           C
ANISOU  901  CA  ALA A 110     1499   1632   1325    164     86     70       C
ATOM    902  C   ALA A 110      -9.726  -6.565   8.007  1.00 10.92           C
ANISOU  902  C   ALA A 110     1325   1500   1325    118    -60    120       C
ATOM    903  O   ALA A 110      -8.911  -6.946   8.849  1.00 12.00           O
ANISOU  903  O   ALA A 110     1384   1759   1415    144   -108    174       O
ATOM    904  CB  ALA A 110      -8.853  -5.181   6.075  1.00 11.95           C
ANISOU  904  CB  ALA A 110     1510   1650   1380     25    214      7       C
ATOM    905  N   ILE A 111     -10.922  -6.083   8.340  1.00 10.78           N
ANISOU  905  N   ILE A 111     1338   1479   1281     60     38     89       N
ATOM    906  CA  ILE A 111     -11.400  -6.115   9.727  1.00 10.99           C
ANISOU  906  CA  ILE A 111     1451   1407   1318     37     47    189       C
ATOM    907  C   ILE A 111     -11.389  -7.529  10.272  1.00 11.43           C
ANISOU  907  C   ILE A 111     1472   1535   1336    -68    -26    217       C
ATOM    908  O   ILE A 111     -10.848  -7.786  11.364  1.00 11.68           O
ANISOU  908  O   ILE A 111     1547   1593   1297     40    -77    268       O
ATOM    909  CB  ILE A 111     -12.798  -5.454   9.841  1.00 11.00           C
ANISOU  909  CB  ILE A 111     1351   1480   1349     99    133    165       C
ATOM    910  CG1 ILE A 111     -12.689  -3.942   9.587  1.00 11.44           C
ANISOU  910  CG1 ILE A 111     1428   1503   1416    201     28    159       C
ATOM    911  CG2 ILE A 111     -13.393  -5.708  11.212  1.00 12.45           C
ANISOU  911  CG2 ILE A 111     1521   1832   1379      7    137    173       C
ATOM    912  CD1 ILE A 111     -14.009  -3.272   9.243  1.00 12.33           C
ANISOU  912  CD1 ILE A 111     1459   1643   1583    213    110      9       C
ATOM    913  N   ILE A 112     -11.973  -8.475   9.529  1.00 11.74           N
ANISOU  913  N   ILE A 112     1543   1497   1421    -34    -34    151       N
ATOM    914  CA  ILE A 112     -11.995  -9.863  10.006  1.00 12.50           C
ANISOU  914  CA  ILE A 112     1644   1510   1595    -40   -147    163       C
ATOM    915  C   ILE A 112     -10.587 -10.398  10.185  1.00 12.63           C
ANISOU  915  C   ILE A 112     1690   1507   1604    105    -88    154       C
ATOM    916  O   ILE A 112     -10.296 -11.087  11.168  1.00 13.19           O
ANISOU  916  O   ILE A 112     1773   1573   1666     41   -198    298       O
ATOM    917  CB  ILE A 112     -12.832 -10.739   9.047  1.00 13.65           C
ANISOU  917  CB  ILE A 112     1796   1615   1776   -198   -207    205       C
ATOM    918  CG1 ILE A 112     -14.276 -10.268   9.002  1.00 14.46           C
ANISOU  918  CG1 ILE A 112     1770   1922   1803   -255   -173    238       C
ATOM    919  CG2 ILE A 112     -12.750 -12.222   9.397  1.00 15.63           C
ANISOU  919  CG2 ILE A 112     2288   1658   1992   -282    -88    264       C
ATOM    920  CD1 ILE A 112     -15.065 -10.454  10.304  1.00 15.68           C
ANISOU  920  CD1 ILE A 112     2053   2055   1849   -131   -124    203       C
ATOM    921  N   HIS A 113      -9.712 -10.140   9.213  1.00 12.90           N
ANISOU  921  N   HIS A 113     1792   1468   1641    164     40     69       N
ATOM    922  CA  HIS A 113      -8.336 -10.606   9.299  1.00 14.31           C
ANISOU  922  CA  HIS A 113     1843   1820   1773    288     54    114       C
ATOM    923  C   HIS A 113      -7.654 -10.087  10.564  1.00 13.79           C
ANISOU  923  C   HIS A 113     1772   1690   1779    224     -3    213       C
ATOM    924  O   HIS A 113      -6.976 -10.844  11.272  1.00 14.92           O
ANISOU  924  O   HIS A 113     1993   1764   1913    437   -154    281       O
ATOM    925  CB  HIS A 113      -7.581 -10.146   8.055  1.00 16.19           C
ANISOU  925  CB  HIS A 113     1775   2337   2040    535    120     44       C
ATOM    926  CG  HIS A 113      -6.160 -10.588   8.035  1.00 20.83           C
ANISOU  926  CG  HIS A 113     2376   2956   2583    614     78    -15       C
ATOM    927  ND1 HIS A 113      -5.109  -9.869   8.576  1.00 22.61           N
ANISOU  927  ND1 HIS A 113     2493   3230   2868    808    110    -20       N
ATOM    928  CD2 HIS A 113      -5.624 -11.724   7.554  1.00 23.08           C
ANISOU  928  CD2 HIS A 113     2681   3161   2928    903    192   -117       C
ATOM    929  CE1 HIS A 113      -3.982 -10.543   8.415  1.00 23.70           C
ANISOU  929  CE1 HIS A 113     2698   3251   3055   1125    157   -113       C
ATOM    930  NE2 HIS A 113      -4.266 -11.673   7.789  1.00 24.32           N
ANISOU  930  NE2 HIS A 113     2786   3346   3110   1093    157   -122       N
ATOM    931  N   VAL A 114      -7.750  -8.781  10.814  1.00 12.75           N
ANISOU  931  N   VAL A 114     1584   1573   1687    225    -39    212       N
ATOM    932  CA  VAL A 114      -7.084  -8.184  11.958  1.00 12.71           C
ANISOU  932  CA  VAL A 114     1606   1650   1574     46   -146    304       C
ATOM    933  C   VAL A 114      -7.677  -8.694  13.267  1.00 12.65           C
ANISOU  933  C   VAL A 114     1594   1648   1567    -97   -193    469       C
ATOM    934  O   VAL A 114      -6.943  -8.922  14.238  1.00 14.10           O
ANISOU  934  O   VAL A 114     1744   1936   1676      7   -377    489       O
ATOM    935  CB  VAL A 114      -7.120  -6.652  11.854  1.00 12.98           C
ANISOU  935  CB  VAL A 114     1522   1769   1640      2   -137    376       C
ATOM    936  CG1 VAL A 114      -6.682  -5.981  13.140  1.00 13.30           C
ANISOU  936  CG1 VAL A 114     1648   1789   1615    -60   -151    216       C
ATOM    937  CG2 VAL A 114      -6.244  -6.211  10.674  1.00 13.48           C
ANISOU  937  CG2 VAL A 114     1538   1944   1639   -134    -75    358       C
ATOM    938  N   LEU A 115      -9.007  -8.874  13.325  1.00 13.25           N
ANISOU  938  N   LEU A 115     1746   1716   1571   -142    -40    423       N
ATOM    939  CA  LEU A 115      -9.595  -9.416  14.541  1.00 14.08           C
ANISOU  939  CA  LEU A 115     1807   1870   1674   -170   -100    450       C
ATOM    940  C   LEU A 115      -9.066 -10.806  14.830  1.00 14.49           C
ANISOU  940  C   LEU A 115     1917   1854   1735   -176   -224    488       C
ATOM    941  O   LEU A 115      -8.742 -11.136  15.976  1.00 15.51           O
ANISOU  941  O   LEU A 115     2143   2046   1706    -99   -275    543       O
ATOM    942  CB  LEU A 115     -11.115  -9.440  14.444  1.00 13.65           C
ANISOU  942  CB  LEU A 115     1749   1843   1593   -149    -41    309       C
ATOM    943  CG  LEU A 115     -11.803  -8.068  14.442  1.00 14.34           C
ANISOU  943  CG  LEU A 115     1876   1868   1705   -222    102    187       C
ATOM    944  CD1 LEU A 115     -13.278  -8.189  14.131  1.00 14.77           C
ANISOU  944  CD1 LEU A 115     1801   1981   1829   -351    175    208       C
ATOM    945  CD2 LEU A 115     -11.615  -7.360  15.741  1.00 15.51           C
ANISOU  945  CD2 LEU A 115     2137   2027   1730   -127     77    -13       C
ATOM    946  N   HIS A 116      -8.923 -11.619  13.792  1.00 15.60           N
ANISOU  946  N   HIS A 116     2128   1801   1996     72   -252    435       N
ATOM    947  CA  HIS A 116      -8.400 -12.947  14.016  1.00 19.29           C
ANISOU  947  CA  HIS A 116     2875   2035   2418    378   -241    662       C
ATOM    948  C   HIS A 116      -6.941 -12.885  14.453  1.00 19.31           C
ANISOU  948  C   HIS A 116     2605   2286   2446    687   -240    720       C
ATOM    949  O   HIS A 116      -6.527 -13.616  15.362  1.00 21.47           O
ANISOU  949  O   HIS A 116     2928   2653   2575    732   -292    888       O
ATOM    950  CB  HIS A 116      -8.552 -13.767  12.734  1.00 23.75           C
ANISOU  950  CB  HIS A 116     3772   2303   2951    597   -120    673       C
ATOM    951  CG  HIS A 116      -8.157 -15.196  12.902  1.00 29.22           C
ANISOU  951  CG  HIS A 116     4654   2842   3607    655    -86    515       C
ATOM    952  ND1 HIS A 116      -6.918 -15.671  12.537  1.00 32.00           N
ANISOU  952  ND1 HIS A 116     5087   3150   3922    625     -7    414       N
ATOM    953  CD2 HIS A 116      -8.836 -16.256  13.396  1.00 31.39           C
ANISOU  953  CD2 HIS A 116     5040   2995   3894    607    -57    517       C
ATOM    954  CE1 HIS A 116      -6.844 -16.964  12.798  1.00 32.76           C
ANISOU  954  CE1 HIS A 116     5240   3157   4052    627     72    443       C
ATOM    955  NE2 HIS A 116      -7.995 -17.346  13.328  1.00 32.83           N
ANISOU  955  NE2 HIS A 116     5273   3131   4070    599     46    474       N
ATOM    956  N   SER A 117      -6.142 -12.028  13.812  1.00 18.74           N
ANISOU  956  N   SER A 117     2170   2510   2439    566   -159    512       N
ATOM    957  CA  SER A 117      -4.720 -11.915  14.116  1.00 19.63           C
ANISOU  957  CA  SER A 117     2068   2820   2572    511   -302    517       C
ATOM    958  C   SER A 117      -4.482 -11.396  15.529  1.00 18.93           C
ANISOU  958  C   SER A 117     1963   2731   2497    468   -481    700       C
ATOM    959  O   SER A 117      -3.564 -11.868  16.217  1.00 21.18           O
ANISOU  959  O   SER A 117     2344   3032   2671    498   -652    741       O
ATOM    960  CB ASER A 117      -4.054 -10.987  13.091  0.53 20.64           C
ANISOU  960  CB ASER A 117     1985   3091   2765    327   -240    446       C
ATOM    961  OG ASER A 117      -2.658 -10.861  13.329  0.53 21.47           O
ANISOU  961  OG ASER A 117     2002   3237   2917    235   -233    441       O
ATOM    962  CB CSER A 117      -4.058 -10.976  13.111  0.47 20.65           C
ANISOU  962  CB CSER A 117     2135   3017   2692    393   -213    380       C
ATOM    963  OG CSER A 117      -4.140 -11.509  11.815  0.47 21.83           O
ANISOU  963  OG CSER A 117     2382   3131   2780    354   -171    281       O
ATOM    964  N   ARG A 118      -5.257 -10.388  15.955  1.00 18.31           N
ANISOU  964  N   ARG A 118     1982   2577   2400    178   -241    732       N
ATOM    965  CA  ARG A 118      -5.044  -9.754  17.252  1.00 18.38           C
ANISOU  965  CA  ARG A 118     2099   2513   2374     82   -412    620       C
ATOM    966  C   ARG A 118      -5.696 -10.509  18.396  1.00 19.01           C
ANISOU  966  C   ARG A 118     2363   2496   2364    -93   -553    656       C
ATOM    967  O   ARG A 118      -5.344 -10.273  19.557  1.00 20.14           O
ANISOU  967  O   ARG A 118     2713   2702   2238   -528   -610    654       O
ATOM    968  CB AARG A 118      -5.521  -8.298  17.249  0.58 18.54           C
ANISOU  968  CB AARG A 118     2155   2520   2367    -85   -388    515       C
ATOM    969  CG AARG A 118      -4.739  -7.449  16.252  0.58 18.88           C
ANISOU  969  CG AARG A 118     2246   2510   2416   -100   -343    447       C
ATOM    970  CD AARG A 118      -5.098  -5.975  16.334  0.58 19.81           C
ANISOU  970  CD AARG A 118     2542   2565   2420   -147   -394    238       C
ATOM    971  NE AARG A 118      -4.892  -5.418  17.661  0.58 20.57           N
ANISOU  971  NE AARG A 118     2800   2616   2398   -116   -544    119       N
ATOM    972  CZ AARG A 118      -3.983  -4.497  17.959  0.58 21.58           C
ANISOU  972  CZ AARG A 118     3078   2729   2394   -131   -568     53       C
ATOM    973  NH1AARG A 118      -3.857  -4.046  19.204  0.58 21.74           N
ANISOU  973  NH1AARG A 118     3107   2780   2374   -137   -619    -71       N
ATOM    974  NH2AARG A 118      -3.168  -4.040  17.035  0.58 22.22           N
ANISOU  974  NH2AARG A 118     3326   2737   2381   -145   -561     53       N
ATOM    975  CB BARG A 118      -5.559  -8.313  17.254  0.42 18.44           C
ANISOU  975  CB BARG A 118     2126   2509   2371      9   -245    647       C
ATOM    976  CG BARG A 118      -4.604  -7.340  16.581  0.42 18.63           C
ANISOU  976  CG BARG A 118     2178   2498   2403     46    -91    694       C
ATOM    977  CD BARG A 118      -5.136  -5.936  16.647  0.42 19.22           C
ANISOU  977  CD BARG A 118     2291   2536   2474     68    -68    616       C
ATOM    978  NE BARG A 118      -4.102  -4.935  16.430  0.42 19.76           N
ANISOU  978  NE BARG A 118     2410   2583   2514    149   -140    575       N
ATOM    979  CZ BARG A 118      -3.550  -4.215  17.397  0.42 19.98           C
ANISOU  979  CZ BARG A 118     2455   2643   2495    203   -122    500       C
ATOM    980  NH1BARG A 118      -2.606  -3.319  17.103  0.42 19.71           N
ANISOU  980  NH1BARG A 118     2454   2613   2422    105   -235    507       N
ATOM    981  NH2BARG A 118      -3.920  -4.408  18.658  0.42 20.56           N
ANISOU  981  NH2BARG A 118     2452   2776   2585    290    -76    404       N
ATOM    982  N   HIS A 119      -6.618 -11.417  18.125  1.00 18.38           N
ANISOU  982  N   HIS A 119     2380   2114   2488   -113   -513    698       N
ATOM    983  CA  HIS A 119      -7.390 -12.072  19.186  1.00 19.60           C
ANISOU  983  CA  HIS A 119     2771   2047   2628   -163   -479    744       C
ATOM    984  C   HIS A 119      -7.425 -13.591  19.060  1.00 23.85           C
ANISOU  984  C   HIS A 119     3384   2414   3263    -27   -438    746       C
ATOM    985  O   HIS A 119      -8.504 -14.188  19.034  1.00 25.24           O
ANISOU  985  O   HIS A 119     3709   2483   3400   -148   -331    507       O
ATOM    986  CB  HIS A 119      -8.806 -11.505  19.254  1.00 18.88           C
ANISOU  986  CB  HIS A 119     2751   2042   2382   -214   -436    620       C
ATOM    987  CG  HIS A 119      -8.799 -10.026  19.419  1.00 18.39           C
ANISOU  987  CG  HIS A 119     2640   2084   2263   -222   -358    466       C
ATOM    988  ND1 HIS A 119      -8.593  -9.393  20.628  1.00 20.11           N
ANISOU  988  ND1 HIS A 119     3043   2273   2325   -303   -234    400       N
ATOM    989  CD2 HIS A 119      -8.904  -9.047  18.496  1.00 17.66           C
ANISOU  989  CD2 HIS A 119     2464   2083   2164   -252   -220    534       C
ATOM    990  CE1 HIS A 119      -8.567  -8.085  20.434  1.00 19.51           C
ANISOU  990  CE1 HIS A 119     2907   2273   2232   -255   -227    407       C
ATOM    991  NE2 HIS A 119      -8.752  -7.851  19.148  1.00 18.43           N
ANISOU  991  NE2 HIS A 119     2643   2201   2157   -199   -217    485       N
ATOM    992  N   PRO A 120      -6.267 -14.250  19.052  1.00 27.64           N
ANISOU  992  N   PRO A 120     3836   2868   3797    196   -389    640       N
ATOM    993  CA  PRO A 120      -6.259 -15.724  19.119  1.00 29.75           C
ANISOU  993  CA  PRO A 120     4147   3165   3991    190   -450    586       C
ATOM    994  C   PRO A 120      -6.953 -16.245  20.374  1.00 30.89           C
ANISOU  994  C   PRO A 120     4423   3328   3986    -18   -675    616       C
ATOM    995  O   PRO A 120      -6.732 -15.749  21.483  1.00 32.18           O
ANISOU  995  O   PRO A 120     4676   3406   4146      2   -672    664       O
ATOM    996  CB  PRO A 120      -4.768 -16.078  19.137  1.00 29.95           C
ANISOU  996  CB  PRO A 120     4120   3128   4133    375   -370    582       C
ATOM    997  CG  PRO A 120      -4.060 -14.925  18.595  1.00 29.27           C
ANISOU  997  CG  PRO A 120     4014   2952   4154    517   -340    653       C
ATOM    998  CD  PRO A 120      -4.906 -13.694  18.965  1.00 27.56           C
ANISOU  998  CD  PRO A 120     3718   2767   3987    502   -372    726       C
ATOM    999  N   GLY A 121      -7.783 -17.273  20.197  1.00 30.11           N
ANISOU  999  N   GLY A 121     4209   3452   3780   -283   -833    615       N
ATOM   1000  CA  GLY A 121      -8.550 -17.833  21.286  1.00 28.57           C
ANISOU 1000  CA  GLY A 121     3985   3447   3424   -301  -1009    694       C
ATOM   1001  C   GLY A 121      -9.756 -17.018  21.692  1.00 26.74           C
ANISOU 1001  C   GLY A 121     3810   3260   3092   -748   -951    744       C
ATOM   1002  O   GLY A 121     -10.500 -17.439  22.581  1.00 26.66           O
ANISOU 1002  O   GLY A 121     3950   3135   3042   -824   -952    808       O
ATOM   1003  N   ASN A 122      -9.981 -15.865  21.071  1.00 24.94           N
ANISOU 1003  N   ASN A 122     3538   3140   2798   -951   -859    840       N
ATOM   1004  CA  ASN A 122     -11.138 -15.055  21.424  1.00 24.49           C
ANISOU 1004  CA  ASN A 122     3397   3252   2655  -1182   -592    785       C
ATOM   1005  C   ASN A 122     -11.911 -14.612  20.198  1.00 22.12           C
ANISOU 1005  C   ASN A 122     3138   2809   2460   -941   -346    625       C
ATOM   1006  O   ASN A 122     -12.702 -13.653  20.279  1.00 23.47           O
ANISOU 1006  O   ASN A 122     3400   2898   2618   -702   -177    442       O
ATOM   1007  CB  ASN A 122     -10.731 -13.835  22.258  1.00 27.57           C
ANISOU 1007  CB  ASN A 122     3760   3932   2782  -1325   -565    726       C
ATOM   1008  CG  ASN A 122     -10.283 -14.228  23.643  1.00 30.33           C
ANISOU 1008  CG  ASN A 122     4029   4512   2984  -1325   -569    786       C
ATOM   1009  OD1 ASN A 122     -11.081 -14.682  24.458  1.00 30.93           O
ANISOU 1009  OD1 ASN A 122     4008   4646   3099  -1279   -653    782       O
ATOM   1010  ND2 ASN A 122      -8.990 -14.092  23.908  1.00 32.15           N
ANISOU 1010  ND2 ASN A 122     4276   4813   3127  -1349   -562    798       N
ATOM   1011  N   PHE A 123     -11.668 -15.247  19.045  1.00 19.11           N
ANISOU 1011  N   PHE A 123     2739   2350   2172   -819   -241    596       N
ATOM   1012  CA  PHE A 123     -12.322 -14.866  17.809  1.00 16.75           C
ANISOU 1012  CA  PHE A 123     2396   2025   1944   -555   -241    490       C
ATOM   1013  C   PHE A 123     -12.528 -16.133  16.981  1.00 15.51           C
ANISOU 1013  C   PHE A 123     2156   1823   1913   -216   -146    380       C
ATOM   1014  O   PHE A 123     -11.950 -16.316  15.924  1.00 17.05           O
ANISOU 1014  O   PHE A 123     2169   2119   2190   -150    -18    177       O
ATOM   1015  CB  PHE A 123     -11.584 -13.774  17.033  1.00 16.22           C
ANISOU 1015  CB  PHE A 123     2220   2024   1919   -628   -217    525       C
ATOM   1016  CG  PHE A 123     -12.449 -13.140  15.978  1.00 15.51           C
ANISOU 1016  CG  PHE A 123     2086   1912   1896   -579   -217    390       C
ATOM   1017  CD1 PHE A 123     -13.575 -12.393  16.335  1.00 15.73           C
ANISOU 1017  CD1 PHE A 123     2185   1873   1918   -554   -233    208       C
ATOM   1018  CD2 PHE A 123     -12.134 -13.265  14.633  1.00 16.10           C
ANISOU 1018  CD2 PHE A 123     2258   1983   1879   -507   -170    371       C
ATOM   1019  CE1 PHE A 123     -14.383 -11.798  15.366  1.00 16.49           C
ANISOU 1019  CE1 PHE A 123     2429   1930   1907   -422   -196    256       C
ATOM   1020  CE2 PHE A 123     -12.891 -12.633  13.661  1.00 16.46           C
ANISOU 1020  CE2 PHE A 123     2342   2051   1863   -469   -223    364       C
ATOM   1021  CZ  PHE A 123     -14.039 -11.907  14.037  1.00 16.30           C
ANISOU 1021  CZ  PHE A 123     2276   2025   1893   -496   -234    294       C
ATOM   1022  N   GLY A 124     -13.406 -16.989  17.465  1.00 14.27           N
ANISOU 1022  N   GLY A 124     1892   1604   1926   -201   -245    296       N
ATOM   1023  CA  GLY A 124     -13.666 -18.266  16.833  1.00 14.71           C
ANISOU 1023  CA  GLY A 124     1859   1666   2065    -47   -272    251       C
ATOM   1024  C   GLY A 124     -14.812 -18.175  15.832  1.00 13.28           C
ANISOU 1024  C   GLY A 124     1674   1515   1858     13   -188    193       C
ATOM   1025  O   GLY A 124     -15.209 -17.093  15.384  1.00 13.62           O
ANISOU 1025  O   GLY A 124     1783   1527   1864     39   -207    315       O
ATOM   1026  N   ALA A 125     -15.329 -19.340  15.455  1.00 13.14           N
ANISOU 1026  N   ALA A 125     1773   1475   1745   -118   -151    100       N
ATOM   1027  CA  ALA A 125     -16.294 -19.408  14.365  1.00 13.84           C
ANISOU 1027  CA  ALA A 125     2056   1505   1698     75    -20    -45       C
ATOM   1028  C   ALA A 125     -17.584 -18.660  14.682  1.00 12.30           C
ANISOU 1028  C   ALA A 125     1768   1361   1544    -66    -10     87       C
ATOM   1029  O   ALA A 125     -18.203 -18.078  13.780  1.00 13.33           O
ANISOU 1029  O   ALA A 125     2001   1488   1575    -24   -187    191       O
ATOM   1030  CB  ALA A 125     -16.586 -20.867  14.027  1.00 15.18           C
ANISOU 1030  CB  ALA A 125     2327   1562   1878     73    -36   -138       C
ATOM   1031  N   CYS A 126     -18.039 -18.692  15.939  1.00 12.20           N
ANISOU 1031  N   CYS A 126     1730   1362   1542    -87     74    162       N
ATOM   1032  CA  CYS A 126     -19.278 -18.005  16.282  1.00 12.16           C
ANISOU 1032  CA  CYS A 126     1690   1283   1646    -91    176    253       C
ATOM   1033  C   CYS A 126     -19.114 -16.505  16.144  1.00 11.98           C
ANISOU 1033  C   CYS A 126     1666   1358   1526    -58     70    211       C
ATOM   1034  O   CYS A 126     -19.950 -15.833  15.525  1.00 12.60           O
ANISOU 1034  O   CYS A 126     1721   1514   1551    -47    -18    228       O
ATOM   1035  CB  CYS A 126     -19.706 -18.358  17.698  1.00 13.06           C
ANISOU 1035  CB  CYS A 126     1860   1325   1776   -228    209    317       C
ATOM   1036  SG  CYS A 126     -19.950 -20.160  17.842  1.00 13.66           S
ANISOU 1036  SG  CYS A 126     1855   1453   1882   -194    100    172       S
ATOM   1037  N   ALA A 127     -18.036 -15.961  16.712  1.00 11.81           N
ANISOU 1037  N   ALA A 127     1688   1276   1521   -179    -15    203       N
ATOM   1038  CA  ALA A 127     -17.807 -14.524  16.633  1.00 11.95           C
ANISOU 1038  CA  ALA A 127     1765   1290   1484   -203      1    250       C
ATOM   1039  C   ALA A 127     -17.517 -14.074  15.208  1.00 11.67           C
ANISOU 1039  C   ALA A 127     1593   1376   1466    -61    -11    210       C
ATOM   1040  O   ALA A 127     -17.979 -13.011  14.784  1.00 12.10           O
ANISOU 1040  O   ALA A 127     1800   1272   1525    -21    -27    274       O
ATOM   1041  CB  ALA A 127     -16.647 -14.154  17.549  1.00 13.33           C
ANISOU 1041  CB  ALA A 127     2017   1500   1550   -275   -232    196       C
ATOM   1042  N   GLN A 128     -16.746 -14.869  14.468  1.00 12.17           N
ANISOU 1042  N   GLN A 128     1677   1465   1482     57    156    294       N
ATOM   1043  CA  GLN A 128     -16.432 -14.512  13.060  1.00 13.10           C
ANISOU 1043  CA  GLN A 128     1775   1609   1594     80    111    264       C
ATOM   1044  C   GLN A 128     -17.721 -14.492  12.229  1.00 12.60           C
ANISOU 1044  C   GLN A 128     1811   1476   1498    -46     35    235       C
ATOM   1045  O   GLN A 128     -17.877 -13.575  11.417  1.00 12.34           O
ANISOU 1045  O   GLN A 128     1811   1430   1449    -24    -23    198       O
ATOM   1046  CB  GLN A 128     -15.432 -15.498  12.454  1.00 15.34           C
ANISOU 1046  CB  GLN A 128     2145   1926   1759    392    290    437       C
ATOM   1047  CG  GLN A 128     -14.976 -15.104  11.057  1.00 20.68           C
ANISOU 1047  CG  GLN A 128     3009   2682   2165    635    514    390       C
ATOM   1048  CD  GLN A 128     -13.849 -15.972  10.552  1.00 25.20           C
ANISOU 1048  CD  GLN A 128     3651   3274   2650    944    601    367       C
ATOM   1049  OE1 GLN A 128     -13.198 -16.683  11.311  1.00 27.74           O
ANISOU 1049  OE1 GLN A 128     3747   3775   3016   1177    431    189       O
ATOM   1050  NE2 GLN A 128     -13.634 -15.944   9.252  1.00 26.98           N
ANISOU 1050  NE2 GLN A 128     4012   3479   2762    741    764    199       N
ATOM   1051  N   GLY A 129     -18.602 -15.478  12.414  1.00 12.47           N
ANISOU 1051  N   GLY A 129     1870   1384   1483   -183    -69    184       N
ATOM   1052  CA  GLY A 129     -19.821 -15.491  11.628  1.00 12.72           C
ANISOU 1052  CA  GLY A 129     1859   1448   1524    100   -120    207       C
ATOM   1053  C   GLY A 129     -20.705 -14.311  11.954  1.00 12.13           C
ANISOU 1053  C   GLY A 129     1770   1362   1477    -52    -69    246       C
ATOM   1054  O   GLY A 129     -21.269 -13.679  11.055  1.00 12.58           O
ANISOU 1054  O   GLY A 129     1822   1411   1545   -120   -118    178       O
ATOM   1055  N   ALA A 130     -20.811 -13.969  13.244  1.00 11.64           N
ANISOU 1055  N   ALA A 130     1582   1327   1513    -70    -78    160       N
ATOM   1056  CA  ALA A 130     -21.636 -12.838  13.653  1.00 11.38           C
ANISOU 1056  CA  ALA A 130     1604   1323   1398   -114    -82    237       C
ATOM   1057  C   ALA A 130     -21.071 -11.525  13.120  1.00 11.06           C
ANISOU 1057  C   ALA A 130     1621   1216   1366    -47     20    185       C
ATOM   1058  O   ALA A 130     -21.815 -10.670  12.625  1.00 11.54           O
ANISOU 1058  O   ALA A 130     1684   1312   1388    -30     56    176       O
ATOM   1059  CB  ALA A 130     -21.785 -12.807  15.172  1.00 12.45           C
ANISOU 1059  CB  ALA A 130     1893   1459   1378   -336     13    249       C
ATOM   1060  N   MET A 131     -19.757 -11.335  13.214  1.00 10.87           N
ANISOU 1060  N   MET A 131     1476   1320   1333   -140    101    240       N
ATOM   1061  CA  MET A 131     -19.160 -10.108  12.702  1.00 10.81           C
ANISOU 1061  CA  MET A 131     1472   1324   1312   -204    -30    211       C
ATOM   1062  C   MET A 131     -19.303 -10.026  11.186  1.00 10.92           C
ANISOU 1062  C   MET A 131     1497   1333   1319   -183   -187    188       C
ATOM   1063  O   MET A 131     -19.560  -8.948  10.649  1.00 11.70           O
ANISOU 1063  O   MET A 131     1601   1386   1459   -157   -109    342       O
ATOM   1064  CB  MET A 131     -17.698 -10.030  13.142  1.00 11.71           C
ANISOU 1064  CB  MET A 131     1540   1352   1555   -153     -8    164       C
ATOM   1065  CG  MET A 131     -17.068  -8.688  12.796  1.00 13.91           C
ANISOU 1065  CG  MET A 131     1921   1490   1874   -184     28     69       C
ATOM   1066  SD  MET A 131     -17.777  -7.261  13.645  1.00 15.56           S
ANISOU 1066  SD  MET A 131     1971   1729   2211   -228    -30    -52       S
ATOM   1067  CE  MET A 131     -17.306  -7.676  15.265  1.00 16.69           C
ANISOU 1067  CE  MET A 131     2232   2081   2028    324    412    252       C
ATOM   1068  N   ASN A 132     -19.184 -11.167  10.510  1.00 11.63           N
ANISOU 1068  N   ASN A 132     1688   1413   1318    -60    -54    127       N
ATOM   1069  CA  ASN A 132     -19.367 -11.168   9.035  1.00 12.46           C
ANISOU 1069  CA  ASN A 132     1853   1507   1373     -4    -32    104       C
ATOM   1070  C   ASN A 132     -20.786 -10.682   8.719  1.00 11.65           C
ANISOU 1070  C   ASN A 132     1845   1286   1295    -28     13    198       C
ATOM   1071  O   ASN A 132     -20.938  -9.864   7.802  1.00 11.89           O
ANISOU 1071  O   ASN A 132     1786   1327   1403      0    -28    160       O
ATOM   1072  CB  ASN A 132     -19.062 -12.536   8.426  1.00 15.34           C
ANISOU 1072  CB  ASN A 132     2329   1948   1551     98    113   -116       C
ATOM   1073  CG  ASN A 132     -17.597 -12.682   8.081  1.00 21.28           C
ANISOU 1073  CG  ASN A 132     3260   2702   2123    341    209   -250       C
ATOM   1074  OD1 ASN A 132     -16.954 -11.715   7.696  1.00 24.91           O
ANISOU 1074  OD1 ASN A 132     3525   3262   2678    153    256   -605       O
ATOM   1075  ND2 ASN A 132     -17.075 -13.887   8.202  1.00 23.99           N
ANISOU 1075  ND2 ASN A 132     3762   3117   2237    726    257   -140       N
ATOM   1076  N   LYS A 133     -21.781 -11.163   9.467  1.00 12.00           N
ANISOU 1076  N   LYS A 133     1717   1394   1448   -132    -93    227       N
ATOM   1077  CA  LYS A 133     -23.151 -10.740   9.222  1.00 12.28           C
ANISOU 1077  CA  LYS A 133     1726   1340   1600   -265   -189    284       C
ATOM   1078  C   LYS A 133     -23.356  -9.266   9.531  1.00 11.40           C
ANISOU 1078  C   LYS A 133     1526   1281   1524   -285   -142    243       C
ATOM   1079  O   LYS A 133     -24.055  -8.577   8.781  1.00 12.19           O
ANISOU 1079  O   LYS A 133     1660   1408   1564   -118   -239    220       O
ATOM   1080  CB  LYS A 133     -24.119 -11.557  10.056  1.00 14.38           C
ANISOU 1080  CB  LYS A 133     2037   1566   1862   -545   -185    285       C
ATOM   1081  CG  LYS A 133     -24.362 -12.956   9.552  1.00 17.57           C
ANISOU 1081  CG  LYS A 133     2579   1948   2151   -701   -206    381       C
ATOM   1082  CD  LYS A 133     -25.618 -13.507  10.246  1.00 20.65           C
ANISOU 1082  CD  LYS A 133     2994   2431   2420   -904   -192    387       C
ATOM   1083  CE  LYS A 133     -25.937 -14.863   9.779  1.00 23.28           C
ANISOU 1083  CE  LYS A 133     3229   2925   2690   -887   -289    370       C
ATOM   1084  NZ  LYS A 133     -27.211 -15.272  10.431  1.00 23.87           N
ANISOU 1084  NZ  LYS A 133     3198   3141   2732   -948   -317    417       N
ATOM   1085  N   ALA A 134     -22.772  -8.764  10.626  1.00 11.04           N
ANISOU 1085  N   ALA A 134     1463   1339   1393   -182   -120    161       N
ATOM   1086  CA  ALA A 134     -22.951  -7.357  10.965  1.00 11.28           C
ANISOU 1086  CA  ALA A 134     1591   1278   1418   -131     -2    107       C
ATOM   1087  C   ALA A 134     -22.349  -6.471   9.890  1.00 10.20           C
ANISOU 1087  C   ALA A 134     1362   1167   1346    -37   -134    132       C
ATOM   1088  O   ALA A 134     -22.921  -5.442   9.522  1.00 11.27           O
ANISOU 1088  O   ALA A 134     1445   1369   1467    -32    -90    189       O
ATOM   1089  CB  ALA A 134     -22.330  -7.059  12.334  1.00 11.81           C
ANISOU 1089  CB  ALA A 134     1654   1493   1341   -296    -52    177       C
ATOM   1090  N   LEU A 135     -21.164  -6.838   9.392  1.00 10.51           N
ANISOU 1090  N   LEU A 135     1393   1327   1275    -71    -12    130       N
ATOM   1091  CA  LEU A 135     -20.533  -6.038   8.341  1.00 11.00           C
ANISOU 1091  CA  LEU A 135     1406   1456   1317     30    -56    297       C
ATOM   1092  C   LEU A 135     -21.316  -6.150   7.035  1.00 11.04           C
ANISOU 1092  C   LEU A 135     1470   1364   1361     -3    -33    296       C
ATOM   1093  O   LEU A 135     -21.392  -5.179   6.267  1.00 11.03           O
ANISOU 1093  O   LEU A 135     1500   1346   1344    -32      5    272       O
ATOM   1094  CB  LEU A 135     -19.072  -6.463   8.164  1.00 11.38           C
ANISOU 1094  CB  LEU A 135     1449   1448   1428    -14   -118    236       C
ATOM   1095  CG  LEU A 135     -18.179  -6.187   9.379  1.00 12.44           C
ANISOU 1095  CG  LEU A 135     1488   1571   1666   -114   -198    185       C
ATOM   1096  CD1 LEU A 135     -16.790  -6.789   9.143  1.00 13.63           C
ANISOU 1096  CD1 LEU A 135     1491   2042   1645   -179   -101    325       C
ATOM   1097  CD2 LEU A 135     -18.045  -4.680   9.685  1.00 15.19           C
ANISOU 1097  CD2 LEU A 135     1982   1641   2149   -258   -534    -48       C
ATOM   1098  N   GLU A 136     -21.896  -7.323   6.755  1.00 11.13           N
ANISOU 1098  N   GLU A 136     1532   1326   1369   -101   -216     84       N
ATOM   1099  CA  GLU A 136     -22.734  -7.465   5.571  1.00 12.04           C
ANISOU 1099  CA  GLU A 136     1689   1312   1575    -62   -287     29       C
ATOM   1100  C   GLU A 136     -23.961  -6.567   5.650  1.00 11.47           C
ANISOU 1100  C   GLU A 136     1501   1352   1503    -45   -138    120       C
ATOM   1101  O   GLU A 136     -24.331  -5.925   4.652  1.00 12.18           O
ANISOU 1101  O   GLU A 136     1716   1478   1434     19   -153    140       O
ATOM   1102  CB  GLU A 136     -23.137  -8.925   5.410  1.00 13.76           C
ANISOU 1102  CB  GLU A 136     2009   1419   1798   -150   -449   -151       C
ATOM   1103  CG  GLU A 136     -23.970  -9.178   4.180  1.00 17.37           C
ANISOU 1103  CG  GLU A 136     2604   1764   2232   -204   -663   -190       C
ATOM   1104  CD  GLU A 136     -24.433 -10.632   4.096  1.00 22.00           C
ANISOU 1104  CD  GLU A 136     3405   2154   2799   -240   -831   -123       C
ATOM   1105  OE1 GLU A 136     -24.064 -11.457   4.953  1.00 24.51           O
ANISOU 1105  OE1 GLU A 136     3823   2281   3207   -438   -764    -47       O
ATOM   1106  OE2 GLU A 136     -25.198 -10.949   3.216  1.00 24.37           O
ANISOU 1106  OE2 GLU A 136     3761   2380   3117   -300   -843    -95       O
ATOM   1107  N   LEU A 137     -24.605  -6.521   6.827  1.00 11.66           N
ANISOU 1107  N   LEU A 137     1443   1430   1556    -50    -49     87       N
ATOM   1108  CA  LEU A 137     -25.758  -5.643   7.014  1.00 12.11           C
ANISOU 1108  CA  LEU A 137     1472   1561   1567    -95     -2    269       C
ATOM   1109  C   LEU A 137     -25.360  -4.190   6.787  1.00 11.34           C
ANISOU 1109  C   LEU A 137     1441   1471   1395   -116    -79    239       C
ATOM   1110  O   LEU A 137     -26.065  -3.435   6.102  1.00 12.21           O
ANISOU 1110  O   LEU A 137     1557   1599   1482    -19    -81    243       O
ATOM   1111  CB  LEU A 137     -26.322  -5.849   8.421  1.00 13.26           C
ANISOU 1111  CB  LEU A 137     1525   1755   1757    -67    143    295       C
ATOM   1112  CG  LEU A 137     -27.480  -4.905   8.785  1.00 14.93           C
ANISOU 1112  CG  LEU A 137     1694   2083   1896     77     39    199       C
ATOM   1113  CD1 LEU A 137     -28.694  -5.108   7.852  1.00 16.30           C
ANISOU 1113  CD1 LEU A 137     1697   2325   2172     38   -141    122       C
ATOM   1114  CD2 LEU A 137     -27.821  -5.112  10.250  1.00 16.44           C
ANISOU 1114  CD2 LEU A 137     2200   2111   1937    110    174    271       C
ATOM   1115  N   PHE A 138     -24.241  -3.773   7.385  1.00 11.13           N
ANISOU 1115  N   PHE A 138     1374   1459   1397   -135   -113    112       N
ATOM   1116  CA  PHE A 138     -23.709  -2.427   7.187  1.00 11.37           C
ANISOU 1116  CA  PHE A 138     1531   1433   1356   -131   -107     81       C
ATOM   1117  C   PHE A 138     -23.539  -2.126   5.698  1.00 10.67           C
ANISOU 1117  C   PHE A 138     1372   1438   1244    -58   -178     74       C
ATOM   1118  O   PHE A 138     -23.990  -1.086   5.204  1.00 11.06           O
ANISOU 1118  O   PHE A 138     1498   1452   1253     91   -166    173       O
ATOM   1119  CB  PHE A 138     -22.382  -2.361   7.970  1.00 11.42           C
ANISOU 1119  CB  PHE A 138     1524   1406   1410   -149   -183     43       C
ATOM   1120  CG  PHE A 138     -21.521  -1.141   7.731  1.00 12.30           C
ANISOU 1120  CG  PHE A 138     1565   1485   1624   -113   -147     77       C
ATOM   1121  CD1 PHE A 138     -20.422  -1.213   6.899  1.00 14.24           C
ANISOU 1121  CD1 PHE A 138     1460   1902   2049   -144   -135    126       C
ATOM   1122  CD2 PHE A 138     -21.731   0.032   8.442  1.00 14.20           C
ANISOU 1122  CD2 PHE A 138     1939   1601   1857    -30    -99    -31       C
ATOM   1123  CE1 PHE A 138     -19.580  -0.146   6.744  1.00 15.56           C
ANISOU 1123  CE1 PHE A 138     1779   1911   2223   -327   -129    100       C
ATOM   1124  CE2 PHE A 138     -20.866   1.125   8.253  1.00 15.85           C
ANISOU 1124  CE2 PHE A 138     2157   1717   2149   -228   -102     61       C
ATOM   1125  CZ  PHE A 138     -19.814   1.000   7.422  1.00 16.71           C
ANISOU 1125  CZ  PHE A 138     2194   1902   2255   -332   -175     35       C
ATOM   1126  N   ARG A 139     -22.882  -3.024   4.959  1.00 10.91           N
ANISOU 1126  N   ARG A 139     1391   1520   1236    -95     -1     13       N
ATOM   1127  CA  ARG A 139     -22.671  -2.786   3.529  1.00 10.88           C
ANISOU 1127  CA  ARG A 139     1384   1493   1257     23   -156     14       C
ATOM   1128  C   ARG A 139     -23.968  -2.727   2.750  1.00 11.05           C
ANISOU 1128  C   ARG A 139     1496   1442   1262     86   -151     66       C
ATOM   1129  O   ARG A 139     -24.115  -1.888   1.847  1.00 11.73           O
ANISOU 1129  O   ARG A 139     1548   1545   1363     38   -154    206       O
ATOM   1130  CB  ARG A 139     -21.758  -3.843   2.925  1.00 11.21           C
ANISOU 1130  CB  ARG A 139     1407   1568   1284     34    -57    105       C
ATOM   1131  CG  ARG A 139     -20.354  -3.867   3.485  1.00 11.68           C
ANISOU 1131  CG  ARG A 139     1407   1631   1400     86    -33    160       C
ATOM   1132  CD  ARG A 139     -19.433  -4.698   2.610  1.00 11.92           C
ANISOU 1132  CD  ARG A 139     1485   1563   1481    -55     13    167       C
ATOM   1133  NE  ARG A 139     -19.928  -6.045   2.386  1.00 11.81           N
ANISOU 1133  NE  ARG A 139     1532   1495   1461     43     90    112       N
ATOM   1134  CZ  ARG A 139     -19.783  -7.071   3.222  1.00 12.21           C
ANISOU 1134  CZ  ARG A 139     1595   1495   1549   -121      2    -13       C
ATOM   1135  NH1 ARG A 139     -20.342  -8.223   2.909  1.00 14.16           N
ANISOU 1135  NH1 ARG A 139     1986   1659   1735   -122     49   -146       N
ATOM   1136  NH2 ARG A 139     -19.064  -6.958   4.337  1.00 12.82           N
ANISOU 1136  NH2 ARG A 139     1717   1594   1558     14     64    171       N
ATOM   1137  N   LYS A 140     -24.910  -3.622   3.057  1.00 10.93           N
ANISOU 1137  N   LYS A 140     1334   1427   1393    -15   -114    -44       N
ATOM   1138  CA  LYS A 140     -26.182  -3.625   2.327  1.00 12.13           C
ANISOU 1138  CA  LYS A 140     1523   1449   1639    -89   -206     59       C
ATOM   1139  C   LYS A 140     -26.949  -2.336   2.573  1.00 11.99           C
ANISOU 1139  C   LYS A 140     1534   1490   1530     -3   -109    127       C
ATOM   1140  O   LYS A 140     -27.576  -1.785   1.663  1.00 12.13           O
ANISOU 1140  O   LYS A 140     1449   1650   1509    -27   -223    218       O
ATOM   1141  CB  LYS A 140     -27.004  -4.843   2.753  1.00 13.99           C
ANISOU 1141  CB  LYS A 140     1829   1428   2060   -198   -277    -16       C
ATOM   1142  CG  LYS A 140     -26.530  -6.127   2.090  1.00 16.70           C
ANISOU 1142  CG  LYS A 140     2353   1610   2382    -88   -492     49       C
ATOM   1143  CD  LYS A 140     -27.290  -7.332   2.554  1.00 20.42           C
ANISOU 1143  CD  LYS A 140     2961   1971   2828   -301   -467     32       C
ATOM   1144  CE  LYS A 140     -26.869  -8.566   1.788  1.00 23.08           C
ANISOU 1144  CE  LYS A 140     3404   2249   3117   -345   -516      3       C
ATOM   1145  NZ  LYS A 140     -27.483  -9.806   2.332  1.00 25.89           N
ANISOU 1145  NZ  LYS A 140     3837   2618   3381   -390   -385     23       N
ATOM   1146  N   ASP A 141     -26.933  -1.847   3.814  1.00 11.37           N
ANISOU 1146  N   ASP A 141     1347   1469   1503    -70     17     61       N
ATOM   1147  CA  ASP A 141     -27.644  -0.613   4.105  1.00 12.02           C
ANISOU 1147  CA  ASP A 141     1439   1585   1544    -26    -79     40       C
ATOM   1148  C   ASP A 141     -26.974   0.584   3.441  1.00 12.06           C
ANISOU 1148  C   ASP A 141     1455   1540   1588     56   -162    165       C
ATOM   1149  O   ASP A 141     -27.661   1.487   2.959  1.00 13.36           O
ANISOU 1149  O   ASP A 141     1521   1711   1845    124   -200    159       O
ATOM   1150  CB  ASP A 141     -27.817  -0.468   5.608  1.00 13.31           C
ANISOU 1150  CB  ASP A 141     1558   1949   1549   -130    -11   -174       C
ATOM   1151  CG  ASP A 141     -28.915  -1.391   6.163  1.00 15.43           C
ANISOU 1151  CG  ASP A 141     1822   2381   1660   -268    -66   -289       C
ATOM   1152  OD1 ASP A 141     -29.678  -2.003   5.394  1.00 16.62           O
ANISOU 1152  OD1 ASP A 141     1990   2506   1819   -366    -47   -155       O
ATOM   1153  OD2 ASP A 141     -29.044  -1.462   7.392  1.00 17.26           O
ANISOU 1153  OD2 ASP A 141     2170   2581   1808   -386    -67   -266       O
ATOM   1154  N   ILE A 142     -25.641   0.604   3.396  1.00 11.57           N
ANISOU 1154  N   ILE A 142     1367   1472   1556     45      0    208       N
ATOM   1155  CA  ILE A 142     -24.968   1.649   2.626  1.00 11.92           C
ANISOU 1155  CA  ILE A 142     1401   1643   1486    -67   -222    224       C
ATOM   1156  C   ILE A 142     -25.333   1.559   1.162  1.00 11.66           C
ANISOU 1156  C   ILE A 142     1345   1570   1514     91   -141    149       C
ATOM   1157  O   ILE A 142     -25.612   2.581   0.511  1.00 12.14           O
ANISOU 1157  O   ILE A 142     1489   1491   1634    109   -199    290       O
ATOM   1158  CB  ILE A 142     -23.448   1.571   2.830  1.00 12.39           C
ANISOU 1158  CB  ILE A 142     1456   1694   1556   -211   -240    132       C
ATOM   1159  CG1 ILE A 142     -23.132   1.940   4.273  1.00 14.17           C
ANISOU 1159  CG1 ILE A 142     1710   1882   1791   -208   -317     54       C
ATOM   1160  CG2 ILE A 142     -22.737   2.458   1.809  1.00 12.59           C
ANISOU 1160  CG2 ILE A 142     1477   1668   1640   -159   -121    172       C
ATOM   1161  CD1 ILE A 142     -21.713   1.700   4.616  1.00 15.65           C
ANISOU 1161  CD1 ILE A 142     1951   2044   1952     23   -325     22       C
ATOM   1162  N   ALA A 143     -25.331   0.343   0.610  1.00 11.61           N
ANISOU 1162  N   ALA A 143     1496   1553   1361     78   -176     54       N
ATOM   1163  CA  ALA A 143     -25.654   0.178  -0.802  1.00 12.77           C
ANISOU 1163  CA  ALA A 143     1732   1667   1453     43   -310    191       C
ATOM   1164  C   ALA A 143     -27.045   0.701  -1.138  1.00 12.96           C
ANISOU 1164  C   ALA A 143     1605   1812   1506    -31   -341    308       C
ATOM   1165  O   ALA A 143     -27.262   1.233  -2.235  1.00 13.31           O
ANISOU 1165  O   ALA A 143     1641   1887   1530     13   -308    288       O
ATOM   1166  CB  ALA A 143     -25.500  -1.285  -1.196  1.00 13.76           C
ANISOU 1166  CB  ALA A 143     1894   1729   1604     95   -187    154       C
ATOM   1167  N   ALA A 144     -28.000   0.538  -0.224  1.00 13.20           N
ANISOU 1167  N   ALA A 144     1428   1945   1644    -14   -192    335       N
ATOM   1168  CA  ALA A 144     -29.328   1.070  -0.472  1.00 13.97           C
ANISOU 1168  CA  ALA A 144     1514   2015   1780     44   -140    376       C
ATOM   1169  C   ALA A 144     -29.287   2.580  -0.624  1.00 13.51           C
ANISOU 1169  C   ALA A 144     1485   1964   1683     74   -175    255       C
ATOM   1170  O   ALA A 144     -29.986   3.145  -1.477  1.00 14.56           O
ANISOU 1170  O   ALA A 144     1562   2126   1845    100   -349    404       O
ATOM   1171  CB  ALA A 144     -30.276   0.646   0.661  1.00 15.55           C
ANISOU 1171  CB  ALA A 144     1726   2156   2027    -54    -10    457       C
ATOM   1172  N   LYS A 145     -28.492   3.252   0.207  1.00 12.81           N
ANISOU 1172  N   LYS A 145     1451   1810   1607     95    -68    130       N
ATOM   1173  CA  LYS A 145     -28.341   4.696   0.078  1.00 13.53           C
ANISOU 1173  CA  LYS A 145     1502   1876   1762    198   -117    101       C
ATOM   1174  C   LYS A 145     -27.610   5.072  -1.200  1.00 13.44           C
ANISOU 1174  C   LYS A 145     1400   1901   1804    302   -148    236       C
ATOM   1175  O   LYS A 145     -27.973   6.062  -1.858  1.00 14.17           O
ANISOU 1175  O   LYS A 145     1508   1936   1940    294   -150    299       O
ATOM   1176  CB  LYS A 145     -27.598   5.290   1.272  1.00 14.25           C
ANISOU 1176  CB  LYS A 145     1578   2001   1836    126   -151     60       C
ATOM   1177  CG  LYS A 145     -28.218   5.072   2.638  1.00 16.51           C
ANISOU 1177  CG  LYS A 145     1942   2289   2041    129   -117    177       C
ATOM   1178  CD  LYS A 145     -29.629   5.622   2.695  1.00 17.49           C
ANISOU 1178  CD  LYS A 145     1855   2644   2144    -75     66     30       C
ATOM   1179  CE  LYS A 145     -30.168   5.511   4.127  1.00 18.60           C
ANISOU 1179  CE  LYS A 145     1883   2872   2312    -21    285   -133       C
ATOM   1180  NZ  LYS A 145     -31.552   6.014   4.177  1.00 19.35           N
ANISOU 1180  NZ  LYS A 145     1902   3013   2438    -87    259   -123       N
ATOM   1181  N   TYR A 146     -26.580   4.299  -1.566  1.00 12.79           N
ANISOU 1181  N   TYR A 146     1331   1839   1689    173     37    309       N
ATOM   1182  CA  TYR A 146     -25.915   4.544  -2.841  1.00 13.06           C
ANISOU 1182  CA  TYR A 146     1479   1925   1557    173    -16    347       C
ATOM   1183  C   TYR A 146     -26.910   4.482  -3.987  1.00 13.64           C
ANISOU 1183  C   TYR A 146     1574   2053   1557     11    -78    437       C
ATOM   1184  O   TYR A 146     -26.868   5.314  -4.902  1.00 15.60           O
ANISOU 1184  O   TYR A 146     1828   2363   1736    -26    -89    583       O
ATOM   1185  CB  TYR A 146     -24.827   3.501  -3.083  1.00 13.10           C
ANISOU 1185  CB  TYR A 146     1481   1914   1585    102   -142    268       C
ATOM   1186  CG  TYR A 146     -23.526   3.696  -2.358  1.00 12.30           C
ANISOU 1186  CG  TYR A 146     1345   1809   1519     90    -41    100       C
ATOM   1187  CD1 TYR A 146     -22.417   2.985  -2.765  1.00 14.81           C
ANISOU 1187  CD1 TYR A 146     1631   2197   1799    115   -140   -198       C
ATOM   1188  CD2 TYR A 146     -23.372   4.557  -1.290  1.00 11.76           C
ANISOU 1188  CD2 TYR A 146     1415   1704   1348     21    -38    122       C
ATOM   1189  CE1 TYR A 146     -21.193   3.137  -2.137  1.00 14.75           C
ANISOU 1189  CE1 TYR A 146     1549   2220   1834    171   -117   -291       C
ATOM   1190  CE2 TYR A 146     -22.137   4.741  -0.656  1.00 11.86           C
ANISOU 1190  CE2 TYR A 146     1447   1639   1421     92     97    101       C
ATOM   1191  CZ  TYR A 146     -21.052   4.066  -1.133  1.00 12.35           C
ANISOU 1191  CZ  TYR A 146     1314   1844   1535     62    -85   -179       C
ATOM   1192  OH  TYR A 146     -19.832   4.307  -0.516  1.00 13.21           O
ANISOU 1192  OH  TYR A 146     1438   1867   1712     84    -83   -256       O
ATOM   1193  N   LYS A 147     -27.801   3.489  -3.975  1.00 13.96           N
ANISOU 1193  N   LYS A 147     1519   2143   1642     54   -288    421       N
ATOM   1194  CA  LYS A 147     -28.768   3.356  -5.061  1.00 16.16           C
ANISOU 1194  CA  LYS A 147     1914   2321   1903    101   -536    464       C
ATOM   1195  C   LYS A 147     -29.708   4.551  -5.103  1.00 16.03           C
ANISOU 1195  C   LYS A 147     1737   2449   1905    159   -329    516       C
ATOM   1196  O   LYS A 147     -30.033   5.051  -6.191  1.00 16.97           O
ANISOU 1196  O   LYS A 147     1945   2598   1906    209   -428    550       O
ATOM   1197  CB  LYS A 147     -29.532   2.052  -4.881  1.00 19.10           C
ANISOU 1197  CB  LYS A 147     2186   2659   2410   -120   -815    366       C
ATOM   1198  CG  LYS A 147     -28.731   0.799  -5.199  1.00 25.02           C
ANISOU 1198  CG  LYS A 147     3264   3170   3072   -188   -743    260       C
ATOM   1199  CD  LYS A 147     -29.573  -0.473  -4.986  1.00 29.38           C
ANISOU 1199  CD  LYS A 147     4076   3520   3567   -150   -814    202       C
ATOM   1200  CE  LYS A 147     -28.798  -1.725  -5.367  1.00 32.20           C
ANISOU 1200  CE  LYS A 147     4626   3763   3846    -64   -884    162       C
ATOM   1201  NZ  LYS A 147     -27.637  -1.976  -4.480  1.00 33.84           N
ANISOU 1201  NZ  LYS A 147     4983   3903   3973    -32   -902    150       N
ATOM   1202  N   GLU A 148     -30.119   5.061  -3.932  1.00 15.99           N
ANISOU 1202  N   GLU A 148     1492   2564   2020    180   -203    545       N
ATOM   1203  CA  GLU A 148     -30.980   6.237  -3.910  1.00 16.55           C
ANISOU 1203  CA  GLU A 148     1588   2621   2079    317   -103    597       C
ATOM   1204  C   GLU A 148     -30.301   7.422  -4.544  1.00 17.03           C
ANISOU 1204  C   GLU A 148     1774   2538   2158    395    -82    647       C
ATOM   1205  O   GLU A 148     -30.965   8.255  -5.153  1.00 19.40           O
ANISOU 1205  O   GLU A 148     2136   2703   2532    538    -53    876       O
ATOM   1206  CB  GLU A 148     -31.384   6.570  -2.478  1.00 17.58           C
ANISOU 1206  CB  GLU A 148     1720   2830   2129    205     40    599       C
ATOM   1207  CG  GLU A 148     -32.278   5.534  -1.913  1.00 18.03           C
ANISOU 1207  CG  GLU A 148     1651   3033   2166      8      3    569       C
ATOM   1208  CD  GLU A 148     -32.584   5.749  -0.452  1.00 19.41           C
ANISOU 1208  CD  GLU A 148     1903   3193   2278   -173     -7    511       C
ATOM   1209  OE1 GLU A 148     -33.379   4.977   0.078  1.00 21.05           O
ANISOU 1209  OE1 GLU A 148     2134   3420   2443   -331     -7    455       O
ATOM   1210  OE2 GLU A 148     -31.970   6.617   0.204  1.00 20.94           O
ANISOU 1210  OE2 GLU A 148     2267   3304   2385   -135     44    484       O
ATOM   1211  N   LEU A 149     -28.991   7.525  -4.421  1.00 16.34           N
ANISOU 1211  N   LEU A 149     1811   2342   2055    243     60    473       N
ATOM   1212  CA  LEU A 149     -28.227   8.608  -5.024  1.00 16.98           C
ANISOU 1212  CA  LEU A 149     2083   2265   2104    331     35    443       C
ATOM   1213  C   LEU A 149     -27.845   8.327  -6.468  1.00 18.17           C
ANISOU 1213  C   LEU A 149     2393   2417   2094    298    163    525       C
ATOM   1214  O   LEU A 149     -27.248   9.194  -7.126  1.00 20.65           O
ANISOU 1214  O   LEU A 149     3078   2484   2282    117    281    510       O
ATOM   1215  CB  LEU A 149     -26.952   8.834  -4.201  1.00 17.90           C
ANISOU 1215  CB  LEU A 149     2056   2425   2320    277    -13    198       C
ATOM   1216  CG  LEU A 149     -27.174   9.509  -2.849  1.00 19.34           C
ANISOU 1216  CG  LEU A 149     2213   2725   2412    294   -252     88       C
ATOM   1217  CD1 LEU A 149     -26.015   9.279  -1.968  1.00 20.41           C
ANISOU 1217  CD1 LEU A 149     2287   2985   2482     79   -388     77       C
ATOM   1218  CD2 LEU A 149     -27.398  11.019  -3.078  1.00 20.37           C
ANISOU 1218  CD2 LEU A 149     2375   2784   2582    360   -154    -44       C
ATOM   1219  N   GLY A 150     -28.142   7.149  -6.992  1.00 19.04           N
ANISOU 1219  N   GLY A 150     2408   2809   2016    521    -73    625       N
ATOM   1220  CA  GLY A 150     -27.645   6.832  -8.323  1.00 21.62           C
ANISOU 1220  CA  GLY A 150     2841   3302   2071    601     32    717       C
ATOM   1221  C   GLY A 150     -26.148   6.600  -8.416  1.00 22.72           C
ANISOU 1221  C   GLY A 150     2886   3571   2175    835    143    863       C
ATOM   1222  O   GLY A 150     -25.595   6.663  -9.531  1.00 24.59           O
ANISOU 1222  O   GLY A 150     3222   3831   2289    767    268    806       O
ATOM   1223  N   TYR A 151     -25.461   6.360  -7.286  1.00 22.18           N
ANISOU 1223  N   TYR A 151     2661   3454   2311   1078    127    873       N
ATOM   1224  CA  TYR A 151     -24.011   6.139  -7.304  1.00 23.40           C
ANISOU 1224  CA  TYR A 151     2904   3502   2485    933     21    760       C
ATOM   1225  C   TYR A 151     -23.742   4.695  -7.666  1.00 25.65           C
ANISOU 1225  C   TYR A 151     3403   3555   2787    758   -199    764       C
ATOM   1226  O   TYR A 151     -24.290   3.808  -7.024  1.00 27.39           O
ANISOU 1226  O   TYR A 151     3733   3692   2980    596   -109    639       O
ATOM   1227  CB  TYR A 151     -23.357   6.541  -5.976  1.00 22.52           C
ANISOU 1227  CB  TYR A 151     2691   3523   2342    662    150    713       C
ATOM   1228  CG  TYR A 151     -21.880   6.195  -5.878  1.00 21.86           C
ANISOU 1228  CG  TYR A 151     2484   3585   2238    546     77    667       C
ATOM   1229  CD1 TYR A 151     -20.970   6.640  -6.851  1.00 22.19           C
ANISOU 1229  CD1 TYR A 151     2538   3651   2243    610     35    761       C
ATOM   1230  CD2 TYR A 151     -21.391   5.453  -4.809  1.00 21.78           C
ANISOU 1230  CD2 TYR A 151     2384   3611   2279    498     -9    449       C
ATOM   1231  CE1 TYR A 151     -19.606   6.339  -6.762  1.00 22.26           C
ANISOU 1231  CE1 TYR A 151     2417   3738   2302    556     -5    641       C
ATOM   1232  CE2 TYR A 151     -20.031   5.142  -4.719  1.00 22.04           C
ANISOU 1232  CE2 TYR A 151     2365   3683   2327    461    -23    349       C
ATOM   1233  CZ  TYR A 151     -19.153   5.593  -5.680  1.00 22.06           C
ANISOU 1233  CZ  TYR A 151     2266   3813   2303    465    -34    450       C
ATOM   1234  OH  TYR A 151     -17.824   5.254  -5.572  1.00 22.70           O
ANISOU 1234  OH  TYR A 151     2292   3952   2383    255    -99    259       O
TER
HETATM 1235  N   NO3 D 201     -16.129 -16.874  19.493  1.00 16.86           N
ANISOU 1235  N   NO3 D 201     2190   2041   2176    -41    -27    366       N
HETATM 1236  O1  NO3 D 201     -17.086 -16.532  20.247  1.00 17.95           O
ANISOU 1236  O1  NO3 D 201     2444   2157   2219     95    220    407       O
HETATM 1237  O2  NO3 D 201     -14.982 -16.367  19.697  1.00 17.51           O
ANISOU 1237  O2  NO3 D 201     2163   2331   2161   -279   -186    318       O
HETATM 1238  O3  NO3 D 201     -16.334 -17.705  18.538  1.00 16.42           O
ANISOU 1238  O3  NO3 D 201     2276   1764   2198     50   -172    192       O
TER
HETATM 1239  NB  HEM C   1     -15.202   4.597   6.497  1.00  9.80           N
ANISOU 1239  NB  HEM C   1     1383   1212   1127      2     63    105       N
HETATM 1240  ND  HEM C   1     -13.330   7.601   4.570  1.00  9.94           N
ANISOU 1240  ND  HEM C   1     1358   1304   1116     29     78     36       N
HETATM 1241  C1A HEM C   1     -14.544   8.747   7.050  1.00 10.50           C
ANISOU 1241  C1A HEM C   1     1544   1278   1168     96    121     66       C
HETATM 1242  C1B HEM C   1     -15.872   4.671   7.698  1.00  9.72           C
ANISOU 1242  C1B HEM C   1     1291   1307   1095      8     83    126       C
HETATM 1243  C1C HEM C   1     -13.940   3.455   4.031  1.00 10.02           C
ANISOU 1243  C1C HEM C   1     1326   1282   1198    143     12     97       C
HETATM 1244  C1D HEM C   1     -12.580   7.491   3.413  1.00  9.90           C
ANISOU 1244  C1D HEM C   1     1373   1272   1115      0     89     73       C
HETATM 1245  C2A HEM C   1     -15.204   9.298   8.195  1.00 11.13           C
ANISOU 1245  C2A HEM C   1     1599   1356   1275    104    202    -34       C
HETATM 1246  C2B HEM C   1     -16.318   3.361   8.092  1.00 10.11           C
ANISOU 1246  C2B HEM C   1     1342   1372   1128     11     63    124       C
HETATM 1247  C2C HEM C   1     -13.218   2.856   2.931  1.00 10.15           C
ANISOU 1247  C2C HEM C   1     1349   1285   1224     43    165      9       C
HETATM 1248  C2D HEM C   1     -11.881   8.736   3.180  1.00 10.19           C
ANISOU 1248  C2D HEM C   1     1389   1313   1169    -43    114    107       C
HETATM 1249  C3A HEM C   1     -15.794   8.288   8.841  1.00 11.11           C
ANISOU 1249  C3A HEM C   1     1517   1404   1299     89    219     34       C
HETATM 1250  C3B HEM C   1     -15.927   2.503   7.131  1.00 10.41           C
ANISOU 1250  C3B HEM C   1     1419   1322   1213    -88     59    147       C
HETATM 1251  C3C HEM C   1     -12.589   3.866   2.283  1.00  9.85           C
ANISOU 1251  C3C HEM C   1     1307   1422   1015    -36    -14    -55       C
HETATM 1252  C3D HEM C   1     -12.209   9.556   4.184  1.00 10.52           C
ANISOU 1252  C3D HEM C   1     1418   1356   1223    117     74     94       C
HETATM 1253  C4A HEM C   1     -15.572   7.074   8.101  1.00 10.45           C
ANISOU 1253  C4A HEM C   1     1485   1309   1176     15    150     24       C
HETATM 1254  C4B HEM C   1     -15.245   3.273   6.119  1.00  9.69           C
ANISOU 1254  C4B HEM C   1     1311   1229   1144      7     57    109       C
HETATM 1255  C4C HEM C   1     -12.901   5.097   2.975  1.00  9.79           C
ANISOU 1255  C4C HEM C   1     1300   1310   1112     26     -3    -83       C
HETATM 1256  C4D HEM C   1     -13.131   8.857   5.063  1.00 10.37           C
ANISOU 1256  C4D HEM C   1     1364   1363   1211    -45     62     82       C
HETATM 1257  CAA HEM C   1     -15.209  10.774   8.588  1.00 11.81           C
ANISOU 1257  CAA HEM C   1     1734   1430   1324     84    216    -88       C
HETATM 1258  CAB HEM C   1     -16.098   0.997   7.052  1.00 11.41           C
ANISOU 1258  CAB HEM C   1     1480   1412   1443    -99    193    197       C
HETATM 1259  CAC HEM C   1     -11.633   3.827   1.112  1.00 10.80           C
ANISOU 1259  CAC HEM C   1     1385   1620   1098     44    -87     -1       C
HETATM 1260  CAD HEM C   1     -11.609  10.941   4.491  1.00 11.71           C
ANISOU 1260  CAD HEM C   1     1603   1454   1393    -75    -17     54       C
HETATM 1261  CBA HEM C   1     -16.607  11.420   8.336  1.00 12.41           C
ANISOU 1261  CBA HEM C   1     1826   1590   1300    215     90    -23       C
HETATM 1262  CBB HEM C   1     -16.014   0.203   8.113  1.00 12.63           C
ANISOU 1262  CBB HEM C   1     1727   1493   1580   -125    188    219       C
HETATM 1263  CBC HEM C   1     -11.193   2.746   0.459  1.00 11.50           C
ANISOU 1263  CBC HEM C   1     1421   1650   1297     29   -132   -242       C
HETATM 1264  CBD HEM C   1     -10.337  10.650   5.346  1.00 12.11           C
ANISOU 1264  CBD HEM C   1     1517   1488   1595   -208     42     22       C
HETATM 1265  CGA HEM C   1     -17.084  11.268   6.925  1.00 13.22           C
ANISOU 1265  CGA HEM C   1     2003   1593   1427     99    149     10       C
HETATM 1266  CGD HEM C   1      -9.551  11.881   5.682  1.00 13.66           C
ANISOU 1266  CGD HEM C   1     1619   1769   1803    -89    211   -207       C
HETATM 1267  CHA HEM C   1     -13.739   9.413   6.165  1.00 10.51           C
ANISOU 1267  CHA HEM C   1     1404   1397   1193     32    188     77       C
HETATM 1268  CHB HEM C   1     -16.039   5.828   8.426  1.00  9.98           C
ANISOU 1268  CHB HEM C   1     1398   1256   1137    -64    112     22       C
HETATM 1269  CHC HEM C   1     -14.667   2.742   4.967  1.00 10.01           C
ANISOU 1269  CHC HEM C   1     1295   1355   1153     79     56    102       C
HETATM 1270  CHD HEM C   1     -12.444   6.349   2.665  1.00  9.99           C
ANISOU 1270  CHD HEM C   1     1413   1244   1140     43    -36      7       C
HETATM 1271  CMA HEM C   1     -16.601   8.376  10.149  1.00 12.73           C
ANISOU 1271  CMA HEM C   1     1852   1618   1368     39    316    -55       C
HETATM 1272  CMB HEM C   1     -17.115   3.110   9.356  1.00 11.49           C
ANISOU 1272  CMB HEM C   1     1600   1557   1207   -114    228    178       C
HETATM 1273  CMC HEM C   1     -13.200   1.376   2.589  1.00 11.90           C
ANISOU 1273  CMC HEM C   1     1881   1328   1312     43    211    -31       C
HETATM 1274  CMD HEM C   1     -10.941   8.987   2.001  1.00 11.32           C
ANISOU 1274  CMD HEM C   1     1606   1523   1171    -97    229     82       C
HETATM 1275  NA  HEM C   1     -14.827   7.386   6.986  1.00 10.16           N
ANISOU 1275  NA  HEM C   1     1342   1312   1208     20     63     11       N
HETATM 1276  NC  HEM C   1     -13.724   4.837   4.055  1.00  9.87           N
ANISOU 1276  NC  HEM C   1     1248   1276   1225    -33     15     55       N
HETATM 1277  O1A HEM C   1     -16.398  11.765   6.002  1.00 14.40           O
ANISOU 1277  O1A HEM C   1     2250   1805   1416    207    221     76       O
HETATM 1278  O1D HEM C   1     -10.105  12.856   6.250  1.00 17.02           O
ANISOU 1278  O1D HEM C   1     2069   2080   2319   -204    308   -506       O
HETATM 1279  O2A HEM C   1     -18.149  10.661   6.684  1.00 14.59           O
ANISOU 1279  O2A HEM C   1     2110   1906   1526   -110   -118    -37       O
HETATM 1280  O2D HEM C   1      -8.353  12.012   5.383  1.00 14.16           O
ANISOU 1280  O2D HEM C   1     1750   1873   1756   -409    142   -129       O
HETATM 1281 FE   HEM C   1     -14.383   6.120   5.459  1.00  9.74          Fe
ANISOU 1281 FE   HEM C   1     1304   1212   1183     65    101     98      Fe
TER
HETATM 1282  O1  OXY C 101     -11.461   5.567   6.224  1.00 19.15           O
ANISOU 1282  O1  OXY C 101     2393   2746   2138    212    178    -42       O
HETATM 1283  O2  OXY C 101     -12.629   5.740   6.630  1.00 14.36           O
ANISOU 1283  O2  OXY C 101     1763   1955   1736    119    240    103       O
TER
HETATM 1284  O   HOH S   1     -12.152  -3.719  26.677  1.00 13.23           O
ANISOU 1284  O   HOH S   1     1635   2098   1292   -171   -102   -142       O
HETATM 1285  O   HOH S   2      -7.637  11.222   2.897  1.00 14.65           O
ANISOU 1285  O   HOH S   2     1779   1983   1803   -336    343   -147       O
HETATM 1286  O   HOH S   3     -25.843  -1.826  13.520  1.00 18.47           O
ANISOU 1286  O   HOH S   3     2744   1742   2532   -563   -960    333       O
HETATM 1287  O   HOH S   4     -23.473   9.642  11.649  1.00 16.47           O
ANISOU 1287  O   HOH S   4     1912   1873   2473   -326    -22   -195       O
HETATM 1288  O   HOH S   5     -21.251  -5.962  -0.051  1.00 17.93           O
ANISOU 1288  O   HOH S   5     1849   2969   1995   -288   -406    193       O
HETATM 1289  O   HOH S   6     -24.205   4.087  19.377  1.00 16.75           O
ANISOU 1289  O   HOH S   6     2430   1992   1943    350    288   -204       O
HETATM 1290  O   HOH S   7     -19.502  -2.949  22.415  1.00 19.46           O
ANISOU 1290  O   HOH S   7     2848   1842   2704   -257   -308    -61       O
HETATM 1291  O   HOH S   8      -9.427  12.213   1.128  1.00 19.39           O
ANISOU 1291  O   HOH S   8     1926   2555   2886   -237    -67    965       O
HETATM 1292  O   HOH S   9     -12.009  12.138   0.170  1.00 17.76           O
ANISOU 1292  O   HOH S   9     1869   2447   2433   -202    -55    570       O
HETATM 1293  O   HOH S  10     -12.073   7.583   8.766  1.00 15.23           O
ANISOU 1293  O   HOH S  10     1943   2179   1663     97     38    208       O
HETATM 1294  O   HOH S  11     -11.487  10.383   8.840  1.00 17.69           O
ANISOU 1294  O   HOH S  11     2302   2366   2053   -126    417    243       O
HETATM 1295  O   HOH S  12     -18.153  -1.890  -6.284  1.00 19.71           O
ANISOU 1295  O   HOH S  12     3315   2452   1721   -318   -808      8       O
HETATM 1296  O   HOH S  13     -19.089  -9.342   5.798  1.00 19.79           O
ANISOU 1296  O   HOH S  13     3359   1998   2165    514    944    517       O
HETATM 1297  O   HOH S  14     -12.411  12.707   7.481  1.00 22.76           O
ANISOU 1297  O   HOH S  14     2498   2801   3349   -369    867  -1092       O
HETATM 1298  O   HOH S  15     -31.694  -0.523   4.030  1.00 26.95           O
ANISOU 1298  O   HOH S  15     2305   3790   4146   -163    458    771       O
HETATM 1299  O   HOH S  16      -5.938   3.762  13.543  1.00 17.08           O
ANISOU 1299  O   HOH S  16     2234   2318   1937    -91   -175    -70       O
HETATM 1300  O   HOH S  17       0.807  12.157   9.389  1.00 26.28           O
ANISOU 1300  O   HOH S  17     2956   3685   3343   -719    107    723       O
HETATM 1301  O   HOH S  18     -14.630  13.705   5.931  1.00 19.82           O
ANISOU 1301  O   HOH S  18     3104   1819   2607    -24    854    -24       O
HETATM 1302  O   HOH S  19      -8.452  -6.247   2.614  1.00 25.67           O
ANISOU 1302  O   HOH S  19     2300   4894   2558   1111    687    313       O
HETATM 1303  O   HOH S  20     -11.646  10.180  -1.993  1.00 16.87           O
ANISOU 1303  O   HOH S  20     1934   2217   2258     15     19    298       O
HETATM 1304  O   HOH S  21       1.161  10.743   6.716  1.00 26.99           O
ANISOU 1304  O   HOH S  21     2886   3353   4014   -443    500   1847       O
HETATM 1305  O   HOH S  22     -15.737   2.082  19.177  1.00 22.14           O
ANISOU 1305  O   HOH S  22     3588   2101   2723    -10   -306    307       O
HETATM 1306  O   HOH S  23     -22.967  13.324   4.857  1.00 23.03           O
ANISOU 1306  O   HOH S  23     3202   2126   3422    448    460    334       O
HETATM 1307  O   HOH S  24      -5.187  -5.242  -6.199  1.00 42.04           O
ANISOU 1307  O   HOH S  24     4674   7626   3674   2646   -770  -2238       O
HETATM 1308  O   HOH S  25      -7.603  -5.476  -5.204  1.00 22.90           O
ANISOU 1308  O   HOH S  25     3718   2588   2395    730     86   -427       O
HETATM 1309  O   HOH S  26     -22.455 -19.307  15.262  1.00 24.80           O
ANISOU 1309  O   HOH S  26     4864   3039   1519  -1541    225     -4       O
HETATM 1310  O   HOH S  27     -22.581 -16.511  14.893  1.00 24.07           O
ANISOU 1310  O   HOH S  27     3035   2794   3315    -18  -1111    360       O
HETATM 1311  O   HOH S  28     -18.255  -1.102  24.048  1.00 27.02           O
ANISOU 1311  O   HOH S  28     2303   2957   5006   -682   -763    639       O
HETATM 1312  O   HOH S  29     -30.735 -14.780  19.856  1.00 23.18           O
ANISOU 1312  O   HOH S  29     2208   2381   4220   -407    860    307       O
HETATM 1313  O   HOH S  30      -1.991  -5.163   9.122  1.00 24.36           O
ANISOU 1313  O   HOH S  30     2596   3652   3007   1134   -299   -195       O
HETATM 1314  O   HOH S  31      -9.102  10.528  15.196  1.00 33.41           O
ANISOU 1314  O   HOH S  31     4464   3575   4656    538  -1090  -1334       O
HETATM 1315  O   HOH S  32      -3.286  16.173   7.374  1.00 35.51           O
ANISOU 1315  O   HOH S  32     2548   5818   5127    686   -856  -1173       O
HETATM 1316  O   HOH S  33     -19.565   4.067  20.744  1.00 22.05           O
ANISOU 1316  O   HOH S  33     2599   2556   3223     27    370    237       O
HETATM 1317  O   HOH S  34     -15.674 -13.910  21.578  1.00 47.57           O
ANISOU 1317  O   HOH S  34     6865   5976   5232    -95    383    797       O
HETATM 1318  O   HOH S  35     -10.641 -11.802   6.019  1.00 29.29           O
ANISOU 1318  O   HOH S  35     5041   2662   3426    209   -174    -24       O
HETATM 1319  O   HOH S  36     -30.248   1.648   4.323  1.00 23.32           O
ANISOU 1319  O   HOH S  36     2027   3117   3718    649    682    284       O
HETATM 1320  O   HOH S  37     -32.823   2.989  12.722  1.00 31.11           O
ANISOU 1320  O   HOH S  37     1879   5942   4001   -414   -112   2096       O
HETATM 1321  O   HOH S  38     -23.646 -15.773  12.484  1.00 22.19           O
ANISOU 1321  O   HOH S  38     2580   3010   2841   -164   -206    731       O
HETATM 1322  O   HOH S  39     -17.941 -18.575  10.908  1.00 37.97           O
ANISOU 1322  O   HOH S  39     7670   3308   3447   1210   -132   -634       O
HETATM 1323  O   HOH S  40     -22.477  -8.379   0.832  1.00 29.90           O
ANISOU 1323  O   HOH S  40     3771   4772   2817  -1974    278   -562       O
HETATM 1324  O   HOH S  41      -9.112  14.786   1.991  1.00 28.45           O
ANISOU 1324  O   HOH S  41     4057   2615   4140   -513   -856   -106       O
HETATM 1325  O   HOH S  42     -12.828   6.270  -8.826  1.00 38.38           O
ANISOU 1325  O   HOH S  42     7641   4768   2173   -306  -1032    282       O
HETATM 1326  O   HOH S  43      -9.393  17.795   7.169  1.00 26.66           O
ANISOU 1326  O   HOH S  43     4149   2363   3616    416    669    659       O
HETATM 1327  O   HOH S  44      -0.839  -2.041  17.877  1.00 43.57           O
ANISOU 1327  O   HOH S  44     3803   4818   7935    258  -1076   1594       O
HETATM 1328  O   HOH S  45     -31.631   0.590  10.306  1.00 36.13           O
ANISOU 1328  O   HOH S  45     3780   4053   5895   -839  -2100   1207       O
HETATM 1329  O   HOH S  46      -9.967  11.241  10.971  1.00 28.00           O
ANISOU 1329  O   HOH S  46     4881   2827   2931  -1252    -77    453       O
HETATM 1330  O   HOH S  47     -20.001   1.101  24.974  1.00 42.06           O
ANISOU 1330  O   HOH S  47     5963   7403   2616  -1640    596  -1370       O
HETATM 1331  O   HOH S  48     -31.309  -7.162  14.550  1.00 43.42           O
ANISOU 1331  O   HOH S  48     5301   4363   6835   -617  -3502    975       O
HETATM 1332  O   HOH S  49     -24.704  -3.285  10.839  1.00 22.01           O
ANISOU 1332  O   HOH S  49     2760   3249   2353    746   -234   -236       O
HETATM 1333  O   HOH S  50     -22.084   5.276  20.521  1.00 21.74           O
ANISOU 1333  O   HOH S  50     2655   2957   2649   -321    208   -484       O
HETATM 1334  O   HOH S  51     -31.805   8.260   2.643  1.00 30.01           O
ANISOU 1334  O   HOH S  51     2372   5313   3716    125    347    952       O
HETATM 1335  O   HOH S  52     -25.858  -1.583  22.425  1.00 29.94           O
ANISOU 1335  O   HOH S  52     5059   4144   2173    330    303    356       O
HETATM 1336  O   HOH S  53      -5.464  -6.027  20.433  1.00 31.21           O
ANISOU 1336  O   HOH S  53     3041   6012   2805    194    -64   1152       O
HETATM 1337  O   HOH S  54     -13.753   3.736  19.427  1.00 29.85           O
ANISOU 1337  O   HOH S  54     3184   3981   4175    297   -184    479       O
HETATM 1338  O   HOH S  55       3.693  11.510   5.473  1.00 42.15           O
ANISOU 1338  O   HOH S  55     5688   5847   4479   1185   -842   -940       O
HETATM 1339  O   HOH S  56     -17.510   4.197  19.064  1.00 23.26           O
ANISOU 1339  O   HOH S  56     2656   4371   1809   -111    -75    276       O
HETATM 1340  O   HOH S  57     -31.032   5.651  14.025  1.00 21.83           O
ANISOU 1340  O   HOH S  57     2425   2759   3110    311    522    358       O
HETATM 1341  O   HOH S  59     -19.682  13.360  -6.042  1.00 31.10           O
ANISOU 1341  O   HOH S  59     4143   4244   3431   1267   1093   1062       O
HETATM 1342  O   HOH S  60     -23.844  -1.044  23.826  1.00 46.90           O
ANISOU 1342  O   HOH S  60     6928   7548   3344    622   1185    400       O
HETATM 1343  O   HOH S  61       5.310   8.284   7.317  1.00 31.90           O
ANISOU 1343  O   HOH S  61     3721   3355   5043  -1078    -75    463       O
HETATM 1344  O   HOH S  62     -31.653  -5.300  17.178  1.00 38.37           O
ANISOU 1344  O   HOH S  62     2830   4195   7555   -715    204    718       O
HETATM 1345  O   HOH S  63     -20.179  10.989   8.456  1.00 19.03           O
ANISOU 1345  O   HOH S  63     2096   2632   2502    -89    287    330       O
HETATM 1346  O   HOH S  65     -21.030   9.416  10.550  1.00 17.30           O
ANISOU 1346  O   HOH S  65     1967   2549   2056     -3     64     21       O
HETATM 1347  O   HOH S  66     -32.392   3.164   4.707  1.00 21.87           O
ANISOU 1347  O   HOH S  66     1758   3674   2879   -309   -293    361       O
HETATM 1348  O   HOH S  67     -13.554   5.325 -10.844  1.00 34.62           O
ANISOU 1348  O   HOH S  67     7138   3539   2477   1393  -1375     18       O
HETATM 1349  O   HOH S  69      -8.623  16.998   0.217  1.00 38.60           O
ANISOU 1349  O   HOH S  69     3428   7711   3526  -1540   -488   -227       O
HETATM 1350  O   HOH S  70      -1.176  12.874  -0.097  1.00 35.40           O
ANISOU 1350  O   HOH S  70     6675   3482   3293  -1491    191    -89       O
HETATM 1351  O   HOH S  71     -26.063   3.464  21.349  1.00 40.83           O
ANISOU 1351  O   HOH S  71     5007   6523   3982    135    276  -1993       O
HETATM 1352  O   HOH S  72     -32.535   4.252  17.565  1.00 44.43           O
ANISOU 1352  O   HOH S  72     4570   5917   6393   1585   2309   1087       O
HETATM 1353  O   HOH S  73       8.026   8.217   6.992  1.00 33.21           O
ANISOU 1353  O   HOH S  73     4642   4054   3923    -71    510   -815       O
HETATM 1354  O   HOH S  74     -20.754 -20.165  13.253  1.00 30.44           O
ANISOU 1354  O   HOH S  74     4939   3708   2917    653    726    268       O
HETATM 1355  O   HOH S  75      -0.559  12.905   5.818  1.00 24.41           O
ANISOU 1355  O   HOH S  75     3492   3280   2504  -1076   -577    676       O
HETATM 1356  O   HOH S  76     -13.185  13.947   9.547  1.00 43.87           O
ANISOU 1356  O   HOH S  76     6174   5772   4722   -156   2135  -2341       O
HETATM 1357  O   HOH S  77     -30.357  -6.821  12.589  1.00 34.11           O
ANISOU 1357  O   HOH S  77     3223   2789   6947    300  -2037   -458       O
HETATM 1358  O   HOH S  78      -8.079  10.393  17.779  1.00 52.92           O
ANISOU 1358  O   HOH S  78     9612   4618   5879  -1894  -1398   -515       O
HETATM 1359  O   HOH S  79     -11.803   9.182  -6.349  1.00 35.24           O
ANISOU 1359  O   HOH S  79     5768   3522   4098  -1820  -1973   1610       O
HETATM 1360  O   HOH S  80     -28.789  -3.210  -0.420  1.00 34.32           O
ANISOU 1360  O   HOH S  80     5119   3881   4042  -1413  -2099    692       O
HETATM 1361  O   HOH S  82     -30.464   1.900   7.680  1.00 33.07           O
ANISOU 1361  O   HOH S  82     2796   3884   5884    706  -1830  -1825       O
HETATM 1362  O   HOH S  83     -35.087   2.828  11.364  1.00 35.38           O
ANISOU 1362  O   HOH S  83     2571   7439   3431   -655   -543   2289       O
HETATM 1363  O   HOH S  84     -26.809 -17.652  14.066  1.00 35.24           O
ANISOU 1363  O   HOH S  84     6423   2802   4163   -975    734    791       O
HETATM 1364  O   HOH S  85     -30.856  -2.463   9.333  1.00 32.41           O
ANISOU 1364  O   HOH S  85     3191   3568   5557   -926   1385   -830       O
HETATM 1365  O   HOH S  88     -16.480  -1.141  -8.474  1.00 30.06           O
ANISOU 1365  O   HOH S  88     3771   5656   1993  -2182    598   -548       O
HETATM 1366  O   HOH S  89      -0.468   2.512  17.839  1.00 51.28           O
ANISOU 1366  O   HOH S  89     7303   9371   2810    682  -1366    287       O
HETATM 1367  O   HOH S  90      -8.195  18.795  -1.660  1.00 29.83           O
ANISOU 1367  O   HOH S  90     2233   3264   5836     12    326   1022       O
HETATM 1368  O   HOH S  92     -21.183 -18.838  10.947  1.00 45.75           O
ANISOU 1368  O   HOH S  92     6640   3825   6919   -411   -974  -1247       O
HETATM 1369  O   HOH S  93     -21.221  14.578   2.872  1.00 37.66           O
ANISOU 1369  O   HOH S  93     5608   2770   5930   1573    810    570       O
HETATM 1370  O   HOH S  94      -1.651   0.985  19.841  1.00 45.00           O
ANISOU 1370  O   HOH S  94     3571   8017   5509  -1955  -1424    556       O
HETATM 1371  O   HOH S  95     -21.656 -15.294   8.602  1.00 35.95           O
ANISOU 1371  O   HOH S  95     4644   4873   4141  -1119  -1193   -146       O
HETATM 1372  O   HOH S  97     -20.272 -11.025   3.590  1.00 34.04           O
ANISOU 1372  O   HOH S  97     4599   4332   4001    700    442    388       O
HETATM 1373  O   HOH S  98      -8.861  14.640  -5.018  1.00 44.40           O
ANISOU 1373  O   HOH S  98     6323   6538   4008   -438  -1579    218       O
HETATM 1374  O   HOH S  99      -9.890  15.480  -1.641  1.00 40.23           O
ANISOU 1374  O   HOH S  99     6470   4450   4364  -2180   1897   -243       O
HETATM 1375  O   HOH S 100     -12.167  14.758  -0.354  1.00 33.60           O
ANISOU 1375  O   HOH S 100     3867   3402   5498    399   1246   1146       O
HETATM 1376  O   HOH S 101     -13.374 -12.426   5.470  1.00 42.22           O
ANISOU 1376  O   HOH S 101     6872   5332   3838  -2308    -19  -1179       O
HETATM 1377  O   HOH S 102      -0.140   4.933  11.439  1.00 17.37           O
ANISOU 1377  O   HOH S 102     1751   2870   1978   -416     85    463       O
HETATM 1378  O   HOH S 106     -31.454  -5.267  10.468  1.00 39.74           O
ANISOU 1378  O   HOH S 106     2686   7030   5383   -440    511   1139       O
HETATM 1379  O   HOH S 107     -34.196   0.540  11.564  1.00 46.95           O
ANISOU 1379  O   HOH S 107     5373   6013   6453   -443  -2218   -709       O
HETATM 1380  O   HOH S 108      -6.278 -13.366  22.411  1.00 43.76           O
ANISOU 1380  O   HOH S 108     5383   5400   5843   -661    764    676       O
HETATM 1381  O   HOH S 109      -3.027  -7.445  12.992  1.00 42.72           O
ANISOU 1381  O   HOH S 109     4425   6876   4932   -175   -917   1277       O
HETATM 1382  O   HOH S 110      -2.857  -7.714  10.327  1.00 45.85           O
ANISOU 1382  O   HOH S 110     3202   6886   7331   1699    386    166       O
HETATM 1383  O   HOH S 111       0.190  -4.103  10.478  1.00 43.00           O
ANISOU 1383  O   HOH S 111     5113   7085   4141   1126    995    344       O
HETATM 1384  O   HOH S 112      -1.019  -6.271   6.827  1.00 38.33           O
ANISOU 1384  O   HOH S 112     3483   6367   4713    782   -851   -884       O
HETATM 1385  O   HOH S 113      -7.828  -8.641   3.987  1.00 36.16           O
ANISOU 1385  O   HOH S 113     3926   4299   5514    659    327  -1156       O
HETATM 1386  O   HOH S 114       8.308  -1.151   5.078  1.00 40.98           O
ANISOU 1386  O   HOH S 114     4366   5418   5785   1834  -1233   -990       O
HETATM 1387  O   HOH S 115       0.159  -0.538  -0.811  1.00 40.76           O
ANISOU 1387  O   HOH S 115     3740   8259   3489   -278    142    310       O
HETATM 1388  O   HOH S 116     -28.771  11.335  10.084  1.00 31.29           O
ANISOU 1388  O   HOH S 116     3219   3847   4823   1345   1171   1430       O
HETATM 1389  O   HOH S 117     -32.614   1.714  -2.367  1.00 37.10           O
ANISOU 1389  O   HOH S 117     3862   5214   5021    -58   -695    716       O
HETATM 1390  O   HOH S 118     -31.969 -12.304   8.119  1.00 49.03           O
ANISOU 1390  O   HOH S 118     5847   5235   7546  -1271  -2003   2261       O
HETATM 1391  O   HOH S 119       1.420   5.356  -2.783  1.00 34.76           O
ANISOU 1391  O   HOH S 119     2575   6626   4007    522    -49   -506       O
HETATM 1392  O   HOH S 120     -14.467 -14.515   6.939  1.00 35.76           O
HETATM 1393  O   HOH S 121     -12.474 -17.514  13.408  1.00 33.18           O
HETATM 1394  O   HOH S 122      -0.273  -1.605  15.134  1.00 39.27           O
TER
HETATM 1395  O1  SO4 B   3      -6.509 -10.655  23.391  1.00 60.39           O
ANISOU 1395  O1  SO4 B   3     8443   8405   6096    616    680   3480       O
HETATM 1396  O2  SO4 B   3      -8.676 -11.435  22.794  1.00 60.03           O
ANISOU 1396  O2  SO4 B   3     8362   8363   6085    709    647   3527       O
HETATM 1397  O3  SO4 B   3      -8.217 -10.868  25.040  1.00 60.13           O
ANISOU 1397  O3  SO4 B   3     8417   8387   6043    575    751   3530       O
HETATM 1398  O4  SO4 B   3      -8.340  -9.131  23.406  1.00 60.40           O
ANISOU 1398  O4  SO4 B   3     8437   8418   6093    647    682   3454       O
HETATM 1399  S   SO4 B   3      -7.939 -10.517  23.654  1.00 60.00           S
ANISOU 1399  S   SO4 B   3     8384   8366   6048    678    657   3538       S
HETATM 1400  O1  SO4 B   4      -5.030   3.342  22.632  1.00 40.69           O
ANISOU 1400  O1  SO4 B   4     4817   5495   5148  -2041   1122    991       O
HETATM 1401  O2  SO4 B   4      -6.347   3.984  20.744  1.00 38.13           O
ANISOU 1401  O2  SO4 B   4     4550   5198   4741  -2062   1390   1099       O
HETATM 1402  O3  SO4 B   4      -7.309   2.622  22.457  1.00 40.72           O
ANISOU 1402  O3  SO4 B   4     4920   5458   5096  -1817    990    757       O
HETATM 1403  O4  SO4 B   4      -6.803   4.935  22.887  1.00 41.54           O
ANISOU 1403  O4  SO4 B   4     5039   5597   5147  -1753   1066    911       O
HETATM 1404  S   SO4 B   4      -6.375   3.723  22.193  1.00 39.76           S
ANISOU 1404  S   SO4 B   4     4736   5418   4951  -1922   1172    921       S
HETATM 1405  O1  SO4 B   5       7.224  -2.566   1.226  1.00 71.35           O
ANISOU 1405  O1  SO4 B   5     7851   9974   9283    -29    726   -580       O
HETATM 1406  O2  SO4 B   5       5.664  -1.997   2.942  1.00 71.35           O
ANISOU 1406  O2  SO4 B   5     7863   9970   9275    -38    738   -569       O
HETATM 1407  O3  SO4 B   5       5.825  -4.246   2.179  1.00 71.48           O
ANISOU 1407  O3  SO4 B   5     7894   9983   9281    -42    746   -569       O
HETATM 1408  O4  SO4 B   5       7.588  -3.298   3.475  1.00 71.45           O
ANISOU 1408  O4  SO4 B   5     7878   9985   9283    -62    750   -571       O
HETATM 1409  S   SO4 B   5       6.578  -3.024   2.456  1.00 71.33           S
ANISOU 1409  S   SO4 B   5     7850   9976   9277    -48    740   -568       S
HETATM 1410  O1  SO4 B   6       2.979  10.346  -6.518  1.00 64.63           O
ANISOU 1410  O1  SO4 B   6    10365   7505   6686  -1448  -1149   2617       O
HETATM 1411  O2  SO4 B   6       2.498   8.802  -4.758  1.00 64.85           O
ANISOU 1411  O2  SO4 B   6    10386   7532   6720  -1442  -1128   2584       O
HETATM 1412  O3  SO4 B   6       4.765   9.279  -5.363  1.00 64.85           O
ANISOU 1412  O3  SO4 B   6    10422   7493   6727  -1467  -1098   2610       O
HETATM 1413  O4  SO4 B   6       3.435  10.931  -4.250  1.00 64.97           O
ANISOU 1413  O4  SO4 B   6    10409   7543   6734  -1448  -1118   2571       O
HETATM 1414  S   SO4 B   6       3.422   9.836  -5.218  1.00 64.72           S
ANISOU 1414  S   SO4 B   6    10388   7498   6704  -1455  -1146   2616       S
HETATM 1415  O1  SO4 B   7      -7.735  15.462  13.443  1.00 66.81           O
ANISOU 1415  O1  SO4 B   7     7772   9787   7825   1162   1427   -554       O
HETATM 1416  O2  SO4 B   7      -9.919  14.514  13.574  1.00 66.68           O
ANISOU 1416  O2  SO4 B   7     7734   9785   7817   1179   1444   -552       O
HETATM 1417  O3  SO4 B   7      -8.272  13.913  15.185  1.00 66.72           O
ANISOU 1417  O3  SO4 B   7     7739   9786   7825   1188   1451   -569       O
HETATM 1418  O4  SO4 B   7      -9.207  16.110  15.195  1.00 66.65           O
ANISOU 1418  O4  SO4 B   7     7719   9784   7820   1179   1436   -554       O
HETATM 1419  S   SO4 B   7      -8.785  15.000  14.352  1.00 66.67           S
ANISOU 1419  S   SO4 B   7     7735   9783   7812   1168   1446   -561       S
TER
END



If you find results from this site helpful for your research, please cite one of our papers:

elNémo is maintained by Yves-Henri Sanejouand.
It was developed by Karsten Suhre.
Between 2003 and 2014, it was hosted by IGS (Marseille).
Last modification: October 18th, 2018.