CNRS Nantes University UFIP UFIP
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***    ***

elNémo ID: 210514173758100016

Job options:

ID        	=	 210514173758100016
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:


ATOM      1  N   GLU A   4      23.677  -9.330  36.136  1.00 70.88      A    N  
ATOM      2  CA  GLU A   4      24.727  -8.464  35.520  1.00 71.27      A    C  
ATOM      3  C   GLU A   4      24.211  -7.678  34.303  1.00 71.20      A    C  
ATOM      4  O   GLU A   4      22.992  -7.597  34.063  1.00 71.51      A    O  
ATOM      5  CB  GLU A   4      25.965  -9.294  35.134  1.00 71.37      A    C  
ATOM      6  CG  GLU A   4      27.027  -9.409  36.227  1.00 71.27      A    C  
ATOM      7  N   ARG A   5      25.144  -7.100  33.541  1.00 70.53      A    N  
ATOM      8  CA  ARG A   5      24.813  -6.349  32.320  1.00 69.18      A    C  
ATOM      9  C   ARG A   5      25.026  -7.233  31.083  1.00 68.52      A    C  
ATOM     10  O   ARG A   5      26.090  -7.842  30.933  1.00 68.40      A    O  
ATOM     11  CB  ARG A   5      25.688  -5.088  32.223  1.00 69.32      A    C  
ATOM     12  CG  ARG A   5      25.306  -4.116  31.112  1.00 69.04      A    C  
ATOM     13  CD  ARG A   5      26.336  -3.014  30.982  1.00 69.10      A    C  
ATOM     14  NE  ARG A   5      25.987  -1.981  30.000  1.00 70.32      A    N  
ATOM     15  CZ  ARG A   5      26.573  -1.811  28.810  1.00 69.28      A    C  
ATOM     16  NH1 ARG A   5      27.543  -2.621  28.400  1.00 70.49      A    N1+
ATOM     17  NH2 ARG A   5      26.177  -0.831  28.015  1.00 67.03      A    N  
ATOM     18  N   PRO A   6      24.029  -7.299  30.177  1.00 67.10      A    N  
ATOM     19  CA  PRO A   6      24.263  -8.081  28.957  1.00 65.87      A    C  
ATOM     20  C   PRO A   6      25.352  -7.461  28.080  1.00 64.54      A    C  
ATOM     21  O   PRO A   6      25.766  -6.322  28.310  1.00 64.60      A    O  
ATOM     22  CB  PRO A   6      22.913  -8.019  28.235  1.00 65.83      A    C  
ATOM     23  CG  PRO A   6      22.224  -6.824  28.786  1.00 66.31      A    C  
ATOM     24  CD  PRO A   6      22.683  -6.696  30.205  1.00 67.17      A    C  
ATOM     25  N   THR A   7      25.813  -8.200  27.084  1.00 62.73      A    N  
ATOM     26  CA  THR A   7      26.711  -7.628  26.106  1.00 62.12      A    C  
ATOM     27  C   THR A   7      25.839  -6.989  25.043  1.00 61.60      A    C  
ATOM     28  O   THR A   7      24.854  -7.583  24.602  1.00 60.87      A    O  
ATOM     29  CB  THR A   7      27.638  -8.687  25.516  1.00 62.14      A    C  
ATOM     30  CG2 THR A   7      28.485  -8.117  24.378  1.00 62.19      A    C  
ATOM     31  OG1 THR A   7      28.504  -9.167  26.556  1.00 63.71      A    O  
ATOM     32  N   PHE A   8      26.193  -5.764  24.681  1.00 61.04      A    N  
ATOM     33  CA  PHE A   8      25.521  -4.999  23.646  1.00 60.95      A    C  
ATOM     34  C   PHE A   8      26.358  -5.006  22.366  1.00 62.02      A    C  
ATOM     35  O   PHE A   8      27.597  -5.095  22.418  1.00 62.44      A    O  
ATOM     36  CB  PHE A   8      25.361  -3.543  24.105  1.00 59.85      A    C  
ATOM     37  CG  PHE A   8      24.369  -3.355  25.201  1.00 57.90      A    C  
ATOM     38  CD1 PHE A   8      24.595  -3.873  26.468  1.00 57.84      A    C  
ATOM     39  CD2 PHE A   8      23.195  -2.651  24.971  1.00 56.19      A    C  
ATOM     40  CE1 PHE A   8      23.655  -3.710  27.495  1.00 55.75      A    C  
ATOM     41  CE2 PHE A   8      22.265  -2.472  25.986  1.00 55.19      A    C  
ATOM     42  CZ  PHE A   8      22.498  -3.003  27.252  1.00 56.53      A    C  
ATOM     43  N   TYR A   9      25.688  -4.920  21.222  1.00 62.50      A    N  
ATOM     44  CA  TYR A   9      26.366  -4.663  19.960  1.00 63.48      A    C  
ATOM     45  C   TYR A   9      25.663  -3.508  19.280  1.00 64.70      A    C  
ATOM     46  O   TYR A   9      24.493  -3.239  19.552  1.00 64.33      A    O  
ATOM     47  CB  TYR A   9      26.355  -5.899  19.064  1.00 63.20      A    C  
ATOM     48  CG  TYR A   9      24.987  -6.282  18.524  1.00 62.27      A    C  
ATOM     49  CD1 TYR A   9      24.052  -6.937  19.324  1.00 60.34      A    C  
ATOM     50  CD2 TYR A   9      24.641  -6.010  17.204  1.00 61.43      A    C  
ATOM     51  CE1 TYR A   9      22.808  -7.310  18.824  1.00 58.76      A    C  
ATOM     52  CE2 TYR A   9      23.405  -6.372  16.706  1.00 62.42      A    C  
ATOM     53  CZ  TYR A   9      22.494  -7.016  17.529  1.00 60.95      A    C  
ATOM     54  OH  TYR A   9      21.279  -7.372  17.031  1.00 62.43      A    O  
ATOM     55  N   ARG A  10      26.380  -2.816  18.407  1.00 65.85      A    N  
ATOM     56  CA  ARG A  10      25.797  -1.708  17.693  1.00 68.14      A    C  
ATOM     57  C   ARG A  10      25.795  -1.918  16.191  1.00 68.37      A    C  
ATOM     58  O   ARG A  10      26.612  -2.668  15.636  1.00 68.42      A    O  
ATOM     59  CB  ARG A  10      26.423  -0.361  18.098  1.00 67.93      A    C  
ATOM     60  CG  ARG A  10      27.662  -0.455  18.946  1.00 69.67      A    C  
ATOM     61  CD  ARG A  10      28.013   0.888  19.595  1.00 71.03      A    C  
ATOM     62  NE  ARG A  10      27.896   2.009  18.651  1.00 77.57      A    N  
ATOM     63  CZ  ARG A  10      28.422   3.216  18.844  1.00 79.77      A    C  
ATOM     64  NH1 ARG A  10      29.114   3.476  19.952  1.00 80.84      A    N1+
ATOM     65  NH2 ARG A  10      28.265   4.160  17.921  1.00 81.42      A    N  
ATOM     66  N   GLN A  11      24.825  -1.278  15.559  1.00 69.40      A    N  
ATOM     67  CA  GLN A  11      24.693  -1.241  14.114  1.00 70.93      A    C  
ATOM     68  C   GLN A  11      23.915   0.007  13.739  1.00 71.83      A    C  
ATOM     69  O   GLN A  11      23.354   0.656  14.613  1.00 71.77      A    O  
ATOM     70  CB  GLN A  11      24.004  -2.500  13.599  1.00 70.93      A    C  
ATOM     71  CG  GLN A  11      22.559  -2.670  14.027  1.00 71.64      A    C  
ATOM     72  CD  GLN A  11      22.059  -4.040  13.662  1.00 75.15      A    C  
ATOM     73  NE2 GLN A  11      21.835  -4.265  12.361  1.00 73.82      A    N  
ATOM     74  OE1 GLN A  11      21.911  -4.914  14.532  1.00 76.60      A    O  
ATOM     75  N   GLU A  12      23.909   0.361  12.455  1.00 73.18      A    N  
ATOM     76  CA  GLU A  12      23.077   1.460  11.966  1.00 75.15      A    C  
ATOM     77  C   GLU A  12      21.991   0.964  11.017  1.00 75.25      A    C  
ATOM     78  O   GLU A  12      22.201  -0.014  10.293  1.00 75.30      A    O  
ATOM     79  CB  GLU A  12      23.927   2.567  11.308  1.00 75.28      A    C  
ATOM     80  CG  GLU A  12      24.572   2.196   9.971  1.00 76.15      A    C  
ATOM     81  CD  GLU A  12      25.760   3.088   9.630  1.00 77.39      A    C  
ATOM     82  OE1 GLU A  12      26.846   2.872  10.222  1.00 79.17      A    O  
ATOM     83  OE2 GLU A  12      25.614   3.993   8.764  1.00 80.38      A    O1-
ATOM     84  N   LEU A  13      20.827   1.622  11.071  1.00 76.00      A    N  
ATOM     85  CA  LEU A  13      19.741   1.444  10.097  1.00 76.74      A    C  
ATOM     86  C   LEU A  13      18.530   2.356  10.382  1.00 77.00      A    C  
ATOM     87  O   LEU A  13      18.339   2.860  11.499  1.00 76.54      A    O  
ATOM     88  CB  LEU A  13      19.288  -0.025  10.012  1.00 77.45      A    C  
ATOM     89  CG  LEU A  13      19.210  -0.728   8.629  1.00 77.96      A    C  
ATOM     90  CD1 LEU A  13      19.039  -2.248   8.790  1.00 78.02      A    C  
ATOM     91  CD2 LEU A  13      18.129  -0.156   7.670  1.00 77.19      A    C  
ATOM     92  N   LYS A  15      17.717   6.279  10.638  1.00 77.65      A    N  
ATOM     93  CA  LYS A  15      19.075   5.838  10.349  1.00 77.09      A    C  
ATOM     94  C   LYS A  15      20.012   6.161  11.527  1.00 76.22      A    C  
ATOM     95  O   LYS A  15      21.152   6.635  11.337  1.00 76.34      A    O  
ATOM     96  CB  LYS A  15      19.562   6.459   9.039  1.00 77.22      A    C  
ATOM     97  CG  LYS A  15      20.838   5.839   8.477  1.00 78.38      A    C  
ATOM     98  CD  LYS A  15      21.424   6.706   7.352  1.00 78.11      A    C  
ATOM     99  CE  LYS A  15      21.679   8.158   7.812  1.00 79.70      A    C  
ATOM    100  NZ  LYS A  15      22.778   8.251   8.831  1.00 80.63      A    N1+
ATOM    101  N   THR A  16      19.518   5.904  12.747  1.00 74.83      A    N  
ATOM    102  CA  THR A  16      20.332   6.056  13.967  1.00 72.76      A    C  
ATOM    103  C   THR A  16      21.162   4.777  14.285  1.00 71.11      A    C  
ATOM    104  O   THR A  16      20.911   3.714  13.700  1.00 70.58      A    O  
ATOM    105  CB  THR A  16      19.477   6.590  15.187  1.00 73.24      A    C  
ATOM    106  CG2 THR A  16      19.231   8.107  15.059  1.00 72.81      A    C  
ATOM    107  OG1 THR A  16      18.202   5.934  15.239  1.00 72.15      A    O  
ATOM    108  N   ILE A  17      22.184   4.917  15.140  1.00 69.16      A    N  
ATOM    109  CA  ILE A  17      22.953   3.789  15.702  1.00 67.53      A    C  
ATOM    110  C   ILE A  17      22.148   3.117  16.824  1.00 65.75      A    C  
ATOM    111  O   ILE A  17      21.872   3.731  17.851  1.00 65.49      A    O  
ATOM    112  CB  ILE A  17      24.314   4.250  16.318  1.00 68.16      A    C  
ATOM    113  CG1 ILE A  17      25.265   4.790  15.239  1.00 69.31      A    C  
ATOM    114  CG2 ILE A  17      24.996   3.119  17.116  1.00 67.92      A    C  
ATOM    115  CD1 ILE A  17      26.252   5.863  15.767  1.00 71.29      A    C  
ATOM    116  N   TRP A  18      21.778   1.857  16.621  1.00 63.35      A    N  
ATOM    117  CA  TRP A  18      21.096   1.080  17.649  1.00 60.44      A    C  
ATOM    118  C   TRP A  18      22.113   0.272  18.439  1.00 59.35      A    C  
ATOM    119  O   TRP A  18      22.983  -0.391  17.861  1.00 59.11      A    O  
ATOM    120  CB  TRP A  18      20.062   0.159  17.010  1.00 60.44      A    C  
ATOM    121  CG  TRP A  18      18.874   0.876  16.436  1.00 59.81      A    C  
ATOM    122  CD1 TRP A  18      18.899   1.923  15.559  1.00 60.98      A    C  
ATOM    123  CD2 TRP A  18      17.477   0.595  16.688  1.00 59.67      A    C  
ATOM    124  CE2 TRP A  18      16.722   1.516  15.925  1.00 59.97      A    C  
ATOM    125  CE3 TRP A  18      16.799  -0.331  17.493  1.00 56.27      A    C  
ATOM    126  NE1 TRP A  18      17.610   2.314  15.253  1.00 60.25      A    N  
ATOM    127  CZ2 TRP A  18      15.313   1.538  15.940  1.00 59.28      A    C  
ATOM    128  CZ3 TRP A  18      15.421  -0.322  17.502  1.00 58.39      A    C  
ATOM    129  CH2 TRP A  18      14.685   0.612  16.734  1.00 59.54      A    C  
ATOM    130  N   GLU A  19      22.008   0.342  19.763  1.00 56.67      A    N  
ATOM    131  CA  GLU A  19      22.871  -0.410  20.655  1.00 55.54      A    C  
ATOM    132  C   GLU A  19      21.952  -1.249  21.543  1.00 52.90      A    C  
ATOM    133  O   GLU A  19      21.222  -0.708  22.379  1.00 51.49      A    O  
ATOM    134  CB  GLU A  19      23.731   0.546  21.497  1.00 55.50      A    C  
ATOM    135  CG  GLU A  19      24.977  -0.097  22.160  1.00 58.59      A    C  
ATOM    136  CD  GLU A  19      25.997   0.950  22.621  1.00 58.44      A    C  
ATOM    137  OE1 GLU A  19      25.688   2.167  22.506  1.00 62.46      A    O  
ATOM    138  OE2 GLU A  19      27.086   0.562  23.107  1.00 60.17      A    O1-
ATOM    139  N   VAL A  20      21.987  -2.559  21.330  1.00 50.68      A    N  
ATOM    140  CA  VAL A  20      21.049  -3.475  21.969  1.00 49.13      A    C  
ATOM    141  C   VAL A  20      21.768  -4.703  22.491  1.00 48.25      A    C  
ATOM    142  O   VAL A  20      22.828  -5.081  21.967  1.00 48.19      A    O  
ATOM    143  CB  VAL A  20      19.889  -3.883  21.015  1.00 49.02      A    C  
ATOM    144  CG1 VAL A  20      19.232  -2.610  20.391  1.00 48.51      A    C  
ATOM    145  CG2 VAL A  20      20.339  -4.880  19.958  1.00 48.28      A    C  
ATOM    146  N   PRO A  21      21.206  -5.335  23.517  1.00 47.35      A    N  
ATOM    147  CA  PRO A  21      21.778  -6.566  23.975  1.00 47.62      A    C  
ATOM    148  C   PRO A  21      21.847  -7.573  22.839  1.00 49.31      A    C  
ATOM    149  O   PRO A  21      20.969  -7.580  21.952  1.00 49.42      A    O  
ATOM    150  CB  PRO A  21      20.807  -7.017  25.061  1.00 47.19      A    C  
ATOM    151  CG  PRO A  21      20.142  -5.796  25.487  1.00 46.24      A    C  
ATOM    152  CD  PRO A  21      20.065  -4.910  24.345  1.00 47.01      A    C  
ATOM    153  N   GLU A  22      22.872  -8.423  22.880  1.00 50.33      A    N  
ATOM    154  CA  GLU A  22      23.111  -9.367  21.801  1.00 51.98      A    C  
ATOM    155  C   GLU A  22      22.051 -10.468  21.674  1.00 51.41      A    C  
ATOM    156  O   GLU A  22      22.017 -11.175  20.677  1.00 51.31      A    O  
ATOM    157  CB  GLU A  22      24.525  -9.948  21.880  1.00 51.46      A    C  
ATOM    158  CG  GLU A  22      24.711 -10.981  22.960  1.00 53.83      A    C  
ATOM    159  CD  GLU A  22      26.173 -11.459  23.114  1.00 55.78      A    C  
ATOM    160  OE1 GLU A  22      27.057 -11.138  22.258  1.00 57.57      A    O  
ATOM    161  OE2 GLU A  22      26.404 -12.163  24.124  1.00 60.49      A    O1-
ATOM    162  N   ARG A  23      21.172 -10.619  22.662  1.00 52.47      A    N  
ATOM    163  CA  ARG A  23      20.077 -11.595  22.535  1.00 52.07      A    C  
ATOM    164  C   ARG A  23      19.067 -11.211  21.443  1.00 52.07      A    C  
ATOM    165  O   ARG A  23      18.351 -12.083  20.909  1.00 52.01      A    O  
ATOM    166  CB  ARG A  23      19.351 -11.764  23.859  1.00 53.00      A    C  
ATOM    167  CG  ARG A  23      18.435 -10.597  24.205  1.00 52.69      A    C  
ATOM    168  CD  ARG A  23      17.907 -10.693  25.640  1.00 54.63      A    C  
ATOM    169  NE  ARG A  23      16.545 -11.225  25.688  1.00 54.36      A    N  
ATOM    170  CZ  ARG A  23      15.813 -11.254  26.799  1.00 57.11      A    C  
ATOM    171  NH1 ARG A  23      16.314 -10.767  27.931  1.00 52.80      A    N1+
ATOM    172  NH2 ARG A  23      14.586 -11.764  26.776  1.00 56.58      A    N  
ATOM    173  N   TYR A  24      19.011  -9.921  21.105  1.00 51.03      A    N  
ATOM    174  CA  TYR A  24      18.137  -9.456  20.029  1.00 50.98      A    C  
ATOM    175  C   TYR A  24      18.894  -9.417  18.710  1.00 51.94      A    C  
ATOM    176  O   TYR A  24      19.739  -8.550  18.510  1.00 51.80      A    O  
ATOM    177  CB  TYR A  24      17.499  -8.075  20.347  1.00 48.97      A    C  
ATOM    178  CG  TYR A  24      16.745  -8.111  21.641  1.00 47.24      A    C  
ATOM    179  CD1 TYR A  24      15.547  -8.819  21.745  1.00 45.34      A    C  
ATOM    180  CD2 TYR A  24      17.233  -7.455  22.772  1.00 44.62      A    C  
ATOM    181  CE1 TYR A  24      14.856  -8.887  22.950  1.00 43.98      A    C  
ATOM    182  CE2 TYR A  24      16.542  -7.500  23.977  1.00 44.54      A    C  
ATOM    183  CZ  TYR A  24      15.351  -8.225  24.051  1.00 45.92      A    C  
ATOM    184  OH  TYR A  24      14.673  -8.303  25.253  1.00 47.02      A    O  
ATOM    185  N   GLN A  25      18.539 -10.329  17.802  1.00 53.66      A    N  
ATOM    186  CA  GLN A  25      19.242 -10.490  16.544  1.00 55.72      A    C  
ATOM    187  C   GLN A  25      18.314 -10.207  15.357  1.00 57.80      A    C  
ATOM    188  O   GLN A  25      17.074 -10.181  15.504  1.00 57.37      A    O  
ATOM    189  CB  GLN A  25      19.799 -11.897  16.450  1.00 55.86      A    C  
ATOM    190  CG  GLN A  25      20.801 -12.267  17.552  1.00 56.67      A    C  
ATOM    191  CD  GLN A  25      22.202 -11.713  17.270  1.00 58.50      A    C  
ATOM    192  NE2 GLN A  25      22.876 -11.212  18.303  1.00 56.32      A    N  
ATOM    193  OE1 GLN A  25      22.653 -11.713  16.128  1.00 61.62      A    O  
ATOM    194  N   ASN A  26      18.924  -9.964  14.192  1.00 59.45      A    N  
ATOM    195  CA  ASN A  26      18.199  -9.762  12.941  1.00 61.84      A    C  
ATOM    196  C   ASN A  26      17.232  -8.600  13.013  1.00 62.72      A    C  
ATOM    197  O   ASN A  26      16.077  -8.709  12.595  1.00 62.05      A    O  
ATOM    198  CB  ASN A  26      17.475 -11.048  12.500  1.00 61.97      A    C  
ATOM    199  CG  ASN A  26      18.438 -12.103  11.981  1.00 65.60      A    C  
ATOM    200  ND2 ASN A  26      18.421 -13.291  12.591  1.00 66.67      A    N  
ATOM    201  OD1 ASN A  26      19.210 -11.838  11.040  1.00 70.75      A    O  
ATOM    202  N   LEU A  27      17.713  -7.484  13.550  1.00 64.33      A    N  
ATOM    203  CA  LEU A  27      16.925  -6.264  13.544  1.00 66.07      A    C  
ATOM    204  C   LEU A  27      16.611  -5.827  12.132  1.00 67.38      A    C  
ATOM    205  O   LEU A  27      17.514  -5.611  11.333  1.00 67.12      A    O  
ATOM    206  CB  LEU A  27      17.612  -5.130  14.325  1.00 65.69      A    C  
ATOM    207  CG  LEU A  27      17.210  -5.087  15.809  1.00 66.30      A    C  
ATOM    208  CD1 LEU A  27      17.967  -6.131  16.612  1.00 66.16      A    C  
ATOM    209  CD2 LEU A  27      17.414  -3.730  16.394  1.00 66.24      A    C  
ATOM    210  N   SER A  28      15.321  -5.703  11.832  1.00 69.19      A    N  
ATOM    211  CA  SER A  28      14.907  -5.139  10.554  1.00 70.96      A    C  
ATOM    212  C   SER A  28      13.823  -4.067  10.739  1.00 72.12      A    C  
ATOM    213  O   SER A  28      12.738  -4.347  11.252  1.00 72.22      A    O  
ATOM    214  CB  SER A  28      14.529  -6.239   9.529  1.00 71.24      A    C  
ATOM    215  OG  SER A  28      13.277  -6.860   9.782  1.00 72.22      A    O  
ATOM    216  N   PRO A  29      14.135  -2.821  10.357  1.00 73.16      A    N  
ATOM    217  CA  PRO A  29      13.231  -1.699  10.560  1.00 74.29      A    C  
ATOM    218  C   PRO A  29      11.798  -1.956  10.111  1.00 75.31      A    C  
ATOM    219  O   PRO A  29      11.569  -2.623   9.110  1.00 75.60      A    O  
ATOM    220  CB  PRO A  29      13.888  -0.590   9.743  1.00 74.26      A    C  
ATOM    221  CG  PRO A  29      15.352  -0.878   9.925  1.00 73.64      A    C  
ATOM    222  CD  PRO A  29      15.402  -2.379   9.748  1.00 73.24      A    C  
ATOM    223  N   VAL A  30      10.858  -1.454  10.900  1.00 76.27      A    N  
ATOM    224  CA  VAL A  30       9.424  -1.604  10.660  1.00 77.89      A    C  
ATOM    225  C   VAL A  30       8.738  -0.324  11.126  1.00 78.86      A    C  
ATOM    226  O   VAL A  30       7.742  -0.377  11.857  1.00 79.56      A    O  
ATOM    227  CB  VAL A  30       8.810  -2.806  11.449  1.00 77.48      A    C  
ATOM    228  CG1 VAL A  30       7.314  -2.949  11.170  1.00 78.07      A    C  
ATOM    229  CG2 VAL A  30       9.494  -4.097  11.099  1.00 78.65      A    C  
ATOM    230  N   GLY A  31       9.279   0.826  10.742  1.00 79.75      A    N  
ATOM    231  CA  GLY A  31       8.630   2.094  11.080  1.00 81.31      A    C  
ATOM    232  C   GLY A  31       9.466   3.080  11.875  1.00 82.29      A    C  
ATOM    233  O   GLY A  31      10.360   2.691  12.639  1.00 82.36      A    O  
ATOM    234  N   SER A  32       9.149   4.364  11.687  1.00 83.21      A    N  
ATOM    235  CA  SER A  32       9.889   5.474  12.290  1.00 83.57      A    C  
ATOM    236  C   SER A  32       8.968   6.598  12.797  1.00 83.80      A    C  
ATOM    237  O   SER A  32       7.748   6.426  12.916  1.00 83.90      A    O  
ATOM    238  CB  SER A  32      10.891   6.036  11.281  1.00 83.87      A    C  
ATOM    239  OG  SER A  32      11.965   6.681  11.942  1.00 83.68      A    O  
ATOM    240  N   GLY A  36       9.359   7.505  18.339  1.00 67.00      A    N  
ATOM    241  CA  GLY A  36      10.493   6.572  18.151  1.00 67.39      A    C  
ATOM    242  C   GLY A  36      10.653   5.962  16.755  1.00 66.79      A    C  
ATOM    243  O   GLY A  36       9.982   6.380  15.792  1.00 67.55      A    O  
ATOM    244  N   SER A  37      11.570   5.007  16.623  1.00 65.23      A    N  
ATOM    245  CA  SER A  37      11.555   4.113  15.461  1.00 63.61      A    C  
ATOM    246  C   SER A  37      11.584   2.691  15.961  1.00 61.96      A    C  
ATOM    247  O   SER A  37      12.118   2.433  17.030  1.00 60.81      A    O  
ATOM    248  CB  SER A  37      12.698   4.387  14.471  1.00 64.26      A    C  
ATOM    249  OG  SER A  37      13.945   4.557  15.112  1.00 64.29      A    O  
ATOM    250  N   VAL A  38      10.986   1.778  15.200  1.00 60.35      A    N  
ATOM    251  CA  VAL A  38      10.787   0.396  15.653  1.00 58.93      A    C  
ATOM    252  C   VAL A  38      11.483  -0.569  14.707  1.00 59.03      A    C  
ATOM    253  O   VAL A  38      11.374  -0.405  13.477  1.00 58.98      A    O  
ATOM    254  CB  VAL A  38       9.272   0.047  15.709  1.00 58.14      A    C  
ATOM    255  CG1 VAL A  38       9.061  -1.339  16.254  1.00 57.86      A    C  
ATOM    256  CG2 VAL A  38       8.533   1.064  16.550  1.00 57.54      A    C  
ATOM    257  N   CYS A  39      12.207  -1.544  15.266  1.00 57.39      A    N  
ATOM    258  CA  CYS A  39      12.750  -2.643  14.477  1.00 57.14      A    C  
ATOM    259  C   CYS A  39      12.110  -3.908  14.951  1.00 55.79      A    C  
ATOM    260  O   CYS A  39      11.833  -4.065  16.133  1.00 55.36      A    O  
ATOM    261  CB  CYS A  39      14.265  -2.784  14.612  1.00 57.15      A    C  
ATOM    262  SG  CYS A  39      15.207  -1.409  13.995  1.00 61.09      A    S  
ATOM    263  N   ALA A  40      11.854  -4.807  14.017  1.00 55.38      A    N  
ATOM    264  CA  ALA A  40      11.440  -6.155  14.343  1.00 55.05      A    C  
ATOM    265  C   ALA A  40      12.711  -6.918  14.650  1.00 54.46      A    C  
ATOM    266  O   ALA A  40      13.743  -6.685  14.006  1.00 54.41      A    O  
ATOM    267  CB  ALA A  40      10.703  -6.795  13.177  1.00 55.69      A    C  
ATOM    268  N   ALA A  41      12.658  -7.807  15.639  1.00 53.48      A    N  
ATOM    269  CA  ALA A  41      13.854  -8.557  15.994  1.00 52.73      A    C  
ATOM    270  C   ALA A  41      13.521  -9.965  16.424  1.00 52.07      A    C  
ATOM    271  O   ALA A  41      12.357 -10.299  16.685  1.00 52.29      A    O  
ATOM    272  CB  ALA A  41      14.650  -7.830  17.097  1.00 51.59      A    C  
ATOM    273  N   PHE A  42      14.558 -10.790  16.496  1.00 51.52      A    N  
ATOM    274  CA  PHE A  42      14.439 -12.147  17.014  1.00 51.40      A    C  
ATOM    275  C   PHE A  42      15.049 -12.169  18.390  1.00 51.13      A    C  
ATOM    276  O   PHE A  42      16.207 -11.817  18.572  1.00 51.46      A    O  
ATOM    277  CB  PHE A  42      15.111 -13.182  16.087  1.00 51.32      A    C  
ATOM    278  CG  PHE A  42      14.893 -14.609  16.523  1.00 52.98      A    C  
ATOM    279  CD1 PHE A  42      13.689 -15.247  16.275  1.00 53.56      A    C  
ATOM    280  CD2 PHE A  42      15.877 -15.299  17.231  1.00 52.68      A    C  
ATOM    281  CE1 PHE A  42      13.491 -16.552  16.685  1.00 53.04      A    C  
ATOM    282  CE2 PHE A  42      15.664 -16.601  17.653  1.00 52.88      A    C  
ATOM    283  CZ  PHE A  42      14.476 -17.217  17.381  1.00 53.22      A    C  
ATOM    284  N   ASP A  43      14.260 -12.568  19.366  1.00 51.98      A    N  
ATOM    285  CA  ASP A  43      14.755 -12.690  20.732  1.00 52.89      A    C  
ATOM    286  C   ASP A  43      15.245 -14.103  20.960  1.00 53.37      A    C  
ATOM    287  O   ASP A  43      14.451 -15.008  21.192  1.00 53.65      A    O  
ATOM    288  CB  ASP A  43      13.649 -12.340  21.737  1.00 52.39      A    C  
ATOM    289  CG  ASP A  43      14.097 -12.486  23.192  1.00 52.82      A    C  
ATOM    290  OD1 ASP A  43      15.304 -12.665  23.491  1.00 54.98      A    O  
ATOM    291  OD2 ASP A  43      13.224 -12.413  24.062  1.00 56.64      A    O1-
ATOM    292  N   THR A  44      16.562 -14.277  20.943  1.00 54.11      A    N  
ATOM    293  CA  THR A  44      17.172 -15.597  21.039  1.00 55.40      A    C  
ATOM    294  C   THR A  44      16.926 -16.291  22.380  1.00 56.42      A    C  
ATOM    295  O   THR A  44      16.964 -17.519  22.463  1.00 57.41      A    O  
ATOM    296  CB  THR A  44      18.697 -15.523  20.790  1.00 55.75      A    C  
ATOM    297  CG2 THR A  44      19.013 -14.972  19.419  1.00 54.33      A    C  
ATOM    298  OG1 THR A  44      19.286 -14.651  21.763  1.00 57.60      A    O  
ATOM    299  N   LYS A  45      16.681 -15.524  23.432  1.00 57.21      A    N  
ATOM    300  CA  LYS A  45      16.389 -16.095  24.746  1.00 58.76      A    C  
ATOM    301  C   LYS A  45      15.082 -16.866  24.742  1.00 59.14      A    C  
ATOM    302  O   LYS A  45      15.010 -17.953  25.297  1.00 59.56      A    O  
ATOM    303  CB  LYS A  45      16.348 -14.977  25.792  1.00 59.31      A    C  
ATOM    304  CG  LYS A  45      16.314 -15.422  27.229  1.00 61.82      A    C  
ATOM    305  CD  LYS A  45      17.005 -14.381  28.142  1.00 64.87      A    C  
ATOM    306  CE  LYS A  45      17.215 -14.909  29.545  1.00 67.32      A    C  
ATOM    307  NZ  LYS A  45      15.941 -15.440  30.091  1.00 68.98      A    N1+
ATOM    308  N   THR A  46      14.062 -16.312  24.085  1.00 59.51      A    N  
ATOM    309  CA  THR A  46      12.714 -16.851  24.142  1.00 59.63      A    C  
ATOM    310  C   THR A  46      12.290 -17.470  22.818  1.00 60.57      A    C  
ATOM    311  O   THR A  46      11.319 -18.230  22.760  1.00 61.46      A    O  
ATOM    312  CB  THR A  46      11.691 -15.750  24.527  1.00 59.70      A    C  
ATOM    313  CG2 THR A  46      12.021 -15.152  25.880  1.00 58.49      A    C  
ATOM    314  OG1 THR A  46      11.726 -14.712  23.542  1.00 59.88      A    O  
ATOM    315  N   GLY A  47      13.009 -17.145  21.745  1.00 61.07      A    N  
ATOM    316  CA  GLY A  47      12.627 -17.584  20.398  1.00 61.43      A    C  
ATOM    317  C   GLY A  47      11.409 -16.815  19.910  1.00 61.49      A    C  
ATOM    318  O   GLY A  47      10.736 -17.228  18.974  1.00 61.47      A    O  
ATOM    319  N   LEU A  48      11.142 -15.680  20.548  1.00 61.76      A    N  
ATOM    320  CA  LEU A  48      10.037 -14.814  20.161  1.00 61.04      A    C  
ATOM    321  C   LEU A  48      10.449 -13.745  19.170  1.00 60.37      A    C  
ATOM    322  O   LEU A  48      11.593 -13.284  19.159  1.00 60.01      A    O  
ATOM    323  CB  LEU A  48       9.400 -14.167  21.397  1.00 61.89      A    C  
ATOM    324  CG  LEU A  48       8.326 -14.987  22.124  1.00 63.48      A    C  
ATOM    325  CD1 LEU A  48       7.716 -14.170  23.252  1.00 64.95      A    C  
ATOM    326  CD2 LEU A  48       7.259 -15.431  21.131  1.00 63.88      A    C  
ATOM    327  N   ARG A  49       9.496 -13.381  18.318  1.00 59.02      A    N  
ATOM    328  CA  ARG A  49       9.618 -12.224  17.468  1.00 57.83      A    C  
ATOM    329  C   ARG A  49       9.195 -11.042  18.321  1.00 55.87      A    C  
ATOM    330  O   ARG A  49       8.160 -11.099  18.983  1.00 55.84      A    O  
ATOM    331  CB  ARG A  49       8.684 -12.352  16.273  1.00 58.59      A    C  
ATOM    332  CG  ARG A  49       9.295 -11.853  14.992  1.00 62.37      A    C  
ATOM    333  CD  ARG A  49      10.031 -12.986  14.264  1.00 67.66      A    C  
ATOM    334  NE  ARG A  49       9.113 -13.762  13.419  1.00 71.77      A    N  
ATOM    335  CZ  ARG A  49       8.674 -14.987  13.704  1.00 74.58      A    C  
ATOM    336  NH1 ARG A  49       9.068 -15.608  14.818  1.00 75.71      A    N1+
ATOM    337  NH2 ARG A  49       7.840 -15.597  12.867  1.00 75.04      A    N  
ATOM    338  N   VAL A  50       9.990  -9.982  18.319  1.00 52.85      A    N  
ATOM    339  CA  VAL A  50       9.724  -8.843  19.180  1.00 51.17      A    C  
ATOM    340  C   VAL A  50       9.854  -7.561  18.393  1.00 49.74      A    C  
ATOM    341  O   VAL A  50      10.526  -7.546  17.369  1.00 49.05      A    O  
ATOM    342  CB  VAL A  50      10.696  -8.779  20.410  1.00 51.40      A    C  
ATOM    343  CG1 VAL A  50      10.596 -10.043  21.291  1.00 49.67      A    C  
ATOM    344  CG2 VAL A  50      12.139  -8.534  19.954  1.00 50.97      A    C  
ATOM    345  N   ALA A  51       9.217  -6.497  18.894  1.00 47.36      A    N  
ATOM    346  CA  ALA A  51       9.358  -5.161  18.337  1.00 46.36      A    C  
ATOM    347  C   ALA A  51      10.310  -4.456  19.278  1.00 45.83      A    C  
ATOM    348  O   ALA A  51      10.162  -4.578  20.482  1.00 46.47      A    O  
ATOM    349  CB  ALA A  51       8.021  -4.420  18.331  1.00 46.07      A    C  
ATOM    350  N   VAL A  52      11.293  -3.744  18.754  1.00 44.77      A    N  
ATOM    351  CA  VAL A  52      12.192  -3.026  19.640  1.00 43.66      A    C  
ATOM    352  C   VAL A  52      12.027  -1.600  19.212  1.00 45.05      A    C  
ATOM    353  O   VAL A  52      12.311  -1.251  18.062  1.00 45.46      A    O  
ATOM    354  CB  VAL A  52      13.635  -3.512  19.491  1.00 44.69      A    C  
ATOM    355  CG1 VAL A  52      14.567  -2.805  20.538  1.00 41.32      A    C  
ATOM    356  CG2 VAL A  52      13.684  -5.010  19.640  1.00 41.99      A    C  
ATOM    357  N   LYS A  53      11.483  -0.790  20.107  1.00 45.59      A    N  
ATOM    358  CA  LYS A  53      11.260   0.633  19.843  1.00 46.02      A    C  
ATOM    359  C   LYS A  53      12.317   1.494  20.537  1.00 45.85      A    C  
ATOM    360  O   LYS A  53      12.475   1.460  21.757  1.00 44.58      A    O  
ATOM    361  CB  LYS A  53       9.886   1.022  20.347  1.00 46.84      A    C  
ATOM    362  CG  LYS A  53       9.606   2.497  20.166  1.00 50.67      A    C  
ATOM    363  CD  LYS A  53       8.131   2.765  20.120  1.00 55.67      A    C  
ATOM    364  CE  LYS A  53       7.649   3.298  21.439  1.00 61.42      A    C  
ATOM    365  NZ  LYS A  53       6.432   4.146  21.199  1.00 63.63      A    N1+
ATOM    366  N   LYS A  54      13.052   2.275  19.765  1.00 45.28      A    N  
ATOM    367  CA  LYS A  54      14.005   3.169  20.370  1.00 46.78      A    C  
ATOM    368  C   LYS A  54      13.356   4.531  20.459  1.00 47.06      A    C  
ATOM    369  O   LYS A  54      13.076   5.151  19.432  1.00 47.28      A    O  
ATOM    370  CB  LYS A  54      15.268   3.265  19.507  1.00 46.01      A    C  
ATOM    371  CG  LYS A  54      16.228   4.321  20.002  1.00 47.39      A    C  
ATOM    372  CD  LYS A  54      17.431   4.399  19.058  1.00 50.52      A    C  
ATOM    373  CE  LYS A  54      18.561   5.172  19.714  1.00 55.41      A    C  
ATOM    374  NZ  LYS A  54      19.707   5.295  18.755  1.00 58.02      A    N1+
ATOM    375  N   LEU A  55      13.115   5.004  21.672  1.00 48.70      A    N  
ATOM    376  CA  LEU A  55      12.440   6.292  21.809  1.00 50.78      A    C  
ATOM    377  C   LEU A  55      13.223   7.411  21.127  1.00 51.37      A    C  
ATOM    378  O   LEU A  55      14.463   7.478  21.191  1.00 50.46      A    O  
ATOM    379  CB  LEU A  55      12.162   6.634  23.270  1.00 50.95      A    C  
ATOM    380  CG  LEU A  55      11.270   5.612  23.966  1.00 51.66      A    C  
ATOM    381  CD1 LEU A  55      11.137   5.996  25.391  1.00 53.99      A    C  
ATOM    382  CD2 LEU A  55       9.881   5.515  23.304  1.00 54.85      A    C  
ATOM    383  N   SER A  56      12.482   8.284  20.463  1.00 52.38      A    N  
ATOM    384  CA  SER A  56      13.106   9.420  19.837  1.00 53.82      A    C  
ATOM    385  C   SER A  56      13.147  10.593  20.805  1.00 53.19      A    C  
ATOM    386  O   SER A  56      12.126  10.966  21.388  1.00 53.43      A    O  
ATOM    387  CB  SER A  56      12.321   9.823  18.597  1.00 53.96      A    C  
ATOM    388  OG  SER A  56      13.101  10.740  17.861  1.00 60.43      A    O  
ATOM    389  N   ARG A  57      14.334  11.173  20.948  1.00 52.67      A    N  
ATOM    390  CA  ARG A  57      14.542  12.363  21.771  1.00 52.64      A    C  
ATOM    391  C   ARG A  57      13.871  12.313  23.192  1.00 50.43      A    C  
ATOM    392  O   ARG A  57      13.238  13.278  23.612  1.00 49.87      A    O  
ATOM    393  CB  ARG A  57      14.223  13.685  20.976  1.00 52.87      A    C  
ATOM    394  CG  ARG A  57      13.225  13.598  19.798  1.00 54.94      A    C  
ATOM    395  CD  ARG A  57      13.191  14.847  18.849  1.00 55.31      A    C  
ATOM    396  NE  ARG A  57      13.877  14.641  17.553  1.00 58.50      A    N  
ATOM    397  CZ  ARG A  57      15.139  15.002  17.312  1.00 60.35      A    C  
ATOM    398  NH1 ARG A  57      15.860  15.609  18.256  1.00 60.07      A    N1+
ATOM    399  NH2 ARG A  57      15.680  14.784  16.127  1.00 60.37      A    N  
ATOM    400  N   PRO A  58      14.064  11.203  23.952  1.00 48.03      A    N  
ATOM    401  CA  PRO A  58      13.123  10.975  25.057  1.00 46.78      A    C  
ATOM    402  C   PRO A  58      13.150  12.030  26.175  1.00 46.42      A    C  
ATOM    403  O   PRO A  58      12.148  12.151  26.883  1.00 46.38      A    O  
ATOM    404  CB  PRO A  58      13.526   9.590  25.583  1.00 46.80      A    C  
ATOM    405  CG  PRO A  58      15.008   9.485  25.237  1.00 45.57      A    C  
ATOM    406  CD  PRO A  58      15.134  10.179  23.913  1.00 48.12      A    C  
ATOM    407  N   PHE A  59      14.259  12.763  26.328  1.00 45.92      A    N  
ATOM    408  CA  PHE A  59      14.464  13.781  27.397  1.00 46.17      A    C  
ATOM    409  C   PHE A  59      14.821  15.181  26.808  1.00 47.02      A    C  
ATOM    410  O   PHE A  59      15.560  15.988  27.397  1.00 46.68      A    O  
ATOM    411  CB  PHE A  59      15.532  13.308  28.409  1.00 45.79      A    C  
ATOM    412  CG  PHE A  59      15.314  11.900  28.887  1.00 45.65      A    C  
ATOM    413  CD1 PHE A  59      14.160  11.571  29.603  1.00 46.00      A    C  
ATOM    414  CD2 PHE A  59      16.220  10.899  28.579  1.00 45.67      A    C  
ATOM    415  CE1 PHE A  59      13.897  10.231  30.033  1.00 46.43      A    C  
ATOM    416  CE2 PHE A  59      15.984   9.568  28.999  1.00 49.66      A    C  
ATOM    417  CZ  PHE A  59      14.822   9.234  29.721  1.00 46.02      A    C  
ATOM    418  N   GLN A  60      14.223  15.484  25.671  1.00 48.01      A    N  
ATOM    419  CA  GLN A  60      14.540  16.712  24.943  1.00 49.31      A    C  
ATOM    420  C   GLN A  60      14.051  17.939  25.701  1.00 49.46      A    C  
ATOM    421  O   GLN A  60      14.702  19.015  25.726  1.00 49.81      A    O  
ATOM    422  CB  GLN A  60      13.961  16.593  23.536  1.00 49.49      A    C  
ATOM    423  CG  GLN A  60      14.056  17.828  22.721  1.00 52.55      A    C  
ATOM    424  CD  GLN A  60      14.098  17.561  21.246  1.00 55.80      A    C  
ATOM    425  NE2 GLN A  60      13.349  18.355  20.496  1.00 55.33      A    N  
ATOM    426  OE1 GLN A  60      14.845  16.680  20.768  1.00 59.28      A    O  
ATOM    427  N   SER A  61      12.903  17.758  26.345  1.00 49.44      A    N  
ATOM    428  CA  SER A  61      12.239  18.809  27.076  1.00 49.89      A    C  
ATOM    429  C   SER A  61      11.489  18.155  28.246  1.00 49.96      A    C  
ATOM    430  O   SER A  61      11.383  16.941  28.328  1.00 48.71      A    O  
ATOM    431  CB  SER A  61      11.224  19.475  26.148  1.00 50.98      A    C  
ATOM    432  OG  SER A  61      10.427  18.456  25.562  1.00 49.98      A    O  
ATOM    433  N   ILE A  62      10.925  18.984  29.107  1.00 49.63      A    N  
ATOM    434  CA  ILE A  62      10.074  18.512  30.179  1.00 49.75      A    C  
ATOM    435  C   ILE A  62       8.917  17.660  29.652  1.00 49.29      A    C  
ATOM    436  O   ILE A  62       8.646  16.594  30.203  1.00 48.89      A    O  
ATOM    437  CB  ILE A  62       9.612  19.694  31.015  1.00 49.78      A    C  
ATOM    438  CG1 ILE A  62      10.689  19.964  32.069  1.00 49.25      A    C  
ATOM    439  CG2 ILE A  62       8.245  19.405  31.641  1.00 51.47      A    C  
ATOM    440  CD1 ILE A  62      10.934  21.399  32.373  1.00 52.99      A    C  
ATOM    441  N   ILE A  63       8.291  18.087  28.559  1.00 49.42      A    N  
ATOM    442  CA  ILE A  63       7.183  17.327  27.950  1.00 49.70      A    C  
ATOM    443  C   ILE A  63       7.582  15.954  27.353  1.00 47.61      A    C  
ATOM    444  O   ILE A  63       6.844  14.996  27.487  1.00 45.90      A    O  
ATOM    445  CB  ILE A  63       6.317  18.211  26.993  1.00 50.22      A    C  
ATOM    446  CG1 ILE A  63       5.578  19.275  27.826  1.00 53.32      A    C  
ATOM    447  CG2 ILE A  63       5.320  17.358  26.217  1.00 53.52      A    C  
ATOM    448  CD1 ILE A  63       4.694  20.304  27.037  1.00 52.10      A    C  
ATOM    449  N   HIS A  64       8.746  15.869  26.725  1.00 46.05      A    N  
ATOM    450  CA  HIS A  64       9.252  14.618  26.209  1.00 46.38      A    C  
ATOM    451  C   HIS A  64       9.587  13.662  27.360  1.00 44.80      A    C  
ATOM    452  O   HIS A  64       9.270  12.481  27.315  1.00 44.14      A    O  
ATOM    453  CB  HIS A  64      10.549  14.842  25.422  1.00 47.13      A    C  
ATOM    454  CG  HIS A  64      10.355  15.224  23.988  1.00 51.49      A    C  
ATOM    455  CD2 HIS A  64      10.331  14.474  22.857  1.00 54.88      A    C  
ATOM    456  ND1 HIS A  64      10.216  16.538  23.581  1.00 56.55      A    N  
ATOM    457  CE1 HIS A  64      10.092  16.580  22.266  1.00 57.42      A    C  
ATOM    458  NE2 HIS A  64      10.157  15.342  21.800  1.00 57.38      A    N  
ATOM    459  N   ALA A  65      10.246  14.190  28.381  1.00 42.75      A    N  
ATOM    460  CA  ALA A  65      10.660  13.372  29.507  1.00 41.08      A    C  
ATOM    461  C   ALA A  65       9.490  12.793  30.284  1.00 39.57      A    C  
ATOM    462  O   ALA A  65       9.529  11.633  30.640  1.00 39.22      A    O  
ATOM    463  CB  ALA A  65      11.559  14.166  30.418  1.00 40.90      A    C  
ATOM    464  N   LYS A  66       8.475  13.604  30.534  1.00 39.32      A    N  
ATOM    465  CA  LYS A  66       7.271  13.145  31.183  1.00 41.11      A    C  
ATOM    466  C   LYS A  66       6.499  12.132  30.299  1.00 41.34      A    C  
ATOM    467  O   LYS A  66       5.888  11.200  30.819  1.00 40.25      A    O  
ATOM    468  CB  LYS A  66       6.353  14.338  31.529  1.00 40.54      A    C  
ATOM    469  CG  LYS A  66       5.095  13.917  32.257  1.00 42.44      A    C  
ATOM    470  CD  LYS A  66       4.262  15.123  32.660  1.00 47.60      A    C  
ATOM    471  CE  LYS A  66       3.098  14.723  33.545  1.00 46.61      A    C  
ATOM    472  NZ  LYS A  66       2.463  15.998  34.134  1.00 52.29      A    N1+
ATOM    473  N   ARG A  67       6.492  12.339  28.982  1.00 42.02      A    N  
ATOM    474  CA  ARG A  67       5.830  11.363  28.092  1.00 44.48      A    C  
ATOM    475  C   ARG A  67       6.588  10.019  28.078  1.00 41.90      A    C  
ATOM    476  O   ARG A  67       5.989   8.942  28.086  1.00 43.67      A    O  
ATOM    477  CB  ARG A  67       5.700  11.918  26.679  1.00 45.21      A    C  
ATOM    478  CG  ARG A  67       5.629  10.818  25.607  1.00 49.51      A    C  
ATOM    479  CD  ARG A  67       5.052  11.255  24.244  1.00 50.56      A    C  
ATOM    480  NE  ARG A  67       5.279  12.666  23.922  1.00 60.35      A    N  
ATOM    481  CZ  ARG A  67       6.441  13.139  23.488  1.00 63.93      A    C  
ATOM    482  NH1 ARG A  67       7.488  12.315  23.394  1.00 64.74      A    N1+
ATOM    483  NH2 ARG A  67       6.552  14.429  23.174  1.00 63.44      A    N  
ATOM    484  N   THR A  68       7.913  10.077  28.029  1.00 41.77      A    N  
ATOM    485  CA  THR A  68       8.749   8.884  28.184  1.00 40.32      A    C  
ATOM    486  C   THR A  68       8.422   8.143  29.476  1.00 39.40      A    C  
ATOM    487  O   THR A  68       8.250   6.913  29.469  1.00 39.20      A    O  
ATOM    488  CB  THR A  68      10.244   9.283  28.198  1.00 41.09      A    C  
ATOM    489  CG2 THR A  68      11.135   8.081  28.337  1.00 41.93      A    C  
ATOM    490  OG1 THR A  68      10.566   9.944  26.971  1.00 39.35      A    O  
ATOM    491  N   TYR A  69       8.378   8.872  30.605  1.00 38.39      A    N  
ATOM    492  CA  TYR A  69       8.035   8.262  31.905  1.00 38.93      A    C  
ATOM    493  C   TYR A  69       6.597   7.653  31.841  1.00 38.89      A    C  
ATOM    494  O   TYR A  69       6.345   6.578  32.318  1.00 39.86      A    O  
ATOM    495  CB  TYR A  69       8.075   9.337  33.032  1.00 38.68      A    C  
ATOM    496  CG  TYR A  69       7.814   8.787  34.402  1.00 37.84      A    C  
ATOM    497  CD1 TYR A  69       8.721   7.921  35.007  1.00 37.79      A    C  
ATOM    498  CD2 TYR A  69       6.642   9.122  35.103  1.00 39.54      A    C  
ATOM    499  CE1 TYR A  69       8.502   7.405  36.297  1.00 36.53      A    C  
ATOM    500  CE2 TYR A  69       6.402   8.611  36.361  1.00 40.13      A    C  
ATOM    501  CZ  TYR A  69       7.348   7.775  36.959  1.00 40.60      A    C  
ATOM    502  OH  TYR A  69       7.099   7.264  38.195  1.00 43.13      A    O  
ATOM    503  N   ARG A  70       5.661   8.373  31.261  1.00 39.27      A    N  
ATOM    504  CA  ARG A  70       4.251   7.963  31.262  1.00 40.37      A    C  
ATOM    505  C   ARG A  70       4.144   6.633  30.466  1.00 41.34      A    C  
ATOM    506  O   ARG A  70       3.501   5.682  30.895  1.00 41.12      A    O  
ATOM    507  CB  ARG A  70       3.432   9.104  30.603  1.00 40.08      A    C  
ATOM    508  CG  ARG A  70       1.967   8.713  30.174  1.00 40.81      A    C  
ATOM    509  CD  ARG A  70       1.422   9.800  29.179  1.00 42.30      A    C  
ATOM    510  NE  ARG A  70       1.301  11.081  29.878  1.00 45.20      A    N  
ATOM    511  CZ  ARG A  70       1.861  12.228  29.494  1.00 45.59      A    C  
ATOM    512  NH1 ARG A  70       2.559  12.299  28.366  0.50 43.79      A    N1+
ATOM    513  NH2 ARG A  70       1.698  13.322  30.247  0.50 40.52      A    N  
ATOM    514  N   GLU A  71       4.838   6.571  29.327  1.00 43.02      A    N  
ATOM    515  CA  GLU A  71       4.891   5.383  28.471  1.00 45.00      A    C  
ATOM    516  C   GLU A  71       5.510   4.188  29.157  1.00 43.69      A    C  
ATOM    517  O   GLU A  71       4.909   3.136  29.166  1.00 43.72      A    O  
ATOM    518  CB  GLU A  71       5.611   5.652  27.139  1.00 45.43      A    C  
ATOM    519  CG  GLU A  71       5.460   4.452  26.159  1.00 49.85      A    C  
ATOM    520  CD  GLU A  71       6.224   4.628  24.843  1.00 50.32      A    C  
ATOM    521  OE1 GLU A  71       6.051   3.741  23.958  1.00 57.96      A    O  
ATOM    522  OE2 GLU A  71       6.974   5.627  24.700  1.00 54.71      A    O1-
ATOM    523  N   LEU A  72       6.693   4.347  29.739  1.00 42.06      A    N  
ATOM    524  CA  LEU A  72       7.304   3.280  30.516  1.00 41.42      A    C  
ATOM    525  C   LEU A  72       6.428   2.812  31.692  1.00 41.35      A    C  
ATOM    526  O   LEU A  72       6.231   1.616  31.855  1.00 41.47      A    O  
ATOM    527  CB  LEU A  72       8.697   3.707  30.999  1.00 41.36      A    C  
ATOM    528  CG  LEU A  72       9.501   2.672  31.766  1.00 43.52      A    C  
ATOM    529  CD1 LEU A  72       9.641   1.322  31.048  1.00 43.67      A    C  
ATOM    530  CD2 LEU A  72      10.867   3.297  32.034  1.00 43.12      A    C  
ATOM    531  N   ARG A  73       5.886   3.737  32.485  1.00 40.33      A    N  
ATOM    532  CA  ARG A  73       5.054   3.347  33.643  1.00 41.57      A    C  
ATOM    533  C   ARG A  73       3.841   2.514  33.201  1.00 40.94      A    C  
ATOM    534  O   ARG A  73       3.528   1.481  33.788  1.00 40.71      A    O  
ATOM    535  CB  ARG A  73       4.576   4.576  34.423  1.00 41.39      A    C  
ATOM    536  CG  ARG A  73       5.588   5.141  35.469  1.00 45.29      A    C  
ATOM    537  CD  ARG A  73       5.771   4.259  36.715  1.00 49.32      A    C  
ATOM    538  NE  ARG A  73       4.521   3.981  37.385  1.00 51.59      A    N  
ATOM    539  CZ  ARG A  73       3.836   4.843  38.132  1.00 56.30      A    C  
ATOM    540  NH1 ARG A  73       4.287   6.073  38.353  1.00 56.76      A    N1+
ATOM    541  NH2 ARG A  73       2.672   4.468  38.660  1.00 55.27      A    N  
ATOM    542  N   LEU A  74       3.169   2.996  32.159  1.00 40.82      A    N  
ATOM    543  CA  LEU A  74       1.939   2.356  31.677  1.00 42.01      A    C  
ATOM    544  C   LEU A  74       2.296   0.950  31.245  1.00 41.06      A    C  
ATOM    545  O   LEU A  74       1.670  -0.002  31.725  1.00 41.14      A    O  
ATOM    546  CB  LEU A  74       1.335   3.131  30.528  1.00 41.38      A    C  
ATOM    547  CG  LEU A  74      -0.161   3.409  30.412  1.00 48.39      A    C  
ATOM    548  CD1 LEU A  74      -0.363   3.481  28.939  1.00 50.73      A    C  
ATOM    549  CD2 LEU A  74      -1.099   2.336  30.987  1.00 50.51      A    C  
ATOM    550  N   LEU A  75       3.293   0.806  30.355  1.00 39.94      A    N  
ATOM    551  CA  LEU A  75       3.642  -0.527  29.858  1.00 40.19      A    C  
ATOM    552  C   LEU A  75       4.073  -1.466  30.930  1.00 40.70      A    C  
ATOM    553  O   LEU A  75       3.818  -2.667  30.828  1.00 39.43      A    O  
ATOM    554  CB  LEU A  75       4.729  -0.493  28.758  1.00 40.67      A    C  
ATOM    555  CG  LEU A  75       4.268   0.075  27.430  1.00 42.68      A    C  
ATOM    556  CD1 LEU A  75       5.498   0.433  26.615  1.00 42.93      A    C  
ATOM    557  CD2 LEU A  75       3.435  -0.965  26.671  1.00 42.42      A    C  
ATOM    558  N   LYS A  76       4.836  -0.976  31.920  1.00 40.89      A    N  
ATOM    559  CA  LYS A  76       5.173  -1.854  33.068  1.00 42.02      A    C  
ATOM    560  C   LYS A  76       3.942  -2.332  33.861  1.00 42.35      A    C  
ATOM    561  O   LYS A  76       3.965  -3.370  34.482  1.00 42.77      A    O  
ATOM    562  CB  LYS A  76       6.097  -1.158  34.066  1.00 41.15      A    C  
ATOM    563  CG  LYS A  76       7.553  -1.172  33.641  1.00 42.81      A    C  
ATOM    564  CD  LYS A  76       8.390  -0.345  34.650  1.00 44.55      A    C  
ATOM    565  CE  LYS A  76       8.926  -1.242  35.767  1.00 44.08      A    C  
ATOM    566  NZ  LYS A  76       9.983  -0.486  36.556  1.00 46.02      A    N1+
ATOM    567  N   HIS A  77       2.896  -1.537  33.899  1.00 43.56      A    N  
ATOM    568  CA  HIS A  77       1.781  -1.898  34.749  1.00 44.43      A    C  
ATOM    569  C   HIS A  77       0.945  -3.029  34.119  1.00 45.17      A    C  
ATOM    570  O   HIS A  77       0.431  -3.935  34.830  1.00 45.03      A    O  
ATOM    571  CB  HIS A  77       0.903  -0.695  35.008  1.00 44.61      A    C  
ATOM    572  CG  HIS A  77      -0.104  -0.918  36.096  1.00 48.70      A    C  
ATOM    573  CD2 HIS A  77      -1.438  -1.143  36.038  1.00 48.93      A    C  
ATOM    574  ND1 HIS A  77       0.232  -0.959  37.433  1.00 53.78      A    N  
ATOM    575  CE1 HIS A  77      -0.859  -1.185  38.153  1.00 53.01      A    C  
ATOM    576  NE2 HIS A  77      -1.885  -1.293  37.327  1.00 50.94      A    N  
ATOM    577  N   MET A  78       0.843  -2.995  32.798  1.00 43.44      A    N  
ATOM    578  CA  MET A  78      -0.095  -3.884  32.070  1.00 44.59      A    C  
ATOM    579  C   MET A  78       0.322  -5.328  32.052  1.00 44.02      A    C  
ATOM    580  O   MET A  78       1.275  -5.709  31.351  1.00 44.26      A    O  
ATOM    581  CB  MET A  78      -0.298  -3.391  30.653  1.00 43.88      A    C  
ATOM    582  CG  MET A  78      -0.937  -1.999  30.614  1.00 48.77      A    C  
ATOM    583  SD  MET A  78      -2.682  -1.805  31.067  1.00 58.22      A    S  
ATOM    584  CE  MET A  78      -2.668  -1.366  32.807  1.00 55.16      A    C  
ATOM    585  N   LYS A  79      -0.397  -6.156  32.807  1.00 43.56      A    N  
ATOM    586  CA  LYS A  79      -0.092  -7.587  32.806  1.00 43.97      A    C  
ATOM    587  C   LYS A  79      -1.319  -8.433  32.533  1.00 43.16      A    C  
ATOM    588  O   LYS A  79      -1.964  -8.930  33.457  1.00 43.73      A    O  
ATOM    589  CB  LYS A  79       0.618  -8.001  34.110  1.00 43.97      A    C  
ATOM    590  CG  LYS A  79       2.017  -7.357  34.183  1.00 46.75      A    C  
ATOM    591  CD  LYS A  79       2.476  -7.165  35.591  1.00 52.62      A    C  
ATOM    592  CE  LYS A  79       3.963  -6.732  35.577  1.00 57.79      A    C  
ATOM    593  NZ  LYS A  79       4.711  -7.295  36.743  1.00 60.21      A    N1+
ATOM    594  N   HIS A  80      -1.633  -8.573  31.255  1.00 42.71      A    N  
ATOM    595  CA  HIS A  80      -2.869  -9.205  30.818  1.00 42.57      A    C  
ATOM    596  C   HIS A  80      -2.735  -9.752  29.416  1.00 42.52      A    C  
ATOM    597  O   HIS A  80      -2.110  -9.131  28.547  1.00 42.56      A    O  
ATOM    598  CB  HIS A  80      -4.002  -8.211  30.888  1.00 42.33      A    C  
ATOM    599  CG  HIS A  80      -5.371  -8.821  30.711  1.00 42.06      A    C  
ATOM    600  CD2 HIS A  80      -6.367  -9.062  31.603  1.00 41.49      A    C  
ATOM    601  ND1 HIS A  80      -5.858  -9.214  29.484  1.00 42.23      A    N  
ATOM    602  CE1 HIS A  80      -7.088  -9.678  29.624  1.00 40.52      A    C  
ATOM    603  NE2 HIS A  80      -7.427  -9.584  30.899  1.00 40.37      A    N  
ATOM    604  N   GLU A  81      -3.333 -10.923  29.194  1.00 42.73      A    N  
ATOM    605  CA  GLU A  81      -3.251 -11.624  27.895  1.00 43.57      A    C  
ATOM    606  C   GLU A  81      -3.686 -10.827  26.667  1.00 41.70      A    C  
ATOM    607  O   GLU A  81      -3.138 -10.998  25.572  1.00 41.59      A    O  
ATOM    608  CB  GLU A  81      -4.108 -12.884  27.942  1.00 44.66      A    C  
ATOM    609  CG  GLU A  81      -3.720 -13.848  29.033  1.00 51.68      A    C  
ATOM    610  CD  GLU A  81      -4.862 -14.824  29.388  1.00 59.86      A    C  
ATOM    611  OE1 GLU A  81      -5.633 -15.205  28.455  1.00 61.77      A    O  
ATOM    612  OE2 GLU A  81      -4.966 -15.202  30.589  1.00 61.80      A    O1-
ATOM    613  N   ASN A  82      -4.661  -9.946  26.850  1.00 40.59      A    N  
ATOM    614  CA  ASN A  82      -5.251  -9.197  25.747  1.00 39.48      A    C  
ATOM    615  C   ASN A  82      -4.827  -7.748  25.749  1.00 39.95      A    C  
ATOM    616  O   ASN A  82      -5.550  -6.871  25.207  1.00 38.06      A    O  
ATOM    617  CB  ASN A  82      -6.797  -9.277  25.869  1.00 39.47      A    C  
ATOM    618  CG  ASN A  82      -7.314 -10.714  25.828  1.00 39.30      A    C  
ATOM    619  ND2 ASN A  82      -7.029 -11.401  24.755  1.00 38.36      A    N  
ATOM    620  OD1 ASN A  82      -7.995 -11.165  26.734  1.00 39.39      A    O  
ATOM    621  N   VAL A  83      -3.688  -7.459  26.401  1.00 39.68      A    N  
ATOM    622  CA  VAL A  83      -3.213  -6.069  26.469  1.00 40.70      A    C  
ATOM    623  C   VAL A  83      -1.713  -6.128  26.252  1.00 41.86      A    C  
ATOM    624  O   VAL A  83      -1.025  -6.912  26.908  1.00 40.87      A    O  
ATOM    625  CB  VAL A  83      -3.433  -5.400  27.856  1.00 40.83      A    C  
ATOM    626  CG1 VAL A  83      -2.885  -3.943  27.825  1.00 40.17      A    C  
ATOM    627  CG2 VAL A  83      -4.932  -5.377  28.247  1.00 42.44      A    C  
ATOM    628  N   ILE A  84      -1.181  -5.298  25.376  1.00 43.16      A    N  
ATOM    629  CA  ILE A  84       0.273  -5.368  25.201  1.00 46.22      A    C  
ATOM    630  C   ILE A  84       1.032  -4.887  26.463  1.00 46.41      A    C  
ATOM    631  O   ILE A  84       0.758  -3.807  26.974  1.00 48.34      A    O  
ATOM    632  CB  ILE A  84       0.735  -4.608  23.953  1.00 47.28      A    C  
ATOM    633  CG1 ILE A  84       2.107  -5.121  23.518  1.00 50.42      A    C  
ATOM    634  CG2 ILE A  84       0.744  -3.103  24.201  1.00 50.33      A    C  
ATOM    635  CD1 ILE A  84       2.038  -6.442  22.708  1.00 55.07      A    C  
ATOM    636  N   GLY A  85       1.954  -5.695  26.969  1.00 46.05      A    N  
ATOM    637  CA  GLY A  85       2.820  -5.256  28.056  1.00 46.18      A    C  
ATOM    638  C   GLY A  85       4.295  -5.217  27.683  1.00 45.90      A    C  
ATOM    639  O   GLY A  85       4.651  -5.319  26.510  1.00 46.45      A    O  
ATOM    640  N   LEU A  86       5.150  -5.036  28.683  1.00 44.30      A    N  
ATOM    641  CA  LEU A  86       6.570  -4.798  28.431  1.00 44.48      A    C  
ATOM    642  C   LEU A  86       7.292  -6.109  28.551  1.00 43.53      A    C  
ATOM    643  O   LEU A  86       7.182  -6.753  29.566  1.00 43.57      A    O  
ATOM    644  CB  LEU A  86       7.134  -3.855  29.471  1.00 43.83      A    C  
ATOM    645  CG  LEU A  86       8.407  -3.069  29.102  1.00 44.88      A    C  
ATOM    646  CD1 LEU A  86       8.373  -2.486  27.699  1.00 42.96      A    C  
ATOM    647  CD2 LEU A  86       8.593  -1.989  30.137  1.00 38.21      A    C  
ATOM    648  N   LEU A  87       8.018  -6.506  27.511  1.00 44.11      A    N  
ATOM    649  CA  LEU A  87       8.869  -7.711  27.585  1.00 43.91      A    C  
ATOM    650  C   LEU A  87      10.271  -7.391  28.083  1.00 44.00      A    C  
ATOM    651  O   LEU A  87      10.917  -8.245  28.664  1.00 44.30      A    O  
ATOM    652  CB  LEU A  87       9.005  -8.369  26.222  1.00 43.54      A    C  
ATOM    653  CG  LEU A  87       7.770  -9.010  25.621  1.00 44.29      A    C  
ATOM    654  CD1 LEU A  87       8.174  -9.563  24.266  1.00 44.43      A    C  
ATOM    655  CD2 LEU A  87       7.251 -10.091  26.511  1.00 43.79      A    C  
ATOM    656  N   ASP A  88      10.747  -6.177  27.815  1.00 43.52      A    N  
ATOM    657  CA  ASP A  88      12.090  -5.735  28.258  1.00 42.80      A    C  
ATOM    658  C   ASP A  88      12.138  -4.221  28.102  1.00 41.48      A    C  
ATOM    659  O   ASP A  88      11.368  -3.643  27.319  1.00 40.79      A    O  
ATOM    660  CB  ASP A  88      13.197  -6.387  27.393  1.00 42.55      A    C  
ATOM    661  CG  ASP A  88      14.602  -6.326  28.030  1.00 46.69      A    C  
ATOM    662  OD1 ASP A  88      14.706  -6.012  29.242  1.00 45.42      A    O  
ATOM    663  OD2 ASP A  88      15.604  -6.651  27.298  1.00 49.90      A    O1-
ATOM    664  N   VAL A  89      12.997  -3.586  28.886  1.00 40.99      A    N  
ATOM    665  CA  VAL A  89      13.379  -2.190  28.699  1.00 41.25      A    C  
ATOM    666  C   VAL A  89      14.854  -2.126  29.036  1.00 41.83      A    C  
ATOM    667  O   VAL A  89      15.302  -2.712  29.988  1.00 40.46      A    O  
ATOM    668  CB  VAL A  89      12.539  -1.151  29.537  1.00 42.48      A    C  
ATOM    669  CG1 VAL A  89      12.568  -1.442  31.052  1.00 42.85      A    C  
ATOM    670  CG2 VAL A  89      13.029   0.284  29.297  1.00 40.37      A    C  
ATOM    671  N   PHE A  90      15.616  -1.469  28.186  1.00 43.16      A    N  
ATOM    672  CA  PHE A  90      17.034  -1.375  28.411  1.00 45.05      A    C  
ATOM    673  C   PHE A  90      17.530  -0.048  27.903  1.00 45.99      A    C  
ATOM    674  O   PHE A  90      16.834   0.683  27.167  1.00 45.38      A    O  
ATOM    675  CB  PHE A  90      17.782  -2.534  27.725  1.00 44.38      A    C  
ATOM    676  CG  PHE A  90      17.594  -2.596  26.231  1.00 45.49      A    C  
ATOM    677  CD1 PHE A  90      18.376  -1.831  25.384  1.00 45.14      A    C  
ATOM    678  CD2 PHE A  90      16.665  -3.464  25.670  1.00 45.77      A    C  
ATOM    679  CE1 PHE A  90      18.219  -1.895  24.009  1.00 46.23      A    C  
ATOM    680  CE2 PHE A  90      16.501  -3.536  24.298  1.00 43.45      A    C  
ATOM    681  CZ  PHE A  90      17.263  -2.756  23.473  1.00 45.48      A    C  
ATOM    682  N   THR A  91      18.747   0.229  28.319  1.00 47.53      A    N  
ATOM    683  CA  THR A  91      19.522   1.380  27.902  1.00 49.14      A    C  
ATOM    684  C   THR A  91      20.967   0.888  27.876  1.00 49.55      A    C  
ATOM    685  O   THR A  91      21.351   0.094  28.721  1.00 49.29      A    O  
ATOM    686  CB  THR A  91      19.343   2.593  28.911  1.00 48.92      A    C  
ATOM    687  CG2 THR A  91      19.462   2.153  30.382  1.00 50.32      A    C  
ATOM    688  OG1 THR A  91      20.318   3.615  28.632  1.00 51.13      A    O  
ATOM    689  N   PRO A  92      21.779   1.367  26.920  1.00 51.59      A    N  
ATOM    690  CA  PRO A  92      23.178   0.970  26.934  1.00 52.42      A    C  
ATOM    691  C   PRO A  92      24.003   1.730  28.002  1.00 53.99      A    C  
ATOM    692  O   PRO A  92      25.168   1.416  28.192  1.00 53.01      A    O  
ATOM    693  CB  PRO A  92      23.663   1.340  25.534  1.00 52.94      A    C  
ATOM    694  CG  PRO A  92      22.443   1.890  24.775  1.00 52.52      A    C  
ATOM    695  CD  PRO A  92      21.465   2.277  25.802  1.00 51.62      A    C  
ATOM    696  N   ALA A  93      23.390   2.698  28.698  1.00 54.82      A    N  
ATOM    697  CA  ALA A  93      24.063   3.478  29.746  1.00 56.08      A    C  
ATOM    698  C   ALA A  93      24.332   2.708  31.036  1.00 57.45      A    C  
ATOM    699  O   ALA A  93      23.484   1.944  31.514  1.00 57.55      A    O  
ATOM    700  CB  ALA A  93      23.268   4.680  30.059  1.00 56.19      A    C  
ATOM    701  N   ARG A  94      25.500   2.940  31.628  1.00 58.44      A    N  
ATOM    702  CA  ARG A  94      25.910   2.189  32.814  1.00 60.00      A    C  
ATOM    703  C   ARG A  94      25.587   2.980  34.086  1.00 59.32      A    C  
ATOM    704  O   ARG A  94      25.697   2.467  35.192  1.00 59.13      A    O  
ATOM    705  CB  ARG A  94      27.402   1.838  32.732  1.00 60.37      A    C  
ATOM    706  CG  ARG A  94      27.849   1.147  31.421  1.00 62.01      A    C  
ATOM    707  CD  ARG A  94      29.381   1.163  31.297  1.00 63.59      A    C  
ATOM    708  NE  ARG A  94      29.936   0.041  30.521  1.00 71.24      A    N  
ATOM    709  CZ  ARG A  94      30.014  -1.224  30.948  1.00 72.22      A    C  
ATOM    710  NH1 ARG A  94      29.545  -1.566  32.147  1.00 73.18      A    N1+
ATOM    711  NH2 ARG A  94      30.545  -2.159  30.166  1.00 72.48      A    N  
ATOM    712  N   SER A  95      25.164   4.233  33.910  1.00 59.11      A    N  
ATOM    713  CA  SER A  95      24.816   5.116  35.015  1.00 59.48      A    C  
ATOM    714  C   SER A  95      23.844   6.163  34.524  1.00 58.81      A    C  
ATOM    715  O   SER A  95      23.673   6.361  33.309  1.00 58.12      A    O  
ATOM    716  CB  SER A  95      26.070   5.832  35.555  1.00 60.19      A    C  
ATOM    717  OG  SER A  95      26.669   6.601  34.517  1.00 61.83      A    O  
ATOM    718  N   LEU A  96      23.240   6.865  35.473  1.00 58.91      A    N  
ATOM    719  CA  LEU A  96      22.299   7.942  35.168  1.00 59.17      A    C  
ATOM    720  C   LEU A  96      22.936   9.094  34.375  1.00 59.96      A    C  
ATOM    721  O   LEU A  96      22.263   9.747  33.550  1.00 59.28      A    O  
ATOM    722  CB  LEU A  96      21.606   8.422  36.447  1.00 58.92      A    C  
ATOM    723  CG  LEU A  96      20.707   9.655  36.376  1.00 59.50      A    C  
ATOM    724  CD1 LEU A  96      19.371   9.356  35.715  1.00 57.34      A    C  
ATOM    725  CD2 LEU A  96      20.510  10.219  37.793  1.00 59.47      A    C  
ATOM    726  N   GLU A  97      24.236   9.316  34.587  1.00 61.24      A    N  
ATOM    727  CA  GLU A  97      24.976  10.317  33.809  1.00 62.45      A    C  
ATOM    728  C   GLU A  97      25.037  10.056  32.303  1.00 62.63      A    C  
ATOM    729  O   GLU A  97      24.885  11.000  31.506  1.00 63.73      A    O  
ATOM    730  CB  GLU A  97      26.381  10.536  34.375  1.00 63.35      A    C  
ATOM    731  CG  GLU A  97      26.362  11.230  35.717  1.00 65.86      A    C  
ATOM    732  CD  GLU A  97      26.358  10.248  36.882  1.00 71.16      A    C  
ATOM    733  OE1 GLU A  97      27.446   9.653  37.147  1.00 74.07      A    O  
ATOM    734  OE2 GLU A  97      25.292  10.092  37.538  1.00 70.17      A    O1-
ATOM    735  N   GLU A  98      25.245   8.800  31.891  1.00 62.54      A    N  
ATOM    736  CA  GLU A  98      25.282   8.475  30.447  1.00 61.81      A    C  
ATOM    737  C   GLU A  98      23.895   8.157  29.896  1.00 60.32      A    C  
ATOM    738  O   GLU A  98      23.738   7.873  28.680  1.00 60.41      A    O  
ATOM    739  CB  GLU A  98      26.182   7.277  30.147  1.00 62.70      A    C  
ATOM    740  CG  GLU A  98      27.377   7.083  31.075  1.00 66.80      A    C  
ATOM    741  CD  GLU A  98      27.764   5.608  31.170  1.00 71.51      A    C  
ATOM    742  OE1 GLU A  98      27.512   4.856  30.184  1.00 71.70      A    O  
ATOM    743  OE2 GLU A  98      28.307   5.197  32.229  1.00 73.13      A    O1-
ATOM    744  N   PHE A  99      22.896   8.177  30.783  1.00 58.02      A    N  
ATOM    745  CA  PHE A  99      21.552   7.724  30.427  1.00 55.77      A    C  
ATOM    746  C   PHE A  99      20.963   8.710  29.459  1.00 55.83      A    C  
ATOM    747  O   PHE A  99      20.676   9.842  29.837  1.00 55.62      A    O  
ATOM    748  CB  PHE A  99      20.681   7.617  31.672  1.00 54.04      A    C  
ATOM    749  CG  PHE A  99      19.272   7.125  31.411  1.00 51.96      A    C  
ATOM    750  CD1 PHE A  99      19.024   6.035  30.576  1.00 46.68      A    C  
ATOM    751  CD2 PHE A  99      18.200   7.710  32.078  1.00 48.89      A    C  
ATOM    752  CE1 PHE A  99      17.707   5.581  30.393  1.00 45.69      A    C  
ATOM    753  CE2 PHE A  99      16.907   7.261  31.886  1.00 45.56      A    C  
ATOM    754  CZ  PHE A  99      16.666   6.200  31.051  1.00 45.82      A    C  
ATOM    755  N   ASN A 100      20.795   8.286  28.214  1.00 56.10      A    N  
ATOM    756  CA  ASN A 100      20.257   9.170  27.168  1.00 57.73      A    C  
ATOM    757  C   ASN A 100      19.252   8.485  26.276  1.00 56.91      A    C  
ATOM    758  O   ASN A 100      18.498   9.148  25.583  1.00 57.50      A    O  
ATOM    759  CB  ASN A 100      21.379   9.671  26.249  1.00 58.61      A    C  
ATOM    760  CG  ASN A 100      22.477  10.362  26.997  1.00 61.56      A    C  
ATOM    761  ND2 ASN A 100      23.684   9.821  26.878  1.00 62.68      A    N  
ATOM    762  OD1 ASN A 100      22.256  11.382  27.675  1.00 65.90      A    O  
ATOM    763  N   ASP A 101      19.299   7.156  26.264  1.00 56.24      A    N  
ATOM    764  CA  ASP A 101      18.529   6.339  25.341  1.00 55.32      A    C  
ATOM    765  C   ASP A 101      17.791   5.271  26.117  1.00 53.88      A    C  
ATOM    766  O   ASP A 101      18.347   4.679  27.058  1.00 53.53      A    O  
ATOM    767  CB  ASP A 101      19.441   5.673  24.311  1.00 56.35      A    C  
ATOM    768  CG  ASP A 101      19.895   6.642  23.201  1.00 59.91      A    C  
ATOM    769  OD1 ASP A 101      19.056   7.397  22.652  1.00 63.83      A    O  
ATOM    770  OD2 ASP A 101      21.098   6.631  22.868  1.00 63.56      A    O1-
ATOM    771  N   VAL A 102      16.542   5.064  25.702  1.00 51.56      A    N  
ATOM    772  CA  VAL A 102      15.586   4.119  26.274  1.00 49.54      A    C  
ATOM    773  C   VAL A 102      15.090   3.251  25.108  1.00 48.35      A    C  
ATOM    774  O   VAL A 102      14.667   3.776  24.060  1.00 48.86      A    O  
ATOM    775  CB  VAL A 102      14.338   4.854  26.901  1.00 49.09      A    C  
ATOM    776  CG1 VAL A 102      13.233   3.852  27.295  1.00 51.35      A    C  
ATOM    777  CG2 VAL A 102      14.721   5.675  28.101  1.00 49.01      A    C  
ATOM    778  N   TYR A 103      15.097   1.939  25.298  1.00 46.19      A    N  
ATOM    779  CA  TYR A 103      14.519   1.028  24.332  1.00 45.30      A    C  
ATOM    780  C   TYR A 103      13.485   0.182  25.015  1.00 44.61      A    C  
ATOM    781  O   TYR A 103      13.761  -0.330  26.093  1.00 43.15      A    O  
ATOM    782  CB  TYR A 103      15.580   0.063  23.835  1.00 46.95      A    C  
ATOM    783  CG  TYR A 103      16.678   0.673  23.030  1.00 47.98      A    C  
ATOM    784  CD1 TYR A 103      17.764   1.296  23.657  1.00 49.95      A    C  
ATOM    785  CD2 TYR A 103      16.670   0.576  21.647  1.00 49.49      A    C  
ATOM    786  CE1 TYR A 103      18.836   1.831  22.887  1.00 53.72      A    C  
ATOM    787  CE2 TYR A 103      17.725   1.092  20.871  1.00 51.98      A    C  
ATOM    788  CZ  TYR A 103      18.801   1.724  21.497  1.00 52.86      A    C  
ATOM    789  OH  TYR A 103      19.830   2.248  20.739  1.00 50.36      A    O  
ATOM    790  N   LEU A 104      12.334   0.008  24.348  1.00 43.47      A    N  
ATOM    791  CA  LEU A 104      11.173  -0.734  24.849  1.00 44.18      A    C  
ATOM    792  C   LEU A 104      10.964  -1.916  23.932  1.00 43.53      A    C  
ATOM    793  O   LEU A 104      11.000  -1.749  22.705  1.00 44.37      A    O  
ATOM    794  CB  LEU A 104       9.897   0.158  24.818  1.00 44.09      A    C  
ATOM    795  CG  LEU A 104       9.920   1.468  25.640  1.00 44.32      A    C  
ATOM    796  CD1 LEU A 104       8.587   2.260  25.507  1.00 47.49      A    C  
ATOM    797  CD2 LEU A 104      10.191   1.157  27.078  1.00 41.78      A    C  
ATOM    798  N   VAL A 105      10.765  -3.100  24.519  1.00 42.92      A    N  
ATOM    799  CA  VAL A 105      10.604  -4.364  23.761  1.00 41.87      A    C  
ATOM    800  C   VAL A 105       9.228  -4.960  24.066  1.00 42.25      A    C  
ATOM    801  O   VAL A 105       8.887  -5.203  25.212  1.00 41.31      A    O  
ATOM    802  CB  VAL A 105      11.654  -5.417  24.136  1.00 40.82      A    C  
ATOM    803  CG1 VAL A 105      11.491  -6.654  23.315  1.00 42.38      A    C  
ATOM    804  CG2 VAL A 105      13.104  -4.895  23.939  1.00 39.67      A    C  
ATOM    805  N   THR A 106       8.466  -5.229  23.019  1.00 43.62      A    N  
ATOM    806  CA  THR A 106       7.130  -5.778  23.167  1.00 45.91      A    C  
ATOM    807  C   THR A 106       6.962  -6.912  22.156  1.00 48.04      A    C  
ATOM    808  O   THR A 106       7.752  -7.059  21.230  1.00 48.21      A    O  
ATOM    809  CB  THR A 106       6.029  -4.718  22.887  1.00 46.15      A    C  
ATOM    810  CG2 THR A 106       6.096  -3.522  23.848  1.00 46.56      A    C  
ATOM    811  OG1 THR A 106       6.164  -4.262  21.539  1.00 47.01      A    O  
ATOM    812  N   HIS A 107       5.944  -7.731  22.344  1.00 50.29      A    N  
ATOM    813  CA  HIS A 107       5.604  -8.723  21.341  1.00 53.30      A    C  
ATOM    814  C   HIS A 107       5.429  -8.139  19.950  1.00 55.20      A    C  
ATOM    815  O   HIS A 107       4.746  -7.118  19.759  1.00 55.84      A    O  
ATOM    816  CB  HIS A 107       4.280  -9.391  21.691  1.00 53.51      A    C  
ATOM    817  CG  HIS A 107       4.370 -10.321  22.840  1.00 53.02      A    C  
ATOM    818  CD2 HIS A 107       3.943 -10.204  24.116  1.00 53.21      A    C  
ATOM    819  ND1 HIS A 107       4.949 -11.566  22.738  1.00 55.76      A    N  
ATOM    820  CE1 HIS A 107       4.883 -12.173  23.908  1.00 55.04      A    C  
ATOM    821  NE2 HIS A 107       4.268 -11.371  24.758  1.00 53.96      A    N  
ATOM    822  N   LEU A 108       5.998  -8.825  18.972  1.00 57.25      A    N  
ATOM    823  CA  LEU A 108       5.793  -8.449  17.605  1.00 59.31      A    C  
ATOM    824  C   LEU A 108       4.498  -9.089  17.173  1.00 60.55      A    C  
ATOM    825  O   LEU A 108       4.364 -10.309  17.144  1.00 59.98      A    O  
ATOM    826  CB  LEU A 108       6.933  -8.924  16.719  1.00 59.56      A    C  
ATOM    827  CG  LEU A 108       6.811  -8.325  15.322  1.00 60.73      A    C  
ATOM    828  CD1 LEU A 108       6.888  -6.778  15.333  1.00 62.82      A    C  
ATOM    829  CD2 LEU A 108       7.858  -8.916  14.402  1.00 63.10      A    C  
ATOM    830  N   MET A 109       3.544  -8.241  16.840  1.00 62.52      A    N  
ATOM    831  CA  MET A 109       2.240  -8.709  16.453  1.00 64.75      A    C  
ATOM    832  C   MET A 109       2.109  -8.576  14.931  1.00 65.62      A    C  
ATOM    833  O   MET A 109       2.544  -7.577  14.328  1.00 65.45      A    O  
ATOM    834  CB  MET A 109       1.160  -7.910  17.195  1.00 65.19      A    C  
ATOM    835  CG  MET A 109       1.088  -8.194  18.708  1.00 65.62      A    C  
ATOM    836  SD  MET A 109       0.625  -9.899  19.068  1.00 71.11      A    S  
ATOM    837  CE  MET A 109      -1.167  -9.865  19.021  1.00 66.14      A    C  
ATOM    838  N   GLY A 110       1.531  -9.601  14.311  1.00 66.78      A    N  
ATOM    839  CA  GLY A 110       1.242  -9.551  12.876  1.00 67.46      A    C  
ATOM    840  C   GLY A 110       0.190  -8.505  12.510  1.00 67.85      A    C  
ATOM    841  O   GLY A 110       0.407  -7.287  12.621  1.00 68.06      A    O  
ATOM    842  N   ALA A 111      -0.958  -8.992  12.067  1.00 67.21      A    N  
ATOM    843  CA  ALA A 111      -1.973  -8.148  11.520  1.00 67.08      A    C  
ATOM    844  C   ALA A 111      -2.515  -7.183  12.584  1.00 66.92      A    C  
ATOM    845  O   ALA A 111      -2.281  -7.355  13.785  1.00 66.63      A    O  
ATOM    846  CB  ALA A 111      -3.092  -9.021  10.955  1.00 66.99      A    C  
ATOM    847  N   ASP A 112      -3.178  -6.127  12.128  1.00 67.02      A    N  
ATOM    848  CA  ASP A 112      -4.126  -5.413  12.977  1.00 66.72      A    C  
ATOM    849  C   ASP A 112      -5.536  -5.751  12.479  1.00 66.27      A    C  
ATOM    850  O   ASP A 112      -5.692  -6.487  11.495  1.00 65.39      A    O  
ATOM    851  CB  ASP A 112      -3.828  -3.909  13.038  1.00 66.88      A    C  
ATOM    852  CG  ASP A 112      -4.010  -3.192  11.708  1.00 67.91      A    C  
ATOM    853  OD1 ASP A 112      -4.788  -3.656  10.847  1.00 69.16      A    O  
ATOM    854  OD2 ASP A 112      -3.383  -2.121  11.535  1.00 69.52      A    O1-
ATOM    855  N   LEU A 113      -6.553  -5.237  13.153  1.00 65.95      A    N  
ATOM    856  CA  LEU A 113      -7.924  -5.509  12.757  1.00 66.22      A    C  
ATOM    857  C   LEU A 113      -8.408  -4.874  11.444  1.00 66.70      A    C  
ATOM    858  O   LEU A 113      -9.442  -5.293  10.934  1.00 65.98      A    O  
ATOM    859  CB  LEU A 113      -8.896  -5.181  13.882  1.00 65.84      A    C  
ATOM    860  CG  LEU A 113      -9.557  -6.396  14.507  1.00 67.02      A    C  
ATOM    861  CD1 LEU A 113      -8.555  -7.270  15.212  1.00 65.46      A    C  
ATOM    862  CD2 LEU A 113     -10.605  -5.913  15.468  1.00 66.65      A    C  
ATOM    863  N   ASN A 114      -7.712  -3.876  10.898  1.00 67.96      A    N  
ATOM    864  CA  ASN A 114      -7.986  -3.509   9.497  1.00 70.01      A    C  
ATOM    865  C   ASN A 114      -7.761  -4.759   8.636  1.00 71.18      A    C  
ATOM    866  O   ASN A 114      -6.618  -5.168   8.394  1.00 71.16      A    O  
ATOM    867  CB  ASN A 114      -7.147  -2.329   9.042  1.00 70.27      A    C  
ATOM    868  CG  ASN A 114      -7.767  -1.004   9.405  1.00 70.57      A    C  
ATOM    869  ND2 ASN A 114      -9.053  -1.018   9.757  1.00 72.15      A    N  
ATOM    870  OD1 ASN A 114      -7.101   0.027   9.373  1.00 71.73      A    O  
ATOM    871  N   ASN A 115      -8.877  -5.381   8.233  1.00 72.36      A    N  
ATOM    872  CA  ASN A 115      -8.928  -6.835   7.955  1.00 73.34      A    C  
ATOM    873  C   ASN A 115     -10.374  -7.333   7.794  1.00 73.22      A    C  
ATOM    874  O   ASN A 115     -11.286  -6.842   8.458  1.00 72.65      A    O  
ATOM    875  CB  ASN A 115      -8.175  -7.622   9.064  1.00 73.34      A    C  
ATOM    876  CG  ASN A 115      -8.841  -8.959   9.446  1.00 75.19      A    C  
ATOM    877  ND2 ASN A 115      -8.423 -10.034   8.782  1.00 76.48      A    N  
ATOM    878  OD1 ASN A 115      -9.676  -9.029  10.362  1.00 76.02      A    O  
ATOM    879  N   GLN A 120     -14.848 -11.448   1.460  1.00 74.91      A    N  
ATOM    880  CA  GLN A 120     -15.794 -11.957   2.446  1.00 74.79      A    C  
ATOM    881  C   GLN A 120     -15.840 -11.024   3.671  1.00 73.88      A    C  
ATOM    882  O   GLN A 120     -15.120 -10.011   3.712  1.00 74.96      A    O  
ATOM    883  CB  GLN A 120     -15.385 -13.382   2.854  1.00 74.92      A    C  
ATOM    884  CG  GLN A 120     -16.539 -14.385   2.950  1.00 75.57      A    C  
ATOM    885  CD  GLN A 120     -16.072 -15.827   2.846  1.00 75.98      A    C  
ATOM    886  NE2 GLN A 120     -14.899 -16.119   3.426  1.00 76.12      A    N  
ATOM    887  OE1 GLN A 120     -16.749 -16.672   2.238  1.00 78.12      A    O  
ATOM    888  N   LYS A 121     -16.702 -11.348   4.642  1.00 71.87      A    N  
ATOM    889  CA  LYS A 121     -16.659 -10.747   6.009  1.00 69.61      A    C  
ATOM    890  C   LYS A 121     -16.386 -11.858   7.058  1.00 66.74      A    C  
ATOM    891  O   LYS A 121     -16.119 -13.027   6.685  1.00 66.93      A    O  
ATOM    892  CB  LYS A 121     -17.944  -9.935   6.335  1.00 69.82      A    C  
ATOM    893  CG  LYS A 121     -19.267 -10.708   6.158  1.00 70.72      A    C  
ATOM    894  CD  LYS A 121     -20.493  -9.860   6.532  1.00 70.77      A    C  
ATOM    895  CE  LYS A 121     -21.813 -10.522   6.124  1.00 72.51      A    C  
ATOM    896  NZ  LYS A 121     -22.069 -11.844   6.804  1.00 73.17      A    N1+
ATOM    897  N   LEU A 122     -16.434 -11.506   8.347  1.00 63.00      A    N  
ATOM    898  CA  LEU A 122     -16.167 -12.481   9.427  1.00 59.22      A    C  
ATOM    899  C   LEU A 122     -17.409 -13.286   9.800  1.00 56.54      A    C  
ATOM    900  O   LEU A 122     -18.524 -12.787   9.631  1.00 55.43      A    O  
ATOM    901  CB  LEU A 122     -15.615 -11.785  10.665  1.00 58.63      A    C  
ATOM    902  CG  LEU A 122     -14.280 -11.060  10.550  1.00 58.48      A    C  
ATOM    903  CD1 LEU A 122     -13.825 -10.760  11.958  1.00 58.19      A    C  
ATOM    904  CD2 LEU A 122     -13.226 -11.886   9.793  1.00 57.74      A    C  
ATOM    905  N   THR A 123     -17.226 -14.525  10.284  1.00 53.49      A    N  
ATOM    906  CA  THR A 123     -18.364 -15.272  10.843  1.00 50.76      A    C  
ATOM    907  C   THR A 123     -18.764 -14.711  12.198  1.00 50.15      A    C  
ATOM    908  O   THR A 123     -17.926 -14.097  12.883  1.00 48.89      A    O  
ATOM    909  CB  THR A 123     -18.093 -16.795  11.005  1.00 51.30      A    C  
ATOM    910  CG2 THR A 123     -17.664 -17.436   9.687  1.00 51.37      A    C  
ATOM    911  OG1 THR A 123     -17.107 -17.028  12.017  1.00 45.67      A    O  
ATOM    912  N   ASP A 124     -20.025 -14.930  12.581  1.00 48.78      A    N  
ATOM    913  CA  ASP A 124     -20.516 -14.546  13.894  1.00 48.41      A    C  
ATOM    914  C   ASP A 124     -19.652 -15.109  15.015  1.00 47.85      A    C  
ATOM    915  O   ASP A 124     -19.376 -14.375  15.946  1.00 45.74      A    O  
ATOM    916  CB  ASP A 124     -21.981 -14.958  14.132  1.00 48.66      A    C  
ATOM    917  CG  ASP A 124     -22.547 -14.377  15.435  1.00 50.48      A    C  
ATOM    918  OD1 ASP A 124     -22.481 -13.132  15.618  1.00 51.80      A    O  
ATOM    919  OD2 ASP A 124     -23.066 -15.151  16.280  1.00 54.33      A    O1-
ATOM    920  N   ASP A 125     -19.224 -16.388  14.933  1.00 46.61      A    N  
ATOM    921  CA  ASP A 125     -18.417 -17.004  16.004  1.00 46.68      A    C  
ATOM    922  C   ASP A 125     -17.082 -16.275  16.179  1.00 45.33      A    C  
ATOM    923  O   ASP A 125     -16.599 -16.100  17.282  1.00 43.91      A    O  
ATOM    924  CB  ASP A 125     -18.073 -18.467  15.696  1.00 48.32      A    C  
ATOM    925  CG  ASP A 125     -19.269 -19.425  15.861  1.00 54.22      A    C  
ATOM    926  OD1 ASP A 125     -20.305 -19.023  16.444  1.00 56.97      A    O  
ATOM    927  OD2 ASP A 125     -19.144 -20.612  15.400  1.00 60.40      A    O1-
ATOM    928  N   HIS A 126     -16.484 -15.910  15.065  1.00 43.03      A    N  
ATOM    929  CA  HIS A 126     -15.261 -15.204  15.078  1.00 44.44      A    C  
ATOM    930  C   HIS A 126     -15.411 -13.743  15.533  1.00 43.88      A    C  
ATOM    931  O   HIS A 126     -14.530 -13.229  16.173  1.00 43.85      A    O  
ATOM    932  CB  HIS A 126     -14.718 -15.248  13.689  1.00 44.34      A    C  
ATOM    933  CG  HIS A 126     -13.289 -14.920  13.598  1.00 46.24      A    C  
ATOM    934  CD2 HIS A 126     -12.623 -14.098  12.759  1.00 49.62      A    C  
ATOM    935  ND1 HIS A 126     -12.343 -15.496  14.421  1.00 52.06      A    N  
ATOM    936  CE1 HIS A 126     -11.153 -15.021  14.098  1.00 50.93      A    C  
ATOM    937  NE2 HIS A 126     -11.296 -14.168  13.097  1.00 49.66      A    N  
ATOM    938  N   VAL A 127     -16.494 -13.065  15.178  1.00 44.20      A    N  
ATOM    939  CA  VAL A 127     -16.745 -11.722  15.744  1.00 43.43      A    C  
ATOM    940  C   VAL A 127     -16.952 -11.808  17.254  1.00 44.42      A    C  
ATOM    941  O   VAL A 127     -16.429 -10.983  18.018  1.00 43.29      A    O  
ATOM    942  CB  VAL A 127     -17.955 -11.082  15.071  1.00 45.22      A    C  
ATOM    943  CG1 VAL A 127     -18.391  -9.765  15.792  1.00 42.26      A    C  
ATOM    944  CG2 VAL A 127     -17.642 -10.884  13.609  1.00 41.89      A    C  
ATOM    945  N   GLN A 128     -17.700 -12.806  17.720  1.00 43.91      A    N  
ATOM    946  CA  GLN A 128     -17.828 -13.020  19.172  1.00 45.13      A    C  
ATOM    947  C   GLN A 128     -16.495 -13.143  19.861  1.00 45.22      A    C  
ATOM    948  O   GLN A 128     -16.289 -12.573  20.935  1.00 44.74      A    O  
ATOM    949  CB  GLN A 128     -18.593 -14.292  19.496  1.00 45.43      A    C  
ATOM    950  CG  GLN A 128     -20.081 -14.194  19.274  1.00 47.47      A    C  
ATOM    951  CD  GLN A 128     -20.737 -15.535  19.465  1.00 51.71      A    C  
ATOM    952  NE2 GLN A 128     -21.844 -15.754  18.774  1.00 53.81      A    N  
ATOM    953  OE1 GLN A 128     -20.237 -16.375  20.195  1.00 54.26      A    O  
ATOM    954  N   PHE A 129     -15.622 -13.951  19.270  1.00 43.58      A    N  
ATOM    955  CA  PHE A 129     -14.335 -14.226  19.852  1.00 44.15      A    C  
ATOM    956  C   PHE A 129     -13.460 -12.970  19.879  1.00 43.21      A    C  
ATOM    957  O   PHE A 129     -12.763 -12.733  20.855  1.00 44.38      A    O  
ATOM    958  CB  PHE A 129     -13.652 -15.358  19.075  1.00 44.94      A    C  
ATOM    959  CG  PHE A 129     -12.272 -15.760  19.607  1.00 45.78      A    C  
ATOM    960  CD1 PHE A 129     -12.073 -16.037  20.948  1.00 48.13      A    C  
ATOM    961  CD2 PHE A 129     -11.194 -15.893  18.719  1.00 49.48      A    C  
ATOM    962  CE1 PHE A 129     -10.804 -16.441  21.428  1.00 49.96      A    C  
ATOM    963  CE2 PHE A 129      -9.905 -16.263  19.174  1.00 48.27      A    C  
ATOM    964  CZ  PHE A 129      -9.723 -16.555  20.536  1.00 47.72      A    C  
ATOM    965  N   LEU A 130     -13.459 -12.197  18.805  1.00 41.81      A    N  
ATOM    966  CA  LEU A 130     -12.607 -11.010  18.775  1.00 40.57      A    C  
ATOM    967  C   LEU A 130     -13.119  -9.939  19.759  1.00 39.54      A    C  
ATOM    968  O   LEU A 130     -12.349  -9.350  20.526  1.00 37.99      A    O  
ATOM    969  CB  LEU A 130     -12.518 -10.448  17.370  1.00 39.99      A    C  
ATOM    970  CG  LEU A 130     -11.793 -11.312  16.347  1.00 42.03      A    C  
ATOM    971  CD1 LEU A 130     -12.212 -10.797  14.997  1.00 40.32      A    C  
ATOM    972  CD2 LEU A 130     -10.333 -11.123  16.521  1.00 47.30      A    C  
ATOM    973  N   ILE A 131     -14.416  -9.662  19.722  1.00 37.17      A    N  
ATOM    974  CA  ILE A 131     -14.992  -8.648  20.644  1.00 37.57      A    C  
ATOM    975  C   ILE A 131     -14.853  -9.087  22.078  1.00 38.62      A    C  
ATOM    976  O   ILE A 131     -14.557  -8.295  22.951  1.00 38.30      A    O  
ATOM    977  CB  ILE A 131     -16.488  -8.331  20.251  1.00 36.92      A    C  
ATOM    978  CG1 ILE A 131     -16.536  -7.929  18.793  1.00 34.20      A    C  
ATOM    979  CG2 ILE A 131     -17.083  -7.239  21.186  1.00 37.08      A    C  
ATOM    980  CD1 ILE A 131     -15.604  -6.748  18.388  1.00 34.10      A    C  
ATOM    981  N   TYR A 132     -15.042 -10.379  22.327  1.00 39.04      A    N  
ATOM    982  CA  TYR A 132     -14.842 -10.910  23.641  1.00 38.44      A    C  
ATOM    983  C   TYR A 132     -13.443 -10.552  24.166  1.00 39.15      A    C  
ATOM    984  O   TYR A 132     -13.264 -10.108  25.292  1.00 38.45      A    O  
ATOM    985  CB  TYR A 132     -14.977 -12.443  23.637  1.00 39.55      A    C  
ATOM    986  CG  TYR A 132     -14.691 -13.003  24.983  1.00 38.11      A    C  
ATOM    987  CD1 TYR A 132     -15.589 -12.805  26.008  1.00 40.94      A    C  
ATOM    988  CD2 TYR A 132     -13.519 -13.703  25.245  1.00 38.15      A    C  
ATOM    989  CE1 TYR A 132     -15.337 -13.263  27.287  1.00 42.93      A    C  
ATOM    990  CE2 TYR A 132     -13.241 -14.162  26.514  1.00 41.93      A    C  
ATOM    991  CZ  TYR A 132     -14.177 -13.931  27.535  1.00 39.59      A    C  
ATOM    992  OH  TYR A 132     -13.987 -14.361  28.818  1.00 43.12      A    O  
ATOM    993  N   GLN A 133     -12.444 -10.806  23.354  1.00 39.34      A    N  
ATOM    994  CA  GLN A 133     -11.100 -10.547  23.758  1.00 39.44      A    C  
ATOM    995  C   GLN A 133     -10.901  -9.054  24.035  1.00 38.16      A    C  
ATOM    996  O   GLN A 133     -10.202  -8.681  24.966  1.00 38.80      A    O  
ATOM    997  CB  GLN A 133     -10.175 -11.052  22.666  1.00 38.84      A    C  
ATOM    998  CG  GLN A 133     -10.103 -12.607  22.605  1.00 40.15      A    C  
ATOM    999  CD  GLN A 133      -9.112 -13.050  21.628  1.00 40.28      A    C  
ATOM   1000  NE2 GLN A 133      -9.533 -13.168  20.401  1.00 43.36      A    N  
ATOM   1001  OE1 GLN A 133      -7.925 -13.164  21.930  1.00 43.44      A    O  
ATOM   1002  N   ILE A 134     -11.545  -8.206  23.261  1.00 37.68      A    N  
ATOM   1003  CA  ILE A 134     -11.316  -6.767  23.366  1.00 37.18      A    C  
ATOM   1004  C   ILE A 134     -11.898  -6.323  24.697  1.00 37.29      A    C  
ATOM   1005  O   ILE A 134     -11.242  -5.635  25.491  1.00 34.27      A    O  
ATOM   1006  CB  ILE A 134     -11.982  -5.969  22.214  1.00 38.32      A    C  
ATOM   1007  CG1 ILE A 134     -11.280  -6.276  20.866  1.00 36.46      A    C  
ATOM   1008  CG2 ILE A 134     -11.882  -4.420  22.485  1.00 33.11      A    C  
ATOM   1009  CD1 ILE A 134     -12.133  -5.804  19.652  1.00 38.99      A    C  
ATOM   1010  N   LEU A 135     -13.130  -6.770  24.945  1.00 34.99      A    N  
ATOM   1011  CA  LEU A 135     -13.790  -6.529  26.226  1.00 35.60      A    C  
ATOM   1012  C   LEU A 135     -13.079  -7.097  27.426  1.00 35.64      A    C  
ATOM   1013  O   LEU A 135     -13.068  -6.448  28.444  1.00 36.09      A    O  
ATOM   1014  CB  LEU A 135     -15.237  -7.063  26.196  1.00 35.19      A    C  
ATOM   1015  CG  LEU A 135     -16.049  -6.290  25.168  1.00 37.64      A    C  
ATOM   1016  CD1 LEU A 135     -17.391  -7.052  25.002  1.00 35.53      A    C  
ATOM   1017  CD2 LEU A 135     -16.281  -4.806  25.563  1.00 34.02      A    C  
ATOM   1018  N   ARG A 136     -12.462  -8.285  27.325  1.00 36.16      A    N  
ATOM   1019  CA  ARG A 136     -11.693  -8.856  28.413  1.00 37.02      A    C  
ATOM   1020  C   ARG A 136     -10.472  -7.950  28.749  1.00 37.31      A    C  
ATOM   1021  O   ARG A 136     -10.198  -7.655  29.922  1.00 39.42      A    O  
ATOM   1022  CB  ARG A 136     -11.203 -10.268  27.985  1.00 36.51      A    C  
ATOM   1023  CG  ARG A 136     -10.586 -11.106  29.092  1.00 37.87      A    C  
ATOM   1024  CD  ARG A 136     -10.308 -12.546  28.618  1.00 39.64      A    C  
ATOM   1025  NE  ARG A 136      -9.821 -13.370  29.720  1.00 46.26      A    N  
ATOM   1026  CZ  ARG A 136      -8.556 -13.672  29.914  1.00 49.17      A    C  
ATOM   1027  NH1 ARG A 136      -7.651 -13.206  29.085  1.00 52.17      A    N1+
ATOM   1028  NH2 ARG A 136      -8.196 -14.434  30.928  1.00 51.32      A    N  
ATOM   1029  N   GLY A 137      -9.747  -7.538  27.720  1.00 37.17      A    N  
ATOM   1030  CA  GLY A 137      -8.662  -6.529  27.834  1.00 36.26      A    C  
ATOM   1031  C   GLY A 137      -9.142  -5.225  28.394  1.00 35.98      A    C  
ATOM   1032  O   GLY A 137      -8.509  -4.671  29.279  1.00 36.08      A    O  
ATOM   1033  N   LEU A 138     -10.277  -4.706  27.894  1.00 36.03      A    N  
ATOM   1034  CA  LEU A 138     -10.825  -3.447  28.421  1.00 36.16      A    C  
ATOM   1035  C   LEU A 138     -11.274  -3.505  29.856  1.00 36.94      A    C  
ATOM   1036  O   LEU A 138     -11.170  -2.512  30.584  1.00 38.76      A    O  
ATOM   1037  CB  LEU A 138     -12.017  -2.961  27.599  1.00 36.99      A    C  
ATOM   1038  CG  LEU A 138     -11.733  -2.224  26.311  1.00 41.61      A    C  
ATOM   1039  CD1 LEU A 138     -13.077  -1.740  25.760  1.00 42.82      A    C  
ATOM   1040  CD2 LEU A 138     -10.784  -1.035  26.598  1.00 43.77      A    C  
ATOM   1041  N   LYS A 139     -11.855  -4.615  30.266  1.00 37.74      A    N  
ATOM   1042  CA  LYS A 139     -12.211  -4.799  31.669  1.00 38.53      A    C  
ATOM   1043  C   LYS A 139     -10.993  -4.599  32.529  1.00 37.89      A    C  
ATOM   1044  O   LYS A 139     -11.045  -3.859  33.521  1.00 38.12      A    O  
ATOM   1045  CB  LYS A 139     -12.769  -6.193  31.947  1.00 38.94      A    C  
ATOM   1046  CG  LYS A 139     -12.941  -6.481  33.474  1.00 39.47      A    C  
ATOM   1047  CD  LYS A 139     -13.598  -7.854  33.754  1.00 39.00      A    C  
ATOM   1048  CE  LYS A 139     -13.880  -7.987  35.270  1.00 43.29      A    C  
ATOM   1049  NZ  LYS A 139     -13.838  -9.441  35.649  1.00 42.69      A    N1+
ATOM   1050  N   TYR A 140      -9.899  -5.266  32.169  1.00 37.46      A    N  
ATOM   1051  CA  TYR A 140      -8.629  -5.068  32.869  1.00 38.28      A    C  
ATOM   1052  C   TYR A 140      -8.183  -3.557  32.894  1.00 38.74      A    C  
ATOM   1053  O   TYR A 140      -8.047  -2.951  33.958  1.00 40.63      A    O  
ATOM   1054  CB  TYR A 140      -7.543  -5.981  32.222  1.00 38.09      A    C  
ATOM   1055  CG  TYR A 140      -6.159  -5.902  32.876  1.00 38.82      A    C  
ATOM   1056  CD1 TYR A 140      -5.870  -6.629  34.016  1.00 39.15      A    C  
ATOM   1057  CD2 TYR A 140      -5.134  -5.107  32.317  1.00 36.92      A    C  
ATOM   1058  CE1 TYR A 140      -4.609  -6.558  34.620  1.00 40.83      A    C  
ATOM   1059  CE2 TYR A 140      -3.890  -5.002  32.922  1.00 37.58      A    C  
ATOM   1060  CZ  TYR A 140      -3.626  -5.748  34.044  1.00 41.49      A    C  
ATOM   1061  OH  TYR A 140      -2.374  -5.678  34.596  1.00 42.64      A    O  
ATOM   1062  N   ILE A 141      -7.938  -2.959  31.730  1.00 38.66      A    N  
ATOM   1063  CA  ILE A 141      -7.501  -1.560  31.615  1.00 37.52      A    C  
ATOM   1064  C   ILE A 141      -8.366  -0.635  32.493  1.00 38.46      A    C  
ATOM   1065  O   ILE A 141      -7.865   0.149  33.325  1.00 36.49      A    O  
ATOM   1066  CB  ILE A 141      -7.549  -1.130  30.096  1.00 39.07      A    C  
ATOM   1067  CG1 ILE A 141      -6.446  -1.889  29.300  1.00 36.19      A    C  
ATOM   1068  CG2 ILE A 141      -7.448   0.362  29.903  1.00 39.25      A    C  
ATOM   1069  CD1 ILE A 141      -6.588  -1.762  27.785  1.00 37.09      A    C  
ATOM   1070  N   HIS A 142      -9.674  -0.737  32.317  1.00 35.94      A    N  
ATOM   1071  CA  HIS A 142     -10.625   0.054  33.043  1.00 37.61      A    C  
ATOM   1072  C   HIS A 142     -10.572  -0.168  34.555  1.00 39.77      A    C  
ATOM   1073  O   HIS A 142     -10.838   0.770  35.305  1.00 41.38      A    O  
ATOM   1074  CB  HIS A 142     -12.040  -0.250  32.538  1.00 37.39      A    C  
ATOM   1075  CG  HIS A 142     -12.329   0.321  31.184  1.00 36.56      A    C  
ATOM   1076  CD2 HIS A 142     -11.512   0.951  30.298  1.00 34.28      A    C  
ATOM   1077  ND1 HIS A 142     -13.579   0.258  30.586  1.00 37.27      A    N  
ATOM   1078  CE1 HIS A 142     -13.510   0.827  29.391  1.00 37.91      A    C  
ATOM   1079  NE2 HIS A 142     -12.280   1.305  29.217  1.00 36.38      A    N  
ATOM   1080  N   SER A 143     -10.229  -1.376  35.004  1.00 40.57      A    N  
ATOM   1081  CA  SER A 143     -10.187  -1.639  36.426  1.00 43.52      A    C  
ATOM   1082  C   SER A 143      -8.973  -0.960  37.094  1.00 44.88      A    C  
ATOM   1083  O   SER A 143      -8.958  -0.788  38.314  1.00 45.19      A    O  
ATOM   1084  CB  SER A 143     -10.168  -3.117  36.735  1.00 42.87      A    C  
ATOM   1085  OG  SER A 143      -8.923  -3.674  36.345  1.00 45.97      A    O  
ATOM   1086  N   ALA A 144      -7.984  -0.595  36.287  1.00 45.53      A    N  
ATOM   1087  CA  ALA A 144      -6.851   0.211  36.720  1.00 46.70      A    C  
ATOM   1088  C   ALA A 144      -7.115   1.737  36.679  1.00 46.79      A    C  
ATOM   1089  O   ALA A 144      -6.204   2.512  36.944  1.00 47.10      A    O  
ATOM   1090  CB  ALA A 144      -5.623  -0.135  35.846  1.00 47.44      A    C  
ATOM   1091  N   ASP A 145      -8.344   2.147  36.348  1.00 46.87      A    N  
ATOM   1092  CA  ASP A 145      -8.739   3.539  36.138  1.00 47.57      A    C  
ATOM   1093  C   ASP A 145      -7.982   4.153  34.976  1.00 46.96      A    C  
ATOM   1094  O   ASP A 145      -7.628   5.326  35.016  1.00 47.55      A    O  
ATOM   1095  CB  ASP A 145      -8.571   4.410  37.410  1.00 49.49      A    C  
ATOM   1096  CG  ASP A 145      -9.817   4.420  38.293  1.00 55.92      A    C  
ATOM   1097  OD1 ASP A 145      -9.703   4.834  39.487  1.00 61.10      A    O  
ATOM   1098  OD2 ASP A 145     -10.910   3.997  37.805  1.00 60.11      A    O1-
ATOM   1099  N   ILE A 146      -7.730   3.348  33.948  1.00 44.49      A    N  
ATOM   1100  CA  ILE A 146      -7.165   3.822  32.689  1.00 43.71      A    C  
ATOM   1101  C   ILE A 146      -8.270   3.867  31.626  1.00 43.66      A    C  
ATOM   1102  O   ILE A 146      -9.105   2.963  31.539  1.00 43.53      A    O  
ATOM   1103  CB  ILE A 146      -6.003   2.962  32.270  1.00 43.33      A    C  
ATOM   1104  CG1 ILE A 146      -4.871   3.148  33.266  1.00 44.90      A    C  
ATOM   1105  CG2 ILE A 146      -5.453   3.360  30.885  1.00 43.06      A    C  
ATOM   1106  CD1 ILE A 146      -3.898   1.994  33.333  1.00 47.12      A    C  
ATOM   1107  N   ILE A 147      -8.334   4.954  30.874  1.00 43.50      A    N  
ATOM   1108  CA  ILE A 147      -9.217   5.024  29.732  1.00 43.98      A    C  
ATOM   1109  C   ILE A 147      -8.331   5.009  28.500  1.00 44.12      A    C  
ATOM   1110  O   ILE A 147      -7.451   5.857  28.386  1.00 44.13      A    O  
ATOM   1111  CB  ILE A 147     -10.069   6.274  29.779  1.00 43.38      A    C  
ATOM   1112  CG1 ILE A 147     -10.864   6.281  31.089  1.00 45.51      A    C  
ATOM   1113  CG2 ILE A 147     -11.044   6.340  28.587  1.00 44.92      A    C  
ATOM   1114  CD1 ILE A 147     -11.445   7.621  31.438  1.00 49.75      A    C  
ATOM   1115  N   HIS A 148      -8.570   4.066  27.578  1.00 42.75      A    N  
ATOM   1116  CA  HIS A 148      -7.872   4.053  26.290  1.00 43.54      A    C  
ATOM   1117  C   HIS A 148      -8.045   5.362  25.491  1.00 43.81      A    C  
ATOM   1118  O   HIS A 148      -7.074   6.039  25.241  1.00 43.09      A    O  
ATOM   1119  CB  HIS A 148      -8.256   2.825  25.425  1.00 42.32      A    C  
ATOM   1120  CG  HIS A 148      -7.280   2.560  24.328  1.00 44.26      A    C  
ATOM   1121  CD2 HIS A 148      -6.362   1.582  24.163  1.00 47.23      A    C  
ATOM   1122  ND1 HIS A 148      -7.132   3.408  23.256  1.00 42.41      A    N  
ATOM   1123  CE1 HIS A 148      -6.168   2.962  22.474  1.00 45.96      A    C  
ATOM   1124  NE2 HIS A 148      -5.684   1.856  23.004  1.00 46.54      A    N  
ATOM   1125  N   ARG A 149      -9.273   5.674  25.065  1.00 43.94      A    N  
ATOM   1126  CA  ARG A 149      -9.633   6.958  24.443  1.00 46.74      A    C  
ATOM   1127  C   ARG A 149      -9.508   7.000  22.965  1.00 46.71      A    C  
ATOM   1128  O   ARG A 149      -9.930   7.966  22.338  1.00 48.03      A    O  
ATOM   1129  CB  ARG A 149      -8.772   8.111  24.952  1.00 46.82      A    C  
ATOM   1130  CG  ARG A 149      -9.226   8.649  26.233  1.00 51.35      A    C  
ATOM   1131  CD  ARG A 149      -8.360   9.826  26.683  1.00 54.28      A    C  
ATOM   1132  NE  ARG A 149      -8.727  10.163  28.053  1.00 58.88      A    N  
ATOM   1133  CZ  ARG A 149      -8.178   9.629  29.145  1.00 61.44      A    C  
ATOM   1134  NH1 ARG A 149      -7.195   8.725  29.058  1.00 61.60      A    N1+
ATOM   1135  NH2 ARG A 149      -8.623  10.013  30.338  1.00 62.82      A    N  
ATOM   1136  N   ASP A 150      -8.848   6.010  22.404  1.00 47.08      A    N  
ATOM   1137  CA  ASP A 150      -8.630   6.036  20.988  1.00 47.35      A    C  
ATOM   1138  C   ASP A 150      -8.577   4.624  20.410  1.00 45.79      A    C  
ATOM   1139  O   ASP A 150      -7.732   4.315  19.541  1.00 44.60      A    O  
ATOM   1140  CB  ASP A 150      -7.351   6.840  20.698  1.00 48.52      A    C  
ATOM   1141  CG  ASP A 150      -7.183   7.156  19.206  1.00 52.31      A    C  
ATOM   1142  OD1 ASP A 150      -8.188   7.475  18.504  1.00 54.18      A    O  
ATOM   1143  OD2 ASP A 150      -6.032   7.050  18.738  1.00 58.19      A    O1-
ATOM   1144  N   LEU A 151      -9.483   3.773  20.879  1.00 42.93      A    N  
ATOM   1145  CA  LEU A 151      -9.578   2.408  20.373  1.00 43.39      A    C  
ATOM   1146  C   LEU A 151     -10.075   2.438  18.932  1.00 42.89      A    C  
ATOM   1147  O   LEU A 151     -11.055   3.120  18.610  1.00 43.08      A    O  
ATOM   1148  CB  LEU A 151     -10.567   1.567  21.196  1.00 43.63      A    C  
ATOM   1149  CG  LEU A 151     -10.186   0.617  22.333  1.00 48.15      A    C  
ATOM   1150  CD1 LEU A 151     -11.412  -0.301  22.566  1.00 47.72      A    C  
ATOM   1151  CD2 LEU A 151      -8.912  -0.227  22.108  1.00 45.37      A    C  
ATOM   1152  N   LYS A 152      -9.415   1.680  18.068  1.00 42.82      A    N  
ATOM   1153  CA  LYS A 152      -9.767   1.646  16.695  1.00 43.83      A    C  
ATOM   1154  C   LYS A 152      -9.128   0.395  16.124  1.00 43.30      A    C  
ATOM   1155  O   LYS A 152      -8.212  -0.116  16.716  1.00 42.06      A    O  
ATOM   1156  CB  LYS A 152      -9.279   2.949  16.015  1.00 44.10      A    C  
ATOM   1157  CG  LYS A 152      -7.773   3.220  16.092  1.00 46.27      A    C  
ATOM   1158  CD  LYS A 152      -7.525   4.720  15.684  1.00 46.28      A    C  
ATOM   1159  CE  LYS A 152      -6.052   5.101  15.754  1.00 52.94      A    C  
ATOM   1160  NZ  LYS A 152      -5.878   6.618  15.993  1.00 51.33      A    N1+
ATOM   1161  N   PRO A 153      -9.637  -0.125  14.987  1.00 44.35      A    N  
ATOM   1162  CA  PRO A 153      -9.096  -1.380  14.446  1.00 45.57      A    C  
ATOM   1163  C   PRO A 153      -7.560  -1.441  14.304  1.00 47.29      A    C  
ATOM   1164  O   PRO A 153      -7.000  -2.525  14.465  1.00 48.37      A    O  
ATOM   1165  CB  PRO A 153      -9.791  -1.486  13.079  1.00 46.25      A    C  
ATOM   1166  CG  PRO A 153     -11.143  -0.897  13.349  1.00 43.79      A    C  
ATOM   1167  CD  PRO A 153     -10.770   0.352  14.170  1.00 43.99      A    C  
ATOM   1168  N   SER A 154      -6.896  -0.305  14.090  1.00 47.56      A    N  
ATOM   1169  CA  SER A 154      -5.442  -0.269  13.934  1.00 49.36      A    C  
ATOM   1170  C   SER A 154      -4.642  -0.345  15.260  1.00 49.69      A    C  
ATOM   1171  O   SER A 154      -3.415  -0.539  15.235  1.00 50.58      A    O  
ATOM   1172  CB  SER A 154      -5.021   0.954  13.094  1.00 50.15      A    C  
ATOM   1173  OG  SER A 154      -5.254   2.170  13.798  1.00 51.57      A    O  
ATOM   1174  N   ASN A 155      -5.335  -0.230  16.404  1.00 48.68      A    N  
ATOM   1175  CA  ASN A 155      -4.733  -0.392  17.742  1.00 48.13      A    C  
ATOM   1176  C   ASN A 155      -5.000  -1.753  18.306  1.00 47.43      A    C  
ATOM   1177  O   ASN A 155      -4.737  -1.993  19.464  1.00 47.10      A    O  
ATOM   1178  CB  ASN A 155      -5.285   0.656  18.727  1.00 49.04      A    C  
ATOM   1179  CG  ASN A 155      -4.768   2.006  18.441  1.00 52.99      A    C  
ATOM   1180  ND2 ASN A 155      -5.482   3.027  18.867  1.00 53.86      A    N  
ATOM   1181  OD1 ASN A 155      -3.728   2.143  17.786  1.00 60.89      A    O  
ATOM   1182  N   LEU A 156      -5.568  -2.633  17.492  1.00 46.22      A    N  
ATOM   1183  CA  LEU A 156      -5.935  -3.949  17.930  1.00 46.09      A    C  
ATOM   1184  C   LEU A 156      -5.173  -4.957  17.076  1.00 47.51      A    C  
ATOM   1185  O   LEU A 156      -5.378  -5.055  15.865  1.00 48.24      A    O  
ATOM   1186  CB  LEU A 156      -7.431  -4.159  17.798  1.00 44.89      A    C  
ATOM   1187  CG  LEU A 156      -8.350  -3.270  18.634  1.00 45.18      A    C  
ATOM   1188  CD1 LEU A 156      -9.780  -3.571  18.278  1.00 42.46      A    C  
ATOM   1189  CD2 LEU A 156      -8.110  -3.505  20.136  1.00 41.03      A    C  
ATOM   1190  N   ALA A 157      -4.279  -5.684  17.706  1.00 48.03      A    N  
ATOM   1191  CA  ALA A 157      -3.393  -6.569  16.988  1.00 49.82      A    C  
ATOM   1192  C   ALA A 157      -3.836  -8.000  17.200  1.00 51.11      A    C  
ATOM   1193  O   ALA A 157      -4.412  -8.327  18.225  1.00 49.61      A    O  
ATOM   1194  CB  ALA A 157      -1.987  -6.380  17.501  1.00 49.63      A    C  
ATOM   1195  N   VAL A 158      -3.548  -8.862  16.229  1.00 54.16      A    N  
ATOM   1196  CA  VAL A 158      -3.933 -10.280  16.305  1.00 57.05      A    C  
ATOM   1197  C   VAL A 158      -2.779 -11.174  15.792  1.00 58.73      A    C  
ATOM   1198  O   VAL A 158      -2.099 -10.811  14.855  1.00 58.39      A    O  
ATOM   1199  CB  VAL A 158      -5.228 -10.564  15.488  1.00 57.61      A    C  
ATOM   1200  CG1 VAL A 158      -6.486 -10.065  16.207  1.00 58.48      A    C  
ATOM   1201  CG2 VAL A 158      -5.142  -9.964  14.090  1.00 58.79      A    C  
ATOM   1202  N   ASN A 159      -2.545 -12.316  16.428  1.00 61.52      A    N  
ATOM   1203  CA  ASN A 159      -1.576 -13.277  15.895  1.00 64.41      A    C  
ATOM   1204  C   ASN A 159      -2.237 -14.213  14.887  1.00 66.73      A    C  
ATOM   1205  O   ASN A 159      -3.324 -13.914  14.357  1.00 67.18      A    O  
ATOM   1206  CB  ASN A 159      -0.904 -14.067  17.015  1.00 64.23      A    C  
ATOM   1207  CG  ASN A 159      -1.866 -15.014  17.744  1.00 64.39      A    C  
ATOM   1208  ND2 ASN A 159      -1.431 -15.506  18.895  1.00 61.90      A    N  
ATOM   1209  OD1 ASN A 159      -2.968 -15.312  17.265  1.00 61.95      A    O  
ATOM   1210  N   GLU A 160      -1.581 -15.345  14.621  1.00 68.93      A    N  
ATOM   1211  CA  GLU A 160      -2.114 -16.360  13.717  1.00 70.59      A    C  
ATOM   1212  C   GLU A 160      -3.460 -16.849  14.220  1.00 70.61      A    C  
ATOM   1213  O   GLU A 160      -4.487 -16.622  13.568  1.00 70.69      A    O  
ATOM   1214  CB  GLU A 160      -1.123 -17.527  13.570  1.00 71.27      A    C  
ATOM   1215  CG  GLU A 160       0.067 -17.199  12.637  1.00 75.03      A    C  
ATOM   1216  CD  GLU A 160      -0.203 -17.500  11.143  1.00 78.93      A    C  
ATOM   1217  OE1 GLU A 160      -1.341 -17.282  10.651  1.00 79.65      A    O  
ATOM   1218  OE2 GLU A 160       0.746 -17.958  10.458  1.00 80.19      A    O1-
ATOM   1219  N   ASP A 161      -3.440 -17.476  15.399  1.00 70.49      A    N  
ATOM   1220  CA  ASP A 161      -4.627 -18.042  16.046  1.00 70.95      A    C  
ATOM   1221  C   ASP A 161      -5.661 -16.982  16.429  1.00 70.00      A    C  
ATOM   1222  O   ASP A 161      -6.597 -17.273  17.181  1.00 70.23      A    O  
ATOM   1223  CB  ASP A 161      -4.202 -18.861  17.282  1.00 71.59      A    C  
ATOM   1224  CG  ASP A 161      -3.092 -19.872  16.963  1.00 74.46      A    C  
ATOM   1225  OD1 ASP A 161      -2.665 -19.945  15.781  1.00 76.72      A    O  
ATOM   1226  OD2 ASP A 161      -2.642 -20.589  17.886  1.00 76.97      A    O1-
ATOM   1227  N   CYS A 162      -5.494 -15.784  15.851  1.00 69.00      A    N  
ATOM   1228  CA  CYS A 162      -6.242 -14.534  16.152  1.00 67.86      A    C  
ATOM   1229  C   CYS A 162      -6.520 -14.276  17.642  1.00 64.62      A    C  
ATOM   1230  O   CYS A 162      -7.618 -13.880  18.058  1.00 64.17      A    O  
ATOM   1231  CB  CYS A 162      -7.473 -14.321  15.234  1.00 68.35      A    C  
ATOM   1232  SG  CYS A 162      -8.387 -15.839  14.753  1.00 76.72      A    S  
ATOM   1233  N   GLU A 163      -5.494 -14.536  18.441  1.00 61.10      A    N  
ATOM   1234  CA  GLU A 163      -5.470 -14.063  19.796  1.00 57.63      A    C  
ATOM   1235  C   GLU A 163      -5.217 -12.553  19.676  1.00 53.58      A    C  
ATOM   1236  O   GLU A 163      -4.405 -12.118  18.873  1.00 52.65      A    O  
ATOM   1237  CB  GLU A 163      -4.406 -14.814  20.601  1.00 58.67      A    C  
ATOM   1238  CG  GLU A 163      -4.878 -16.239  21.035  1.00 62.79      A    C  
ATOM   1239  CD  GLU A 163      -3.737 -17.249  21.204  1.00 69.15      A    C  
ATOM   1240  OE1 GLU A 163      -2.566 -16.920  20.894  1.00 73.20      A    O  
ATOM   1241  OE2 GLU A 163      -4.006 -18.390  21.639  1.00 70.93      A    O1-
ATOM   1242  N   LEU A 164      -5.938 -11.771  20.460  1.00 49.17      A    N  
ATOM   1243  CA  LEU A 164      -6.008 -10.332  20.276  1.00 46.41      A    C  
ATOM   1244  C   LEU A 164      -5.316  -9.616  21.453  1.00 45.29      A    C  
ATOM   1245  O   LEU A 164      -5.462 -10.023  22.613  1.00 44.89      A    O  
ATOM   1246  CB  LEU A 164      -7.500  -9.901  20.145  1.00 44.51      A    C  
ATOM   1247  CG  LEU A 164      -7.758  -8.430  19.886  1.00 43.76      A    C  
ATOM   1248  CD1 LEU A 164      -8.896  -8.280  18.917  1.00 41.79      A    C  
ATOM   1249  CD2 LEU A 164      -7.994  -7.610  21.214  1.00 40.37      A    C  
ATOM   1250  N   LYS A 165      -4.551  -8.576  21.141  1.00 43.95      A    N  
ATOM   1251  CA  LYS A 165      -3.996  -7.683  22.156  1.00 42.86      A    C  
ATOM   1252  C   LYS A 165      -4.283  -6.218  21.809  1.00 42.50      A    C  
ATOM   1253  O   LYS A 165      -4.200  -5.835  20.654  1.00 41.36      A    O  
ATOM   1254  CB  LYS A 165      -2.489  -7.921  22.352  1.00 43.09      A    C  
ATOM   1255  CG  LYS A 165      -2.120  -9.326  22.824  1.00 43.01      A    C  
ATOM   1256  CD  LYS A 165      -0.681  -9.429  23.359  1.00 44.72      A    C  
ATOM   1257  CE  LYS A 165      -0.248 -10.899  23.402  1.00 47.55      A    C  
ATOM   1258  NZ  LYS A 165      -0.703 -11.623  24.646  1.00 51.27      A    N1+
ATOM   1259  N   ILE A 166      -4.630  -5.424  22.824  1.00 42.20      A    N  
ATOM   1260  CA  ILE A 166      -4.936  -4.020  22.696  1.00 42.10      A    C  
ATOM   1261  C   ILE A 166      -3.609  -3.280  22.786  1.00 44.14      A    C  
ATOM   1262  O   ILE A 166      -2.829  -3.484  23.736  1.00 42.05      A    O  
ATOM   1263  CB  ILE A 166      -5.843  -3.519  23.834  1.00 42.35      A    C  
ATOM   1264  CG1 ILE A 166      -7.231  -4.184  23.767  1.00 41.02      A    C  
ATOM   1265  CG2 ILE A 166      -5.955  -1.997  23.762  1.00 42.82      A    C  
ATOM   1266  CD1 ILE A 166      -8.177  -3.891  24.947  1.00 42.34      A    C  
ATOM   1267  N   LEU A 167      -3.374  -2.439  21.794  1.00 46.30      A    N  
ATOM   1268  CA  LEU A 167      -2.122  -1.707  21.628  1.00 52.12      A    C  
ATOM   1269  C   LEU A 167      -2.179  -0.193  21.896  1.00 55.00      A    C  
ATOM   1270  O   LEU A 167      -3.259   0.464  21.793  1.00 54.74      A    O  
ATOM   1271  CB  LEU A 167      -1.674  -1.832  20.174  1.00 52.84      A    C  
ATOM   1272  CG  LEU A 167      -1.190  -3.105  19.509  1.00 55.22      A    C  
ATOM   1273  CD1 LEU A 167      -1.156  -2.846  17.989  1.00 59.04      A    C  
ATOM   1274  CD2 LEU A 167       0.193  -3.477  20.036  1.00 59.54      A    C  
ATOM   1275  N   ASP A 168      -0.976   0.327  22.178  1.00 58.58      A    N  
ATOM   1276  CA  ASP A 168      -0.578   1.746  22.052  1.00 61.38      A    C  
ATOM   1277  C   ASP A 168      -1.699   2.759  22.284  1.00 62.33      A    C  
ATOM   1278  O   ASP A 168      -2.323   3.252  21.327  1.00 63.28      A    O  
ATOM   1279  CB  ASP A 168       0.237   1.961  20.745  1.00 62.38      A    C  
ATOM   1280  CG  ASP A 168      -0.131   3.257  19.992  1.00 64.78      A    C  
ATOM   1281  OD1 ASP A 168       0.549   4.296  20.208  1.00 66.82      A    O  
ATOM   1282  OD2 ASP A 168      -1.093   3.221  19.177  1.00 65.85      A    O1-
ATOM   1283  N   ARG A 186     -11.465   9.788  13.099  1.00 55.47      A    N  
ATOM   1284  CA  ARG A 186     -12.324   9.809  14.288  1.00 54.34      A    C  
ATOM   1285  C   ARG A 186     -13.605   8.981  14.159  1.00 52.23      A    C  
ATOM   1286  O   ARG A 186     -14.596   9.205  14.881  1.00 51.56      A    O  
ATOM   1287  CB  ARG A 186     -12.667  11.259  14.659  1.00 56.07      A    C  
ATOM   1288  CG  ARG A 186     -13.777  11.900  13.814  1.00 59.84      A    C  
ATOM   1289  CD  ARG A 186     -14.052  11.127  12.492  1.00 67.17      A    C  
ATOM   1290  NE  ARG A 186     -13.321  11.613  11.319  1.00 72.04      A    N  
ATOM   1291  CZ  ARG A 186     -13.831  12.476  10.443  1.00 73.19      A    C  
ATOM   1292  NH1 ARG A 186     -15.062  12.947  10.630  1.00 73.46      A    N1+
ATOM   1293  NH2 ARG A 186     -13.116  12.873   9.394  1.00 72.43      A    N  
ATOM   1294  N   TRP A 187     -13.578   8.003  13.266  1.00 49.42      A    N  
ATOM   1295  CA  TRP A 187     -14.738   7.165  13.011  1.00 47.43      A    C  
ATOM   1296  C   TRP A 187     -15.228   6.349  14.212  1.00 45.76      A    C  
ATOM   1297  O   TRP A 187     -16.409   5.951  14.278  1.00 44.94      A    O  
ATOM   1298  CB  TRP A 187     -14.440   6.252  11.821  1.00 48.97      A    C  
ATOM   1299  CG  TRP A 187     -14.295   7.040  10.530  1.00 51.33      A    C  
ATOM   1300  CD1 TRP A 187     -14.610   8.362  10.333  1.00 52.88      A    C  
ATOM   1301  CD2 TRP A 187     -13.842   6.547   9.269  1.00 53.01      A    C  
ATOM   1302  CE2 TRP A 187     -13.887   7.622   8.358  1.00 52.28      A    C  
ATOM   1303  CE3 TRP A 187     -13.372   5.305   8.822  1.00 55.13      A    C  
ATOM   1304  NE1 TRP A 187     -14.364   8.717   9.031  1.00 53.71      A    N  
ATOM   1305  CZ2 TRP A 187     -13.483   7.495   7.021  1.00 54.30      A    C  
ATOM   1306  CZ3 TRP A 187     -12.967   5.182   7.467  1.00 54.35      A    C  
ATOM   1307  CH2 TRP A 187     -13.030   6.265   6.598  1.00 53.45      A    C  
ATOM   1308  N   TYR A 188     -14.327   6.110  15.159  1.00 44.01      A    N  
ATOM   1309  CA  TYR A 188     -14.644   5.264  16.322  1.00 44.26      A    C  
ATOM   1310  C   TYR A 188     -14.769   5.996  17.670  1.00 45.22      A    C  
ATOM   1311  O   TYR A 188     -15.074   5.392  18.677  1.00 44.02      A    O  
ATOM   1312  CB  TYR A 188     -13.638   4.137  16.401  1.00 43.46      A    C  
ATOM   1313  CG  TYR A 188     -13.460   3.426  15.098  1.00 42.30      A    C  
ATOM   1314  CD1 TYR A 188     -14.224   2.329  14.775  1.00 43.90      A    C  
ATOM   1315  CD2 TYR A 188     -12.498   3.866  14.179  1.00 43.10      A    C  
ATOM   1316  CE1 TYR A 188     -14.087   1.689  13.538  1.00 42.04      A    C  
ATOM   1317  CE2 TYR A 188     -12.325   3.228  12.964  1.00 44.20      A    C  
ATOM   1318  CZ  TYR A 188     -13.102   2.122  12.662  1.00 43.17      A    C  
ATOM   1319  OH  TYR A 188     -12.902   1.486  11.455  1.00 44.33      A    O  
ATOM   1320  N   ARG A 189     -14.570   7.308  17.679  1.00 47.96      A    N  
ATOM   1321  CA  ARG A 189     -14.536   8.075  18.929  1.00 50.50      A    C  
ATOM   1322  C   ARG A 189     -15.944   8.449  19.392  1.00 50.33      A    C  
ATOM   1323  O   ARG A 189     -16.789   8.803  18.579  1.00 50.53      A    O  
ATOM   1324  CB  ARG A 189     -13.691   9.348  18.758  1.00 51.47      A    C  
ATOM   1325  CG  ARG A 189     -12.208   9.178  19.114  1.00 55.54      A    C  
ATOM   1326  CD  ARG A 189     -11.524  10.520  19.477  1.00 55.86      A    C  
ATOM   1327  NE  ARG A 189     -11.172  11.264  18.266  1.00 66.83      A    N  
ATOM   1328  CZ  ARG A 189      -9.993  11.184  17.633  1.00 70.03      A    C  
ATOM   1329  NH1 ARG A 189      -9.020  10.398  18.106  1.00 72.33      A    N1+
ATOM   1330  NH2 ARG A 189      -9.775  11.898  16.525  1.00 69.92      A    N  
ATOM   1331  N   ALA A 190     -16.171   8.404  20.707  1.00 50.10      A    N  
ATOM   1332  CA  ALA A 190     -17.474   8.688  21.310  1.00 49.36      A    C  
ATOM   1333  C   ALA A 190     -17.978  10.102  20.990  1.00 49.77      A    C  
ATOM   1334  O   ALA A 190     -17.179  11.019  20.846  1.00 50.15      A    O  
ATOM   1335  CB  ALA A 190     -17.390   8.453  22.798  1.00 48.64      A    C  
ATOM   1336  N   PRO A 191     -19.294  10.277  20.808  1.00 50.25      A    N  
ATOM   1337  CA  PRO A 191     -19.770  11.599  20.396  1.00 51.28      A    C  
ATOM   1338  C   PRO A 191     -19.597  12.659  21.455  1.00 52.71      A    C  
ATOM   1339  O   PRO A 191     -19.429  13.842  21.097  1.00 52.65      A    O  
ATOM   1340  CB  PRO A 191     -21.251  11.380  20.115  1.00 51.17      A    C  
ATOM   1341  CG  PRO A 191     -21.600  10.142  20.863  1.00 50.54      A    C  
ATOM   1342  CD  PRO A 191     -20.390   9.297  20.846  1.00 50.13      A    C  
ATOM   1343  N   GLU A 192     -19.572  12.248  22.727  1.00 53.68      A    N  
ATOM   1344  CA  GLU A 192     -19.418  13.219  23.819  1.00 54.43      A    C  
ATOM   1345  C   GLU A 192     -18.142  13.989  23.597  1.00 55.33      A    C  
ATOM   1346  O   GLU A 192     -18.129  15.204  23.759  1.00 54.35      A    O  
ATOM   1347  CB  GLU A 192     -19.531  12.623  25.235  1.00 54.17      A    C  
ATOM   1348  CG  GLU A 192     -18.617  11.462  25.595  1.00 52.17      A    C  
ATOM   1349  CD  GLU A 192     -19.209  10.094  25.242  1.00 49.75      A    C  
ATOM   1350  OE1 GLU A 192     -20.037   9.990  24.299  1.00 47.54      A    O  
ATOM   1351  OE2 GLU A 192     -18.816   9.120  25.906  1.00 47.08      A    O1-
ATOM   1352  N   ILE A 193     -17.107  13.290  23.121  1.00 56.49      A    N  
ATOM   1353  CA  ILE A 193     -15.878  13.952  22.696  1.00 57.16      A    C  
ATOM   1354  C   ILE A 193     -16.015  14.873  21.455  1.00 58.23      A    C  
ATOM   1355  O   ILE A 193     -15.450  15.957  21.416  1.00 57.90      A    O  
ATOM   1356  CB  ILE A 193     -14.705  12.960  22.456  1.00 56.43      A    C  
ATOM   1357  CG1 ILE A 193     -14.652  11.922  23.565  1.00 54.54      A    C  
ATOM   1358  CG2 ILE A 193     -13.392  13.739  22.406  1.00 54.83      A    C  
ATOM   1359  CD1 ILE A 193     -13.792  10.715  23.195  1.00 52.64      A    C  
ATOM   1360  N   MET A 194     -16.741  14.444  20.435  1.00 59.84      A    N  
ATOM   1361  CA  MET A 194     -16.865  15.309  19.256  1.00 61.20      A    C  
ATOM   1362  C   MET A 194     -17.825  16.493  19.426  1.00 62.21      A    C  
ATOM   1363  O   MET A 194     -17.723  17.520  18.741  1.00 61.95      A    O  
ATOM   1364  CB  MET A 194     -17.208  14.480  18.051  1.00 61.70      A    C  
ATOM   1365  CG  MET A 194     -15.999  13.692  17.597  1.00 62.29      A    C  
ATOM   1366  SD  MET A 194     -16.637  12.887  16.190  1.00 58.89      A    S  
ATOM   1367  CE  MET A 194     -17.704  11.675  16.985  1.00 59.26      A    C  
ATOM   1368  N   LEU A 195     -18.764  16.332  20.337  1.00 63.59      A    N  
ATOM   1369  CA  LEU A 195     -19.444  17.477  20.859  1.00 65.83      A    C  
ATOM   1370  C   LEU A 195     -18.394  17.980  21.861  1.00 67.28      A    C  
ATOM   1371  O   LEU A 195     -17.369  17.335  22.054  1.00 68.34      A    O  
ATOM   1372  CB  LEU A 195     -20.757  17.034  21.494  1.00 65.62      A    C  
ATOM   1373  CG  LEU A 195     -21.919  16.813  20.501  1.00 66.32      A    C  
ATOM   1374  CD1 LEU A 195     -22.854  15.633  20.877  1.00 66.39      A    C  
ATOM   1375  CD2 LEU A 195     -22.727  18.098  20.312  1.00 67.46      A    C  
ATOM   1376  N   ASN A 196     -18.564  19.125  22.485  1.00 68.36      A    N  
ATOM   1377  CA  ASN A 196     -17.546  19.441  23.483  1.00 69.53      A    C  
ATOM   1378  C   ASN A 196     -18.180  19.262  24.855  1.00 69.76      A    C  
ATOM   1379  O   ASN A 196     -18.382  20.229  25.575  1.00 69.12      A    O  
ATOM   1380  CB  ASN A 196     -16.979  20.857  23.257  1.00 69.50      A    C  
ATOM   1381  CG  ASN A 196     -15.688  21.125  24.026  1.00 69.26      A    C  
ATOM   1382  ND2 ASN A 196     -15.555  22.359  24.492  1.00 71.11      A    N  
ATOM   1383  OD1 ASN A 196     -14.818  20.256  24.185  1.00 67.75      A    O  
ATOM   1384  N   TRP A 197     -18.554  18.019  25.174  1.00 70.68      A    N  
ATOM   1385  CA  TRP A 197     -19.034  17.685  26.525  1.00 72.02      A    C  
ATOM   1386  C   TRP A 197     -17.821  17.124  27.243  1.00 73.06      A    C  
ATOM   1387  O   TRP A 197     -16.861  16.718  26.576  1.00 74.14      A    O  
ATOM   1388  CB  TRP A 197     -20.195  16.672  26.515  1.00 70.83      A    C  
ATOM   1389  CG  TRP A 197     -21.325  16.972  25.527  1.00 70.15      A    C  
ATOM   1390  CD1 TRP A 197     -21.493  18.111  24.787  1.00 68.77      A    C  
ATOM   1391  CD2 TRP A 197     -22.441  16.117  25.202  1.00 69.12      A    C  
ATOM   1392  CE2 TRP A 197     -23.225  16.799  24.252  1.00 69.31      A    C  
ATOM   1393  CE3 TRP A 197     -22.839  14.831  25.609  1.00 69.55      A    C  
ATOM   1394  NE1 TRP A 197     -22.628  18.013  24.024  1.00 69.56      A    N  
ATOM   1395  CZ2 TRP A 197     -24.409  16.244  23.705  1.00 70.61      A    C  
ATOM   1396  CZ3 TRP A 197     -24.014  14.281  25.061  1.00 69.31      A    C  
ATOM   1397  CH2 TRP A 197     -24.783  14.991  24.125  1.00 68.84      A    C  
ATOM   1398  N   MET A 198     -17.833  17.132  28.577  1.00 74.25      A    N  
ATOM   1399  CA  MET A 198     -16.688  16.607  29.343  1.00 74.48      A    C  
ATOM   1400  C   MET A 198     -17.064  15.710  30.530  1.00 74.02      A    C  
ATOM   1401  O   MET A 198     -16.226  15.408  31.387  1.00 73.94      A    O  
ATOM   1402  CB  MET A 198     -15.707  17.729  29.711  1.00 75.01      A    C  
ATOM   1403  CG  MET A 198     -14.799  18.164  28.529  1.00 75.35      A    C  
ATOM   1404  SD  MET A 198     -14.513  19.954  28.395  1.00 76.31      A    S  
ATOM   1405  CE  MET A 198     -13.163  20.015  27.192  1.00 76.64      A    C  
ATOM   1406  N   HIS A 199     -18.333  15.292  30.558  1.00 73.32      A    N  
ATOM   1407  CA  HIS A 199     -18.793  14.103  31.308  1.00 72.63      A    C  
ATOM   1408  C   HIS A 199     -18.200  12.835  30.643  1.00 72.08      A    C  
ATOM   1409  O   HIS A 199     -18.934  12.151  29.894  1.00 72.28      A    O  
ATOM   1410  CB  HIS A 199     -20.333  13.954  31.222  1.00 73.05      A    C  
ATOM   1411  CG  HIS A 199     -21.122  14.826  32.156  1.00 74.03      A    C  
ATOM   1412  CD2 HIS A 199     -22.023  14.507  33.119  1.00 75.16      A    C  
ATOM   1413  ND1 HIS A 199     -21.105  16.206  32.091  1.00 76.06      A    N  
ATOM   1414  CE1 HIS A 199     -21.934  16.698  33.001  1.00 76.62      A    C  
ATOM   1415  NE2 HIS A 199     -22.506  15.689  33.637  1.00 75.36      A    N  
ATOM   1416  N   TYR A 200     -16.905  12.552  30.873  1.00 70.77      A    N  
ATOM   1417  CA  TYR A 200     -16.194  11.388  30.254  1.00 69.96      A    C  
ATOM   1418  C   TYR A 200     -16.130  10.133  31.118  1.00 67.13      A    C  
ATOM   1419  O   TYR A 200     -15.386  10.099  32.097  1.00 68.09      A    O  
ATOM   1420  CB  TYR A 200     -14.728  11.720  29.908  1.00 70.57      A    C  
ATOM   1421  CG  TYR A 200     -14.515  12.651  28.734  1.00 72.02      A    C  
ATOM   1422  CD1 TYR A 200     -15.491  12.804  27.732  1.00 73.33      A    C  
ATOM   1423  CD2 TYR A 200     -13.319  13.359  28.603  1.00 73.42      A    C  
ATOM   1424  CE1 TYR A 200     -15.290  13.672  26.653  1.00 73.42      A    C  
ATOM   1425  CE2 TYR A 200     -13.104  14.224  27.526  1.00 73.18      A    C  
ATOM   1426  CZ  TYR A 200     -14.089  14.369  26.562  1.00 72.49      A    C  
ATOM   1427  OH  TYR A 200     -13.869  15.215  25.509  1.00 73.00      A    O  
ATOM   1428  N   ASN A 201     -16.867   9.098  30.732  1.00 62.68      A    N  
ATOM   1429  CA  ASN A 201     -16.718   7.788  31.316  1.00 58.45      A    C  
ATOM   1430  C   ASN A 201     -15.589   6.973  30.635  1.00 54.74      A    C  
ATOM   1431  O   ASN A 201     -15.149   7.260  29.525  1.00 53.15      A    O  
ATOM   1432  CB  ASN A 201     -18.020   6.989  31.101  1.00 60.30      A    C  
ATOM   1433  CG  ASN A 201     -19.109   7.370  32.047  1.00 61.81      A    C  
ATOM   1434  ND2 ASN A 201     -19.596   8.608  31.933  1.00 63.41      A    N  
ATOM   1435  OD1 ASN A 201     -19.524   6.559  32.883  1.00 64.12      A    O  
ATOM   1436  N   GLN A 202     -15.164   5.931  31.311  1.00 50.21      A    N  
ATOM   1437  CA  GLN A 202     -14.413   4.864  30.684  1.00 48.44      A    C  
ATOM   1438  C   GLN A 202     -15.244   4.246  29.532  1.00 46.68      A    C  
ATOM   1439  O   GLN A 202     -14.697   3.626  28.660  1.00 44.72      A    O  
ATOM   1440  CB  GLN A 202     -14.119   3.804  31.715  1.00 47.13      A    C  
ATOM   1441  CG  GLN A 202     -13.445   4.373  32.950  1.00 51.11      A    C  
ATOM   1442  CD  GLN A 202     -13.034   3.291  33.843  1.00 52.62      A    C  
ATOM   1443  NE2 GLN A 202     -11.695   3.167  34.089  1.00 49.64      A    N  
ATOM   1444  OE1 GLN A 202     -13.889   2.499  34.263  1.00 49.63      A    O  
ATOM   1445  N   THR A 203     -16.568   4.401  29.571  1.00 45.81      A    N  
ATOM   1446  CA  THR A 203     -17.410   3.908  28.469  1.00 45.53      A    C  
ATOM   1447  C   THR A 203     -17.261   4.665  27.159  1.00 43.74      A    C  
ATOM   1448  O   THR A 203     -17.933   4.322  26.196  1.00 43.58      A    O  
ATOM   1449  CB  THR A 203     -18.919   3.909  28.795  1.00 44.39      A    C  
ATOM   1450  CG2 THR A 203     -19.235   2.953  29.962  1.00 45.62      A    C  
ATOM   1451  OG1 THR A 203     -19.347   5.253  29.053  1.00 48.89      A    O  
ATOM   1452  N   VAL A 204     -16.420   5.702  27.086  1.00 41.44      A    N  
ATOM   1453  CA  VAL A 204     -16.025   6.166  25.767  1.00 38.55      A    C  
ATOM   1454  C   VAL A 204     -15.409   5.010  24.966  1.00 36.98      A    C  
ATOM   1455  O   VAL A 204     -15.617   4.933  23.748  1.00 35.83      A    O  
ATOM   1456  CB  VAL A 204     -14.978   7.306  25.777  1.00 39.75      A    C  
ATOM   1457  CG1 VAL A 204     -15.565   8.567  26.320  1.00 38.98      A    C  
ATOM   1458  CG2 VAL A 204     -13.779   6.847  26.554  1.00 39.23      A    C  
ATOM   1459  N   ASP A 205     -14.663   4.130  25.628  1.00 34.66      A    N  
ATOM   1460  CA  ASP A 205     -14.048   2.994  24.944  1.00 36.54      A    C  
ATOM   1461  C   ASP A 205     -15.119   1.963  24.491  1.00 36.73      A    C  
ATOM   1462  O   ASP A 205     -14.899   1.229  23.548  1.00 36.77      A    O  
ATOM   1463  CB  ASP A 205     -12.997   2.295  25.806  1.00 35.91      A    C  
ATOM   1464  CG  ASP A 205     -11.785   3.189  26.119  1.00 38.82      A    C  
ATOM   1465  OD1 ASP A 205     -11.537   4.123  25.323  1.00 35.35      A    O  
ATOM   1466  OD2 ASP A 205     -11.087   2.909  27.115  1.00 37.32      A    O1-
ATOM   1467  N   ILE A 206     -16.239   1.893  25.197  1.00 37.11      A    N  
ATOM   1468  CA  ILE A 206     -17.324   0.944  24.876  1.00 37.02      A    C  
ATOM   1469  C   ILE A 206     -18.060   1.378  23.628  1.00 36.83      A    C  
ATOM   1470  O   ILE A 206     -18.440   0.529  22.818  1.00 38.23      A    O  
ATOM   1471  CB  ILE A 206     -18.344   0.820  26.037  1.00 37.41      A    C  
ATOM   1472  CG1 ILE A 206     -17.715   0.104  27.241  1.00 36.06      A    C  
ATOM   1473  CG2 ILE A 206     -19.566   0.010  25.601  1.00 37.38      A    C  
ATOM   1474  CD1 ILE A 206     -17.243  -1.340  26.989  1.00 41.54      A    C  
ATOM   1475  N   TRP A 207     -18.250   2.689  23.451  1.00 37.15      A    N  
ATOM   1476  CA  TRP A 207     -18.630   3.254  22.138  1.00 36.52      A    C  
ATOM   1477  C   TRP A 207     -17.721   2.789  21.015  1.00 36.09      A    C  
ATOM   1478  O   TRP A 207     -18.214   2.318  20.000  1.00 35.61      A    O  
ATOM   1479  CB  TRP A 207     -18.629   4.783  22.127  1.00 37.70      A    C  
ATOM   1480  CG  TRP A 207     -19.227   5.340  20.838  1.00 35.41      A    C  
ATOM   1481  CD1 TRP A 207     -18.560   5.620  19.676  1.00 35.99      A    C  
ATOM   1482  CD2 TRP A 207     -20.620   5.625  20.573  1.00 35.56      A    C  
ATOM   1483  CE2 TRP A 207     -20.715   6.074  19.238  1.00 36.94      A    C  
ATOM   1484  CE3 TRP A 207     -21.779   5.547  21.335  1.00 35.41      A    C  
ATOM   1485  NE1 TRP A 207     -19.451   6.086  18.710  1.00 34.88      A    N  
ATOM   1486  CZ2 TRP A 207     -21.913   6.473  18.669  1.00 38.22      A    C  
ATOM   1487  CZ3 TRP A 207     -22.993   5.957  20.745  1.00 38.70      A    C  
ATOM   1488  CH2 TRP A 207     -23.042   6.392  19.437  1.00 37.48      A    C  
ATOM   1489  N   SER A 208     -16.405   2.941  21.165  1.00 36.50      A    N  
ATOM   1490  CA  SER A 208     -15.473   2.499  20.122  1.00 35.68      A    C  
ATOM   1491  C   SER A 208     -15.609   0.998  19.824  1.00 36.98      A    C  
ATOM   1492  O   SER A 208     -15.570   0.591  18.671  1.00 36.99      A    O  
ATOM   1493  CB  SER A 208     -14.045   2.850  20.527  1.00 36.58      A    C  
ATOM   1494  OG  SER A 208     -13.961   4.225  20.936  1.00 36.52      A    O  
ATOM   1495  N   VAL A 209     -15.741   0.159  20.845  1.00 35.81      A    N  
ATOM   1496  CA  VAL A 209     -15.954  -1.258  20.605  1.00 37.12      A    C  
ATOM   1497  C   VAL A 209     -17.239  -1.504  19.795  1.00 37.52      A    C  
ATOM   1498  O   VAL A 209     -17.253  -2.377  18.939  1.00 37.89      A    O  
ATOM   1499  CB  VAL A 209     -16.032  -2.083  21.901  1.00 36.21      A    C  
ATOM   1500  CG1 VAL A 209     -16.263  -3.622  21.604  1.00 38.20      A    C  
ATOM   1501  CG2 VAL A 209     -14.765  -1.902  22.711  1.00 36.83      A    C  
ATOM   1502  N   GLY A 210     -18.296  -0.767  20.104  1.00 37.05      A    N  
ATOM   1503  CA  GLY A 210     -19.569  -0.870  19.393  1.00 38.06      A    C  
ATOM   1504  C   GLY A 210     -19.340  -0.556  17.905  1.00 37.61      A    C  
ATOM   1505  O   GLY A 210     -19.823  -1.259  17.023  1.00 37.52      A    O  
ATOM   1506  N   CYS A 211     -18.565   0.469  17.611  1.00 36.71      A    N  
ATOM   1507  CA  CYS A 211     -18.361   0.808  16.197  1.00 36.69      A    C  
ATOM   1508  C   CYS A 211     -17.543  -0.276  15.472  1.00 37.12      A    C  
ATOM   1509  O   CYS A 211     -17.739  -0.502  14.262  1.00 36.09      A    O  
ATOM   1510  CB  CYS A 211     -17.601   2.117  16.114  1.00 37.53      A    C  
ATOM   1511  SG  CYS A 211     -18.557   3.542  16.591  1.00 40.49      A    S  
ATOM   1512  N   ILE A 212     -16.531  -0.815  16.175  1.00 36.14      A    N  
ATOM   1513  CA  ILE A 212     -15.652  -1.883  15.619  1.00 36.90      A    C  
ATOM   1514  C   ILE A 212     -16.481  -3.151  15.365  1.00 38.30      A    C  
ATOM   1515  O   ILE A 212     -16.437  -3.767  14.291  1.00 38.35      A    O  
ATOM   1516  CB  ILE A 212     -14.508  -2.174  16.594  1.00 36.07      A    C  
ATOM   1517  CG1 ILE A 212     -13.581  -0.956  16.652  1.00 36.08      A    C  
ATOM   1518  CG2 ILE A 212     -13.592  -3.327  16.081  1.00 38.31      A    C  
ATOM   1519  CD1 ILE A 212     -12.663  -1.006  17.864  1.00 39.56      A    C  
ATOM   1520  N   MET A 213     -17.250  -3.542  16.354  1.00 39.62      A    N  
ATOM   1521  CA  MET A 213     -18.072  -4.728  16.215  1.00 41.77      A    C  
ATOM   1522  C   MET A 213     -18.995  -4.616  14.994  1.00 43.01      A    C  
ATOM   1523  O   MET A 213     -19.188  -5.598  14.258  1.00 43.51      A    O  
ATOM   1524  CB  MET A 213     -18.937  -4.909  17.452  1.00 41.47      A    C  
ATOM   1525  CG  MET A 213     -19.812  -6.174  17.403  1.00 40.71      A    C  
ATOM   1526  SD  MET A 213     -20.512  -6.456  19.003  1.00 44.03      A    S  
ATOM   1527  CE  MET A 213     -22.107  -7.234  18.710  1.00 43.75      A    C  
ATOM   1528  N   ALA A 214     -19.610  -3.448  14.821  1.00 42.86      A    N  
ATOM   1529  CA  ALA A 214     -20.526  -3.209  13.704  1.00 44.57      A    C  
ATOM   1530  C   ALA A 214     -19.798  -3.350  12.380  1.00 44.81      A    C  
ATOM   1531  O   ALA A 214     -20.333  -3.906  11.434  1.00 45.35      A    O  
ATOM   1532  CB  ALA A 214     -21.151  -1.800  13.830  1.00 44.40      A    C  
ATOM   1533  N   GLU A 215     -18.556  -2.877  12.325  1.00 45.42      A    N  
ATOM   1534  CA  GLU A 215     -17.770  -2.967  11.119  1.00 46.86      A    C  
ATOM   1535  C   GLU A 215     -17.404  -4.428  10.837  1.00 47.40      A    C  
ATOM   1536  O   GLU A 215     -17.388  -4.846   9.684  1.00 47.87      A    O  
ATOM   1537  CB  GLU A 215     -16.507  -2.154  11.267  1.00 47.47      A    C  
ATOM   1538  CG  GLU A 215     -15.720  -2.019   9.992  1.00 50.74      A    C  
ATOM   1539  CD  GLU A 215     -14.665  -0.960  10.100  1.00 54.96      A    C  
ATOM   1540  OE1 GLU A 215     -14.848  -0.008  10.916  1.00 57.25      A    O  
ATOM   1541  OE2 GLU A 215     -13.677  -1.047   9.340  1.00 57.09      A    O1-
ATOM   1542  N   LEU A 216     -17.101  -5.187  11.876  1.00 47.92      A    N  
ATOM   1543  CA  LEU A 216     -16.796  -6.617  11.747  1.00 48.75      A    C  
ATOM   1544  C   LEU A 216     -18.014  -7.362  11.291  1.00 49.69      A    C  
ATOM   1545  O   LEU A 216     -17.912  -8.298  10.531  1.00 50.66      A    O  
ATOM   1546  CB  LEU A 216     -16.402  -7.203  13.084  1.00 47.69      A    C  
ATOM   1547  CG  LEU A 216     -15.057  -6.805  13.669  1.00 47.31      A    C  
ATOM   1548  CD1 LEU A 216     -14.807  -7.707  14.860  1.00 43.96      A    C  
ATOM   1549  CD2 LEU A 216     -13.966  -6.896  12.623  1.00 46.10      A    C  
ATOM   1550  N   LEU A 217     -19.182  -6.940  11.742  1.00 50.86      A    N  
ATOM   1551  CA  LEU A 217     -20.395  -7.640  11.366  1.00 51.85      A    C  
ATOM   1552  C   LEU A 217     -20.856  -7.379   9.928  1.00 53.08      A    C  
ATOM   1553  O   LEU A 217     -21.361  -8.291   9.292  1.00 54.38      A    O  
ATOM   1554  CB  LEU A 217     -21.526  -7.404  12.364  1.00 51.11      A    C  
ATOM   1555  CG  LEU A 217     -21.374  -8.181  13.669  1.00 51.18      A    C  
ATOM   1556  CD1 LEU A 217     -22.320  -7.677  14.740  1.00 54.01      A    C  
ATOM   1557  CD2 LEU A 217     -21.525  -9.685  13.460  1.00 53.95      A    C  
ATOM   1558  N   THR A 218     -20.655  -6.169   9.412  1.00 53.76      A    N  
ATOM   1559  CA  THR A 218     -21.225  -5.767   8.144  1.00 55.02      A    C  
ATOM   1560  C   THR A 218     -20.191  -5.453   7.073  1.00 55.56      A    C  
ATOM   1561  O   THR A 218     -20.556  -5.227   5.918  1.00 57.28      A    O  
ATOM   1562  CB  THR A 218     -22.098  -4.484   8.289  1.00 55.10      A    C  
ATOM   1563  CG2 THR A 218     -23.098  -4.590   9.450  1.00 55.33      A    C  
ATOM   1564  OG1 THR A 218     -21.238  -3.362   8.470  1.00 54.35      A    O  
ATOM   1565  N   GLY A 219     -18.914  -5.412   7.422  1.00 55.25      A    N  
ATOM   1566  CA  GLY A 219     -17.874  -5.090   6.435  1.00 54.93      A    C  
ATOM   1567  C   GLY A 219     -17.673  -3.602   6.155  1.00 55.71      A    C  
ATOM   1568  O   GLY A 219     -16.697  -3.214   5.482  1.00 56.13      A    O  
ATOM   1569  N   ARG A 220     -18.574  -2.753   6.648  1.00 54.18      A    N  
ATOM   1570  CA  ARG A 220     -18.434  -1.323   6.383  1.00 54.49      A    C  
ATOM   1571  C   ARG A 220     -18.305  -0.474   7.659  1.00 52.42      A    C  
ATOM   1572  O   ARG A 220     -18.800  -0.856   8.688  1.00 50.36      A    O  
ATOM   1573  CB  ARG A 220     -19.540  -0.785   5.442  1.00 55.26      A    C  
ATOM   1574  CG  ARG A 220     -20.983  -0.972   5.883  1.00 57.04      A    C  
ATOM   1575  CD  ARG A 220     -21.965  -0.418   4.792  1.00 57.82      A    C  
ATOM   1576  NE  ARG A 220     -22.113  -1.300   3.605  1.00 65.02      A    N  
ATOM   1577  CZ  ARG A 220     -21.761  -0.993   2.338  1.00 67.04      A    C  
ATOM   1578  NH1 ARG A 220     -21.232   0.177   2.026  1.00 67.53      A    N1+
ATOM   1579  NH2 ARG A 220     -21.947  -1.867   1.357  1.00 68.14      A    N  
ATOM   1580  N   THR A 221     -17.619   0.662   7.563  1.00 51.48      A    N  
ATOM   1581  CA  THR A 221     -17.452   1.565   8.691  1.00 50.48      A    C  
ATOM   1582  C   THR A 221     -18.857   2.042   9.055  1.00 49.84      A    C  
ATOM   1583  O   THR A 221     -19.665   2.415   8.176  1.00 49.51      A    O  
ATOM   1584  CB  THR A 221     -16.556   2.773   8.319  1.00 52.10      A    C  
ATOM   1585  CG2 THR A 221     -16.171   3.570   9.558  1.00 49.78      A    C  
ATOM   1586  OG1 THR A 221     -15.358   2.326   7.648  1.00 52.79      A    O  
ATOM   1587  N   LEU A 222     -19.182   1.973  10.339  1.00 48.62      A    N  
ATOM   1588  CA  LEU A 222     -20.509   2.366  10.802  1.00 48.10      A    C  
ATOM   1589  C   LEU A 222     -20.765   3.876  10.641  1.00 48.23      A    C  
ATOM   1590  O   LEU A 222     -21.828   4.287  10.179  1.00 49.04      A    O  
ATOM   1591  CB  LEU A 222     -20.733   1.895  12.237  1.00 47.49      A    C  
ATOM   1592  CG  LEU A 222     -22.069   2.185  12.881  1.00 47.46      A    C  
ATOM   1593  CD1 LEU A 222     -23.294   1.662  12.054  1.00 50.19      A    C  
ATOM   1594  CD2 LEU A 222     -22.077   1.627  14.301  1.00 46.51      A    C  
ATOM   1595  N   PHE A 223     -19.792   4.708  10.987  1.00 48.63      A    N  
ATOM   1596  CA  PHE A 223     -20.009   6.146  10.905  1.00 49.02      A    C  
ATOM   1597  C   PHE A 223     -18.876   6.852  10.156  1.00 50.24      A    C  
ATOM   1598  O   PHE A 223     -18.004   7.452  10.784  1.00 51.22      A    O  
ATOM   1599  CB  PHE A 223     -20.127   6.746  12.308  1.00 48.53      A    C  
ATOM   1600  CG  PHE A 223     -21.247   6.184  13.132  1.00 45.49      A    C  
ATOM   1601  CD1 PHE A 223     -22.536   6.276  12.709  1.00 43.51      A    C  
ATOM   1602  CD2 PHE A 223     -20.992   5.634  14.373  1.00 44.91      A    C  
ATOM   1603  CE1 PHE A 223     -23.581   5.775  13.492  1.00 45.63      A    C  
ATOM   1604  CE2 PHE A 223     -22.018   5.157  15.161  1.00 43.92      A    C  
ATOM   1605  CZ  PHE A 223     -23.311   5.230  14.714  1.00 44.53      A    C  
ATOM   1606  N   PRO A 224     -18.873   6.766   8.811  1.00 51.54      A    N  
ATOM   1607  CA  PRO A 224     -17.733   7.280   8.020  1.00 52.35      A    C  
ATOM   1608  C   PRO A 224     -17.715   8.812   7.779  1.00 53.70      A    C  
ATOM   1609  O   PRO A 224     -17.680   9.255   6.646  1.00 53.89      A    O  
ATOM   1610  CB  PRO A 224     -17.837   6.490   6.701  1.00 52.54      A    C  
ATOM   1611  CG  PRO A 224     -19.280   6.075   6.582  1.00 52.38      A    C  
ATOM   1612  CD  PRO A 224     -19.900   6.108   7.979  1.00 50.46      A    C  
ATOM   1613  N   GLY A 225     -17.706   9.613   8.841  1.00 54.69      A    N  
ATOM   1614  CA  GLY A 225     -17.842  11.061   8.702  1.00 56.27      A    C  
ATOM   1615  C   GLY A 225     -16.686  11.761   8.001  1.00 57.44      A    C  
ATOM   1616  O   GLY A 225     -15.522  11.343   8.129  1.00 57.77      A    O  
ATOM   1617  N   THR A 226     -16.998  12.832   7.270  1.00 58.25      A    N  
ATOM   1618  CA  THR A 226     -15.963  13.601   6.551  1.00 59.34      A    C  
ATOM   1619  C   THR A 226     -15.282  14.609   7.473  1.00 60.03      A    C  
ATOM   1620  O   THR A 226     -14.062  14.840   7.376  1.00 61.45      A    O  
ATOM   1621  CB  THR A 226     -16.526  14.283   5.298  1.00 59.52      A    C  
ATOM   1622  CG2 THR A 226     -16.976  13.232   4.292  1.00 60.11      A    C  
ATOM   1623  OG1 THR A 226     -17.666  15.085   5.660  1.00 61.19      A    O  
ATOM   1624  N   ASP A 227     -16.076  15.222   8.351  1.00 60.04      A    N  
ATOM   1625  CA  ASP A 227     -15.595  16.106   9.419  1.00 58.81      A    C  
ATOM   1626  C   ASP A 227     -16.382  15.757  10.672  1.00 57.64      A    C  
ATOM   1627  O   ASP A 227     -17.197  14.867  10.630  1.00 56.82      A    O  
ATOM   1628  CB  ASP A 227     -15.718  17.591   9.046  1.00 59.84      A    C  
ATOM   1629  CG  ASP A 227     -17.098  17.970   8.495  1.00 61.86      A    C  
ATOM   1630  OD1 ASP A 227     -18.116  17.606   9.103  1.00 61.93      A    O  
ATOM   1631  OD2 ASP A 227     -17.155  18.669   7.452  1.00 66.30      A    O1-
ATOM   1632  N   HIS A 228     -16.139  16.438  11.787  1.00 57.07      A    N  
ATOM   1633  CA  HIS A 228     -16.828  16.064  13.023  1.00 56.65      A    C  
ATOM   1634  C   HIS A 228     -18.328  16.322  12.969  1.00 55.17      A    C  
ATOM   1635  O   HIS A 228     -19.096  15.656  13.649  1.00 55.26      A    O  
ATOM   1636  CB  HIS A 228     -16.200  16.739  14.219  1.00 56.93      A    C  
ATOM   1637  CG  HIS A 228     -14.780  16.323  14.463  1.00 61.34      A    C  
ATOM   1638  CD2 HIS A 228     -13.802  15.925  13.608  1.00 64.34      A    C  
ATOM   1639  ND1 HIS A 228     -14.226  16.283  15.725  1.00 64.00      A    N  
ATOM   1640  CE1 HIS A 228     -12.965  15.889  15.636  1.00 66.02      A    C  
ATOM   1641  NE2 HIS A 228     -12.686  15.657  14.365  1.00 67.29      A    N  
ATOM   1642  N   ILE A 229     -18.746  17.272  12.138  1.00 53.52      A    N  
ATOM   1643  CA  ILE A 229     -20.169  17.583  12.018  1.00 52.29      A    C  
ATOM   1644  C   ILE A 229     -20.917  16.535  11.253  1.00 50.61      A    C  
ATOM   1645  O   ILE A 229     -21.961  16.071  11.690  1.00 49.17      A    O  
ATOM   1646  CB  ILE A 229     -20.415  18.982  11.395  1.00 52.85      A    C  
ATOM   1647  CG1 ILE A 229     -19.970  20.038  12.381  1.00 52.54      A    C  
ATOM   1648  CG2 ILE A 229     -21.899  19.170  11.047  1.00 52.21      A    C  
ATOM   1649  CD1 ILE A 229     -20.410  19.702  13.782  1.00 59.13      A    C  
ATOM   1650  N   ASP A 230     -20.370  16.176  10.103  1.00 50.06      A    N  
ATOM   1651  CA  ASP A 230     -20.888  15.072   9.308  1.00 50.50      A    C  
ATOM   1652  C   ASP A 230     -21.001  13.839  10.223  1.00 49.79      A    C  
ATOM   1653  O   ASP A 230     -22.044  13.210  10.329  1.00 49.66      A    O  
ATOM   1654  CB  ASP A 230     -19.940  14.816   8.111  1.00 50.66      A    C  
ATOM   1655  CG  ASP A 230     -20.482  13.794   7.135  1.00 53.44      A    C  
ATOM   1656  OD1 ASP A 230     -21.727  13.736   6.928  1.00 56.16      A    O  
ATOM   1657  OD2 ASP A 230     -19.661  13.036   6.577  1.00 55.34      A    O1-
ATOM   1658  N   GLN A 231     -19.934  13.560  10.954  1.00 49.44      A    N  
ATOM   1659  CA  GLN A 231     -19.906  12.398  11.841  1.00 48.40      A    C  
ATOM   1660  C   GLN A 231     -21.050  12.413  12.866  1.00 47.44      A    C  
ATOM   1661  O   GLN A 231     -21.776  11.431  13.027  1.00 46.05      A    O  
ATOM   1662  CB  GLN A 231     -18.582  12.390  12.578  1.00 48.67      A    C  
ATOM   1663  CG  GLN A 231     -18.464  11.243  13.526  1.00 49.41      A    C  
ATOM   1664  CD  GLN A 231     -17.890  10.058  12.871  1.00 50.01      A    C  
ATOM   1665  NE2 GLN A 231     -18.163   8.909  13.419  1.00 50.37      A    N  
ATOM   1666  OE1 GLN A 231     -17.154  10.172  11.891  1.00 56.46      A    O  
ATOM   1667  N   LEU A 232     -21.223  13.531  13.564  1.00 46.85      A    N  
ATOM   1668  CA  LEU A 232     -22.306  13.602  14.559  1.00 47.07      A    C  
ATOM   1669  C   LEU A 232     -23.719  13.393  13.945  1.00 46.88      A    C  
ATOM   1670  O   LEU A 232     -24.626  12.785  14.543  1.00 45.45      A    O  
ATOM   1671  CB  LEU A 232     -22.190  14.934  15.308  1.00 47.57      A    C  
ATOM   1672  CG  LEU A 232     -22.642  14.999  16.770  1.00 52.12      A    C  
ATOM   1673  CD1 LEU A 232     -23.170  16.392  17.126  1.00 53.95      A    C  
ATOM   1674  CD2 LEU A 232     -23.704  13.991  17.071  1.00 53.42      A    C  
ATOM   1675  N   LYS A 233     -23.902  13.925  12.744  1.00 47.71      A    N  
ATOM   1676  CA  LYS A 233     -25.148  13.754  11.983  1.00 49.52      A    C  
ATOM   1677  C   LYS A 233     -25.456  12.290  11.738  1.00 47.75      A    C  
ATOM   1678  O   LYS A 233     -26.576  11.845  11.952  1.00 47.90      A    O  
ATOM   1679  CB  LYS A 233     -25.000  14.459  10.651  1.00 49.56      A    C  
ATOM   1680  CG  LYS A 233     -26.266  15.082  10.085  1.00 55.15      A    C  
ATOM   1681  CD  LYS A 233     -25.922  15.958   8.855  1.00 53.72      A    C  
ATOM   1682  CE  LYS A 233     -24.924  17.078   9.241  1.00 58.51      A    C  
ATOM   1683  NZ  LYS A 233     -24.575  17.994   8.089  1.00 59.12      A    N1+
ATOM   1684  N   LEU A 234     -24.455  11.534  11.283  1.00 47.24      A    N  
ATOM   1685  CA  LEU A 234     -24.615  10.076  11.063  1.00 46.22      A    C  
ATOM   1686  C   LEU A 234     -24.907   9.382  12.376  1.00 45.79      A    C  
ATOM   1687  O   LEU A 234     -25.792   8.516  12.458  1.00 45.51      A    O  
ATOM   1688  CB  LEU A 234     -23.341   9.485  10.484  1.00 46.29      A    C  
ATOM   1689  CG  LEU A 234     -22.997  10.064   9.118  1.00 47.42      A    C  
ATOM   1690  CD1 LEU A 234     -21.553   9.767   8.781  1.00 47.16      A    C  
ATOM   1691  CD2 LEU A 234     -23.994   9.470   8.064  1.00 46.98      A    C  
ATOM   1692  N   ILE A 235     -24.178   9.761  13.427  1.00 43.71      A    N  
ATOM   1693  CA  ILE A 235     -24.439   9.151  14.715  1.00 42.35      A    C  
ATOM   1694  C   ILE A 235     -25.883   9.405  15.123  1.00 43.81      A    C  
ATOM   1695  O   ILE A 235     -26.612   8.487  15.494  1.00 42.06      A    O  
ATOM   1696  CB  ILE A 235     -23.450   9.636  15.799  1.00 42.45      A    C  
ATOM   1697  CG1 ILE A 235     -22.040   9.038  15.506  1.00 39.29      A    C  
ATOM   1698  CG2 ILE A 235     -23.936   9.200  17.163  1.00 40.77      A    C  
ATOM   1699  CD1 ILE A 235     -20.887   9.650  16.358  1.00 40.26      A    C  
ATOM   1700  N   LEU A 236     -26.306  10.660  15.061  1.00 45.55      A    N  
ATOM   1701  CA  LEU A 236     -27.631  10.977  15.600  1.00 48.19      A    C  
ATOM   1702  C   LEU A 236     -28.746  10.329  14.777  1.00 50.05      A    C  
ATOM   1703  O   LEU A 236     -29.780   9.941  15.314  1.00 50.53      A    O  
ATOM   1704  CB  LEU A 236     -27.825  12.495  15.738  1.00 48.11      A    C  
ATOM   1705  CG  LEU A 236     -26.950  13.166  16.826  1.00 47.56      A    C  
ATOM   1706  CD1 LEU A 236     -27.394  14.602  16.994  1.00 51.52      A    C  
ATOM   1707  CD2 LEU A 236     -27.084  12.450  18.134  1.00 42.27      A    C  
ATOM   1708  N   ARG A 237     -28.506  10.202  13.481  1.00 52.13      A    N  
ATOM   1709  CA  ARG A 237     -29.450   9.537  12.609  1.00 54.76      A    C  
ATOM   1710  C   ARG A 237     -29.751   8.137  13.160  1.00 54.56      A    C  
ATOM   1711  O   ARG A 237     -30.909   7.771  13.308  1.00 55.56      A    O  
ATOM   1712  CB  ARG A 237     -28.906   9.522  11.183  1.00 55.84      A    C  
ATOM   1713  CG  ARG A 237     -29.747   8.728  10.200  1.00 60.40      A    C  
ATOM   1714  CD  ARG A 237     -29.718   9.364   8.827  1.00 66.56      A    C  
ATOM   1715  NE  ARG A 237     -30.690   8.690   7.971  1.00 71.41      A    N  
ATOM   1716  CZ  ARG A 237     -30.380   7.752   7.084  1.00 72.38      A    C  
ATOM   1717  NH1 ARG A 237     -29.113   7.374   6.909  1.00 71.66      A    N1+
ATOM   1718  NH2 ARG A 237     -31.346   7.194   6.375  1.00 73.22      A    N  
ATOM   1719  N   LEU A 238     -28.724   7.390  13.559  1.00 54.17      A    N  
ATOM   1720  CA  LEU A 238     -28.923   6.045  14.121  1.00 53.57      A    C  
ATOM   1721  C   LEU A 238     -29.469   5.982  15.557  1.00 53.85      A    C  
ATOM   1722  O   LEU A 238     -30.374   5.185  15.836  1.00 54.93      A    O  
ATOM   1723  CB  LEU A 238     -27.627   5.230  14.041  1.00 53.89      A    C  
ATOM   1724  CG  LEU A 238     -27.675   3.770  14.509  1.00 54.80      A    C  
ATOM   1725  CD1 LEU A 238     -28.365   2.895  13.454  1.00 55.12      A    C  
ATOM   1726  CD2 LEU A 238     -26.255   3.313  14.760  1.00 55.03      A    C  
ATOM   1727  N   VAL A 239     -28.908   6.776  16.473  1.00 53.27      A    N  
ATOM   1728  CA  VAL A 239     -29.181   6.571  17.903  1.00 52.79      A    C  
ATOM   1729  C   VAL A 239     -30.317   7.454  18.439  1.00 53.60      A    C  
ATOM   1730  O   VAL A 239     -30.817   7.225  19.550  1.00 54.36      A    O  
ATOM   1731  CB  VAL A 239     -27.904   6.709  18.796  1.00 51.77      A    C  
ATOM   1732  CG1 VAL A 239     -26.810   5.743  18.340  1.00 51.61      A    C  
ATOM   1733  CG2 VAL A 239     -27.372   8.149  18.796  1.00 49.57      A    C  
ATOM   1734  N   GLY A 240     -30.716   8.442  17.651  1.00 53.94      A    N  
ATOM   1735  CA  GLY A 240     -31.707   9.425  18.083  1.00 55.28      A    C  
ATOM   1736  C   GLY A 240     -31.042  10.721  18.543  1.00 55.72      A    C  
ATOM   1737  O   GLY A 240     -29.889  10.724  18.976  1.00 54.47      A    O  
ATOM   1738  N   THR A 241     -31.763  11.827  18.415  1.00 56.70      A    N  
ATOM   1739  CA  THR A 241     -31.352  13.083  19.022  1.00 58.16      A    C  
ATOM   1740  C   THR A 241     -31.486  12.931  20.547  1.00 58.48      A    C  
ATOM   1741  O   THR A 241     -32.286  12.118  21.029  1.00 59.10      A    O  
ATOM   1742  CB  THR A 241     -32.169  14.308  18.470  1.00 58.97      A    C  
ATOM   1743  CG2 THR A 241     -31.566  14.833  17.165  1.00 58.61      A    C  
ATOM   1744  OG1 THR A 241     -33.527  13.915  18.233  1.00 58.91      A    O  
ATOM   1745  N   PRO A 242     -30.642  13.641  21.319  1.00 59.03      A    N  
ATOM   1746  CA  PRO A 242     -30.680  13.459  22.772  1.00 59.64      A    C  
ATOM   1747  C   PRO A 242     -32.088  13.624  23.357  1.00 60.18      A    C  
ATOM   1748  O   PRO A 242     -32.834  14.512  22.939  1.00 60.65      A    O  
ATOM   1749  CB  PRO A 242     -29.761  14.562  23.298  1.00 59.47      A    C  
ATOM   1750  CG  PRO A 242     -28.872  14.918  22.170  1.00 59.67      A    C  
ATOM   1751  CD  PRO A 242     -29.594  14.586  20.893  1.00 59.26      A    C  
ATOM   1752  N   GLY A 243     -32.444  12.747  24.291  1.00 61.05      A    N  
ATOM   1753  CA  GLY A 243     -33.685  12.858  25.050  1.00 62.26      A    C  
ATOM   1754  C   GLY A 243     -33.543  13.889  26.165  1.00 63.02      A    C  
ATOM   1755  O   GLY A 243     -32.424  14.233  26.567  1.00 62.91      A    O  
ATOM   1756  N   ALA A 244     -34.674  14.380  26.675  1.00 63.34      A    N  
ATOM   1757  CA  ALA A 244     -34.660  15.401  27.711  1.00 63.06      A    C  
ATOM   1758  C   ALA A 244     -33.791  14.987  28.904  1.00 62.59      A    C  
ATOM   1759  O   ALA A 244     -33.065  15.828  29.449  1.00 62.72      A    O  
ATOM   1760  CB  ALA A 244     -36.080  15.757  28.143  1.00 63.96      A    C  
ATOM   1761  N   GLU A 245     -33.810  13.697  29.250  1.00 61.13      A    N  
ATOM   1762  CA  GLU A 245     -33.010  13.164  30.355  1.00 60.28      A    C  
ATOM   1763  C   GLU A 245     -31.507  13.378  30.201  1.00 58.54      A    C  
ATOM   1764  O   GLU A 245     -30.833  13.681  31.172  1.00 58.58      A    O  
ATOM   1765  CB  GLU A 245     -33.272  11.674  30.583  1.00 61.35      A    C  
ATOM   1766  CG  GLU A 245     -32.088  10.958  31.285  1.00 65.81      A    C  
ATOM   1767  CD  GLU A 245     -32.484   9.922  32.346  1.00 71.79      A    C  
ATOM   1768  OE1 GLU A 245     -33.574   9.311  32.239  1.00 75.15      A    O  
ATOM   1769  OE2 GLU A 245     -31.685   9.710  33.297  1.00 73.71      A    O1-
ATOM   1770  N   LEU A 246     -30.988  13.190  28.996  1.00 56.47      A    N  
ATOM   1771  CA  LEU A 246     -29.594  13.482  28.705  1.00 54.22      A    C  
ATOM   1772  C   LEU A 246     -29.435  15.007  28.593  1.00 53.52      A    C  
ATOM   1773  O   LEU A 246     -28.438  15.568  28.998  1.00 50.82      A    O  
ATOM   1774  CB  LEU A 246     -29.133  12.774  27.420  1.00 53.86      A    C  
ATOM   1775  CG  LEU A 246     -27.777  13.162  26.811  1.00 53.86      A    C  
ATOM   1776  CD1 LEU A 246     -26.642  12.950  27.843  1.00 51.47      A    C  
ATOM   1777  CD2 LEU A 246     -27.491  12.425  25.509  1.00 52.90      A    C  
ATOM   1778  N   LEU A 247     -30.443  15.676  28.047  1.00 53.79      A    N  
ATOM   1779  CA  LEU A 247     -30.375  17.120  27.916  1.00 53.71      A    C  
ATOM   1780  C   LEU A 247     -30.258  17.803  29.283  1.00 53.02      A    C  
ATOM   1781  O   LEU A 247     -29.675  18.866  29.385  1.00 53.58      A    O  
ATOM   1782  CB  LEU A 247     -31.553  17.650  27.093  1.00 54.92      A    C  
ATOM   1783  CG  LEU A 247     -31.200  18.432  25.815  1.00 55.10      A    C  
ATOM   1784  CD1 LEU A 247     -30.146  17.745  24.994  1.00 57.42      A    C  
ATOM   1785  CD2 LEU A 247     -32.435  18.613  24.984  1.00 56.83      A    C  
ATOM   1786  N   LYS A 248     -30.749  17.161  30.333  1.00 52.11      A    N  
ATOM   1787  CA  LYS A 248     -30.631  17.698  31.688  1.00 52.00      A    C  
ATOM   1788  C   LYS A 248     -29.194  17.659  32.202  1.00 51.06      A    C  
ATOM   1789  O   LYS A 248     -28.909  18.188  33.271  1.00 49.98      A    O  
ATOM   1790  CB  LYS A 248     -31.517  16.939  32.668  1.00 51.58      A    C  
ATOM   1791  CG  LYS A 248     -33.013  17.150  32.470  1.00 55.91      A    C  
ATOM   1792  CD  LYS A 248     -33.757  16.451  33.591  1.00 62.05      A    C  
ATOM   1793  CE  LYS A 248     -35.276  16.635  33.464  1.00 64.42      A    C  
ATOM   1794  NZ  LYS A 248     -35.975  15.972  34.614  1.00 65.42      A    N1+
ATOM   1795  N   LYS A 249     -28.302  17.038  31.432  1.00 49.91      A    N  
ATOM   1796  CA  LYS A 249     -26.906  16.867  31.822  1.00 49.90      A    C  
ATOM   1797  C   LYS A 249     -25.958  17.811  31.083  1.00 49.75      A    C  
ATOM   1798  O   LYS A 249     -24.763  17.813  31.320  1.00 49.23      A    O  
ATOM   1799  CB  LYS A 249     -26.475  15.428  31.569  1.00 50.76      A    C  
ATOM   1800  CG  LYS A 249     -27.263  14.410  32.396  1.00 51.45      A    C  
ATOM   1801  CD  LYS A 249     -26.666  13.033  32.304  1.00 54.78      A    C  
ATOM   1802  CE  LYS A 249     -27.646  12.027  32.909  1.00 57.35      A    C  
ATOM   1803  NZ  LYS A 249     -27.370  10.595  32.525  1.00 57.08      A    N1+
ATOM   1804  N   ILE A 250     -26.498  18.627  30.198  1.00 50.29      A    N  
ATOM   1805  CA  ILE A 250     -25.667  19.523  29.416  1.00 51.75      A    C  
ATOM   1806  C   ILE A 250     -25.664  20.924  30.049  1.00 53.80      A    C  
ATOM   1807  O   ILE A 250     -26.675  21.598  30.061  1.00 53.99      A    O  
ATOM   1808  CB  ILE A 250     -26.096  19.508  27.919  1.00 51.08      A    C  
ATOM   1809  CG1 ILE A 250     -25.765  18.149  27.288  1.00 51.29      A    C  
ATOM   1810  CG2 ILE A 250     -25.417  20.615  27.122  1.00 49.47      A    C  
ATOM   1811  CD1 ILE A 250     -26.556  17.925  26.026  1.00 55.83      A    C  
ATOM   1812  N   SER A 251     -24.504  21.347  30.545  1.00 56.58      A    N  
ATOM   1813  CA  SER A 251     -24.383  22.565  31.359  1.00 59.84      A    C  
ATOM   1814  C   SER A 251     -24.351  23.893  30.608  1.00 61.91      A    C  
ATOM   1815  O   SER A 251     -24.581  24.946  31.219  1.00 62.63      A    O  
ATOM   1816  CB  SER A 251     -23.111  22.498  32.192  1.00 59.94      A    C  
ATOM   1817  OG  SER A 251     -22.581  23.814  32.370  1.00 61.26      A    O  
ATOM   1818  N   SER A 252     -24.016  23.850  29.318  1.00 63.96      A    N  
ATOM   1819  CA  SER A 252     -23.818  25.039  28.488  1.00 65.39      A    C  
ATOM   1820  C   SER A 252     -25.093  25.419  27.769  1.00 65.94      A    C  
ATOM   1821  O   SER A 252     -25.764  24.561  27.225  1.00 66.46      A    O  
ATOM   1822  CB  SER A 252     -22.720  24.751  27.461  1.00 66.13      A    C  
ATOM   1823  OG  SER A 252     -22.761  25.668  26.364  1.00 67.85      A    O  
ATOM   1824  N   GLU A 253     -25.435  26.705  27.741  1.00 66.60      A    N  
ATOM   1825  CA  GLU A 253     -26.648  27.118  27.020  1.00 67.43      A    C  
ATOM   1826  C   GLU A 253     -26.553  26.967  25.490  1.00 66.25      A    C  
ATOM   1827  O   GLU A 253     -27.485  26.484  24.860  1.00 66.29      A    O  
ATOM   1828  CB  GLU A 253     -27.061  28.540  27.404  1.00 67.91      A    C  
ATOM   1829  CG  GLU A 253     -28.500  28.920  26.998  1.00 68.86      A    C  
ATOM   1830  CD  GLU A 253     -28.821  30.380  27.334  1.00 69.92      A    C  
ATOM   1831  OE1 GLU A 253     -27.891  31.103  27.767  1.00 71.48      A    O  
ATOM   1832  OE2 GLU A 253     -29.997  30.802  27.159  1.00 73.91      A    O1-
ATOM   1833  N   SER A 254     -25.424  27.381  24.911  1.00 65.72      A    N  
ATOM   1834  CA  SER A 254     -25.193  27.262  23.458  1.00 63.90      A    C  
ATOM   1835  C   SER A 254     -25.171  25.799  23.025  1.00 62.21      A    C  
ATOM   1836  O   SER A 254     -25.841  25.427  22.052  1.00 60.21      A    O  
ATOM   1837  CB  SER A 254     -23.892  27.953  23.049  1.00 64.85      A    C  
ATOM   1838  OG  SER A 254     -22.749  27.295  23.582  1.00 66.61      A    O  
ATOM   1839  N   ALA A 255     -24.410  24.982  23.767  1.00 60.31      A    N  
ATOM   1840  CA  ALA A 255     -24.375  23.521  23.577  1.00 59.05      A    C  
ATOM   1841  C   ALA A 255     -25.781  22.889  23.558  1.00 59.43      A    C  
ATOM   1842  O   ALA A 255     -26.090  22.063  22.692  1.00 57.35      A    O  
ATOM   1843  CB  ALA A 255     -23.511  22.861  24.648  1.00 58.13      A    C  
ATOM   1844  N   ARG A 256     -26.625  23.276  24.521  1.00 60.10      A    N  
ATOM   1845  CA  ARG A 256     -27.990  22.763  24.563  1.00 60.85      A    C  
ATOM   1846  C   ARG A 256     -28.702  23.334  23.358  1.00 61.73      A    C  
ATOM   1847  O   ARG A 256     -29.322  22.596  22.599  1.00 60.50      A    O  
ATOM   1848  CB  ARG A 256     -28.700  23.192  25.855  1.00 61.31      A    C  
ATOM   1849  CG  ARG A 256     -28.267  22.431  27.131  1.00 61.77      A    C  
ATOM   1850  CD  ARG A 256     -29.099  22.837  28.394  1.00 61.34      A    C  
ATOM   1851  NE  ARG A 256     -29.048  24.271  28.657  1.00 61.62      A    N  
ATOM   1852  CZ  ARG A 256     -28.168  24.881  29.456  1.00 62.98      A    C  
ATOM   1853  NH1 ARG A 256     -27.235  24.201  30.130  1.00 62.78      A    N1+
ATOM   1854  NH2 ARG A 256     -28.235  26.194  29.601  1.00 63.08      A    N  
ATOM   1855  N   ASN A 257     -28.556  24.654  23.165  1.00 63.14      A    N  
ATOM   1856  CA  ASN A 257     -29.136  25.340  22.005  1.00 65.25      A    C  
ATOM   1857  C   ASN A 257     -28.805  24.696  20.682  1.00 65.64      A    C  
ATOM   1858  O   ASN A 257     -29.681  24.616  19.832  1.00 65.05      A    O  
ATOM   1859  CB  ASN A 257     -28.743  26.824  21.965  1.00 65.84      A    C  
ATOM   1860  CG  ASN A 257     -29.733  27.705  22.696  1.00 68.92      A    C  
ATOM   1861  ND2 ASN A 257     -29.300  28.915  23.075  1.00 68.56      A    N  
ATOM   1862  OD1 ASN A 257     -30.884  27.299  22.926  1.00 73.75      A    O  
ATOM   1863  N   TYR A 258     -27.541  24.263  20.523  1.00 66.51      A    N  
ATOM   1864  CA  TYR A 258     -27.033  23.587  19.326  1.00 67.37      A    C  
ATOM   1865  C   TYR A 258     -27.752  22.275  19.103  1.00 68.38      A    C  
ATOM   1866  O   TYR A 258     -28.405  22.108  18.086  1.00 68.60      A    O  
ATOM   1867  CB  TYR A 258     -25.534  23.324  19.466  1.00 67.38      A    C  
ATOM   1868  CG  TYR A 258     -24.803  22.868  18.226  1.00 67.37      A    C  
ATOM   1869  CD1 TYR A 258     -24.798  23.638  17.071  1.00 68.50      A    C  
ATOM   1870  CD2 TYR A 258     -24.060  21.692  18.226  1.00 68.44      A    C  
ATOM   1871  CE1 TYR A 258     -24.094  23.237  15.930  1.00 68.46      A    C  
ATOM   1872  CE2 TYR A 258     -23.351  21.281  17.088  1.00 68.41      A    C  
ATOM   1873  CZ  TYR A 258     -23.370  22.068  15.949  1.00 68.86      A    C  
ATOM   1874  OH  TYR A 258     -22.676  21.688  14.816  1.00 68.88      A    O  
ATOM   1875  N   ILE A 259     -27.638  21.348  20.051  1.00 69.68      A    N  
ATOM   1876  CA  ILE A 259     -28.303  20.042  19.949  1.00 71.56      A    C  
ATOM   1877  C   ILE A 259     -29.807  20.139  19.649  1.00 72.74      A    C  
ATOM   1878  O   ILE A 259     -30.295  19.455  18.746  1.00 73.05      A    O  
ATOM   1879  CB  ILE A 259     -28.068  19.183  21.222  1.00 71.56      A    C  
ATOM   1880  CG1 ILE A 259     -26.745  18.435  21.123  1.00 72.18      A    C  
ATOM   1881  CG2 ILE A 259     -29.180  18.200  21.450  1.00 71.23      A    C  
ATOM   1882  CD1 ILE A 259     -25.688  19.054  22.001  1.00 75.56      A    C  
ATOM   1883  N   GLN A 260     -30.528  20.985  20.401  1.00 74.46      A    N  
ATOM   1884  CA  GLN A 260     -31.984  21.146  20.212  1.00 75.95      A    C  
ATOM   1885  C   GLN A 260     -32.351  21.974  18.962  1.00 77.03      A    C  
ATOM   1886  O   GLN A 260     -33.528  22.076  18.605  1.00 77.17      A    O  
ATOM   1887  CB  GLN A 260     -32.698  21.652  21.492  1.00 75.78      A    C  
ATOM   1888  CG  GLN A 260     -32.165  22.962  22.062  1.00 76.10      A    C  
ATOM   1889  CD  GLN A 260     -33.046  23.596  23.137  1.00 76.14      A    C  
ATOM   1890  NE2 GLN A 260     -33.357  24.889  22.957  1.00 74.35      A    N  
ATOM   1891  OE1 GLN A 260     -33.407  22.957  24.130  1.00 75.39      A    O  
ATOM   1892  N   SER A 261     -31.342  22.541  18.296  1.00 78.37      A    N  
ATOM   1893  CA  SER A 261     -31.522  23.201  16.989  1.00 79.49      A    C  
ATOM   1894  C   SER A 261     -31.486  22.193  15.848  1.00 80.45      A    C  
ATOM   1895  O   SER A 261     -32.124  22.397  14.804  1.00 80.82      A    O  
ATOM   1896  CB  SER A 261     -30.426  24.239  16.730  1.00 79.53      A    C  
ATOM   1897  OG  SER A 261     -29.232  23.621  16.258  1.00 79.60      A    O  
ATOM   1898  N   LEU A 262     -30.714  21.125  16.030  1.00 81.06      A    N  
ATOM   1899  CA  LEU A 262     -30.597  20.124  14.989  1.00 82.07      A    C  
ATOM   1900  C   LEU A 262     -31.958  19.482  14.731  1.00 82.92      A    C  
ATOM   1901  O   LEU A 262     -32.785  19.351  15.652  1.00 83.20      A    O  
ATOM   1902  CB  LEU A 262     -29.531  19.082  15.332  1.00 81.84      A    C  
ATOM   1903  CG  LEU A 262     -28.112  19.602  15.126  1.00 81.60      A    C  
ATOM   1904  CD1 LEU A 262     -27.067  18.523  15.395  1.00 81.12      A    C  
ATOM   1905  CD2 LEU A 262     -27.968  20.180  13.720  1.00 81.32      A    C  
ATOM   1906  N   THR A 263     -32.196  19.136  13.466  1.00 83.45      A    N  
ATOM   1907  CA  THR A 263     -33.415  18.438  13.073  1.00 83.91      A    C  
ATOM   1908  C   THR A 263     -33.535  17.165  13.901  1.00 83.94      A    C  
ATOM   1909  O   THR A 263     -32.573  16.396  14.027  1.00 84.07      A    O  
ATOM   1910  CB  THR A 263     -33.468  18.146  11.538  1.00 84.06      A    C  
ATOM   1911  CG2 THR A 263     -32.336  17.195  11.082  1.00 83.63      A    C  
ATOM   1912  OG1 THR A 263     -34.746  17.594  11.203  1.00 83.56      A    O  
ATOM   1913  N   GLN A 264     -34.714  16.981  14.481  1.00 84.00      A    N  
ATOM   1914  CA  GLN A 264     -34.931  15.990  15.524  1.00 84.19      A    C  
ATOM   1915  C   GLN A 264     -35.149  14.582  14.957  1.00 84.06      A    C  
ATOM   1916  O   GLN A 264     -36.208  14.273  14.396  1.00 84.12      A    O  
ATOM   1917  CB  GLN A 264     -36.096  16.440  16.425  1.00 84.46      A    C  
ATOM   1918  CG  GLN A 264     -36.078  15.889  17.852  1.00 85.78      A    C  
ATOM   1919  CD  GLN A 264     -35.032  16.533  18.777  1.00 87.60      A    C  
ATOM   1920  NE2 GLN A 264     -34.344  17.584  18.304  1.00 87.20      A    N  
ATOM   1921  OE1 GLN A 264     -34.851  16.075  19.909  1.00 88.64      A    O  
ATOM   1922  N   MET A 265     -34.133  13.735  15.124  1.00 83.62      A    N  
ATOM   1923  CA  MET A 265     -34.123  12.377  14.571  1.00 83.05      A    C  
ATOM   1924  C   MET A 265     -34.600  11.355  15.596  1.00 82.67      A    C  
ATOM   1925  O   MET A 265     -34.197  11.422  16.760  1.00 82.35      A    O  
ATOM   1926  CB  MET A 265     -32.706  12.001  14.092  1.00 83.04      A    C  
ATOM   1927  CG  MET A 265     -32.132  12.890  12.978  1.00 82.88      A    C  
ATOM   1928  SD  MET A 265     -32.881  12.632  11.340  1.00 84.12      A    S  
ATOM   1929  CE  MET A 265     -34.018  14.009  11.210  1.00 84.60      A    C  
ATOM   1930  N   PRO A 266     -35.463  10.408  15.167  1.00 82.57      A    N  
ATOM   1931  CA  PRO A 266     -35.894   9.295  16.025  1.00 82.33      A    C  
ATOM   1932  C   PRO A 266     -34.830   8.193  16.063  1.00 82.02      A    C  
ATOM   1933  O   PRO A 266     -34.035   8.080  15.127  1.00 81.80      A    O  
ATOM   1934  CB  PRO A 266     -37.152   8.778  15.313  1.00 82.41      A    C  
ATOM   1935  CG  PRO A 266     -36.901   9.058  13.863  1.00 82.31      A    C  
ATOM   1936  CD  PRO A 266     -36.091  10.343  13.826  1.00 82.79      A    C  
ATOM   1937  N   LYS A 267     -34.802   7.393  17.125  1.00 81.85      A    N  
ATOM   1938  CA  LYS A 267     -33.892   6.256  17.155  1.00 81.66      A    C  
ATOM   1939  C   LYS A 267     -34.319   5.299  16.053  1.00 81.54      A    C  
ATOM   1940  O   LYS A 267     -35.460   4.828  16.053  1.00 82.12      A    O  
ATOM   1941  CB  LYS A 267     -33.889   5.547  18.515  1.00 81.68      A    C  
ATOM   1942  CG  LYS A 267     -33.191   4.178  18.492  1.00 81.20      A    C  
ATOM   1943  CD  LYS A 267     -32.560   3.837  19.822  1.00 81.53      A    C  
ATOM   1944  CE  LYS A 267     -31.592   2.656  19.682  1.00 82.01      A    C  
ATOM   1945  NZ  LYS A 267     -32.209   1.280  19.685  1.00 82.10      A    N1+
ATOM   1946  N   MET A 268     -33.421   5.026  15.107  1.00 80.84      A    N  
ATOM   1947  CA  MET A 268     -33.751   4.085  14.036  1.00 80.15      A    C  
ATOM   1948  C   MET A 268     -33.661   2.653  14.561  1.00 79.21      A    C  
ATOM   1949  O   MET A 268     -33.209   2.417  15.688  1.00 79.03      A    O  
ATOM   1950  CB  MET A 268     -32.907   4.315  12.773  1.00 80.37      A    C  
ATOM   1951  CG  MET A 268     -33.214   5.632  12.037  1.00 81.91      A    C  
ATOM   1952  SD  MET A 268     -34.943   6.214  12.106  1.00 88.34      A    S  
ATOM   1953  CE  MET A 268     -35.705   5.355  10.711  1.00 87.20      A    C  
ATOM   1954  N   ASN A 269     -34.137   1.698  13.778  1.00 77.90      A    N  
ATOM   1955  CA  ASN A 269     -34.102   0.337  14.248  1.00 76.96      A    C  
ATOM   1956  C   ASN A 269     -32.740  -0.193  13.894  1.00 75.68      A    C  
ATOM   1957  O   ASN A 269     -32.271   0.005  12.770  1.00 76.11      A    O  
ATOM   1958  CB  ASN A 269     -35.210  -0.507  13.612  1.00 77.46      A    C  
ATOM   1959  CG  ASN A 269     -35.607  -1.683  14.476  1.00 78.77      A    C  
ATOM   1960  ND2 ASN A 269     -34.616  -2.450  14.934  1.00 78.52      A    N  
ATOM   1961  OD1 ASN A 269     -36.794  -1.891  14.750  1.00 80.61      A    O  
ATOM   1962  N   PHE A 270     -32.088  -0.821  14.862  1.00 73.66      A    N  
ATOM   1963  CA  PHE A 270     -30.769  -1.388  14.639  1.00 71.68      A    C  
ATOM   1964  C   PHE A 270     -30.827  -2.605  13.717  1.00 71.45      A    C  
ATOM   1965  O   PHE A 270     -30.046  -2.687  12.765  1.00 72.04      A    O  
ATOM   1966  CB  PHE A 270     -30.098  -1.723  15.973  1.00 70.45      A    C  
ATOM   1967  CG  PHE A 270     -29.370  -0.565  16.594  1.00 67.44      A    C  
ATOM   1968  CD1 PHE A 270     -29.901   0.715  16.556  1.00 63.49      A    C  
ATOM   1969  CD2 PHE A 270     -28.153  -0.767  17.238  1.00 65.18      A    C  
ATOM   1970  CE1 PHE A 270     -29.218   1.768  17.138  1.00 64.12      A    C  
ATOM   1971  CE2 PHE A 270     -27.479   0.278  17.824  1.00 63.91      A    C  
ATOM   1972  CZ  PHE A 270     -28.004   1.547  17.779  1.00 63.84      A    C  
ATOM   1973  N   ALA A 271     -31.760  -3.524  13.977  1.00 70.88      A    N  
ATOM   1974  CA  ALA A 271     -31.985  -4.682  13.098  1.00 70.65      A    C  
ATOM   1975  C   ALA A 271     -31.942  -4.277  11.634  1.00 70.30      A    C  
ATOM   1976  O   ALA A 271     -31.280  -4.937  10.823  1.00 70.92      A    O  
ATOM   1977  CB  ALA A 271     -33.305  -5.386  13.420  1.00 70.59      A    C  
ATOM   1978  N   ASN A 272     -32.602  -3.169  11.305  1.00 69.16      A    N  
ATOM   1979  CA  ASN A 272     -32.644  -2.723   9.924  1.00 68.59      A    C  
ATOM   1980  C   ASN A 272     -31.304  -2.176   9.423  1.00 67.63      A    C  
ATOM   1981  O   ASN A 272     -31.144  -1.911   8.230  1.00 68.21      A    O  
ATOM   1982  CB  ASN A 272     -33.815  -1.753   9.685  1.00 69.23      A    C  
ATOM   1983  CG  ASN A 272     -35.175  -2.351  10.083  1.00 71.05      A    C  
ATOM   1984  ND2 ASN A 272     -35.234  -3.679  10.260  1.00 72.62      A    N  
ATOM   1985  OD1 ASN A 272     -36.155  -1.620  10.239  1.00 73.91      A    O  
ATOM   1986  N   VAL A 273     -30.328  -2.029  10.317  1.00 65.56      A    N  
ATOM   1987  CA  VAL A 273     -28.994  -1.619   9.888  1.00 63.31      A    C  
ATOM   1988  C   VAL A 273     -28.062  -2.820   9.844  1.00 62.28      A    C  
ATOM   1989  O   VAL A 273     -27.148  -2.888   8.992  1.00 61.86      A    O  
ATOM   1990  CB  VAL A 273     -28.388  -0.527  10.804  1.00 63.39      A    C  
ATOM   1991  CG1 VAL A 273     -27.116   0.013  10.178  1.00 63.48      A    C  
ATOM   1992  CG2 VAL A 273     -29.380   0.611  11.033  1.00 63.00      A    C  
ATOM   1993  N   PHE A 274     -28.323  -3.755  10.763  1.00 60.41      A    N  
ATOM   1994  CA  PHE A 274     -27.575  -5.002  10.938  1.00 59.53      A    C  
ATOM   1995  C   PHE A 274     -28.455  -6.217  10.534  1.00 60.15      A    C  
ATOM   1996  O   PHE A 274     -28.945  -6.996  11.373  1.00 58.90      A    O  
ATOM   1997  CB  PHE A 274     -27.006  -5.080  12.382  1.00 57.70      A    C  
ATOM   1998  CG  PHE A 274     -26.261  -3.810  12.802  1.00 54.08      A    C  
ATOM   1999  CD1 PHE A 274     -24.994  -3.528  12.306  1.00 54.28      A    C  
ATOM   2000  CD2 PHE A 274     -26.845  -2.893  13.658  1.00 52.55      A    C  
ATOM   2001  CE1 PHE A 274     -24.306  -2.326  12.677  1.00 51.98      A    C  
ATOM   2002  CE2 PHE A 274     -26.181  -1.714  14.028  1.00 49.77      A    C  
ATOM   2003  CZ  PHE A 274     -24.911  -1.433  13.528  1.00 51.46      A    C  
ATOM   2004  N   ILE A 275     -28.669  -6.316   9.214  1.00 61.72      A    N  
ATOM   2005  CA  ILE A 275     -29.516  -7.355   8.584  1.00 62.16      A    C  
ATOM   2006  C   ILE A 275     -28.877  -8.736   8.663  1.00 62.06      A    C  
ATOM   2007  O   ILE A 275     -27.758  -8.948   8.172  1.00 62.30      A    O  
ATOM   2008  CB  ILE A 275     -29.842  -7.008   7.095  1.00 62.75      A    C  
ATOM   2009  CG1 ILE A 275     -30.850  -5.841   7.014  1.00 62.86      A    C  
ATOM   2010  CG2 ILE A 275     -30.330  -8.267   6.313  1.00 62.72      A    C  
ATOM   2011  CD1 ILE A 275     -32.193  -6.090   7.748  1.00 64.02      A    C  
ATOM   2012  N   GLY A 276     -29.596  -9.667   9.288  1.00 61.96      A    N  
ATOM   2013  CA  GLY A 276     -29.139 -11.049   9.368  1.00 61.31      A    C  
ATOM   2014  C   GLY A 276     -28.080 -11.281  10.434  1.00 60.56      A    C  
ATOM   2015  O   GLY A 276     -27.631 -12.411  10.635  1.00 60.68      A    O  
ATOM   2016  N   ALA A 277     -27.665 -10.211  11.109  1.00 59.99      A    N  
ATOM   2017  CA  ALA A 277     -26.815 -10.344  12.293  1.00 58.39      A    C  
ATOM   2018  C   ALA A 277     -27.554 -11.185  13.305  1.00 57.27      A    C  
ATOM   2019  O   ALA A 277     -28.778 -11.096  13.418  1.00 56.68      A    O  
ATOM   2020  CB  ALA A 277     -26.498  -8.980  12.895  1.00 58.62      A    C  
ATOM   2021  N   ASN A 278     -26.802 -12.028  14.014  1.00 56.08      A    N  
ATOM   2022  CA  ASN A 278     -27.285 -12.703  15.222  1.00 55.63      A    C  
ATOM   2023  C   ASN A 278     -27.969 -11.689  16.147  1.00 55.57      A    C  
ATOM   2024  O   ASN A 278     -27.380 -10.644  16.455  1.00 54.89      A    O  
ATOM   2025  CB  ASN A 278     -26.097 -13.362  15.923  1.00 55.16      A    C  
ATOM   2026  CG  ASN A 278     -26.442 -13.923  17.266  1.00 55.03      A    C  
ATOM   2027  ND2 ASN A 278     -25.519 -14.690  17.831  1.00 55.98      A    N  
ATOM   2028  OD1 ASN A 278     -27.507 -13.664  17.813  1.00 56.73      A    O  
ATOM   2029  N   PRO A 279     -29.218 -11.975  16.585  1.00 54.75      A    N  
ATOM   2030  CA  PRO A 279     -30.011 -10.957  17.271  1.00 53.84      A    C  
ATOM   2031  C   PRO A 279     -29.442 -10.512  18.623  1.00 53.00      A    C  
ATOM   2032  O   PRO A 279     -29.784  -9.446  19.106  1.00 52.99      A    O  
ATOM   2033  CB  PRO A 279     -31.389 -11.643  17.457  1.00 54.44      A    C  
ATOM   2034  CG  PRO A 279     -31.382 -12.769  16.511  1.00 54.54      A    C  
ATOM   2035  CD  PRO A 279     -29.973 -13.233  16.436  1.00 55.34      A    C  
ATOM   2036  N   LEU A 280     -28.594 -11.336  19.224  1.00 52.43      A    N  
ATOM   2037  CA  LEU A 280     -27.895 -10.982  20.449  1.00 51.72      A    C  
ATOM   2038  C   LEU A 280     -26.778  -9.985  20.172  1.00 50.79      A    C  
ATOM   2039  O   LEU A 280     -26.518  -9.138  20.998  1.00 52.77      A    O  
ATOM   2040  CB  LEU A 280     -27.321 -12.227  21.119  1.00 51.38      A    C  
ATOM   2041  CG  LEU A 280     -28.349 -13.235  21.655  1.00 51.45      A    C  
ATOM   2042  CD1 LEU A 280     -27.674 -14.564  21.795  1.00 51.76      A    C  
ATOM   2043  CD2 LEU A 280     -29.006 -12.780  22.982  1.00 51.19      A    C  
ATOM   2044  N   ALA A 281     -26.135 -10.090  19.015  1.00 50.27      A    N  
ATOM   2045  CA  ALA A 281     -25.193  -9.075  18.545  1.00 49.70      A    C  
ATOM   2046  C   ALA A 281     -25.891  -7.735  18.519  1.00 49.96      A    C  
ATOM   2047  O   ALA A 281     -25.370  -6.756  19.043  1.00 48.80      A    O  
ATOM   2048  CB  ALA A 281     -24.700  -9.409  17.160  1.00 49.59      A    C  
ATOM   2049  N   VAL A 282     -27.087  -7.707  17.916  1.00 49.47      A    N  
ATOM   2050  CA  VAL A 282     -27.861  -6.472  17.747  1.00 48.80      A    C  
ATOM   2051  C   VAL A 282     -28.234  -5.906  19.122  1.00 48.40      A    C  
ATOM   2052  O   VAL A 282     -28.064  -4.693  19.382  1.00 47.89      A    O  
ATOM   2053  CB  VAL A 282     -29.116  -6.685  16.813  1.00 50.00      A    C  
ATOM   2054  CG1 VAL A 282     -30.033  -5.404  16.766  1.00 50.13      A    C  
ATOM   2055  CG2 VAL A 282     -28.663  -7.032  15.407  1.00 49.09      A    C  
ATOM   2056  N   ASP A 283     -28.649  -6.787  20.026  1.00 46.75      A    N  
ATOM   2057  CA  ASP A 283     -28.998  -6.346  21.367  1.00 48.01      A    C  
ATOM   2058  C   ASP A 283     -27.789  -5.727  22.109  1.00 46.81      A    C  
ATOM   2059  O   ASP A 283     -27.914  -4.685  22.786  1.00 46.79      A    O  
ATOM   2060  CB  ASP A 283     -29.497  -7.524  22.207  1.00 48.51      A    C  
ATOM   2061  CG  ASP A 283     -30.250  -7.062  23.415  1.00 53.85      A    C  
ATOM   2062  OD1 ASP A 283     -31.305  -6.405  23.218  1.00 57.57      A    O  
ATOM   2063  OD2 ASP A 283     -29.779  -7.313  24.552  1.00 58.04      A    O1-
ATOM   2064  N   LEU A 284     -26.646  -6.399  22.014  1.00 44.67      A    N  
ATOM   2065  CA  LEU A 284     -25.419  -5.838  22.596  1.00 44.31      A    C  
ATOM   2066  C   LEU A 284     -25.083  -4.490  21.976  1.00 43.94      A    C  
ATOM   2067  O   LEU A 284     -24.765  -3.538  22.716  1.00 43.59      A    O  
ATOM   2068  CB  LEU A 284     -24.252  -6.806  22.491  1.00 43.71      A    C  
ATOM   2069  CG  LEU A 284     -22.950  -6.294  23.124  1.00 42.13      A    C  
ATOM   2070  CD1 LEU A 284     -23.215  -6.012  24.578  1.00 39.42      A    C  
ATOM   2071  CD2 LEU A 284     -21.919  -7.376  22.913  1.00 38.10      A    C  
ATOM   2072  N   LEU A 285     -25.191  -4.387  20.651  1.00 43.09      A    N  
ATOM   2073  CA  LEU A 285     -24.927  -3.147  19.977  1.00 43.92      A    C  
ATOM   2074  C   LEU A 285     -25.763  -1.990  20.464  1.00 44.94      A    C  
ATOM   2075  O   LEU A 285     -25.250  -0.854  20.573  1.00 44.34      A    O  
ATOM   2076  CB  LEU A 285     -25.024  -3.252  18.458  1.00 44.34      A    C  
ATOM   2077  CG  LEU A 285     -23.820  -3.945  17.812  1.00 46.33      A    C  
ATOM   2078  CD1 LEU A 285     -24.196  -4.472  16.419  1.00 47.57      A    C  
ATOM   2079  CD2 LEU A 285     -22.600  -3.054  17.731  1.00 42.51      A    C  
ATOM   2080  N   GLU A 286     -27.044  -2.261  20.721  1.00 45.03      A    N  
ATOM   2081  CA  GLU A 286     -27.970  -1.257  21.247  1.00 46.37      A    C  
ATOM   2082  C   GLU A 286     -27.570  -0.832  22.631  1.00 45.74      A    C  
ATOM   2083  O   GLU A 286     -27.897   0.279  23.030  1.00 47.02      A    O  
ATOM   2084  CB  GLU A 286     -29.414  -1.785  21.321  1.00 47.28      A    C  
ATOM   2085  CG  GLU A 286     -30.018  -1.975  19.982  1.00 52.83      A    C  
ATOM   2086  CD  GLU A 286     -31.479  -2.358  20.046  1.00 59.17      A    C  
ATOM   2087  OE1 GLU A 286     -32.281  -1.507  19.627  1.00 63.02      A    O  
ATOM   2088  OE2 GLU A 286     -31.814  -3.486  20.500  1.00 60.30      A    O1-
ATOM   2089  N   LYS A 287     -26.885  -1.700  23.378  1.00 44.77      A    N  
ATOM   2090  CA  LYS A 287     -26.409  -1.291  24.712  1.00 44.60      A    C  
ATOM   2091  C   LYS A 287     -25.113  -0.495  24.690  1.00 43.50      A    C  
ATOM   2092  O   LYS A 287     -24.823   0.237  25.655  1.00 42.51      A    O  
ATOM   2093  CB  LYS A 287     -26.278  -2.502  25.619  1.00 45.55      A    C  
ATOM   2094  CG  LYS A 287     -27.683  -3.111  25.980  1.00 48.82      A    C  
ATOM   2095  CD  LYS A 287     -27.488  -4.383  26.800  1.00 52.63      A    C  
ATOM   2096  CE  LYS A 287     -28.788  -4.926  27.387  1.00 53.37      A    C  
ATOM   2097  NZ  LYS A 287     -29.797  -5.204  26.351  1.00 56.79      A    N1+
ATOM   2098  N   MET A 288     -24.321  -0.654  23.624  1.00 41.85      A    N  
ATOM   2099  CA  MET A 288     -23.006  -0.027  23.518  1.00 41.62      A    C  
ATOM   2100  C   MET A 288     -23.140   1.317  22.865  1.00 41.34      A    C  
ATOM   2101  O   MET A 288     -22.458   2.282  23.235  1.00 39.71      A    O  
ATOM   2102  CB  MET A 288     -22.065  -0.879  22.661  1.00 41.02      A    C  
ATOM   2103  CG  MET A 288     -21.752  -2.213  23.254  1.00 41.25      A    C  
ATOM   2104  SD  MET A 288     -20.588  -3.147  22.229  1.00 44.32      A    S  
ATOM   2105  CE  MET A 288     -19.847  -4.120  23.499  1.00 43.28      A    C  
ATOM   2106  N   LEU A 289     -24.030   1.380  21.873  1.00 41.62      A    N  
ATOM   2107  CA  LEU A 289     -24.146   2.551  21.053  1.00 42.15      A    C  
ATOM   2108  C   LEU A 289     -25.265   3.418  21.584  1.00 44.24      A    C  
ATOM   2109  O   LEU A 289     -26.238   3.694  20.896  1.00 44.20      A    O  
ATOM   2110  CB  LEU A 289     -24.323   2.197  19.584  1.00 41.88      A    C  
ATOM   2111  CG  LEU A 289     -23.099   1.516  18.954  1.00 42.27      A    C  
ATOM   2112  CD1 LEU A 289     -23.376   1.053  17.508  1.00 43.35      A    C  
ATOM   2113  CD2 LEU A 289     -21.881   2.427  18.980  1.00 40.06      A    C  
ATOM   2114  N   VAL A 290     -25.087   3.842  22.825  1.00 45.04      A    N  
ATOM   2115  CA  VAL A 290     -26.056   4.655  23.529  1.00 47.44      A    C  
ATOM   2116  C   VAL A 290     -25.405   6.032  23.700  1.00 47.82      A    C  
ATOM   2117  O   VAL A 290     -24.221   6.137  24.039  1.00 47.76      A    O  
ATOM   2118  CB  VAL A 290     -26.403   3.978  24.870  1.00 46.63      A    C  
ATOM   2119  CG1 VAL A 290     -26.875   4.965  25.869  1.00 50.69      A    C  
ATOM   2120  CG2 VAL A 290     -27.471   2.891  24.654  1.00 49.88      A    C  
ATOM   2121  N   LEU A 291     -26.154   7.082  23.412  1.00 48.86      A    N  
ATOM   2122  CA  LEU A 291     -25.584   8.431  23.407  1.00 50.68      A    C  
ATOM   2123  C   LEU A 291     -25.197   8.836  24.832  1.00 50.58      A    C  
ATOM   2124  O   LEU A 291     -24.128   9.394  25.047  1.00 50.80      A    O  
ATOM   2125  CB  LEU A 291     -26.584   9.416  22.798  1.00 51.46      A    C  
ATOM   2126  CG  LEU A 291     -26.080  10.738  22.268  1.00 52.85      A    C  
ATOM   2127  CD1 LEU A 291     -25.314  10.458  21.007  1.00 57.55      A    C  
ATOM   2128  CD2 LEU A 291     -27.246  11.639  21.972  1.00 53.34      A    C  
ATOM   2129  N   ASP A 292     -26.052   8.511  25.805  1.00 49.72      A    N  
ATOM   2130  CA  ASP A 292     -25.800   8.846  27.203  1.00 50.12      A    C  
ATOM   2131  C   ASP A 292     -24.795   7.913  27.801  1.00 50.11      A    C  
ATOM   2132  O   ASP A 292     -25.072   6.727  27.981  1.00 50.26      A    O  
ATOM   2133  CB  ASP A 292     -27.100   8.773  28.038  1.00 50.17      A    C  
ATOM   2134  CG  ASP A 292     -26.938   9.344  29.454  1.00 52.08      A    C  
ATOM   2135  OD1 ASP A 292     -25.805   9.428  30.006  1.00 51.42      A    O  
ATOM   2136  OD2 ASP A 292     -27.983   9.719  30.022  1.00 55.14      A    O1-
ATOM   2137  N   SER A 293     -23.650   8.441  28.189  1.00 49.57      A    N  
ATOM   2138  CA  SER A 293     -22.616   7.551  28.683  1.00 50.83      A    C  
ATOM   2139  C   SER A 293     -22.966   6.839  30.000  1.00 50.77      A    C  
ATOM   2140  O   SER A 293     -22.501   5.725  30.243  1.00 49.75      A    O  
ATOM   2141  CB  SER A 293     -21.248   8.246  28.757  1.00 50.87      A    C  
ATOM   2142  OG  SER A 293     -21.194   9.130  29.856  1.00 52.69      A    O  
ATOM   2143  N   ASP A 294     -23.799   7.464  30.839  1.00 51.03      A    N  
ATOM   2144  CA  ASP A 294     -24.131   6.866  32.130  1.00 51.43      A    C  
ATOM   2145  C   ASP A 294     -25.023   5.635  31.971  1.00 50.41      A    C  
ATOM   2146  O   ASP A 294     -25.224   4.895  32.918  1.00 49.63      A    O  
ATOM   2147  CB  ASP A 294     -24.778   7.893  33.075  1.00 52.91      A    C  
ATOM   2148  CG  ASP A 294     -23.941   9.203  33.195  1.00 57.71      A    C  
ATOM   2149  OD1 ASP A 294     -22.815   9.150  33.756  1.00 61.33      A    O  
ATOM   2150  OD2 ASP A 294     -24.427  10.282  32.742  1.00 62.13      A    O1-
ATOM   2151  N   LYS A 295     -25.543   5.424  30.767  1.00 48.76      A    N  
ATOM   2152  CA  LYS A 295     -26.474   4.335  30.501  1.00 48.62      A    C  
ATOM   2153  C   LYS A 295     -25.814   3.251  29.619  1.00 47.20      A    C  
ATOM   2154  O   LYS A 295     -26.402   2.222  29.336  1.00 45.60      A    O  
ATOM   2155  CB  LYS A 295     -27.727   4.900  29.818  1.00 48.19      A    C  
ATOM   2156  CG  LYS A 295     -28.610   5.775  30.775  1.00 50.72      A    C  
ATOM   2157  CD  LYS A 295     -29.853   6.317  30.093  1.00 52.10      A    C  
ATOM   2158  CE  LYS A 295     -30.874   6.964  31.073  1.00 56.20      A    C  
ATOM   2159  NZ  LYS A 295     -30.887   6.323  32.428  1.00 61.37      A    N1+
ATOM   2160  N   ARG A 296     -24.602   3.535  29.149  1.00 45.00      A    N  
ATOM   2161  CA  ARG A 296     -23.894   2.644  28.227  1.00 43.71      A    C  
ATOM   2162  C   ARG A 296     -23.422   1.420  29.027  1.00 42.63      A    C  
ATOM   2163  O   ARG A 296     -23.014   1.538  30.194  1.00 42.67      A    O  
ATOM   2164  CB  ARG A 296     -22.719   3.462  27.638  1.00 44.07      A    C  
ATOM   2165  CG  ARG A 296     -22.161   3.034  26.327  1.00 43.63      A    C  
ATOM   2166  CD  ARG A 296     -21.188   4.083  25.723  1.00 43.52      A    C  
ATOM   2167  NE  ARG A 296     -21.779   5.336  25.222  1.00 40.60      A    N  
ATOM   2168  CZ  ARG A 296     -21.110   6.483  25.153  1.00 43.13      A    C  
ATOM   2169  NH1 ARG A 296     -19.838   6.541  25.559  1.00 37.26      A    N1+
ATOM   2170  NH2 ARG A 296     -21.688   7.568  24.678  1.00 40.39      A    N  
ATOM   2171  N   ILE A 297     -23.490   0.237  28.446  1.00 41.94      A    N  
ATOM   2172  CA  ILE A 297     -22.985  -0.987  29.116  1.00 41.25      A    C  
ATOM   2173  C   ILE A 297     -21.447  -0.853  29.388  1.00 41.59      A    C  
ATOM   2174  O   ILE A 297     -20.749  -0.230  28.585  1.00 41.44      A    O  
ATOM   2175  CB  ILE A 297     -23.343  -2.262  28.282  1.00 40.72      A    C  
ATOM   2176  CG1 ILE A 297     -23.337  -3.490  29.175  1.00 41.35      A    C  
ATOM   2177  CG2 ILE A 297     -22.416  -2.375  26.954  1.00 38.82      A    C  
ATOM   2178  CD1 ILE A 297     -24.020  -4.765  28.580  1.00 41.47      A    C  
ATOM   2179  N   THR A 298     -20.953  -1.394  30.511  1.00 40.26      A    N  
ATOM   2180  CA  THR A 298     -19.540  -1.311  30.883  1.00 39.55      A    C  
ATOM   2181  C   THR A 298     -18.899  -2.592  30.349  1.00 39.50      A    C  
ATOM   2182  O   THR A 298     -19.613  -3.474  29.855  1.00 38.35      A    O  
ATOM   2183  CB  THR A 298     -19.375  -1.256  32.413  1.00 40.56      A    C  
ATOM   2184  CG2 THR A 298     -20.266  -0.137  33.053  1.00 40.39      A    C  
ATOM   2185  OG1 THR A 298     -19.765  -2.527  32.956  1.00 38.77      A    O  
ATOM   2186  N   ALA A 299     -17.566  -2.704  30.422  1.00 37.65      A    N  
ATOM   2187  CA  ALA A 299     -16.845  -3.861  29.910  1.00 37.23      A    C  
ATOM   2188  C   ALA A 299     -17.199  -5.117  30.684  1.00 38.26      A    C  
ATOM   2189  O   ALA A 299     -17.452  -6.171  30.053  1.00 34.84      A    O  
ATOM   2190  CB  ALA A 299     -15.300  -3.630  29.966  1.00 37.76      A    C  
ATOM   2191  N   ALA A 300     -17.150  -5.030  32.037  1.00 39.16      A    N  
ATOM   2192  CA  ALA A 300     -17.484  -6.161  32.933  1.00 38.50      A    C  
ATOM   2193  C   ALA A 300     -18.919  -6.696  32.639  1.00 39.95      A    C  
ATOM   2194  O   ALA A 300     -19.159  -7.916  32.546  1.00 40.51      A    O  
ATOM   2195  CB  ALA A 300     -17.439  -5.704  34.340  1.00 39.46      A    C  
ATOM   2196  N   GLN A 301     -19.856  -5.769  32.517  1.00 40.41      A    N  
ATOM   2197  CA  GLN A 301     -21.255  -6.114  32.151  1.00 41.34      A    C  
ATOM   2198  C   GLN A 301     -21.396  -6.721  30.734  1.00 41.60      A    C  
ATOM   2199  O   GLN A 301     -22.085  -7.708  30.567  1.00 42.15      A    O  
ATOM   2200  CB  GLN A 301     -22.122  -4.894  32.244  1.00 40.40      A    C  
ATOM   2201  CG  GLN A 301     -22.362  -4.393  33.664  1.00 43.52      A    C  
ATOM   2202  CD  GLN A 301     -23.119  -3.099  33.672  1.00 44.50      A    C  
ATOM   2203  NE2 GLN A 301     -23.072  -2.386  32.570  1.00 42.44      A    N  
ATOM   2204  OE1 GLN A 301     -23.757  -2.735  34.670  1.00 49.99      A    O  
ATOM   2205  N   ALA A 302     -20.752  -6.125  29.716  1.00 41.82      A    N  
ATOM   2206  CA  ALA A 302     -20.759  -6.678  28.348  1.00 41.74      A    C  
ATOM   2207  C   ALA A 302     -20.264  -8.112  28.293  1.00 42.14      A    C  
ATOM   2208  O   ALA A 302     -20.842  -8.910  27.578  1.00 42.27      A    O  
ATOM   2209  CB  ALA A 302     -19.973  -5.776  27.344  1.00 40.95      A    C  
ATOM   2210  N   LEU A 303     -19.234  -8.459  29.074  1.00 40.40      A    N  
ATOM   2211  CA  LEU A 303     -18.707  -9.816  29.041  1.00 41.32      A    C  
ATOM   2212  C   LEU A 303     -19.736 -10.880  29.486  1.00 42.19      A    C  
ATOM   2213  O   LEU A 303     -19.613 -12.054  29.168  1.00 39.36      A    O  
ATOM   2214  CB  LEU A 303     -17.535  -9.934  30.015  1.00 40.52      A    C  
ATOM   2215  CG  LEU A 303     -16.241  -9.242  29.578  1.00 41.48      A    C  
ATOM   2216  CD1 LEU A 303     -15.224  -9.243  30.678  1.00 40.07      A    C  
ATOM   2217  CD2 LEU A 303     -15.707  -9.995  28.365  1.00 36.88      A    C  
ATOM   2218  N   ALA A 304     -20.651 -10.464  30.348  1.00 43.96      A    N  
ATOM   2219  CA  ALA A 304     -21.625 -11.410  30.900  1.00 45.21      A    C  
ATOM   2220  C   ALA A 304     -22.831 -11.533  30.002  1.00 46.12      A    C  
ATOM   2221  O   ALA A 304     -23.689 -12.360  30.277  1.00 49.21      A    O  
ATOM   2222  CB  ALA A 304     -22.034 -11.003  32.329  1.00 44.38      A    C  
ATOM   2223  N   HIS A 305     -22.912 -10.719  28.945  1.00 46.91      A    N  
ATOM   2224  CA  HIS A 305     -24.058 -10.674  28.020  1.00 46.45      A    C  
ATOM   2225  C   HIS A 305     -24.152 -11.963  27.240  1.00 47.14      A    C  
ATOM   2226  O   HIS A 305     -23.134 -12.522  26.862  1.00 46.39      A    O  
ATOM   2227  CB  HIS A 305     -23.886  -9.535  27.018  1.00 46.41      A    C  
ATOM   2228  CG  HIS A 305     -25.085  -9.271  26.162  1.00 44.13      A    C  
ATOM   2229  CD2 HIS A 305     -26.088  -8.377  26.295  1.00 46.13      A    C  
ATOM   2230  ND1 HIS A 305     -25.292  -9.888  24.950  1.00 43.02      A    N  
ATOM   2231  CE1 HIS A 305     -26.395  -9.429  24.400  1.00 42.83      A    C  
ATOM   2232  NE2 HIS A 305     -26.896  -8.504  25.192  1.00 44.60      A    N  
ATOM   2233  N   ALA A 306     -25.378 -12.399  26.934  1.00 47.89      A    N  
ATOM   2234  CA  ALA A 306     -25.614 -13.732  26.377  1.00 47.71      A    C  
ATOM   2235  C   ALA A 306     -24.818 -13.962  25.096  1.00 47.35      A    C  
ATOM   2236  O   ALA A 306     -24.389 -15.087  24.818  1.00 48.46      A    O  
ATOM   2237  CB  ALA A 306     -27.121 -13.933  26.142  1.00 48.12      A    C  
ATOM   2238  N   TYR A 307     -24.538 -12.888  24.355  1.00 46.48      A    N  
ATOM   2239  CA  TYR A 307     -23.773 -12.979  23.093  1.00 46.16      A    C  
ATOM   2240  C   TYR A 307     -22.427 -13.671  23.231  1.00 46.71      A    C  
ATOM   2241  O   TYR A 307     -21.951 -14.267  22.251  1.00 48.25      A    O  
ATOM   2242  CB  TYR A 307     -23.584 -11.588  22.451  1.00 44.84      A    C  
ATOM   2243  CG  TYR A 307     -22.910 -11.568  21.095  1.00 43.33      A    C  
ATOM   2244  CD1 TYR A 307     -23.482 -12.223  19.989  1.00 44.27      A    C  
ATOM   2245  CD2 TYR A 307     -21.706 -10.867  20.883  1.00 44.08      A    C  
ATOM   2246  CE1 TYR A 307     -22.868 -12.207  18.734  1.00 41.61      A    C  
ATOM   2247  CE2 TYR A 307     -21.093 -10.848  19.612  1.00 39.43      A    C  
ATOM   2248  CZ  TYR A 307     -21.695 -11.512  18.556  1.00 42.85      A    C  
ATOM   2249  OH  TYR A 307     -21.144 -11.507  17.304  1.00 45.56      A    O  
ATOM   2250  N   PHE A 308     -21.803 -13.583  24.411  1.00 46.76      A    N  
ATOM   2251  CA  PHE A 308     -20.489 -14.240  24.662  1.00 46.45      A    C  
ATOM   2252  C   PHE A 308     -20.548 -15.575  25.420  1.00 47.96      A    C  
ATOM   2253  O   PHE A 308     -19.502 -16.098  25.841  1.00 47.64      A    O  
ATOM   2254  CB  PHE A 308     -19.515 -13.267  25.384  1.00 45.13      A    C  
ATOM   2255  CG  PHE A 308     -19.343 -11.954  24.657  1.00 42.25      A    C  
ATOM   2256  CD1 PHE A 308     -18.739 -11.908  23.408  1.00 40.06      A    C  
ATOM   2257  CD2 PHE A 308     -19.857 -10.786  25.194  1.00 41.23      A    C  
ATOM   2258  CE1 PHE A 308     -18.601 -10.694  22.731  1.00 42.70      A    C  
ATOM   2259  CE2 PHE A 308     -19.752  -9.580  24.538  1.00 41.27      A    C  
ATOM   2260  CZ  PHE A 308     -19.110  -9.523  23.300  1.00 39.77      A    C  
ATOM   2261  N   ALA A 309     -21.757 -16.135  25.583  1.00 49.27      A    N  
ATOM   2262  CA  ALA A 309     -21.948 -17.422  26.283  1.00 50.23      A    C  
ATOM   2263  C   ALA A 309     -20.817 -18.435  26.113  1.00 51.47      A    C  
ATOM   2264  O   ALA A 309     -20.346 -19.026  27.096  1.00 53.17      A    O  
ATOM   2265  CB  ALA A 309     -23.277 -18.057  25.863  1.00 50.46      A    C  
ATOM   2266  N   GLN A 310     -20.391 -18.654  24.874  1.00 52.08      A    N  
ATOM   2267  CA  GLN A 310     -19.436 -19.715  24.584  1.00 53.83      A    C  
ATOM   2268  C   GLN A 310     -17.998 -19.443  25.039  1.00 53.84      A    C  
ATOM   2269  O   GLN A 310     -17.176 -20.375  25.083  1.00 53.81      A    O  
ATOM   2270  CB  GLN A 310     -19.503 -20.134  23.105  1.00 53.63      A    C  
ATOM   2271  CG  GLN A 310     -19.099 -19.082  22.074  1.00 56.52      A    C  
ATOM   2272  CD  GLN A 310     -19.069 -19.616  20.627  1.00 56.48      A    C  
ATOM   2273  NE2 GLN A 310     -19.846 -18.984  19.731  1.00 56.03      A    N  
ATOM   2274  OE1 GLN A 310     -18.324 -20.550  20.318  1.00 60.08      A    O  
ATOM   2275  N   TYR A 311     -17.706 -18.178  25.382  1.00 53.58      A    N  
ATOM   2276  CA  TYR A 311     -16.347 -17.756  25.778  1.00 53.11      A    C  
ATOM   2277  C   TYR A 311     -16.302 -17.220  27.197  1.00 52.09      A    C  
ATOM   2278  O   TYR A 311     -15.239 -17.260  27.822  1.00 51.94      A    O  
ATOM   2279  CB  TYR A 311     -15.794 -16.677  24.824  1.00 54.08      A    C  
ATOM   2280  CG  TYR A 311     -15.710 -17.115  23.390  1.00 53.22      A    C  
ATOM   2281  CD1 TYR A 311     -14.763 -18.049  22.975  1.00 54.19      A    C  
ATOM   2282  CD2 TYR A 311     -16.566 -16.584  22.454  1.00 52.09      A    C  
ATOM   2283  CE1 TYR A 311     -14.697 -18.463  21.636  1.00 54.48      A    C  
ATOM   2284  CE2 TYR A 311     -16.512 -16.973  21.123  1.00 54.10      A    C  
ATOM   2285  CZ  TYR A 311     -15.579 -17.915  20.722  1.00 55.74      A    C  
ATOM   2286  OH  TYR A 311     -15.561 -18.294  19.393  1.00 57.61      A    O  
ATOM   2287  N   HIS A 312     -17.444 -16.729  27.699  1.00 51.19      A    N  
ATOM   2288  CA  HIS A 312     -17.491 -16.106  29.031  1.00 51.99      A    C  
ATOM   2289  C   HIS A 312     -17.027 -17.013  30.178  1.00 52.67      A    C  
ATOM   2290  O   HIS A 312     -17.612 -18.071  30.428  1.00 51.60      A    O  
ATOM   2291  CB  HIS A 312     -18.888 -15.549  29.339  1.00 51.09      A    C  
ATOM   2292  CG  HIS A 312     -19.016 -14.870  30.674  1.00 51.09      A    C  
ATOM   2293  CD2 HIS A 312     -20.027 -14.885  31.579  1.00 49.09      A    C  
ATOM   2294  ND1 HIS A 312     -18.066 -13.999  31.182  1.00 52.25      A    N  
ATOM   2295  CE1 HIS A 312     -18.477 -13.526  32.348  1.00 50.89      A    C  
ATOM   2296  NE2 HIS A 312     -19.666 -14.043  32.610  1.00 51.60      A    N  
ATOM   2297  N   ASP A 313     -15.998 -16.580  30.903  1.00 52.93      A    N  
ATOM   2298  CA  ASP A 313     -15.647 -17.261  32.154  1.00 54.29      A    C  
ATOM   2299  C   ASP A 313     -15.377 -16.309  33.309  1.00 54.97      A    C  
ATOM   2300  O   ASP A 313     -14.282 -15.749  33.435  1.00 54.54      A    O  
ATOM   2301  CB  ASP A 313     -14.489 -18.235  31.962  1.00 54.94      A    C  
ATOM   2302  CG  ASP A 313     -14.122 -18.980  33.253  1.00 54.86      A    C  
ATOM   2303  OD1 ASP A 313     -14.776 -18.779  34.310  1.00 54.22      A    O  
ATOM   2304  OD2 ASP A 313     -13.156 -19.772  33.196  1.00 54.97      A    O1-
ATOM   2305  N   PRO A 314     -16.367 -16.153  34.191  1.00 55.25      A    N  
ATOM   2306  CA  PRO A 314     -16.240 -15.077  35.152  1.00 56.04      A    C  
ATOM   2307  C   PRO A 314     -15.100 -15.255  36.144  1.00 56.62      A    C  
ATOM   2308  O   PRO A 314     -14.825 -14.343  36.893  1.00 57.70      A    O  
ATOM   2309  CB  PRO A 314     -17.604 -15.047  35.864  1.00 55.89      A    C  
ATOM   2310  CG  PRO A 314     -18.263 -16.353  35.562  1.00 55.93      A    C  
ATOM   2311  CD  PRO A 314     -17.601 -16.945  34.348  1.00 55.92      A    C  
ATOM   2312  N   ASP A 315     -14.444 -16.407  36.149  1.00 57.35      A    N  
ATOM   2313  CA  ASP A 315     -13.252 -16.601  36.972  1.00 57.64      A    C  
ATOM   2314  C   ASP A 315     -11.970 -16.512  36.141  1.00 56.97      A    C  
ATOM   2315  O   ASP A 315     -10.875 -16.768  36.651  1.00 57.04      A    O  
ATOM   2316  CB  ASP A 315     -13.311 -17.964  37.665  1.00 58.61      A    C  
ATOM   2317  CG  ASP A 315     -14.572 -18.151  38.491  1.00 60.42      A    C  
ATOM   2318  OD1 ASP A 315     -15.016 -17.178  39.154  1.00 65.31      A    O  
ATOM   2319  OD2 ASP A 315     -15.101 -19.282  38.509  1.00 62.35      A    O1-
ATOM   2320  N   ASP A 316     -12.097 -16.202  34.847  1.00 56.15      A    N  
ATOM   2321  CA  ASP A 316     -10.908 -15.975  34.018  1.00 54.19      A    C  
ATOM   2322  C   ASP A 316     -10.979 -14.647  33.284  1.00 51.81      A    C  
ATOM   2323  O   ASP A 316     -10.648 -14.558  32.097  1.00 50.68      A    O  
ATOM   2324  CB  ASP A 316     -10.641 -17.121  33.038  1.00 55.50      A    C  
ATOM   2325  CG  ASP A 316      -9.241 -17.031  32.425  1.00 58.04      A    C  
ATOM   2326  OD1 ASP A 316      -8.401 -16.299  33.005  1.00 62.56      A    O  
ATOM   2327  OD2 ASP A 316      -8.978 -17.645  31.357  1.00 61.96      A    O1-
ATOM   2328  N   GLU A 317     -11.436 -13.633  34.014  1.00 49.68      A    N  
ATOM   2329  CA  GLU A 317     -11.582 -12.258  33.514  1.00 47.24      A    C  
ATOM   2330  C   GLU A 317     -11.016 -11.311  34.576  1.00 46.72      A    C  
ATOM   2331  O   GLU A 317     -11.767 -10.591  35.230  1.00 45.76      A    O  
ATOM   2332  CB  GLU A 317     -13.038 -11.980  33.188  1.00 46.79      A    C  
ATOM   2333  CG  GLU A 317     -13.441 -12.673  31.862  1.00 45.53      A    C  
ATOM   2334  CD  GLU A 317     -14.927 -12.896  31.693  1.00 47.10      A    C  
ATOM   2335  OE1 GLU A 317     -15.710 -12.314  32.472  1.00 47.01      A    O  
ATOM   2336  OE2 GLU A 317     -15.303 -13.643  30.734  1.00 49.35      A    O1-
ATOM   2337  N   PRO A 318      -9.692 -11.371  34.771  1.00 46.32      A    N  
ATOM   2338  CA  PRO A 318      -9.000 -10.710  35.856  1.00 46.87      A    C  
ATOM   2339  C   PRO A 318      -8.908  -9.184  35.747  1.00 46.75      A    C  
ATOM   2340  O   PRO A 318      -9.008  -8.577  34.651  1.00 45.33      A    O  
ATOM   2341  CB  PRO A 318      -7.605 -11.378  35.835  1.00 46.58      A    C  
ATOM   2342  CG  PRO A 318      -7.434 -11.848  34.495  1.00 46.74      A    C  
ATOM   2343  CD  PRO A 318      -8.768 -12.211  33.985  1.00 47.22      A    C  
ATOM   2344  N   VAL A 319      -8.745  -8.579  36.915  1.00 47.47      A    N  
ATOM   2345  CA  VAL A 319      -8.716  -7.137  37.067  1.00 47.46      A    C  
ATOM   2346  C   VAL A 319      -7.306  -6.760  37.447  1.00 47.12      A    C  
ATOM   2347  O   VAL A 319      -6.490  -7.621  37.828  1.00 45.90      A    O  
ATOM   2348  CB  VAL A 319      -9.740  -6.651  38.124  1.00 48.00      A    C  
ATOM   2349  CG1 VAL A 319     -11.172  -7.076  37.697  1.00 49.56      A    C  
ATOM   2350  CG2 VAL A 319      -9.375  -7.173  39.526  1.00 48.87      A    C  
ATOM   2351  N   ALA A 320      -7.017  -5.474  37.303  1.00 47.46      A    N  
ATOM   2352  CA  ALA A 320      -5.668  -4.966  37.467  1.00 48.47      A    C  
ATOM   2353  C   ALA A 320      -5.415  -4.460  38.878  1.00 49.71      A    C  
ATOM   2354  O   ALA A 320      -6.333  -4.037  39.580  1.00 49.29      A    O  
ATOM   2355  CB  ALA A 320      -5.439  -3.810  36.485  1.00 48.03      A    C  
ATOM   2356  N   ASP A 321      -4.153  -4.417  39.272  1.00 52.02      A    N  
ATOM   2357  CA  ASP A 321      -3.810  -3.588  40.425  1.00 54.33      A    C  
ATOM   2358  C   ASP A 321      -4.091  -2.096  40.190  1.00 55.51      A    C  
ATOM   2359  O   ASP A 321      -4.143  -1.616  39.053  1.00 53.37      A    O  
ATOM   2360  CB  ASP A 321      -2.374  -3.832  40.843  1.00 55.78      A    C  
ATOM   2361  CG  ASP A 321      -2.143  -5.248  41.224  1.00 58.50      A    C  
ATOM   2362  OD1 ASP A 321      -3.146  -5.957  41.451  1.00 60.34      A    O  
ATOM   2363  OD2 ASP A 321      -0.966  -5.669  41.294  1.00 65.40      A    O1-
ATOM   2364  N   PRO A 322      -4.253  -1.334  41.289  1.00 57.22      A    N  
ATOM   2365  CA  PRO A 322      -4.617   0.083  41.120  1.00 57.44      A    C  
ATOM   2366  C   PRO A 322      -3.444   0.848  40.465  1.00 56.56      A    C  
ATOM   2367  O   PRO A 322      -2.286   0.557  40.733  1.00 56.10      A    O  
ATOM   2368  CB  PRO A 322      -4.845   0.549  42.563  1.00 58.16      A    C  
ATOM   2369  CG  PRO A 322      -3.891  -0.340  43.380  1.00 58.32      A    C  
ATOM   2370  CD  PRO A 322      -4.019  -1.694  42.703  1.00 57.55      A    C  
ATOM   2371  N   TYR A 323      -3.744   1.751  39.549  1.00 55.93      A    N  
ATOM   2372  CA  TYR A 323      -2.655   2.389  38.796  1.00 55.03      A    C  
ATOM   2373  C   TYR A 323      -2.496   3.877  39.174  1.00 54.66      A    C  
ATOM   2374  O   TYR A 323      -3.376   4.704  38.928  1.00 55.59      A    O  
ATOM   2375  CB  TYR A 323      -2.833   2.199  37.287  1.00 53.80      A    C  
ATOM   2376  CG  TYR A 323      -1.772   2.885  36.452  1.00 52.60      A    C  
ATOM   2377  CD1 TYR A 323      -0.421   2.533  36.562  1.00 52.23      A    C  
ATOM   2378  CD2 TYR A 323      -2.116   3.886  35.561  1.00 50.21      A    C  
ATOM   2379  CE1 TYR A 323       0.551   3.184  35.784  1.00 50.55      A    C  
ATOM   2380  CE2 TYR A 323      -1.161   4.524  34.784  1.00 50.44      A    C  
ATOM   2381  CZ  TYR A 323       0.159   4.165  34.913  1.00 50.51      A    C  
ATOM   2382  OH  TYR A 323       1.076   4.808  34.149  1.00 54.30      A    O  
ATOM   2383  N   ASP A 324      -1.337   4.196  39.733  1.00 54.68      A    N  
ATOM   2384  CA  ASP A 324      -1.063   5.510  40.298  1.00 53.12      A    C  
ATOM   2385  C   ASP A 324      -0.605   6.482  39.226  1.00 52.89      A    C  
ATOM   2386  O   ASP A 324       0.573   6.461  38.817  1.00 53.08      A    O  
ATOM   2387  CB  ASP A 324      -0.039   5.320  41.419  1.00 53.37      A    C  
ATOM   2388  CG  ASP A 324       0.414   6.635  42.048  1.00 53.91      A    C  
ATOM   2389  OD1 ASP A 324      -0.136   7.709  41.715  1.00 53.77      A    O  
ATOM   2390  OD2 ASP A 324       1.332   6.556  42.890  1.00 58.68      A    O1-
ATOM   2391  N   GLN A 325      -1.548   7.294  38.744  1.00 52.24      A    N  
ATOM   2392  CA  GLN A 325      -1.314   8.358  37.741  1.00 53.35      A    C  
ATOM   2393  C   GLN A 325      -1.197   9.762  38.380  1.00 51.74      A    C  
ATOM   2394  O   GLN A 325      -1.370  10.795  37.701  1.00 51.45      A    O  
ATOM   2395  CB  GLN A 325      -2.462   8.449  36.718  1.00 52.85      A    C  
ATOM   2396  CG  GLN A 325      -2.743   7.180  35.920  1.00 56.24      A    C  
ATOM   2397  CD  GLN A 325      -3.863   7.353  34.911  1.00 57.61      A    C  
ATOM   2398  NE2 GLN A 325      -4.968   6.645  35.125  1.00 62.12      A    N  
ATOM   2399  OE1 GLN A 325      -3.735   8.106  33.947  1.00 63.33      A    O  
ATOM   2400  N   SER A 326      -0.937   9.807  39.672  1.00 51.07      A    N  
ATOM   2401  CA  SER A 326      -0.795  11.116  40.338  1.00 50.92      A    C  
ATOM   2402  C   SER A 326       0.300  11.977  39.650  1.00 50.34      A    C  
ATOM   2403  O   SER A 326       0.196  13.237  39.588  1.00 49.50      A    O  
ATOM   2404  CB  SER A 326      -0.494  10.912  41.819  1.00 50.95      A    C  
ATOM   2405  OG  SER A 326       0.671  10.113  41.997  1.00 49.26      A    O  
ATOM   2406  N   PHE A 327       1.288  11.289  39.057  1.00 49.33      A    N  
ATOM   2407  CA  PHE A 327       2.433  11.961  38.421  1.00 48.24      A    C  
ATOM   2408  C   PHE A 327       1.934  12.886  37.377  1.00 49.03      A    C  
ATOM   2409  O   PHE A 327       2.572  13.899  37.088  1.00 49.15      A    O  
ATOM   2410  CB  PHE A 327       3.467  10.962  37.840  1.00 47.06      A    C  
ATOM   2411  CG  PHE A 327       2.982  10.212  36.578  1.00 46.71      A    C  
ATOM   2412  CD1 PHE A 327       2.436   8.936  36.675  1.00 47.26      A    C  
ATOM   2413  CD2 PHE A 327       3.099  10.791  35.312  1.00 47.28      A    C  
ATOM   2414  CE1 PHE A 327       1.973   8.219  35.492  1.00 46.55      A    C  
ATOM   2415  CE2 PHE A 327       2.670  10.109  34.147  1.00 46.49      A    C  
ATOM   2416  CZ  PHE A 327       2.099   8.824  34.245  1.00 44.73      A    C  
ATOM   2417  N   GLU A 328       0.753  12.579  36.833  1.00 50.10      A    N  
ATOM   2418  CA  GLU A 328       0.188  13.383  35.756  1.00 51.32      A    C  
ATOM   2419  C   GLU A 328       0.020  14.871  36.082  1.00 51.91      A    C  
ATOM   2420  O   GLU A 328       0.203  15.732  35.226  1.00 52.35      A    O  
ATOM   2421  CB  GLU A 328      -1.131  12.762  35.235  1.00 52.53      A    C  
ATOM   2422  CG  GLU A 328      -0.928  11.444  34.446  1.00 51.87      A    C  
ATOM   2423  CD  GLU A 328      -0.289  11.636  33.069  1.00 53.27      A    C  
ATOM   2424  OE1 GLU A 328       0.109  12.755  32.724  1.00 55.12      A    O  
ATOM   2425  OE2 GLU A 328      -0.209  10.655  32.298  1.00 57.24      A    O1-
ATOM   2426  N   SER A 329      -0.311  15.171  37.324  1.00 52.57      A    N  
ATOM   2427  CA  SER A 329      -0.515  16.559  37.741  1.00 53.50      A    C  
ATOM   2428  C   SER A 329       0.781  17.279  38.206  1.00 53.40      A    C  
ATOM   2429  O   SER A 329       0.725  18.464  38.536  1.00 53.67      A    O  
ATOM   2430  CB  SER A 329      -1.569  16.599  38.844  1.00 53.38      A    C  
ATOM   2431  OG  SER A 329      -1.182  15.803  39.959  1.00 56.08      A    O  
ATOM   2432  N   ARG A 330       1.924  16.577  38.198  1.00 52.29      A    N  
ATOM   2433  CA  ARG A 330       3.154  17.090  38.771  1.00 51.84      A    C  
ATOM   2434  C   ARG A 330       3.966  17.866  37.785  1.00 51.83      A    C  
ATOM   2435  O   ARG A 330       3.988  17.542  36.599  1.00 52.72      A    O  
ATOM   2436  CB  ARG A 330       3.992  15.976  39.389  1.00 50.83      A    C  
ATOM   2437  CG  ARG A 330       3.343  15.463  40.633  1.00 52.39      A    C  
ATOM   2438  CD  ARG A 330       4.201  14.566  41.473  1.00 56.18      A    C  
ATOM   2439  NE  ARG A 330       3.294  13.890  42.392  1.00 58.84      A    N  
ATOM   2440  CZ  ARG A 330       3.058  12.583  42.399  1.00 58.34      A    C  
ATOM   2441  NH1 ARG A 330       3.708  11.783  41.562  1.00 57.67      A    N1+
ATOM   2442  NH2 ARG A 330       2.199  12.074  43.283  1.00 58.64      A    N  
ATOM   2443  N   ASP A 331       4.619  18.911  38.294  1.00 51.34      A    N  
ATOM   2444  CA  ASP A 331       5.432  19.812  37.484  1.00 51.16      A    C  
ATOM   2445  C   ASP A 331       6.875  19.771  37.977  1.00 49.05      A    C  
ATOM   2446  O   ASP A 331       7.270  20.430  38.936  1.00 48.84      A    O  
ATOM   2447  CB  ASP A 331       4.807  21.195  37.461  1.00 52.78      A    C  
ATOM   2448  CG  ASP A 331       3.461  21.205  36.680  1.00 59.12      A    C  
ATOM   2449  OD1 ASP A 331       3.509  21.149  35.428  1.00 61.61      A    O  
ATOM   2450  OD2 ASP A 331       2.357  21.231  37.314  1.00 65.93      A    O1-
ATOM   2451  N   LEU A 332       7.628  18.901  37.338  1.00 47.46      A    N  
ATOM   2452  CA  LEU A 332       8.989  18.605  37.709  1.00 46.63      A    C  
ATOM   2453  C   LEU A 332       9.955  19.090  36.640  1.00 46.68      A    C  
ATOM   2454  O   LEU A 332       9.562  19.516  35.564  1.00 47.22      A    O  
ATOM   2455  CB  LEU A 332       9.145  17.082  37.925  1.00 45.70      A    C  
ATOM   2456  CG  LEU A 332       8.116  16.344  38.791  1.00 43.53      A    C  
ATOM   2457  CD1 LEU A 332       8.451  14.868  38.917  1.00 41.42      A    C  
ATOM   2458  CD2 LEU A 332       8.048  16.964  40.170  1.00 44.09      A    C  
ATOM   2459  N   LEU A 333      11.233  18.958  36.947  1.00 47.43      A    N  
ATOM   2460  CA  LEU A 333      12.357  19.305  36.085  1.00 47.52      A    C  
ATOM   2461  C   LEU A 333      12.711  18.127  35.207  1.00 47.69      A    C  
ATOM   2462  O   LEU A 333      12.402  16.984  35.563  1.00 47.54      A    O  
ATOM   2463  CB  LEU A 333      13.556  19.598  36.985  1.00 48.18      A    C  
ATOM   2464  CG  LEU A 333      13.453  20.869  37.843  1.00 50.36      A    C  
ATOM   2465  CD1 LEU A 333      14.801  21.153  38.530  1.00 50.93      A    C  
ATOM   2466  CD2 LEU A 333      12.998  22.074  37.001  1.00 49.94      A    C  
ATOM   2467  N   ILE A 334      13.361  18.386  34.071  1.00 46.79      A    N  
ATOM   2468  CA  ILE A 334      13.712  17.348  33.131  1.00 47.54      A    C  
ATOM   2469  C   ILE A 334      14.538  16.344  33.837  1.00 46.46      A    C  
ATOM   2470  O   ILE A 334      14.277  15.168  33.699  1.00 47.18      A    O  
ATOM   2471  CB  ILE A 334      14.539  17.832  31.893  1.00 48.02      A    C  
ATOM   2472  CG1 ILE A 334      13.689  18.564  30.893  1.00 49.81      A    C  
ATOM   2473  CG2 ILE A 334      15.052  16.632  31.084  1.00 48.18      A    C  
ATOM   2474  CD1 ILE A 334      14.497  18.955  29.614  1.00 49.28      A    C  
ATOM   2475  N   ASP A 335      15.543  16.779  34.607  1.00 46.02      A    N  
ATOM   2476  CA  ASP A 335      16.413  15.808  35.288  1.00 45.76      A    C  
ATOM   2477  C   ASP A 335      15.689  14.906  36.314  1.00 44.35      A    C  
ATOM   2478  O   ASP A 335      16.098  13.784  36.534  1.00 42.92      A    O  
ATOM   2479  CB  ASP A 335      17.598  16.521  35.935  1.00 47.64      A    C  
ATOM   2480  CG  ASP A 335      18.634  17.047  34.896  1.00 50.93      A    C  
ATOM   2481  OD1 ASP A 335      18.456  16.978  33.656  1.00 57.19      A    O  
ATOM   2482  OD2 ASP A 335      19.655  17.575  35.355  1.00 62.25      A    O1-
ATOM   2483  N   GLU A 336      14.596  15.394  36.908  1.00 43.61      A    N  
ATOM   2484  CA  GLU A 336      13.802  14.564  37.812  1.00 43.81      A    C  
ATOM   2485  C   GLU A 336      12.910  13.523  37.078  1.00 43.07      A    C  
ATOM   2486  O   GLU A 336      12.817  12.386  37.511  1.00 42.24      A    O  
ATOM   2487  CB  GLU A 336      12.920  15.442  38.687  1.00 44.41      A    C  
ATOM   2488  CG  GLU A 336      13.713  16.233  39.690  1.00 48.04      A    C  
ATOM   2489  CD  GLU A 336      12.845  17.183  40.449  1.00 51.64      A    C  
ATOM   2490  OE1 GLU A 336      11.963  17.845  39.833  1.00 48.25      A    O  
ATOM   2491  OE2 GLU A 336      13.057  17.257  41.684  1.00 57.96      A    O1-
ATOM   2492  N   TRP A 337      12.226  13.939  36.017  1.00 42.40      A    N  
ATOM   2493  CA  TRP A 337      11.536  12.972  35.136  1.00 43.05      A    C  
ATOM   2494  C   TRP A 337      12.520  11.951  34.577  1.00 43.98      A    C  
ATOM   2495  O   TRP A 337      12.255  10.744  34.549  1.00 44.17      A    O  
ATOM   2496  CB  TRP A 337      10.875  13.683  33.978  1.00 42.42      A    C  
ATOM   2497  CG  TRP A 337       9.680  14.483  34.303  1.00 41.84      A    C  
ATOM   2498  CD1 TRP A 337       9.469  15.778  33.993  1.00 42.76      A    C  
ATOM   2499  CD2 TRP A 337       8.477  14.012  34.917  1.00 43.46      A    C  
ATOM   2500  CE2 TRP A 337       7.592  15.094  34.989  1.00 42.27      A    C  
ATOM   2501  CE3 TRP A 337       8.059  12.766  35.401  1.00 43.43      A    C  
ATOM   2502  NE1 TRP A 337       8.214  16.173  34.426  1.00 44.01      A    N  
ATOM   2503  CZ2 TRP A 337       6.328  14.988  35.567  1.00 44.58      A    C  
ATOM   2504  CZ3 TRP A 337       6.799  12.674  35.986  1.00 42.60      A    C  
ATOM   2505  CH2 TRP A 337       5.953  13.770  36.046  1.00 41.48      A    C  
ATOM   2506  N   LYS A 338      13.684  12.423  34.139  1.00 44.86      A    N  
ATOM   2507  CA  LYS A 338      14.728  11.504  33.682  1.00 46.45      A    C  
ATOM   2508  C   LYS A 338      15.144  10.491  34.747  1.00 46.45      A    C  
ATOM   2509  O   LYS A 338      15.218   9.282  34.472  1.00 45.33      A    O  
ATOM   2510  CB  LYS A 338      15.967  12.295  33.183  1.00 46.57      A    C  
ATOM   2511  CG  LYS A 338      16.963  11.417  32.474  1.00 48.67      A    C  
ATOM   2512  CD  LYS A 338      18.263  12.118  32.103  1.00 50.50      A    C  
ATOM   2513  CE  LYS A 338      18.362  12.304  30.616  1.00 54.80      A    C  
ATOM   2514  NZ  LYS A 338      19.792  12.339  30.152  1.00 59.84      A    N1+
ATOM   2515  N   SER A 339      15.441  10.968  35.971  1.00 45.36      A    N  
ATOM   2516  CA  SER A 339      15.888  10.069  37.036  1.00 44.75      A    C  
ATOM   2517  C   SER A 339      14.789   9.071  37.419  1.00 43.71      A    C  
ATOM   2518  O   SER A 339      15.080   7.926  37.697  1.00 42.22      A    O  
ATOM   2519  CB  SER A 339      16.281  10.846  38.299  1.00 44.88      A    C  
ATOM   2520  OG  SER A 339      16.715   9.921  39.274  1.00 49.54      A    O  
ATOM   2521  N   LEU A 340      13.548   9.565  37.492  1.00 44.11      A    N  
ATOM   2522  CA  LEU A 340      12.363   8.734  37.724  1.00 43.90      A    C  
ATOM   2523  C   LEU A 340      12.273   7.653  36.658  1.00 43.20      A    C  
ATOM   2524  O   LEU A 340      11.980   6.504  36.964  1.00 43.35      A    O  
ATOM   2525  CB  LEU A 340      11.104   9.609  37.702  1.00 44.74      A    C  
ATOM   2526  CG  LEU A 340      10.812  10.476  38.927  1.00 44.94      A    C  
ATOM   2527  CD1 LEU A 340       9.585  11.334  38.621  1.00 48.34      A    C  
ATOM   2528  CD2 LEU A 340      10.553   9.577  40.145  1.00 47.92      A    C  
ATOM   2529  N   THR A 341      12.560   8.011  35.401  1.00 41.41      A    N  
ATOM   2530  CA  THR A 341      12.558   7.017  34.306  1.00 41.32      A    C  
ATOM   2531  C   THR A 341      13.680   6.000  34.499  1.00 42.18      A    C  
ATOM   2532  O   THR A 341      13.471   4.787  34.410  1.00 41.01      A    O  
ATOM   2533  CB  THR A 341      12.631   7.686  32.924  1.00 40.34      A    C  
ATOM   2534  CG2 THR A 341      12.619   6.668  31.841  1.00 40.86      A    C  
ATOM   2535  OG1 THR A 341      11.489   8.552  32.765  1.00 41.40      A    O  
ATOM   2536  N   TYR A 342      14.868   6.478  34.812  1.00 42.40      A    N  
ATOM   2537  CA  TYR A 342      15.955   5.568  35.115  1.00 43.97      A    C  
ATOM   2538  C   TYR A 342      15.619   4.600  36.266  1.00 44.10      A    C  
ATOM   2539  O   TYR A 342      15.913   3.420  36.157  1.00 44.80      A    O  
ATOM   2540  CB  TYR A 342      17.180   6.370  35.480  1.00 45.14      A    C  
ATOM   2541  CG  TYR A 342      18.441   5.568  35.518  1.00 48.33      A    C  
ATOM   2542  CD1 TYR A 342      18.969   5.020  34.349  1.00 46.86      A    C  
ATOM   2543  CD2 TYR A 342      19.151   5.394  36.725  1.00 51.33      A    C  
ATOM   2544  CE1 TYR A 342      20.171   4.330  34.359  1.00 48.75      A    C  
ATOM   2545  CE2 TYR A 342      20.337   4.661  36.747  1.00 51.58      A    C  
ATOM   2546  CZ  TYR A 342      20.851   4.151  35.555  1.00 50.63      A    C  
ATOM   2547  OH  TYR A 342      22.036   3.418  35.535  1.00 49.83      A    O  
ATOM   2548  N   ASP A 343      14.959   5.084  37.328  1.00 45.32      A    N  
ATOM   2549  CA  ASP A 343      14.521   4.230  38.466  1.00 46.04      A    C  
ATOM   2550  C   ASP A 343      13.664   3.050  37.939  1.00 46.20      A    C  
ATOM   2551  O   ASP A 343      13.821   1.878  38.364  1.00 45.06      A    O  
ATOM   2552  CB  ASP A 343      13.704   5.040  39.511  1.00 47.51      A    C  
ATOM   2553  CG  ASP A 343      14.572   6.029  40.379  1.00 53.59      A    C  
ATOM   2554  OD1 ASP A 343      15.827   5.891  40.442  1.00 50.68      A    O  
ATOM   2555  OD2 ASP A 343      13.953   6.941  41.022  1.00 57.53      A    O1-
ATOM   2556  N   GLU A 344      12.752   3.368  37.011  1.00 45.20      A    N  
ATOM   2557  CA  GLU A 344      11.846   2.356  36.426  1.00 44.89      A    C  
ATOM   2558  C   GLU A 344      12.551   1.365  35.487  1.00 44.82      A    C  
ATOM   2559  O   GLU A 344      12.155   0.199  35.383  1.00 43.61      A    O  
ATOM   2560  CB  GLU A 344      10.650   3.045  35.743  1.00 45.13      A    C  
ATOM   2561  CG  GLU A 344       9.769   3.857  36.709  1.00 45.90      A    C  
ATOM   2562  CD  GLU A 344       8.826   3.010  37.588  1.00 51.13      A    C  
ATOM   2563  OE1 GLU A 344       8.460   1.864  37.210  1.00 51.18      A    O  
ATOM   2564  OE2 GLU A 344       8.451   3.494  38.669  1.00 50.53      A    O1-
ATOM   2565  N   VAL A 345      13.623   1.812  34.819  1.00 44.70      A    N  
ATOM   2566  CA  VAL A 345      14.396   0.933  33.945  1.00 44.63      A    C  
ATOM   2567  C   VAL A 345      15.109  -0.092  34.780  1.00 46.69      A    C  
ATOM   2568  O   VAL A 345      15.056  -1.286  34.471  1.00 46.58      A    O  
ATOM   2569  CB  VAL A 345      15.467   1.714  33.048  1.00 44.30      A    C  
ATOM   2570  CG1 VAL A 345      16.294   0.749  32.242  1.00 41.27      A    C  
ATOM   2571  CG2 VAL A 345      14.746   2.686  32.097  1.00 45.35      A    C  
ATOM   2572  N   ILE A 346      15.816   0.392  35.805  1.00 47.74      A    N  
ATOM   2573  CA  ILE A 346      16.597  -0.448  36.729  1.00 50.39      A    C  
ATOM   2574  C   ILE A 346      15.783  -1.480  37.478  1.00 50.76      A    C  
ATOM   2575  O   ILE A 346      16.230  -2.626  37.646  1.00 52.11      A    O  
ATOM   2576  CB  ILE A 346      17.337   0.432  37.818  1.00 49.61      A    C  
ATOM   2577  CG1 ILE A 346      18.330   1.351  37.153  1.00 51.11      A    C  
ATOM   2578  CG2 ILE A 346      18.015  -0.431  38.887  1.00 52.29      A    C  
ATOM   2579  CD1 ILE A 346      19.032   0.717  35.964  1.00 50.58      A    C  
ATOM   2580  N   SER A 347      14.603  -1.068  37.922  1.00 50.72      A    N  
ATOM   2581  CA  SER A 347      13.732  -1.905  38.731  1.00 51.67      A    C  
ATOM   2582  C   SER A 347      12.887  -2.898  37.931  1.00 52.36      A    C  
ATOM   2583  O   SER A 347      12.137  -3.702  38.519  1.00 52.22      A    O  
ATOM   2584  CB  SER A 347      12.819  -1.014  39.598  1.00 51.97      A    C  
ATOM   2585  OG  SER A 347      11.805  -0.347  38.838  1.00 49.88      A    O  
ATOM   2586  N   PHE A 348      12.992  -2.837  36.604  1.00 52.55      A    N  
ATOM   2587  CA  PHE A 348      12.223  -3.737  35.716  1.00 52.69      A    C  
ATOM   2588  C   PHE A 348      12.504  -5.222  35.954  1.00 54.29      A    C  
ATOM   2589  O   PHE A 348      13.662  -5.644  35.992  1.00 54.64      A    O  
ATOM   2590  CB  PHE A 348      12.445  -3.415  34.238  1.00 50.95      A    C  
ATOM   2591  CG  PHE A 348      11.658  -4.314  33.309  1.00 48.77      A    C  
ATOM   2592  CD1 PHE A 348      10.299  -4.095  33.115  1.00 47.27      A    C  
ATOM   2593  CD2 PHE A 348      12.267  -5.382  32.653  1.00 46.09      A    C  
ATOM   2594  CE1 PHE A 348       9.537  -4.929  32.277  1.00 46.89      A    C  
ATOM   2595  CE2 PHE A 348      11.508  -6.244  31.814  1.00 44.01      A    C  
ATOM   2596  CZ  PHE A 348      10.154  -5.997  31.625  1.00 45.74      A    C  
ATOM   2597  N   VAL A 349      11.432  -6.009  36.085  1.00 55.73      A    N  
ATOM   2598  CA  VAL A 349      11.554  -7.469  36.128  1.00 57.59      A    C  
ATOM   2599  C   VAL A 349      10.692  -8.107  35.029  1.00 58.01      A    C  
ATOM   2600  O   VAL A 349       9.480  -7.831  34.961  1.00 57.00      A    O  
ATOM   2601  CB  VAL A 349      11.105  -8.048  37.506  1.00 57.61      A    C  
ATOM   2602  CG1 VAL A 349      11.444  -9.540  37.600  1.00 58.81      A    C  
ATOM   2603  CG2 VAL A 349      11.736  -7.258  38.675  1.00 58.97      A    C  
ATOM   2604  N   PRO A 350      11.301  -8.969  34.189  1.00 59.17      A    N  
ATOM   2605  CA  PRO A 350      10.605  -9.676  33.106  1.00 60.89      A    C  
ATOM   2606  C   PRO A 350       9.419 -10.528  33.596  1.00 62.08      A    C  
ATOM   2607  O   PRO A 350       9.364 -10.856  34.775  1.00 62.39      A    O  
ATOM   2608  CB  PRO A 350      11.688 -10.592  32.539  1.00 61.26      A    C  
ATOM   2609  CG  PRO A 350      12.986  -9.940  32.917  1.00 60.65      A    C  
ATOM   2610  CD  PRO A 350      12.732  -9.324  34.251  1.00 59.23      A    C  
ATOM   2611  N   PRO A 351       8.473 -10.887  32.695  1.00 63.51      A    N  
ATOM   2612  CA  PRO A 351       7.344 -11.768  33.092  1.00 64.24      A    C  
ATOM   2613  C   PRO A 351       7.729 -13.229  33.408  1.00 64.62      A    C  
ATOM   2614  O   PRO A 351       8.850 -13.661  33.123  1.00 65.49      A    O  
ATOM   2615  CB  PRO A 351       6.409 -11.720  31.879  1.00 64.22      A    C  
ATOM   2616  CG  PRO A 351       7.310 -11.437  30.722  1.00 64.17      A    C  
ATOM   2617  CD  PRO A 351       8.382 -10.498  31.274  1.00 63.85      A    C  
TER   
END


A second structure was input as follows:


ATOM      1  N   GLU A   4      26.246  -7.913  35.721  1.00 73.88      A    N  
ANISOU    1  N   GLU A   4     8980   9232   9859    957  -1257   -886  A    N  
ATOM      2  CA  GLU A   4      25.351  -8.714  34.839  1.00 59.19      A    C  
ANISOU    2  CA  GLU A   4     7179   7365   7948    951  -1224   -834  A    C  
ATOM      3  C   GLU A   4      24.830  -7.938  33.610  1.00 66.13      A    C  
ANISOU    3  C   GLU A   4     7960   8338   8828    887  -1042   -792  A    C  
ATOM      4  O   GLU A   4      23.934  -8.423  32.915  1.00 57.01      A    O  
ANISOU    4  O   GLU A   4     6857   7178   7626    867  -1000   -736  A    O  
ATOM      5  CB  GLU A   4      24.164  -9.256  35.650  1.00 51.89      A    C  
ANISOU    5  CB  GLU A   4     6449   6344   6925    902  -1272   -725  A    C  
ATOM      6  N   ARG A   5      25.395  -6.758  33.328  1.00 61.05      A    N  
ANISOU    6  N   ARG A   5     7184   7774   8239    853   -939   -822  A    N  
ATOM      7  CA  ARG A   5      24.970  -5.951  32.167  1.00 48.13      A    C  
ANISOU    7  CA  ARG A   5     5468   6221   6601    789   -773   -783  A    C  
ATOM      8  C   ARG A   5      25.335  -6.652  30.866  1.00 40.74      A    C  
ANISOU    8  C   ARG A   5     4460   5337   5684    843   -753   -847  A    C  
ATOM      9  O   ARG A   5      26.488  -7.011  30.671  1.00 37.79      A    O  
ANISOU    9  O   ARG A   5     3991   4994   5374    914   -806   -965  A    O  
ATOM     10  CB  ARG A   5      25.630  -4.573  32.171  1.00 38.34      A    C  
ANISOU   10  CB  ARG A   5     4107   5045   5415    741   -678   -808  A    C  
ATOM     11  CG  ARG A   5      25.370  -3.721  30.927  1.00 42.83      A    C  
ANISOU   11  CG  ARG A   5     4596   5696   5981    678   -515   -777  A    C  
ATOM     12  CD  ARG A   5      26.079  -2.383  31.062  1.00 53.52      A    C  
ANISOU   12  CD  ARG A   5     5844   7099   7389    624   -436   -803  A    C  
ATOM     13  NE  ARG A   5      25.911  -1.485  29.914  1.00 50.22      A    N  
ANISOU   13  NE  ARG A   5     5363   6752   6965    555   -282   -771  A    N  
ATOM     14  CZ  ARG A   5      26.544  -1.598  28.743  1.00 54.76      A    C  
ANISOU   14  CZ  ARG A   5     5843   7401   7562    564   -214   -836  A    C  
ATOM     15  NH1 ARG A   5      27.370  -2.618  28.489  1.00 55.20      A    N1+
ANISOU   15  NH1 ARG A   5     5840   7479   7656    647   -283   -943  A    N1+
ATOM     16  NH2 ARG A   5      26.334  -0.691  27.799  1.00 41.08      A    N  
ANISOU   16  NH2 ARG A   5     4077   5720   5810    489    -76   -795  A    N  
ATOM     17  N   PRO A   6      24.363  -6.807  29.948  1.00 36.11      A    N  
ANISOU   17  N   PRO A   6     3911   4763   5044    811   -675   -779  A    N  
ATOM     18  CA  PRO A   6      24.685  -7.478  28.684  1.00 35.53      A    C  
ANISOU   18  CA  PRO A   6     3777   4742   4982    863   -655   -843  A    C  
ATOM     19  C   PRO A   6      25.682  -6.678  27.837  1.00 25.99      A    C  
ANISOU   19  C   PRO A   6     2407   3640   3828    851   -547   -920  A    C  
ATOM     20  O   PRO A   6      25.874  -5.475  28.085  1.00 33.12      A    O  
ANISOU   20  O   PRO A   6     3258   4574   4751    783   -465   -898  A    O  
ATOM     21  CB  PRO A   6      23.318  -7.546  27.943  1.00 42.14      A    C  
ANISOU   21  CB  PRO A   6     4693   5572   5748    814   -580   -739  A    C  
ATOM     22  CG  PRO A   6      22.289  -6.999  28.865  1.00 40.99      A    C  
ANISOU   22  CG  PRO A   6     4646   5370   5558    741   -569   -632  A    C  
ATOM     23  CD  PRO A   6      22.991  -6.252  29.963  1.00 38.50      A    C  
ANISOU   23  CD  PRO A   6     4299   5048   5282    726   -593   -655  A    C  
ATOM     24  N   THR A   7      26.259  -7.330  26.840  1.00 27.92      A    N  
ANISOU   24  N   THR A   7     2578   3938   4093    909   -541  -1009  A    N  
ATOM     25  CA  THR A   7      27.076  -6.658  25.837  1.00 32.78      A    C  
ANISOU   25  CA  THR A   7     3050   4661   4743    883   -417  -1079  A    C  
ATOM     26  C   THR A   7      26.186  -6.125  24.726  1.00 37.60      A    C  
ANISOU   26  C   THR A   7     3689   5310   5286    813   -279   -990  A    C  
ATOM     27  O   THR A   7      25.304  -6.841  24.246  1.00 29.03      A    O  
ANISOU   27  O   THR A   7     2690   4193   4146    833   -298   -941  A    O  
ATOM     28  CB  THR A   7      28.096  -7.619  25.228  1.00 43.74      A    C  
ANISOU   28  CB  THR A   7     4343   6097   6180    980   -471  -1227  A    C  
ATOM     29  CG2 THR A   7      28.864  -6.963  24.078  1.00 35.93      A    C  
ANISOU   29  CG2 THR A   7     3208   5230   5213    941   -320  -1299  A    C  
ATOM     30  OG1 THR A   7      29.016  -8.020  26.240  1.00 46.09      A    O  
ANISOU   30  OG1 THR A   7     4603   6360   6549   1050   -606  -1322  A    O  
ATOM     31  N   PHE A   8      26.392  -4.862  24.357  1.00 29.77      A    N  
ANISOU   31  N   PHE A   8     2635   4377   4298    728   -146   -968  A    N  
ATOM     32  CA  PHE A   8      25.608  -4.219  23.298  1.00 28.02      A    C  
ANISOU   32  CA  PHE A   8     2448   4188   4012    657    -16   -884  A    C  
ATOM     33  C   PHE A   8      26.325  -4.219  21.958  1.00 35.77      A    C  
ANISOU   33  C   PHE A   8     3335   5268   4990    653     84   -962  A    C  
ATOM     34  O   PHE A   8      27.560  -4.336  21.875  1.00 32.93      A    O  
ANISOU   34  O   PHE A   8     2851   4969   4691    680     90  -1085  A    O  
ATOM     35  CB  PHE A   8      25.271  -2.774  23.692  1.00 29.26      A    C  
ANISOU   35  CB  PHE A   8     2620   4336   4162    556     65   -798  A    C  
ATOM     36  CG  PHE A   8      24.196  -2.668  24.738  1.00 24.63      A    C  
ANISOU   36  CG  PHE A   8     2147   3659   3551    543     -1   -699  A    C  
ATOM     37  CD1 PHE A   8      24.414  -3.111  26.049  1.00 28.52      A    C  
ANISOU   37  CD1 PHE A   8     2662   4095   4079    585   -120   -721  A    C  
ATOM     38  CD2 PHE A   8      22.989  -2.109  24.416  1.00 25.04      A    C  
ANISOU   38  CD2 PHE A   8     2283   3686   3543    487     56   -590  A    C  
ATOM     39  CE1 PHE A   8      23.429  -2.999  27.004  1.00 28.97      A    C  
ANISOU   39  CE1 PHE A   8     2824   4077   4105    561   -168   -633  A    C  
ATOM     40  CE2 PHE A   8      21.985  -1.976  25.365  1.00 27.76      A    C  
ANISOU   40  CE2 PHE A   8     2721   3959   3869    468      7   -510  A    C  
ATOM     41  CZ  PHE A   8      22.190  -2.434  26.663  1.00 24.35      A    C  
ANISOU   41  CZ  PHE A   8     2313   3476   3464    501   -100   -530  A    C  
ATOM     42  N   TYR A   9      25.543  -4.108  20.900  1.00 29.73      A    N  
ANISOU   42  N   TYR A   9     2628   4518   4151    622    162   -897  A    N  
ATOM     43  CA  TYR A   9      26.068  -3.844  19.585  1.00 31.80      A    C  
ANISOU   43  CA  TYR A   9     2824   4872   4388    592    284   -945  A    C  
ATOM     44  C   TYR A   9      25.283  -2.744  18.921  1.00 35.42      A    C  
ANISOU   44  C   TYR A   9     3353   5332   4775    496    400   -832  A    C  
ATOM     45  O   TYR A   9      24.089  -2.532  19.201  1.00 26.54      A    O  
ANISOU   45  O   TYR A   9     2339   4135   3610    479    370   -722  A    O  
ATOM     46  CB  TYR A   9      26.135  -5.116  18.698  1.00 29.77      A    C  
ANISOU   46  CB  TYR A   9     2561   4644   4105    677    249  -1017  A    C  
ATOM     47  CG  TYR A   9      24.826  -5.707  18.188  1.00 32.49      A    C  
ANISOU   47  CG  TYR A   9     3034   4936   4376    702    216   -931  A    C  
ATOM     48  CD1 TYR A   9      23.955  -6.366  19.052  1.00 31.02      A    C  
ANISOU   48  CD1 TYR A   9     2942   4653   4191    744     92   -872  A    C  
ATOM     49  CD2 TYR A   9      24.496  -5.653  16.848  1.00 28.62      A    C  
ANISOU   49  CD2 TYR A   9     2569   4491   3813    682    306   -914  A    C  
ATOM     50  CE1 TYR A   9      22.785  -6.937  18.576  1.00 27.36      A    C  
ANISOU   50  CE1 TYR A   9     2583   4144   3668    764     63   -805  A    C  
ATOM     51  CE2 TYR A   9      23.331  -6.214  16.357  1.00 29.96      A    C  
ANISOU   51  CE2 TYR A   9     2848   4614   3921    710    268   -847  A    C  
ATOM     52  CZ  TYR A   9      22.473  -6.865  17.218  1.00 29.37      A    C  
ANISOU   52  CZ  TYR A   9     2855   4446   3858    751    147   -794  A    C  
ATOM     53  OH  TYR A   9      21.321  -7.419  16.703  1.00 27.22      A    O  
ANISOU   53  OH  TYR A   9     2682   4130   3531    772    114   -735  A    O  
ATOM     54  N   ARG A  10      25.978  -2.041  18.040  1.00 33.30      A    N  
ANISOU   54  N   ARG A  10     3018   5144   4491    431    529   -868  A    N  
ATOM     55  CA  ARG A  10      25.472  -0.869  17.395  1.00 37.42      A    C  
ANISOU   55  CA  ARG A  10     3602   5668   4949    330    642   -773  A    C  
ATOM     56  C   ARG A  10      25.327  -1.096  15.923  1.00 33.08      A    C  
ANISOU   56  C   ARG A  10     3081   5170   4316    323    724   -779  A    C  
ATOM     57  O   ARG A  10      26.228  -1.630  15.263  1.00 36.93      A    O  
ANISOU   57  O   ARG A  10     3481   5740   4809    346    766   -888  A    O  
ATOM     58  CB  ARG A  10      26.414   0.319  17.646  1.00 43.84      A    C  
ANISOU   58  CB  ARG A  10     4331   6521   5806    237    732   -797  A    C  
ATOM     59  CG  ARG A  10      26.103   1.534  16.774  1.00 57.96      A    C  
ANISOU   59  CG  ARG A  10     6182   8320   7521    125    861   -715  A    C  
ATOM     60  CD  ARG A  10      26.148   2.848  17.535  1.00 81.06      A    C  
ANISOU   60  CD  ARG A  10     9111  11207  10481     39    888   -655  A    C  
ATOM     61  NE  ARG A  10      27.406   3.076  18.239  1.00 82.56      A    N  
ANISOU   61  NE  ARG A  10     9165  11439  10766     21    898   -753  A    N  
ATOM     62  CZ  ARG A  10      27.818   4.265  18.672  1.00 94.81      A    C  
ANISOU   62  CZ  ARG A  10    10688  12983  12352    -70    951   -733  A    C  
ATOM     63  NH1 ARG A  10      28.981   4.367  19.301  1.00111.76      A    N1+
ANISOU   63  NH1 ARG A  10    12700  15171  14591    -77    950   -835  A    N1+
ATOM     64  NH2 ARG A  10      27.078   5.356  18.477  1.00 90.48      A    N  
ANISOU   64  NH2 ARG A  10    10244  12384  11750   -150    997   -617  A    N  
ATOM     65  N   GLN A  11      24.186  -0.692  15.388  1.00 41.84      A    N  
ANISOU   65  N   GLN A  11     4316   6234   5347    292    744   -667  A    N  
ATOM     66  CA  GLN A  11      24.011  -0.646  13.967  1.00 37.89      A    C  
ANISOU   66  CA  GLN A  11     3865   5777   4755    266    832   -656  A    C  
ATOM     67  C   GLN A  11      23.130   0.522  13.577  1.00 42.27      A    C  
ANISOU   67  C   GLN A  11     4538   6284   5241    184    885   -531  A    C  
ATOM     68  O   GLN A  11      22.367   1.073  14.389  1.00 33.97      A    O  
ANISOU   68  O   GLN A  11     3541   5155   4210    169    832   -450  A    O  
ATOM     69  CB  GLN A  11      23.426  -1.959  13.455  1.00 36.16      A    C  
ANISOU   69  CB  GLN A  11     3689   5549   4502    365    756   -678  A    C  
ATOM     70  CG  GLN A  11      22.009  -2.203  13.875  1.00 33.96      A    C  
ANISOU   70  CG  GLN A  11     3522   5172   4207    402    657   -581  A    C  
ATOM     71  CD  GLN A  11      21.543  -3.580  13.525  1.00 33.02      A    C  
ANISOU   71  CD  GLN A  11     3432   5039   4073    500    571   -614  A    C  
ATOM     72  NE2 GLN A  11      21.485  -3.880  12.235  1.00 32.10      A    N  
ANISOU   72  NE2 GLN A  11     3345   4968   3884    513    622   -634  A    N  
ATOM     73  OE1 GLN A  11      21.236  -4.381  14.411  1.00 40.37      A    O  
ANISOU   73  OE1 GLN A  11     4367   5919   5055    563    457   -622  A    O  
ATOM     74  N   GLU A  12      23.247   0.911  12.319  1.00 40.43      A    N  
ANISOU   74  N   GLU A  12     4345   6095   4921    129    990   -523  A    N  
ATOM     75  CA  GLU A  12      22.410   1.940  11.779  1.00 37.48      A    C  
ANISOU   75  CA  GLU A  12     4100   5670   4469     61   1031   -410  A    C  
ATOM     76  C   GLU A  12      21.253   1.288  11.068  1.00 38.55      A    C  
ANISOU   76  C   GLU A  12     4346   5766   4534    126    971   -365  A    C  
ATOM     77  O   GLU A  12      21.444   0.421  10.222  1.00 37.95      A    O  
ANISOU   77  O   GLU A  12     4262   5741   4416    173    985   -422  A    O  
ATOM     78  CB  GLU A  12      23.182   2.838  10.817  1.00 43.47      A    C  
ANISOU   78  CB  GLU A  12     4864   6489   5163    -50   1178   -415  A    C  
ATOM     79  CG  GLU A  12      22.630   4.253  10.773  1.00 70.04      A    C  
ANISOU   79  CG  GLU A  12     8340   9786   8485   -145   1212   -301  A    C  
ATOM     80  CD  GLU A  12      22.791   4.902   9.418  1.00106.69      A    C  
ANISOU   80  CD  GLU A  12    13072  14457  13008   -234   1331   -270  A    C  
ATOM     81  OE1 GLU A  12      23.073   6.121   9.379  1.00135.03      A    O  
ANISOU   81  OE1 GLU A  12    16698  18027  16579   -345   1403   -221  A    O  
ATOM     82  OE2 GLU A  12      22.623   4.192   8.396  1.00 52.55      A    O1-
ANISOU   82  OE2 GLU A  12     6257   7635   6072   -195   1348   -294  A    O1-
ATOM     83  N   LEU A  13      20.047   1.702  11.429  1.00 36.11      A    N  
ANISOU   83  N   LEU A  13     4134   5367   4219    131    902   -270  A    N  
ATOM     84  CA  LEU A  13      18.818   1.207  10.810  1.00 47.66      A    C  
ANISOU   84  CA  LEU A  13     5703   6782   5623    190    838   -224  A    C  
ATOM     85  C   LEU A  13      17.899   2.387  10.528  1.00 57.95      A    C  
ANISOU   85  C   LEU A  13     7129   8015   6875    134    843   -121  A    C  
ATOM     86  O   LEU A  13      17.757   3.269  11.373  1.00 40.31      A    O  
ANISOU   86  O   LEU A  13     4893   5736   4686     91    832    -77  A    O  
ATOM     87  CB  LEU A  13      18.107   0.260  11.765  1.00 63.42      A    C  
ANISOU   87  CB  LEU A  13     7680   8729   7687    275    713   -231  A    C  
ATOM     88  CG  LEU A  13      18.705  -1.135  11.861  1.00 60.65      A    C  
ANISOU   88  CG  LEU A  13     7247   8424   7372    354    672   -326  A    C  
ATOM     89  CD1 LEU A  13      18.735  -1.589  13.310  1.00 62.76      A    C  
ANISOU   89  CD1 LEU A  13     7456   8656   7736    390    583   -343  A    C  
ATOM     90  CD2 LEU A  13      17.905  -2.099  11.001  1.00 63.00      A    C  
ANISOU   90  CD2 LEU A  13     7612   8709   7617    425    621   -329  A    C  
ATOM     91  N   LYS A  15      18.412   4.975   8.956  1.00 47.30      A    N  
ANISOU   91  N   LYS A  15     5948   6658   5368    -74   1037    -13  A    N  
ATOM     92  CA  LYS A  15      19.152   6.198   9.206  1.00 47.49      A    C  
ANISOU   92  CA  LYS A  15     5960   6683   5401   -185   1119     11  A    C  
ATOM     93  C   LYS A  15      19.126   6.673  10.666  1.00 51.01      A    C  
ANISOU   93  C   LYS A  15     6336   7086   5958   -190   1066     23  A    C  
ATOM     94  O   LYS A  15      19.225   7.863  10.952  1.00 47.39      A    O  
ANISOU   94  O   LYS A  15     5912   6587   5506   -270   1093     72  A    O  
ATOM     95  CB  LYS A  15      18.635   7.269   8.246  1.00 45.05      A    C  
ANISOU   95  CB  LYS A  15     5818   6316   4983   -255   1150    100  A    C  
ATOM     96  CG  LYS A  15      18.607   6.746   6.809  1.00 51.85      A    C  
ANISOU   96  CG  LYS A  15     6761   7217   5723   -245   1196     88  A    C  
ATOM     97  CD  LYS A  15      18.944   7.809   5.798  1.00 38.99      A    C  
ANISOU   97  CD  LYS A  15     5257   5581   3980   -362   1298    141  A    C  
ATOM     98  CE  LYS A  15      19.254   7.205   4.422  1.00 36.66      A    C  
ANISOU   98  CE  LYS A  15     5013   5352   3562   -365   1372    107  A    C  
ATOM     99  NZ  LYS A  15      19.141   8.264   3.384  1.00 61.94      A    N1+
ANISOU   99  NZ  LYS A  15     8396   8509   6628   -465   1434    187  A    N1+
ATOM    100  N   THR A  16      19.052   5.732  11.599  1.00 57.64      A    N  
ANISOU  100  N   THR A  16     7083   7936   6883   -108    990    -27  A    N  
ATOM    101  CA  THR A  16      19.280   6.068  12.998  1.00 69.65      A    C  
ANISOU  101  CA  THR A  16     8523   9435   8505   -115    951    -34  A    C  
ATOM    102  C   THR A  16      20.036   4.948  13.722  1.00 56.48      A    C  
ANISOU  102  C   THR A  16     6721   7824   6915    -55    923   -128  A    C  
ATOM    103  O   THR A  16      19.925   3.769  13.366  1.00 41.32      A    O  
ANISOU  103  O   THR A  16     4785   5932   4982     21    889   -173  A    O  
ATOM    104  CB  THR A  16      17.967   6.448  13.726  1.00 62.33      A    C  
ANISOU  104  CB  THR A  16     7665   8414   7604    -83    851     35  A    C  
ATOM    105  CG2 THR A  16      16.878   5.400  13.512  1.00 55.58      A    C  
ANISOU  105  CG2 THR A  16     6854   7534   6731     11    765     38  A    C  
ATOM    106  OG1 THR A  16      18.219   6.597  15.127  1.00 63.20      A    O  
ANISOU  106  OG1 THR A  16     7694   8510   7809    -82    813     17  A    O  
ATOM    107  N   ILE A  17      20.816   5.354  14.720  1.00 57.09      A    N  
ANISOU  107  N   ILE A  17     6707   7913   7072    -87    933   -159  A    N  
ATOM    108  CA  ILE A  17      21.613   4.439  15.521  1.00 49.36      A    C  
ANISOU  108  CA  ILE A  17     5603   6978   6173    -32    894   -250  A    C  
ATOM    109  C   ILE A  17      20.720   3.561  16.433  1.00 48.06      A    C  
ANISOU  109  C   ILE A  17     5456   6759   6047     60    766   -240  A    C  
ATOM    110  O   ILE A  17      19.825   4.046  17.143  1.00 41.30      A    O  
ANISOU  110  O   ILE A  17     4655   5833   5206     56    712   -174  A    O  
ATOM    111  CB  ILE A  17      22.610   5.211  16.405  1.00 69.05      A    C  
ANISOU  111  CB  ILE A  17     8005   9488   8745    -92    927   -284  A    C  
ATOM    112  CG1 ILE A  17      23.658   5.925  15.546  1.00 88.75      A    C  
ANISOU  112  CG1 ILE A  17    10462  12050  11212   -191   1061   -315  A    C  
ATOM    113  CG2 ILE A  17      23.293   4.267  17.382  1.00 61.11      A    C  
ANISOU  113  CG2 ILE A  17     6885   8509   7826    -21    857   -376  A    C  
ATOM    114  CD1 ILE A  17      24.401   7.030  16.277  1.00 77.73      A    C  
ANISOU  114  CD1 ILE A  17     9006  10649   9879   -275   1102   -319  A    C  
ATOM    115  N   TRP A  18      20.953   2.262  16.380  1.00 35.71      A    N  
ANISOU  115  N   TRP A  18     3847   5226   4496    139    720   -307  A    N  
ATOM    116  CA  TRP A  18      20.372   1.328  17.313  1.00 26.19      A    C  
ANISOU  116  CA  TRP A  18     2648   3975   3332    217    603   -312  A    C  
ATOM    117  C   TRP A  18      21.459   0.611  18.052  1.00 32.04      A    C  
ANISOU  117  C   TRP A  18     3280   4750   4143    259    564   -408  A    C  
ATOM    118  O   TRP A  18      22.352  -0.005  17.450  1.00 31.41      A    O  
ANISOU  118  O   TRP A  18     3131   4736   4067    286    593   -493  A    O  
ATOM    119  CB  TRP A  18      19.535   0.345  16.618  1.00 23.39      A    C  
ANISOU  119  CB  TRP A  18     2356   3605   2926    280    559   -302  A    C  
ATOM    120  CG  TRP A  18      18.259   0.944  16.119  1.00 31.26      A    C  
ANISOU  120  CG  TRP A  18     3464   4549   3865    256    562   -211  A    C  
ATOM    121  CD1 TRP A  18      18.132   1.977  15.235  1.00 40.20      A    C  
ANISOU  121  CD1 TRP A  18     4651   5684   4939    192    639   -163  A    C  
ATOM    122  CD2 TRP A  18      16.926   0.594  16.528  1.00 28.58      A    C  
ANISOU  122  CD2 TRP A  18     3193   4141   3525    292    478   -161  A    C  
ATOM    123  CE2 TRP A  18      16.047   1.438  15.818  1.00 32.43      A    C  
ANISOU  123  CE2 TRP A  18     3767   4596   3958    258    505    -93  A    C  
ATOM    124  CE3 TRP A  18      16.387  -0.390  17.387  1.00 23.08      A    C  
ANISOU  124  CE3 TRP A  18     2498   3406   2864    347    384   -171  A    C  
ATOM    125  NE1 TRP A  18      16.809   2.274  15.041  1.00 42.63      A    N  
ANISOU  125  NE1 TRP A  18     5058   5928   5213    199    599    -91  A    N  
ATOM    126  CZ2 TRP A  18      14.662   1.365  15.952  1.00 25.75      A    C  
ANISOU  126  CZ2 TRP A  18     2993   3688   3105    282    440    -44  A    C  
ATOM    127  CZ3 TRP A  18      15.009  -0.448  17.556  1.00 23.05      A    C  
ANISOU  127  CZ3 TRP A  18     2568   3343   2849    357    331   -117  A    C  
ATOM    128  CH2 TRP A  18      14.146   0.393  16.800  1.00 22.80      A    C  
ANISOU  128  CH2 TRP A  18     2606   3286   2771    329    359    -61  A    C  
ATOM    129  N   GLU A  19      21.392   0.696  19.367  1.00 28.60      A    N  
ANISOU  129  N   GLU A  19     2833   4267   3765    267    495   -399  A    N  
ATOM    130  CA AGLU A  19      22.371   0.046  20.213  0.60 22.87      A    C  
ANISOU  130  CA AGLU A  19     2019   3559   3110    315    435   -487  A    C  
ATOM    131  CA BGLU A  19      22.360   0.067  20.251  0.40 24.27      A    C  
ANISOU  131  CA BGLU A  19     2197   3735   3288    314    433   -486  A    C  
ATOM    132  C   GLU A  19      21.591  -0.860  21.171  1.00 26.65      A    C  
ANISOU  132  C   GLU A  19     2558   3969   3600    377    311   -464  A    C  
ATOM    133  O   GLU A  19      20.865  -0.374  22.063  1.00 24.51      A    O  
ANISOU  133  O   GLU A  19     2340   3639   3333    352    279   -399  A    O  
ATOM    134  CB AGLU A  19      23.226   1.071  20.984  0.60 27.78      A    C  
ANISOU  134  CB AGLU A  19     2569   4194   3792    256    467   -507  A    C  
ATOM    135  CB BGLU A  19      23.047   1.115  21.122  0.40 25.86      A    C  
ANISOU  135  CB BGLU A  19     2341   3938   3547    256    458   -493  A    C  
ATOM    136  CG AGLU A  19      24.415   0.435  21.723  0.60 24.30      A    C  
ANISOU  136  CG AGLU A  19     2023   3780   3429    308    407   -618  A    C  
ATOM    137  CG BGLU A  19      23.684   2.251  20.362  0.40 27.26      A    C  
ANISOU  137  CG BGLU A  19     2475   4167   3714    168    583   -495  A    C  
ATOM    138  CD AGLU A  19      25.509   1.413  22.141  0.60 29.47      A    C  
ANISOU  138  CD AGLU A  19     2579   4471   4146    249    461   -667  A    C  
ATOM    139  CD BGLU A  19      24.252   3.305  21.296  0.40 26.81      A    C  
ANISOU  139  CD BGLU A  19     2369   4100   3719    108    597   -496  A    C  
ATOM    140  OE1AGLU A  19      25.427   2.603  21.784  0.60 42.37      A    O  
ANISOU  140  OE1AGLU A  19     4225   6111   5761    159    554   -614  A    O  
ATOM    141  OE1BGLU A  19      25.421   3.155  21.709  0.40 39.39      A    O  
ANISOU  141  OE1BGLU A  19     3852   5734   5379    119    592   -591  A    O  
ATOM    142  OE2AGLU A  19      26.473   0.976  22.838  0.60 28.32      A    O1-
ANISOU  142  OE2AGLU A  19     2346   4342   4074    294    400   -763  A    O1-
ATOM    143  OE2BGLU A  19      23.546   4.280  21.617  0.40 25.27      A    O1-
ANISOU  143  OE2BGLU A  19     2241   3853   3507     56    608   -411  A    O1-
ATOM    144  N   VAL A  20      21.717  -2.168  20.955  1.00 24.43      A    N  
ANISOU  144  N   VAL A  20     2273   3691   3318    456    245   -521  A    N  
ATOM    145  CA  VAL A  20      20.873  -3.137  21.640  1.00 23.03      A    C  
ANISOU  145  CA  VAL A  20     2172   3443   3134    507    134   -492  A    C  
ATOM    146  C   VAL A  20      21.712  -4.292  22.165  1.00 22.63      A    C  
ANISOU  146  C   VAL A  20     2079   3390   3130    587     34   -585  A    C  
ATOM    147  O   VAL A  20      22.802  -4.562  21.662  1.00 24.96      A    O  
ANISOU  147  O   VAL A  20     2284   3746   3453    620     52   -680  A    O  
ATOM    148  CB  VAL A  20      19.721  -3.640  20.739  1.00 21.67      A    C  
ANISOU  148  CB  VAL A  20     2083   3252   2900    522    135   -442  A    C  
ATOM    149  CG1 VAL A  20      19.013  -2.468  20.075  1.00 22.57      A    C  
ANISOU  149  CG1 VAL A  20     2235   3372   2970    452    228   -364  A    C  
ATOM    150  CG2 VAL A  20      20.175  -4.632  19.677  1.00 22.16      A    C  
ANISOU  150  CG2 VAL A  20     2117   3359   2945    585    131   -513  A    C  
ATOM    151  N   PRO A  21      21.215  -4.973  23.195  1.00 19.75      A    N  
ANISOU  151  N   PRO A  21     1781   2951   2771    617    -74   -563  A    N  
ATOM    152  CA  PRO A  21      21.844  -6.187  23.650  1.00 21.08      A    C  
ANISOU  152  CA  PRO A  21     1940   3096   2971    700   -190   -641  A    C  
ATOM    153  C   PRO A  21      21.994  -7.275  22.596  1.00 21.34      A    C  
ANISOU  153  C   PRO A  21     1963   3155   2989    769   -212   -701  A    C  
ATOM    154  O   PRO A  21      21.123  -7.429  21.724  1.00 21.78      A    O  
ANISOU  154  O   PRO A  21     2070   3212   2993    759   -173   -653  A    O  
ATOM    155  CB  PRO A  21      20.935  -6.654  24.785  1.00 21.81      A    C  
ANISOU  155  CB  PRO A  21     2146   3095   3046    697   -285   -576  A    C  
ATOM    156  CG  PRO A  21      20.220  -5.438  25.229  1.00 23.18      A    C  
ANISOU  156  CG  PRO A  21     2346   3258   3203    613   -214   -489  A    C  
ATOM    157  CD  PRO A  21      20.003  -4.662  23.972  1.00 19.20      A    C  
ANISOU  157  CD  PRO A  21     1807   2814   2675    574    -94   -466  A    C  
ATOM    158  N   GLU A  22      23.077  -8.060  22.691  1.00 23.47      A    N  
ANISOU  158  N   GLU A  22     2168   3442   3307    846   -286   -813  A    N  
ATOM    159  CA  GLU A  22      23.302  -9.160  21.756  1.00 23.00      A    C  
ANISOU  159  CA  GLU A  22     2092   3406   3240    922   -320   -886  A    C  
ATOM    160  C   GLU A  22      22.190 -10.152  21.746  1.00 21.06      A    C  
ANISOU  160  C   GLU A  22     1968   3082   2949    951   -401   -829  A    C  
ATOM    161  O   GLU A  22      21.979 -10.892  20.780  1.00 24.99      A    O  
ANISOU  161  O   GLU A  22     2477   3595   3422    995   -406   -855  A    O  
ATOM    162  CB  GLU A  22      24.636  -9.864  22.084  1.00 30.25      A    C  
ANISOU  162  CB  GLU A  22     2924   4342   4229   1009   -412  -1025  A    C  
ATOM    163  CG  GLU A  22      25.808  -9.039  21.641  1.00 37.89      A    C  
ANISOU  163  CG  GLU A  22     3743   5413   5241    987   -309  -1112  A    C  
ATOM    164  CD  GLU A  22      27.156  -9.575  22.136  1.00 44.87      A    C  
ANISOU  164  CD  GLU A  22     4525   6315   6209   1069   -403  -1260  A    C  
ATOM    165  OE1 GLU A  22      27.192 -10.399  23.093  1.00 36.81      A    O  
ANISOU  165  OE1 GLU A  22     3563   5210   5214   1137   -560  -1279  A    O  
ATOM    166  OE2 GLU A  22      28.166  -9.128  21.577  1.00 59.26      A    O1-
ANISOU  166  OE2 GLU A  22     6211   8234   8072   1060   -319  -1358  A    O1-
ATOM    167  N   ARG A  23      21.421 -10.169  22.827  1.00 21.64      A    N  
ANISOU  167  N   ARG A  23     2139   3072   3012    919   -461   -748  A    N  
ATOM    168  CA  ARG A  23      20.233 -10.992  22.888  1.00 21.59      A    C  
ANISOU  168  CA  ARG A  23     2252   2990   2962    921   -523   -682  A    C  
ATOM    169  C   ARG A  23      19.363 -10.868  21.662  1.00 23.72      A    C  
ANISOU  169  C   ARG A  23     2538   3291   3184    899   -440   -638  A    C  
ATOM    170  O   ARG A  23      18.775 -11.844  21.222  1.00 22.38      A    O  
ANISOU  170  O   ARG A  23     2428   3084   2990    935   -495   -635  A    O  
ATOM    171  CB  ARG A  23      19.430 -10.587  24.125  1.00 23.87      A    C  
ANISOU  171  CB  ARG A  23     2626   3208   3235    855   -543   -590  A    C  
ATOM    172  CG  ARG A  23      18.061 -11.205  24.244  1.00 20.29      A    C  
ANISOU  172  CG  ARG A  23     2290   2682   2735    828   -579   -512  A    C  
ATOM    173  CD  ARG A  23      17.412 -10.882  25.581  1.00 19.01      A    C  
ANISOU  173  CD  ARG A  23     2207   2457   2557    761   -601   -440  A    C  
ATOM    174  NE  ARG A  23      16.041 -11.351  25.632  1.00 19.93      A    N  
ANISOU  174  NE  ARG A  23     2423   2518   2633    720   -611   -370  A    N  
ATOM    175  CZ  ARG A  23      15.227 -11.167  26.655  1.00 22.03      A    C  
ANISOU  175  CZ  ARG A  23     2765   2732   2874    652   -616   -306  A    C  
ATOM    176  NH1 ARG A  23      15.658 -10.565  27.765  1.00 25.51      A    N1+
ANISOU  176  NH1 ARG A  23     3206   3162   3323    624   -623   -299  A    N1+
ATOM    177  NH2 ARG A  23      13.985 -11.594  26.587  1.00 21.67      A    N  
ANISOU  177  NH2 ARG A  23     2791   2645   2795    609   -614   -253  A    N  
ATOM    178  N   TYR A  24      19.244  -9.657  21.147  1.00 19.97      A    N  
ANISOU  178  N   TYR A  24     2020   2873   2693    836   -315   -601  A    N  
ATOM    179  CA  TYR A  24      18.294  -9.344  20.075  1.00 19.06      A    C  
ANISOU  179  CA  TYR A  24     1938   2777   2526    806   -239   -546  A    C  
ATOM    180  C   TYR A  24      19.023  -9.335  18.744  1.00 18.88      A    C  
ANISOU  180  C   TYR A  24     1844   2839   2489    838   -171   -614  A    C  
ATOM    181  O   TYR A  24      19.889  -8.513  18.511  1.00 21.33      A    O  
ANISOU  181  O   TYR A  24     2074   3216   2813    811    -89   -648  A    O  
ATOM    182  CB  TYR A  24      17.584  -8.003  20.364  1.00 16.37      A    C  
ANISOU  182  CB  TYR A  24     1618   2434   2169    717   -157   -456  A    C  
ATOM    183  CG  TYR A  24      16.834  -8.051  21.661  1.00 16.93      A    C  
ANISOU  183  CG  TYR A  24     1757   2429   2248    684   -216   -397  A    C  
ATOM    184  CD1 TYR A  24      15.711  -8.861  21.805  1.00 16.62      A    C  
ANISOU  184  CD1 TYR A  24     1804   2325   2185    687   -276   -357  A    C  
ATOM    185  CD2 TYR A  24      17.252  -7.315  22.750  1.00 18.55      A    C  
ANISOU  185  CD2 TYR A  24     1941   2626   2482    647   -212   -387  A    C  
ATOM    186  CE1 TYR A  24      15.026  -8.938  23.027  1.00 16.01      A    C  
ANISOU  186  CE1 TYR A  24     1793   2183   2109    646   -323   -308  A    C  
ATOM    187  CE2 TYR A  24      16.581  -7.357  23.978  1.00 19.72      A    C  
ANISOU  187  CE2 TYR A  24     2156   2708   2629    613   -263   -337  A    C  
ATOM    188  CZ  TYR A  24      15.475  -8.168  24.109  1.00 18.16      A    C  
ANISOU  188  CZ  TYR A  24     2046   2451   2403    610   -313   -298  A    C  
ATOM    189  OH  TYR A  24      14.794  -8.274  25.279  1.00 17.16      A    O  
ANISOU  189  OH  TYR A  24     1990   2264   2267    567   -353   -253  A    O  
ATOM    190  N   GLN A  25      18.671 -10.307  17.922  1.00 20.57      A    N  
ANISOU  190  N   GLN A  25     2092   3048   2677    893   -209   -638  A    N  
ATOM    191  CA  GLN A  25      19.348 -10.592  16.659  1.00 22.63      A    C  
ANISOU  191  CA  GLN A  25     2294   3387   2919    937   -162   -719  A    C  
ATOM    192  C   GLN A  25      18.420 -10.269  15.467  1.00 22.47      A    C  
ANISOU  192  C   GLN A  25     2327   3382   2828    911    -91   -662  A    C  
ATOM    193  O   GLN A  25      17.159 -10.157  15.592  1.00 21.92      A    O  
ANISOU  193  O   GLN A  25     2342   3252   2733    880   -109   -575  A    O  
ATOM    194  CB  GLN A  25      19.776 -12.077  16.619  1.00 22.38      A    C  
ANISOU  194  CB  GLN A  25     2258   3334   2912   1038   -279   -809  A    C  
ATOM    195  CG  GLN A  25      20.823 -12.475  17.647  1.00 25.01      A    C  
ANISOU  195  CG  GLN A  25     2537   3652   3314   1081   -365   -885  A    C  
ATOM    196  CD  GLN A  25      22.160 -11.975  17.253  1.00 27.86      A    C  
ANISOU  196  CD  GLN A  25     2768   4113   3705   1090   -290   -984  A    C  
ATOM    197  NE2 GLN A  25      22.819 -11.195  18.144  1.00 26.65      A    N  
ANISOU  197  NE2 GLN A  25     2559   3969   3599   1052   -270   -990  A    N  
ATOM    198  OE1 GLN A  25      22.651 -12.323  16.173  1.00 29.19      A    O  
ANISOU  198  OE1 GLN A  25     2881   4350   3858   1132   -250  -1065  A    O  
ATOM    199  N   ASN A  26      19.036 -10.111  14.288  1.00 23.56      A    N  
ANISOU  199  N   ASN A  26     2416   3603   2932    922    -10   -718  A    N  
ATOM    200  CA  ASN A  26      18.318  -9.893  13.028  1.00 28.15      A    C  
ANISOU  200  CA  ASN A  26     3052   4205   3439    910     51   -682  A    C  
ATOM    201  C   ASN A  26      17.295  -8.774  13.063  1.00 26.35      A    C  
ANISOU  201  C   ASN A  26     2893   3943   3177    831    102   -567  A    C  
ATOM    202  O   ASN A  26      16.144  -8.992  12.676  1.00 24.58      A    O  
ANISOU  202  O   ASN A  26     2749   3672   2919    838     71   -516  A    O  
ATOM    203  CB  ASN A  26      17.654 -11.199  12.626  1.00 25.62      A    C  
ANISOU  203  CB  ASN A  26     2788   3839   3105    985    -47   -700  A    C  
ATOM    204  CG  ASN A  26      18.648 -12.334  12.469  1.00 36.86      A    C  
ANISOU  204  CG  ASN A  26     4150   5296   4562   1073   -107   -822  A    C  
ATOM    205  ND2 ASN A  26      18.450 -13.367  13.240  1.00 35.53      A    N  
ANISOU  205  ND2 ASN A  26     4011   5053   4437   1126   -236   -836  A    N  
ATOM    206  OD1 ASN A  26      19.589 -12.274  11.666  1.00 48.99      A    O  
ANISOU  206  OD1 ASN A  26     5613   6920   6081   1092    -39   -906  A    O  
ATOM    207  N   LEU A  27      17.718  -7.573  13.499  1.00 23.79      A    N  
ANISOU  207  N   LEU A  27     2534   3640   2865    760    178   -537  A    N  
ATOM    208  CA  LEU A  27      16.857  -6.376  13.539  1.00 20.17      A    C  
ANISOU  208  CA  LEU A  27     2134   3150   2378    686    227   -438  A    C  
ATOM    209  C   LEU A  27      16.459  -5.931  12.148  1.00 28.44      A    C  
ANISOU  209  C   LEU A  27     3239   4226   3344    669    296   -412  A    C  
ATOM    210  O   LEU A  27      17.296  -5.931  11.261  1.00 31.75      A    O  
ANISOU  210  O   LEU A  27     3621   4715   3724    671    366   -467  A    O  
ATOM    211  CB  LEU A  27      17.513  -5.207  14.284  1.00 22.20      A    C  
ANISOU  211  CB  LEU A  27     2341   3425   2669    615    289   -420  A    C  
ATOM    212  CG  LEU A  27      17.207  -5.143  15.793  1.00 27.49      A    C  
ANISOU  212  CG  LEU A  27     3011   4032   3401    603    220   -388  A    C  
ATOM    213  CD1 LEU A  27      17.877  -6.289  16.522  1.00 27.72      A    C  
ANISOU  213  CD1 LEU A  27     2993   4055   3484    666    133   -460  A    C  
ATOM    214  CD2 LEU A  27      17.600  -3.781  16.374  1.00 28.85      A    C  
ANISOU  214  CD2 LEU A  27     3152   4213   3595    527    287   -353  A    C  
ATOM    215  N   SER A  28      15.171  -5.648  11.954  1.00 26.66      A    N  
ANISOU  215  N   SER A  28     3100   3943   3089    657    270   -337  A    N  
ATOM    216  CA  SER A  28      14.670  -5.152  10.667  1.00 28.98      A    C  
ANISOU  216  CA  SER A  28     3466   4245   3298    644    319   -305  A    C  
ATOM    217  C   SER A  28      13.497  -4.204  10.880  1.00 29.71      A    C  
ANISOU  217  C   SER A  28     3632   4274   3384    602    307   -217  A    C  
ATOM    218  O   SER A  28      12.517  -4.610  11.526  1.00 24.42      A    O  
ANISOU  218  O   SER A  28     2984   3542   2753    623    226   -193  A    O  
ATOM    219  CB  SER A  28      14.219  -6.305   9.801  1.00 31.13      A    C  
ANISOU  219  CB  SER A  28     3776   4516   3537    719    264   -341  A    C  
ATOM    220  OG  SER A  28      13.297  -7.144  10.463  1.00 48.18      A    O  
ANISOU  220  OG  SER A  28     5957   6607   5743    759    158   -330  A    O  
ATOM    221  N   PRO A  29      13.596  -2.954  10.343  1.00 27.38      A    N  
ANISOU  221  N   PRO A  29     3377   3989   3039    541    384   -172  A    N  
ATOM    222  CA  PRO A  29      12.560  -1.936  10.551  1.00 37.21      A    C  
ANISOU  222  CA  PRO A  29     4688   5170   4280    504    367    -97  A    C  
ATOM    223  C   PRO A  29      11.200  -2.396  10.094  1.00 33.10      A    C  
ANISOU  223  C   PRO A  29     4240   4594   3741    553    287    -77  A    C  
ATOM    224  O   PRO A  29      11.091  -3.088   9.093  1.00 32.89      A    O  
ANISOU  224  O   PRO A  29     4249   4584   3663    599    274   -105  A    O  
ATOM    225  CB  PRO A  29      13.039  -0.763   9.681  1.00 34.01      A    C  
ANISOU  225  CB  PRO A  29     4332   4788   3802    441    459    -65  A    C  
ATOM    226  CG  PRO A  29      14.505  -0.929   9.628  1.00 49.20      A    C  
ANISOU  226  CG  PRO A  29     6174   6793   5727    418    540   -123  A    C  
ATOM    227  CD  PRO A  29      14.703  -2.416   9.529  1.00 43.67      A    C  
ANISOU  227  CD  PRO A  29     5424   6123   5045    498    491   -196  A    C  
ATOM    228  N   VAL A  30      10.161  -2.040  10.845  1.00 24.96      A    N  
ANISOU  228  N   VAL A  30     3226   3500   2756    544    232    -40  A    N  
ATOM    229  CA  VAL A  30       8.804  -2.326  10.431  1.00 38.73      A    C  
ANISOU  229  CA  VAL A  30     5032   5193   4492    584    157    -27  A    C  
ATOM    230  C   VAL A  30       7.888  -1.113  10.555  1.00 39.00      A    C  
ANISOU  230  C   VAL A  30     5117   5172   4530    553    143     23  A    C  
ATOM    231  O   VAL A  30       8.155  -0.161  11.300  1.00 33.06      A    O  
ANISOU  231  O   VAL A  30     4343   4413   3805    501    175     50  A    O  
ATOM    232  CB  VAL A  30       8.208  -3.516  11.199  1.00 43.30      A    C  
ANISOU  232  CB  VAL A  30     5572   5746   5135    621     81    -57  A    C  
ATOM    233  CG1 VAL A  30       8.993  -4.775  10.898  1.00 44.58      A    C  
ANISOU  233  CG1 VAL A  30     5702   5950   5288    666     75   -111  A    C  
ATOM    234  CG2 VAL A  30       8.198  -3.258  12.698  1.00 30.02      A    C  
ANISOU  234  CG2 VAL A  30     3836   4046   3525    581     76    -44  A    C  
ATOM    235  N   GLY A  31       6.816  -1.149   9.773  1.00 40.94      A    N  
ANISOU  235  N   GLY A  31     5432   5379   4746    590     86     28  A    N  
ATOM    236  CA  GLY A  31       5.762  -0.139   9.858  1.00 53.33      A    C  
ANISOU  236  CA  GLY A  31     7048   6886   6328    580     46     60  A    C  
ATOM    237  C   GLY A  31       6.077   1.162   9.142  1.00 79.00      A    C  
ANISOU  237  C   GLY A  31    10379  10124   9511    545     87    105  A    C  
ATOM    238  O   GLY A  31       5.161   1.948   8.863  1.00 50.15      A    O  
ANISOU  238  O   GLY A  31     6793   6413   5851    553     35    126  A    O  
ATOM    239  N   SER A  32       7.371   1.377   8.854  1.00 72.93      A    N  
ANISOU  239  N   SER A  32     9605   9409   8696    503    175    113  A    N  
ATOM    240  CA  SER A  32       7.909   2.603   8.248  1.00 65.63      A    C  
ANISOU  240  CA  SER A  32     8756   8478   7701    448    236    158  A    C  
ATOM    241  C   SER A  32       7.195   3.897   8.670  1.00 63.57      A    C  
ANISOU  241  C   SER A  32     8541   8146   7466    420    199    201  A    C  
ATOM    242  O   SER A  32       6.885   4.753   7.837  1.00117.38      A    O  
ANISOU  242  O   SER A  32    15469  14917  14214    411    184    238  A    O  
ATOM    243  CB  SER A  32       7.959   2.457   6.719  1.00 93.68      A    C  
ANISOU  243  CB  SER A  32    12412  12039  11143    469    247    162  A    C  
ATOM    244  OG  SER A  32       6.740   1.948   6.208  1.00 85.53      A    O  
ANISOU  244  OG  SER A  32    11431  10961  10105    541    149    149  A    O  
ATOM    245  N   GLY A  36       6.198   4.140  14.884  1.00 30.98      A    N  
ANISOU  245  N   GLY A  36     4050   3990   3730    357    129    147  A    N  
ATOM    246  CA  GLY A  36       7.304   4.860  15.498  1.00 45.35      A    C  
ANISOU  246  CA  GLY A  36     5837   5832   5561    300    190    165  A    C  
ATOM    247  C   GLY A  36       8.580   4.397  14.819  1.00 59.78      A    C  
ANISOU  247  C   GLY A  36     7658   7715   7342    290    254    162  A    C  
ATOM    248  O   GLY A  36       8.583   4.037  13.634  1.00 54.19      A    O  
ANISOU  248  O   GLY A  36     7002   7017   6572    315    259    162  A    O  
ATOM    249  N   SER A  37       9.660   4.395  15.588  1.00 36.00      A    N  
ANISOU  249  N   SER A  37     4577   4741   4361    256    301    150  A    N  
ATOM    250  CA  SER A  37      10.894   3.770  15.199  1.00 34.15      A    C  
ANISOU  250  CA  SER A  37     4303   4568   4104    253    356    123  A    C  
ATOM    251  C   SER A  37      10.857   2.377  15.885  1.00 21.86      A    C  
ANISOU  251  C   SER A  37     2688   3030   2589    300    311     79  A    C  
ATOM    252  O   SER A  37      11.128   2.262  17.068  1.00 20.38      A    O  
ANISOU  252  O   SER A  37     2445   2843   2455    288    299     66  A    O  
ATOM    253  CB  SER A  37      12.051   4.627  15.697  1.00 33.66      A    C  
ANISOU  253  CB  SER A  37     4198   4532   4062    190    422    126  A    C  
ATOM    254  OG  SER A  37      13.254   4.260  15.095  1.00 49.89      A    O  
ANISOU  254  OG  SER A  37     6218   6649   6089    177    487     96  A    O  
ATOM    255  N   VAL A  38      10.426   1.372  15.118  1.00 19.82      A    N  
ANISOU  255  N   VAL A  38     2454   2775   2299    352    280     60  A    N  
ATOM    256  CA  VAL A  38      10.214   0.004  15.599  1.00 17.42      A    C  
ANISOU  256  CA  VAL A  38     2119   2475   2026    397    225     24  A    C  
ATOM    257  C   VAL A  38      10.939  -0.974  14.663  1.00 20.11      A    C  
ANISOU  257  C   VAL A  38     2451   2861   2328    438    239    -17  A    C  
ATOM    258  O   VAL A  38      10.819  -0.853  13.426  1.00 20.29      A    O  
ANISOU  258  O   VAL A  38     2526   2894   2289    451    260    -11  A    O  
ATOM    259  CB  VAL A  38       8.721  -0.348  15.662  1.00 17.77      A    C  
ANISOU  259  CB  VAL A  38     2202   2468   2083    423    157     32  A    C  
ATOM    260  CG1 VAL A  38       8.534  -1.736  16.203  1.00 18.96      A    C  
ANISOU  260  CG1 VAL A  38     2327   2615   2262    456    104      0  A    C  
ATOM    261  CG2 VAL A  38       8.001   0.627  16.596  1.00 18.80      A    C  
ANISOU  261  CG2 VAL A  38     2330   2559   2253    385    146     59  A    C  
ATOM    262  N   CYS A  39      11.685  -1.941  15.240  1.00 21.27      A    N  
ANISOU  262  N   CYS A  39     2541   3034   2508    462    221    -63  A    N  
ATOM    263  CA  CYS A  39      12.280  -3.035  14.464  1.00 20.34      A    C  
ANISOU  263  CA  CYS A  39     2408   2956   2365    514    215   -116  A    C  
ATOM    264  C   CYS A  39      11.742  -4.336  14.966  1.00 20.58      A    C  
ANISOU  264  C   CYS A  39     2441   2953   2427    562    128   -139  A    C  
ATOM    265  O   CYS A  39      11.592  -4.540  16.207  1.00 23.45      A    O  
ANISOU  265  O   CYS A  39     2787   3283   2839    548     88   -133  A    O  
ATOM    266  CB  CYS A  39      13.793  -3.061  14.578  1.00 24.57      A    C  
ANISOU  266  CB  CYS A  39     2869   3552   2913    507    266   -166  A    C  
ATOM    267  SG  CYS A  39      14.686  -1.729  13.731  1.00 27.88      A    S  
ANISOU  267  SG  CYS A  39     3281   4027   3286    442    387   -154  A    S  
ATOM    268  N   ALA A  40      11.503  -5.270  14.053  1.00 18.01      A    N  
ANISOU  268  N   ALA A  40     2142   2631   2069    615     97   -167  A    N  
ATOM    269  CA  ALA A  40      11.293  -6.635  14.448  1.00 17.61      A    C  
ANISOU  269  CA  ALA A  40     2091   2553   2047    663     16   -201  A    C  
ATOM    270  C   ALA A  40      12.693  -7.247  14.728  1.00 16.78      A    C  
ANISOU  270  C   ALA A  40     1921   2491   1964    692     15   -265  A    C  
ATOM    271  O   ALA A  40      13.688  -6.848  14.114  1.00 20.17      A    O  
ANISOU  271  O   ALA A  40     2311   2983   2372    691     83   -296  A    O  
ATOM    272  CB  ALA A  40      10.608  -7.415  13.320  1.00 19.98      A    C  
ANISOU  272  CB  ALA A  40     2438   2844   2308    714    -20   -216  A    C  
ATOM    273  N   ALA A  41      12.731  -8.208  15.632  1.00 17.33      A    N  
ANISOU  273  N   ALA A  41     1986   2524   2075    717    -63   -287  A    N  
ATOM    274  CA  ALA A  41      14.001  -8.907  16.017  1.00 17.81      A    C  
ANISOU  274  CA  ALA A  41     1992   2610   2167    757    -93   -357  A    C  
ATOM    275  C   ALA A  41      13.709 -10.300  16.498  1.00 16.96      A    C  
ANISOU  275  C   ALA A  41     1918   2445   2081    806   -203   -381  A    C  
ATOM    276  O   ALA A  41      12.577 -10.680  16.746  1.00 21.15      A    O  
ANISOU  276  O   ALA A  41     2511   2917   2610    791   -248   -340  A    O  
ATOM    277  CB  ALA A  41      14.738  -8.171  17.136  1.00 20.61      A    C  
ANISOU  277  CB  ALA A  41     2297   2972   2561    716    -70   -353  A    C  
ATOM    278  N   PHE A  42      14.767 -11.114  16.488  1.00 17.59      A    N  
ANISOU  278  N   PHE A  42     1957   2545   2181    866   -247   -459  A    N  
ATOM    279  CA  PHE A  42      14.743 -12.442  17.036  1.00 18.39      A    C  
ANISOU  279  CA  PHE A  42     2094   2586   2307    914   -363   -490  A    C  
ATOM    280  C   PHE A  42      15.314 -12.444  18.431  1.00 16.61      A    C  
ANISOU  280  C   PHE A  42     1861   2328   2123    901   -412   -494  A    C  
ATOM    281  O   PHE A  42      16.452 -11.975  18.638  1.00 19.66      A    O  
ANISOU  281  O   PHE A  42     2172   2763   2536    910   -382   -541  A    O  
ATOM    282  CB  PHE A  42      15.589 -13.381  16.146  1.00 18.77      A    C  
ANISOU  282  CB  PHE A  42     2107   2673   2354   1003   -398   -587  A    C  
ATOM    283  CG  PHE A  42      15.548 -14.799  16.563  1.00 19.96      A    C  
ANISOU  283  CG  PHE A  42     2303   2753   2527   1063   -531   -624  A    C  
ATOM    284  CD1 PHE A  42      14.396 -15.572  16.367  1.00 24.10      A    C  
ANISOU  284  CD1 PHE A  42     2912   3211   3035   1064   -591   -587  A    C  
ATOM    285  CD2 PHE A  42      16.662 -15.398  17.134  1.00 25.19      A    C  
ANISOU  285  CD2 PHE A  42     2929   3410   3231   1119   -605   -700  A    C  
ATOM    286  CE1 PHE A  42      14.400 -16.928  16.741  1.00 27.23      A    C  
ANISOU  286  CE1 PHE A  42     3362   3534   3449   1116   -720   -621  A    C  
ATOM    287  CE2 PHE A  42      16.641 -16.726  17.497  1.00 24.36      A    C  
ANISOU  287  CE2 PHE A  42     2882   3230   3144   1178   -740   -735  A    C  
ATOM    288  CZ  PHE A  42      15.524 -17.474  17.310  1.00 26.42      A    C  
ANISOU  288  CZ  PHE A  42     3233   3422   3383   1172   -795   -692  A    C  
ATOM    289  N   ASP A  43      14.520 -12.921  19.383  1.00 16.76      A    N  
ANISOU  289  N   ASP A  43     1956   2264   2149    873   -482   -446  A    N  
ATOM    290  CA  ASP A  43      14.895 -12.967  20.767  1.00 16.79      A    C  
ANISOU  290  CA  ASP A  43     1978   2223   2179    854   -536   -439  A    C  
ATOM    291  C   ASP A  43      15.608 -14.306  21.016  1.00 18.61      A    C  
ANISOU  291  C   ASP A  43     2232   2411   2430    933   -663   -509  A    C  
ATOM    292  O   ASP A  43      14.973 -15.333  21.171  1.00 20.42      A    O  
ANISOU  292  O   ASP A  43     2544   2567   2648    943   -746   -495  A    O  
ATOM    293  CB  ASP A  43      13.686 -12.829  21.680  1.00 18.58      A    C  
ANISOU  293  CB  ASP A  43     2284   2383   2391    777   -545   -356  A    C  
ATOM    294  CG  ASP A  43      14.080 -12.699  23.135  1.00 18.71      A    C  
ANISOU  294  CG  ASP A  43     2326   2359   2424    747   -587   -343  A    C  
ATOM    295  OD1 ASP A  43      15.258 -12.990  23.517  1.00 18.56      A    O  
ANISOU  295  OD1 ASP A  43     2277   2343   2431    799   -644   -403  A    O  
ATOM    296  OD2 ASP A  43      13.227 -12.238  23.914  1.00 24.71      A    O1-
ANISOU  296  OD2 ASP A  43     3130   3087   3170    673   -563   -280  A    O1-
ATOM    297  N   THR A  44      16.917 -14.246  21.093  1.00 18.69      A    N  
ANISOU  297  N   THR A  44     2166   2462   2473    984   -677   -586  A    N  
ATOM    298  CA  THR A  44      17.715 -15.470  21.352  1.00 19.58      A    C  
ANISOU  298  CA  THR A  44     2292   2533   2614   1072   -809   -669  A    C  
ATOM    299  C   THR A  44      17.471 -16.142  22.691  1.00 23.92      A    C  
ANISOU  299  C   THR A  44     2949   2974   3166   1060   -929   -636  A    C  
ATOM    300  O   THR A  44      17.844 -17.295  22.860  1.00 26.85      A    O  
ANISOU  300  O   THR A  44     3367   3286   3550   1129  -1057   -689  A    O  
ATOM    301  CB  THR A  44      19.190 -15.194  21.272  1.00 20.35      A    C  
ANISOU  301  CB  THR A  44     2276   2699   2757   1127   -802   -769  A    C  
ATOM    302  CG2 THR A  44      19.657 -14.660  19.955  1.00 19.82      A    C  
ANISOU  302  CG2 THR A  44     2104   2743   2685   1142   -688   -820  A    C  
ATOM    303  OG1 THR A  44      19.602 -14.346  22.346  1.00 23.40      A    O  
ANISOU  303  OG1 THR A  44     2641   3083   3166   1082   -785   -748  A    O  
ATOM    304  N   LYS A  45      16.953 -15.440  23.687  1.00 21.53      A    N  
ANISOU  304  N   LYS A  45     2690   2642   2849    976   -897   -558  A    N  
ATOM    305  CA  LYS A  45      16.658 -16.075  24.943  1.00 22.29      A    C  
ANISOU  305  CA  LYS A  45     2903   2636   2932    953  -1002   -522  A    C  
ATOM    306  C   LYS A  45      15.413 -16.958  24.864  1.00 27.99      A    C  
ANISOU  306  C   LYS A  45     3738   3281   3614    917  -1042   -465  A    C  
ATOM    307  O   LYS A  45      15.301 -17.922  25.615  1.00 25.71      A    O  
ANISOU  307  O   LYS A  45     3560   2896   3313    921  -1157   -456  A    O  
ATOM    308  CB  LYS A  45      16.471 -14.987  26.018  1.00 26.85      A    C  
ANISOU  308  CB  LYS A  45     3486   3215   3501    870   -943   -460  A    C  
ATOM    309  CG  LYS A  45      16.303 -15.476  27.445  1.00 29.23      A    C  
ANISOU  309  CG  LYS A  45     3910   3417   3779    837  -1040   -424  A    C  
ATOM    310  CD  LYS A  45      16.169 -14.280  28.390  1.00 30.63      A    C  
ANISOU  310  CD  LYS A  45     4077   3614   3948    759   -968   -373  A    C  
ATOM    311  CE  LYS A  45      15.986 -14.749  29.823  1.00 34.70      A    C  
ANISOU  311  CE  LYS A  45     4725   4032   4427    722  -1059   -336  A    C  
ATOM    312  NZ  LYS A  45      17.161 -15.529  30.290  1.00 40.72      A    N1+
ANISOU  312  NZ  LYS A  45     5516   4742   5211    810  -1205   -407  A    N1+
ATOM    313  N   THR A  46      14.498 -16.662  23.951  1.00 26.26      A    N  
ANISOU  313  N   THR A  46     3497   3101   3379    885   -953   -429  A    N  
ATOM    314  CA  THR A  46      13.220 -17.371  23.878  1.00 25.55      A    C  
ANISOU  314  CA  THR A  46     3502   2946   3261    838   -977   -377  A    C  
ATOM    315  C   THR A  46      12.999 -18.080  22.534  1.00 24.34      A    C  
ANISOU  315  C   THR A  46     3331   2807   3108    900   -992   -417  A    C  
ATOM    316  O   THR A  46      12.162 -18.963  22.438  1.00 28.71      A    O  
ANISOU  316  O   THR A  46     3967   3296   3648    883  -1046   -395  A    O  
ATOM    317  CB  THR A  46      12.024 -16.414  24.128  1.00 30.25      A    C  
ANISOU  317  CB  THR A  46     4101   3558   3834    733   -868   -297  A    C  
ATOM    318  CG2 THR A  46      12.141 -15.686  25.431  1.00 33.51      A    C  
ANISOU  318  CG2 THR A  46     4532   3959   4240    669   -846   -258  A    C  
ATOM    319  OG1 THR A  46      11.947 -15.466  23.052  1.00 26.13      A    O  
ANISOU  319  OG1 THR A  46     3482   3126   3319    742   -761   -302  A    O  
ATOM    320  N   GLY A  47      13.716 -17.704  21.473  1.00 20.83      A    N  
ANISOU  320  N   GLY A  47     2786   2451   2680    964   -942   -476  A    N  
ATOM    321  CA  GLY A  47      13.428 -18.225  20.152  1.00 23.07      A    C  
ANISOU  321  CA  GLY A  47     3053   2758   2954   1015   -939   -510  A    C  
ATOM    322  C   GLY A  47      12.169 -17.646  19.495  1.00 28.98      A    C  
ANISOU  322  C   GLY A  47     3804   3529   3678    954   -849   -449  A    C  
ATOM    323  O   GLY A  47      11.726 -18.163  18.439  1.00 27.13      A    O  
ANISOU  323  O   GLY A  47     3575   3300   3432    992   -859   -469  A    O  
ATOM    324  N   HIS A  48      11.586 -16.579  20.080  1.00 22.01      A    N  
ANISOU  324  N   HIS A  48     2916   2659   2788    868   -767   -382  A    N  
ATOM    325  CA  HIS A  48      10.465 -15.918  19.454  1.00 22.74      A    C  
ANISOU  325  CA  HIS A  48     3001   2776   2864    821   -687   -337  A    C  
ATOM    326  C   HIS A  48      10.845 -14.590  18.860  1.00 17.28      A    C  
ANISOU  326  C   HIS A  48     2228   2172   2165    817   -578   -334  A    C  
ATOM    327  O   HIS A  48      11.894 -14.015  19.195  1.00 18.81      A    O  
ANISOU  327  O   HIS A  48     2369   2407   2372    826   -548   -355  A    O  
ATOM    328  CB  HIS A  48       9.325 -15.753  20.482  1.00 25.21      A    C  
ANISOU  328  CB  HIS A  48     3373   3032   3175    725   -680   -269  A    C  
ATOM    329  CG  HIS A  48       8.816 -17.064  20.982  1.00 31.18      A    C  
ANISOU  329  CG  HIS A  48     4221   3696   3929    711   -779   -264  A    C  
ATOM    330  CD2 HIS A  48       8.780 -17.598  22.226  1.00 34.76      A    C  
ANISOU  330  CD2 HIS A  48     4753   4077   4377    664   -838   -240  A    C  
ATOM    331  ND1 HIS A  48       8.326 -18.036  20.132  1.00 38.48      A    N  
ANISOU  331  ND1 HIS A  48     5177   4590   4853    748   -833   -287  A    N  
ATOM    332  CE1 HIS A  48       8.000 -19.109  20.833  1.00 43.95      A    C  
ANISOU  332  CE1 HIS A  48     5962   5194   5544    720   -921   -277  A    C  
ATOM    333  NE2 HIS A  48       8.265 -18.870  22.105  1.00 35.68      A    N  
ANISOU  333  NE2 HIS A  48     4950   4119   4490    668   -925   -246  A    N  
ATOM    334  N   ARG A  49      10.014 -14.092  17.986  1.00 18.78      A    N  
ANISOU  334  N   ARG A  49     2413   2387   2337    802   -521   -311  A    N  
ATOM    335  CA  ARG A  49      10.219 -12.752  17.448  1.00 21.36      A    C  
ANISOU  335  CA  ARG A  49     2684   2783   2649    785   -419   -296  A    C  
ATOM    336  C   ARG A  49       9.645 -11.704  18.409  1.00 18.46      A    C  
ANISOU  336  C   ARG A  49     2317   2403   2292    702   -371   -237  A    C  
ATOM    337  O   ARG A  49       8.711 -11.984  19.152  1.00 20.25      A    O  
ANISOU  337  O   ARG A  49     2589   2576   2529    656   -400   -205  A    O  
ATOM    338  CB  ARG A  49       9.598 -12.582  16.078  1.00 22.67      A    C  
ANISOU  338  CB  ARG A  49     2855   2974   2782    807   -387   -297  A    C  
ATOM    339  CG  ARG A  49       9.997 -13.625  15.056  1.00 27.15      A    C  
ANISOU  339  CG  ARG A  49     3428   3555   3335    888   -434   -358  A    C  
ATOM    340  CD  ARG A  49       9.629 -13.146  13.651  1.00 30.46      A    C  
ANISOU  340  CD  ARG A  49     3849   4017   3708    908   -382   -360  A    C  
ATOM    341  NE  ARG A  49      10.680 -12.286  13.081  1.00 45.96      A    N  
ANISOU  341  NE  ARG A  49     5761   6060   5643    915   -296   -378  A    N  
ATOM    342  CZ  ARG A  49      10.484 -11.325  12.167  1.00 62.93      A    C  
ANISOU  342  CZ  ARG A  49     7917   8248   7746    899   -221   -357  A    C  
ATOM    343  NH1 ARG A  49      11.514 -10.604  11.732  1.00 37.75      A    N1+
ANISOU  343  NH1 ARG A  49     4685   5128   4530    892   -140   -375  A    N1+
ATOM    344  NH2 ARG A  49       9.274 -11.065  11.684  1.00 44.93      A    N  
ANISOU  344  NH2 ARG A  49     5688   5936   5448    887   -230   -318  A    N  
ATOM    345  N   VAL A  50      10.258 -10.548  18.405  1.00 17.71      A    N  
ANISOU  345  N   VAL A  50     2174   2360   2196    684   -297   -229  A    N  
ATOM    346  CA  VAL A  50       9.817  -9.432  19.252  1.00 16.43      A    C  
ANISOU  346  CA  VAL A  50     2005   2192   2045    614   -249   -178  A    C  
ATOM    347  C   VAL A  50       9.873  -8.156  18.432  1.00 16.77      A    C  
ANISOU  347  C   VAL A  50     2017   2285   2070    602   -166   -162  A    C  
ATOM    348  O   VAL A  50      10.407  -8.115  17.306  1.00 15.95      A    O  
ANISOU  348  O   VAL A  50     1896   2225   1940    640   -136   -188  A    O  
ATOM    349  CB  VAL A  50      10.714  -9.277  20.507  1.00 18.38      A    C  
ANISOU  349  CB  VAL A  50     2233   2434   2317    595   -261   -184  A    C  
ATOM    350  CG1 VAL A  50      10.620 -10.474  21.444  1.00 18.00      A    C  
ANISOU  350  CG1 VAL A  50     2239   2323   2279    598   -352   -191  A    C  
ATOM    351  CG2 VAL A  50      12.131  -8.953  20.147  1.00 17.75      A    C  
ANISOU  351  CG2 VAL A  50     2089   2413   2243    631   -230   -227  A    C  
ATOM    352  N   ALA A  51       9.234  -7.100  19.001  1.00 15.36      A    N  
ANISOU  352  N   ALA A  51     1838   2096   1901    544   -127   -119  A    N  
ATOM    353  CA  ALA A  51       9.309  -5.780  18.503  1.00 16.42      A    C  
ANISOU  353  CA  ALA A  51     1954   2262   2022    522    -58    -96  A    C  
ATOM    354  C   ALA A  51      10.122  -4.926  19.464  1.00 14.52      A    C  
ANISOU  354  C   ALA A  51     1676   2038   1805    483    -22    -88  A    C  
ATOM    355  O   ALA A  51       9.898  -5.011  20.677  1.00 16.09      A    O  
ANISOU  355  O   ALA A  51     1878   2206   2030    452    -47    -77  A    O  
ATOM    356  CB  ALA A  51       7.880  -5.192  18.355  1.00 16.90      A    C  
ANISOU  356  CB  ALA A  51     2046   2293   2081    494    -55    -64  A    C  
ATOM    357  N   VAL A  52      11.077  -4.163  18.911  1.00 16.79      A    N  
ANISOU  357  N   VAL A  52     1928   2372   2081    481     38    -95  A    N  
ATOM    358  CA  VAL A  52      11.920  -3.249  19.708  1.00 16.25      A    C  
ANISOU  358  CA  VAL A  52     1815   2321   2038    442     76    -91  A    C  
ATOM    359  C   VAL A  52      11.590  -1.806  19.261  1.00 19.06      A    C  
ANISOU  359  C   VAL A  52     2182   2684   2378    398    139    -50  A    C  
ATOM    360  O   VAL A  52      11.778  -1.465  18.073  1.00 19.68      A    O  
ANISOU  360  O   VAL A  52     2272   2788   2418    405    182    -47  A    O  
ATOM    361  CB  VAL A  52      13.413  -3.535  19.497  1.00 18.63      A    C  
ANISOU  361  CB  VAL A  52     2059   2673   2347    468     95   -144  A    C  
ATOM    362  CG1 VAL A  52      14.288  -2.706  20.407  1.00 20.07      A    C  
ANISOU  362  CG1 VAL A  52     2190   2869   2566    430    122   -150  A    C  
ATOM    363  CG2 VAL A  52      13.688  -5.023  19.674  1.00 19.47      A    C  
ANISOU  363  CG2 VAL A  52     2166   2767   2463    526     19   -192  A    C  
ATOM    364  N   LYS A  53      11.036  -0.984  20.169  1.00 16.78      A    N  
ANISOU  364  N   LYS A  53     1897   2364   2114    356    141    -18  A    N  
ATOM    365  CA  LYS A  53      10.708   0.417  19.888  1.00 17.95      A    C  
ANISOU  365  CA  LYS A  53     2060   2506   2254    317    184     18  A    C  
ATOM    366  C   LYS A  53      11.784   1.279  20.537  1.00 19.25      A    C  
ANISOU  366  C   LYS A  53     2178   2691   2445    278    226     16  A    C  
ATOM    367  O   LYS A  53      12.003   1.226  21.747  1.00 18.89      A    O  
ANISOU  367  O   LYS A  53     2107   2635   2436    264    204      7  A    O  
ATOM    368  CB  LYS A  53       9.323   0.767  20.452  1.00 18.69      A    C  
ANISOU  368  CB  LYS A  53     2182   2554   2364    302    153     41  A    C  
ATOM    369  CG  LYS A  53       8.814   2.203  20.206  1.00 17.96      A    C  
ANISOU  369  CG  LYS A  53     2114   2441   2271    272    177     72  A    C  
ATOM    370  CD  LYS A  53       7.462   2.352  20.942  1.00 20.57      A    C  
ANISOU  370  CD  LYS A  53     2452   2733   2629    264    138     72  A    C  
ATOM    371  CE  LYS A  53       6.836   3.683  20.748  1.00 27.30      A    C  
ANISOU  371  CE  LYS A  53     3328   3559   3487    247    143     91  A    C  
ATOM    372  NZ  LYS A  53       5.458   3.723  21.322  1.00 22.93      A    N1+
ANISOU  372  NZ  LYS A  53     2771   2976   2964    248    105     73  A    N1+
ATOM    373  N   LYS A  54      12.401   2.117  19.731  1.00 17.02      A    N  
ANISOU  373  N   LYS A  54     1893   2432   2139    255    285     26  A    N  
ATOM    374  CA  LYS A  54      13.314   3.120  20.240  1.00 17.00      A    C  
ANISOU  374  CA  LYS A  54     1852   2444   2164    206    330     28  A    C  
ATOM    375  C   LYS A  54      12.603   4.449  20.393  1.00 18.09      A    C  
ANISOU  375  C   LYS A  54     2028   2541   2304    165    339     74  A    C  
ATOM    376  O   LYS A  54      12.053   5.001  19.418  1.00 21.55      A    O  
ANISOU  376  O   LYS A  54     2526   2962   2702    159    354    105  A    O  
ATOM    377  CB  LYS A  54      14.508   3.266  19.300  1.00 20.32      A    C  
ANISOU  377  CB  LYS A  54     2242   2918   2559    191    398      5  A    C  
ATOM    378  CG  LYS A  54      15.468   4.353  19.713  1.00 20.92      A    C  
ANISOU  378  CG  LYS A  54     2275   3009   2664    131    451      5  A    C  
ATOM    379  CD  LYS A  54      16.507   4.602  18.665  1.00 27.71      A    C  
ANISOU  379  CD  LYS A  54     3114   3923   3493     99    533    -16  A    C  
ATOM    380  CE  LYS A  54      17.685   5.337  19.251  1.00 30.31      A    C  
ANISOU  380  CE  LYS A  54     3369   4278   3869     45    579    -42  A    C  
ATOM    381  NZ  LYS A  54      18.607   5.753  18.186  1.00 34.66      A    N1+
ANISOU  381  NZ  LYS A  54     3904   4882   4384     -5    675    -59  A    N1+
ATOM    382  N   LEU A  55      12.598   4.980  21.604  1.00 17.35      A    N  
ANISOU  382  N   LEU A  55     1909   2428   2254    140    324     76  A    N  
ATOM    383  CA  LEU A  55      11.886   6.244  21.822  1.00 16.93      A    C  
ANISOU  383  CA  LEU A  55     1889   2333   2209    107    324    110  A    C  
ATOM    384  C   LEU A  55      12.649   7.407  21.195  1.00 22.46      A    C  
ANISOU  384  C   LEU A  55     2600   3037   2896     59    382    133  A    C  
ATOM    385  O   LEU A  55      13.871   7.408  21.143  1.00 20.90      A    O  
ANISOU  385  O   LEU A  55     2356   2880   2707     35    427    113  A    O  
ATOM    386  CB  LEU A  55      11.632   6.480  23.300  1.00 16.24      A    C  
ANISOU  386  CB  LEU A  55     1775   2227   2169     96    293    101  A    C  
ATOM    387  CG  LEU A  55      10.721   5.438  24.002  1.00 17.85      A    C  
ANISOU  387  CG  LEU A  55     1984   2418   2379    126    240     85  A    C  
ATOM    388  CD1 LEU A  55      10.444   5.774  25.448  1.00 20.46      A    C  
ANISOU  388  CD1 LEU A  55     2298   2732   2744    105    219     76  A    C  
ATOM    389  CD2 LEU A  55       9.435   5.319  23.171  1.00 20.16      A    C  
ANISOU  389  CD2 LEU A  55     2325   2688   2648    150    220     98  A    C  
ATOM    390  N   SER A  56      11.900   8.402  20.717  1.00 21.98      A    N  
ANISOU  390  N   SER A  56     2604   2932   2817     43    376    170  A    N  
ATOM    391  CA  SER A  56      12.462   9.525  20.008  1.00 21.01      A    C  
ANISOU  391  CA  SER A  56     2517   2798   2668    -11    425    201  A    C  
ATOM    392  C   SER A  56      12.746  10.676  20.973  1.00 16.93      A    C  
ANISOU  392  C   SER A  56     1979   2254   2199    -56    427    208  A    C  
ATOM    393  O   SER A  56      11.824  11.159  21.633  1.00 21.91      A    O  
ANISOU  393  O   SER A  56     2627   2841   2858    -44    377    214  A    O  
ATOM    394  CB  SER A  56      11.489  10.028  18.959  1.00 26.68      A    C  
ANISOU  394  CB  SER A  56     3334   3467   3335      0    403    239  A    C  
ATOM    395  OG  SER A  56      11.999  11.218  18.380  1.00 32.18      A    O  
ANISOU  395  OG  SER A  56     4085   4139   4002    -60    444    275  A    O  
ATOM    396  N   ARG A  57      14.016  11.060  21.039  1.00 19.51      A    N  
ANISOU  396  N   ARG A  57     2264   2610   2540   -109    485    200  A    N  
ATOM    397  CA  ARG A  57      14.450  12.253  21.829  1.00 21.54      A    C  
ANISOU  397  CA  ARG A  57     2502   2840   2842   -162    493    208  A    C  
ATOM    398  C   ARG A  57      13.822  12.268  23.234  1.00 18.36      A    C  
ANISOU  398  C   ARG A  57     2068   2414   2493   -132    431    189  A    C  
ATOM    399  O   ARG A  57      13.179  13.232  23.643  1.00 18.24      A    O  
ANISOU  399  O   ARG A  57     2085   2347   2496   -143    398    205  A    O  
ATOM    400  CB  ARG A  57      14.132  13.544  21.067  1.00 22.08      A    C  
ANISOU  400  CB  ARG A  57     2663   2850   2877   -208    503    259  A    C  
ATOM    401  CG  ARG A  57      14.705  13.592  19.647  1.00 22.96      A    C  
ANISOU  401  CG  ARG A  57     2826   2979   2917   -249    571    283  A    C  
ATOM    402  CD  ARG A  57      14.150  14.799  18.932  1.00 29.14      A    C  
ANISOU  402  CD  ARG A  57     3728   3686   3657   -285    557    341  A    C  
ATOM    403  NE  ARG A  57      14.702  14.989  17.604  1.00 31.50      A    N  
ANISOU  403  NE  ARG A  57     4096   3994   3877   -340    625    372  A    N  
ATOM    404  CZ  ARG A  57      15.830  15.633  17.321  1.00 31.82      A    C  
ANISOU  404  CZ  ARG A  57     4133   4051   3906   -433    708    380  A    C  
ATOM    405  NH1 ARG A  57      16.598  16.156  18.272  1.00 28.48      A    N1+
ANISOU  405  NH1 ARG A  57     3631   3637   3553   -478    729    359  A    N1+
ATOM    406  NH2 ARG A  57      16.214  15.703  16.047  1.00 32.42      A    N  
ANISOU  406  NH2 ARG A  57     4282   4139   3895   -483    775    408  A    N  
ATOM    407  N   PRO A  58      14.043  11.207  24.016  1.00 15.97      A    N  
ANISOU  407  N   PRO A  58     1703   2149   2214    -97    411    149  A    N  
ATOM    408  CA  PRO A  58      13.181  10.999  25.162  1.00 15.72      A    C  
ANISOU  408  CA  PRO A  58     1665   2097   2211    -66    355    135  A    C  
ATOM    409  C   PRO A  58      13.329  12.020  26.252  1.00 15.72      A    C  
ANISOU  409  C   PRO A  58     1645   2071   2256    -96    341    129  A    C  
ATOM    410  O   PRO A  58      12.373  12.237  26.996  1.00 16.05      A    O  
ANISOU  410  O   PRO A  58     1701   2086   2312    -80    300    124  A    O  
ATOM    411  CB  PRO A  58      13.533   9.598  25.645  1.00 16.07      A    C  
ANISOU  411  CB  PRO A  58     1665   2180   2259    -29    338     99  A    C  
ATOM    412  CG  PRO A  58      14.893   9.377  25.115  1.00 18.66      A    C  
ANISOU  412  CG  PRO A  58     1949   2552   2588    -45    384     80  A    C  
ATOM    413  CD  PRO A  58      14.933  10.067  23.799  1.00 17.66      A    C  
ANISOU  413  CD  PRO A  58     1866   2422   2424    -78    434    114  A    C  
ATOM    414  N   PHE A  59      14.498  12.650  26.375  1.00 16.75      A    N  
ANISOU  414  N   PHE A  59     1740   2212   2413   -141    376    123  A    N  
ATOM    415  CA  PHE A  59      14.665  13.632  27.437  1.00 16.70      A    C  
ANISOU  415  CA  PHE A  59     1715   2178   2453   -168    357    114  A    C  
ATOM    416  C   PHE A  59      15.071  14.995  26.892  1.00 20.28      A    C  
ANISOU  416  C   PHE A  59     2195   2596   2913   -228    389    143  A    C  
ATOM    417  O   PHE A  59      15.738  15.791  27.591  1.00 20.05      A    O  
ANISOU  417  O   PHE A  59     2134   2556   2929   -265    392    130  A    O  
ATOM    418  CB  PHE A  59      15.672  13.131  28.442  1.00 17.78      A    C  
ANISOU  418  CB  PHE A  59     1779   2349   2627   -165    352     70  A    C  
ATOM    419  CG  PHE A  59      15.394  11.716  28.917  1.00 16.53      A    C  
ANISOU  419  CG  PHE A  59     1609   2217   2455   -112    316     46  A    C  
ATOM    420  CD1 PHE A  59      14.254  11.459  29.643  1.00 16.97      A    C  
ANISOU  420  CD1 PHE A  59     1698   2252   2499    -85    273     46  A    C  
ATOM    421  CD2 PHE A  59      16.230  10.664  28.571  1.00 19.85      A    C  
ANISOU  421  CD2 PHE A  59     1992   2681   2869    -91    327     18  A    C  
ATOM    422  CE1 PHE A  59      13.932  10.167  30.027  1.00 17.29      A    C  
ANISOU  422  CE1 PHE A  59     1742   2308   2518    -49    244     30  A    C  
ATOM    423  CE2 PHE A  59      15.958   9.375  29.006  1.00 17.88      A    C  
ANISOU  423  CE2 PHE A  59     1746   2443   2604    -43    285     -2  A    C  
ATOM    424  CZ  PHE A  59      14.810   9.132  29.720  1.00 16.64      A    C  
ANISOU  424  CZ  PHE A  59     1632   2259   2431    -26    245      9  A    C  
ATOM    425  N   GLN A  60      14.566  15.317  25.718  1.00 16.57      A    N  
ANISOU  425  N   GLN A  60     1795   2101   2399   -236    404    183  A    N  
ATOM    426  CA  GLN A  60      14.865  16.619  25.111  1.00 19.39      A    C  
ANISOU  426  CA  GLN A  60     2203   2412   2750   -299    429    220  A    C  
ATOM    427  C   GLN A  60      14.326  17.806  25.858  1.00 14.86      A    C  
ANISOU  427  C   GLN A  60     1656   1775   2214   -308    379    225  A    C  
ATOM    428  O   GLN A  60      14.887  18.914  25.793  1.00 15.96      A    O  
ANISOU  428  O   GLN A  60     1816   1878   2371   -369    395    243  A    O  
ATOM    429  CB  GLN A  60      14.374  16.660  23.661  1.00 20.99      A    C  
ANISOU  429  CB  GLN A  60     2497   2594   2885   -301    443    264  A    C  
ATOM    430  CG  GLN A  60      14.715  17.933  22.940  1.00 25.47      A    C  
ANISOU  430  CG  GLN A  60     3138   3107   3430   -375    470    309  A    C  
ATOM    431  CD  GLN A  60      14.734  17.752  21.438  1.00 32.27      A    C  
ANISOU  431  CD  GLN A  60     4079   3971   4211   -395    512    348  A    C  
ATOM    432  NE2 GLN A  60      13.831  18.465  20.749  1.00 33.93      A    N  
ANISOU  432  NE2 GLN A  60     4407   4105   4380   -388    466    392  A    N  
ATOM    433  OE1 GLN A  60      15.563  16.963  20.888  1.00 28.88      A    O  
ANISOU  433  OE1 GLN A  60     3609   3609   3755   -412    580    333  A    O  
ATOM    434  N   SER A  61      13.193  17.582  26.471  1.00 14.65      A    N  
ANISOU  434  N   SER A  61     1635   1733   2197   -250    320    208  A    N  
ATOM    435  CA  SER A  61      12.385  18.608  27.140  1.00 14.08      A    C  
ANISOU  435  CA  SER A  61     1589   1603   2157   -240    261    200  A    C  
ATOM    436  C   SER A  61      11.619  17.981  28.243  1.00 14.82      A    C  
ANISOU  436  C   SER A  61     1638   1720   2273   -188    224    155  A    C  
ATOM    437  O   SER A  61      11.490  16.746  28.291  1.00 15.34      A    O  
ANISOU  437  O   SER A  61     1676   1836   2319   -157    235    141  A    O  
ATOM    438  CB  SER A  61      11.388  19.218  26.152  1.00 18.48      A    C  
ANISOU  438  CB  SER A  61     2241   2097   2682   -224    224    232  A    C  
ATOM    439  OG  SER A  61      10.487  18.186  25.677  1.00 20.91      A    O  
ANISOU  439  OG  SER A  61     2558   2429   2957   -167    209    224  A    O  
ATOM    440  N   ILE A  62      10.989  18.819  29.068  1.00 16.44      A    N  
ANISOU  440  N   ILE A  62     1846   1887   2513   -177    177    131  A    N  
ATOM    441  CA  ILE A  62      10.094  18.325  30.134  1.00 18.03      A    C  
ANISOU  441  CA  ILE A  62     2012   2112   2729   -135    147     83  A    C  
ATOM    442  C   ILE A  62       8.967  17.523  29.518  1.00 17.90      A    C  
ANISOU  442  C   ILE A  62     2017   2106   2680    -91    133     79  A    C  
ATOM    443  O   ILE A  62       8.645  16.423  30.022  1.00 17.89      A    O  
ANISOU  443  O   ILE A  62     1981   2148   2666    -71    141     55  A    O  
ATOM    444  CB  ILE A  62       9.521  19.458  30.984  1.00 18.70      A    C  
ANISOU  444  CB  ILE A  62     2098   2154   2853   -129    100     50  A    C  
ATOM    445  CG1 ILE A  62      10.628  20.028  31.877  1.00 22.65      A    C  
ANISOU  445  CG1 ILE A  62     2563   2655   3389   -168    111     42  A    C  
ATOM    446  CG2 ILE A  62       8.392  18.940  31.864  1.00 17.86      A    C  
ANISOU  446  CG2 ILE A  62     1962   2075   2751    -89     78     -4  A    C  
ATOM    447  CD1 ILE A  62      10.278  21.329  32.541  1.00 25.36      A    C  
ANISOU  447  CD1 ILE A  62     2916   2946   3774   -169     64     15  A    C  
ATOM    448  N   ILE A  63       8.349  18.021  28.454  1.00 15.14      A    N  
ANISOU  448  N   ILE A  63     1726   1710   2315    -76    108    100  A    N  
ATOM    449  CA  ILE A  63       7.231  17.272  27.845  1.00 18.52      A    C  
ANISOU  449  CA  ILE A  63     2171   2146   2720    -29     88     88  A    C  
ATOM    450  C   ILE A  63       7.692  15.906  27.330  1.00 17.32      A    C  
ANISOU  450  C   ILE A  63     2006   2045   2528    -28    130    108  A    C  
ATOM    451  O   ILE A  63       6.998  14.901  27.568  1.00 16.71      A    O  
ANISOU  451  O   ILE A  63     1903   2001   2444      0    125     81  A    O  
ATOM    452  CB  ILE A  63       6.536  18.072  26.743  1.00 20.82      A    C  
ANISOU  452  CB  ILE A  63     2539   2371   3000     -8     40    107  A    C  
ATOM    453  CG1 ILE A  63       5.792  19.215  27.398  1.00 24.27      A    C  
ANISOU  453  CG1 ILE A  63     2979   2760   3485     10    -21     66  A    C  
ATOM    454  CG2 ILE A  63       5.663  17.176  25.848  1.00 20.21      A    C  
ANISOU  454  CG2 ILE A  63     2484   2304   2891     37     23    103  A    C  
ATOM    455  CD1 ILE A  63       5.398  20.319  26.433  1.00 40.13      A    C  
ANISOU  455  CD1 ILE A  63     5079   4683   5488     25    -81     88  A    C  
ATOM    456  N   HIS A  64       8.821  15.820  26.646  1.00 15.23      A    N  
ANISOU  456  N   HIS A  64     1755   1793   2239    -60    174    148  A    N  
ATOM    457  CA  HIS A  64       9.289  14.525  26.167  1.00 14.23      A    C  
ANISOU  457  CA  HIS A  64     1611   1718   2079    -52    210    156  A    C  
ATOM    458  C   HIS A  64       9.609  13.607  27.332  1.00 16.27      A    C  
ANISOU  458  C   HIS A  64     1805   2023   2355    -48    218    123  A    C  
ATOM    459  O   HIS A  64       9.303  12.391  27.313  1.00 13.43      A    O  
ANISOU  459  O   HIS A  64     1433   1694   1976    -21    216    110  A    O  
ATOM    460  CB  HIS A  64      10.535  14.640  25.275  1.00 15.57      A    C  
ANISOU  460  CB  HIS A  64     1795   1900   2222    -92    263    191  A    C  
ATOM    461  CG  HIS A  64      10.209  15.025  23.872  1.00 18.44      A    C  
ANISOU  461  CG  HIS A  64     2239   2228   2538    -93    262    229  A    C  
ATOM    462  CD2 HIS A  64       9.132  15.660  23.357  1.00 23.77      A    C  
ANISOU  462  CD2 HIS A  64     2984   2846   3203    -67    209    240  A    C  
ATOM    463  ND1 HIS A  64      10.986  14.654  22.800  1.00 24.72      A    N  
ANISOU  463  ND1 HIS A  64     3058   3050   3286   -114    313    255  A    N  
ATOM    464  CE1 HIS A  64      10.455  15.122  21.690  1.00 28.64      A    C  
ANISOU  464  CE1 HIS A  64     3644   3501   3737   -110    297    289  A    C  
ATOM    465  NE2 HIS A  64       9.328  15.738  21.995  1.00 32.11      A    N  
ANISOU  465  NE2 HIS A  64     4116   3886   4200    -79    227    280  A    N  
ATOM    466  N   ALA A  65      10.235  14.164  28.365  1.00 13.35      A    N  
ANISOU  466  N   ALA A  65     1399   1653   2019    -75    220    109  A    N  
ATOM    467  CA  ALA A  65      10.654  13.341  29.481  1.00 12.75      A    C  
ANISOU  467  CA  ALA A  65     1276   1614   1952    -72    221     79  A    C  
ATOM    468  C   ALA A  65       9.437  12.755  30.188  1.00 13.69      A    C  
ANISOU  468  C   ALA A  65     1397   1738   2066    -46    192     51  A    C  
ATOM    469  O   ALA A  65       9.457  11.581  30.605  1.00 12.61      A    O  
ANISOU  469  O   ALA A  65     1251   1631   1912    -36    191     39  A    O  
ATOM    470  CB  ALA A  65      11.504  14.148  30.446  1.00 11.72      A    C  
ANISOU  470  CB  ALA A  65     1114   1477   1860   -103    221     66  A    C  
ATOM    471  N   LYS A  66       8.410  13.600  30.405  1.00 13.91      A    N  
ANISOU  471  N   LYS A  66     1437   1736   2111    -40    169     35  A    N  
ATOM    472  CA  LYS A  66       7.176  13.128  31.067  1.00 14.14      A    C  
ANISOU  472  CA  LYS A  66     1459   1775   2139    -25    153     -5  A    C  
ATOM    473  C   LYS A  66       6.444  12.108  30.157  1.00 15.66      A    C  
ANISOU  473  C   LYS A  66     1668   1979   2304      1    150      1  A    C  
ATOM    474  O   LYS A  66       5.946  11.083  30.680  1.00 13.44      A    O  
ANISOU  474  O   LYS A  66     1377   1723   2008      1    153    -20  A    O  
ATOM    475  CB  LYS A  66       6.296  14.311  31.508  1.00 15.45      A    C  
ANISOU  475  CB  LYS A  66     1622   1912   2339    -21    125    -39  A    C  
ATOM    476  CG  LYS A  66       5.150  13.895  32.398  1.00 16.41      A    C  
ANISOU  476  CG  LYS A  66     1719   2056   2462    -16    121    -94  A    C  
ATOM    477  CD  LYS A  66       4.286  15.086  32.800  1.00 17.32      A    C  
ANISOU  477  CD  LYS A  66     1821   2145   2615     -4     93   -143  A    C  
ATOM    478  CE  LYS A  66       3.289  14.660  33.844  1.00 18.98      A    C  
ANISOU  478  CE  LYS A  66     1997   2392   2824    -13    104   -208  A    C  
ATOM    479  NZ  LYS A  66       2.464  15.847  34.200  1.00 30.71      A    N1+
ANISOU  479  NZ  LYS A  66     3459   3856   4353      5     74   -269  A    N1+
ATOM    480  N   ARG A  67       6.468  12.293  28.823  1.00 13.39      A    N  
ANISOU  480  N   ARG A  67     1412   1672   2004     18    147     31  A    N  
ATOM    481  CA  ARG A  67       5.897  11.330  27.909  1.00 13.24      A    C  
ANISOU  481  CA  ARG A  67     1411   1661   1958     45    142     35  A    C  
ATOM    482  C   ARG A  67       6.601   9.987  28.014  1.00 13.93      A    C  
ANISOU  482  C   ARG A  67     1487   1787   2020     42    164     45  A    C  
ATOM    483  O   ARG A  67       5.966   8.914  27.900  1.00 13.58      A    O  
ANISOU  483  O   ARG A  67     1444   1756   1959     57    155     32  A    O  
ATOM    484  CB  ARG A  67       5.953  11.780  26.449  1.00 15.88      A    C  
ANISOU  484  CB  ARG A  67     1794   1968   2273     63    134     69  A    C  
ATOM    485  CG  ARG A  67       5.009  12.881  26.124  1.00 23.68      A    C  
ANISOU  485  CG  ARG A  67     2809   2906   3280     82     91     56  A    C  
ATOM    486  CD  ARG A  67       5.252  13.330  24.678  1.00 23.97      A    C  
ANISOU  486  CD  ARG A  67     2917   2908   3283     91     82    101  A    C  
ATOM    487  NE  ARG A  67       4.258  14.300  24.277  1.00 29.60      A    N  
ANISOU  487  NE  ARG A  67     3672   3563   4012    120     22     85  A    N  
ATOM    488  CZ  ARG A  67       4.287  14.943  23.119  1.00 26.80      A    C  
ANISOU  488  CZ  ARG A  67     3398   3159   3626    128     -4    121  A    C  
ATOM    489  NH1 ARG A  67       5.237  14.697  22.249  1.00 25.06      A    N1+
ANISOU  489  NH1 ARG A  67     3218   2949   3353    103     40    172  A    N1+
ATOM    490  NH2 ARG A  67       3.339  15.818  22.826  1.00 30.93      A    N  
ANISOU  490  NH2 ARG A  67     3963   3622   4168    163    -75    100  A    N  
ATOM    491  N   THR A  68       7.928  10.017  28.117  1.00 11.62      A    N  
ANISOU  491  N   THR A  68     1183   1509   1725     25    186     64  A    N  
ATOM    492  CA  THR A  68       8.729   8.808  28.205  1.00 12.82      A    C  
ANISOU  492  CA  THR A  68     1321   1691   1857     31    196     65  A    C  
ATOM    493  C   THR A  68       8.343   8.072  29.472  1.00 13.46      A    C  
ANISOU  493  C   THR A  68     1394   1782   1939     24    178     39  A    C  
ATOM    494  O   THR A  68       8.092   6.855  29.462  1.00 12.98      A    O  
ANISOU  494  O   THR A  68     1346   1732   1857     36    166     33  A    O  
ATOM    495  CB  THR A  68      10.238   9.173  28.201  1.00 13.20      A    C  
ANISOU  495  CB  THR A  68     1345   1755   1917     12    220     74  A    C  
ATOM    496  CG2 THR A  68      11.114   7.971  28.361  1.00 15.05      A    C  
ANISOU  496  CG2 THR A  68     1557   2019   2140     26    218     60  A    C  
ATOM    497  OG1 THR A  68      10.549   9.774  26.936  1.00 12.75      A    O  
ANISOU  497  OG1 THR A  68     1307   1692   1847      7    246    101  A    O  
ATOM    498  N   TYR A  69       8.326   8.814  30.596  1.00 11.89      A    N  
ANISOU  498  N   TYR A  69     1181   1575   1761      0    175     22  A    N  
ATOM    499  CA  TYR A  69       7.988   8.258  31.885  1.00 11.65      A    C  
ANISOU  499  CA  TYR A  69     1155   1551   1720    -18    164     -1  A    C  
ATOM    500  C   TYR A  69       6.593   7.642  31.852  1.00 11.05      A    C  
ANISOU  500  C   TYR A  69     1093   1477   1630    -18    161    -19  A    C  
ATOM    501  O   TYR A  69       6.387   6.498  32.329  1.00 11.87      A    O  
ANISOU  501  O   TYR A  69     1217   1587   1706    -29    155    -24  A    O  
ATOM    502  CB  TYR A  69       8.072   9.325  32.962  1.00 11.78      A    C  
ANISOU  502  CB  TYR A  69     1156   1561   1760    -41    165    -20  A    C  
ATOM    503  CG  TYR A  69       7.768   8.823  34.328  1.00 11.30      A    C  
ANISOU  503  CG  TYR A  69     1108   1507   1677    -64    157    -44  A    C  
ATOM    504  CD1 TYR A  69       8.627   7.949  34.974  1.00 11.60      A    C  
ANISOU  504  CD1 TYR A  69     1166   1550   1691    -67    139    -40  A    C  
ATOM    505  CD2 TYR A  69       6.612   9.197  34.973  1.00 12.47      A    C  
ANISOU  505  CD2 TYR A  69     1255   1658   1825    -83    166    -77  A    C  
ATOM    506  CE1 TYR A  69       8.366   7.486  36.239  1.00 12.62      A    C  
ANISOU  506  CE1 TYR A  69     1327   1679   1788    -93    129    -58  A    C  
ATOM    507  CE2 TYR A  69       6.324   8.769  36.239  1.00 12.40      A    C  
ANISOU  507  CE2 TYR A  69     1266   1659   1787   -115    170   -101  A    C  
ATOM    508  CZ  TYR A  69       7.206   7.933  36.902  1.00 12.82      A    C  
ANISOU  508  CZ  TYR A  69     1353   1710   1806   -124    151    -87  A    C  
ATOM    509  OH  TYR A  69       6.861   7.507  38.183  1.00 16.12      A    O  
ANISOU  509  OH  TYR A  69     1811   2132   2181   -162    153   -106  A    O  
ATOM    510  N   ARG A  70       5.626   8.361  31.298  1.00 12.11      A    N  
ANISOU  510  N   ARG A  70     1219   1600   1784     -8    163    -31  A    N  
ATOM    511  CA  ARG A  70       4.250   7.882  31.177  1.00 12.14      A    C  
ANISOU  511  CA  ARG A  70     1222   1606   1786     -7    159    -61  A    C  
ATOM    512  C   ARG A  70       4.165   6.572  30.434  1.00 12.76      A    C  
ANISOU  512  C   ARG A  70     1320   1689   1838      7    153    -46  A    C  
ATOM    513  O   ARG A  70       3.475   5.637  30.903  1.00 12.19      A    O  
ANISOU  513  O   ARG A  70     1256   1626   1750    -15    155    -65  A    O  
ATOM    514  CB  ARG A  70       3.407   8.937  30.476  1.00 13.30      A    C  
ANISOU  514  CB  ARG A  70     1355   1733   1964     16    145    -80  A    C  
ATOM    515  CG  ARG A  70       1.952   8.526  30.285  1.00 14.89      A    C  
ANISOU  515  CG  ARG A  70     1542   1939   2177     22    136   -126  A    C  
ATOM    516  CD  ARG A  70       1.163   9.548  29.500  1.00 15.42      A    C  
ANISOU  516  CD  ARG A  70     1601   1979   2279     60    103   -150  A    C  
ATOM    517  NE  ARG A  70       1.127  10.806  30.235  1.00 14.78      A    N  
ANISOU  517  NE  ARG A  70     1501   1887   2228     53     98   -177  A    N  
ATOM    518  CZ  ARG A  70       1.692  11.946  29.844  1.00 20.05      A    C  
ANISOU  518  CZ  ARG A  70     2189   2521   2908     69     78   -151  A    C  
ATOM    519  NH1 ARG A  70       2.365  12.055  28.702  1.00 23.68      A    N1+
ANISOU  519  NH1 ARG A  70     2692   2957   3349     87     67    -97  A    N1+
ATOM    520  NH2 ARG A  70       1.598  13.006  30.633  1.00 20.56      A    N  
ANISOU  520  NH2 ARG A  70     2235   2574   3003     63     69   -183  A    N  
ATOM    521  N   GLU A  71       4.786   6.499  29.272  1.00 11.02      A    N  
ANISOU  521  N   GLU A  71     1111   1463   1610     39    147    -15  A    N  
ATOM    522  CA  GLU A  71       4.681   5.278  28.457  1.00 10.45      A    C  
ANISOU  522  CA  GLU A  71     1059   1396   1515     61    135     -5  A    C  
ATOM    523  C   GLU A  71       5.296   4.092  29.198  1.00 11.13      A    C  
ANISOU  523  C   GLU A  71     1160   1491   1577     45    130      0  A    C  
ATOM    524  O   GLU A  71       4.756   3.032  29.209  1.00 11.46      A    O  
ANISOU  524  O   GLU A  71     1220   1531   1603     41    119     -8  A    O  
ATOM    525  CB  GLU A  71       5.255   5.487  27.069  1.00 11.39      A    C  
ANISOU  525  CB  GLU A  71     1191   1512   1625     97    134     23  A    C  
ATOM    526  CG  GLU A  71       5.220   4.224  26.238  1.00 12.98      A    C  
ANISOU  526  CG  GLU A  71     1412   1720   1800    124    121     27  A    C  
ATOM    527  CD  GLU A  71       5.474   4.407  24.768  1.00 14.93      A    C  
ANISOU  527  CD  GLU A  71     1680   1964   2029    158    121     47  A    C  
ATOM    528  OE1 GLU A  71       6.023   5.441  24.349  1.00 15.98      A    O  
ANISOU  528  OE1 GLU A  71     1817   2092   2160    156    139     66  A    O  
ATOM    529  OE2 GLU A  71       5.065   3.525  23.955  1.00 15.25      A    O1-
ANISOU  529  OE2 GLU A  71     1738   2004   2050    188    103     42  A    O1-
ATOM    530  N   LEU A  72       6.461   4.297  29.794  1.00 10.58      A    N  
ANISOU  530  N   LEU A  72     1086   1428   1506     39    133     10  A    N  
ATOM    531  CA  LEU A  72       7.123   3.236  30.507  1.00 11.31      A    C  
ANISOU  531  CA  LEU A  72     1202   1520   1577     32    112     11  A    C  
ATOM    532  C   LEU A  72       6.260   2.791  31.699  1.00 11.39      A    C  
ANISOU  532  C   LEU A  72     1237   1521   1568    -11    110     -5  A    C  
ATOM    533  O   LEU A  72       6.110   1.583  31.945  1.00 11.32      A    O  
ANISOU  533  O   LEU A  72     1269   1500   1532    -22     88     -4  A    O  
ATOM    534  CB  LEU A  72       8.532   3.671  30.939  1.00 12.25      A    C  
ANISOU  534  CB  LEU A  72     1302   1645   1706     38    109     14  A    C  
ATOM    535  CG  LEU A  72       9.342   2.622  31.710  1.00 11.89      A    C  
ANISOU  535  CG  LEU A  72     1283   1592   1642     43     70      7  A    C  
ATOM    536  CD1 LEU A  72       9.425   1.322  30.920  1.00 11.62      A    C  
ANISOU  536  CD1 LEU A  72     1270   1555   1589     76     43      9  A    C  
ATOM    537  CD2 LEU A  72      10.715   3.157  32.059  1.00 15.60      A    C  
ANISOU  537  CD2 LEU A  72     1721   2072   2135     53     62     -2  A    C  
ATOM    538  N   ARG A  73       5.684   3.750  32.467  1.00 10.91      A    N  
ANISOU  538  N   ARG A  73     1160   1465   1521    -43    132    -24  A    N  
ATOM    539  CA  ARG A  73       4.856   3.382  33.569  1.00 10.97      A    C  
ANISOU  539  CA  ARG A  73     1191   1471   1505    -94    143    -45  A    C  
ATOM    540  C   ARG A  73       3.665   2.548  33.108  1.00 12.48      A    C  
ANISOU  540  C   ARG A  73     1392   1663   1690   -108    149    -59  A    C  
ATOM    541  O   ARG A  73       3.297   1.534  33.723  1.00 13.25      A    O  
ANISOU  541  O   ARG A  73     1532   1751   1752   -149    148    -61  A    O  
ATOM    542  CB  ARG A  73       4.330   4.619  34.322  1.00 13.00      A    C  
ANISOU  542  CB  ARG A  73     1417   1739   1782   -118    170    -75  A    C  
ATOM    543  CG  ARG A  73       5.399   5.303  35.196  1.00 13.91      A    C  
ANISOU  543  CG  ARG A  73     1534   1853   1898   -122    162    -69  A    C  
ATOM    544  CD  ARG A  73       5.755   4.535  36.498  1.00 15.93      A    C  
ANISOU  544  CD  ARG A  73     1847   2102   2104   -158    149    -68  A    C  
ATOM    545  NE  ARG A  73       4.518   4.169  37.206  1.00 17.32      A    N  
ANISOU  545  NE  ARG A  73     2044   2286   2249   -215    180    -95  A    N  
ATOM    546  CZ  ARG A  73       3.786   4.992  37.928  1.00 19.40      A    C  
ANISOU  546  CZ  ARG A  73     2285   2570   2519   -248    214   -134  A    C  
ATOM    547  NH1 ARG A  73       4.153   6.231  38.145  1.00 21.49      A    N1+
ANISOU  547  NH1 ARG A  73     2511   2839   2815   -228    214   -147  A    N1+
ATOM    548  NH2 ARG A  73       2.630   4.578  38.446  1.00 23.90      A    N  
ANISOU  548  NH2 ARG A  73     2864   3155   3061   -304    251   -167  A    N  
ATOM    549  N   LEU A  74       3.018   2.985  32.035  1.00 11.94      A    N  
ANISOU  549  N   LEU A  74     1286   1597   1652    -78    153    -70  A    N  
ATOM    550  CA  LEU A  74       1.848   2.278  31.570  1.00 12.61      A    C  
ANISOU  550  CA  LEU A  74     1367   1682   1740    -89    155    -92  A    C  
ATOM    551  C   LEU A  74       2.223   0.867  31.095  1.00 11.73      A    C  
ANISOU  551  C   LEU A  74     1301   1555   1601    -77    127    -67  A    C  
ATOM    552  O   LEU A  74       1.561  -0.104  31.465  1.00 11.89      A    O  
ANISOU  552  O   LEU A  74     1349   1568   1601   -119    128    -78  A    O  
ATOM    553  CB  LEU A  74       1.194   3.061  30.415  1.00 12.22      A    C  
ANISOU  553  CB  LEU A  74     1278   1633   1732    -45    147   -111  A    C  
ATOM    554  CG  LEU A  74       0.352   4.251  30.786  1.00 12.40      A    C  
ANISOU  554  CG  LEU A  74     1255   1665   1791    -53    163   -157  A    C  
ATOM    555  CD1 LEU A  74       0.099   5.133  29.569  1.00 14.68      A    C  
ANISOU  555  CD1 LEU A  74     1527   1939   2114      4    136   -161  A    C  
ATOM    556  CD2 LEU A  74      -0.958   3.820  31.417  1.00 15.84      A    C  
ANISOU  556  CD2 LEU A  74     1667   2117   2235   -103    186   -215  A    C  
ATOM    557  N   LEU A  75       3.256   0.738  30.295  1.00 11.88      A    N  
ANISOU  557  N   LEU A  75     1328   1570   1618    -25    103    -37  A    N  
ATOM    558  CA  LEU A  75       3.695  -0.577  29.789  1.00 12.11      A    C  
ANISOU  558  CA  LEU A  75     1395   1583   1623     -4     69    -21  A    C  
ATOM    559  C   LEU A  75       4.109  -1.481  30.926  1.00 13.76      A    C  
ANISOU  559  C   LEU A  75     1658   1773   1796    -41     50    -12  A    C  
ATOM    560  O   LEU A  75       3.753  -2.645  30.934  1.00 14.91      A    O  
ANISOU  560  O   LEU A  75     1848   1897   1921    -57     26    -10  A    O  
ATOM    561  CB  LEU A  75       4.828  -0.442  28.792  1.00 13.11      A    C  
ANISOU  561  CB  LEU A  75     1511   1717   1753     57     54     -1  A    C  
ATOM    562  CG  LEU A  75       4.421   0.064  27.450  1.00 14.12      A    C  
ANISOU  562  CG  LEU A  75     1616   1854   1898     96     61     -3  A    C  
ATOM    563  CD1 LEU A  75       5.709   0.473  26.723  1.00 18.34      A    C  
ANISOU  563  CD1 LEU A  75     2138   2403   2429    136     67     16  A    C  
ATOM    564  CD2 LEU A  75       3.645  -1.046  26.718  1.00 16.53      A    C  
ANISOU  564  CD2 LEU A  75     1940   2145   2194    110     36    -13  A    C  
ATOM    565  N   LYS A  76       4.784  -0.941  31.948  1.00 11.86      A    N  
ANISOU  565  N   LYS A  76     1424   1534   1547    -59     54     -7  A    N  
ATOM    566  CA  LYS A  76       5.161  -1.802  33.073  1.00 13.82      A    C  
ANISOU  566  CA  LYS A  76     1742   1757   1753    -93     25      2  A    C  
ATOM    567  C   LYS A  76       3.990  -2.304  33.866  1.00 12.58      A    C  
ANISOU  567  C   LYS A  76     1626   1589   1567   -170     48     -8  A    C  
ATOM    568  O   LYS A  76       4.079  -3.355  34.533  1.00 16.40      A    O  
ANISOU  568  O   LYS A  76     2189   2038   2005   -205     18      4  A    O  
ATOM    569  CB  LYS A  76       6.141  -1.083  34.010  1.00 13.65      A    C  
ANISOU  569  CB  LYS A  76     1720   1738   1728    -93     19      4  A    C  
ATOM    570  CG  LYS A  76       7.542  -0.980  33.473  1.00 12.07      A    C  
ANISOU  570  CG  LYS A  76     1494   1542   1550    -29    -14     10  A    C  
ATOM    571  CD  LYS A  76       8.516  -0.374  34.474  1.00 14.99      A    C  
ANISOU  571  CD  LYS A  76     1864   1910   1920    -31    -29      5  A    C  
ATOM    572  CE  LYS A  76       8.768  -1.240  35.670  1.00 15.16      A    C  
ANISOU  572  CE  LYS A  76     1971   1895   1895    -55    -78      7  A    C  
ATOM    573  NZ  LYS A  76       9.721  -0.609  36.609  1.00 17.09      A    N1+
ANISOU  573  NZ  LYS A  76     2215   2138   2142    -50   -101     -3  A    N1+
ATOM    574  N   HIS A  77       2.901  -1.544  33.864  1.00 12.21      A    N  
ANISOU  574  N   HIS A  77     1529   1569   1542   -201    100    -36  A    N  
ATOM    575  CA  HIS A  77       1.730  -1.919  34.587  1.00 13.32      A    C  
ANISOU  575  CA  HIS A  77     1690   1710   1659   -282    137    -59  A    C  
ATOM    576  C   HIS A  77       0.975  -3.070  33.927  1.00 14.44      A    C  
ANISOU  576  C   HIS A  77     1853   1834   1799   -297    125    -63  A    C  
ATOM    577  O   HIS A  77       0.340  -3.853  34.618  1.00 14.59      A    O  
ANISOU  577  O   HIS A  77     1923   1838   1781   -375    141    -68  A    O  
ATOM    578  CB  HIS A  77       0.775  -0.724  34.764  1.00 14.47      A    C  
ANISOU  578  CB  HIS A  77     1761   1895   1841   -303    193   -105  A    C  
ATOM    579  CG  HIS A  77      -0.257  -0.974  35.812  1.00 16.67      A    C  
ANISOU  579  CG  HIS A  77     2058   2186   2091   -397    243   -140  A    C  
ATOM    580  CD2 HIS A  77      -1.545  -1.376  35.740  1.00 21.18      A    C  
ANISOU  580  CD2 HIS A  77     2605   2771   2671   -453    281   -182  A    C  
ATOM    581  ND1 HIS A  77       0.055  -0.919  37.141  1.00 22.31      A    N  
ANISOU  581  ND1 HIS A  77     2826   2899   2751   -452    260   -133  A    N  
ATOM    582  CE1 HIS A  77      -1.008  -1.245  37.855  1.00 21.72      A    C  
ANISOU  582  CE1 HIS A  77     2765   2840   2650   -543    314   -169  A    C  
ATOM    583  NE2 HIS A  77      -1.985  -1.516  37.024  1.00 22.30      A    N  
ANISOU  583  NE2 HIS A  77     2784   2925   2765   -546    330   -201  A    N  
ATOM    584  N   MET A  78       0.958  -3.098  32.587  1.00 13.65      A    N  
ANISOU  584  N   MET A  78     1711   1737   1738   -232    103    -63  A    N  
ATOM    585  CA  MET A  78      -0.006  -3.942  31.900  1.00 13.72      A    C  
ANISOU  585  CA  MET A  78     1718   1735   1758   -246     99    -81  A    C  
ATOM    586  C   MET A  78       0.443  -5.363  31.926  1.00 14.84      A    C  
ANISOU  586  C   MET A  78     1944   1834   1862   -253     50    -50  A    C  
ATOM    587  O   MET A  78       1.420  -5.706  31.241  1.00 17.44      A    O  
ANISOU  587  O   MET A  78     2288   2148   2191   -182      0    -27  A    O  
ATOM    588  CB  MET A  78      -0.167  -3.473  30.464  1.00 15.03      A    C  
ANISOU  588  CB  MET A  78     1823   1915   1972   -169     84    -93  A    C  
ATOM    589  CG  MET A  78      -0.815  -2.131  30.332  1.00 17.78      A    C  
ANISOU  589  CG  MET A  78     2097   2295   2362   -160    118   -129  A    C  
ATOM    590  SD  MET A  78      -2.386  -1.896  31.082  1.00 18.39      A    S  
ANISOU  590  SD  MET A  78     2130   2396   2462   -239    170   -196  A    S  
ATOM    591  CE  MET A  78      -2.566  -0.114  30.898  1.00 27.77      A    C  
ANISOU  591  CE  MET A  78     3241   3611   3698   -193    183   -229  A    C  
ATOM    592  N   LYS A  79      -0.327  -6.235  32.627  1.00 12.47      A    N  
ANISOU  592  N   LYS A  79     1697   1510   1531   -341     64    -57  A    N  
ATOM    593  CA ALYS A  79      -0.039  -7.642  32.761  0.50 13.99      A    C  
ANISOU  593  CA ALYS A  79     1985   1648   1682   -362     13    -28  A    C  
ATOM    594  CA BLYS A  79      -0.040  -7.642  32.751  0.50 14.09      A    C  
ANISOU  594  CA BLYS A  79     1998   1662   1696   -361     12    -29  A    C  
ATOM    595  C   LYS A  79      -1.302  -8.444  32.528  1.00 14.24      A    C  
ANISOU  595  C   LYS A  79     2022   1668   1722   -428     30    -53  A    C  
ATOM    596  O   LYS A  79      -1.927  -8.947  33.472  1.00 17.13      A    O  
ANISOU  596  O   LYS A  79     2443   2016   2048   -534     63    -56  A    O  
ATOM    597  CB ALYS A  79       0.565  -7.936  34.122  0.50 17.61      A    C  
ANISOU  597  CB ALYS A  79     2540   2075   2075   -416      1      1  A    C  
ATOM    598  CB BLYS A  79       0.587  -7.943  34.093  0.50 17.65      A    C  
ANISOU  598  CB BLYS A  79     2544   2080   2081   -413     -1      1  A    C  
ATOM    599  CG ALYS A  79       1.922  -7.273  34.291  0.50 17.71      A    C  
ANISOU  599  CG ALYS A  79     2546   2096   2089   -343    -32     19  A    C  
ATOM    600  CG BLYS A  79       1.938  -7.266  34.234  0.50 17.32      A    C  
ANISOU  600  CG BLYS A  79     2494   2047   2041   -339    -33     19  A    C  
ATOM    601  CD ALYS A  79       2.470  -7.471  35.678  0.50 25.10      A    C  
ANISOU  601  CD ALYS A  79     3577   3001   2961   -392    -50     41  A    C  
ATOM    602  CD BLYS A  79       2.613  -7.657  35.515  0.50 23.08      A    C  
ANISOU  602  CD BLYS A  79     3327   2736   2707   -378    -67     45  A    C  
ATOM    603  CE ALYS A  79       3.853  -6.852  35.815  0.50 32.85      A    C  
ANISOU  603  CE ALYS A  79     4543   3987   3952   -314    -91     50  A    C  
ATOM    604  CE BLYS A  79       3.957  -6.964  35.680  0.50 26.82      A    C  
ANISOU  604  CE BLYS A  79     3782   3220   3191   -303   -101     52  A    C  
ATOM    605  NZ ALYS A  79       3.790  -5.408  36.155  0.50 33.65      A    N1+
ANISOU  605  NZ ALYS A  79     4566   4141   4078   -317    -31     32  A    N1+
ATOM    606  NZ BLYS A  79       4.661  -7.462  36.897  0.50 22.68      A    N1+
ANISOU  606  NZ BLYS A  79     3369   2646   2602   -330   -155     74  A    N1+
ATOM    607  N   HIS A  80      -1.682  -8.559  31.267  1.00 12.24      A    N  
ANISOU  607  N   HIS A  80     1713   1422   1516   -371     11    -74  A    N  
ATOM    608  CA  HIS A  80      -2.906  -9.220  30.852  1.00 11.71      A    C  
ANISOU  608  CA  HIS A  80     1630   1346   1473   -420     23   -108  A    C  
ATOM    609  C   HIS A  80      -2.782  -9.759  29.424  1.00 11.83      A    C  
ANISOU  609  C   HIS A  80     1631   1345   1521   -332    -38   -109  A    C  
ATOM    610  O   HIS A  80      -2.150  -9.106  28.568  1.00 12.30      A    O  
ANISOU  610  O   HIS A  80     1646   1426   1601   -235    -59   -104  A    O  
ATOM    611  CB  HIS A  80      -4.047  -8.181  30.908  1.00 12.64      A    C  
ANISOU  611  CB  HIS A  80     1644   1519   1638   -452     94   -168  A    C  
ATOM    612  CG  HIS A  80      -5.408  -8.735  30.684  1.00 13.10      A    C  
ANISOU  612  CG  HIS A  80     1669   1578   1729   -517    119   -220  A    C  
ATOM    613  CD2 HIS A  80      -6.385  -9.027  31.566  1.00 12.09      A    C  
ANISOU  613  CD2 HIS A  80     1542   1460   1591   -640    181   -255  A    C  
ATOM    614  ND1 HIS A  80      -5.947  -8.991  29.448  1.00 12.27      A    N  
ANISOU  614  ND1 HIS A  80     1516   1471   1677   -463     82   -250  A    N  
ATOM    615  CE1 HIS A  80      -7.175  -9.455  29.579  1.00 13.04      A    C  
ANISOU  615  CE1 HIS A  80     1584   1571   1801   -546    116   -304  A    C  
ATOM    616  NE2 HIS A  80      -7.479  -9.448  30.867  1.00 13.08      A    N  
ANISOU  616  NE2 HIS A  80     1612   1587   1770   -658    183   -311  A    N  
ATOM    617  N   GLU A  81      -3.399 -10.890  29.161  1.00 14.20      A    N  
ANISOU  617  N   GLU A  81     1966   1607   1821   -371    -63   -119  A    N  
ATOM    618  CA  GLU A  81      -3.284 -11.547  27.860  1.00 13.17      A    C  
ANISOU  618  CA  GLU A  81     1834   1455   1715   -291   -128   -123  A    C  
ATOM    619  C   GLU A  81      -3.734 -10.711  26.680  1.00 12.08      A    C  
ANISOU  619  C   GLU A  81     1600   1359   1632   -214   -123   -161  A    C  
ATOM    620  O   GLU A  81      -3.323 -10.923  25.563  1.00 14.78      A    O  
ANISOU  620  O   GLU A  81     1939   1695   1982   -126   -172   -157  A    O  
ATOM    621  CB  GLU A  81      -4.008 -12.879  27.837  1.00 17.87      A    C  
ANISOU  621  CB  GLU A  81     2484   2000   2308   -356   -154   -132  A    C  
ATOM    622  CG  GLU A  81      -3.521 -13.869  28.920  1.00 20.46      A    C  
ANISOU  622  CG  GLU A  81     2936   2266   2571   -430   -179    -88  A    C  
ATOM    623  CD  GLU A  81      -4.318 -13.770  30.255  1.00 39.30      A    C  
ANISOU  623  CD  GLU A  81     5347   4656   4928   -575   -100    -93  A    C  
ATOM    624  OE1 GLU A  81      -4.759 -12.653  30.741  1.00 37.16      A    O  
ANISOU  624  OE1 GLU A  81     5001   4446   4672   -606    -22   -122  A    O  
ATOM    625  OE2 GLU A  81      -4.493 -14.851  30.858  1.00 57.62      A    O1-
ANISOU  625  OE2 GLU A  81     7771   6917   7206   -662   -118    -72  A    O1-
ATOM    626  N   ASN A  82      -4.743  -9.854  26.918  1.00 11.54      A    N  
ANISOU  626  N   ASN A  82     1455   1329   1600   -255    -65   -207  A    N  
ATOM    627  CA  ASN A  82      -5.329  -9.068  25.837  1.00 11.03      A    C  
ANISOU  627  CA  ASN A  82     1309   1294   1589   -186    -73   -250  A    C  
ATOM    628  C   ASN A  82      -4.859  -7.610  25.831  1.00 10.48      A    C  
ANISOU  628  C   ASN A  82     1195   1263   1525   -135    -48   -244  A    C  
ATOM    629  O   ASN A  82      -5.517  -6.764  25.200  1.00 11.25      A    O  
ANISOU  629  O   ASN A  82     1226   1383   1667    -95    -48   -286  A    O  
ATOM    630  CB  ASN A  82      -6.867  -9.150  25.872  1.00 10.87      A    C  
ANISOU  630  CB  ASN A  82     1225   1286   1622   -249    -45   -322  A    C  
ATOM    631  CG  ASN A  82      -7.347 -10.576  25.870  1.00 11.83      A    C  
ANISOU  631  CG  ASN A  82     1391   1364   1738   -311    -67   -329  A    C  
ATOM    632  ND2 ASN A  82      -7.011 -11.314  24.826  1.00 12.40      A    N  
ANISOU  632  ND2 ASN A  82     1497   1404   1810   -240   -137   -314  A    N  
ATOM    633  OD1 ASN A  82      -7.986 -11.035  26.781  1.00 14.04      A    O  
ANISOU  633  OD1 ASN A  82     1682   1639   2013   -423    -22   -347  A    O  
ATOM    634  N   VAL A  83      -3.756  -7.319  26.484  1.00 10.71      A    N  
ANISOU  634  N   VAL A  83     1261   1295   1514   -132    -37   -195  A    N  
ATOM    635  CA  VAL A  83      -3.160  -5.981  26.454  1.00 10.61      A    C  
ANISOU  635  CA  VAL A  83     1214   1312   1504    -84    -17   -183  A    C  
ATOM    636  C   VAL A  83      -1.664  -6.126  26.178  1.00 11.62      A    C  
ANISOU  636  C   VAL A  83     1388   1431   1595    -25    -47   -129  A    C  
ATOM    637  O   VAL A  83      -1.018  -7.057  26.697  1.00 13.43      A    O  
ANISOU  637  O   VAL A  83     1678   1635   1790    -46    -68   -102  A    O  
ATOM    638  CB  VAL A  83      -3.380  -5.221  27.779  1.00 11.73      A    C  
ANISOU  638  CB  VAL A  83     1337   1478   1644   -155     40   -196  A    C  
ATOM    639  CG1 VAL A  83      -2.882  -3.812  27.695  1.00 11.21      A    C  
ANISOU  639  CG1 VAL A  83     1233   1437   1591   -107     53   -190  A    C  
ATOM    640  CG2 VAL A  83      -4.830  -5.245  28.197  1.00 12.42      A    C  
ANISOU  640  CG2 VAL A  83     1374   1580   1767   -228     78   -260  A    C  
ATOM    641  N   ILE A  84      -1.132  -5.264  25.324  1.00 11.91      A    N  
ANISOU  641  N   ILE A  84     1400   1486   1640     47    -54   -120  A    N  
ATOM    642  CA  ILE A  84       0.327  -5.315  25.120  1.00 12.50      A    C  
ANISOU  642  CA  ILE A  84     1504   1562   1683     95    -69    -80  A    C  
ATOM    643  C   ILE A  84       1.077  -5.235  26.455  1.00 14.58      A    C  
ANISOU  643  C   ILE A  84     1790   1825   1925     50    -51    -58  A    C  
ATOM    644  O   ILE A  84       0.639  -4.509  27.346  1.00 15.16      A    O  
ANISOU  644  O   ILE A  84     1842   1909   2006      0    -12    -68  A    O  
ATOM    645  CB  ILE A  84       0.768  -4.268  24.075  1.00 15.00      A    C  
ANISOU  645  CB  ILE A  84     1793   1902   2006    162    -64    -74  A    C  
ATOM    646  CG1 ILE A  84       2.146  -4.648  23.470  1.00 17.03      A    C  
ANISOU  646  CG1 ILE A  84     2073   2164   2234    216    -82    -48  A    C  
ATOM    647  CG2 ILE A  84       0.695  -2.888  24.640  1.00 17.17      A    C  
ANISOU  647  CG2 ILE A  84     2033   2194   2298    141    -24    -74  A    C  
ATOM    648  CD1 ILE A  84       2.143  -5.906  22.688  1.00 21.99      A    C  
ANISOU  648  CD1 ILE A  84     2732   2775   2848    252   -127    -58  A    C  
ATOM    649  N   GLY A  85       2.162  -5.997  26.534  1.00 15.11      A    N  
ANISOU  649  N   GLY A  85     1899   1876   1965     75    -85    -36  A    N  
ATOM    650  CA  GLY A  85       2.984  -6.012  27.722  1.00 17.28      A    C  
ANISOU  650  CA  GLY A  85     2205   2142   2218     45    -87    -19  A    C  
ATOM    651  C   GLY A  85       4.442  -5.726  27.393  1.00 16.36      A    C  
ANISOU  651  C   GLY A  85     2077   2041   2098    109   -103     -7  A    C  
ATOM    652  O   GLY A  85       4.887  -5.847  26.242  1.00 16.65      A    O  
ANISOU  652  O   GLY A  85     2096   2092   2140    170   -116    -12  A    O  
ATOM    653  N   LEU A  86       5.167  -5.486  28.439  1.00 13.67      A    N  
ANISOU  653  N   LEU A  86     1751   1698   1746     88   -104      3  A    N  
ATOM    654  CA  LEU A  86       6.574  -5.209  28.319  1.00 13.75      A    C  
ANISOU  654  CA  LEU A  86     1741   1723   1760    138   -119      3  A    C  
ATOM    655  C   LEU A  86       7.401  -6.440  28.598  1.00 14.49      A    C  
ANISOU  655  C   LEU A  86     1887   1784   1835    166   -189     -3  A    C  
ATOM    656  O   LEU A  86       7.419  -6.937  29.698  1.00 16.41      A    O  
ANISOU  656  O   LEU A  86     2190   1990   2055    128   -220      5  A    O  
ATOM    657  CB  LEU A  86       6.980  -4.078  29.254  1.00 15.63      A    C  
ANISOU  657  CB  LEU A  86     1955   1978   2007    109    -86      9  A    C  
ATOM    658  CG  LEU A  86       8.333  -3.367  29.070  1.00 16.64      A    C  
ANISOU  658  CG  LEU A  86     2036   2133   2152    150    -81      3  A    C  
ATOM    659  CD1 LEU A  86       8.428  -2.690  27.702  1.00 15.81      A    C  
ANISOU  659  CD1 LEU A  86     1880   2063   2065    186    -43      2  A    C  
ATOM    660  CD2 LEU A  86       8.471  -2.355  30.202  1.00 17.59      A    C  
ANISOU  660  CD2 LEU A  86     2146   2258   2278    110    -55      7  A    C  
ATOM    661  N   LEU A  87       8.097  -6.881  27.564  1.00 12.88      A    N  
ANISOU  661  N   LEU A  87     1662   1592   1640    233   -215    -20  A    N  
ATOM    662  CA  LEU A  87       8.996  -8.024  27.682  1.00 14.66      A    C  
ANISOU  662  CA  LEU A  87     1926   1788   1856    278   -293    -40  A    C  
ATOM    663  C   LEU A  87      10.381  -7.613  28.223  1.00 13.21      A    C  
ANISOU  663  C   LEU A  87     1713   1619   1686    308   -309    -59  A    C  
ATOM    664  O   LEU A  87      11.042  -8.408  28.919  1.00 15.31      A    O  
ANISOU  664  O   LEU A  87     2027   1846   1943    327   -385    -74  A    O  
ATOM    665  CB  LEU A  87       9.144  -8.719  26.340  1.00 16.88      A    C  
ANISOU  665  CB  LEU A  87     2192   2080   2141    342   -314    -63  A    C  
ATOM    666  CG  LEU A  87       7.857  -9.371  25.774  1.00 19.58      A    C  
ANISOU  666  CG  LEU A  87     2568   2397   2474    323   -320    -53  A    C  
ATOM    667  CD1 LEU A  87       8.168 -10.115  24.467  1.00 22.26      A    C  
ANISOU  667  CD1 LEU A  87     2897   2746   2814    398   -352    -83  A    C  
ATOM    668  CD2 LEU A  87       7.132 -10.267  26.773  1.00 27.45      A    C  
ANISOU  668  CD2 LEU A  87     3649   3330   3449    264   -362    -37  A    C  
ATOM    669  N   ASP A  88      10.803  -6.413  27.898  1.00 13.39      A    N  
ANISOU  669  N   ASP A  88     1663   1694   1731    311   -247    -63  A    N  
ATOM    670  CA  ASP A  88      12.105  -5.888  28.316  1.00 15.17      A    C  
ANISOU  670  CA  ASP A  88     1844   1942   1980    334   -253    -88  A    C  
ATOM    671  C   ASP A  88      12.139  -4.401  28.092  1.00 11.79      A    C  
ANISOU  671  C   ASP A  88     1350   1558   1571    306   -170    -75  A    C  
ATOM    672  O   ASP A  88      11.372  -3.868  27.297  1.00 13.53      A    O  
ANISOU  672  O   ASP A  88     1556   1797   1788    293   -117    -54  A    O  
ATOM    673  CB  ASP A  88      13.205  -6.577  27.520  1.00 13.98      A    C  
ANISOU  673  CB  ASP A  88     1657   1809   1845    409   -292   -138  A    C  
ATOM    674  CG  ASP A  88      14.567  -6.422  28.098  1.00 16.46      A    C  
ANISOU  674  CG  ASP A  88     1931   2134   2188    440   -326   -181  A    C  
ATOM    675  OD1 ASP A  88      14.775  -6.009  29.293  1.00 17.23      A    O  
ANISOU  675  OD1 ASP A  88     2048   2211   2290    410   -344   -173  A    O  
ATOM    676  OD2 ASP A  88      15.542  -6.771  27.290  1.00 17.64      A    O1-
ANISOU  676  OD2 ASP A  88     2023   2318   2359    501   -337   -237  A    O1-
ATOM    677  N   VAL A  89      12.972  -3.713  28.838  1.00 12.37      A    N  
ANISOU  677  N   VAL A  89     1393   1642   1665    298   -167    -86  A    N  
ATOM    678  CA  VAL A  89      13.307  -2.304  28.623  1.00 12.82      A    C  
ANISOU  678  CA  VAL A  89     1386   1738   1746    277    -97    -81  A    C  
ATOM    679  C   VAL A  89      14.771  -2.164  28.933  1.00 17.22      A    C  
ANISOU  679  C   VAL A  89     1890   2315   2336    304   -118   -125  A    C  
ATOM    680  O   VAL A  89      15.225  -2.686  29.930  1.00 17.07      A    O  
ANISOU  680  O   VAL A  89     1900   2267   2320    317   -185   -145  A    O  
ATOM    681  CB  VAL A  89      12.418  -1.344  29.465  1.00 12.98      A    C  
ANISOU  681  CB  VAL A  89     1425   1745   1763    216    -64    -47  A    C  
ATOM    682  CG1 VAL A  89      12.405  -1.705  30.955  1.00 14.91      A    C  
ANISOU  682  CG1 VAL A  89     1722   1951   1993    193   -114    -47  A    C  
ATOM    683  CG2 VAL A  89      12.859   0.089  29.239  1.00 16.69      A    C  
ANISOU  683  CG2 VAL A  89     1835   2246   2262    197     -5    -44  A    C  
ATOM    684  N   PHE A  90      15.479  -1.456  28.075  1.00 15.46      A    N  
ANISOU  684  N   PHE A  90     1597   2141   2137    310    -62   -144  A    N  
ATOM    685  CA  PHE A  90      16.935  -1.314  28.239  1.00 18.68      A    C  
ANISOU  685  CA  PHE A  90     1934   2577   2586    335    -73   -200  A    C  
ATOM    686  C   PHE A  90      17.436  -0.011  27.692  1.00 20.88      A    C  
ANISOU  686  C   PHE A  90     2145   2900   2888    300     12   -200  A    C  
ATOM    687  O   PHE A  90      16.747   0.708  26.951  1.00 17.37      A    O  
ANISOU  687  O   PHE A  90     1711   2466   2423    265     78   -156  A    O  
ATOM    688  CB  PHE A  90      17.653  -2.499  27.579  1.00 17.14      A    C  
ANISOU  688  CB  PHE A  90     1718   2399   2396    401   -117   -258  A    C  
ATOM    689  CG  PHE A  90      17.487  -2.571  26.085  1.00 17.56      A    C  
ANISOU  689  CG  PHE A  90     1749   2493   2429    412    -57   -258  A    C  
ATOM    690  CD1 PHE A  90      18.205  -1.733  25.249  1.00 17.25      A    C  
ANISOU  690  CD1 PHE A  90     1637   2512   2405    394     25   -278  A    C  
ATOM    691  CD2 PHE A  90      16.612  -3.499  25.516  1.00 17.62      A    C  
ANISOU  691  CD2 PHE A  90     1816   2479   2401    437    -84   -239  A    C  
ATOM    692  CE1 PHE A  90      18.079  -1.811  23.874  1.00 20.93      A    C  
ANISOU  692  CE1 PHE A  90     2096   3017   2841    402     80   -278  A    C  
ATOM    693  CE2 PHE A  90      16.492  -3.598  24.134  1.00 17.84      A    C  
ANISOU  693  CE2 PHE A  90     1829   2544   2406    454    -35   -244  A    C  
ATOM    694  CZ  PHE A  90      17.180  -2.713  23.316  1.00 17.13      A    C  
ANISOU  694  CZ  PHE A  90     1676   2512   2322    434     50   -259  A    C  
ATOM    695  N   THR A  91      18.647   0.312  28.154  1.00 20.03      A    N  
ANISOU  695  N   THR A  91     1973   2814   2825    304      4   -250  A    N  
ATOM    696  CA  THR A  91      19.396   1.463  27.707  1.00 19.37      A    C  
ANISOU  696  CA  THR A  91     1813   2772   2772    265     81   -263  A    C  
ATOM    697  C   THR A  91      20.862   1.068  27.662  1.00 21.72      A    C  
ANISOU  697  C   THR A  91     2023   3112   3119    303     61   -352  A    C  
ATOM    698  O   THR A  91      21.322   0.311  28.507  1.00 22.29      A    O  
ANISOU  698  O   THR A  91     2097   3162   3213    349    -28   -398  A    O  
ATOM    699  CB  THR A  91      19.216   2.675  28.661  1.00 20.19      A    C  
ANISOU  699  CB  THR A  91     1923   2853   2896    212     95   -232  A    C  
ATOM    700  CG2 THR A  91      19.629   2.342  30.075  1.00 22.20      A    C  
ANISOU  700  CG2 THR A  91     2184   3077   3174    234     11   -263  A    C  
ATOM    701  OG1 THR A  91      19.998   3.789  28.153  1.00 20.23      A    O  
ANISOU  701  OG1 THR A  91     1858   2897   2932    167    171   -245  A    O  
ATOM    702  N   PRO A  92      21.568   1.544  26.644  1.00 20.47      A    N  
ANISOU  702  N   PRO A  92     1793   3012   2973    281    143   -382  A    N  
ATOM    703  CA  PRO A  92      23.031   1.332  26.586  1.00 23.55      A    C  
ANISOU  703  CA  PRO A  92     2075   3452   3420    306    139   -483  A    C  
ATOM    704  C   PRO A  92      23.765   2.150  27.611  1.00 30.42      A    C  
ANISOU  704  C   PRO A  92     2892   4316   4350    277    125   -511  A    C  
ATOM    705  O   PRO A  92      24.968   1.934  27.809  1.00 27.33      A    O  
ANISOU  705  O   PRO A  92     2409   3958   4018    305    100   -605  A    O  
ATOM    706  CB  PRO A  92      23.373   1.767  25.167  1.00 32.55      A    C  
ANISOU  706  CB  PRO A  92     3167   4657   4544    267    253   -493  A    C  
ATOM    707  CG  PRO A  92      22.319   2.733  24.798  1.00 31.46      A    C  
ANISOU  707  CG  PRO A  92     3104   4493   4356    203    317   -393  A    C  
ATOM    708  CD  PRO A  92      21.076   2.218  25.436  1.00 23.69      A    C  
ANISOU  708  CD  PRO A  92     2217   3444   3340    233    241   -333  A    C  
ATOM    709  N   ALA A  93      23.101   3.074  28.289  1.00 23.59      A    N  
ANISOU  709  N   ALA A  93     2079   3410   3475    228    134   -442  A    N  
ATOM    710  CA  ALA A  93      23.810   3.861  29.289  1.00 24.41      A    C  
ANISOU  710  CA  ALA A  93     2132   3505   3635    204    116   -473  A    C  
ATOM    711  C   ALA A  93      24.200   3.038  30.518  1.00 30.95      A    C  
ANISOU  711  C   ALA A  93     2970   4297   4491    269     -9   -523  A    C  
ATOM    712  O   ALA A  93      23.475   2.168  30.976  1.00 26.98      A    O  
ANISOU  712  O   ALA A  93     2555   3748   3946    309    -82   -494  A    O  
ATOM    713  CB  ALA A  93      22.960   5.062  29.709  1.00 26.95      A    C  
ANISOU  713  CB  ALA A  93     2511   3790   3941    139    151   -391  A    C  
ATOM    714  N   ARG A  94      25.367   3.341  31.073  1.00 30.66      A    N  
ANISOU  714  N   ARG A  94     2847   4277   4523    277    -37   -601  A    N  
ATOM    715  CA  ARG A  94      25.833   2.644  32.255  1.00 30.41      A    C  
ANISOU  715  CA  ARG A  94     2830   4206   4519    342   -166   -655  A    C  
ATOM    716  C   ARG A  94      25.519   3.394  33.532  1.00 39.20      A    C  
ANISOU  716  C   ARG A  94     3994   5268   5631    313   -204   -617  A    C  
ATOM    717  O   ARG A  94      25.796   2.922  34.636  1.00 41.13      A    O  
ANISOU  717  O   ARG A  94     4274   5470   5884    359   -315   -650  A    O  
ATOM    718  CB  ARG A  94      27.350   2.433  32.132  1.00 28.17      A    C  
ANISOU  718  CB  ARG A  94     2414   3970   4318    381   -192   -783  A    C  
ATOM    719  CG  ARG A  94      27.738   1.734  30.837  1.00 32.17      A    C  
ANISOU  719  CG  ARG A  94     2858   4538   4827    409   -145   -836  A    C  
ATOM    720  CD  ARG A  94      29.252   1.605  30.697  1.00 41.96      A    C  
ANISOU  720  CD  ARG A  94     3948   5837   6158    442   -160   -978  A    C  
ATOM    721  NE  ARG A  94      29.627   0.381  29.985  1.00 54.85      A    N  
ANISOU  721  NE  ARG A  94     5547   7500   7794    519   -196  -1054  A    N  
ATOM    722  CZ  ARG A  94      29.696  -0.834  30.537  1.00 55.38      A    C  
ANISOU  722  CZ  ARG A  94     5661   7520   7862    618   -339  -1097  A    C  
ATOM    723  NH1 ARG A  94      29.410  -1.022  31.827  1.00 75.85      A    N1+
ANISOU  723  NH1 ARG A  94     8346  10029  10443    646   -458  -1067  A    N1+
ATOM    724  NH2 ARG A  94      30.049  -1.867  29.793  1.00 57.72      A    N  
ANISOU  724  NH2 ARG A  94     5920   7847   8164    685   -365  -1172  A    N  
ATOM    725  N   SER A  95      24.949   4.577  33.390  1.00 36.86      A    N  
ANISOU  725  N   SER A  95     3709   4975   5323    238   -118   -552  A    N  
ATOM    726  CA  SER A  95      24.680   5.401  34.531  1.00 28.59      A    C  
ANISOU  726  CA  SER A  95     2698   3886   4280    208   -143   -522  A    C  
ATOM    727  C   SER A  95      23.677   6.453  34.156  1.00 24.03      A    C  
ANISOU  727  C   SER A  95     2159   3303   3668    137    -53   -437  A    C  
ATOM    728  O   SER A  95      23.457   6.739  32.958  1.00 24.84      A    O  
ANISOU  728  O   SER A  95     2243   3437   3758    104     34   -409  A    O  
ATOM    729  CB  SER A  95      25.967   6.098  35.005  1.00 29.91      A    C  
ANISOU  729  CB  SER A  95     2762   4070   4531    201   -159   -602  A    C  
ATOM    730  OG  SER A  95      26.321   7.156  34.115  1.00 32.51      A    O  
ANISOU  730  OG  SER A  95     3012   4445   4896    129    -46   -600  A    O  
ATOM    731  N   LEU A  96      23.108   7.088  35.184  1.00 27.85      A    N  
ANISOU  731  N   LEU A  96     2699   3745   4138    115    -79   -401  A    N  
ATOM    732  CA  LEU A  96      22.115   8.125  34.986  1.00 26.21      A    C  
ANISOU  732  CA  LEU A  96     2530   3525   3905     57    -11   -330  A    C  
ATOM    733  C   LEU A  96      22.674   9.257  34.165  1.00 28.64      A    C  
ANISOU  733  C   LEU A  96     2765   3861   4258      0     73   -332  A    C  
ATOM    734  O   LEU A  96      21.997   9.836  33.322  1.00 32.87      A    O  
ANISOU  734  O   LEU A  96     3325   4396   4767    -41    143   -277  A    O  
ATOM    735  CB  LEU A  96      21.639   8.635  36.330  1.00 28.64      A    C  
ANISOU  735  CB  LEU A  96     2891   3788   4201     48    -58   -315  A    C  
ATOM    736  CG  LEU A  96      20.627   9.772  36.349  1.00 22.08      A    C  
ANISOU  736  CG  LEU A  96     2097   2939   3352     -3     -7   -258  A    C  
ATOM    737  CD1 LEU A  96      19.350   9.413  35.566  1.00 22.53      A    C  
ANISOU  737  CD1 LEU A  96     2214   2995   3352     -8     34   -200  A    C  
ATOM    738  CD2 LEU A  96      20.298  10.128  37.789  1.00 31.67      A    C  
ANISOU  738  CD2 LEU A  96     3359   4118   4557     -4    -61   -262  A    C  
ATOM    739  N   GLU A  97      23.968   9.537  34.394  1.00 30.49      A    N  
ANISOU  739  N   GLU A  97     2909   4116   4560     -4     63   -403  A    N  
ATOM    740  CA  GLU A  97      24.633  10.654  33.779  1.00 31.96      A    C  
ANISOU  740  CA  GLU A  97     3023   4326   4796    -71    142   -414  A    C  
ATOM    741  C   GLU A  97      24.622  10.529  32.244  1.00 35.69      A    C  
ANISOU  741  C   GLU A  97     3477   4840   5242    -99    234   -393  A    C  
ATOM    742  O   GLU A  97      24.395  11.512  31.540  1.00 48.97      A    O  
ANISOU  742  O   GLU A  97     5172   6520   6916   -167    312   -348  A    O  
ATOM    743  CB  GLU A  97      26.080  10.753  34.322  1.00 33.69      A    C  
ANISOU  743  CB  GLU A  97     3135   4567   5098    -64    106   -511  A    C  
ATOM    744  CG  GLU A  97      26.212  11.095  35.822  1.00 39.17      A    C  
ANISOU  744  CG  GLU A  97     3844   5217   5821    -43     16   -533  A    C  
ATOM    745  CD  GLU A  97      25.287  10.332  36.797  1.00 64.15      A    C  
ANISOU  745  CD  GLU A  97     7117   8337   8921     14    -70   -500  A    C  
ATOM    746  OE1 GLU A  97      24.426  11.001  37.426  1.00 60.02      A    O  
ANISOU  746  OE1 GLU A  97     6662   7776   8368    -10    -73   -449  A    O  
ATOM    747  OE2 GLU A  97      25.439   9.089  36.988  1.00 36.14      A    O1-
ANISOU  747  OE2 GLU A  97     3588   4789   5354     79   -138   -532  A    O1-
ATOM    748  N   GLU A  98      24.790   9.319  31.722  1.00 30.89      A    N  
ANISOU  748  N   GLU A  98     2858   4264   4616    -47    221   -424  A    N  
ATOM    749  CA  GLU A  98      24.855   9.136  30.276  1.00 30.52      A    C  
ANISOU  749  CA  GLU A  98     2794   4262   4541    -69    307   -415  A    C  
ATOM    750  C   GLU A  98      23.560   8.558  29.684  1.00 26.32      A    C  
ANISOU  750  C   GLU A  98     2360   3711   3929    -45    310   -343  A    C  
ATOM    751  O   GLU A  98      23.507   8.163  28.510  1.00 31.74      A    O  
ANISOU  751  O   GLU A  98     3048   4432   4581    -46    363   -337  A    O  
ATOM    752  CB  GLU A  98      26.063   8.276  29.880  1.00 43.83      A    C  
ANISOU  752  CB  GLU A  98     4377   6008   6267    -33    305   -515  A    C  
ATOM    753  CG  GLU A  98      26.175   6.929  30.564  1.00 46.87      A    C  
ANISOU  753  CG  GLU A  98     4769   6382   6656     64    192   -567  A    C  
ATOM    754  CD  GLU A  98      27.390   6.142  30.109  1.00 60.84      A    C  
ANISOU  754  CD  GLU A  98     6429   8212   8475    107    185   -678  A    C  
ATOM    755  OE1 GLU A  98      28.454   6.757  29.873  1.00 64.14      A    O  
ANISOU  755  OE1 GLU A  98     6737   8677   8955     63    240   -745  A    O  
ATOM    756  OE2 GLU A  98      27.295   4.900  29.996  1.00 47.03      A    O1-
ANISOU  756  OE2 GLU A  98     4701   6464   6705    183    123   -706  A    O1-
ATOM    757  N   PHE A  99      22.525   8.558  30.491  1.00 26.51      A    N  
ANISOU  757  N   PHE A  99     2465   3684   3924    -27    255   -294  A    N  
ATOM    758  CA  PHE A  99      21.208   8.016  30.079  1.00 23.57      A    C  
ANISOU  758  CA  PHE A  99     2182   3289   3483     -5    250   -232  A    C  
ATOM    759  C   PHE A  99      20.495   8.961  29.104  1.00 26.11      A    C  
ANISOU  759  C   PHE A  99     2546   3603   3773    -58    325   -167  A    C  
ATOM    760  O   PHE A  99      19.970  10.000  29.491  1.00 30.54      A    O  
ANISOU  760  O   PHE A  99     3139   4127   4337    -96    331   -129  A    O  
ATOM    761  CB  PHE A  99      20.393   7.810  31.339  1.00 26.13      A    C  
ANISOU  761  CB  PHE A  99     2570   3566   3792     19    176   -211  A    C  
ATOM    762  CG  PHE A  99      18.991   7.250  31.134  1.00 21.35      A    C  
ANISOU  762  CG  PHE A  99     2050   2937   3126     37    166   -158  A    C  
ATOM    763  CD1 PHE A  99      18.731   6.170  30.307  1.00 19.63      A    C  
ANISOU  763  CD1 PHE A  99     1850   2734   2874     72    164   -156  A    C  
ATOM    764  CD2 PHE A  99      17.941   7.779  31.879  1.00 20.99      A    C  
ANISOU  764  CD2 PHE A  99     2060   2852   3062     18    151   -119  A    C  
ATOM    765  CE1 PHE A  99      17.460   5.663  30.198  1.00 19.82      A    C  
ANISOU  765  CE1 PHE A  99     1946   2734   2850     84    150   -115  A    C  
ATOM    766  CE2 PHE A  99      16.660   7.263  31.763  1.00 17.96      A    C  
ANISOU  766  CE2 PHE A  99     1743   2451   2631     29    142    -83  A    C  
ATOM    767  CZ  PHE A  99      16.436   6.202  30.949  1.00 18.94      A    C  
ANISOU  767  CZ  PHE A  99     1883   2588   2725     61    141    -81  A    C  
ATOM    768  N   ASN A 100      20.472   8.585  27.832  1.00 27.89      A    N  
ANISOU  768  N   ASN A 100     2775   3858   3963    -58    375   -159  A    N  
ATOM    769  CA  ASN A 100      19.771   9.357  26.832  1.00 25.93      A    C  
ANISOU  769  CA  ASN A 100     2584   3595   3672   -101    433    -97  A    C  
ATOM    770  C   ASN A 100      18.920   8.607  25.833  1.00 23.19      A    C  
ANISOU  770  C   ASN A 100     2296   3252   3264    -68    439    -67  A    C  
ATOM    771  O   ASN A 100      18.283   9.226  24.979  1.00 29.61      A    O  
ANISOU  771  O   ASN A 100     3167   4046   4037    -97    476    -16  A    O  
ATOM    772  CB  ASN A 100      20.718  10.232  26.085  1.00 34.66      A    C  
ANISOU  772  CB  ASN A 100     3648   4728   4793   -170    515   -107  A    C  
ATOM    773  CG  ASN A 100      20.765  11.593  26.689  1.00 73.84      A    C  
ANISOU  773  CG  ASN A 100     8616   9650   9788   -227    521    -83  A    C  
ATOM    774  ND2 ASN A 100      19.668  12.349  26.554  1.00 52.22      A    N  
ANISOU  774  ND2 ASN A 100     5963   6860   7020   -244    515    -18  A    N  
ATOM    775  OD1 ASN A 100      21.704  11.911  27.388  1.00 42.37      A    O  
ANISOU  775  OD1 ASN A 100     4560   5678   5862   -247    517   -129  A    O  
ATOM    776  N   ASP A 101      18.881   7.296  25.927  1.00 27.14      A    N  
ANISOU  776  N   ASP A 101     2788   3769   3755     -7    396    -98  A    N  
ATOM    777  CA  ASP A 101      18.025   6.506  25.048  1.00 26.15      A    C  
ANISOU  777  CA  ASP A 101     2718   3642   3574     28    391    -73  A    C  
ATOM    778  C   ASP A 101      17.344   5.403  25.800  1.00 22.94      A    C  
ANISOU  778  C   ASP A 101     2341   3213   3164     84    312    -79  A    C  
ATOM    779  O   ASP A 101      17.898   4.860  26.770  1.00 22.52      A    O  
ANISOU  779  O   ASP A 101     2256   3159   3142    109    262   -120  A    O  
ATOM    780  CB  ASP A 101      18.866   5.922  23.930  1.00 27.78      A    C  
ANISOU  780  CB  ASP A 101     2885   3906   3765     40    437   -113  A    C  
ATOM    781  CG  ASP A 101      19.186   6.971  22.857  1.00 41.02      A    C  
ANISOU  781  CG  ASP A 101     4570   5600   5417    -27    529    -88  A    C  
ATOM    782  OD1 ASP A 101      18.244   7.506  22.197  1.00 42.19      A    O  
ANISOU  782  OD1 ASP A 101     4798   5715   5516    -46    545    -26  A    O  
ATOM    783  OD2 ASP A 101      20.358   7.312  22.729  1.00 41.12      A    O1-
ANISOU  783  OD2 ASP A 101     4513   5655   5458    -65    581   -130  A    O1-
ATOM    784  N   VAL A 102      16.115   5.095  25.348  1.00 19.42      A    N  
ANISOU  784  N   VAL A 102     1961   2741   2676     99    300    -40  A    N  
ATOM    785  CA  VAL A 102      15.277   4.089  25.917  1.00 17.86      A    C  
ANISOU  785  CA  VAL A 102     1802   2519   2466    137    237    -38  A    C  
ATOM    786  C   VAL A 102      14.680   3.241  24.805  1.00 17.61      A    C  
ANISOU  786  C   VAL A 102     1805   2494   2393    171    236    -31  A    C  
ATOM    787  O   VAL A 102      14.082   3.763  23.861  1.00 18.25      A    O  
ANISOU  787  O   VAL A 102     1919   2571   2446    159    270      2  A    O  
ATOM    788  CB  VAL A 102      14.109   4.753  26.698  1.00 21.87      A    C  
ANISOU  788  CB  VAL A 102     2352   2984   2975    112    221     -2  A    C  
ATOM    789  CG1 VAL A 102      13.150   3.707  27.239  1.00 20.35      A    C  
ANISOU  789  CG1 VAL A 102     2203   2768   2763    136    169     -1  A    C  
ATOM    790  CG2 VAL A 102      14.663   5.622  27.825  1.00 23.96      A    C  
ANISOU  790  CG2 VAL A 102     2586   3239   3276     80    218    -11  A    C  
ATOM    791  N   TYR A 103      14.778   1.918  24.985  1.00 15.69      A    N  
ANISOU  791  N   TYR A 103     1565   2251   2144    216    186    -60  A    N  
ATOM    792  CA  TYR A 103      14.199   0.913  24.097  1.00 15.01      A    C  
ANISOU  792  CA  TYR A 103     1514   2166   2024    256    168    -59  A    C  
ATOM    793  C   TYR A 103      13.217   0.041  24.836  1.00 15.06      A    C  
ANISOU  793  C   TYR A 103     1570   2130   2024    268    105    -50  A    C  
ATOM    794  O   TYR A 103      13.503  -0.418  25.960  1.00 15.84      A    O  
ANISOU  794  O   TYR A 103     1672   2209   2138    270     57    -65  A    O  
ATOM    795  CB  TYR A 103      15.279   0.026  23.524  1.00 17.92      A    C  
ANISOU  795  CB  TYR A 103     1842   2572   2394    299    161   -113  A    C  
ATOM    796  CG  TYR A 103      16.331   0.720  22.700  1.00 16.25      A    C  
ANISOU  796  CG  TYR A 103     1575   2414   2187    281    234   -136  A    C  
ATOM    797  CD1 TYR A 103      17.332   1.464  23.301  1.00 18.31      A    C  
ANISOU  797  CD1 TYR A 103     1775   2694   2489    249    259   -160  A    C  
ATOM    798  CD2 TYR A 103      16.324   0.611  21.317  1.00 20.05      A    C  
ANISOU  798  CD2 TYR A 103     2066   2927   2626    290    280   -137  A    C  
ATOM    799  CE1 TYR A 103      18.334   2.055  22.535  1.00 20.06      A    C  
ANISOU  799  CE1 TYR A 103     1940   2968   2715    222    335   -188  A    C  
ATOM    800  CE2 TYR A 103      17.331   1.172  20.540  1.00 21.77      A    C  
ANISOU  800  CE2 TYR A 103     2235   3199   2838    264    357   -163  A    C  
ATOM    801  CZ  TYR A 103      18.337   1.877  21.158  1.00 18.63      A    C  
ANISOU  801  CZ  TYR A 103     1771   2822   2485    226    386   -190  A    C  
ATOM    802  OH  TYR A 103      19.342   2.503  20.406  1.00 24.50      A    O  
ANISOU  802  OH  TYR A 103     2463   3621   3225    183    474   -218  A    O  
ATOM    803  N   LEU A 104      12.050  -0.190  24.217  1.00 12.49      A    N  
ANISOU  803  N   LEU A 104     1288   1787   1673    273    102    -25  A    N  
ATOM    804  CA  LEU A 104      11.023  -0.983  24.781  1.00 13.51      A    C  
ANISOU  804  CA  LEU A 104     1462   1878   1794    274     55    -17  A    C  
ATOM    805  C   LEU A 104      10.835  -2.216  23.917  1.00 15.13      A    C  
ANISOU  805  C   LEU A 104     1690   2082   1977    319     22    -33  A    C  
ATOM    806  O   LEU A 104      10.764  -2.107  22.688  1.00 18.69      A    O  
ANISOU  806  O   LEU A 104     2138   2553   2409    341     48    -32  A    O  
ATOM    807  CB  LEU A 104       9.700  -0.190  24.715  1.00 13.07      A    C  
ANISOU  807  CB  LEU A 104     1427   1803   1734    242     76     13  A    C  
ATOM    808  CG  LEU A 104       9.706   1.166  25.415  1.00 12.96      A    C  
ANISOU  808  CG  LEU A 104     1395   1787   1743    200    107     26  A    C  
ATOM    809  CD1 LEU A 104       8.480   1.933  24.998  1.00 17.63      A    C  
ANISOU  809  CD1 LEU A 104     2002   2363   2333    187    121     43  A    C  
ATOM    810  CD2 LEU A 104       9.795   1.066  26.922  1.00 14.82      A    C  
ANISOU  810  CD2 LEU A 104     1630   2006   1991    173     85     19  A    C  
ATOM    811  N   VAL A 105      10.746  -3.381  24.544  1.00 11.39      A    N  
ANISOU  811  N   VAL A 105     1246   1581   1502    332    -38    -47  A    N  
ATOM    812  CA  VAL A 105      10.544  -4.595  23.824  1.00 13.97      A    C  
ANISOU  812  CA  VAL A 105     1600   1898   1812    374    -79    -64  A    C  
ATOM    813  C   VAL A 105       9.193  -5.236  24.129  1.00 14.37      A    C  
ANISOU  813  C   VAL A 105     1704   1904   1853    351   -111    -47  A    C  
ATOM    814  O   VAL A 105       8.843  -5.397  25.308  1.00 13.52      A    O  
ANISOU  814  O   VAL A 105     1625   1764   1747    310   -131    -35  A    O  
ATOM    815  CB  VAL A 105      11.651  -5.637  24.145  1.00 14.73      A    C  
ANISOU  815  CB  VAL A 105     1692   1988   1915    419   -138   -106  A    C  
ATOM    816  CG1 VAL A 105      11.488  -6.877  23.260  1.00 14.04      A    C  
ANISOU  816  CG1 VAL A 105     1631   1892   1811    471   -184   -130  A    C  
ATOM    817  CG2 VAL A 105      13.033  -5.038  23.978  1.00 15.50      A    C  
ANISOU  817  CG2 VAL A 105     1723   2134   2033    437   -107   -137  A    C  
ATOM    818  N   THR A 106       8.435  -5.614  23.080  1.00 14.95      A    N  
ANISOU  818  N   THR A 106     1792   1976   1914    373   -114    -48  A    N  
ATOM    819  CA  THR A 106       7.161  -6.260  23.238  1.00 13.67      A    C  
ANISOU  819  CA  THR A 106     1671   1776   1749    350   -142    -41  A    C  
ATOM    820  C   THR A 106       7.102  -7.485  22.332  1.00 16.97      A    C  
ANISOU  820  C   THR A 106     2114   2180   2154    400   -190    -62  A    C  
ATOM    821  O   THR A 106       7.967  -7.678  21.516  1.00 16.92      A    O  
ANISOU  821  O   THR A 106     2090   2201   2139    453   -192    -84  A    O  
ATOM    822  CB  THR A 106       5.984  -5.310  22.868  1.00 15.49      A    C  
ANISOU  822  CB  THR A 106     1887   2009   1986    323   -101    -27  A    C  
ATOM    823  CG2 THR A 106       6.180  -3.992  23.485  1.00 14.96      A    C  
ANISOU  823  CG2 THR A 106     1791   1959   1933    289    -55    -11  A    C  
ATOM    824  OG1 THR A 106       5.884  -5.197  21.430  1.00 15.96      A    O  
ANISOU  824  OG1 THR A 106     1943   2087   2033    370    -95    -33  A    O  
ATOM    825  N   HIS A 107       5.965  -8.174  22.472  1.00 19.00      A    N  
ANISOU  825  N   HIS A 107     1932   2740   2548     98     76    -85  A    N  
ATOM    826  CA  HIS A 107       5.617  -9.206  21.514  1.00 27.37      A    C  
ANISOU  826  CA  HIS A 107     2999   3809   3591    139     96   -113  A    C  
ATOM    827  C   HIS A 107       5.495  -8.559  20.166  1.00 20.35      A    C  
ANISOU  827  C   HIS A 107     2101   2955   2677    137    130   -106  A    C  
ATOM    828  O   HIS A 107       5.040  -7.448  20.056  1.00 20.60      A    O  
ANISOU  828  O   HIS A 107     2142   2984   2700    100    131    -88  A    O  
ATOM    829  CB  HIS A 107       4.296  -9.890  21.887  1.00 22.42      A    C  
ANISOU  829  CB  HIS A 107     2424   3136   2958    147     81   -137  A    C  
ATOM    830  CG  HIS A 107       4.464 -10.957  22.912  1.00 28.77      A    C  
ANISOU  830  CG  HIS A 107     3237   3910   3782    165     54   -150  A    C  
ATOM    831  CD2 HIS A 107       3.901 -11.125  24.132  1.00 34.62      A    C  
ANISOU  831  CD2 HIS A 107     4008   4611   4533    150     26   -148  A    C  
ATOM    832  ND1 HIS A 107       5.317 -12.022  22.728  1.00 37.83      A    N  
ANISOU  832  ND1 HIS A 107     4361   5072   4940    204     54   -165  A    N  
ATOM    833  CE1 HIS A 107       5.274 -12.801  23.793  1.00 48.31      A    C  
ANISOU  833  CE1 HIS A 107     5704   6365   6284    212     23   -171  A    C  
ATOM    834  NE2 HIS A 107       4.420 -12.283  24.657  1.00 29.05      A    N  
ANISOU  834  NE2 HIS A 107     3298   3894   3845    178      8   -160  A    N  
ATOM    835  N   LEU A 108       5.819  -9.329  19.137  1.00 24.50      A    N  
ANISOU  835  N   LEU A 108     2611   3510   3186    178    153   -124  A    N  
ATOM    836  CA  LEU A 108       5.568  -8.895  17.762  1.00 22.85      A    C  
ANISOU  836  CA  LEU A 108     2402   3335   2946    183    186   -122  A    C  
ATOM    837  C   LEU A 108       4.223  -9.521  17.342  1.00 20.21      A    C  
ANISOU  837  C   LEU A 108     2120   2966   2592    200    179   -154  A    C  
ATOM    838  O   LEU A 108       4.084 -10.762  17.391  1.00 23.29      A    O  
ANISOU  838  O   LEU A 108     2526   3339   2985    238    170   -184  A    O  
ATOM    839  CB  LEU A 108       6.647  -9.393  16.845  1.00 18.95      A    C  
ANISOU  839  CB  LEU A 108     1865   2894   2440    224    216   -126  A    C  
ATOM    840  CG  LEU A 108       6.591  -8.988  15.359  1.00 19.42      A    C  
ANISOU  840  CG  LEU A 108     1920   2998   2463    234    254   -121  A    C  
ATOM    841  CD1 LEU A 108       6.808  -7.495  15.202  1.00 24.31      A    C  
ANISOU  841  CD1 LEU A 108     2518   3639   3081    182    265    -77  A    C  
ATOM    842  CD2 LEU A 108       7.622  -9.776  14.533  1.00 24.25      A    C  
ANISOU  842  CD2 LEU A 108     2493   3661   3058    289    286   -133  A    C  
ATOM    843  N   MET A 109       3.208  -8.711  17.049  1.00 17.94      A    N  
ANISOU  843  N   MET A 109     1862   2662   2290    170    180   -146  A    N  
ATOM    844  CA  MET A 109       1.926  -9.201  16.538  1.00 17.37      A    C  
ANISOU  844  CA  MET A 109     1835   2561   2201    183    175   -172  A    C  
ATOM    845  C   MET A 109       1.969  -9.485  15.069  1.00 23.36      A    C  
ANISOU  845  C   MET A 109     2596   3353   2927    214    200   -187  A    C  
ATOM    846  O   MET A 109       2.856  -9.062  14.411  1.00 23.02      A    O  
ANISOU  846  O   MET A 109     2519   3357   2870    219    227   -172  A    O  
ATOM    847  CB  MET A 109       0.807  -8.187  16.824  1.00 26.59      A    C  
ANISOU  847  CB  MET A 109     3033   3701   3369    140    164   -158  A    C  
ATOM    848  CG  MET A 109       0.806  -7.682  18.276  1.00 34.34      A    C  
ANISOU  848  CG  MET A 109     4014   4655   4378    108    141   -141  A    C  
ATOM    849  SD  MET A 109       0.803  -9.025  19.471  1.00 30.45      A    S  
ANISOU  849  SD  MET A 109     3532   4128   3909    130    114   -160  A    S  
ATOM    850  CE  MET A 109      -0.818  -9.771  19.179  1.00 39.17      A    C  
ANISOU  850  CE  MET A 109     4683   5192   5005    140    103   -184  A    C  
ATOM    851  N   GLY A 110       0.933 -10.161  14.556  1.00 22.32      A    N  
ANISOU  851  N   GLY A 110     2505   3194   2781    234    189   -215  A    N  
ATOM    852  CA  GLY A 110       0.928 -10.529  13.127  1.00 24.89      A    C  
ANISOU  852  CA  GLY A 110     2840   3547   3070    271    209   -233  A    C  
ATOM    853  C   GLY A 110       0.165  -9.577  12.217  1.00 25.16      A    C  
ANISOU  853  C   GLY A 110     2894   3588   3078    247    221   -222  A    C  
ATOM    854  O   GLY A 110       0.474  -9.427  11.063  1.00 28.02      A    O  
ANISOU  854  O   GLY A 110     3253   3989   3407    267    246   -223  A    O  
ATOM    855  N   ALA A 111      -0.919  -9.005  12.708  1.00 19.90      A    N  
ANISOU  855  N   ALA A 111     2254   2884   2425    210    201   -214  A    N  
ATOM    856  CA  ALA A 111      -1.699  -8.166  11.864  1.00 19.68      A    C  
ANISOU  856  CA  ALA A 111     2247   2858   2374    191    206   -205  A    C  
ATOM    857  C   ALA A 111      -2.571  -7.361  12.718  1.00 20.38      A    C  
ANISOU  857  C   ALA A 111     2348   2911   2485    147    187   -188  A    C  
ATOM    858  O   ALA A 111      -3.011  -7.844  13.750  1.00 22.17      A    O  
ANISOU  858  O   ALA A 111     2585   3101   2738    143    165   -195  A    O  
ATOM    859  CB  ALA A 111      -2.585  -9.030  10.958  1.00 23.91      A    C  
ANISOU  859  CB  ALA A 111     2822   3375   2889    222    194   -238  A    C  
ATOM    860  N   ASP A 112      -3.002  -6.226  12.231  1.00 16.80      A    N  
ANISOU  860  N   ASP A 112     1903   2464   2018    118    194   -168  A    N  
ATOM    861  CA  ASP A 112      -4.012  -5.451  12.975  1.00 16.27      A    C  
ANISOU  861  CA  ASP A 112     1854   2359   1970     82    173   -156  A    C  
ATOM    862  C   ASP A 112      -5.403  -5.815  12.489  1.00 19.41      A    C  
ANISOU  862  C   ASP A 112     2289   2724   2361     90    157   -175  A    C  
ATOM    863  O   ASP A 112      -5.558  -6.661  11.546  1.00 19.73      A    O  
ANISOU  863  O   ASP A 112     2345   2770   2382    121    157   -197  A    O  
ATOM    864  CB  ASP A 112      -3.725  -3.956  12.917  1.00 15.40      A    C  
ANISOU  864  CB  ASP A 112     1730   2265   1855     45    182   -123  A    C  
ATOM    865  CG  ASP A 112      -4.043  -3.298  11.591  1.00 19.14      A    C  
ANISOU  865  CG  ASP A 112     2217   2758   2299     40    193   -115  A    C  
ATOM    866  OD1 ASP A 112      -4.756  -3.847  10.765  1.00 19.32      A    O  
ANISOU  866  OD1 ASP A 112     2264   2774   2302     60    191   -135  A    O  
ATOM    867  OD2 ASP A 112      -3.513  -2.187  11.356  1.00 22.42      A    O1-
ANISOU  867  OD2 ASP A 112     2616   3197   2707     13    204    -85  A    O1-
ATOM    868  N   LEU A 113      -6.430  -5.258  13.101  1.00 16.19      A    N  
ANISOU  868  N   LEU A 113     1898   2285   1971     64    139   -167  A    N  
ATOM    869  CA  LEU A 113      -7.771  -5.755  12.813  1.00 15.89      A    C  
ANISOU  869  CA  LEU A 113     1890   2213   1936     70    120   -183  A    C  
ATOM    870  C   LEU A 113      -8.240  -5.319  11.439  1.00 23.55      A    C  
ANISOU  870  C   LEU A 113     2877   3193   2877     72    123   -185  A    C  
ATOM    871  O   LEU A 113      -8.958  -6.075  10.789  1.00 26.28      A    O  
ANISOU  871  O   LEU A 113     3246   3522   3216     91    109   -206  A    O  
ATOM    872  CB  LEU A 113      -8.788  -5.355  13.880  1.00 18.92      A    C  
ANISOU  872  CB  LEU A 113     2282   2561   2346     47    102   -174  A    C  
ATOM    873  CG  LEU A 113      -9.240  -6.458  14.823  1.00 34.60      A    C  
ANISOU  873  CG  LEU A 113     4272   4518   4358     58     86   -186  A    C  
ATOM    874  CD1 LEU A 113     -10.214  -5.891  15.854  1.00 24.32      A    C  
ANISOU  874  CD1 LEU A 113     2976   3189   3076     36     77   -172  A    C  
ATOM    875  CD2 LEU A 113      -9.898  -7.580  14.033  1.00 35.98      A    C  
ANISOU  875  CD2 LEU A 113     4466   4676   4530     81     71   -208  A    C  
ATOM    876  N   ASN A 114      -7.768  -4.192  10.921  1.00 18.26      A    N  
ANISOU  876  N   ASN A 114     2198   2551   2188     54    139   -164  A    N  
ATOM    877  CA  ASN A 114      -8.074  -3.900   9.507  1.00 21.42      A    C  
ANISOU  877  CA  ASN A 114     2618   2966   2555     60    145   -165  A    C  
ATOM    878  C   ASN A 114      -7.615  -5.006   8.557  1.00 24.09      A    C  
ANISOU  878  C   ASN A 114     2962   3324   2866    101    153   -190  A    C  
ATOM    879  O   ASN A 114      -8.266  -5.238   7.526  1.00 23.33      A    O  
ANISOU  879  O   ASN A 114     2894   3222   2746    115    144   -205  A    O  
ATOM    880  CB  ASN A 114      -7.440  -2.604   9.069  1.00 23.04      A    C  
ANISOU  880  CB  ASN A 114     2810   3203   2743     34    163   -135  A    C  
ATOM    881  CG  ASN A 114      -8.019  -1.415   9.758  1.00 23.33      A    C  
ANISOU  881  CG  ASN A 114     2849   3215   2800     -2    149   -113  A    C  
ATOM    882  ND2 ASN A 114      -7.165  -0.523  10.192  1.00 25.78      A    N  
ANISOU  882  ND2 ASN A 114     3137   3543   3116    -26    158    -87  A    N  
ATOM    883  OD1 ASN A 114      -9.266  -1.295   9.909  1.00 24.08      A    O  
ANISOU  883  OD1 ASN A 114     2968   3275   2908     -8    127   -120  A    O  
ATOM    884  N   ASN A 115      -6.461  -5.619   8.850  1.00 22.04      A    N  
ANISOU  884  N   ASN A 115     2677   3090   2607    121    171   -196  A    N  
ATOM    885  CA  ASN A 115      -5.866  -6.662   8.007  1.00 23.64      A    C  
ANISOU  885  CA  ASN A 115     2884   3316   2782    167    182   -220  A    C  
ATOM    886  C   ASN A 115      -6.555  -8.035   8.142  1.00 32.24      A    C  
ANISOU  886  C   ASN A 115     4000   4367   3885    197    152   -255  A    C  
ATOM    887  O   ASN A 115      -6.395  -8.897   7.279  1.00 40.60      A    O  
ANISOU  887  O   ASN A 115     5077   5433   4917    236    151   -282  A    O  
ATOM    888  CB  ASN A 115      -4.334  -6.669   8.244  1.00 28.21      A    C  
ANISOU  888  CB  ASN A 115     3420   3941   3357    177    212   -208  A    C  
ATOM    889  CG  ASN A 115      -3.678  -5.423   7.639  1.00 49.24      A    C  
ANISOU  889  CG  ASN A 115     6062   6649   5997    154    240   -173  A    C  
ATOM    890  ND2 ASN A 115      -3.579  -5.409   6.320  1.00 55.24      A    N  
ANISOU  890  ND2 ASN A 115     6835   7440   6714    175    259   -177  A    N  
ATOM    891  OD1 ASN A 115      -3.376  -4.444   8.334  1.00 52.22      A    O  
ANISOU  891  OD1 ASN A 115     6417   7029   6395    116    243   -143  A    O  
ATOM    892  N   GLN A 120     -14.415  -7.155   4.348  1.00 22.98      A    N  
ANISOU  892  N   GLN A 120     3021   3006   2702    143    -24   -282  A    N  
ATOM    893  CA  GLN A 120     -15.260  -8.335   4.215  1.00 24.65      A    C  
ANISOU  893  CA  GLN A 120     3256   3176   2932    159    -67   -306  A    C  
ATOM    894  C   GLN A 120     -15.827  -8.657   5.574  1.00 22.37      A    C  
ANISOU  894  C   GLN A 120     2943   2856   2699    138    -78   -294  A    C  
ATOM    895  O   GLN A 120     -15.213  -8.360   6.598  1.00 28.86      A    O  
ANISOU  895  O   GLN A 120     3735   3694   3536    127    -52   -280  A    O  
ATOM    896  CB  GLN A 120     -14.453  -9.533   3.661  1.00 24.46      A    C  
ANISOU  896  CB  GLN A 120     3251   3162   2882    204    -68   -338  A    C  
ATOM    897  CG  GLN A 120     -13.867  -9.342   2.256  1.00 24.87      A    C  
ANISOU  897  CG  GLN A 120     3329   3249   2872    232    -53   -351  A    C  
ATOM    898  CD  GLN A 120     -14.890  -9.469   1.158  1.00 27.96      A    C  
ANISOU  898  CD  GLN A 120     3764   3612   3246    239    -93   -365  A    C  
ATOM    899  NE2 GLN A 120     -14.612  -8.848   0.022  1.00 43.19      A    N  
ANISOU  899  NE2 GLN A 120     5714   5574   5123    249    -77   -363  A    N  
ATOM    900  OE1 GLN A 120     -15.893 -10.132   1.306  1.00 38.17      A    O  
ANISOU  900  OE1 GLN A 120     5073   4858   4571    235   -139   -375  A    O  
ATOM    901  N   LYS A 121     -17.033  -9.195   5.602  1.00 19.25      A    N  
ANISOU  901  N   LYS A 121     2561   2418   2334    132   -119   -297  A    N  
ATOM    902  CA  LYS A 121     -17.680  -9.591   6.828  1.00 18.16      A    C  
ANISOU  902  CA  LYS A 121     2402   2251   2248    113   -133   -284  A    C  
ATOM    903  C   LYS A 121     -16.963 -10.767   7.480  1.00 20.62      A    C  
ANISOU  903  C   LYS A 121     2707   2557   2570    132   -134   -298  A    C  
ATOM    904  O   LYS A 121     -16.524 -11.722   6.807  1.00 19.51      A    O  
ANISOU  904  O   LYS A 121     2590   2412   2410    163   -150   -325  A    O  
ATOM    905  CB  LYS A 121     -19.147 -10.051   6.520  1.00 21.32      A    C  
ANISOU  905  CB  LYS A 121     2816   2606   2678    103   -182   -283  A    C  
ATOM    906  CG  LYS A 121     -20.041  -9.014   5.864  1.00 25.69      A    C  
ANISOU  906  CG  LYS A 121     3378   3157   3227     87   -191   -270  A    C  
ATOM    907  CD  LYS A 121     -21.443  -9.537   5.732  1.00 30.18      A    C  
ANISOU  907  CD  LYS A 121     3951   3682   3833     75   -240   -265  A    C  
ATOM    908  CE  LYS A 121     -22.297  -8.563   4.958  1.00 37.13      A    C  
ANISOU  908  CE  LYS A 121     4842   4558   4708     62   -254   -255  A    C  
ATOM    909  NZ  LYS A 121     -23.742  -8.750   5.241  1.00 60.06      A    N1+
ANISOU  909  NZ  LYS A 121     7733   7425   7662     42   -292   -238  A    N1+
ATOM    910  N   LEU A 122     -16.862 -10.718   8.794  1.00 17.13      A    N  
ANISOU  910  N   LEU A 122     2236   2114   2158    115   -119   -279  A    N  
ATOM    911  CA  LEU A 122     -16.435 -11.905   9.577  1.00 15.93      A    C  
ANISOU  911  CA  LEU A 122     2078   1949   2028    128   -129   -288  A    C  
ATOM    912  C   LEU A 122     -17.620 -12.751   9.959  1.00 16.57      A    C  
ANISOU  912  C   LEU A 122     2162   1984   2151    115   -170   -280  A    C  
ATOM    913  O   LEU A 122     -18.746 -12.288  10.004  1.00 17.97      A    O  
ANISOU  913  O   LEU A 122     2333   2145   2349     93   -183   -262  A    O  
ATOM    914  CB  LEU A 122     -15.686 -11.456  10.796  1.00 15.43      A    C  
ANISOU  914  CB  LEU A 122     1984   1908   1972    117    -94   -271  A    C  
ATOM    915  CG  LEU A 122     -14.422 -10.602  10.512  1.00 15.89      A    C  
ANISOU  915  CG  LEU A 122     2031   2012   1994    125    -54   -272  A    C  
ATOM    916  CD1 LEU A 122     -13.598 -10.443  11.804  1.00 17.38      A    C  
ANISOU  916  CD1 LEU A 122     2193   2215   2196    117    -29   -259  A    C  
ATOM    917  CD2 LEU A 122     -13.510 -11.122   9.408  1.00 16.33      A    C  
ANISOU  917  CD2 LEU A 122     2106   2088   2012    160    -49   -299  A    C  
ATOM    918  N   THR A 123     -17.386 -14.022  10.228  1.00 14.05      A    N  
ANISOU  918  N   THR A 123     1850   1641   1847    131   -194   -293  A    N  
ATOM    919  CA  THR A 123     -18.431 -14.861  10.779  1.00 15.52      A    C  
ANISOU  919  CA  THR A 123     2034   1784   2079    114   -234   -280  A    C  
ATOM    920  C   THR A 123     -18.817 -14.370  12.163  1.00 14.93      A    C  
ANISOU  920  C   THR A 123     1924   1715   2034     84   -211   -244  A    C  
ATOM    921  O   THR A 123     -18.029 -13.784  12.927  1.00 13.49      A    O  
ANISOU  921  O   THR A 123     1723   1562   1841     82   -172   -236  A    O  
ATOM    922  CB  THR A 123     -18.045 -16.340  10.879  1.00 15.01      A    C  
ANISOU  922  CB  THR A 123     1986   1691   2026    135   -267   -299  A    C  
ATOM    923  CG2 THR A 123     -17.571 -16.881   9.538  1.00 16.28      A    C  
ANISOU  923  CG2 THR A 123     2186   1848   2153    173   -289   -338  A    C  
ATOM    924  OG1 THR A 123     -17.045 -16.489  11.882  1.00 14.98      A    O  
ANISOU  924  OG1 THR A 123     1962   1705   2022    141   -239   -295  A    O  
ATOM    925  N   ASP A 124     -20.072 -14.626  12.518  1.00 14.23      A    N  
ANISOU  925  N   ASP A 124     1825   1596   1984     61   -236   -221  A    N  
ATOM    926  CA  ASP A 124     -20.538 -14.282  13.854  1.00 15.77      A    C  
ANISOU  926  CA  ASP A 124     1988   1796   2207     36   -216   -186  A    C  
ATOM    927  C   ASP A 124     -19.678 -14.923  14.944  1.00 15.12      A    C  
ANISOU  927  C   ASP A 124     1897   1718   2130     41   -203   -183  A    C  
ATOM    928  O   ASP A 124     -19.377 -14.269  15.960  1.00 13.66      A    O  
ANISOU  928  O   ASP A 124     1692   1557   1942     33   -168   -167  A    O  
ATOM    929  CB  ASP A 124     -22.030 -14.672  14.049  1.00 15.69      A    C  
ANISOU  929  CB  ASP A 124     1966   1755   2242     12   -249   -158  A    C  
ATOM    930  CG  ASP A 124     -22.612 -14.073  15.310  1.00 14.82      A    C  
ANISOU  930  CG  ASP A 124     1820   1658   2152    -10   -219   -121  A    C  
ATOM    931  OD1 ASP A 124     -22.633 -12.850  15.397  1.00 16.06      A    O  
ANISOU  931  OD1 ASP A 124     1968   1843   2292    -13   -186   -117  A    O  
ATOM    932  OD2 ASP A 124     -23.027 -14.897  16.192  1.00 17.34      A    O1-
ANISOU  932  OD2 ASP A 124     2125   1960   2505    -24   -231    -97  A    O1-
ATOM    933  N   ASP A 125     -19.274 -16.191  14.800  1.00 15.67      A    N  
ANISOU  933  N   ASP A 125     1984   1763   2207     56   -235   -199  A    N  
ATOM    934  CA  ASP A 125     -18.440 -16.817  15.863  1.00 15.43      A    C  
ANISOU  934  CA  ASP A 125     1945   1734   2183     62   -225   -196  A    C  
ATOM    935  C   ASP A 125     -17.085 -16.088  15.993  1.00 13.78      A    C  
ANISOU  935  C   ASP A 125     1731   1566   1937     80   -182   -211  A    C  
ATOM    936  O   ASP A 125     -16.572 -15.941  17.068  1.00 15.72      A    O  
ANISOU  936  O   ASP A 125     1961   1825   2185     74   -160   -197  A    O  
ATOM    937  CB  ASP A 125     -18.204 -18.312  15.568  1.00 17.13      A    C  
ANISOU  937  CB  ASP A 125     2184   1913   2412     79   -272   -214  A    C  
ATOM    938  CG  ASP A 125     -19.431 -19.189  15.873  1.00 34.40      A    C  
ANISOU  938  CG  ASP A 125     4369   4056   4646     54   -317   -188  A    C  
ATOM    939  OD1 ASP A 125     -20.288 -18.782  16.691  1.00 37.57      A    O  
ANISOU  939  OD1 ASP A 125     4744   4461   5071     25   -304   -150  A    O  
ATOM    940  OD2 ASP A 125     -19.508 -20.314  15.286  1.00 39.02      A    O1-
ANISOU  940  OD2 ASP A 125     4981   4603   5243     67   -367   -205  A    O1-
ATOM    941  N   HIS A 126     -16.510 -15.676  14.861  1.00 12.84      A    N  
ANISOU  941  N   HIS A 126     1627   1466   1784    100   -174   -238  A    N  
ATOM    942  CA  HIS A 126     -15.211 -14.982  14.868  1.00 14.82      A    C  
ANISOU  942  CA  HIS A 126     1871   1758   2004    115   -135   -249  A    C  
ATOM    943  C   HIS A 126     -15.391 -13.616  15.551  1.00 12.47      A    C  
ANISOU  943  C   HIS A 126     1551   1484   1702     90   -101   -224  A    C  
ATOM    944  O   HIS A 126     -14.583 -13.200  16.380  1.00 14.79      A    O  
ANISOU  944  O   HIS A 126     1829   1800   1991     87    -75   -217  A    O  
ATOM    945  CB  HIS A 126     -14.766 -14.776  13.408  1.00 14.64      A    C  
ANISOU  945  CB  HIS A 126     1867   1752   1944    139   -134   -278  A    C  
ATOM    946  CG  HIS A 126     -13.324 -14.426  13.213  1.00 16.39      A    C  
ANISOU  946  CG  HIS A 126     2080   2013   2133    161   -100   -292  A    C  
ATOM    947  CD2 HIS A 126     -12.266 -14.420  14.047  1.00 22.07      A    C  
ANISOU  947  CD2 HIS A 126     2779   2752   2852    166    -78   -288  A    C  
ATOM    948  ND1 HIS A 126     -12.843 -14.022  11.990  1.00 17.90      A    N  
ANISOU  948  ND1 HIS A 126     2284   2231   2286    181    -88   -311  A    N  
ATOM    949  CE1 HIS A 126     -11.545 -13.799  12.080  1.00 16.67      A    C  
ANISOU  949  CE1 HIS A 126     2112   2111   2111    197    -58   -315  A    C  
ATOM    950  NE2 HIS A 126     -11.178 -14.007  13.322  1.00 19.48      A    N  
ANISOU  950  NE2 HIS A 126     2449   2463   2490    188    -53   -302  A    N  
ATOM    951  N   VAL A 127     -16.503 -12.918  15.236  1.00 11.70      A    N  
ANISOU  951  N   VAL A 127     1453   1381   1610     71   -103   -211  A    N  
ATOM    952  CA  VAL A 127     -16.791 -11.634  15.897  1.00 11.93      A    C  
ANISOU  952  CA  VAL A 127     1465   1430   1639     51    -74   -188  A    C  
ATOM    953  C   VAL A 127     -16.956 -11.798  17.393  1.00 12.20      A    C  
ANISOU  953  C   VAL A 127     1481   1459   1695     38    -66   -166  A    C  
ATOM    954  O   VAL A 127     -16.406 -11.000  18.171  1.00 12.15      A    O  
ANISOU  954  O   VAL A 127     1464   1473   1677     33    -39   -157  A    O  
ATOM    955  CB  VAL A 127     -18.029 -10.962  15.295  1.00 12.47      A    C  
ANISOU  955  CB  VAL A 127     1536   1490   1714     37    -83   -179  A    C  
ATOM    956  CG1 VAL A 127     -18.408  -9.663  16.008  1.00 13.62      A    C  
ANISOU  956  CG1 VAL A 127     1666   1651   1859     20    -56   -158  A    C  
ATOM    957  CG2 VAL A 127     -17.760 -10.669  13.826  1.00 18.56      A    C  
ANISOU  957  CG2 VAL A 127     2326   2269   2455     50    -88   -201  A    C  
ATOM    958  N   GLN A 128     -17.682 -12.825  17.823  1.00 12.55      A    N  
ANISOU  958  N   GLN A 128     1524   1475   1768     32    -90   -154  A    N  
ATOM    959  CA  GLN A 128     -17.802 -13.091  19.254  1.00 12.16      A    C  
ANISOU  959  CA  GLN A 128     1461   1423   1738     21    -83   -130  A    C  
ATOM    960  C   GLN A 128     -16.435 -13.167  19.915  1.00 12.87      A    C  
ANISOU  960  C   GLN A 128     1549   1528   1811     33    -66   -138  A    C  
ATOM    961  O   GLN A 128     -16.181 -12.556  20.954  1.00 12.74      A    O  
ANISOU  961  O   GLN A 128     1523   1528   1790     26    -43   -124  A    O  
ATOM    962  CB  GLN A 128     -18.581 -14.391  19.525  1.00 14.61      A    C  
ANISOU  962  CB  GLN A 128     1770   1699   2082     14   -116   -115  A    C  
ATOM    963  CG  GLN A 128     -20.044 -14.324  19.213  1.00 14.49      A    C  
ANISOU  963  CG  GLN A 128     1747   1668   2092     -4   -132    -95  A    C  
ATOM    964  CD  GLN A 128     -20.683 -15.670  19.382  1.00 19.49      A    C  
ANISOU  964  CD  GLN A 128     2379   2265   2761    -14   -170    -80  A    C  
ATOM    965  NE2 GLN A 128     -21.776 -15.917  18.654  1.00 23.58      A    N  
ANISOU  965  NE2 GLN A 128     2897   2760   3303    -25   -200    -73  A    N  
ATOM    966  OE1 GLN A 128     -20.202 -16.489  20.150  1.00 21.64      A    O  
ANISOU  966  OE1 GLN A 128     2652   2529   3042    -12   -177    -73  A    O  
ATOM    967  N   PHE A 129     -15.530 -13.926  19.301  1.00 12.21      A    N  
ANISOU  967  N   PHE A 129     1478   1442   1721     53    -80   -163  A    N  
ATOM    968  CA  PHE A 129     -14.231 -14.168  19.890  1.00 12.82      A    C  
ANISOU  968  CA  PHE A 129     1551   1533   1788     66    -69   -171  A    C  
ATOM    969  C   PHE A 129     -13.363 -12.906  19.937  1.00 11.30      A    C  
ANISOU  969  C   PHE A 129     1349   1375   1568     66    -37   -174  A    C  
ATOM    970  O   PHE A 129     -12.719 -12.623  20.945  1.00 12.50      A    O  
ANISOU  970  O   PHE A 129     1492   1538   1718     63    -23   -165  A    O  
ATOM    971  CB  PHE A 129     -13.503 -15.279  19.124  1.00 13.20      A    C  
ANISOU  971  CB  PHE A 129     1612   1569   1832     92    -92   -199  A    C  
ATOM    972  CG  PHE A 129     -12.243 -15.768  19.816  1.00 17.17      A    C  
ANISOU  972  CG  PHE A 129     2109   2081   2334    108    -88   -205  A    C  
ATOM    973  CD1 PHE A 129     -12.241 -15.995  21.163  1.00 22.89      A    C  
ANISOU  973  CD1 PHE A 129     2826   2798   3074     96    -88   -184  A    C  
ATOM    974  CD2 PHE A 129     -11.084 -15.973  19.098  1.00 23.20      A    C  
ANISOU  974  CD2 PHE A 129     2874   2862   3078    137    -85   -232  A    C  
ATOM    975  CE1 PHE A 129     -11.097 -16.436  21.813  1.00 25.98      A    C  
ANISOU  975  CE1 PHE A 129     3212   3193   3464    109    -88   -190  A    C  
ATOM    976  CE2 PHE A 129      -9.908 -16.436  19.737  1.00 22.67      A    C  
ANISOU  976  CE2 PHE A 129     2798   2804   3013    153    -82   -239  A    C  
ATOM    977  CZ  PHE A 129      -9.927 -16.629  21.102  1.00 22.99      A    C  
ANISOU  977  CZ  PHE A 129     2832   2832   3071    137    -86   -216  A    C  
ATOM    978  N   LEU A 130     -13.373 -12.139  18.842  1.00 11.86      A    N  
ANISOU  978  N   LEU A 130     1423   1462   1619     68    -28   -185  A    N  
ATOM    979  CA  LEU A 130     -12.604 -10.913  18.798  1.00 12.15      A    C  
ANISOU  979  CA  LEU A 130     1451   1530   1634     64     -1   -184  A    C  
ATOM    980  C   LEU A 130     -13.095  -9.883  19.784  1.00 10.35      A    C  
ANISOU  980  C   LEU A 130     1218   1305   1410     44     14   -161  A    C  
ATOM    981  O   LEU A 130     -12.322  -9.289  20.551  1.00 12.42      A    O  
ANISOU  981  O   LEU A 130     1472   1581   1665     39     28   -154  A    O  
ATOM    982  CB  LEU A 130     -12.595 -10.366  17.371  1.00 12.22      A    C  
ANISOU  982  CB  LEU A 130     1469   1554   1622     70      4   -197  A    C  
ATOM    983  CG  LEU A 130     -11.755 -11.168  16.381  1.00 15.46      A    C  
ANISOU  983  CG  LEU A 130     1886   1973   2016     98     -1   -222  A    C  
ATOM    984  CD1 LEU A 130     -12.122 -10.696  14.977  1.00 16.37      A    C  
ANISOU  984  CD1 LEU A 130     2014   2096   2109    101      0   -231  A    C  
ATOM    985  CD2 LEU A 130     -10.279 -10.994  16.618  1.00 17.10      A    C  
ANISOU  985  CD2 LEU A 130     2076   2210   2211    109     19   -225  A    C  
ATOM    986  N   ILE A 131     -14.419  -9.638  19.774  1.00 11.13      A    N  
ANISOU  986  N   ILE A 131     1320   1389   1520     32      9   -149  A    N  
ATOM    987  CA  ILE A 131     -14.960  -8.621  20.680  1.00 10.06      A    C  
ANISOU  987  CA  ILE A 131     1179   1257   1385     17     23   -130  A    C  
ATOM    988  C   ILE A 131     -14.824  -9.076  22.125  1.00 10.71      A    C  
ANISOU  988  C   ILE A 131     1257   1334   1477     17     25   -117  A    C  
ATOM    989  O   ILE A 131     -14.556  -8.263  23.010  1.00 11.66      A    O  
ANISOU  989  O   ILE A 131     1378   1465   1588     12     39   -107  A    O  
ATOM    990  CB  ILE A 131     -16.428  -8.244  20.312  1.00 10.12      A    C  
ANISOU  990  CB  ILE A 131     1187   1253   1403      8     19   -120  A    C  
ATOM    991  CG1 ILE A 131     -16.513  -7.720  18.864  1.00 12.62      A    C  
ANISOU  991  CG1 ILE A 131     1513   1576   1707     10     14   -133  A    C  
ATOM    992  CG2 ILE A 131     -16.968  -7.213  21.250  1.00 10.06      A    C  
ANISOU  992  CG2 ILE A 131     1176   1251   1395      1     34   -103  A    C  
ATOM    993  CD1 ILE A 131     -15.591  -6.543  18.543  1.00 11.94      A    C  
ANISOU  993  CD1 ILE A 131     1429   1512   1595      8     30   -138  A    C  
ATOM    994  N   TYR A 132     -15.032 -10.356  22.397  1.00 10.68      A    N  
ANISOU  994  N   TYR A 132     1254   1313   1492     20      9   -114  A    N  
ATOM    995  CA  TYR A 132     -14.866 -10.904  23.737  1.00 10.11      A    C  
ANISOU  995  CA  TYR A 132     1178   1235   1428     19     10    -99  A    C  
ATOM    996  C   TYR A 132     -13.474 -10.495  24.273  1.00 10.57      A    C  
ANISOU  996  C   TYR A 132     1237   1311   1470     24     20   -106  A    C  
ATOM    997  O   TYR A 132     -13.344 -10.004  25.393  1.00 11.14      A    O  
ANISOU  997  O   TYR A 132     1310   1388   1534     20     30    -94  A    O  
ATOM    998  CB  TYR A 132     -15.045 -12.423  23.764  1.00 11.02      A    C  
ANISOU  998  CB  TYR A 132     1295   1326   1565     22    -15    -96  A    C  
ATOM    999  CG  TYR A 132     -14.685 -13.027  25.097  1.00 11.65      A    C  
ANISOU  999  CG  TYR A 132     1374   1401   1651     20    -16    -81  A    C  
ATOM   1000  CD1 TYR A 132     -15.546 -12.851  26.164  1.00 12.56      A    C  
ANISOU 1000  CD1 TYR A 132     1485   1517   1771      9     -5    -52  A    C  
ATOM   1001  CD2 TYR A 132     -13.491 -13.676  25.326  1.00 12.64      A    C  
ANISOU 1001  CD2 TYR A 132     1504   1526   1775     32    -26    -93  A    C  
ATOM   1002  CE1 TYR A 132     -15.229 -13.358  27.433  1.00 13.34      A    C  
ANISOU 1002  CE1 TYR A 132     1586   1611   1870      9     -6    -36  A    C  
ATOM   1003  CE2 TYR A 132     -13.169 -14.132  26.605  1.00 13.80      A    C  
ANISOU 1003  CE2 TYR A 132     1651   1668   1924     30    -28    -77  A    C  
ATOM   1004  CZ  TYR A 132     -14.056 -13.957  27.642  1.00 13.04      A    C  
ANISOU 1004  CZ  TYR A 132     1555   1570   1830     18    -18    -48  A    C  
ATOM   1005  OH  TYR A 132     -13.696 -14.374  28.907  1.00 15.96      A    O  
ANISOU 1005  OH  TYR A 132     1929   1937   2198     17    -20    -32  A    O  
ATOM   1006  N   GLN A 133     -12.439 -10.735  23.455  1.00  9.59      A    N  
ANISOU 1006  N   GLN A 133     1112   1195   1339     36     15   -127  A    N  
ATOM   1007  CA  GLN A 133     -11.095 -10.440  23.896  1.00 11.05      A    C  
ANISOU 1007  CA  GLN A 133     1291   1395   1511     41     21   -131  A    C  
ATOM   1008  C   GLN A 133     -10.845  -8.931  24.097  1.00 10.24      A    C  
ANISOU 1008  C   GLN A 133     1187   1311   1391     29     38   -126  A    C  
ATOM   1009  O   GLN A 133     -10.146  -8.528  25.000  1.00 10.70      A    O  
ANISOU 1009  O   GLN A 133     1245   1375   1445     26     39   -120  A    O  
ATOM   1010  CB  GLN A 133     -10.070 -10.986  22.903  1.00 11.89      A    C  
ANISOU 1010  CB  GLN A 133     1392   1512   1615     57     16   -152  A    C  
ATOM   1011  CG  GLN A 133     -10.011 -12.517  22.899  1.00 11.75      A    C  
ANISOU 1011  CG  GLN A 133     1378   1474   1614     73     -6   -161  A    C  
ATOM   1012  CD  GLN A 133      -9.050 -12.990  21.864  1.00 12.65      A    C  
ANISOU 1012  CD  GLN A 133     1487   1600   1718     97     -8   -185  A    C  
ATOM   1013  NE2 GLN A 133      -9.532 -13.224  20.674  1.00 15.36      A    N  
ANISOU 1013  NE2 GLN A 133     1839   1940   2057    106    -14   -200  A    N  
ATOM   1014  OE1 GLN A 133      -7.855 -13.083  22.121  1.00 13.62      A    O  
ANISOU 1014  OE1 GLN A 133     1598   1738   1839    108     -4   -191  A    O  
ATOM   1015  N   ILE A 134     -11.389  -8.102  23.228  1.00 10.27      A    N  
ANISOU 1015  N   ILE A 134     1194   1321   1388     23     44   -128  A    N  
ATOM   1016  CA  ILE A 134     -11.268  -6.646  23.427  1.00 10.26      A    C  
ANISOU 1016  CA  ILE A 134     1194   1330   1373     11     55   -121  A    C  
ATOM   1017  C   ILE A 134     -11.894  -6.248  24.758  1.00  9.21      A    C  
ANISOU 1017  C   ILE A 134     1071   1188   1241      6     58   -107  A    C  
ATOM   1018  O   ILE A 134     -11.323  -5.528  25.543  1.00 10.81      A    O  
ANISOU 1018  O   ILE A 134     1278   1394   1434      3     58   -103  A    O  
ATOM   1019  CB  ILE A 134     -11.954  -5.852  22.291  1.00 11.79      A    C  
ANISOU 1019  CB  ILE A 134     1393   1529   1560      5     59   -123  A    C  
ATOM   1020  CG1 ILE A 134     -11.257  -6.167  20.952  1.00 12.50      A    C  
ANISOU 1020  CG1 ILE A 134     1475   1632   1641     12     59   -136  A    C  
ATOM   1021  CG2 ILE A 134     -11.916  -4.379  22.587  1.00 14.31      A    C  
ANISOU 1021  CG2 ILE A 134     1717   1851   1867     -7     65   -115  A    C  
ATOM   1022  CD1 ILE A 134     -12.049  -5.672  19.763  1.00 14.26      A    C  
ANISOU 1022  CD1 ILE A 134     1706   1855   1857      8     60   -140  A    C  
ATOM   1023  N   LEU A 135     -13.090  -6.754  25.001  1.00  9.88      A    N  
ANISOU 1023  N   LEU A 135     1158   1259   1336      8     58    -98  A    N  
ATOM   1024  CA  LEU A 135     -13.772  -6.439  26.252  1.00 10.48      A    C  
ANISOU 1024  CA  LEU A 135     1242   1332   1410      8     65    -83  A    C  
ATOM   1025  C   LEU A 135     -13.053  -6.971  27.495  1.00  9.85      A    C  
ANISOU 1025  C   LEU A 135     1166   1250   1327     11     61    -77  A    C  
ATOM   1026  O   LEU A 135     -13.042  -6.311  28.558  1.00 10.94      A    O  
ANISOU 1026  O   LEU A 135     1316   1390   1451     14     66    -70  A    O  
ATOM   1027  CB  LEU A 135     -15.219  -6.934  26.201  1.00 10.80      A    C  
ANISOU 1027  CB  LEU A 135     1278   1363   1466      8     68    -70  A    C  
ATOM   1028  CG  LEU A 135     -16.108  -6.203  25.238  1.00 10.96      A    C  
ANISOU 1028  CG  LEU A 135     1296   1382   1487      4     70    -72  A    C  
ATOM   1029  CD1 LEU A 135     -17.398  -7.051  25.126  1.00 13.22      A    C  
ANISOU 1029  CD1 LEU A 135     1570   1657   1795      3     67    -59  A    C  
ATOM   1030  CD2 LEU A 135     -16.403  -4.776  25.674  1.00 12.35      A    C  
ANISOU 1030  CD2 LEU A 135     1480   1565   1647      7     81    -70  A    C  
ATOM   1031  N   ARG A 136     -12.490  -8.157  27.386  1.00 10.36      A    N  
ANISOU 1031  N   ARG A 136     1224   1309   1404     15     50    -80  A    N  
ATOM   1032  CA  ARG A 136     -11.681  -8.713  28.457  1.00 12.20      A    C  
ANISOU 1032  CA  ARG A 136     1461   1539   1635     19     43    -76  A    C  
ATOM   1033  C   ARG A 136     -10.458  -7.823  28.820  1.00  9.93      A    C  
ANISOU 1033  C   ARG A 136     1177   1262   1332     18     40    -83  A    C  
ATOM   1034  O   ARG A 136     -10.242  -7.483  29.972  1.00 11.25      A    O  
ANISOU 1034  O   ARG A 136     1357   1429   1490     18     37    -75  A    O  
ATOM   1035  CB  ARG A 136     -11.279 -10.137  28.090  1.00 13.01      A    C  
ANISOU 1035  CB  ARG A 136     1555   1632   1755     25     27    -82  A    C  
ATOM   1036  CG  ARG A 136     -10.644 -10.916  29.210  1.00 13.11      A    C  
ANISOU 1036  CG  ARG A 136     1573   1637   1770     30     15    -74  A    C  
ATOM   1037  CD  ARG A 136     -10.448 -12.378  28.799  1.00 13.74      A    C  
ANISOU 1037  CD  ARG A 136     1648   1702   1871     38     -4    -79  A    C  
ATOM   1038  NE  ARG A 136      -9.716 -13.120  29.787  1.00 15.49      A    N  
ANISOU 1038  NE  ARG A 136     1874   1915   2097     43    -18    -73  A    N  
ATOM   1039  CZ  ARG A 136      -8.443 -13.478  29.708  1.00 23.90      A    C  
ANISOU 1039  CZ  ARG A 136     2933   2983   3165     54    -31    -87  A    C  
ATOM   1040  NH1 ARG A 136      -7.724 -13.192  28.633  1.00 23.74      A    N1+
ANISOU 1040  NH1 ARG A 136     2900   2977   3144     62    -27   -108  A    N1+
ATOM   1041  NH2 ARG A 136      -7.863 -14.148  30.718  1.00 25.17      A    N  
ANISOU 1041  NH2 ARG A 136     3099   3133   3330     57    -47    -79  A    N  
ATOM   1042  N   GLY A 137      -9.752  -7.376  27.765  1.00 10.08      A    N  
ANISOU 1042  N   GLY A 137     1185   1293   1351     15     39    -96  A    N  
ATOM   1043  CA  GLY A 137      -8.664  -6.410  27.933  1.00 10.31      A    C  
ANISOU 1043  CA  GLY A 137     1214   1333   1371      9     35    -97  A    C  
ATOM   1044  C   GLY A 137      -9.167  -5.103  28.517  1.00 10.10      A    C  
ANISOU 1044  C   GLY A 137     1205   1303   1330      2     38    -90  A    C  
ATOM   1045  O   GLY A 137      -8.540  -4.505  29.404  1.00 10.55      A    O  
ANISOU 1045  O   GLY A 137     1272   1359   1377     -1     28    -88  A    O  
ATOM   1046  N   LEU A 138     -10.320  -4.625  28.068  1.00 10.53      A    N  
ANISOU 1046  N   LEU A 138     1264   1355   1380      2     49    -89  A    N  
ATOM   1047  CA  LEU A 138     -10.817  -3.339  28.535  1.00 10.29      A    C  
ANISOU 1047  CA  LEU A 138     1252   1321   1335     -1     50    -86  A    C  
ATOM   1048  C   LEU A 138     -11.302  -3.391  29.969  1.00 10.34      A    C  
ANISOU 1048  C   LEU A 138     1277   1320   1331      9     53    -78  A    C  
ATOM   1049  O   LEU A 138     -11.108  -2.458  30.737  1.00 11.01      A    O  
ANISOU 1049  O   LEU A 138     1383   1402   1401     12     45    -79  A    O  
ATOM   1050  CB  LEU A 138     -11.954  -2.838  27.648  1.00 12.51      A    C  
ANISOU 1050  CB  LEU A 138     1533   1602   1618     -1     60    -87  A    C  
ATOM   1051  CG  LEU A 138     -11.597  -2.141  26.330  1.00 17.33      A    C  
ANISOU 1051  CG  LEU A 138     2135   2219   2228    -13     58    -93  A    C  
ATOM   1052  CD1 LEU A 138     -12.916  -1.684  25.684  1.00 16.43      A    C  
ANISOU 1052  CD1 LEU A 138     2026   2102   2116    -12     65    -93  A    C  
ATOM   1053  CD2 LEU A 138     -10.694  -0.959  26.609  1.00 16.40      A    C  
ANISOU 1053  CD2 LEU A 138     2028   2103   2102    -23     46    -92  A    C  
ATOM   1054  N   LYS A 139     -11.872  -4.529  30.384  1.00 10.28      A    N  
ANISOU 1054  N   LYS A 139     1264   1309   1330     16     59    -70  A    N  
ATOM   1055  CA  LYS A 139     -12.227  -4.707  31.807  1.00 10.61      A    C  
ANISOU 1055  CA  LYS A 139     1324   1348   1359     27     64    -58  A    C  
ATOM   1056  C   LYS A 139     -10.984  -4.509  32.663  1.00 10.44      A    C  
ANISOU 1056  C   LYS A 139     1316   1324   1326     26     46    -62  A    C  
ATOM   1057  O   LYS A 139     -11.026  -3.821  33.687  1.00 11.00      A    O  
ANISOU 1057  O   LYS A 139     1412   1393   1376     35     42    -60  A    O  
ATOM   1058  CB  LYS A 139     -12.833  -6.075  32.091  1.00 11.78      A    C  
ANISOU 1058  CB  LYS A 139     1462   1495   1520     29     69    -44  A    C  
ATOM   1059  CG  LYS A 139     -13.172  -6.299  33.542  1.00 11.12      A    C  
ANISOU 1059  CG  LYS A 139     1396   1411   1420     39     76    -28  A    C  
ATOM   1060  CD  LYS A 139     -13.562  -7.708  33.866  1.00 12.73      A    C  
ANISOU 1060  CD  LYS A 139     1589   1611   1638     37     77    -10  A    C  
ATOM   1061  CE  LYS A 139     -13.791  -7.903  35.340  1.00 13.70      A    C  
ANISOU 1061  CE  LYS A 139     1730   1736   1739     47     85      9  A    C  
ATOM   1062  NZ  LYS A 139     -14.098  -9.313  35.660  1.00 14.27      A    N1+
ANISOU 1062  NZ  LYS A 139     1792   1803   1828     41     82     31  A    N1+
ATOM   1063  N   TYR A 140      -9.875  -5.112  32.225  1.00 10.07      A    N  
ANISOU 1063  N   TYR A 140     1254   1279   1294     20     32    -67  A    N  
ATOM   1064  CA  TYR A 140      -8.641  -4.973  32.938  1.00 11.31      A    C  
ANISOU 1064  CA  TYR A 140     1418   1432   1445     17     12    -69  A    C  
ATOM   1065  C   TYR A 140      -8.097  -3.522  32.954  1.00 10.13      A    C  
ANISOU 1065  C   TYR A 140     1282   1283   1286      9     -1    -75  A    C  
ATOM   1066  O   TYR A 140      -7.804  -2.950  34.001  1.00 10.96      A    O  
ANISOU 1066  O   TYR A 140     1411   1379   1374     13    -16    -73  A    O  
ATOM   1067  CB  TYR A 140      -7.612  -5.927  32.338  1.00 10.53      A    C  
ANISOU 1067  CB  TYR A 140     1295   1339   1368     14      3    -73  A    C  
ATOM   1068  CG  TYR A 140      -6.202  -5.816  32.915  1.00 10.11      A    C  
ANISOU 1068  CG  TYR A 140     1241   1285   1317     11    -21    -74  A    C  
ATOM   1069  CD1 TYR A 140      -5.278  -4.951  32.376  1.00 10.48      A    C  
ANISOU 1069  CD1 TYR A 140     1276   1339   1368     -1    -31    -78  A    C  
ATOM   1070  CD2 TYR A 140      -5.820  -6.609  33.982  1.00 11.62      A    C  
ANISOU 1070  CD2 TYR A 140     1440   1467   1506     18    -34    -68  A    C  
ATOM   1071  CE1 TYR A 140      -4.014  -4.812  32.911  1.00 11.96      A    C  
ANISOU 1071  CE1 TYR A 140     1458   1525   1559     -6    -55    -76  A    C  
ATOM   1072  CE2 TYR A 140      -4.566  -6.528  34.522  1.00 11.56      A    C  
ANISOU 1072  CE2 TYR A 140     1433   1458   1503     15    -59    -68  A    C  
ATOM   1073  CZ  TYR A 140      -3.643  -5.640  33.967  1.00 14.06      A    C  
ANISOU 1073  CZ  TYR A 140     1734   1782   1827      3    -70    -71  A    C  
ATOM   1074  OH  TYR A 140      -2.378  -5.542  34.527  1.00 14.62      A    O  
ANISOU 1074  OH  TYR A 140     1799   1851   1905     -2    -98    -69  A    O  
ATOM   1075  N   ILE A 141      -8.033  -2.891  31.790  1.00 11.06      A    N  
ANISOU 1075  N   ILE A 141     1385   1406   1410     -1      2    -80  A    N  
ATOM   1076  CA  ILE A 141      -7.559  -1.512  31.677  1.00 11.23      A    C  
ANISOU 1076  CA  ILE A 141     1416   1424   1425    -13    -13    -82  A    C  
ATOM   1077  C   ILE A 141      -8.425  -0.587  32.563  1.00 10.52      A    C  
ANISOU 1077  C   ILE A 141     1362   1323   1313     -2    -15    -83  A    C  
ATOM   1078  O   ILE A 141      -7.923   0.235  33.352  1.00 12.54      A    O  
ANISOU 1078  O   ILE A 141     1642   1566   1556     -2    -37    -85  A    O  
ATOM   1079  CB  ILE A 141      -7.535  -1.055  30.197  1.00 12.96      A    C  
ANISOU 1079  CB  ILE A 141     1615   1655   1655    -25     -5    -84  A    C  
ATOM   1080  CG1 ILE A 141      -6.441  -1.830  29.455  1.00 16.66      A    C  
ANISOU 1080  CG1 ILE A 141     2051   2138   2141    -32     -5    -83  A    C  
ATOM   1081  CG2 ILE A 141      -7.222   0.437  30.118  1.00 17.70      A    C  
ANISOU 1081  CG2 ILE A 141     2229   2247   2249    -39    -23    -82  A    C  
ATOM   1082  CD1 ILE A 141      -6.655  -1.814  27.948  1.00 16.37      A    C  
ANISOU 1082  CD1 ILE A 141     1994   2116   2110    -37     10    -85  A    C  
ATOM   1083  N   HIS A 142      -9.734  -0.695  32.412  1.00 10.17      A    N  
ANISOU 1083  N   HIS A 142     1322   1281   1264     11      8    -84  A    N  
ATOM   1084  CA  HIS A 142     -10.635   0.185  33.129  1.00 10.42      A    C  
ANISOU 1084  CA  HIS A 142     1383   1304   1273     26     12    -85  A    C  
ATOM   1085  C   HIS A 142     -10.544  -0.036  34.613  1.00 11.44      A    C  
ANISOU 1085  C   HIS A 142     1538   1427   1380     43      7    -83  A    C  
ATOM   1086  O   HIS A 142     -10.716   0.914  35.424  1.00 12.80      A    O  
ANISOU 1086  O   HIS A 142     1745   1590   1529     57     -4    -89  A    O  
ATOM   1087  CB  HIS A 142     -12.070  -0.015  32.653  1.00 11.92      A    C  
ANISOU 1087  CB  HIS A 142     1564   1500   1467     37     38    -83  A    C  
ATOM   1088  CG  HIS A 142     -12.306   0.538  31.281  1.00 10.50      A    C  
ANISOU 1088  CG  HIS A 142     1369   1322   1299     25     40    -87  A    C  
ATOM   1089  CD2 HIS A 142     -11.485   1.247  30.469  1.00 11.98      A    C  
ANISOU 1089  CD2 HIS A 142     1552   1508   1494      7     23    -91  A    C  
ATOM   1090  ND1 HIS A 142     -13.452   0.292  30.553  1.00 12.16      A    N  
ANISOU 1090  ND1 HIS A 142     1564   1538   1519     29     59    -84  A    N  
ATOM   1091  CE1 HIS A 142     -13.356   0.903  29.377  1.00 13.64      A    C  
ANISOU 1091  CE1 HIS A 142     1744   1724   1715     15     53    -88  A    C  
ATOM   1092  NE2 HIS A 142     -12.172   1.498  29.313  1.00 12.47      A    N  
ANISOU 1092  NE2 HIS A 142     1601   1572   1563      2     32    -92  A    N  
ATOM   1093  N   SER A 143     -10.273  -1.259  35.021  1.00 11.04      A    N  
ANISOU 1093  N   SER A 143     1476   1381   1336     43     10    -75  A    N  
ATOM   1094  CA  SER A 143     -10.127  -1.569  36.474  1.00 11.20      A    C  
ANISOU 1094  CA  SER A 143     1523   1398   1334     58      4    -70  A    C  
ATOM   1095  C   SER A 143      -8.941  -0.860  37.118  1.00 13.07      A    C  
ANISOU 1095  C   SER A 143     1784   1622   1560     54    -31    -77  A    C  
ATOM   1096  O   SER A 143      -8.952  -0.711  38.356  1.00 16.76      A    O  
ANISOU 1096  O   SER A 143     2286   2083   2000     69    -40    -77  A    O  
ATOM   1097  CB  SER A 143     -10.090  -3.061  36.720  1.00 12.02      A    C  
ANISOU 1097  CB  SER A 143     1610   1507   1449     57     14    -57  A    C  
ATOM   1098  OG  SER A 143      -8.839  -3.620  36.388  1.00 13.58      A    O  
ANISOU 1098  OG  SER A 143     1790   1703   1667     43     -7    -59  A    O  
ATOM   1099  N   ALA A 144      -7.956  -0.473  36.298  1.00 14.08      A    N  
ANISOU 1099  N   ALA A 144     1894   1747   1710     31    -51    -82  A    N  
ATOM   1100  CA  ALA A 144      -6.807   0.352  36.748  1.00 16.46      A    C  
ANISOU 1100  CA  ALA A 144     2213   2034   2008     21    -90    -86  A    C  
ATOM   1101  C   ALA A 144      -7.123   1.847  36.687  1.00 16.89      A    C  
ANISOU 1101  C   ALA A 144     2295   2074   2048     23   -104    -95  A    C  
ATOM   1102  O   ALA A 144      -6.194   2.648  36.880  1.00 19.01      A    O  
ANISOU 1102  O   ALA A 144     2576   2327   2319     10   -141    -96  A    O  
ATOM   1103  CB  ALA A 144      -5.588   0.070  35.878  1.00 18.18      A    C  
ANISOU 1103  CB  ALA A 144     2392   2257   2257     -4   -104    -81  A    C  
ATOM   1104  N   ASP A 145      -8.374   2.246  36.354  1.00 13.87      A    N  
ANISOU 1104  N   ASP A 145     1919   1695   1656     37    -80    -99  A    N  
ATOM   1105  CA  ASP A 145      -8.747   3.616  36.160  1.00 16.60      A    C  
ANISOU 1105  CA  ASP A 145     2289   2028   1992     40    -93   -108  A    C  
ATOM   1106  C   ASP A 145      -7.945   4.228  35.042  1.00 16.13      A    C  
ANISOU 1106  C   ASP A 145     2208   1964   1958      8   -112   -105  A    C  
ATOM   1107  O   ASP A 145      -7.551   5.408  35.093  1.00 20.21      A    O  
ANISOU 1107  O   ASP A 145     2747   2460   2471      0   -146   -108  A    O  
ATOM   1108  CB  ASP A 145      -8.600   4.390  37.497  1.00 20.32      A    C  
ANISOU 1108  CB  ASP A 145     2811   2477   2431     59   -122   -118  A    C  
ATOM   1109  CG  ASP A 145      -9.521   5.546  37.616  1.00 29.41      A    C  
ANISOU 1109  CG  ASP A 145     3998   3616   3561     81   -123   -131  A    C  
ATOM   1110  OD1 ASP A 145     -10.630   5.507  37.076  1.00 32.11      A    O  
ANISOU 1110  OD1 ASP A 145     4326   3970   3903     93    -91   -131  A    O  
ATOM   1111  OD2 ASP A 145      -9.142   6.502  38.326  1.00 35.81      A    O1-
ANISOU 1111  OD2 ASP A 145     4851   4403   4353     89   -161   -142  A    O1-
ATOM   1112  N   ILE A 146      -7.721   3.462  33.985  1.00 14.19      A    N  
ANISOU 1112  N   ILE A 146     1918   1737   1735     -8    -93    -96  A    N  
ATOM   1113  CA  ILE A 146      -7.103   3.897  32.756  1.00 16.41      A    C  
ANISOU 1113  CA  ILE A 146     2173   2022   2039    -35   -100    -89  A    C  
ATOM   1114  C   ILE A 146      -8.190   3.868  31.666  1.00 20.01      A    C  
ANISOU 1114  C   ILE A 146     2615   2490   2499    -32    -71    -90  A    C  
ATOM   1115  O   ILE A 146      -9.021   2.920  31.618  1.00 19.79      A    O  
ANISOU 1115  O   ILE A 146     2575   2473   2470    -16    -41    -92  A    O  
ATOM   1116  CB  ILE A 146      -5.908   3.025  32.353  1.00 15.20      A    C  
ANISOU 1116  CB  ILE A 146     1981   1885   1907    -53   -103    -80  A    C  
ATOM   1117  CG1 ILE A 146      -4.754   3.088  33.406  1.00 19.30      A    C  
ANISOU 1117  CG1 ILE A 146     2513   2393   2429    -59   -137    -77  A    C  
ATOM   1118  CG2 ILE A 146      -5.397   3.456  30.971  1.00 20.02      A    C  
ANISOU 1118  CG2 ILE A 146     2561   2507   2537    -78   -102    -71  A    C  
ATOM   1119  CD1 ILE A 146      -3.716   2.017  33.284  1.00 17.90      A    C  
ANISOU 1119  CD1 ILE A 146     2299   2231   2270    -66   -137    -69  A    C  
ATOM   1120  N   ILE A 147      -8.247   4.925  30.867  1.00 15.20      A    N  
ANISOU 1120  N   ILE A 147     2008   1874   1894    -45    -82    -89  A    N  
ATOM   1121  CA  ILE A 147      -9.137   4.950  29.705  1.00 15.56      A    C  
ANISOU 1121  CA  ILE A 147     2039   1928   1944    -46    -59    -89  A    C  
ATOM   1122  C   ILE A 147      -8.240   4.992  28.474  1.00 14.30      A    C  
ANISOU 1122  C   ILE A 147     1849   1784   1803    -74    -62    -78  A    C  
ATOM   1123  O   ILE A 147      -7.284   5.787  28.405  1.00 15.20      A    O  
ANISOU 1123  O   ILE A 147     1963   1890   1922    -96    -89    -68  A    O  
ATOM   1124  CB  ILE A 147     -10.062   6.155  29.739  1.00 15.87      A    C  
ANISOU 1124  CB  ILE A 147     2108   1948   1972    -36    -68    -96  A    C  
ATOM   1125  CG1 ILE A 147     -10.901   6.180  31.056  1.00 20.08      A    C  
ANISOU 1125  CG1 ILE A 147     2673   2472   2483     -3    -63   -107  A    C  
ATOM   1126  CG2 ILE A 147     -10.999   6.146  28.511  1.00 17.62      A    C  
ANISOU 1126  CG2 ILE A 147     2314   2180   2201    -37    -47    -95  A    C  
ATOM   1127  CD1 ILE A 147     -11.761   7.409  31.216  1.00 23.30      A    C  
ANISOU 1127  CD1 ILE A 147     3115   2862   2878     14    -75   -117  A    C  
ATOM   1128  N   HIS A 148      -8.533   4.156  27.478  1.00 11.71      A    N  
ANISOU 1128  N   HIS A 148     1494   1475   1483    -74    -35    -77  A    N  
ATOM   1129  CA  HIS A 148      -7.687   4.157  26.293  1.00 11.37      A    C  
ANISOU 1129  CA  HIS A 148     1420   1450   1450    -97    -34    -65  A    C  
ATOM   1130  C   HIS A 148      -7.869   5.447  25.510  1.00 11.12      A    C  
ANISOU 1130  C   HIS A 148     1399   1410   1416   -114    -46    -58  A    C  
ATOM   1131  O   HIS A 148      -6.856   6.159  25.176  1.00 12.92      A    O  
ANISOU 1131  O   HIS A 148     1618   1641   1651   -140    -64    -43  A    O  
ATOM   1132  CB  HIS A 148      -8.009   2.937  25.441  1.00 12.43      A    C  
ANISOU 1132  CB  HIS A 148     1531   1604   1588    -87     -4    -71  A    C  
ATOM   1133  CG  HIS A 148      -7.099   2.738  24.277  1.00 13.91      A    C  
ANISOU 1133  CG  HIS A 148     1687   1816   1781   -101      3    -62  A    C  
ATOM   1134  CD2 HIS A 148      -6.194   1.749  24.014  1.00 14.48      A    C  
ANISOU 1134  CD2 HIS A 148     1732   1909   1860    -98     13    -62  A    C  
ATOM   1135  ND1 HIS A 148      -7.048   3.584  23.205  1.00 14.33      A    N  
ANISOU 1135  ND1 HIS A 148     1737   1875   1831   -118      2    -52  A    N  
ATOM   1136  CE1 HIS A 148      -6.131   3.152  22.342  1.00 16.13      A    C  
ANISOU 1136  CE1 HIS A 148     1936   2131   2061   -125     14    -43  A    C  
ATOM   1137  NE2 HIS A 148      -5.594   2.050  22.828  1.00 14.14      A    N  
ANISOU 1137  NE2 HIS A 148     1668   1887   1816   -112     20    -51  A    N  
ATOM   1138  N   ARG A 149      -9.134   5.771  25.181  1.00 12.01      A    N  
ANISOU 1138  N   ARG A 149     1528   1514   1522   -101    -38    -65  A    N  
ATOM   1139  CA AARG A 149      -9.539   7.016  24.479  0.70 12.38      A    C  
ANISOU 1139  CA AARG A 149     1590   1549   1566   -114    -52    -59  A    C  
ATOM   1140  CA BARG A 149      -9.532   7.017  24.494  0.30 12.95      A    C  
ANISOU 1140  CA BARG A 149     1663   1621   1639   -114    -52    -59  A    C  
ATOM   1141  C   ARG A 149      -9.319   7.036  22.985  1.00 13.04      A    C  
ANISOU 1141  C   ARG A 149     1652   1651   1652   -132    -42    -48  A    C  
ATOM   1142  O   ARG A 149      -9.863   7.905  22.304  1.00 14.16      A    O  
ANISOU 1142  O   ARG A 149     1806   1783   1791   -140    -50    -43  A    O  
ATOM   1143  CB AARG A 149      -8.965   8.320  25.121  0.70 13.94      A    C  
ANISOU 1143  CB AARG A 149     1812   1721   1762   -129    -90    -53  A    C  
ATOM   1144  CB BARG A 149      -8.887   8.269  25.126  0.30 15.29      A    C  
ANISOU 1144  CB BARG A 149     1981   1894   1933   -130    -89    -52  A    C  
ATOM   1145  CG AARG A 149      -9.236   8.506  26.590  0.70 21.79      A    C  
ANISOU 1145  CG AARG A 149     2839   2695   2748   -107   -105    -67  A    C  
ATOM   1146  CG BARG A 149      -8.924   8.314  26.637  0.30 19.09      A    C  
ANISOU 1146  CG BARG A 149     2490   2356   2408   -110   -104    -65  A    C  
ATOM   1147  CD AARG A 149      -8.657   9.860  27.109  0.70 22.03      A    C  
ANISOU 1147  CD AARG A 149     2898   2695   2776   -122   -150    -61  A    C  
ATOM   1148  CD BARG A 149      -8.140   9.515  27.170  0.30 22.19      A    C  
ANISOU 1148  CD BARG A 149     2906   2723   2801   -129   -149    -57  A    C  
ATOM   1149  NE AARG A 149      -8.816  10.002  28.573  0.70 27.93      A    N  
ANISOU 1149  NE AARG A 149     3680   3421   3511    -97   -166    -78  A    N  
ATOM   1150  NE BARG A 149      -8.309   9.678  28.617  0.30 23.43      A    N  
ANISOU 1150  NE BARG A 149     3098   2859   2945   -105   -166    -73  A    N  
ATOM   1151  CZ AARG A 149      -8.054   9.398  29.500  0.70 26.80      A    C  
ANISOU 1151  CZ AARG A 149     3535   3280   3366    -95   -172    -78  A    C  
ATOM   1152  CZ BARG A 149      -9.260  10.419  29.180  0.30 16.41      A    C  
ANISOU 1152  CZ BARG A 149     2248   1947   2041    -80   -176    -88  A    C  
ATOM   1153  NH1AARG A 149      -7.007   8.611  29.169  0.70 24.49      A    N1+
ANISOU 1153  NH1AARG A 149     3206   3011   3089   -116   -164    -65  A    N1+
ATOM   1154  NH1BARG A 149     -10.128  11.070  28.422  0.30 19.16      A    N1+
ANISOU 1154  NH1BARG A 149     2604   2288   2389    -77   -174    -89  A    N1+
ATOM   1155  NH2AARG A 149      -8.335   9.583  30.787  0.70 35.16      A    N  
ANISOU 1155  NH2AARG A 149     4631   4322   4407    -69   -186    -93  A    N  
ATOM   1156  NH2BARG A 149      -9.358  10.499  30.502  0.30 15.51      A    N  
ANISOU 1156  NH2BARG A 149     2166   1816   1909    -56   -190   -102  A    N  
ATOM   1157  N   ASP A 150      -8.595   6.068  22.425  1.00 12.14      A    N  
ANISOU 1157  N   ASP A 150     1507   1564   1541   -137    -23    -44  A    N  
ATOM   1158  CA  ASP A 150      -8.378   6.038  20.964  1.00 11.95      A    C  
ANISOU 1158  CA  ASP A 150     1464   1562   1514   -150    -10    -33  A    C  
ATOM   1159  C   ASP A 150      -8.432   4.625  20.432  1.00 12.73      A    C  
ANISOU 1159  C   ASP A 150     1542   1683   1612   -132     17    -44  A    C  
ATOM   1160  O   ASP A 150      -7.606   4.199  19.592  1.00 13.66      A    O  
ANISOU 1160  O   ASP A 150     1635   1829   1728   -138     30    -37  A    O  
ATOM   1161  CB  ASP A 150      -7.095   6.765  20.579  1.00 13.33      A    C  
ANISOU 1161  CB  ASP A 150     1624   1749   1692   -179    -23     -8  A    C  
ATOM   1162  CG  ASP A 150      -7.050   7.179  19.118  1.00 17.00      A    C  
ANISOU 1162  CG  ASP A 150     2078   2232   2148   -196    -14      7  A    C  
ATOM   1163  OD1 ASP A 150      -8.122   7.286  18.472  1.00 16.62      A    O  
ANISOU 1163  OD1 ASP A 150     2046   2177   2092   -188     -9     -1  A    O  
ATOM   1164  OD2 ASP A 150      -5.953   7.421  18.590  1.00 18.15      A    O1-
ANISOU 1164  OD2 ASP A 150     2200   2401   2295   -218    -13     29  A    O1-
ATOM   1165  N   LEU A 151      -9.426   3.856  20.914  1.00 11.03      A    N  
ANISOU 1165  N   LEU A 151     1336   1458   1399   -109     25    -61  A    N  
ATOM   1166  CA  LEU A 151      -9.605   2.517  20.377  1.00 13.20      A    C  
ANISOU 1166  CA  LEU A 151     1595   1746   1675    -93     44    -72  A    C  
ATOM   1167  C   LEU A 151     -10.097   2.551  18.925  1.00 12.24      A    C  
ANISOU 1167  C   LEU A 151     1473   1634   1544    -94     52    -72  A    C  
ATOM   1168  O   LEU A 151     -10.934   3.358  18.568  1.00 13.14      A    O  
ANISOU 1168  O   LEU A 151     1603   1735   1655   -100     45    -69  A    O  
ATOM   1169  CB  LEU A 151     -10.554   1.713  21.252  1.00 13.32      A    C  
ANISOU 1169  CB  LEU A 151     1618   1745   1697    -72     48    -84  A    C  
ATOM   1170  CG  LEU A 151     -10.079   1.130  22.569  1.00 21.36      A    C  
ANISOU 1170  CG  LEU A 151     2635   2759   2722    -64     45    -86  A    C  
ATOM   1171  CD1 LEU A 151     -11.271   0.397  23.213  1.00 24.21      A    C  
ANISOU 1171  CD1 LEU A 151     3005   3107   3088    -47     52    -93  A    C  
ATOM   1172  CD2 LEU A 151      -8.940   0.102  22.319  1.00 18.79      A    C  
ANISOU 1172  CD2 LEU A 151     2286   2454   2400    -62     52    -88  A    C  
ATOM   1173  N   LYS A 152      -9.525   1.694  18.088  1.00 11.28      A    N  
ANISOU 1173  N   LYS A 152     1333   1535   1416    -88     66    -76  A    N  
ATOM   1174  CA  LYS A 152      -9.824   1.605  16.689  1.00 10.84      A    C  
ANISOU 1174  CA  LYS A 152     1279   1492   1347    -87     74    -77  A    C  
ATOM   1175  C   LYS A 152      -9.126   0.357  16.144  1.00 12.20      A    C  
ANISOU 1175  C   LYS A 152     1434   1687   1514    -68     89    -87  A    C  
ATOM   1176  O   LYS A 152      -8.192  -0.187  16.787  1.00 12.02      A    O  
ANISOU 1176  O   LYS A 152     1395   1676   1499    -63     93    -88  A    O  
ATOM   1177  CB  LYS A 152      -9.386   2.847  15.925  1.00 12.23      A    C  
ANISOU 1177  CB  LYS A 152     1456   1680   1510   -110     70    -57  A    C  
ATOM   1178  CG  LYS A 152      -7.922   3.236  16.221  1.00 13.30      A    C  
ANISOU 1178  CG  LYS A 152     1570   1835   1647   -126     73    -38  A    C  
ATOM   1179  CD  LYS A 152      -7.563   4.530  15.520  1.00 14.15      A    C  
ANISOU 1179  CD  LYS A 152     1680   1951   1746   -154     66    -13  A    C  
ATOM   1180  CE  LYS A 152      -6.204   4.973  15.928  1.00 15.95      A    C  
ANISOU 1180  CE  LYS A 152     1885   2196   1981   -174     63      9  A    C  
ATOM   1181  NZ  LYS A 152      -5.752   6.241  15.271  1.00 18.02      A    N1+
ANISOU 1181  NZ  LYS A 152     2145   2465   2238   -207     53     39  A    N1+
ATOM   1182  N   PRO A 153      -9.530  -0.117  14.980  1.00 12.36      A    N  
ANISOU 1182  N   PRO A 153     1461   1716   1520    -57     94    -96  A    N  
ATOM   1183  CA  PRO A 153      -8.897  -1.349  14.457  1.00 12.31      A    C  
ANISOU 1183  CA  PRO A 153     1441   1729   1505    -33    106   -111  A    C  
ATOM   1184  C   PRO A 153      -7.391  -1.364  14.340  1.00 11.81      A    C  
ANISOU 1184  C   PRO A 153     1353   1701   1435    -33    122   -101  A    C  
ATOM   1185  O   PRO A 153      -6.793  -2.369  14.612  1.00 13.64      A    O  
ANISOU 1185  O   PRO A 153     1571   1940   1671    -14    128   -114  A    O  
ATOM   1186  CB  PRO A 153      -9.607  -1.556  13.129  1.00 12.05      A    C  
ANISOU 1186  CB  PRO A 153     1426   1698   1454    -23    107   -121  A    C  
ATOM   1187  CG  PRO A 153     -10.968  -0.873  13.323  1.00 13.32      A    C  
ANISOU 1187  CG  PRO A 153     1607   1827   1626    -36     90   -118  A    C  
ATOM   1188  CD  PRO A 153     -10.701   0.301  14.194  1.00 13.25      A    C  
ANISOU 1188  CD  PRO A 153     1594   1814   1626    -59     87    -99  A    C  
ATOM   1189  N   SER A 154      -6.773  -0.247  14.025  1.00 11.75      A    N  
ANISOU 1189  N   SER A 154     1335   1712   1418    -56    127    -78  A    N  
ATOM   1190  CA  SER A 154      -5.300  -0.203  13.895  1.00 12.53      A    C  
ANISOU 1190  CA  SER A 154     1401   1846   1511    -59    144    -63  A    C  
ATOM   1191  C   SER A 154      -4.600  -0.328  15.235  1.00 12.61      A    C  
ANISOU 1191  C   SER A 154     1394   1851   1547    -64    135    -59  A    C  
ATOM   1192  O   SER A 154      -3.385  -0.584  15.237  1.00 14.17      A    O  
ANISOU 1192  O   SER A 154     1561   2076   1746    -60    146    -50  A    O  
ATOM   1193  CB  SER A 154      -4.838   1.097  13.211  1.00 14.67      A    C  
ANISOU 1193  CB  SER A 154     1664   2139   1769    -88    148    -32  A    C  
ATOM   1194  OG  SER A 154      -5.214   2.262  13.922  1.00 15.78      A    O  
ANISOU 1194  OG  SER A 154     1817   2251   1926   -118    126    -16  A    O  
ATOM   1195  N   ASN A 155      -5.317  -0.144  16.352  1.00 11.42      A    N  
ANISOU 1195  N   ASN A 155     1262   1663   1414    -71    115    -64  A    N  
ATOM   1196  CA  ASN A 155      -4.764  -0.315  17.709  1.00 12.77      A    C  
ANISOU 1196  CA  ASN A 155     1424   1823   1605    -74    103    -63  A    C  
ATOM   1197  C   ASN A 155      -5.086  -1.682  18.324  1.00 12.49      A    C  
ANISOU 1197  C   ASN A 155     1393   1773   1579    -46    102    -85  A    C  
ATOM   1198  O   ASN A 155      -4.928  -1.872  19.507  1.00 13.15      A    O  
ANISOU 1198  O   ASN A 155     1478   1841   1677    -47     90    -87  A    O  
ATOM   1199  CB  ASN A 155      -5.241   0.827  18.641  1.00 11.15      A    C  
ANISOU 1199  CB  ASN A 155     1239   1589   1409    -97     81    -52  A    C  
ATOM   1200  CG  ASN A 155      -4.403   2.097  18.481  1.00 12.59      A    C  
ANISOU 1200  CG  ASN A 155     1410   1782   1592   -127     74    -24  A    C  
ATOM   1201  ND2 ASN A 155      -4.988   3.222  18.843  1.00 13.03      A    N  
ANISOU 1201  ND2 ASN A 155     1489   1812   1649   -146     54    -16  A    N  
ATOM   1202  OD1 ASN A 155      -3.226   2.070  18.043  1.00 13.55      A    O  
ANISOU 1202  OD1 ASN A 155     1500   1935   1713   -134     84     -8  A    O  
ATOM   1203  N   LEU A 156      -5.586  -2.604  17.507  1.00 11.55      A    N  
ANISOU 1203  N   LEU A 156     1280   1657   1452    -24    111   -104  A    N  
ATOM   1204  CA  LEU A 156      -5.905  -3.975  17.936  1.00 11.66      A    C  
ANISOU 1204  CA  LEU A 156     1300   1656   1476      1    106   -124  A    C  
ATOM   1205  C   LEU A 156      -5.167  -4.948  17.050  1.00 15.25      A    C  
ANISOU 1205  C   LEU A 156     1738   2136   1920     28    118   -138  A    C  
ATOM   1206  O   LEU A 156      -5.226  -4.876  15.835  1.00 17.28      A    O  
ANISOU 1206  O   LEU A 156     1998   2410   2157     36    130   -142  A    O  
ATOM   1207  CB  LEU A 156      -7.382  -4.218  17.798  1.00 12.07      A    C  
ANISOU 1207  CB  LEU A 156     1377   1680   1528      4     98   -135  A    C  
ATOM   1208  CG  LEU A 156      -8.207  -3.252  18.657  1.00 14.03      A    C  
ANISOU 1208  CG  LEU A 156     1640   1906   1785    -16     88   -122  A    C  
ATOM   1209  CD1 LEU A 156      -9.689  -3.303  18.291  1.00 17.70      A    C  
ANISOU 1209  CD1 LEU A 156     2125   2349   2251    -14     82   -128  A    C  
ATOM   1210  CD2 LEU A 156      -8.033  -3.562  20.138  1.00 14.33      A    C  
ANISOU 1210  CD2 LEU A 156     1678   1929   1839    -16     79   -121  A    C  
ATOM   1211  N   ALA A 157      -4.354  -5.785  17.652  1.00 16.15      A    N  
ANISOU 1211  N   ALA A 157     1837   2253   2046     44    117   -145  A    N  
ATOM   1212  CA  ALA A 157      -3.481  -6.674  16.879  1.00 16.75      A    C  
ANISOU 1212  CA  ALA A 157     1895   2357   2112     74    129   -158  A    C  
ATOM   1213  C   ALA A 157      -3.778  -8.096  17.256  1.00 15.07      A    C  
ANISOU 1213  C   ALA A 157     1695   2120   1912    102    114   -181  A    C  
ATOM   1214  O   ALA A 157      -4.135  -8.405  18.411  1.00 14.28      A    O  
ANISOU 1214  O   ALA A 157     1603   1992   1833     94     97   -180  A    O  
ATOM   1215  CB  ALA A 157      -2.033  -6.334  17.111  1.00 25.57      A    C  
ANISOU 1215  CB  ALA A 157     2976   3506   3234     70    140   -142  A    C  
ATOM   1216  N   VAL A 158      -3.619  -9.002  16.268  1.00 15.02      A    N  
ANISOU 1216  N   VAL A 158     1691   2125   1891    135    119   -204  A    N  
ATOM   1217  CA  VAL A 158      -3.861 -10.372  16.501  1.00 18.45      A    C  
ANISOU 1217  CA  VAL A 158     2140   2534   2338    163    100   -226  A    C  
ATOM   1218  C   VAL A 158      -2.637 -11.145  16.044  1.00 23.19      A    C  
ANISOU 1218  C   VAL A 158     2719   3163   2930    201    111   -241  A    C  
ATOM   1219  O   VAL A 158      -1.761 -10.633  15.312  1.00 22.15      A    O  
ANISOU 1219  O   VAL A 158     2563   3074   2778    208    137   -235  A    O  
ATOM   1220  CB  VAL A 158      -5.073 -10.941  15.769  1.00 28.37      A    C  
ANISOU 1220  CB  VAL A 158     3429   3764   3587    173     86   -244  A    C  
ATOM   1221  CG1 VAL A 158      -6.353 -10.462  16.392  1.00 29.04      A    C  
ANISOU 1221  CG1 VAL A 158     3531   3816   3686    141     72   -230  A    C  
ATOM   1222  CG2 VAL A 158      -5.015 -10.614  14.281  1.00 33.92      A    C  
ANISOU 1222  CG2 VAL A 158     4138   4495   4257    187    102   -252  A    C  
ATOM   1223  N   ASN A 159      -2.591 -12.364  16.521  1.00 21.49      A    N  
ANISOU 1223  N   ASN A 159     2511   2923   2730    224     91   -259  A    N  
ATOM   1224  CA  ASN A 159      -1.716 -13.385  15.953  1.00 24.53      A    C  
ANISOU 1224  CA  ASN A 159     2888   3325   3107    271     93   -284  A    C  
ATOM   1225  C   ASN A 159      -2.510 -14.422  15.088  1.00 26.37      A    C  
ANISOU 1225  C   ASN A 159     3158   3533   3330    302     73   -315  A    C  
ATOM   1226  O   ASN A 159      -3.748 -14.323  14.876  1.00 23.23      A    O  
ANISOU 1226  O   ASN A 159     2790   3105   2931    284     58   -316  A    O  
ATOM   1227  CB  ASN A 159      -0.913 -14.021  17.082  1.00 21.32      A    C  
ANISOU 1227  CB  ASN A 159     2462   2910   2727    279     79   -282  A    C  
ATOM   1228  CG  ASN A 159      -1.726 -14.921  17.976  1.00 20.67      A    C  
ANISOU 1228  CG  ASN A 159     2407   2775   2670    276     44   -288  A    C  
ATOM   1229  ND2 ASN A 159      -1.138 -15.369  19.102  1.00 28.99      A    N  
ANISOU 1229  ND2 ASN A 159     3449   3818   3747    276     29   -282  A    N  
ATOM   1230  OD1 ASN A 159      -2.859 -15.250  17.663  1.00 21.67      A    O  
ANISOU 1230  OD1 ASN A 159     2566   2872   2796    272     28   -296  A    O  
ATOM   1231  N   GLU A 160      -1.795 -15.435  14.581  1.00 28.14      A    N  
ANISOU 1231  N   GLU A 160     3381   3765   3544    351     71   -342  A    N  
ATOM   1232  CA  GLU A 160      -2.431 -16.496  13.771  1.00 32.43      A    C  
ANISOU 1232  CA  GLU A 160     3963   4281   4077    385     46   -375  A    C  
ATOM   1233  C   GLU A 160      -3.506 -17.275  14.492  1.00 33.19      A    C  
ANISOU 1233  C   GLU A 160     4090   4317   4205    371      2   -378  A    C  
ATOM   1234  O   GLU A 160      -4.462 -17.728  13.863  1.00 37.41      A    O  
ANISOU 1234  O   GLU A 160     4659   4823   4733    377    -22   -393  A    O  
ATOM   1235  CB  GLU A 160      -1.378 -17.514  13.278  1.00 37.57      A    C  
ANISOU 1235  CB  GLU A 160     4608   4950   4717    445     48   -405  A    C  
ATOM   1236  CG  GLU A 160      -0.427 -16.976  12.229  1.00 62.93      A    C  
ANISOU 1236  CG  GLU A 160     7796   8225   7890    473     91   -409  A    C  
ATOM   1237  CD  GLU A 160      -1.083 -16.778  10.879  1.00 81.49      A    C  
ANISOU 1237  CD  GLU A 160    10178  10583  10200    486     97   -423  A    C  
ATOM   1238  OE1 GLU A 160      -1.780 -15.757  10.692  1.00105.47      A    O  
ANISOU 1238  OE1 GLU A 160    13219  13623  13230    443    107   -401  A    O  
ATOM   1239  OE2 GLU A 160      -0.878 -17.637   9.996  1.00 76.41      A    O1-
ANISOU 1239  OE2 GLU A 160     9556   9944   9532    539     91   -458  A    O1-
ATOM   1240  N   ASP A 161      -3.334 -17.463  15.801  1.00 26.75      A    N  
ANISOU 1240  N   ASP A 161     3260   3484   3420    351     -9   -362  A    N  
ATOM   1241  CA  ASP A 161      -4.305 -18.167  16.622  1.00 23.68      A    C  
ANISOU 1241  CA  ASP A 161     2895   3042   3061    333    -48   -356  A    C  
ATOM   1242  C   ASP A 161      -5.446 -17.259  17.028  1.00 26.56      A    C  
ANISOU 1242  C   ASP A 161     3264   3393   3433    285    -43   -329  A    C  
ATOM   1243  O   ASP A 161      -6.254 -17.637  17.846  1.00 26.46      A    O  
ANISOU 1243  O   ASP A 161     3264   3344   3446    263    -67   -315  A    O  
ATOM   1244  CB  ASP A 161      -3.652 -18.814  17.847  1.00 27.96      A    C  
ANISOU 1244  CB  ASP A 161     3424   3569   3631    337    -63   -350  A    C  
ATOM   1245  CG  ASP A 161      -2.748 -20.000  17.464  1.00 41.19      A    C  
ANISOU 1245  CG  ASP A 161     5102   5243   5304    390    -79   -382  A    C  
ATOM   1246  OD1 ASP A 161      -2.940 -20.566  16.362  1.00 38.27      A    O  
ANISOU 1246  OD1 ASP A 161     4755   4867   4917    424    -88   -411  A    O  
ATOM   1247  OD2 ASP A 161      -1.836 -20.345  18.256  1.00 45.89      A    O1-
ANISOU 1247  OD2 ASP A 161     5678   5843   5917    401    -81   -378  A    O1-
ATOM   1248  N   CYS A 162      -5.548 -16.092  16.388  1.00 23.41      A    N  
ANISOU 1248  N   CYS A 162     2857   3025   3011    269    -15   -320  A    N  
ATOM   1249  CA  CYS A 162      -6.595 -15.115  16.651  1.00 27.18      A    C  
ANISOU 1249  CA  CYS A 162     3339   3495   3493    227     -9   -296  A    C  
ATOM   1250  C   CYS A 162      -6.577 -14.576  18.093  1.00 21.86      A    C  
ANISOU 1250  C   CYS A 162     2649   2816   2839    197     -5   -268  A    C  
ATOM   1251  O   CYS A 162      -7.610 -14.156  18.611  1.00 21.94      A    O  
ANISOU 1251  O   CYS A 162     2667   2807   2860    167    -10   -250  A    O  
ATOM   1252  CB  CYS A 162      -7.934 -15.732  16.357  1.00 26.91      A    C  
ANISOU 1252  CB  CYS A 162     3334   3418   3470    223    -41   -301  A    C  
ATOM   1253  SG  CYS A 162      -9.241 -14.504  16.053  1.00 30.44      A    S  
ANISOU 1253  SG  CYS A 162     3787   3864   3912    186    -31   -282  A    S  
ATOM   1254  N   GLU A 163      -5.438 -14.594  18.724  1.00 17.61      A    N  
ANISOU 1254  N   GLU A 163     2089   2296   2305    203      4   -265  A    N  
ATOM   1255  CA  GLU A 163      -5.292 -14.033  20.061  1.00 16.81      A    C  
ANISOU 1255  CA  GLU A 163     1977   2193   2218    176      6   -240  A    C  
ATOM   1256  C   GLU A 163      -5.038 -12.531  19.866  1.00 16.07      A    C  
ANISOU 1256  C   GLU A 163     1868   2130   2107    154     34   -225  A    C  
ATOM   1257  O   GLU A 163      -4.130 -12.120  19.139  1.00 18.58      A    O  
ANISOU 1257  O   GLU A 163     2166   2482   2410    165     53   -229  A    O  
ATOM   1258  CB  GLU A 163      -4.182 -14.727  20.810  1.00 20.84      A    C  
ANISOU 1258  CB  GLU A 163     2472   2704   2742    193     -3   -243  A    C  
ATOM   1259  CG  GLU A 163      -4.514 -16.224  20.986  1.00 30.32      A    C  
ANISOU 1259  CG  GLU A 163     3692   3869   3960    215    -34   -258  A    C  
ATOM   1260  CD  GLU A 163      -3.385 -17.146  21.473  1.00 39.65      A    C  
ANISOU 1260  CD  GLU A 163     4862   5049   5153    242    -48   -268  A    C  
ATOM   1261  OE1 GLU A 163      -2.186 -16.919  21.184  1.00 39.77      A    O  
ANISOU 1261  OE1 GLU A 163     4853   5098   5160    261    -32   -275  A    O  
ATOM   1262  OE2 GLU A 163      -3.736 -18.158  22.120  1.00 58.16      A    O1-
ANISOU 1262  OE2 GLU A 163     7224   7357   7519    245    -78   -269  A    O1-
ATOM   1263  N   LEU A 164      -5.846 -11.683  20.547  1.00 12.74      A    N  
ANISOU 1263  N   LEU A 164     1454   1697   1690    122     34   -204  A    N  
ATOM   1264  CA  LEU A 164      -5.839 -10.269  20.376  1.00 13.29      A    C  
ANISOU 1264  CA  LEU A 164     1516   1785   1747    100     53   -190  A    C  
ATOM   1265  C   LEU A 164      -5.231  -9.503  21.517  1.00 13.83      A    C  
ANISOU 1265  C   LEU A 164     1574   1861   1822     80     54   -172  A    C  
ATOM   1266  O   LEU A 164      -5.403  -9.897  22.687  1.00 13.84      A    O  
ANISOU 1266  O   LEU A 164     1581   1840   1836     77     41   -166  A    O  
ATOM   1267  CB  LEU A 164      -7.312  -9.848  20.313  1.00 13.38      A    C  
ANISOU 1267  CB  LEU A 164     1548   1776   1759     82     49   -184  A    C  
ATOM   1268  CG  LEU A 164      -7.604  -8.394  20.057  1.00 12.57      A    C  
ANISOU 1268  CG  LEU A 164     1446   1686   1643     59     62   -170  A    C  
ATOM   1269  CD1 LEU A 164      -8.806  -8.181  19.137  1.00 13.54      A    C  
ANISOU 1269  CD1 LEU A 164     1585   1799   1760     55     61   -173  A    C  
ATOM   1270  CD2 LEU A 164      -7.826  -7.625  21.350  1.00 13.07      A    C  
ANISOU 1270  CD2 LEU A 164     1512   1740   1714     39     60   -152  A    C  
ATOM   1271  N   LYS A 165      -4.503  -8.434  21.190  1.00 13.07      A    N  
ANISOU 1271  N   LYS A 165     1460   1790   1715     68     68   -161  A    N  
ATOM   1272  CA  LYS A 165      -4.013  -7.473  22.165  1.00 12.03      A    C  
ANISOU 1272  CA  LYS A 165     1322   1661   1588     46     64   -142  A    C  
ATOM   1273  C   LYS A 165      -4.406  -6.074  21.813  1.00 13.13      A    C  
ANISOU 1273  C   LYS A 165     1467   1805   1715     21     71   -129  A    C  
ATOM   1274  O   LYS A 165      -4.382  -5.715  20.652  1.00 14.34      A    O  
ANISOU 1274  O   LYS A 165     1614   1978   1855     21     85   -131  A    O  
ATOM   1275  CB  LYS A 165      -2.502  -7.560  22.362  1.00 14.54      A    C  
ANISOU 1275  CB  LYS A 165     1611   2003   1912     51     64   -138  A    C  
ATOM   1276  CG  LYS A 165      -2.054  -8.904  22.897  1.00 16.77      A    C  
ANISOU 1276  CG  LYS A 165     1889   2275   2209     76     53   -150  A    C  
ATOM   1277  CD  LYS A 165      -0.583  -8.909  23.226  1.00 17.88      A    C  
ANISOU 1277  CD  LYS A 165     1997   2436   2359     80     49   -143  A    C  
ATOM   1278  CE  LYS A 165      -0.036 -10.330  23.358  1.00 24.59      A    C  
ANISOU 1278  CE  LYS A 165     2839   3284   3222    112     40   -159  A    C  
ATOM   1279  NZ  LYS A 165      -0.603 -11.029  24.519  1.00 20.60      A    N1+
ANISOU 1279  NZ  LYS A 165     2359   2742   2728    112     17   -161  A    N1+
ATOM   1280  N   ILE A 166      -4.760  -5.300  22.838  1.00 11.23      A    N  
ANISOU 1280  N   ILE A 166     1241   1548   1478      4     61   -118  A    N  
ATOM   1281  CA  ILE A 166      -4.949  -3.875  22.776  1.00 10.72      A    C  
ANISOU 1281  CA  ILE A 166     1184   1484   1406    -20     61   -104  A    C  
ATOM   1282  C   ILE A 166      -3.623  -3.157  22.919  1.00 10.65      A    C  
ANISOU 1282  C   ILE A 166     1153   1494   1400    -36     56    -89  A    C  
ATOM   1283  O   ILE A 166      -2.847  -3.458  23.821  1.00 11.68      A    O  
ANISOU 1283  O   ILE A 166     1274   1622   1540    -34     44    -86  A    O  
ATOM   1284  CB  ILE A 166      -5.852  -3.418  23.910  1.00 10.35      A    C  
ANISOU 1284  CB  ILE A 166     1163   1411   1359    -27     50   -101  A    C  
ATOM   1285  CG1 ILE A 166      -7.243  -4.109  23.787  1.00 11.19      A    C  
ANISOU 1285  CG1 ILE A 166     1285   1501   1466    -15     56   -110  A    C  
ATOM   1286  CG2 ILE A 166      -6.032  -1.895  23.878  1.00 11.58      A    C  
ANISOU 1286  CG2 ILE A 166     1330   1564   1507    -49     45    -89  A    C  
ATOM   1287  CD1 ILE A 166      -8.178  -3.893  24.975  1.00 12.91      A    C  
ANISOU 1287  CD1 ILE A 166     1524   1696   1684    -16     50   -105  A    C  
ATOM   1288  N  ALEU A 167      -3.372  -2.207  22.011  0.60 10.09      A    N  
ANISOU 1288  N  ALEU A 167     1073   1440   1320    -51     64    -77  A    N  
ATOM   1289  N  BLEU A 167      -3.365  -2.188  22.055  0.40 10.26      A    N  
ANISOU 1289  N  BLEU A 167     1096   1462   1343    -52     63    -77  A    N  
ATOM   1290  CA ALEU A 167      -2.144  -1.375  22.013  0.60 11.47      A    C  
ANISOU 1290  CA ALEU A 167     1224   1634   1501    -72     58    -56  A    C  
ATOM   1291  CA BLEU A 167      -2.198  -1.333  22.235  0.40 11.51      A    C  
ANISOU 1291  CA BLEU A 167     1232   1634   1507    -74     54    -56  A    C  
ATOM   1292  C  ALEU A 167      -2.537   0.084  21.811  0.60 12.08      A    C  
ANISOU 1292  C  ALEU A 167     1317   1703   1571   -100     48    -41  A    C  
ATOM   1293  C  BLEU A 167      -2.544   0.095  21.832  0.40 12.05      A    C  
ANISOU 1293  C  BLEU A 167     1313   1698   1567   -100     48    -41  A    C  
ATOM   1294  O  ALEU A 167      -3.718   0.387  21.580  0.60 10.89      A    O  
ANISOU 1294  O  ALEU A 167     1193   1535   1411    -99     49    -48  A    O  
ATOM   1295  O  BLEU A 167      -3.713   0.394  21.553  0.40 10.99      A    O  
ANISOU 1295  O  BLEU A 167     1205   1547   1423    -99     50    -48  A    O  
ATOM   1296  CB ALEU A 167      -1.198  -1.788  20.871  0.60 13.33      A    C  
ANISOU 1296  CB ALEU A 167     1423   1910   1732    -64     79    -51  A    C  
ATOM   1297  CB BLEU A 167      -1.002  -1.909  21.467  0.40 12.85      A    C  
ANISOU 1297  CB BLEU A 167     1361   1841   1679    -63     70    -52  A    C  
ATOM   1298  CG ALEU A 167      -1.007  -3.263  20.634  0.60 14.94      A    C  
ANISOU 1298  CG ALEU A 167     1616   2124   1937    -29     90    -72  A    C  
ATOM   1299  CG BLEU A 167      -1.226  -2.344  20.025  0.40 12.18      A    C  
ANISOU 1299  CG BLEU A 167     1270   1781   1577    -47     96    -60  A    C  
ATOM   1300  CD1ALEU A 167      -1.925  -3.822  19.548  0.60 15.39      A    C  
ANISOU 1300  CD1ALEU A 167     1688   2182   1976     -9    107    -91  A    C  
ATOM   1301  CD1BLEU A 167      -1.420  -1.143  19.103  0.40 12.55      A    C  
ANISOU 1301  CD1BLEU A 167     1319   1841   1610    -71    103    -42  A    C  
ATOM   1302  CD2ALEU A 167       0.425  -3.534  20.251  0.60 17.11      A    C  
ANISOU 1302  CD2ALEU A 167     1846   2436   2217    -21    102    -63  A    C  
ATOM   1303  CD2BLEU A 167      -0.037  -3.168  19.535  0.40 15.14      A    C  
ANISOU 1303  CD2BLEU A 167     1606   2192   1954    -26    112    -62  A    C  
ATOM   1304  N   ASP A 168      -1.563   0.989  21.855  1.00 12.35      A    N  
ANISOU 1304  N   ASP A 168     1333   1747   1613   -125     36    -17  A    N  
ATOM   1305  CA  ASP A 168      -1.776   2.363  21.384  1.00 12.36      A    C  
ANISOU 1305  CA  ASP A 168     1345   1743   1609   -153     27      1  A    C  
ATOM   1306  C   ASP A 168      -0.538   2.774  20.619  1.00 14.82      A    C  
ANISOU 1306  C   ASP A 168     1618   2090   1925   -173     33     29  A    C  
ATOM   1307  O   ASP A 168       0.491   2.987  21.217  1.00 15.14      A    O  
ANISOU 1307  O   ASP A 168     1636   2134   1983   -188     17     46  A    O  
ATOM   1308  CB  ASP A 168      -2.098   3.314  22.544  1.00 15.22      A    C  
ANISOU 1308  CB  ASP A 168     1739   2069   1976   -168     -6      4  A    C  
ATOM   1309  CG  ASP A 168      -2.533   4.696  22.077  1.00 16.55      A    C  
ANISOU 1309  CG  ASP A 168     1926   2223   2139   -193    -20     19  A    C  
ATOM   1310  OD1 ASP A 168      -2.346   5.023  20.904  1.00 17.69      A    O  
ANISOU 1310  OD1 ASP A 168     2054   2390   2277   -205     -6     34  A    O  
ATOM   1311  OD2 ASP A 168      -3.040   5.450  22.968  1.00 20.63      A    O1-
ANISOU 1311  OD2 ASP A 168     2476   2705   2656   -198    -47     14  A    O1-
ATOM   1312  N   ARG A 186     -11.478   9.946  13.258  1.00 17.21      A    N  
ANISOU 1312  N   ARG A 186     2189   2235   2117   -217    -28     29  A    N  
ATOM   1313  CA  ARG A 186     -12.504  10.177  14.262  1.00 17.31      A    C  
ANISOU 1313  CA  ARG A 186     2219   2212   2144   -198    -44     10  A    C  
ATOM   1314  C   ARG A 186     -13.671   9.201  14.085  1.00 14.17      A    C  
ANISOU 1314  C   ARG A 186     1823   1813   1749   -170    -31    -14  A    C  
ATOM   1315  O   ARG A 186     -14.665   9.299  14.808  1.00 13.79      A    O  
ANISOU 1315  O   ARG A 186     1785   1741   1713   -152    -38    -28  A    O  
ATOM   1316  CB  ARG A 186     -13.024  11.605  14.205  1.00 24.93      A    C  
ANISOU 1316  CB  ARG A 186     3212   3147   3112   -211    -76     21  A    C  
ATOM   1317  CG  ARG A 186     -13.700  11.928  12.924  1.00 27.22      A    C  
ANISOU 1317  CG  ARG A 186     3513   3437   3392   -216    -82     27  A    C  
ATOM   1318  CD  ARG A 186     -14.269  13.343  12.988  1.00 37.39      A    C  
ANISOU 1318  CD  ARG A 186     4830   4688   4686   -225   -117     36  A    C  
ATOM   1319  NE  ARG A 186     -13.249  14.384  13.039  1.00 29.81      A    N  
ANISOU 1319  NE  ARG A 186     3876   3723   3726   -259   -140     63  A    N  
ATOM   1320  CZ  ARG A 186     -12.564  14.829  11.972  1.00 29.80      A    C  
ANISOU 1320  CZ  ARG A 186     3872   3740   3713   -289   -142     95  A    C  
ATOM   1321  NH1 ARG A 186     -12.726  14.298  10.772  1.00 27.85      A    N1+
ANISOU 1321  NH1 ARG A 186     3617   3518   3446   -289   -122     99  A    N1+
ATOM   1322  NH2 ARG A 186     -11.667  15.794  12.134  1.00 47.10      A    N  
ANISOU 1322  NH2 ARG A 186     6065   5923   5909   -323   -166    123  A    N  
ATOM   1323  N   TRP A 187     -13.519   8.163  13.247  1.00 13.99      A    N  
ANISOU 1323  N   TRP A 187     1785   1815   1715   -162    -10    -18  A    N  
ATOM   1324  CA  TRP A 187     -14.625   7.238  12.965  1.00 11.99      A    C  
ANISOU 1324  CA  TRP A 187     1533   1556   1465   -139     -4    -37  A    C  
ATOM   1325  C   TRP A 187     -15.101   6.397  14.140  1.00 11.42      A    C  
ANISOU 1325  C   TRP A 187     1453   1475   1411   -118      3    -56  A    C  
ATOM   1326  O   TRP A 187     -16.256   5.897  14.121  1.00 12.40      A    O  
ANISOU 1326  O   TRP A 187     1579   1585   1546   -101      0    -67  A    O  
ATOM   1327  CB  TRP A 187     -14.277   6.286  11.824  1.00 13.77      A    C  
ANISOU 1327  CB  TRP A 187     1751   1809   1672   -135     12    -41  A    C  
ATOM   1328  CG  TRP A 187     -14.119   6.966  10.482  1.00 13.20      A    C  
ANISOU 1328  CG  TRP A 187     1691   1749   1577   -149      8    -25  A    C  
ATOM   1329  CD1 TRP A 187     -14.509   8.223  10.162  1.00 17.81      A    C  
ANISOU 1329  CD1 TRP A 187     2292   2315   2159   -167    -13     -9  A    C  
ATOM   1330  CD2 TRP A 187     -13.605   6.388   9.277  1.00 15.04      A    C  
ANISOU 1330  CD2 TRP A 187     1920   2011   1783   -146     22    -23  A    C  
ATOM   1331  CE2 TRP A 187     -13.719   7.363   8.275  1.00 15.72      A    C  
ANISOU 1331  CE2 TRP A 187     2024   2099   1851   -165     11     -4  A    C  
ATOM   1332  CE3 TRP A 187     -13.031   5.170   8.967  1.00 19.04      A    C  
ANISOU 1332  CE3 TRP A 187     2414   2543   2277   -129     44    -36  A    C  
ATOM   1333  NE1 TRP A 187     -14.250   8.472   8.833  1.00 16.87      A    N  
ANISOU 1333  NE1 TRP A 187     2181   2215   2015   -178    -12      5  A    N  
ATOM   1334  CZ2 TRP A 187     -13.266   7.154   6.957  1.00 20.63      A    C  
ANISOU 1334  CZ2 TRP A 187     2648   2751   2439   -165     24      6  A    C  
ATOM   1335  CZ3 TRP A 187     -12.658   4.928   7.608  1.00 21.14      A    C  
ANISOU 1335  CZ3 TRP A 187     2686   2837   2510   -125     55    -32  A    C  
ATOM   1336  CH2 TRP A 187     -12.719   5.934   6.666  1.00 22.26      A    C  
ANISOU 1336  CH2 TRP A 187     2842   2983   2631   -143     48    -10  A    C  
ATOM   1337  N   TYR A 188     -14.251   6.309  15.175  1.00 11.46      A    N  
ANISOU 1337  N   TYR A 188     1449   1485   1421   -120      9    -55  A    N  
ATOM   1338  CA  TYR A 188     -14.528   5.436  16.338  1.00 11.35      A    C  
ANISOU 1338  CA  TYR A 188     1427   1464   1422   -102     17    -68  A    C  
ATOM   1339  C   TYR A 188     -14.758   6.255  17.614  1.00 11.22      A    C  
ANISOU 1339  C   TYR A 188     1423   1427   1413    -99      6    -67  A    C  
ATOM   1340  O   TYR A 188     -14.881   5.680  18.718  1.00 12.49      A    O  
ANISOU 1340  O   TYR A 188     1580   1584   1582    -84     13    -75  A    O  
ATOM   1341  CB  TYR A 188     -13.436   4.350  16.518  1.00 10.18      A    C  
ANISOU 1341  CB  TYR A 188     1259   1337   1270    -99     33    -71  A    C  
ATOM   1342  CG  TYR A 188     -13.231   3.582  15.245  1.00 10.78      A    C  
ANISOU 1342  CG  TYR A 188     1328   1434   1335    -95     43    -75  A    C  
ATOM   1343  CD1 TYR A 188     -14.008   2.475  14.904  1.00 12.62      A    C  
ANISOU 1343  CD1 TYR A 188     1559   1662   1573    -77     46    -89  A    C  
ATOM   1344  CD2 TYR A 188     -12.346   4.069  14.270  1.00 12.87      A    C  
ANISOU 1344  CD2 TYR A 188     1589   1721   1582   -111     47    -61  A    C  
ATOM   1345  CE1 TYR A 188     -13.864   1.819  13.703  1.00 13.00      A    C  
ANISOU 1345  CE1 TYR A 188     1608   1725   1607    -72     51    -96  A    C  
ATOM   1346  CE2 TYR A 188     -12.188   3.419  13.074  1.00 13.17      A    C  
ANISOU 1346  CE2 TYR A 188     1624   1779   1602   -104     58    -65  A    C  
ATOM   1347  CZ  TYR A 188     -12.954   2.296  12.756  1.00 12.28      A    C  
ANISOU 1347  CZ  TYR A 188     1516   1659   1492    -82     59    -85  A    C  
ATOM   1348  OH  TYR A 188     -12.806   1.700  11.562  1.00 15.75      A    O  
ANISOU 1348  OH  TYR A 188     1957   2115   1912    -71     65    -92  A    O  
ATOM   1349  N   ARG A 189     -14.794   7.584  17.524  1.00 10.97      A    N  
ANISOU 1349  N   ARG A 189     1410   1381   1377   -110    -14    -58  A    N  
ATOM   1350  CA  ARG A 189     -14.850   8.462  18.701  1.00 11.92      A    C  
ANISOU 1350  CA  ARG A 189     1547   1480   1502   -105    -29    -60  A    C  
ATOM   1351  C   ARG A 189     -16.271   8.673  19.198  1.00 14.37      A    C  
ANISOU 1351  C   ARG A 189     1870   1772   1819    -81    -31    -72  A    C  
ATOM   1352  O   ARG A 189     -17.169   8.909  18.437  1.00 15.23      A    O  
ANISOU 1352  O   ARG A 189     1982   1874   1931    -77    -36    -72  A    O  
ATOM   1353  CB  ARG A 189     -14.235   9.806  18.300  1.00 20.27      A    C  
ANISOU 1353  CB  ARG A 189     2620   2527   2554   -131    -54    -45  A    C  
ATOM   1354  CG  ARG A 189     -13.536  10.599  19.364  1.00 33.32      A    C  
ANISOU 1354  CG  ARG A 189     4289   4164   4209   -137    -75    -41  A    C  
ATOM   1355  CD  ARG A 189     -12.476  11.479  18.680  1.00 22.69      A    C  
ANISOU 1355  CD  ARG A 189     2943   2819   2860   -173    -95    -17  A    C  
ATOM   1356  NE  ARG A 189     -11.186  11.351  19.326  1.00 30.84      A    N  
ANISOU 1356  NE  ARG A 189     3963   3860   3895   -188    -99     -8  A    N  
ATOM   1357  CZ  ARG A 189     -10.466  12.407  19.727  1.00 26.41      A    C  
ANISOU 1357  CZ  ARG A 189     3416   3279   3338   -209   -132      6  A    C  
ATOM   1358  NH1 ARG A 189      -9.302  12.230  20.315  1.00 35.94      A    N1+
ANISOU 1358  NH1 ARG A 189     4609   4495   4551   -224   -139     15  A    N1+
ATOM   1359  NH2 ARG A 189     -10.907  13.661  19.498  1.00 38.69      A    N  
ANISOU 1359  NH2 ARG A 189     5000   4806   4895   -219   -164     13  A    N  
ATOM   1360  N   ALA A 190     -16.459   8.603  20.522  1.00 14.02      A    N  
ANISOU 1360  N   ALA A 190     1832   1719   1776    -61    -28    -81  A    N  
ATOM   1361  CA  ALA A 190     -17.735   8.807  21.092  1.00 13.51      A    C  
ANISOU 1361  CA  ALA A 190     1775   1642   1716    -34    -26    -89  A    C  
ATOM   1362  C   ALA A 190     -18.288  10.235  20.846  1.00 11.73      A    C  
ANISOU 1362  C   ALA A 190     1574   1394   1490    -31    -51    -89  A    C  
ATOM   1363  O   ALA A 190     -17.522  11.172  20.827  1.00 15.78      A    O  
ANISOU 1363  O   ALA A 190     2106   1893   1996    -47    -74    -84  A    O  
ATOM   1364  CB  ALA A 190     -17.687   8.523  22.564  1.00 17.29      A    C  
ANISOU 1364  CB  ALA A 190     2258   2121   2190    -14    -16    -96  A    C  
ATOM   1365  N   PRO A 191     -19.603  10.337  20.697  1.00 14.42      A    N  
ANISOU 1365  N   PRO A 191     1913   1729   1838     -9    -47    -94  A    N  
ATOM   1366  CA  PRO A 191     -20.218  11.604  20.355  1.00 16.05      A    C  
ANISOU 1366  CA  PRO A 191     2142   1911   2045     -3    -72    -95  A    C  
ATOM   1367  C   PRO A 191     -19.947  12.646  21.437  1.00 15.20      A    C  
ANISOU 1367  C   PRO A 191     2064   1783   1927     11    -92   -104  A    C  
ATOM   1368  O   PRO A 191     -19.758  13.801  21.085  1.00 16.47      A    O  
ANISOU 1368  O   PRO A 191     2251   1921   2087      1   -122   -102  A    O  
ATOM   1369  CB  PRO A 191     -21.695  11.238  20.214  1.00 16.18      A    C  
ANISOU 1369  CB  PRO A 191     2142   1930   2075     22    -59   -100  A    C  
ATOM   1370  CG  PRO A 191     -21.875   9.966  20.944  1.00 18.55      A    C  
ANISOU 1370  CG  PRO A 191     2418   2251   2381     35    -29   -100  A    C  
ATOM   1371  CD  PRO A 191     -20.611   9.265  20.734  1.00 16.64      A    C  
ANISOU 1371  CD  PRO A 191     2170   2022   2131      8    -23    -96  A    C  
ATOM   1372  N   GLU A 192     -19.926  12.284  22.716  1.00 14.20      A    N  
ANISOU 1372  N   GLU A 192     1940   1660   1793     33    -77   -114  A    N  
ATOM   1373  CA  GLU A 192     -19.662  13.288  23.750  1.00 15.01      A    C  
ANISOU 1373  CA  GLU A 192     2079   1741   1883     50   -100   -124  A    C  
ATOM   1374  C   GLU A 192     -18.310  13.942  23.582  1.00 16.03      A    C  
ANISOU 1374  C   GLU A 192     2226   1856   2007     17   -131   -116  A    C  
ATOM   1375  O   GLU A 192     -18.133  15.113  23.930  1.00 16.46      A    O  
ANISOU 1375  O   GLU A 192     2315   1882   2056     20   -165   -122  A    O  
ATOM   1376  CB  GLU A 192     -19.880  12.720  25.164  1.00 14.46      A    C  
ANISOU 1376  CB  GLU A 192     2010   1683   1801     83    -77   -135  A    C  
ATOM   1377  CG  GLU A 192     -18.971  11.528  25.581  1.00 15.41      A    C  
ANISOU 1377  CG  GLU A 192     2110   1824   1919     66    -56   -129  A    C  
ATOM   1378  CD  GLU A 192     -19.514  10.153  25.190  1.00 14.61      A    C  
ANISOU 1378  CD  GLU A 192     1969   1750   1830     65    -22   -121  A    C  
ATOM   1379  OE1 GLU A 192     -19.084   9.162  25.886  1.00 16.08      A    O  
ANISOU 1379  OE1 GLU A 192     2146   1952   2014     66     -3   -118  A    O  
ATOM   1380  OE2 GLU A 192     -20.388  10.062  24.276  1.00 15.53      A    O1-
ANISOU 1380  OE2 GLU A 192     2071   1870   1962     65    -17   -117  A    O1-
ATOM   1381  N   ILE A 193     -17.320  13.233  23.074  1.00 14.97      A    N  
ANISOU 1381  N   ILE A 193     2071   1741   1877    -16   -122   -103  A    N  
ATOM   1382  CA  ILE A 193     -16.021  13.807  22.817  1.00 17.10      A    C  
ANISOU 1382  CA  ILE A 193     2350   2003   2147    -52   -150    -90  A    C  
ATOM   1383  C   ILE A 193     -16.126  14.800  21.627  1.00 20.81      A    C  
ANISOU 1383  C   ILE A 193     2828   2456   2621    -75   -176    -76  A    C  
ATOM   1384  O   ILE A 193     -15.656  15.942  21.704  1.00 23.10      A    O  
ANISOU 1384  O   ILE A 193     3145   2719   2911    -89   -213    -70  A    O  
ATOM   1385  CB  ILE A 193     -14.962  12.729  22.554  1.00 18.75      A    C  
ANISOU 1385  CB  ILE A 193     2527   2241   2359    -77   -129    -78  A    C  
ATOM   1386  CG1 ILE A 193     -14.810  11.806  23.765  1.00 17.93      A    C  
ANISOU 1386  CG1 ILE A 193     2415   2147   2249    -57   -109    -88  A    C  
ATOM   1387  CG2 ILE A 193     -13.639  13.384  22.188  1.00 22.60      A    C  
ANISOU 1387  CG2 ILE A 193     3015   2722   2848   -116   -156    -58  A    C  
ATOM   1388  CD1 ILE A 193     -13.914  10.576  23.551  1.00 22.60      A    C  
ANISOU 1388  CD1 ILE A 193     2974   2768   2845    -73    -87    -80  A    C  
ATOM   1389  N   MET A 194     -16.778  14.365  20.580  1.00 18.89      A    N  
ANISOU 1389  N   MET A 194     2567   2228   2384    -77   -157    -72  A    N  
ATOM   1390  CA  MET A 194     -16.970  15.174  19.368  1.00 22.53      A    C  
ANISOU 1390  CA  MET A 194     3035   2677   2846    -97   -179    -58  A    C  
ATOM   1391  C   MET A 194     -17.751  16.479  19.707  1.00 20.73      A    C  
ANISOU 1391  C   MET A 194     2843   2411   2621    -77   -213    -67  A    C  
ATOM   1392  O   MET A 194     -17.564  17.501  19.023  1.00 18.98      A    O  
ANISOU 1392  O   MET A 194     2641   2169   2401    -99   -246    -54  A    O  
ATOM   1393  CB  MET A 194     -17.788  14.398  18.343  1.00 25.53      A    C  
ANISOU 1393  CB  MET A 194     3393   3077   3231    -93   -155    -57  A    C  
ATOM   1394  CG  MET A 194     -17.333  12.988  17.939  1.00 33.76      A    C  
ANISOU 1394  CG  MET A 194     4402   4154   4271   -101   -120    -54  A    C  
ATOM   1395  SD  MET A 194     -16.090  13.036  16.646  1.00 23.18      A    S  
ANISOU 1395  SD  MET A 194     3052   2834   2923   -145   -122    -28  A    S  
ATOM   1396  CE  MET A 194     -16.919  14.095  15.464  1.00 35.47      A    C  
ANISOU 1396  CE  MET A 194     4629   4371   4477   -153   -149    -18  A    C  
ATOM   1397  N   LEU A 195     -18.668  16.431  20.701  1.00 17.39      A    N  
ANISOU 1397  N   LEU A 195     2430   1980   2196    -33   -205    -90  A    N  
ATOM   1398  CA  LEU A 195     -19.501  17.573  21.138  1.00 16.70      A    C  
ANISOU 1398  CA  LEU A 195     2377   1859   2109     -3   -233   -104  A    C  
ATOM   1399  C   LEU A 195     -18.878  18.379  22.262  1.00 21.98      A    C  
ANISOU 1399  C   LEU A 195     3082   2501   2768      6   -264   -115  A    C  
ATOM   1400  O   LEU A 195     -19.507  19.336  22.727  1.00 24.09      A    O  
ANISOU 1400  O   LEU A 195     3383   2738   3032     36   -290   -131  A    O  
ATOM   1401  CB  LEU A 195     -20.836  17.113  21.620  1.00 17.65      A    C  
ANISOU 1401  CB  LEU A 195     2486   1990   2232     44   -206   -122  A    C  
ATOM   1402  CG  LEU A 195     -21.804  16.524  20.591  1.00 18.64      A    C  
ANISOU 1402  CG  LEU A 195     2580   2131   2370     45   -185   -116  A    C  
ATOM   1403  CD1 LEU A 195     -22.847  15.620  21.240  1.00 20.59      A    C  
ANISOU 1403  CD1 LEU A 195     2801   2400   2621     82   -148   -126  A    C  
ATOM   1404  CD2 LEU A 195     -22.443  17.621  19.784  1.00 22.37      A    C  
ANISOU 1404  CD2 LEU A 195     3072   2576   2849     46   -218   -114  A    C  
ATOM   1405  N   ASN A 196     -17.683  18.009  22.704  1.00 18.55      A    N  
ANISOU 1405  N   ASN A 196     2643   2076   2329    -18   -264   -107  A    N  
ATOM   1406  CA  ASN A 196     -16.981  18.724  23.780  1.00 17.86      A    C  
ANISOU 1406  CA  ASN A 196     2591   1960   2233    -15   -298   -116  A    C  
ATOM   1407  C   ASN A 196     -17.778  18.798  25.073  1.00 21.96      A    C  
ANISOU 1407  C   ASN A 196     3136   2471   2738     41   -292   -145  A    C  
ATOM   1408  O   ASN A 196     -17.811  19.838  25.780  1.00 22.19      A    O  
ANISOU 1408  O   ASN A 196     3210   2464   2757     63   -330   -161  A    O  
ATOM   1409  CB  ASN A 196     -16.647  20.171  23.319  1.00 21.03      A    C  
ANISOU 1409  CB  ASN A 196     3029   2320   2642    -37   -356   -105  A    C  
ATOM   1410  CG  ASN A 196     -15.613  20.817  24.192  1.00 27.44      A    C  
ANISOU 1410  CG  ASN A 196     3873   3103   3450    -50   -399   -105  A    C  
ATOM   1411  ND2 ASN A 196     -15.857  22.066  24.526  1.00 24.11      A    N  
ANISOU 1411  ND2 ASN A 196     3498   2635   3026    -35   -449   -116  A    N  
ATOM   1412  OD1 ASN A 196     -14.569  20.217  24.522  1.00 28.99      A    O  
ANISOU 1412  OD1 ASN A 196     4052   3318   3647    -74   -391    -95  A    O  
ATOM   1413  N   TRP A 197     -18.446  17.701  25.408  1.00 19.20      A    N  
ANISOU 1413  N   TRP A 197     2757   2155   2384     68   -243   -152  A    N  
ATOM   1414  CA  TRP A 197     -19.245  17.672  26.609  1.00 19.19      A    C  
ANISOU 1414  CA  TRP A 197     2772   2154   2365    122   -228   -176  A    C  
ATOM   1415  C   TRP A 197     -18.437  17.525  27.885  1.00 25.13      A    C  
ANISOU 1415  C   TRP A 197     3547   2902   3098    130   -235   -185  A    C  
ATOM   1416  O   TRP A 197     -18.958  17.829  28.966  1.00 27.48      A    O  
ANISOU 1416  O   TRP A 197     3874   3192   3376    177   -234   -208  A    O  
ATOM   1417  CB  TRP A 197     -20.326  16.612  26.526  1.00 20.50      A    C  
ANISOU 1417  CB  TRP A 197     2900   2355   2536    145   -176   -176  A    C  
ATOM   1418  CG  TRP A 197     -21.494  16.998  25.686  1.00 19.28      A    C  
ANISOU 1418  CG  TRP A 197     2735   2196   2395    160   -174   -176  A    C  
ATOM   1419  CD1 TRP A 197     -21.739  18.248  25.053  1.00 17.63      A    C  
ANISOU 1419  CD1 TRP A 197     2553   1954   2192    158   -215   -179  A    C  
ATOM   1420  CD2 TRP A 197     -22.613  16.186  25.378  1.00 18.67      A    C  
ANISOU 1420  CD2 TRP A 197     2618   2146   2329    177   -135   -172  A    C  
ATOM   1421  CE2 TRP A 197     -23.516  16.963  24.600  1.00 19.75      A    C  
ANISOU 1421  CE2 TRP A 197     2760   2267   2479    189   -153   -173  A    C  
ATOM   1422  CE3 TRP A 197     -22.957  14.854  25.674  1.00 20.05      A    C  
ANISOU 1422  CE3 TRP A 197     2756   2357   2507    184    -90   -165  A    C  
ATOM   1423  NE1 TRP A 197     -22.957  18.211  24.430  1.00 21.09      A    N  
ANISOU 1423  NE1 TRP A 197     2971   2399   2643    178   -201   -178  A    N  
ATOM   1424  CZ2 TRP A 197     -24.714  16.432  24.091  1.00 22.12      A    C  
ANISOU 1424  CZ2 TRP A 197     3024   2586   2796    204   -126   -168  A    C  
ATOM   1425  CZ3 TRP A 197     -24.164  14.333  25.165  1.00 25.40      A    C  
ANISOU 1425  CZ3 TRP A 197     3398   3052   3202    197    -65   -158  A    C  
ATOM   1426  CH2 TRP A 197     -25.030  15.130  24.401  1.00 24.87      A    C  
ANISOU 1426  CH2 TRP A 197     3334   2969   3148    208    -83   -160  A    C  
ATOM   1427  N   MET A 198     -17.186  17.110  27.745  1.00 21.38      A    N  
ANISOU 1427  N   MET A 198     3060   2433   2630     87   -243   -170  A    N  
ATOM   1428  CA AMET A 198     -16.265  16.908  28.863  0.70 31.69      A    C  
ANISOU 1428  CA AMET A 198     4383   3735   3922     87   -253   -175  A    C  
ATOM   1429  CA BMET A 198     -16.288  16.955  28.884  0.30 29.36      A    C  
ANISOU 1429  CA BMET A 198     4091   3439   3626     89   -255   -176  A    C  
ATOM   1430  C   MET A 198     -16.795  15.886  29.871  1.00 27.80      A    C  
ANISOU 1430  C   MET A 198     3881   3271   3412    125   -210   -187  A    C  
ATOM   1431  O   MET A 198     -17.706  15.102  29.555  1.00 29.16      A    O  
ANISOU 1431  O   MET A 198     4019   3471   3588    140   -166   -183  A    O  
ATOM   1432  CB AMET A 198     -15.887  18.248  29.521  0.70 27.79      A    C  
ANISOU 1432  CB AMET A 198     3947   3195   3417     97   -312   -189  A    C  
ATOM   1433  CB BMET A 198     -16.056  18.324  29.556  0.30 32.18      A    C  
ANISOU 1433  CB BMET A 198     4507   3749   3971    104   -312   -192  A    C  
ATOM   1434  CG AMET A 198     -15.136  19.197  28.587  0.70 29.73      A    C  
ANISOU 1434  CG AMET A 198     4201   3412   3682     50   -361   -170  A    C  
ATOM   1435  CG BMET A 198     -15.466  19.360  28.601  0.30 34.76      A    C  
ANISOU 1435  CG BMET A 198     4844   4044   4318     61   -361   -175  A    C  
ATOM   1436  SD AMET A 198     -13.666  18.490  27.795  0.70 35.12      A    S  
ANISOU 1436  SD AMET A 198     4838   4119   4389    -18   -357   -135  A    S  
ATOM   1437  SD BMET A 198     -15.678  21.081  29.097  0.30 43.97      A    S  
ANISOU 1437  SD BMET A 198     6081   5150   5474     86   -430   -196  A    S  
ATOM   1438  CE AMET A 198     -12.446  18.547  29.115  0.70 33.69      A    C  
ANISOU 1438  CE AMET A 198     4683   3920   4199    -24   -392   -139  A    C  
ATOM   1439  CE BMET A 198     -17.092  21.577  28.109  0.30 27.29      A    C  
ANISOU 1439  CE BMET A 198     3963   3035   3371    108   -418   -200  A    C  
ATOM   1440  N   HIS A 199     -16.132  15.766  31.017  1.00 27.63      A    N  
ANISOU 1440  N   HIS A 199     3883   3244   3372    135   -220   -195  A    N  
ATOM   1441  CA  HIS A 199     -16.537  14.730  31.998  1.00 30.23      A    C  
ANISOU 1441  CA  HIS A 199     4203   3602   3683    166   -179   -200  A    C  
ATOM   1442  C   HIS A 199     -16.699  13.322  31.373  1.00 24.85      A    C  
ANISOU 1442  C   HIS A 199     3464   2959   3019    147   -131   -182  A    C  
ATOM   1443  O   HIS A 199     -17.692  12.647  31.617  1.00 30.62      A    O  
ANISOU 1443  O   HIS A 199     4176   3715   3744    175    -91   -183  A    O  
ATOM   1444  CB  HIS A 199     -17.885  15.112  32.643  1.00 29.31      A    C  
ANISOU 1444  CB  HIS A 199     4107   3486   3544    226   -160   -220  A    C  
ATOM   1445  CG  HIS A 199     -17.935  16.506  33.161  1.00 55.24      A    C  
ANISOU 1445  CG  HIS A 199     7449   6732   6810    254   -206   -242  A    C  
ATOM   1446  CD2 HIS A 199     -18.582  17.603  32.704  1.00 61.76      A    C  
ANISOU 1446  CD2 HIS A 199     8296   7531   7640    271   -229   -254  A    C  
ATOM   1447  ND1 HIS A 199     -17.276  16.894  34.307  1.00 69.28      A    N  
ANISOU 1447  ND1 HIS A 199     9274   8488   8561    270   -237   -258  A    N  
ATOM   1448  CE1 HIS A 199     -17.510  18.173  34.532  1.00 56.12      A    C  
ANISOU 1448  CE1 HIS A 199     7657   6783   6883    296   -279   -279  A    C  
ATOM   1449  NE2 HIS A 199     -18.300  18.627  33.573  1.00 78.54      A    N  
ANISOU 1449  NE2 HIS A 199    10481   9620   9740    298   -275   -276  A    N  
ATOM   1450  N   TYR A 200     -15.731  12.873  30.607  1.00 23.40      A    N  
ANISOU 1450  N   TYR A 200     3253   2783   2855    101   -137   -165  A    N  
ATOM   1451  CA  TYR A 200     -15.869  11.610  29.897  1.00 20.54      A    C  
ANISOU 1451  CA  TYR A 200     2842   2452   2510     84    -99   -150  A    C  
ATOM   1452  C   TYR A 200     -15.747  10.463  30.867  1.00 28.90      A    C  
ANISOU 1452  C   TYR A 200     3891   3532   3557     98    -72   -149  A    C  
ATOM   1453  O   TYR A 200     -15.085  10.586  31.913  1.00 31.42      A    O  
ANISOU 1453  O   TYR A 200     4238   3842   3861    105    -88   -156  A    O  
ATOM   1454  CB  TYR A 200     -14.808  11.506  28.787  1.00 21.61      A    C  
ANISOU 1454  CB  TYR A 200     2955   2591   2667     36   -112   -134  A    C  
ATOM   1455  CG  TYR A 200     -14.918  12.697  27.826  1.00 24.31      A    C  
ANISOU 1455  CG  TYR A 200     3309   2911   3017     20   -141   -131  A    C  
ATOM   1456  CD1 TYR A 200     -16.169  13.100  27.338  1.00 26.27      A    C  
ANISOU 1456  CD1 TYR A 200     3560   3155   3267     41   -132   -136  A    C  
ATOM   1457  CD2 TYR A 200     -13.811  13.441  27.471  1.00 24.39      A    C  
ANISOU 1457  CD2 TYR A 200     3329   2903   3034    -15   -179   -119  A    C  
ATOM   1458  CE1 TYR A 200     -16.292  14.184  26.508  1.00 23.38      A    C  
ANISOU 1458  CE1 TYR A 200     3208   2767   2908     27   -161   -133  A    C  
ATOM   1459  CE2 TYR A 200     -13.911  14.566  26.680  1.00 25.24      A    C  
ANISOU 1459  CE2 TYR A 200     3452   2990   3149    -31   -208   -114  A    C  
ATOM   1460  CZ  TYR A 200     -15.165  14.946  26.199  1.00 22.87      A    C  
ANISOU 1460  CZ  TYR A 200     3156   2683   2848     -8   -200   -121  A    C  
ATOM   1461  OH  TYR A 200     -15.331  16.093  25.430  1.00 25.35      A    O  
ANISOU 1461  OH  TYR A 200     3488   2972   3169    -22   -233   -116  A    O  
ATOM   1462  N   ASN A 201     -16.464   9.398  30.585  1.00 20.57      A    N  
ANISOU 1462  N   ASN A 201     2802   2502   2512    103    -33   -142  A    N  
ATOM   1463  CA  ASN A 201     -16.286   8.196  31.411  1.00 26.65      A    C  
ANISOU 1463  CA  ASN A 201     3559   3292   3275    110     -9   -137  A    C  
ATOM   1464  C   ASN A 201     -15.628   7.105  30.601  1.00 17.44      A    C  
ANISOU 1464  C   ASN A 201     2356   2141   2132     77      0   -124  A    C  
ATOM   1465  O   ASN A 201     -15.288   7.276  29.418  1.00 16.32      A    O  
ANISOU 1465  O   ASN A 201     2198   1997   2006     50     -9   -119  A    O  
ATOM   1466  CB  ASN A 201     -17.545   7.740  32.166  1.00 27.42      A    C  
ANISOU 1466  CB  ASN A 201     3652   3406   3360    147     25   -137  A    C  
ATOM   1467  CG  ASN A 201     -18.649   7.181  31.268  1.00 29.28      A    C  
ANISOU 1467  CG  ASN A 201     3850   3657   3618    147     52   -126  A    C  
ATOM   1468  ND2 ASN A 201     -19.881   7.342  31.740  1.00 29.84      A    N  
ANISOU 1468  ND2 ASN A 201     3921   3737   3680    181     75   -126  A    N  
ATOM   1469  OD1 ASN A 201     -18.415   6.581  30.208  1.00 31.74      A    O  
ANISOU 1469  OD1 ASN A 201     4133   3974   3952    118     54   -117  A    O  
ATOM   1470  N   GLN A 202     -15.391   5.977  31.237  1.00 16.51      A    N  
ANISOU 1470  N   GLN A 202     2225   2037   2011     79     16   -118  A    N  
ATOM   1471  CA  GLN A 202     -14.654   4.904  30.613  1.00 14.94      A    C  
ANISOU 1471  CA  GLN A 202     1995   1850   1831     53     23   -108  A    C  
ATOM   1472  C   GLN A 202     -15.451   4.348  29.423  1.00 14.55      A    C  
ANISOU 1472  C   GLN A 202     1914   1811   1802     46     41   -103  A    C  
ATOM   1473  O   GLN A 202     -14.888   3.683  28.546  1.00 14.68      A    O  
ANISOU 1473  O   GLN A 202     1908   1837   1835     25     42    -98  A    O  
ATOM   1474  CB  GLN A 202     -14.358   3.769  31.611  1.00 16.82      A    C  
ANISOU 1474  CB  GLN A 202     2228   2099   2063     61     34   -103  A    C  
ATOM   1475  CG  GLN A 202     -13.620   4.291  32.821  1.00 21.31      A    C  
ANISOU 1475  CG  GLN A 202     2831   2655   2609     70     13   -110  A    C  
ATOM   1476  CD  GLN A 202     -13.295   3.194  33.807  1.00 19.46      A    C  
ANISOU 1476  CD  GLN A 202     2596   2430   2368     76     21   -103  A    C  
ATOM   1477  NE2 GLN A 202     -12.082   3.239  34.347  1.00 24.20      A    N  
ANISOU 1477  NE2 GLN A 202     3209   3021   2964     66     -4   -105  A    N  
ATOM   1478  OE1 GLN A 202     -14.106   2.300  34.020  1.00 21.31      A    O  
ANISOU 1478  OE1 GLN A 202     2816   2678   2605     88     49    -94  A    O  
ATOM   1479  N   THR A 203     -16.774   4.553  29.402  1.00 14.70      A    N  
ANISOU 1479  N   THR A 203     1933   1833   1821     66     57   -102  A    N  
ATOM   1480  CA  THR A 203     -17.528   3.993  28.293  1.00 15.53      A    C  
ANISOU 1480  CA  THR A 203     2009   1946   1948     58     70    -95  A    C  
ATOM   1481  C   THR A 203     -17.351   4.791  26.983  1.00 11.15      A    C  
ANISOU 1481  C   THR A 203     1455   1383   1401     40     53    -99  A    C  
ATOM   1482  O   THR A 203     -17.888   4.332  25.968  1.00 13.44      A    O  
ANISOU 1482  O   THR A 203     1723   1677   1706     33     59    -95  A    O  
ATOM   1483  CB  THR A 203     -19.030   3.827  28.541  1.00 17.75      A    C  
ANISOU 1483  CB  THR A 203     2280   2233   2232     82     91    -90  A    C  
ATOM   1484  CG2 THR A 203     -19.302   3.022  29.807  1.00 18.21      A    C  
ANISOU 1484  CG2 THR A 203     2335   2304   2281    100    112    -81  A    C  
ATOM   1485  OG1 THR A 203     -19.635   5.105  28.590  1.00 17.13      A    O  
ANISOU 1485  OG1 THR A 203     2220   2144   2144    100     84    -98  A    O  
ATOM   1486  N   VAL A 204     -16.467   5.811  26.975  1.00 13.40      A    N  
ANISOU 1486  N   VAL A 204     1760   1655   1675     29     28   -105  A    N  
ATOM   1487  CA  VAL A 204     -16.003   6.272  25.622  1.00 13.49      A    C  
ANISOU 1487  CA  VAL A 204     1766   1664   1695      3     14   -101  A    C  
ATOM   1488  C   VAL A 204     -15.328   5.120  24.856  1.00 10.98      A    C  
ANISOU 1488  C   VAL A 204     1420   1363   1389    -16     24    -96  A    C  
ATOM   1489  O   VAL A 204     -15.437   4.989  23.629  1.00 12.28      A    O  
ANISOU 1489  O   VAL A 204     1572   1534   1560    -28     26    -93  A    O  
ATOM   1490  CB  VAL A 204     -15.082   7.510  25.637  1.00 13.36      A    C  
ANISOU 1490  CB  VAL A 204     1772   1633   1672    -12    -16   -101  A    C  
ATOM   1491  CG1 VAL A 204     -15.776   8.697  26.278  1.00 13.54      A    C  
ANISOU 1491  CG1 VAL A 204     1827   1633   1684      9    -31   -110  A    C  
ATOM   1492  CG2 VAL A 204     -13.733   7.192  26.282  1.00 13.64      A    C  
ANISOU 1492  CG2 VAL A 204     1808   1671   1704    -25    -25    -98  A    C  
ATOM   1493  N   ASP A 205     -14.668   4.206  25.599  1.00 10.42      A    N  
ANISOU 1493  N   ASP A 205     1342   1300   1317    -13     31    -95  A    N  
ATOM   1494  CA  ASP A 205     -14.045   3.082  24.953  1.00 11.38      A    C  
ANISOU 1494  CA  ASP A 205     1440   1437   1448    -25     40    -92  A    C  
ATOM   1495  C   ASP A 205     -15.044   2.026  24.461  1.00 10.04      A    C  
ANISOU 1495  C   ASP A 205     1253   1273   1290    -16     56    -93  A    C  
ATOM   1496  O   ASP A 205     -14.830   1.350  23.462  1.00 10.70      A    O  
ANISOU 1496  O   ASP A 205     1321   1364   1381    -24     58    -94  A    O  
ATOM   1497  CB  ASP A 205     -13.050   2.411  25.923  1.00 11.20      A    C  
ANISOU 1497  CB  ASP A 205     1414   1419   1423    -25     39    -92  A    C  
ATOM   1498  CG  ASP A 205     -11.769   3.216  26.128  1.00 12.29      A    C  
ANISOU 1498  CG  ASP A 205     1559   1554   1555    -40     18    -90  A    C  
ATOM   1499  OD1 ASP A 205     -11.420   4.066  25.281  1.00 11.83      A    O  
ANISOU 1499  OD1 ASP A 205     1501   1496   1498    -57      7    -85  A    O  
ATOM   1500  OD2 ASP A 205     -11.124   2.947  27.143  1.00 12.85      A    O1-
ANISOU 1500  OD2 ASP A 205     1636   1624   1624    -37     12    -90  A    O1-
ATOM   1501  N   ILE A 206     -16.155   1.911  25.205  1.00 10.90      A    N  
ANISOU 1501  N   ILE A 206     1365   1377   1401      1     65    -90  A    N  
ATOM   1502  CA  ILE A 206     -17.229   0.995  24.806  1.00 12.27      A    C  
ANISOU 1502  CA  ILE A 206     1521   1553   1590      7     76    -86  A    C  
ATOM   1503  C   ILE A 206     -17.894   1.464  23.517  1.00 11.13      A    C  
ANISOU 1503  C   ILE A 206     1373   1404   1452      2     71    -87  A    C  
ATOM   1504  O   ILE A 206     -18.226   0.676  22.673  1.00 11.53      A    O  
ANISOU 1504  O   ILE A 206     1410   1456   1515     -3     70    -87  A    O  
ATOM   1505  CB  ILE A 206     -18.235   0.824  25.951  1.00 10.68      A    C  
ANISOU 1505  CB  ILE A 206     1319   1350   1389     27     91    -78  A    C  
ATOM   1506  CG1 ILE A 206     -17.630   0.114  27.160  1.00 13.86      A    C  
ANISOU 1506  CG1 ILE A 206     1725   1759   1784     31     97    -74  A    C  
ATOM   1507  CG2 ILE A 206     -19.486   0.039  25.488  1.00 13.76      A    C  
ANISOU 1507  CG2 ILE A 206     1688   1742   1800     29     99    -68  A    C  
ATOM   1508  CD1 ILE A 206     -17.178  -1.306  26.909  1.00 16.76      A    C  
ANISOU 1508  CD1 ILE A 206     2075   2128   2165     22     96    -71  A    C  
ATOM   1509  N   TRP A 207     -18.096   2.761  23.380  1.00 10.90      A    N  
ANISOU 1509  N   TRP A 207     1360   1368   1415      2     62    -90  A    N  
ATOM   1510  CA  TRP A 207     -18.564   3.304  22.099  1.00 10.76      A    C  
ANISOU 1510  CA  TRP A 207     1341   1345   1400     -6     52    -91  A    C  
ATOM   1511  C   TRP A 207     -17.690   2.820  20.971  1.00 11.05      A    C  
ANISOU 1511  C   TRP A 207     1372   1391   1436    -24     48    -92  A    C  
ATOM   1512  O   TRP A 207     -18.160   2.326  19.966  1.00 10.79      A    O  
ANISOU 1512  O   TRP A 207     1331   1359   1410    -26     45    -93  A    O  
ATOM   1513  CB  TRP A 207     -18.560   4.825  22.131  1.00 11.01      A    C  
ANISOU 1513  CB  TRP A 207     1395   1365   1422     -6     38    -92  A    C  
ATOM   1514  CG  TRP A 207     -19.005   5.414  20.815  1.00 10.71      A    C  
ANISOU 1514  CG  TRP A 207     1361   1322   1388    -15     26    -91  A    C  
ATOM   1515  CD1 TRP A 207     -18.266   5.673  19.736  1.00 12.22      A    C  
ANISOU 1515  CD1 TRP A 207     1554   1517   1572    -35     16    -88  A    C  
ATOM   1516  CD2 TRP A 207     -20.365   5.699  20.449  1.00 10.35      A    C  
ANISOU 1516  CD2 TRP A 207     1311   1267   1353     -3     23    -90  A    C  
ATOM   1517  CE2 TRP A 207     -20.356   6.127  19.123  1.00 11.15      A    C  
ANISOU 1517  CE2 TRP A 207     1418   1365   1453    -18      8    -89  A    C  
ATOM   1518  CE3 TRP A 207     -21.596   5.627  21.130  1.00 10.77      A    C  
ANISOU 1518  CE3 TRP A 207     1356   1318   1417     21     32    -89  A    C  
ATOM   1519  NE1 TRP A 207     -19.055   6.105  18.687  1.00 11.38      A    N  
ANISOU 1519  NE1 TRP A 207     1452   1404   1470    -38      5    -87  A    N  
ATOM   1520  CZ2 TRP A 207     -21.519   6.495  18.450  1.00 12.70      A    C  
ANISOU 1520  CZ2 TRP A 207     1613   1550   1660    -12     -2    -87  A    C  
ATOM   1521  CZ3 TRP A 207     -22.729   6.008  20.470  1.00 11.32      A    C  
ANISOU 1521  CZ3 TRP A 207     1421   1380   1501     27     25    -86  A    C  
ATOM   1522  CH2 TRP A 207     -22.685   6.426  19.140  1.00 12.59      A    C  
ANISOU 1522  CH2 TRP A 207     1590   1534   1661     11      5    -86  A    C  
ATOM   1523  N   SER A 208     -16.354   2.974  21.112  1.00  9.99      A    N  
ANISOU 1523  N   SER A 208     1241   1264   1291    -34     45    -93  A    N  
ATOM   1524  CA  SER A 208     -15.458   2.517  20.073  1.00 10.25      A    C  
ANISOU 1524  CA  SER A 208     1264   1311   1320    -47     45    -94  A    C  
ATOM   1525  C   SER A 208     -15.591   1.043  19.777  1.00  9.54      A    C  
ANISOU 1525  C   SER A 208     1160   1227   1238    -40     53    -99  A    C  
ATOM   1526  O   SER A 208     -15.578   0.629  18.624  1.00 10.91      A    O  
ANISOU 1526  O   SER A 208     1330   1407   1409    -42     52   -103  A    O  
ATOM   1527  CB  SER A 208     -14.001   2.849  20.477  1.00 11.76      A    C  
ANISOU 1527  CB  SER A 208     1455   1512   1502    -59     43    -89  A    C  
ATOM   1528  OG  SER A 208     -13.867   4.229  20.825  1.00 11.78      A    O  
ANISOU 1528  OG  SER A 208     1475   1503   1499    -68     29    -84  A    O  
ATOM   1529  N   VAL A 209     -15.753   0.246  20.831  1.00 10.89      A    N  
ANISOU 1529  N   VAL A 209     1325   1395   1418    -29     59    -99  A    N  
ATOM   1530  CA  VAL A 209     -15.964  -1.199  20.627  1.00 12.08      A    C  
ANISOU 1530  CA  VAL A 209     1464   1545   1581    -22     61   -103  A    C  
ATOM   1531  C   VAL A 209     -17.202  -1.477  19.814  1.00 11.50      A    C  
ANISOU 1531  C   VAL A 209     1388   1461   1519    -20     55   -103  A    C  
ATOM   1532  O   VAL A 209     -17.185  -2.334  18.937  1.00 12.04      A    O  
ANISOU 1532  O   VAL A 209     1453   1530   1590    -19     49   -110  A    O  
ATOM   1533  CB  VAL A 209     -16.007  -1.997  21.957  1.00 12.41      A    C  
ANISOU 1533  CB  VAL A 209     1501   1584   1632    -14     68    -98  A    C  
ATOM   1534  CG1 VAL A 209     -16.279  -3.474  21.663  1.00 13.71      A    C  
ANISOU 1534  CG1 VAL A 209     1655   1743   1811    -10     64   -100  A    C  
ATOM   1535  CG2 VAL A 209     -14.700  -1.876  22.662  1.00 14.70      A    C  
ANISOU 1535  CG2 VAL A 209     1793   1882   1911    -16     69   -100  A    C  
ATOM   1536  N   GLY A 210     -18.296  -0.759  20.104  1.00 10.58      A    N  
ANISOU 1536  N   GLY A 210     1274   1336   1408    -17     55    -95  A    N  
ATOM   1537  CA  GLY A 210     -19.519  -0.907  19.348  1.00 12.38      A    C  
ANISOU 1537  CA  GLY A 210     1497   1554   1651    -16     46    -93  A    C  
ATOM   1538  C   GLY A 210     -19.299  -0.615  17.870  1.00  9.82      A    C  
ANISOU 1538  C   GLY A 210     1183   1232   1317    -23     35   -101  A    C  
ATOM   1539  O   GLY A 210     -19.771  -1.372  16.988  1.00 11.33      A    O  
ANISOU 1539  O   GLY A 210     1372   1417   1516    -23     22   -105  A    O  
ATOM   1540  N   CYS A 211     -18.594   0.444  17.598  1.00  9.88      A    N  
ANISOU 1540  N   CYS A 211     1202   1247   1305    -31     35   -102  A    N  
ATOM   1541  CA  CYS A 211     -18.241   0.787  16.190  1.00 10.30      A    C  
ANISOU 1541  CA  CYS A 211     1265   1307   1343    -40     27   -106  A    C  
ATOM   1542  C   CYS A 211     -17.442  -0.304  15.501  1.00  9.57      A    C  
ANISOU 1542  C   CYS A 211     1169   1227   1242    -37     29   -115  A    C  
ATOM   1543  O   CYS A 211     -17.640  -0.648  14.322  1.00 12.06      A    O  
ANISOU 1543  O   CYS A 211     1491   1542   1549    -35     21   -122  A    O  
ATOM   1544  CB  CYS A 211     -17.460   2.097  16.164  1.00 10.94      A    C  
ANISOU 1544  CB  CYS A 211     1356   1395   1407    -51     28    -99  A    C  
ATOM   1545  SG  CYS A 211     -18.492   3.545  16.628  1.00 12.48      A    S  
ANISOU 1545  SG  CYS A 211     1563   1571   1609    -50     18    -92  A    S  
ATOM   1546  N   ILE A 212     -16.480  -0.827  16.248  1.00  9.36      A    N  
ANISOU 1546  N   ILE A 212     1133   1210   1214    -33     41   -117  A    N  
ATOM   1547  CA  ILE A 212     -15.615  -1.894  15.723  1.00 10.75      A    C  
ANISOU 1547  CA  ILE A 212     1305   1398   1382    -25     43   -129  A    C  
ATOM   1548  C   ILE A 212     -16.426  -3.170  15.478  1.00 11.61      A    C  
ANISOU 1548  C   ILE A 212     1415   1491   1507    -14     31   -137  A    C  
ATOM   1549  O   ILE A 212     -16.314  -3.782  14.405  1.00 12.48      A    O  
ANISOU 1549  O   ILE A 212     1532   1603   1607     -5     23   -149  A    O  
ATOM   1550  CB  ILE A 212     -14.463  -2.142  16.678  1.00 10.70      A    C  
ANISOU 1550  CB  ILE A 212     1287   1403   1374    -24     55   -128  A    C  
ATOM   1551  CG1 ILE A 212     -13.553  -0.918  16.718  1.00 12.43      A    C  
ANISOU 1551  CG1 ILE A 212     1507   1638   1580    -38     61   -117  A    C  
ATOM   1552  CG2 ILE A 212     -13.656  -3.398  16.296  1.00 13.83      A    C  
ANISOU 1552  CG2 ILE A 212     1678   1810   1768    -10     57   -141  A    C  
ATOM   1553  CD1 ILE A 212     -12.556  -0.899  17.863  1.00 14.79      A    C  
ANISOU 1553  CD1 ILE A 212     1796   1943   1882    -40     67   -112  A    C  
ATOM   1554  N   MET A 213     -17.257  -3.561  16.440  1.00  9.75      A    N  
ANISOU 1554  N   MET A 213     1172   1239   1295    -13     27   -131  A    N  
ATOM   1555  CA  MET A 213     -18.070  -4.729  16.295  1.00 11.60      A    C  
ANISOU 1555  CA  MET A 213     1404   1455   1549     -8     12   -132  A    C  
ATOM   1556  C   MET A 213     -18.982  -4.657  15.087  1.00 11.18      A    C  
ANISOU 1556  C   MET A 213     1360   1390   1498     -8     -7   -137  A    C  
ATOM   1557  O   MET A 213     -19.088  -5.624  14.299  1.00 12.05      A    O  
ANISOU 1557  O   MET A 213     1479   1491   1610     -1    -26   -149  A    O  
ATOM   1558  CB  MET A 213     -18.850  -4.994  17.579  1.00 12.02      A    C  
ANISOU 1558  CB  MET A 213     1443   1496   1626     -9     14   -117  A    C  
ATOM   1559  CG  MET A 213     -19.840  -6.143  17.502  1.00 13.45      A    C  
ANISOU 1559  CG  MET A 213     1618   1657   1835     -9     -6   -112  A    C  
ATOM   1560  SD  MET A 213     -20.521  -6.509  19.086  1.00 13.58      A    S  
ANISOU 1560  SD  MET A 213     1616   1667   1875    -12      5    -89  A    S  
ATOM   1561  CE  MET A 213     -21.888  -7.574  18.586  1.00 14.22      A    C  
ANISOU 1561  CE  MET A 213     1688   1724   1993    -18    -25    -77  A    C  
ATOM   1562  N   ALA A 214     -19.645  -3.505  14.912  1.00 10.52      A    N  
ANISOU 1562  N   ALA A 214     1278   1306   1412    -17     -7   -128  A    N  
ATOM   1563  CA  ALA A 214     -20.467  -3.297  13.733  1.00 11.07      A    C  
ANISOU 1563  CA  ALA A 214     1360   1365   1482    -18    -27   -130  A    C  
ATOM   1564  C   ALA A 214     -19.699  -3.528  12.441  1.00 11.55      A    C  
ANISOU 1564  C   ALA A 214     1438   1435   1514    -12    -33   -146  A    C  
ATOM   1565  O   ALA A 214     -20.179  -4.225  11.547  1.00 12.68      A    O  
ANISOU 1565  O   ALA A 214     1594   1566   1660     -6    -55   -156  A    O  
ATOM   1566  CB  ALA A 214     -21.059  -1.918  13.779  1.00 12.28      A    C  
ANISOU 1566  CB  ALA A 214     1513   1518   1634    -25    -25   -119  A    C  
ATOM   1567  N   GLU A 215     -18.510  -2.967  12.340  1.00 11.31      A    N  
ANISOU 1567  N   GLU A 215     1411   1430   1458    -14    -14   -148  A    N  
ATOM   1568  CA  GLU A 215     -17.674  -3.096  11.196  1.00 14.51      A    C  
ANISOU 1568  CA  GLU A 215     1830   1852   1832     -6    -10   -160  A    C  
ATOM   1569  C   GLU A 215     -17.206  -4.530  10.955  1.00 14.42      A    C  
ANISOU 1569  C   GLU A 215     1822   1840   1818     13    -17   -178  A    C  
ATOM   1570  O   GLU A 215     -17.161  -4.962   9.795  1.00 14.32      A    O  
ANISOU 1570  O   GLU A 215     1827   1829   1785     26    -28   -193  A    O  
ATOM   1571  CB  GLU A 215     -16.463  -2.208  11.430  1.00 15.74      A    C  
ANISOU 1571  CB  GLU A 215     1979   2036   1968    -14     13   -152  A    C  
ATOM   1572  CG  GLU A 215     -15.566  -2.137  10.228  1.00 17.51      A    C  
ANISOU 1572  CG  GLU A 215     2212   2285   2155     -8     23   -157  A    C  
ATOM   1573  CD  GLU A 215     -14.526  -1.021  10.383  1.00 18.65      A    C  
ANISOU 1573  CD  GLU A 215     2346   2455   2283    -23     44   -139  A    C  
ATOM   1574  OE1 GLU A 215     -14.767  -0.053  11.117  1.00 16.19      A    O  
ANISOU 1574  OE1 GLU A 215     2031   2135   1985    -40     42   -125  A    O  
ATOM   1575  OE2 GLU A 215     -13.472  -1.105   9.660  1.00 24.01      A    O1-
ANISOU 1575  OE2 GLU A 215     3023   3165   2935    -17     59   -141  A    O1-
ATOM   1576  N   LEU A 216     -16.927  -5.274  12.004  1.00 12.85      A    N  
ANISOU 1576  N   LEU A 216     1609   1637   1639     18    -12   -179  A    N  
ATOM   1577  CA  LEU A 216     -16.584  -6.710  11.818  1.00 13.81      A    C  
ANISOU 1577  CA  LEU A 216     1735   1750   1761     37    -24   -198  A    C  
ATOM   1578  C   LEU A 216     -17.750  -7.474  11.253  1.00 14.30      A    C  
ANISOU 1578  C   LEU A 216     1811   1781   1841     41    -58   -204  A    C  
ATOM   1579  O   LEU A 216     -17.567  -8.376  10.396  1.00 14.99      A    O  
ANISOU 1579  O   LEU A 216     1918   1862   1915     60    -76   -225  A    O  
ATOM   1580  CB  LEU A 216     -16.101  -7.344  13.109  1.00 14.54      A    C  
ANISOU 1580  CB  LEU A 216     1811   1841   1873     38    -16   -194  A    C  
ATOM   1581  CG  LEU A 216     -14.921  -6.700  13.835  1.00 17.53      A    C  
ANISOU 1581  CG  LEU A 216     2174   2246   2241     34     12   -187  A    C  
ATOM   1582  CD1 LEU A 216     -14.554  -7.537  15.024  1.00 19.19      A    C  
ANISOU 1582  CD1 LEU A 216     2372   2447   2470     39     13   -185  A    C  
ATOM   1583  CD2 LEU A 216     -13.774  -6.529  12.903  1.00 21.56      A    C  
ANISOU 1583  CD2 LEU A 216     2686   2785   2719     46     26   -197  A    C  
ATOM   1584  N   LEU A 217     -18.948  -7.163  11.710  1.00 12.86      A    N  
ANISOU 1584  N   LEU A 217     1621   1579   1687     24    -69   -188  A    N  
ATOM   1585  CA  LEU A 217     -20.113  -7.854  11.247  1.00 15.25      A    C  
ANISOU 1585  CA  LEU A 217     1931   1850   2011     23   -106   -189  A    C  
ATOM   1586  C   LEU A 217     -20.522  -7.532   9.789  1.00 18.94      A    C  
ANISOU 1586  C   LEU A 217     2423   2314   2459     27   -126   -200  A    C  
ATOM   1587  O   LEU A 217     -21.010  -8.400   9.070  1.00 18.85      A    O  
ANISOU 1587  O   LEU A 217     2429   2279   2452     36   -160   -212  A    O  
ATOM   1588  CB  LEU A 217     -21.269  -7.584  12.163  1.00 15.13      A    C  
ANISOU 1588  CB  LEU A 217     1894   1821   2033      6   -109   -164  A    C  
ATOM   1589  CG  LEU A 217     -21.181  -8.252  13.530  1.00 17.25      A    C  
ANISOU 1589  CG  LEU A 217     2142   2085   2326      2    -99   -151  A    C  
ATOM   1590  CD1 LEU A 217     -22.189  -7.589  14.460  1.00 19.72      A    C  
ANISOU 1590  CD1 LEU A 217     2432   2396   2664    -12    -89   -125  A    C  
ATOM   1591  CD2 LEU A 217     -21.452  -9.751  13.413  1.00 22.14      A    C  
ANISOU 1591  CD2 LEU A 217     2767   2676   2968      7   -132   -157  A    C  
ATOM   1592  N   THR A 218     -20.387  -6.280   9.394  1.00 14.73      A    N  
ANISOU 1592  N   THR A 218     1894   1800   1904     21   -109   -194  A    N  
ATOM   1593  CA  THR A 218     -20.897  -5.781   8.098  1.00 15.85      A    C  
ANISOU 1593  CA  THR A 218     2058   1938   2026     20   -128   -198  A    C  
ATOM   1594  C   THR A 218     -19.826  -5.642   7.061  1.00 18.07      A    C  
ANISOU 1594  C   THR A 218     2362   2246   2259     36   -115   -213  A    C  
ATOM   1595  O   THR A 218     -20.137  -5.551   5.858  1.00 20.99      A    O  
ANISOU 1595  O   THR A 218     2759   2612   2606     41   -135   -223  A    O  
ATOM   1596  CB  THR A 218     -21.517  -4.371   8.265  1.00 18.67      A    C  
ANISOU 1596  CB  THR A 218     2407   2298   2389      2   -120   -178  A    C  
ATOM   1597  CG2 THR A 218     -22.635  -4.363   9.208  1.00 18.59      A    C  
ANISOU 1597  CG2 THR A 218     2373   2267   2422     -9   -129   -161  A    C  
ATOM   1598  OG1 THR A 218     -20.533  -3.462   8.691  1.00 16.85      A    O  
ANISOU 1598  OG1 THR A 218     2169   2096   2139     -3    -86   -171  A    O  
ATOM   1599  N   GLY A 219     -18.591  -5.619   7.489  1.00 16.32      A    N  
ANISOU 1599  N   GLY A 219     2129   2051   2019     42    -83   -216  A    N  
ATOM   1600  CA  GLY A 219     -17.453  -5.343   6.627  1.00 20.55      A    C  
ANISOU 1600  CA  GLY A 219     2677   2622   2509     55    -61   -224  A    C  
ATOM   1601  C   GLY A 219     -17.262  -3.879   6.269  1.00 21.09      A    C  
ANISOU 1601  C   GLY A 219     2746   2712   2557     37    -43   -205  A    C  
ATOM   1602  O   GLY A 219     -16.305  -3.539   5.550  1.00 28.53      A    O  
ANISOU 1602  O   GLY A 219     3693   3687   3461     43    -23   -205  A    O  
ATOM   1603  N   ARG A 220     -18.083  -2.990   6.831  1.00 18.56      A    N  
ANISOU 1603  N   ARG A 220     2415   2376   2262     14    -49   -186  A    N  
ATOM   1604  CA  ARG A 220     -17.953  -1.562   6.499  1.00 20.34      A    C  
ANISOU 1604  CA  ARG A 220     2643   2616   2470     -3    -39   -167  A    C  
ATOM   1605  C   ARG A 220     -17.945  -0.685   7.719  1.00 19.58      A    C  
ANISOU 1605  C   ARG A 220     2525   2517   2397    -21    -26   -150  A    C  
ATOM   1606  O   ARG A 220     -18.522  -1.022   8.765  1.00 17.83      A    O  
ANISOU 1606  O   ARG A 220     2289   2277   2210    -22    -31   -149  A    O  
ATOM   1607  CB  ARG A 220     -19.050  -1.114   5.604  1.00 24.00      A    C  
ANISOU 1607  CB  ARG A 220     3128   3059   2930     -9    -67   -165  A    C  
ATOM   1608  CG  ARG A 220     -20.428  -1.282   6.125  1.00 28.69      A    C  
ANISOU 1608  CG  ARG A 220     3715   3619   3567    -14    -94   -163  A    C  
ATOM   1609  CD  ARG A 220     -21.446  -1.243   4.971  1.00 55.56      A    C  
ANISOU 1609  CD  ARG A 220     7143   7001   6966    -12   -128   -166  A    C  
ATOM   1610  NE  ARG A 220     -21.894   0.124   4.770  1.00 53.99      A    N  
ANISOU 1610  NE  ARG A 220     6948   6800   6765    -28   -132   -148  A    N  
ATOM   1611  CZ  ARG A 220     -23.048   0.501   4.218  1.00 56.30      A    C  
ANISOU 1611  CZ  ARG A 220     7251   7069   7070    -33   -164   -144  A    C  
ATOM   1612  NH1 ARG A 220     -23.927  -0.385   3.774  1.00 67.51      A    N1+
ANISOU 1612  NH1 ARG A 220     8679   8465   8507    -25   -198   -155  A    N1+
ATOM   1613  NH2 ARG A 220     -23.326   1.796   4.139  1.00 63.05      A    N  
ANISOU 1613  NH2 ARG A 220     8109   7923   7924    -46   -166   -127  A    N  
ATOM   1614  N   THR A 221     -17.252   0.430   7.604  1.00 18.37      A    N  
ANISOU 1614  N   THR A 221     2371   2384   2225    -36    -10   -134  A    N  
ATOM   1615  CA  THR A 221     -17.219   1.400   8.673  1.00 16.16      A    C  
ANISOU 1615  CA  THR A 221     2078   2099   1964    -53     -4   -118  A    C  
ATOM   1616  C   THR A 221     -18.663   1.814   9.027  1.00 15.61      A    C  
ANISOU 1616  C   THR A 221     2010   1997   1922    -56    -26   -114  A    C  
ATOM   1617  O   THR A 221     -19.469   2.168   8.162  1.00 16.10      A    O  
ANISOU 1617  O   THR A 221     2088   2047   1981    -59    -46   -113  A    O  
ATOM   1618  CB  THR A 221     -16.487   2.642   8.236  1.00 15.37      A    C  
ANISOU 1618  CB  THR A 221     1981   2017   1840    -71      4    -98  A    C  
ATOM   1619  CG2 THR A 221     -16.187   3.509   9.402  1.00 17.78      A    C  
ANISOU 1619  CG2 THR A 221     2275   2318   2163    -85     10    -85  A    C  
ATOM   1620  OG1 THR A 221     -15.236   2.300   7.619  1.00 21.00      A    O  
ANISOU 1620  OG1 THR A 221     2691   2765   2523    -67     25    -98  A    O  
ATOM   1621  N   LEU A 222     -18.990   1.828  10.317  1.00 13.28      A    N  
ANISOU 1621  N   LEU A 222     1700   1691   1656    -56    -22   -112  A    N  
ATOM   1622  CA  LEU A 222     -20.339   2.242  10.722  1.00 11.95      A    C  
ANISOU 1622  CA  LEU A 222     1530   1497   1514    -56    -38   -107  A    C  
ATOM   1623  C   LEU A 222     -20.616   3.727  10.510  1.00 12.50      A    C  
ANISOU 1623  C   LEU A 222     1610   1559   1578    -66    -46    -95  A    C  
ATOM   1624  O   LEU A 222     -21.677   4.071   9.950  1.00 13.27      A    O  
ANISOU 1624  O   LEU A 222     1717   1641   1684    -66    -67    -93  A    O  
ATOM   1625  CB  LEU A 222     -20.598   1.874  12.203  1.00 12.34      A    C  
ANISOU 1625  CB  LEU A 222     1560   1541   1589    -48    -27   -106  A    C  
ATOM   1626  CG  LEU A 222     -21.969   2.159  12.807  1.00 12.86      A    C  
ANISOU 1626  CG  LEU A 222     1616   1587   1684    -43    -36   -100  A    C  
ATOM   1627  CD1 LEU A 222     -23.014   1.466  11.967  1.00 14.30      A    C  
ANISOU 1627  CD1 LEU A 222     1797   1754   1881    -40    -58   -102  A    C  
ATOM   1628  CD2 LEU A 222     -22.003   1.779  14.250  1.00 11.43      A    C  
ANISOU 1628  CD2 LEU A 222     1417   1407   1520    -35    -20    -97  A    C  
ATOM   1629  N   PHE A 223     -19.682   4.585  10.935  1.00 11.96      A    N  
ANISOU 1629  N   PHE A 223     1545   1503   1498    -77    -36    -86  A    N  
ATOM   1630  CA  PHE A 223     -19.852   6.026  10.859  1.00 13.48      A    C  
ANISOU 1630  CA  PHE A 223     1751   1685   1687    -88    -49    -74  A    C  
ATOM   1631  C   PHE A 223     -18.646   6.667  10.122  1.00 12.66      A    C  
ANISOU 1631  C   PHE A 223     1657   1600   1554   -108    -43    -61  A    C  
ATOM   1632  O   PHE A 223     -17.763   7.234  10.754  1.00 14.47      A    O  
ANISOU 1632  O   PHE A 223     1881   1836   1779   -119    -37    -51  A    O  
ATOM   1633  CB  PHE A 223     -19.954   6.598  12.255  1.00 12.13      A    C  
ANISOU 1633  CB  PHE A 223     1574   1503   1532    -84    -45    -72  A    C  
ATOM   1634  CG  PHE A 223     -21.077   6.083  13.105  1.00 12.11      A    C  
ANISOU 1634  CG  PHE A 223     1558   1488   1556    -65    -44    -80  A    C  
ATOM   1635  CD1 PHE A 223     -22.382   6.252  12.728  1.00 13.19      A    C  
ANISOU 1635  CD1 PHE A 223     1696   1608   1710    -56    -59    -79  A    C  
ATOM   1636  CD2 PHE A 223     -20.805   5.508  14.320  1.00 13.23      A    C  
ANISOU 1636  CD2 PHE A 223     1684   1633   1706    -56    -26    -84  A    C  
ATOM   1637  CE1 PHE A 223     -23.405   5.831  13.533  1.00 12.08      A    C  
ANISOU 1637  CE1 PHE A 223     1537   1458   1594    -40    -56    -81  A    C  
ATOM   1638  CE2 PHE A 223     -21.830   5.087  15.140  1.00 13.35      A    C  
ANISOU 1638  CE2 PHE A 223     1687   1641   1745    -39    -22    -85  A    C  
ATOM   1639  CZ  PHE A 223     -23.130   5.283  14.763  1.00 12.92      A    C  
ANISOU 1639  CZ  PHE A 223     1630   1574   1708    -31    -35    -82  A    C  
ATOM   1640  N   PRO A 224     -18.552   6.484   8.787  1.00 14.17      A    N  
ANISOU 1640  N   PRO A 224     1859   1802   1722   -112    -47    -58  A    N  
ATOM   1641  CA  PRO A 224     -17.374   7.029   8.049  1.00 16.47      A    C  
ANISOU 1641  CA  PRO A 224     2156   2119   1983   -130    -39    -42  A    C  
ATOM   1642  C   PRO A 224     -17.581   8.524   7.691  1.00 15.53      A    C  
ANISOU 1642  C   PRO A 224     2055   1986   1859   -150    -59    -20  A    C  
ATOM   1643  O   PRO A 224     -17.876   8.914   6.552  1.00 17.90      A    O  
ANISOU 1643  O   PRO A 224     2373   2286   2141   -157    -72    -12  A    O  
ATOM   1644  CB  PRO A 224     -17.366   6.171   6.785  1.00 17.75      A    C  
ANISOU 1644  CB  PRO A 224     2326   2298   2119   -120    -35    -49  A    C  
ATOM   1645  CG  PRO A 224     -18.788   5.828   6.533  1.00 19.50      A    C  
ANISOU 1645  CG  PRO A 224     2559   2492   2358   -107    -58    -63  A    C  
ATOM   1646  CD  PRO A 224     -19.436   5.684   7.928  1.00 17.06      A    C  
ANISOU 1646  CD  PRO A 224     2232   2161   2086    -98    -59    -70  A    C  
ATOM   1647  N   GLY A 225     -17.533   9.352   8.697  1.00 14.13      A    N  
ANISOU 1647  N   GLY A 225     1877   1792   1701   -157    -67    -14  A    N  
ATOM   1648  CA  GLY A 225     -17.735  10.789   8.444  1.00 13.86      A    C  
ANISOU 1648  CA  GLY A 225     1862   1738   1665   -175    -92      4  A    C  
ATOM   1649  C   GLY A 225     -16.640  11.395   7.575  1.00 14.05      A    C  
ANISOU 1649  C   GLY A 225     1892   1785   1663   -203    -90     31  A    C  
ATOM   1650  O   GLY A 225     -15.467  10.990   7.652  1.00 16.09      A    O  
ANISOU 1650  O   GLY A 225     2132   2074   1910   -212    -67     39  A    O  
ATOM   1651  N   THR A 226     -17.024  12.369   6.756  1.00 14.53      A    N  
ANISOU 1651  N   THR A 226     1974   1832   1714   -218   -114     49  A    N  
ATOM   1652  CA  THR A 226     -16.084  13.077   5.888  1.00 13.45      A    C  
ANISOU 1652  CA  THR A 226     1844   1715   1552   -248   -114     81  A    C  
ATOM   1653  C   THR A 226     -15.261  14.117   6.662  1.00 16.31      A    C  
ANISOU 1653  C   THR A 226     2203   2067   1926   -274   -126    103  A    C  
ATOM   1654  O   THR A 226     -14.207  14.563   6.178  1.00 22.40      A    O  
ANISOU 1654  O   THR A 226     2968   2861   2681   -303   -121    134  A    O  
ATOM   1655  CB  THR A 226     -16.806  13.828   4.808  1.00 14.90      A    C  
ANISOU 1655  CB  THR A 226     2056   1883   1722   -257   -141     94  A    C  
ATOM   1656  CG2 THR A 226     -17.547  12.855   3.917  1.00 19.30      A    C  
ANISOU 1656  CG2 THR A 226     2620   2450   2265   -235   -134     75  A    C  
ATOM   1657  OG1 THR A 226     -17.732  14.768   5.397  1.00 18.69      A    O  
ANISOU 1657  OG1 THR A 226     2553   2318   2230   -254   -176     90  A    O  
ATOM   1658  N   ASP A 227     -15.805  14.585   7.766  1.00 13.10      A    N  
ANISOU 1658  N   ASP A 227     1803   1625   1548   -265   -146     89  A    N  
ATOM   1659  CA  ASP A 227     -15.237  15.699   8.554  1.00 16.45      A    C  
ANISOU 1659  CA  ASP A 227     2236   2028   1987   -286   -170    106  A    C  
ATOM   1660  C   ASP A 227     -15.885  15.681   9.933  1.00 14.50      A    C  
ANISOU 1660  C   ASP A 227     1991   1752   1765   -259   -180     77  A    C  
ATOM   1661  O   ASP A 227     -16.692  14.785  10.192  1.00 14.10      A    O  
ANISOU 1661  O   ASP A 227     1933   1704   1721   -229   -163     51  A    O  
ATOM   1662  CB  ASP A 227     -15.383  17.052   7.827  1.00 16.57      A    C  
ANISOU 1662  CB  ASP A 227     2278   2021   1997   -313   -207    134  A    C  
ATOM   1663  CG  ASP A 227     -16.840  17.494   7.593  1.00 16.67      A    C  
ANISOU 1663  CG  ASP A 227     2318   1999   2019   -293   -234    118  A    C  
ATOM   1664  OD1 ASP A 227     -17.734  17.006   8.269  1.00 16.42      A    O  
ANISOU 1664  OD1 ASP A 227     2282   1953   2004   -259   -230     87  A    O  
ATOM   1665  OD2 ASP A 227     -17.082  18.402   6.720  1.00 18.60      A    O1-
ANISOU 1665  OD2 ASP A 227     2585   2227   2256   -311   -262    141  A    O1-
ATOM   1666  N   HIS A 228     -15.570  16.631  10.788  1.00 14.10      A    N  
ANISOU 1666  N   HIS A 228     1954   1675   1729   -269   -206     84  A    N  
ATOM   1667  CA  HIS A 228     -16.076  16.639  12.124  1.00 14.33      A    C  
ANISOU 1667  CA  HIS A 228     1989   1680   1776   -241   -212     57  A    C  
ATOM   1668  C   HIS A 228     -17.608  16.727  12.186  1.00 12.41      A    C  
ANISOU 1668  C   HIS A 228     1761   1414   1543   -208   -221     34  A    C  
ATOM   1669  O   HIS A 228     -18.237  15.986  12.903  1.00 13.02      A    O  
ANISOU 1669  O   HIS A 228     1826   1493   1628   -177   -203      9  A    O  
ATOM   1670  CB  HIS A 228     -15.458  17.815  12.892  1.00 14.77      A    C  
ANISOU 1670  CB  HIS A 228     2064   1707   1841   -259   -247     69  A    C  
ATOM   1671  CG  HIS A 228     -15.629  17.707  14.353  1.00 17.62      A    C  
ANISOU 1671  CG  HIS A 228     2431   2051   2214   -231   -249     43  A    C  
ATOM   1672  CD2 HIS A 228     -14.906  17.039  15.259  1.00 19.59      A    C  
ANISOU 1672  CD2 HIS A 228     2662   2315   2464   -227   -231     35  A    C  
ATOM   1673  ND1 HIS A 228     -16.625  18.359  15.045  1.00 30.32      A    N  
ANISOU 1673  ND1 HIS A 228     4066   3624   3832   -202   -272     21  A    N  
ATOM   1674  CE1 HIS A 228     -16.535  18.053  16.319  1.00 25.66      A    C  
ANISOU 1674  CE1 HIS A 228     3475   3031   3246   -179   -265      2  A    C  
ATOM   1675  NE2 HIS A 228     -15.500  17.265  16.483  1.00 22.42      A    N  
ANISOU 1675  NE2 HIS A 228     3041   2649   2832   -196   -241     10  A    N  
ATOM   1676  N   ILE A 229     -18.188  17.701  11.462  1.00 13.44      A    N  
ANISOU 1676  N   ILE A 229     1915   1520   1674   -215   -252     45  A    N  
ATOM   1677  CA  ILE A 229     -19.653  17.900  11.515  1.00 15.63      A    C  
ANISOU 1677  CA  ILE A 229     2203   1772   1963   -183   -266     25  A    C  
ATOM   1678  C   ILE A 229     -20.329  16.668  10.962  1.00 12.79      A    C  
ANISOU 1678  C   ILE A 229     1821   1436   1601   -167   -237     13  A    C  
ATOM   1679  O   ILE A 229     -21.323  16.201  11.526  1.00 14.17      A    O  
ANISOU 1679  O   ILE A 229     1986   1607   1792   -134   -228     -8  A    O  
ATOM   1680  CB  ILE A 229     -20.072  19.142  10.739  1.00 19.95      A    C  
ANISOU 1680  CB  ILE A 229     2781   2289   2511   -196   -307     41  A    C  
ATOM   1681  CG1 ILE A 229     -19.595  20.394  11.469  1.00 25.26      A    C  
ANISOU 1681  CG1 ILE A 229     3480   2927   3191   -205   -344     47  A    C  
ATOM   1682  CG2 ILE A 229     -21.606  19.172  10.604  1.00 22.25      A    C  
ANISOU 1682  CG2 ILE A 229     3076   2562   2815   -160   -317     21  A    C  
ATOM   1683  CD1 ILE A 229     -19.616  21.635  10.599  1.00 29.62      A    C  
ANISOU 1683  CD1 ILE A 229     4063   3452   3742   -231   -389     72  A    C  
ATOM   1684  N   ASP A 230     -19.777  16.126   9.875  1.00 14.08      A    N  
ANISOU 1684  N   ASP A 230     1976   1627   1747   -188   -222     28  A    N  
ATOM   1685  CA  ASP A 230     -20.428  14.962   9.218  1.00 15.01      A    C  
ANISOU 1685  CA  ASP A 230     2078   1765   1861   -173   -202     16  A    C  
ATOM   1686  C   ASP A 230     -20.401  13.721  10.135  1.00 13.72      A    C  
ANISOU 1686  C   ASP A 230     1889   1618   1707   -152   -171     -5  A    C  
ATOM   1687  O   ASP A 230     -21.376  12.948  10.209  1.00 14.28      A    O  
ANISOU 1687  O   ASP A 230     1947   1688   1791   -128   -164    -21  A    O  
ATOM   1688  CB  ASP A 230     -19.728  14.638   7.900  1.00 17.57      A    C  
ANISOU 1688  CB  ASP A 230     2403   2116   2157   -197   -194     34  A    C  
ATOM   1689  CG  ASP A 230     -20.503  13.647   7.034  1.00 15.00      A    C  
ANISOU 1689  CG  ASP A 230     2073   1801   1826   -181   -186     22  A    C  
ATOM   1690  OD1 ASP A 230     -21.718  13.884   6.802  1.00 16.16      A    O  
ANISOU 1690  OD1 ASP A 230     2230   1924   1987   -168   -208     14  A    O  
ATOM   1691  OD2 ASP A 230     -19.923  12.637   6.685  1.00 17.25      A    O1-
ANISOU 1691  OD2 ASP A 230     2345   2115   2095   -181   -160     19  A    O1-
ATOM   1692  N   GLN A 231     -19.332  13.561  10.855  1.00 12.97      A    N  
ANISOU 1692  N   GLN A 231     1783   1537   1607   -161   -155     -2  A    N  
ATOM   1693  CA  GLN A 231     -19.190  12.464  11.836  1.00 12.88      A    C  
ANISOU 1693  CA  GLN A 231     1749   1539   1605   -143   -128    -19  A    C  
ATOM   1694  C   GLN A 231     -20.334  12.487  12.833  1.00 12.33      A    C  
ANISOU 1694  C   GLN A 231     1680   1450   1557   -113   -131    -37  A    C  
ATOM   1695  O   GLN A 231     -20.974  11.477  13.075  1.00 13.11      A    O  
ANISOU 1695  O   GLN A 231     1760   1556   1666    -94   -114    -49  A    O  
ATOM   1696  CB  GLN A 231     -17.839  12.558  12.528  1.00 14.86      A    C  
ANISOU 1696  CB  GLN A 231     1994   1802   1850   -158   -119    -12  A    C  
ATOM   1697  CG  GLN A 231     -17.494  11.371  13.399  1.00 12.95      A    C  
ANISOU 1697  CG  GLN A 231     1730   1577   1614   -144    -91    -26  A    C  
ATOM   1698  CD  GLN A 231     -17.299  10.132  12.555  1.00 14.80      A    C  
ANISOU 1698  CD  GLN A 231     1947   1840   1838   -143    -69    -28  A    C  
ATOM   1699  NE2 GLN A 231     -17.764   8.992  13.054  1.00 13.86      A    N  
ANISOU 1699  NE2 GLN A 231     1812   1725   1728   -122    -53    -45  A    N  
ATOM   1700  OE1 GLN A 231     -16.813  10.234  11.445  1.00 15.64      A    O  
ANISOU 1700  OE1 GLN A 231     2056   1961   1927   -160    -68    -15  A    O  
ATOM   1701  N   LEU A 232     -20.577  13.668  13.400  1.00 13.12      A    N  
ANISOU 1701  N   LEU A 232     1799   1523   1663   -107   -154    -36  A    N  
ATOM   1702  CA  LEU A 232     -21.692  13.799  14.343  1.00 12.52      A    C  
ANISOU 1702  CA  LEU A 232     1723   1431   1605    -74   -155    -53  A    C  
ATOM   1703  C   LEU A 232     -23.044  13.586  13.697  1.00 14.14      A    C  
ANISOU 1703  C   LEU A 232     1921   1629   1823    -57   -160    -57  A    C  
ATOM   1704  O   LEU A 232     -23.912  12.956  14.260  1.00 14.53      A    O  
ANISOU 1704  O   LEU A 232     1950   1682   1887    -31   -145    -67  A    O  
ATOM   1705  CB  LEU A 232     -21.671  15.157  15.094  1.00 13.25      A    C  
ANISOU 1705  CB  LEU A 232     1843   1494   1699    -66   -182    -55  A    C  
ATOM   1706  CG  LEU A 232     -20.659  15.106  16.190  1.00 16.64      A    C  
ANISOU 1706  CG  LEU A 232     2274   1927   2120    -68   -174    -58  A    C  
ATOM   1707  CD1 LEU A 232     -20.226  16.508  16.601  1.00 20.67      A    C  
ANISOU 1707  CD1 LEU A 232     2819   2408   2629    -75   -211    -55  A    C  
ATOM   1708  CD2 LEU A 232     -21.159  14.309  17.386  1.00 20.40      A    C  
ANISOU 1708  CD2 LEU A 232     2736   2413   2602    -36   -148    -76  A    C  
ATOM   1709  N   LYS A 233     -23.223  14.107  12.497  1.00 13.93      A    N  
ANISOU 1709  N   LYS A 233     1906   1593   1791    -73   -183    -46  A    N  
ATOM   1710  CA  LYS A 233     -24.492  13.913  11.807  1.00 14.03      A    C  
ANISOU 1710  CA  LYS A 233     1914   1600   1819    -59   -192    -48  A    C  
ATOM   1711  C   LYS A 233     -24.752  12.439  11.561  1.00 15.38      A    C  
ANISOU 1711  C   LYS A 233     2058   1792   1994    -55   -169    -54  A    C  
ATOM   1712  O   LYS A 233     -25.883  11.970  11.783  1.00 15.72      A    O  
ANISOU 1712  O   LYS A 233     2082   1831   2061    -33   -167    -60  A    O  
ATOM   1713  CB  LYS A 233     -24.517  14.705  10.504  1.00 20.36      A    C  
ANISOU 1713  CB  LYS A 233     2740   2388   2610    -80   -222    -34  A    C  
ATOM   1714  CG  LYS A 233     -24.799  16.190  10.770  1.00 28.92      A    C  
ANISOU 1714  CG  LYS A 233     3849   3440   3699    -73   -256    -31  A    C  
ATOM   1715  CD  LYS A 233     -24.826  17.036   9.495  1.00 36.03      A    C  
ANISOU 1715  CD  LYS A 233     4776   4325   4590    -96   -289    -14  A    C  
ATOM   1716  CE  LYS A 233     -25.626  16.345   8.400  1.00 59.67      A    C  
ANISOU 1716  CE  LYS A 233     7760   7326   7585    -94   -292    -13  A    C  
ATOM   1717  NZ  LYS A 233     -24.838  15.296   7.681  1.00 45.59      A    N1+
ANISOU 1717  NZ  LYS A 233     5968   5573   5780   -115   -268     -7  A    N1+
ATOM   1718  N   LEU A 234     -23.729  11.687  11.153  1.00 12.74      A    N  
ANISOU 1718  N   LEU A 234     1720   1480   1642    -75   -154    -50  A    N  
ATOM   1719  CA  LEU A 234     -23.927  10.245  10.937  1.00 12.17      A    C  
ANISOU 1719  CA  LEU A 234     1626   1423   1575    -69   -135    -57  A    C  
ATOM   1720  C   LEU A 234     -24.269   9.512  12.230  1.00 13.10      A    C  
ANISOU 1720  C   LEU A 234     1720   1547   1712    -49   -115    -66  A    C  
ATOM   1721  O   LEU A 234     -25.144   8.639  12.275  1.00 13.87      A    O  
ANISOU 1721  O   LEU A 234     1797   1644   1828    -37   -110    -70  A    O  
ATOM   1722  CB  LEU A 234     -22.682   9.605  10.303  1.00 12.78      A    C  
ANISOU 1722  CB  LEU A 234     1704   1524   1625    -88   -122    -54  A    C  
ATOM   1723  CG  LEU A 234     -22.341  10.129   8.911  1.00 15.29      A    C  
ANISOU 1723  CG  LEU A 234     2044   1846   1919   -108   -137    -42  A    C  
ATOM   1724  CD1 LEU A 234     -21.098   9.441   8.484  1.00 17.85      A    C  
ANISOU 1724  CD1 LEU A 234     2365   2199   2217   -120   -116    -39  A    C  
ATOM   1725  CD2 LEU A 234     -23.474   9.903   7.942  1.00 17.87      A    C  
ANISOU 1725  CD2 LEU A 234     2376   2159   2252   -101   -159    -45  A    C  
ATOM   1726  N   ILE A 235     -23.567   9.865  13.296  1.00 11.01      A    N  
ANISOU 1726  N   ILE A 235     1457   1284   1442    -46   -102    -68  A    N  
ATOM   1727  CA  ILE A 235     -23.856   9.268  14.595  1.00 12.89      A    C  
ANISOU 1727  CA  ILE A 235     1676   1527   1693    -27    -81    -75  A    C  
ATOM   1728  C   ILE A 235     -25.314   9.514  14.996  1.00 12.64      A    C  
ANISOU 1728  C   ILE A 235     1634   1484   1685      0    -85    -76  A    C  
ATOM   1729  O   ILE A 235     -26.011   8.574  15.391  1.00 13.02      A    O  
ANISOU 1729  O   ILE A 235     1657   1540   1752     11    -71    -76  A    O  
ATOM   1730  CB  ILE A 235     -22.870   9.786  15.684  1.00 11.37      A    C  
ANISOU 1730  CB  ILE A 235     1495   1338   1488    -27    -73    -78  A    C  
ATOM   1731  CG1 ILE A 235     -21.477   9.250  15.398  1.00 11.48      A    C  
ANISOU 1731  CG1 ILE A 235     1508   1369   1486    -50    -63    -74  A    C  
ATOM   1732  CG2 ILE A 235     -23.397   9.361  17.073  1.00 13.84      A    C  
ANISOU 1732  CG2 ILE A 235     1794   1654   1813     -1    -53    -84  A    C  
ATOM   1733  CD1 ILE A 235     -20.406   9.874  16.227  1.00 13.83      A    C  
ANISOU 1733  CD1 ILE A 235     1817   1665   1771    -57    -63    -72  A    C  
ATOM   1734  N   LEU A 236     -25.742  10.764  14.939  1.00 12.61      A    N  
ANISOU 1734  N   LEU A 236     1648   1462   1683      7   -106    -77  A    N  
ATOM   1735  CA  LEU A 236     -27.066  11.115  15.461  1.00 14.11      A    C  
ANISOU 1735  CA  LEU A 236     1826   1642   1893     38   -108    -80  A    C  
ATOM   1736  C   LEU A 236     -28.203  10.570  14.616  1.00 14.95      A    C  
ANISOU 1736  C   LEU A 236     1912   1747   2023     40   -117    -74  A    C  
ATOM   1737  O   LEU A 236     -29.296  10.362  15.149  1.00 16.35      A    O  
ANISOU 1737  O   LEU A 236     2063   1926   2223     65   -109    -71  A    O  
ATOM   1738  CB  LEU A 236     -27.194  12.628  15.639  1.00 17.72      A    C  
ANISOU 1738  CB  LEU A 236     2311   2078   2345     50   -130    -84  A    C  
ATOM   1739  CG  LEU A 236     -26.216  13.170  16.645  1.00 17.57      A    C  
ANISOU 1739  CG  LEU A 236     2312   2056   2307     53   -125    -91  A    C  
ATOM   1740  CD1 LEU A 236     -26.193  14.700  16.662  1.00 23.18      A    C  
ANISOU 1740  CD1 LEU A 236     3058   2738   3011     59   -157    -94  A    C  
ATOM   1741  CD2 LEU A 236     -26.490  12.608  18.023  1.00 24.56      A    C  
ANISOU 1741  CD2 LEU A 236     3181   2955   3195     81    -95    -97  A    C  
ATOM   1742  N   ARG A 237     -27.928  10.250  13.360  1.00 15.52      A    N  
ANISOU 1742  N   ARG A 237     1990   1817   2087     16   -133    -69  A    N  
ATOM   1743  CA  ARG A 237     -28.916   9.604  12.535  1.00 17.59      A    C  
ANISOU 1743  CA  ARG A 237     2236   2075   2371     15   -146    -64  A    C  
ATOM   1744  C   ARG A 237     -29.210   8.199  12.987  1.00 17.30      A    C  
ANISOU 1744  C   ARG A 237     2167   2053   2352     19   -126    -62  A    C  
ATOM   1745  O   ARG A 237     -30.334   7.722  12.812  1.00 18.46      A    O  
ANISOU 1745  O   ARG A 237     2289   2196   2528     26   -135    -55  A    O  
ATOM   1746  CB  ARG A 237     -28.492   9.613  11.080  1.00 19.54      A    C  
ANISOU 1746  CB  ARG A 237     2505   2317   2601     -8   -169    -62  A    C  
ATOM   1747  CG  ARG A 237     -28.938  10.896  10.420  1.00 34.95      A    C  
ANISOU 1747  CG  ARG A 237     4479   4248   4551     -8   -200    -58  A    C  
ATOM   1748  CD  ARG A 237     -28.528  10.989   8.967  1.00 34.27      A    C  
ANISOU 1748  CD  ARG A 237     4419   4160   4443    -31   -222    -53  A    C  
ATOM   1749  NE  ARG A 237     -29.261  10.117   8.049  1.00 30.50      A    N  
ANISOU 1749  NE  ARG A 237     3933   3680   3977    -34   -238    -52  A    N  
ATOM   1750  CZ  ARG A 237     -28.892   9.933   6.770  1.00 32.01      A    C  
ANISOU 1750  CZ  ARG A 237     4147   3871   4144    -51   -255    -50  A    C  
ATOM   1751  NH1 ARG A 237     -27.791  10.552   6.307  1.00 34.61      A    N1+
ANISOU 1751  NH1 ARG A 237     4505   4209   4438    -69   -252    -45  A    N1+
ATOM   1752  NH2 ARG A 237     -29.585   9.134   5.960  1.00 24.87      A    N  
ANISOU 1752  NH2 ARG A 237     3239   2961   3250    -51   -274    -52  A    N  
ATOM   1753  N   LEU A 238     -28.250   7.518  13.565  1.00 16.11      A    N  
ANISOU 1753  N   LEU A 238     2015   1918   2188     12   -103    -65  A    N  
ATOM   1754  CA  LEU A 238     -28.475   6.192  14.088  1.00 13.97      A    C  
ANISOU 1754  CA  LEU A 238     1718   1658   1933     14    -87    -62  A    C  
ATOM   1755  C   LEU A 238     -29.040   6.266  15.487  1.00 14.83      A    C  
ANISOU 1755  C   LEU A 238     1804   1774   2057     37    -63    -57  A    C  
ATOM   1756  O   LEU A 238     -30.015   5.567  15.799  1.00 17.53      A    O  
ANISOU 1756  O   LEU A 238     2115   2120   2427     45    -58    -46  A    O  
ATOM   1757  CB  LEU A 238     -27.170   5.348  14.078  1.00 14.08      A    C  
ANISOU 1757  CB  LEU A 238     1740   1684   1926     -1    -73    -68  A    C  
ATOM   1758  CG  LEU A 238     -27.387   3.911  14.547  1.00 16.42      A    C  
ANISOU 1758  CG  LEU A 238     2011   1988   2240     -1    -61    -64  A    C  
ATOM   1759  CD1 LEU A 238     -28.244   3.100  13.575  1.00 21.59      A    C  
ANISOU 1759  CD1 LEU A 238     2655   2631   2918     -8    -86    -60  A    C  
ATOM   1760  CD2 LEU A 238     -26.084   3.145  14.769  1.00 19.38      A    C  
ANISOU 1760  CD2 LEU A 238     2393   2375   2596    -10    -47    -72  A    C  
ATOM   1761  N   VAL A 239     -28.426   7.049  16.378  1.00 14.49      A    N  
ANISOU 1761  N   VAL A 239     1776   1735   1994     48    -49    -64  A    N  
ATOM   1762  CA  VAL A 239     -28.717   6.950  17.810  1.00 14.00      A    C  
ANISOU 1762  CA  VAL A 239     1699   1686   1936     71    -21    -61  A    C  
ATOM   1763  C   VAL A 239     -29.742   7.951  18.278  1.00 16.77      A    C  
ANISOU 1763  C   VAL A 239     2045   2032   2297    101    -22    -60  A    C  
ATOM   1764  O   VAL A 239     -30.171   7.893  19.444  1.00 20.26      A    O  
ANISOU 1764  O   VAL A 239     2471   2486   2739    127      3    -56  A    O  
ATOM   1765  CB  VAL A 239     -27.448   6.989  18.686  1.00 14.76      A    C  
ANISOU 1765  CB  VAL A 239     1815   1790   2005     68     -5    -69  A    C  
ATOM   1766  CG1 VAL A 239     -26.462   5.920  18.209  1.00 16.88      A    C  
ANISOU 1766  CG1 VAL A 239     2082   2065   2267     41     -4    -70  A    C  
ATOM   1767  CG2 VAL A 239     -26.818   8.373  18.687  1.00 17.81      A    C  
ANISOU 1767  CG2 VAL A 239     2235   2163   2370     70    -20    -80  A    C  
ATOM   1768  N   GLY A 240     -30.088   8.868  17.389  1.00 15.63      A    N  
ANISOU 1768  N   GLY A 240     1915   1869   2155    101    -49    -63  A    N  
ATOM   1769  CA  GLY A 240     -31.096   9.904  17.664  1.00 16.10      A    C  
ANISOU 1769  CA  GLY A 240     1972   1921   2224    133    -56    -65  A    C  
ATOM   1770  C   GLY A 240     -30.529  11.135  18.330  1.00 19.76      A    C  
ANISOU 1770  C   GLY A 240     2471   2374   2663    149    -59    -80  A    C  
ATOM   1771  O   GLY A 240     -29.489  11.114  18.928  1.00 20.03      A    O  
ANISOU 1771  O   GLY A 240     2524   2413   2675    142    -48    -86  A    O  
ATOM   1772  N   THR A 241     -31.323  12.196  18.209  1.00 25.69      A    N  
ANISOU 1772  N   THR A 241     3228   3110   3423    174    -76    -84  A    N  
ATOM   1773  CA  THR A 241     -31.263  13.429  19.012  1.00 32.13      A    C  
ANISOU 1773  CA  THR A 241     4073   3913   4221    206    -81    -99  A    C  
ATOM   1774  C   THR A 241     -31.361  13.107  20.525  1.00 17.80      A    C  
ANISOU 1774  C   THR A 241     2247   2121   2395    238    -44   -103  A    C  
ATOM   1775  O   THR A 241     -32.004  12.157  20.928  1.00 21.84      A    O  
ANISOU 1775  O   THR A 241     2719   2657   2923    247    -15    -90  A    O  
ATOM   1776  CB  THR A 241     -32.445  14.382  18.514  1.00 23.43      A    C  
ANISOU 1776  CB  THR A 241     2970   2794   3140    233   -106   -100  A    C  
ATOM   1777  CG2 THR A 241     -33.880  13.842  18.921  1.00 39.64      A    C  
ANISOU 1777  CG2 THR A 241     4971   4869   5223    265    -81    -89  A    C  
ATOM   1778  OG1 THR A 241     -32.307  15.696  19.066  1.00 34.26      A    O  
ANISOU 1778  OG1 THR A 241     4377   4146   4495    262   -122   -117  A    O  
ATOM   1779  N   PRO A 242     -30.643  13.874  21.387  1.00 22.53      A    N  
ANISOU 1779  N   PRO A 242     2883   2711   2966    254    -45   -119  A    N  
ATOM   1780  CA  PRO A 242     -30.806  13.574  22.818  1.00 20.04      A    C  
ANISOU 1780  CA  PRO A 242     2560   2417   2638    289    -10   -123  A    C  
ATOM   1781  C   PRO A 242     -32.248  13.553  23.382  1.00 20.41      A    C  
ANISOU 1781  C   PRO A 242     2573   2484   2700    336     15   -117  A    C  
ATOM   1782  O   PRO A 242     -33.019  14.458  23.110  1.00 24.08      A    O  
ANISOU 1782  O   PRO A 242     3040   2935   3174    364     -2   -124  A    O  
ATOM   1783  CB  PRO A 242     -30.043  14.719  23.481  1.00 23.89      A    C  
ANISOU 1783  CB  PRO A 242     3100   2883   3095    306    -30   -144  A    C  
ATOM   1784  CG  PRO A 242     -28.999  15.081  22.541  1.00 28.17      A    C  
ANISOU 1784  CG  PRO A 242     3670   3401   3634    261    -65   -144  A    C  
ATOM   1785  CD  PRO A 242     -29.608  14.875  21.159  1.00 24.80      A    C  
ANISOU 1785  CD  PRO A 242     3219   2971   3233    238    -79   -131  A    C  
ATOM   1786  N   GLY A 243     -32.539  12.557  24.209  1.00 20.06      A    N  
ANISOU 1786  N   GLY A 243     2495   2471   2655    346     55   -104  A    N  
ATOM   1787  CA  GLY A 243     -33.776  12.447  24.958  1.00 23.48      A    C  
ANISOU 1787  CA  GLY A 243     2892   2932   3098    392     88    -93  A    C  
ATOM   1788  C   GLY A 243     -33.848  13.448  26.088  1.00 26.54      A    C  
ANISOU 1788  C   GLY A 243     3312   3320   3453    447     98   -115  A    C  
ATOM   1789  O   GLY A 243     -32.856  14.121  26.412  1.00 22.27      A    O  
ANISOU 1789  O   GLY A 243     2822   2757   2882    446     77   -138  A    O  
ATOM   1790  N   ALA A 244     -35.017  13.533  26.708  1.00 23.00      A    N  
ANISOU 1790  N   ALA A 244     2832   2897   3010    496    127   -109  A    N  
ATOM   1791  CA  ALA A 244     -35.226  14.454  27.808  1.00 29.50      A    C  
ANISOU 1791  CA  ALA A 244     3684   3724   3801    559    140   -130  A    C  
ATOM   1792  C   ALA A 244     -34.238  14.243  28.922  1.00 22.19      A    C  
ANISOU 1792  C   ALA A 244     2793   2806   2832    562    156   -141  A    C  
ATOM   1793  O   ALA A 244     -33.728  15.244  29.479  1.00 24.03      A    O  
ANISOU 1793  O   ALA A 244     3082   3017   3032    592    135   -170  A    O  
ATOM   1794  CB  ALA A 244     -36.652  14.295  28.367  1.00 32.29      A    C  
ANISOU 1794  CB  ALA A 244     3986   4118   4166    610    182   -114  A    C  
ATOM   1795  N   GLU A 245     -34.014  12.984  29.297  1.00 24.65      A    N  
ANISOU 1795  N   GLU A 245     3076   3145   3145    536    187   -117  A    N  
ATOM   1796  CA  GLU A 245     -33.146  12.670  30.436  1.00 30.90      A    C  
ANISOU 1796  CA  GLU A 245     3898   3947   3897    541    205   -123  A    C  
ATOM   1797  C   GLU A 245     -31.734  13.175  30.173  1.00 24.09      A    C  
ANISOU 1797  C   GLU A 245     3092   3045   3016    509    161   -146  A    C  
ATOM   1798  O   GLU A 245     -31.095  13.758  31.056  1.00 25.02      A    O  
ANISOU 1798  O   GLU A 245     3257   3153   3096    533    153   -168  A    O  
ATOM   1799  CB  GLU A 245     -33.150  11.154  30.756  1.00 31.96      A    C  
ANISOU 1799  CB  GLU A 245     3988   4115   4041    512    241    -90  A    C  
ATOM   1800  CG  GLU A 245     -32.168  10.663  31.817  1.00 37.75      A    C  
ANISOU 1800  CG  GLU A 245     4750   4857   4737    508    255    -92  A    C  
ATOM   1801  CD  GLU A 245     -32.306   9.156  32.101  1.00 35.78      A    C  
ANISOU 1801  CD  GLU A 245     4455   4638   4501    481    290    -57  A    C  
ATOM   1802  OE1 GLU A 245     -32.052   8.314  31.200  1.00 43.75      A    O  
ANISOU 1802  OE1 GLU A 245     5440   5640   5545    429    276    -41  A    O  
ATOM   1803  OE2 GLU A 245     -32.693   8.804  33.237  1.00 44.80      A    O1-
ANISOU 1803  OE2 GLU A 245     5587   5814   5620    512    330    -43  A    O1-
ATOM   1804  N   LEU A 246     -31.232  12.943  28.957  1.00 17.80      A    N  
ANISOU 1804  N   LEU A 246     2290   2228   2247    454    131   -140  A    N  
ATOM   1805  CA  LEU A 246     -29.906  13.410  28.621  1.00 15.91      A    C  
ANISOU 1805  CA  LEU A 246     2097   1955   1995    421     92   -156  A    C  
ATOM   1806  C   LEU A 246     -29.808  14.967  28.513  1.00 18.42      A    C  
ANISOU 1806  C   LEU A 246     2464   2237   2300    446     51   -183  A    C  
ATOM   1807  O   LEU A 246     -28.802  15.580  28.948  1.00 20.06      A    O  
ANISOU 1807  O   LEU A 246     2720   2420   2481    442     24   -201  A    O  
ATOM   1808  CB  LEU A 246     -29.455  12.742  27.301  1.00 16.37      A    C  
ANISOU 1808  CB  LEU A 246     2133   2005   2083    360     76   -141  A    C  
ATOM   1809  CG  LEU A 246     -28.088  13.150  26.800  1.00 14.71      A    C  
ANISOU 1809  CG  LEU A 246     1961   1767   1864    321     38   -152  A    C  
ATOM   1810  CD1 LEU A 246     -27.058  12.904  27.901  1.00 17.64      A    C  
ANISOU 1810  CD1 LEU A 246     2357   2141   2204    320     45   -158  A    C  
ATOM   1811  CD2 LEU A 246     -27.814  12.287  25.589  1.00 15.37      A    C  
ANISOU 1811  CD2 LEU A 246     2016   1854   1974    270     33   -134  A    C  
ATOM   1812  N   LEU A 247     -30.793  15.626  27.912  1.00 19.79      A    N  
ANISOU 1812  N   LEU A 247     2627   2401   2493    468     40   -186  A    N  
ATOM   1813  CA  LEU A 247     -30.760  17.085  27.833  1.00 19.44      A    C  
ANISOU 1813  CA  LEU A 247     2630   2319   2436    493     -2   -211  A    C  
ATOM   1814  C   LEU A 247     -30.659  17.746  29.213  1.00 16.93      A    C  
ANISOU 1814  C   LEU A 247     2355   1999   2079    549      3   -237  A    C  
ATOM   1815  O   LEU A 247     -30.047  18.810  29.366  1.00 21.37      A    O  
ANISOU 1815  O   LEU A 247     2974   2522   2623    557    -41   -259  A    O  
ATOM   1816  CB  LEU A 247     -32.028  17.585  27.126  1.00 25.07      A    C  
ANISOU 1816  CB  LEU A 247     3319   3029   3178    519     -8   -209  A    C  
ATOM   1817  CG  LEU A 247     -32.079  17.325  25.619  1.00 28.60      A    C  
ANISOU 1817  CG  LEU A 247     3741   3464   3660    467    -30   -192  A    C  
ATOM   1818  CD1 LEU A 247     -33.511  17.554  25.110  1.00 32.50      A    C  
ANISOU 1818  CD1 LEU A 247     4200   3966   4185    498    -25   -185  A    C  
ATOM   1819  CD2 LEU A 247     -31.067  18.201  24.889  1.00 31.19      A    C  
ANISOU 1819  CD2 LEU A 247     4117   3748   3983    431    -83   -202  A    C  
ATOM   1820  N   LYS A 248     -31.305  17.151  30.199  1.00 18.55      A    N  
ANISOU 1820  N   LYS A 248     2537   2243   2270    589     51   -232  A    N  
ATOM   1821  CA  LYS A 248     -31.264  17.656  31.575  1.00 21.97      A    C  
ANISOU 1821  CA  LYS A 248     3009   2680   2657    648     62   -255  A    C  
ATOM   1822  C   LYS A 248     -29.868  17.652  32.154  1.00 17.66      A    C  
ANISOU 1822  C   LYS A 248     2512   2115   2082    622     39   -266  A    C  
ATOM   1823  O   LYS A 248     -29.668  18.222  33.214  1.00 21.49      A    O  
ANISOU 1823  O   LYS A 248     3043   2592   2528    666     34   -290  A    O  
ATOM   1824  CB  LYS A 248     -32.100  16.805  32.507  1.00 25.24      A    C  
ANISOU 1824  CB  LYS A 248     3383   3148   3059    686    125   -239  A    C  
ATOM   1825  CG  LYS A 248     -33.579  16.741  32.234  1.00 41.79      A    C  
ANISOU 1825  CG  LYS A 248     5425   5272   5180    721    157   -225  A    C  
ATOM   1826  CD  LYS A 248     -34.226  18.100  32.161  1.00 43.15      A    C  
ANISOU 1826  CD  LYS A 248     5626   5421   5348    777    131   -253  A    C  
ATOM   1827  CE  LYS A 248     -35.612  18.060  32.793  1.00 55.73      A    C  
ANISOU 1827  CE  LYS A 248     7178   7059   6937    846    181   -246  A    C  
ATOM   1828  NZ  LYS A 248     -36.562  17.119  32.138  1.00 57.49      A    N1+
ANISOU 1828  NZ  LYS A 248     7319   7317   7207    823    214   -207  A    N1+
ATOM   1829  N   LYS A 249     -28.937  16.905  31.554  1.00 17.55      A    N  
ANISOU 1829  N   LYS A 249     2485   2097   2086    556     30   -248  A    N  
ATOM   1830  CA  LYS A 249     -27.574  16.833  32.048  1.00 17.26      A    C  
ANISOU 1830  CA  LYS A 249     2486   2044   2028    527      9   -255  A    C  
ATOM   1831  C   LYS A 249     -26.604  17.747  31.355  1.00 18.17      A    C  
ANISOU 1831  C   LYS A 249     2642   2112   2150    491    -53   -266  A    C  
ATOM   1832  O   LYS A 249     -25.417  17.724  31.698  1.00 20.11      A    O  
ANISOU 1832  O   LYS A 249     2915   2342   2382    464    -75   -269  A    O  
ATOM   1833  CB  LYS A 249     -27.037  15.407  31.866  1.00 22.36      A    C  
ANISOU 1833  CB  LYS A 249     3091   2717   2687    478     36   -228  A    C  
ATOM   1834  CG  LYS A 249     -27.879  14.410  32.579  1.00 20.31      A    C  
ANISOU 1834  CG  LYS A 249     2792   2504   2422    505     93   -212  A    C  
ATOM   1835  CD  LYS A 249     -27.364  12.996  32.215  1.00 33.67      A    C  
ANISOU 1835  CD  LYS A 249     4444   4216   4134    451    112   -185  A    C  
ATOM   1836  CE  LYS A 249     -28.260  11.945  32.818  1.00 30.05      A    C  
ANISOU 1836  CE  LYS A 249     3941   3801   3676    471    166   -161  A    C  
ATOM   1837  NZ  LYS A 249     -27.734  10.589  32.507  1.00 24.94      A    N1+
ANISOU 1837  NZ  LYS A 249     3260   3168   3049    420    178   -136  A    N1+
ATOM   1838  N   ILE A 250     -27.085  18.570  30.434  1.00 17.12      A    N  
ANISOU 1838  N   ILE A 250     2512   1955   2039    491    -80   -269  A    N  
ATOM   1839  CA  ILE A 250     -26.231  19.513  29.719  1.00 22.16      A    C  
ANISOU 1839  CA  ILE A 250     3187   2547   2685    455   -140   -275  A    C  
ATOM   1840  C   ILE A 250     -26.215  20.873  30.455  1.00 25.03      A    C  
ANISOU 1840  C   ILE A 250     3616   2871   3023    502   -183   -306  A    C  
ATOM   1841  O   ILE A 250     -27.230  21.529  30.485  1.00 28.16      A    O  
ANISOU 1841  O   ILE A 250     4019   3262   3420    551   -184   -321  A    O  
ATOM   1842  CB  ILE A 250     -26.656  19.549  28.237  1.00 21.27      A    C  
ANISOU 1842  CB  ILE A 250     3042   2429   2610    421   -150   -257  A    C  
ATOM   1843  CG1 ILE A 250     -26.601  18.113  27.621  1.00 24.84      A    C  
ANISOU 1843  CG1 ILE A 250     3437   2920   3082    379   -110   -230  A    C  
ATOM   1844  CG2 ILE A 250     -25.793  20.551  27.475  1.00 26.13      A    C  
ANISOU 1844  CG2 ILE A 250     3696   2999   3233    383   -210   -258  A    C  
ATOM   1845  CD1 ILE A 250     -25.313  17.345  27.878  1.00 39.68      A    C  
ANISOU 1845  CD1 ILE A 250     5317   4807   4954    336   -105   -220  A    C  
ATOM   1846  N   SER A 251     -25.060  21.238  31.055  1.00 27.12      A    N  
ANISOU 1846  N   SER A 251     3927   3109   3269    488   -218   -317  A    N  
ATOM   1847  CA  SER A 251     -24.888  22.470  31.908  1.00 29.57      A    C  
ANISOU 1847  CA  SER A 251     4308   3377   3550    531   -265   -349  A    C  
ATOM   1848  C   SER A 251     -25.000  23.808  31.197  1.00 38.32      A    C  
ANISOU 1848  C   SER A 251     5453   4435   4674    531   -326   -359  A    C  
ATOM   1849  O   SER A 251     -25.239  24.822  31.857  1.00 54.94      A    O  
ANISOU 1849  O   SER A 251     7612   6506   6757    582   -360   -390  A    O  
ATOM   1850  CB  SER A 251     -23.507  22.478  32.590  1.00 40.58      A    C  
ANISOU 1850  CB  SER A 251     5741   4751   4926    503   -298   -352  A    C  
ATOM   1851  OG  SER A 251     -23.132  21.220  33.101  1.00 53.45      A    O  
ANISOU 1851  OG  SER A 251     7339   6423   6547    487   -251   -338  A    O  
ATOM   1852  N   SER A 252     -24.798  23.821  29.869  1.00 36.19      A    N  
ANISOU 1852  N   SER A 252     5156   4156   4440    474   -342   -334  A    N  
ATOM   1853  CA  SER A 252     -24.603  25.039  29.084  1.00 41.67      A    C  
ANISOU 1853  CA  SER A 252     5885   4797   5150    454   -406   -336  A    C  
ATOM   1854  C   SER A 252     -25.739  25.304  28.145  1.00 30.72      A    C  
ANISOU 1854  C   SER A 252     4473   3412   3787    470   -400   -332  A    C  
ATOM   1855  O   SER A 252     -26.083  24.471  27.288  1.00 40.85      A    O  
ANISOU 1855  O   SER A 252     5700   4730   5092    441   -363   -308  A    O  
ATOM   1856  CB  SER A 252     -23.324  24.946  28.229  1.00 48.44      A    C  
ANISOU 1856  CB  SER A 252     6735   5642   6027    371   -436   -306  A    C  
ATOM   1857  OG  SER A 252     -22.175  24.789  29.042  1.00 91.79      A    O  
ANISOU 1857  OG  SER A 252    12250  11125  11502    353   -451   -307  A    O  
ATOM   1858  N   GLU A 253     -26.277  26.513  28.253  1.00 49.17      A    N  
ANISOU 1858  N   GLU A 253     6854   5709   6120    513   -443   -355  A    N  
ATOM   1859  CA  GLU A 253     -27.346  26.965  27.365  1.00 58.25      A    C  
ANISOU 1859  CA  GLU A 253     7989   6852   7294    530   -449   -353  A    C  
ATOM   1860  C   GLU A 253     -26.975  26.850  25.883  1.00 45.29      A    C  
ANISOU 1860  C   GLU A 253     6320   5204   5683    458   -466   -319  A    C  
ATOM   1861  O   GLU A 253     -27.782  26.440  25.087  1.00 39.90      A    O  
ANISOU 1861  O   GLU A 253     5594   4544   5021    454   -440   -306  A    O  
ATOM   1862  CB  GLU A 253     -27.729  28.420  27.674  1.00 83.56      A    C  
ANISOU 1862  CB  GLU A 253    11256  10003  10491    582   -508   -384  A    C  
ATOM   1863  CG  GLU A 253     -28.125  28.687  29.121  1.00 81.38      A    C  
ANISOU 1863  CG  GLU A 253    11016   9729  10177    663   -496   -423  A    C  
ATOM   1864  CD  GLU A 253     -28.630  30.099  29.337  1.00 90.12      A    C  
ANISOU 1864  CD  GLU A 253    12183  10782  11277    721   -555   -456  A    C  
ATOM   1865  OE1 GLU A 253     -28.689  30.863  28.355  1.00 50.97      A    O  
ANISOU 1865  OE1 GLU A 253     7238   5783   6346    696   -604   -447  A    O  
ATOM   1866  OE2 GLU A 253     -28.965  30.448  30.492  1.00 85.72      A    O1-
ANISOU 1866  OE2 GLU A 253    11663  10221  10685    795   -552   -492  A    O1-
ATOM   1867  N   SER A 254     -25.747  27.204  25.516  1.00 60.70      A    N  
ANISOU 1867  N   SER A 254     8297   7127   7640    398   -509   -303  A    N  
ATOM   1868  CA  SER A 254     -25.318  27.127  24.105  1.00 49.99      A    C  
ANISOU 1868  CA  SER A 254     6918   5767   6308    328   -525   -268  A    C  
ATOM   1869  C   SER A 254     -25.214  25.683  23.567  1.00 39.83      A    C  
ANISOU 1869  C   SER A 254     5568   4537   5030    292   -463   -243  A    C  
ATOM   1870  O   SER A 254     -25.585  25.399  22.435  1.00 37.33      A    O  
ANISOU 1870  O   SER A 254     5219   4233   4732    266   -454   -223  A    O  
ATOM   1871  CB  SER A 254     -23.991  27.886  23.913  1.00 41.07      A    C  
ANISOU 1871  CB  SER A 254     5829   4596   5180    274   -585   -253  A    C  
ATOM   1872  OG  SER A 254     -23.097  27.684  24.994  1.00 58.87      A    O  
ANISOU 1872  OG  SER A 254     8104   6850   7416    273   -586   -263  A    O  
ATOM   1873  N   ALA A 255     -24.702  24.759  24.372  1.00 29.17      A    N  
ANISOU 1873  N   ALA A 255     4200   3219   3665    290   -426   -245  A    N  
ATOM   1874  CA  ALA A 255     -24.542  23.395  23.949  1.00 30.72      A    C  
ANISOU 1874  CA  ALA A 255     4342   3464   3868    258   -373   -224  A    C  
ATOM   1875  C   ALA A 255     -25.896  22.715  23.727  1.00 18.92      A    C  
ANISOU 1875  C   ALA A 255     2802   2001   2384    292   -328   -226  A    C  
ATOM   1876  O   ALA A 255     -26.034  21.840  22.867  1.00 29.49      A    O  
ANISOU 1876  O   ALA A 255     4098   3368   3738    262   -300   -205  A    O  
ATOM   1877  CB  ALA A 255     -23.756  22.638  24.993  1.00 28.66      A    C  
ANISOU 1877  CB  ALA A 255     4078   3224   3589    257   -348   -228  A    C  
ATOM   1878  N   ARG A 256     -26.758  23.031  24.704  1.00 39.56      A    N  
ANISOU 1878  N   ARG A 256     5429   4616   4987    358   -317   -251  A    N  
ATOM   1879  CA  ARG A 256     -28.183  22.864  24.640  1.00 37.45      A    C  
ANISOU 1879  CA  ARG A 256     5132   4368   4731    404   -288   -257  A    C  
ATOM   1880  C   ARG A 256     -28.656  23.707  23.474  1.00 38.52      A    C  
ANISOU 1880  C   ARG A 256     5276   4472   4889    394   -329   -250  A    C  
ATOM   1881  O   ARG A 256     -29.076  23.140  22.502  1.00 29.58      A    O  
ANISOU 1881  O   ARG A 256     4104   3358   3777    368   -314   -232  A    O  
ATOM   1882  CB  ARG A 256     -28.873  23.290  25.963  1.00 34.89      A    C  
ANISOU 1882  CB  ARG A 256     4829   4045   4383    481   -276   -286  A    C  
ATOM   1883  CG  ARG A 256     -28.523  22.430  27.173  1.00 30.07      A    C  
ANISOU 1883  CG  ARG A 256     4212   3468   3747    496   -232   -291  A    C  
ATOM   1884  CD  ARG A 256     -29.547  22.522  28.320  1.00 35.60      A    C  
ANISOU 1884  CD  ARG A 256     4911   4189   4426    576   -200   -313  A    C  
ATOM   1885  NE  ARG A 256     -29.831  23.891  28.752  1.00 28.75      A    N  
ANISOU 1885  NE  ARG A 256     4100   3281   3543    629   -242   -343  A    N  
ATOM   1886  CZ  ARG A 256     -29.182  24.576  29.705  1.00 39.18      A    C  
ANISOU 1886  CZ  ARG A 256     5482   4575   4832    654   -272   -369  A    C  
ATOM   1887  NH1 ARG A 256     -28.157  24.069  30.379  1.00 42.43      A    N1+
ANISOU 1887  NH1 ARG A 256     5908   4992   5221    630   -267   -367  A    N1+
ATOM   1888  NH2 ARG A 256     -29.582  25.824  29.999  1.00 49.97      A    N  
ANISOU 1888  NH2 ARG A 256     6898   5902   6186    707   -313   -400  A    N  
ATOM   1889  N   ASN A 257     -28.518  25.052  23.492  1.00 32.51      A    N  
ANISOU 1889  N   ASN A 257     4567   3662   4123    408   -385   -266  A    N  
ATOM   1890  CA  ASN A 257     -28.964  25.756  22.285  1.00 35.52      A    C  
ANISOU 1890  CA  ASN A 257     4953   4016   4527    391   -424   -255  A    C  
ATOM   1891  C   ASN A 257     -28.353  25.166  21.018  1.00 32.10      A    C  
ANISOU 1891  C   ASN A 257     4495   3593   4108    318   -422   -222  A    C  
ATOM   1892  O   ASN A 257     -29.051  25.024  20.043  1.00 29.00      A    O  
ANISOU 1892  O   ASN A 257     4077   3207   3736    311   -422   -209  A    O  
ATOM   1893  CB  ASN A 257     -28.746  27.256  22.362  1.00 34.34      A    C  
ANISOU 1893  CB  ASN A 257     4867   3806   4373    405   -492   -270  A    C  
ATOM   1894  CG  ASN A 257     -29.636  27.916  23.402  1.00 49.88      A    C  
ANISOU 1894  CG  ASN A 257     6861   5761   6329    489   -495   -307  A    C  
ATOM   1895  ND2 ASN A 257     -29.264  29.110  23.835  1.00 53.80      A    N  
ANISOU 1895  ND2 ASN A 257     7420   6206   6814    508   -554   -327  A    N  
ATOM   1896  OD1 ASN A 257     -30.634  27.336  23.829  1.00 54.98      A    O  
ANISOU 1896  OD1 ASN A 257     7470   6446   6976    536   -447   -315  A    O  
ATOM   1897  N   TYR A 258     -27.057  24.784  21.051  1.00 37.38      A    N  
ANISOU 1897  N   TYR A 258     5167   4267   4766    269   -422   -207  A    N  
ATOM   1898  CA  TYR A 258     -26.420  24.070  19.892  1.00 35.73      A    C  
ANISOU 1898  CA  TYR A 258     4929   4079   4566    205   -412   -176  A    C  
ATOM   1899  C   TYR A 258     -27.159  22.820  19.648  1.00 24.82      A    C  
ANISOU 1899  C   TYR A 258     3494   2742   3194    212   -359   -171  A    C  
ATOM   1900  O   TYR A 258     -27.737  22.640  18.547  1.00 39.98      A    O  
ANISOU 1900  O   TYR A 258     5394   4667   5131    197   -361   -157  A    O  
ATOM   1901  CB  TYR A 258     -24.899  23.731  20.105  1.00 35.88      A    C  
ANISOU 1901  CB  TYR A 258     4955   4105   4572    155   -411   -163  A    C  
ATOM   1902  CG  TYR A 258     -24.167  23.103  18.912  1.00 25.84      A    C  
ANISOU 1902  CG  TYR A 258     3657   2854   3306     94   -402   -131  A    C  
ATOM   1903  CD1 TYR A 258     -23.936  23.846  17.753  1.00 38.61      A    C  
ANISOU 1903  CD1 TYR A 258     5290   4449   4930     56   -441   -110  A    C  
ATOM   1904  CD2 TYR A 258     -23.674  21.814  18.932  1.00 36.03      A    C  
ANISOU 1904  CD2 TYR A 258     4911   4187   4592     73   -357   -123  A    C  
ATOM   1905  CE1 TYR A 258     -23.289  23.314  16.652  1.00 23.95      A    C  
ANISOU 1905  CE1 TYR A 258     3413   2614   3073      5   -430    -82  A    C  
ATOM   1906  CE2 TYR A 258     -22.991  21.274  17.839  1.00 33.92      A    C  
ANISOU 1906  CE2 TYR A 258     4623   3939   4326     23   -348    -97  A    C  
ATOM   1907  CZ  TYR A 258     -22.805  22.029  16.685  1.00 43.22      A    C  
ANISOU 1907  CZ  TYR A 258     5816   5097   5507    -10   -383    -76  A    C  
ATOM   1908  OH  TYR A 258     -22.141  21.520  15.568  1.00 35.69      A    O  
ANISOU 1908  OH  TYR A 258     4845   4167   4550    -56   -372    -50  A    O  
ATOM   1909  N   ILE A 259     -27.246  21.936  20.640  1.00 30.77      A    N  
ANISOU 1909  N   ILE A 259     3368   3531   4791    559    -85   -363  A    N  
ATOM   1910  CA  ILE A 259     -27.794  20.589  20.411  1.00 52.72      A    C  
ANISOU 1910  CA  ILE A 259     6115   6367   7552    533    -90   -348  A    C  
ATOM   1911  C   ILE A 259     -29.191  20.661  19.771  1.00 61.01      A    C  
ANISOU 1911  C   ILE A 259     7107   7418   8657    571   -129   -341  A    C  
ATOM   1912  O   ILE A 259     -29.521  19.843  18.911  1.00 47.16      A    O  
ANISOU 1912  O   ILE A 259     5345   5684   6890    554   -164   -308  A    O  
ATOM   1913  CB  ILE A 259     -27.826  19.731  21.699  1.00 59.81      A    C  
ANISOU 1913  CB  ILE A 259     6985   7319   8421    504    -31   -384  A    C  
ATOM   1914  N   GLN A 260     -29.983  21.663  20.174  1.00 73.85      A    N  
ANISOU 1914  N   GLN A 260     8695   9021  10345    620   -124   -373  A    N  
ATOM   1915  CA  GLN A 260     -31.288  21.983  19.536  1.00 80.05      A    C  
ANISOU 1915  CA  GLN A 260     9424   9798  11195    664   -167   -365  A    C  
ATOM   1916  C   GLN A 260     -31.159  22.518  18.084  1.00 79.37      A    C  
ANISOU 1916  C   GLN A 260     9375   9662  11118    680   -240   -314  A    C  
ATOM   1917  O   GLN A 260     -32.097  22.413  17.287  1.00 61.50      A    O  
ANISOU 1917  O   GLN A 260     7076   7401   8889    702   -289   -292  A    O  
ATOM   1918  CB  GLN A 260     -32.059  23.013  20.394  1.00 56.67      A    C  
ANISOU 1918  CB  GLN A 260     6414   6819   8299    717   -140   -416  A    C  
ATOM   1919  CG  GLN A 260     -33.423  23.457  19.844  1.00 55.40      A    C  
ANISOU 1919  CG  GLN A 260     6189   6647   8214    771   -183   -414  A    C  
ATOM   1920  CD  GLN A 260     -33.639  24.966  19.963  1.00 77.11      A    C  
ANISOU 1920  CD  GLN A 260     8939   9332  11027    833   -193   -437  A    C  
ATOM   1921  NE2 GLN A 260     -33.784  25.449  21.194  1.00 43.73      A    N  
ANISOU 1921  NE2 GLN A 260     4686   5108   6819    852   -133   -496  A    N  
ATOM   1922  OE1 GLN A 260     -33.669  25.689  18.957  1.00 65.23      A    O  
ANISOU 1922  OE1 GLN A 260     7459   7774   9550    861   -253   -401  A    O  
ATOM   1923  N   SER A 261     -30.009  23.097  17.747  1.00 86.25      A    N  
ANISOU 1923  N   SER A 261    10321  10490  11960    669   -249   -294  A    N  
ATOM   1924  CA  SER A 261     -29.801  23.646  16.404  1.00 60.69      A    C  
ANISOU 1924  CA  SER A 261     7128   7205   8726    680   -315   -245  A    C  
ATOM   1925  C   SER A 261     -29.533  22.572  15.331  1.00 50.18      A    C  
ANISOU 1925  C   SER A 261     5823   5902   7342    638   -349   -197  A    C  
ATOM   1926  O   SER A 261     -29.615  22.876  14.143  1.00 52.55      A    O  
ANISOU 1926  O   SER A 261     6149   6172   7644    647   -408   -154  A    O  
ATOM   1927  CB  SER A 261     -28.675  24.700  16.401  1.00 61.58      A    C  
ANISOU 1927  CB  SER A 261     7311   7261   8826    679   -310   -239  A    C  
ATOM   1928  OG  SER A 261     -27.401  24.107  16.160  1.00 53.44      A    O  
ANISOU 1928  OG  SER A 261     6338   6242   7723    626   -298   -216  A    O  
ATOM   1929  N   LEU A 262     -29.254  21.325  15.716  1.00 29.71      A    N  
ANISOU 1929  N   LEU A 262     3223   3364   4703    594   -316   -204  A    N  
ATOM   1930  CA  LEU A 262     -29.078  20.259  14.700  1.00 34.27      A    C  
ANISOU 1930  CA  LEU A 262     3822   3966   5233    557   -347   -163  A    C  
ATOM   1931  C   LEU A 262     -30.496  19.732  14.484  1.00 52.64      A    C  
ANISOU 1931  C   LEU A 262     6079   6323   7597    573   -375   -164  A    C  
ATOM   1932  O   LEU A 262     -31.359  19.889  15.361  1.00 52.25      A    O  
ANISOU 1932  O   LEU A 262     5965   6291   7595    598   -349   -202  A    O  
ATOM   1933  CB  LEU A 262     -28.134  19.133  15.168  1.00 26.70      A    C  
ANISOU 1933  CB  LEU A 262     2890   3047   4209    505   -303   -169  A    C  
ATOM   1934  CG  LEU A 262     -27.486  18.133  14.151  1.00 30.75      A    C  
ANISOU 1934  CG  LEU A 262     3449   3575   4661    462   -327   -131  A    C  
ATOM   1935  CD1 LEU A 262     -26.071  17.834  14.614  1.00 32.67      A    C  
ANISOU 1935  CD1 LEU A 262     3741   3823   4850    426   -284   -136  A    C  
ATOM   1936  CD2 LEU A 262     -28.233  16.799  13.865  1.00 39.52      A    C  
ANISOU 1936  CD2 LEU A 262     4525   4733   5759    439   -341   -124  A    C  
ATOM   1937  N   ALA A 263     -30.736  19.123  13.324  1.00 80.50      A    N  
ANISOU 1937  N   ALA A 263     9620   9862  11106    556   -427   -126  A    N  
ATOM   1938  CA  ALA A 263     -32.042  18.545  13.009  1.00 68.41      A    C  
ANISOU 1938  CA  ALA A 263     8024   8363   9608    565   -459   -123  A    C  
ATOM   1939  C   ALA A 263     -32.339  17.371  13.934  1.00 46.10      A    C  
ANISOU 1939  C   ALA A 263     5154   5595   6768    534   -410   -153  A    C  
ATOM   1940  O   ALA A 263     -31.477  16.533  14.199  1.00 36.11      A    O  
ANISOU 1940  O   ALA A 263     3925   4351   5445    491   -377   -153  A    O  
ATOM   1941  CB  ALA A 263     -32.094  18.101  11.555  1.00 68.87      A    C  
ANISOU 1941  CB  ALA A 263     8115   8417   9636    546   -525    -74  A    C  
ATOM   1942  N   GLN A 264     -33.570  17.339  14.437  1.00 57.89      A    N  
ANISOU 1942  N   GLN A 264     6566   7113   8314    557   -405   -177  A    N  
ATOM   1943  CA  GLN A 264     -34.009  16.282  15.335  1.00 62.72      A    C  
ANISOU 1943  CA  GLN A 264     7130   7782   8919    528   -359   -205  A    C  
ATOM   1944  C   GLN A 264     -34.116  14.974  14.558  1.00 52.45      A    C  
ANISOU 1944  C   GLN A 264     5839   6513   7578    482   -390   -176  A    C  
ATOM   1945  O   GLN A 264     -34.829  14.894  13.565  1.00 45.95      A    O  
ANISOU 1945  O   GLN A 264     4998   5688   6774    489   -450   -150  A    O  
ATOM   1946  CB  GLN A 264     -35.358  16.645  15.974  1.00 49.70      A    C  
ANISOU 1946  CB  GLN A 264     5389   6153   7342    565   -348   -238  A    C  
ATOM   1947  N   MET A 265     -33.337  13.980  14.982  1.00 66.53      A    N  
ANISOU 1947  N   MET A 265     7655   8319   9303    435   -351   -180  A    N  
ATOM   1948  CA  MET A 265     -33.425  12.609  14.467  1.00 53.55      A    C  
ANISOU 1948  CA  MET A 265     6020   6706   7621    388   -369   -159  A    C  
ATOM   1949  C   MET A 265     -33.996  11.700  15.571  1.00 31.54      A    C  
ANISOU 1949  C   MET A 265     3177   3969   4837    360   -321   -189  A    C  
ATOM   1950  O   MET A 265     -33.576  11.771  16.693  1.00 27.57      A    O  
ANISOU 1950  O   MET A 265     2674   3475   4325    356   -263   -215  A    O  
ATOM   1951  CB  MET A 265     -32.026  12.080  14.054  1.00 47.92      A    C  
ANISOU 1951  CB  MET A 265     5391   5980   6837    353   -364   -139  A    C  
ATOM   1952  CG  MET A 265     -31.292  12.867  12.957  1.00 41.51      A    C  
ANISOU 1952  CG  MET A 265     4642   5123   6008    368   -404   -109  A    C  
ATOM   1953  SD  MET A 265     -32.265  13.177  11.449  1.00 81.36      A    S  
ANISOU 1953  SD  MET A 265     9678  10155  11082    388   -491    -73  A    S  
ATOM   1954  CE  MET A 265     -32.824  11.527  11.007  1.00 84.25      A    C  
ANISOU 1954  CE  MET A 265    10028  10566  11419    338   -511    -64  A    C  
ATOM   1955  N   PRO A 266     -34.965  10.840  15.235  1.00 40.54      A    N  
ANISOU 1955  N   PRO A 266     4273   5142   5990    339   -346   -182  A    N  
ATOM   1956  CA  PRO A 266     -35.306   9.782  16.177  1.00 32.37      A    C  
ANISOU 1956  CA  PRO A 266     3203   4151   4943    300   -301   -201  A    C  
ATOM   1957  C   PRO A 266     -34.250   8.665  16.085  1.00 25.59      A    C  
ANISOU 1957  C   PRO A 266     2412   3297   4015    251   -288   -186  A    C  
ATOM   1958  O   PRO A 266     -33.616   8.486  15.034  1.00 38.73      A    O  
ANISOU 1958  O   PRO A 266     4135   4935   5644    242   -328   -158  A    O  
ATOM   1959  CB  PRO A 266     -36.678   9.300  15.673  1.00 42.11      A    C  
ANISOU 1959  CB  PRO A 266     4369   5414   6216    293   -341   -194  A    C  
ATOM   1960  CG  PRO A 266     -36.710   9.661  14.218  1.00 40.65      A    C  
ANISOU 1960  CG  PRO A 266     4213   5198   6033    311   -416   -160  A    C  
ATOM   1961  CD  PRO A 266     -35.619  10.650  13.927  1.00 44.36      A    C  
ANISOU 1961  CD  PRO A 266     4749   5621   6484    340   -419   -151  A    C  
ATOM   1962  N   LYS A 267     -34.043   7.954  17.185  1.00 26.72      A    N  
ANISOU 1962  N   LYS A 267     2550   3467   4137    220   -233   -205  A    N  
ATOM   1963  CA  LYS A 267     -33.151   6.805  17.180  1.00 27.64      A    C  
ANISOU 1963  CA  LYS A 267     2723   3587   4192    173   -222   -192  A    C  
ATOM   1964  C   LYS A 267     -33.720   5.698  16.301  1.00 25.49      A    C  
ANISOU 1964  C   LYS A 267     2448   3328   3911    138   -266   -171  A    C  
ATOM   1965  O   LYS A 267     -34.949   5.460  16.267  1.00 29.77      A    O  
ANISOU 1965  O   LYS A 267     2924   3897   4489    133   -282   -175  A    O  
ATOM   1966  CB  LYS A 267     -32.996   6.305  18.604  1.00 35.61      A    C  
ANISOU 1966  CB  LYS A 267     3720   4626   5187    148   -158   -216  A    C  
ATOM   1967  CG  LYS A 267     -32.070   5.141  18.778  1.00 39.41      A    C  
ANISOU 1967  CG  LYS A 267     4256   5107   5609    103   -144   -203  A    C  
ATOM   1968  CD  LYS A 267     -32.336   4.496  20.122  1.00 45.92      A    C  
ANISOU 1968  CD  LYS A 267     5053   5969   6426     72    -91   -223  A    C  
ATOM   1969  CE  LYS A 267     -31.673   3.150  20.173  1.00 35.96      A    C  
ANISOU 1969  CE  LYS A 267     3839   4710   5114     25    -87   -207  A    C  
ATOM   1970  NZ  LYS A 267     -32.286   2.173  19.224  1.00 33.05      A    N1+
ANISOU 1970  NZ  LYS A 267     3466   4346   4746     -2   -131   -187  A    N1+
ATOM   1971  N   MET A 268     -32.833   5.028  15.561  1.00 24.89      A    N  
ANISOU 1971  N   MET A 268     2439   3233   3784    116   -287   -149  A    N  
ATOM   1972  CA  MET A 268     -33.257   3.925  14.688  1.00 24.88      A    C  
ANISOU 1972  CA  MET A 268     2445   3240   3767     81   -329   -131  A    C  
ATOM   1973  C   MET A 268     -33.265   2.627  15.488  1.00 22.55      A    C  
ANISOU 1973  C   MET A 268     2148   2972   3450     32   -295   -138  A    C  
ATOM   1974  O   MET A 268     -32.473   2.449  16.434  1.00 26.52      A    O  
ANISOU 1974  O   MET A 268     2675   3475   3926     23   -246   -149  A    O  
ATOM   1975  CB  MET A 268     -32.348   3.765  13.481  1.00 24.12      A    C  
ANISOU 1975  CB  MET A 268     2424   3114   3628     77   -366   -107  A    C  
ATOM   1976  CG  MET A 268     -32.555   4.764  12.334  1.00 27.41      A    C  
ANISOU 1976  CG  MET A 268     2847   3507   4062    112   -418    -90  A    C  
ATOM   1977  SD  MET A 268     -31.156   4.560  11.179  1.00 31.27      A    S  
ANISOU 1977  SD  MET A 268     3434   3961   4486    103   -439    -67  A    S  
ATOM   1978  CE  MET A 268     -31.332   5.988  10.106  1.00 32.99      A    C  
ANISOU 1978  CE  MET A 268     3660   4150   4725    146   -490    -46  A    C  
ATOM   1979  N   ASN A 269     -34.151   1.713  15.111  1.00 22.53      A    N  
ANISOU 1979  N   ASN A 269     2119   2989   3454     -1   -322   -131  A    N  
ATOM   1980  CA  ASN A 269     -34.113   0.364  15.662  1.00 26.13      A    C  
ANISOU 1980  CA  ASN A 269     2585   3461   3883    -53   -300   -133  A    C  
ATOM   1981  C   ASN A 269     -32.981  -0.398  15.005  1.00 21.95      A    C  
ANISOU 1981  C   ASN A 269     2138   2904   3299    -71   -314   -116  A    C  
ATOM   1982  O   ASN A 269     -32.981  -0.598  13.810  1.00 24.04      A    O  
ANISOU 1982  O   ASN A 269     2432   3152   3552    -74   -362   -103  A    O  
ATOM   1983  CB  ASN A 269     -35.438  -0.348  15.418  1.00 26.12      A    C  
ANISOU 1983  CB  ASN A 269     2529   3488   3909    -85   -328   -129  A    C  
ATOM   1984  CG  ASN A 269     -35.541  -1.649  16.168  1.00 36.32      A    C  
ANISOU 1984  CG  ASN A 269     3821   4798   5179   -140   -299   -132  A    C  
ATOM   1985  ND2 ASN A 269     -36.744  -1.994  16.575  1.00 54.41      A    N  
ANISOU 1985  ND2 ASN A 269     6044   7125   7505   -165   -296   -138  A    N  
ATOM   1986  OD1 ASN A 269     -34.550  -2.346  16.368  1.00 28.86      A    O  
ANISOU 1986  OD1 ASN A 269     2939   3836   4191   -160   -282   -126  A    O  
ATOM   1987  N   PHE A 270     -31.972  -0.804  15.786  1.00 23.66      A    N  
ANISOU 1987  N   PHE A 270     2395   3113   3482    -83   -271   -122  A    N  
ATOM   1988  CA  PHE A 270     -30.788  -1.442  15.187  1.00 22.11      A    C  
ANISOU 1988  CA  PHE A 270     2276   2888   3238    -92   -280   -110  A    C  
ATOM   1989  C   PHE A 270     -31.109  -2.757  14.497  1.00 22.41      A    C  
ANISOU 1989  C   PHE A 270     2335   2922   3258   -134   -313    -99  A    C  
ATOM   1990  O   PHE A 270     -30.371  -3.181  13.624  1.00 21.76      A    O  
ANISOU 1990  O   PHE A 270     2311   2815   3141   -137   -335    -92  A    O  
ATOM   1991  CB  PHE A 270     -29.765  -1.718  16.251  1.00 20.89      A    C  
ANISOU 1991  CB  PHE A 270     2151   2729   3056    -99   -231   -116  A    C  
ATOM   1992  CG  PHE A 270     -29.080  -0.536  16.782  1.00 18.69      A    C  
ANISOU 1992  CG  PHE A 270     1875   2445   2783    -61   -201   -126  A    C  
ATOM   1993  CD1 PHE A 270     -29.569   0.760  16.644  1.00 21.19      A    C  
ANISOU 1993  CD1 PHE A 270     2154   2763   3135    -24   -208   -132  A    C  
ATOM   1994  CD2 PHE A 270     -27.876  -0.715  17.441  1.00 18.19      A    C  
ANISOU 1994  CD2 PHE A 270     1853   2371   2688    -63   -168   -127  A    C  
ATOM   1995  CE1 PHE A 270     -28.866   1.822  17.188  1.00 21.39      A    C  
ANISOU 1995  CE1 PHE A 270     2187   2779   3162      7   -179   -143  A    C  
ATOM   1996  CE2 PHE A 270     -27.205   0.341  17.966  1.00 20.32      A    C  
ANISOU 1996  CE2 PHE A 270     2126   2634   2959    -33   -141   -137  A    C  
ATOM   1997  CZ  PHE A 270     -27.704   1.594  17.875  1.00 19.49      A    C  
ANISOU 1997  CZ  PHE A 270     1987   2531   2888      0   -145   -146  A    C  
ATOM   1998  N   ALA A 271     -32.222  -3.389  14.863  1.00 23.30      A    N  
ANISOU 1998  N   ALA A 271     2399   3060   3392   -167   -317   -102  A    N  
ATOM   1999  CA  ALA A 271     -32.617  -4.615  14.155  1.00 25.62      A    C  
ANISOU 1999  CA  ALA A 271     2713   3351   3672   -209   -353    -93  A    C  
ATOM   2000  C   ALA A 271     -32.940  -4.330  12.681  1.00 34.70      A    C  
ANISOU 2000  C   ALA A 271     3874   4488   4823   -197   -413    -84  A    C  
ATOM   2001  O   ALA A 271     -32.824  -5.211  11.826  1.00 29.72      A    O  
ANISOU 2001  O   ALA A 271     3286   3841   4166   -224   -446    -78  A    O  
ATOM   2002  CB  ALA A 271     -33.801  -5.284  14.870  1.00 29.77      A    C  
ANISOU 2002  CB  ALA A 271     3179   3909   4224   -251   -344    -97  A    C  
ATOM   2003  N   ASN A 272     -33.316  -3.085  12.381  1.00 32.65      A    N  
ANISOU 2003  N   ASN A 272     3578   4233   4592   -158   -428    -83  A    N  
ATOM   2004  CA  ASN A 272     -33.589  -2.648  10.997  1.00 35.23      A    C  
ANISOU 2004  CA  ASN A 272     3917   4549   4920   -142   -488    -71  A    C  
ATOM   2005  C   ASN A 272     -32.395  -2.105  10.249  1.00 28.36      A    C  
ANISOU 2005  C   ASN A 272     3115   3646   4013   -114   -494    -64  A    C  
ATOM   2006  O   ASN A 272     -32.517  -1.640   9.088  1.00 31.53      A    O  
ANISOU 2006  O   ASN A 272     3534   4036   4408   -100   -540    -51  A    O  
ATOM   2007  CB  ASN A 272     -34.667  -1.568  11.023  1.00 33.00      A    C  
ANISOU 2007  CB  ASN A 272     3561   4285   4691   -113   -506    -71  A    C  
ATOM   2008  CG  ASN A 272     -35.984  -2.070  11.598  1.00 60.89      A    C  
ANISOU 2008  CG  ASN A 272     7017   7854   8263   -141   -507    -79  A    C  
ATOM   2009  ND2 ASN A 272     -36.715  -1.168  12.233  1.00 51.55      A    N  
ANISOU 2009  ND2 ASN A 272     5763   6692   7130   -113   -490    -89  A    N  
ATOM   2010  OD1 ASN A 272     -36.347  -3.255  11.464  1.00 45.35      A    O  
ANISOU 2010  OD1 ASN A 272     5055   5894   6283   -189   -520    -77  A    O  
ATOM   2011  N   VAL A 273     -31.263  -2.057  10.930  1.00 24.97      A    N  
ANISOU 2011  N   VAL A 273     2720   3204   3560   -104   -445    -70  A    N  
ATOM   2012  CA  VAL A 273     -30.015  -1.578  10.387  1.00 19.32      A    C  
ANISOU 2012  CA  VAL A 273     2067   2464   2812    -80   -440    -65  A    C  
ATOM   2013  C   VAL A 273     -28.976  -2.715  10.101  1.00 34.47      A    C  
ANISOU 2013  C   VAL A 273     4054   4363   4680   -105   -430    -66  A    C  
ATOM   2014  O   VAL A 273     -28.220  -2.661   9.128  1.00 36.76      A    O  
ANISOU 2014  O   VAL A 273     4398   4632   4935    -97   -446    -60  A    O  
ATOM   2015  CB  VAL A 273     -29.344  -0.591  11.394  1.00 25.10      A    C  
ANISOU 2015  CB  VAL A 273     2789   3194   3555    -48   -392    -73  A    C  
ATOM   2016  CG1 VAL A 273     -28.005  -0.138  10.883  1.00 23.19      A    C  
ANISOU 2016  CG1 VAL A 273     2608   2926   3278    -28   -384    -68  A    C  
ATOM   2017  CG2 VAL A 273     -30.254   0.607  11.651  1.00 25.79      A    C  
ANISOU 2017  CG2 VAL A 273     2813   3293   3692    -17   -399    -75  A    C  
ATOM   2018  N   PHE A 274     -28.843  -3.667  11.027  1.00 22.64      A    N  
ANISOU 2018  N   PHE A 274     2554   2869   3177   -131   -398    -74  A    N  
ATOM   2019  CA  PHE A 274     -27.933  -4.808  10.895  1.00 19.29      A    C  
ANISOU 2019  CA  PHE A 274     2189   2427   2714   -152   -388    -76  A    C  
ATOM   2020  C   PHE A 274     -28.755  -6.049  10.515  1.00 18.94      A    C  
ANISOU 2020  C   PHE A 274     2145   2384   2667   -196   -419    -77  A    C  
ATOM   2021  O   PHE A 274     -28.895  -7.034  11.283  1.00 18.44      A    O  
ANISOU 2021  O   PHE A 274     2078   2324   2605   -226   -402    -80  A    O  
ATOM   2022  CB  PHE A 274     -27.238  -5.020  12.217  1.00 16.75      A    C  
ANISOU 2022  CB  PHE A 274     1867   2107   2390   -152   -336    -83  A    C  
ATOM   2023  CG  PHE A 274     -26.427  -3.848  12.643  1.00 18.58      A    C  
ANISOU 2023  CG  PHE A 274     2099   2337   2625   -114   -306    -85  A    C  
ATOM   2024  CD1 PHE A 274     -25.227  -3.610  12.041  1.00 22.23      A    C  
ANISOU 2024  CD1 PHE A 274     2612   2778   3057    -96   -302    -83  A    C  
ATOM   2025  CD2 PHE A 274     -26.880  -2.970  13.579  1.00 17.69      A    C  
ANISOU 2025  CD2 PHE A 274     1934   2243   2543    -99   -283    -90  A    C  
ATOM   2026  CE1 PHE A 274     -24.473  -2.506  12.402  1.00 21.57      A    C  
ANISOU 2026  CE1 PHE A 274     2527   2691   2976    -64   -277    -84  A    C  
ATOM   2027  CE2 PHE A 274     -26.144  -1.873  13.969  1.00 17.85      A    C  
ANISOU 2027  CE2 PHE A 274     1958   2259   2566    -66   -257    -94  A    C  
ATOM   2028  CZ  PHE A 274     -24.910  -1.657  13.380  1.00 18.58      A    C  
ANISOU 2028  CZ  PHE A 274     2102   2329   2627    -50   -256    -90  A    C  
ATOM   2029  N   ILE A 275     -29.283  -5.988   9.318  1.00 19.46      A    N  
ANISOU 2029  N   ILE A 275     2219   2448   2727   -200   -467    -71  A    N  
ATOM   2030  CA  ILE A 275     -30.154  -7.058   8.794  1.00 19.77      A    C  
ANISOU 2030  CA  ILE A 275     2258   2489   2765   -243   -506    -71  A    C  
ATOM   2031  C   ILE A 275     -29.397  -8.378   8.697  1.00 19.50      A    C  
ANISOU 2031  C   ILE A 275     2286   2429   2695   -269   -497    -79  A    C  
ATOM   2032  O   ILE A 275     -28.259  -8.404   8.205  1.00 25.64      A    O  
ANISOU 2032  O   ILE A 275     3120   3184   3437   -251   -487    -82  A    O  
ATOM   2033  CB  ILE A 275     -30.688  -6.655   7.401  1.00 21.32      A    C  
ANISOU 2033  CB  ILE A 275     2462   2684   2955   -239   -565    -63  A    C  
ATOM   2034  CG1 ILE A 275     -31.574  -5.401   7.517  1.00 28.57      A    C  
ANISOU 2034  CG1 ILE A 275     3313   3626   3917   -212   -579    -55  A    C  
ATOM   2035  CG2 ILE A 275     -31.463  -7.817   6.738  1.00 24.16      A    C  
ANISOU 2035  CG2 ILE A 275     2832   3042   3305   -286   -608    -65  A    C  
ATOM   2036  CD1 ILE A 275     -32.832  -5.599   8.339  1.00 32.02      A    C  
ANISOU 2036  CD1 ILE A 275     3674   4092   4401   -233   -579    -58  A    C  
ATOM   2037  N   GLY A 276     -29.991  -9.461   9.230  1.00 21.40      A    N  
ANISOU 2037  N   GLY A 276     2513   2671   2945   -310   -497    -81  A    N  
ATOM   2038  CA  GLY A 276     -29.387 -10.782   9.151  1.00 24.46      A    C  
ANISOU 2038  CA  GLY A 276     2959   3032   3305   -336   -493    -87  A    C  
ATOM   2039  C   GLY A 276     -28.386 -11.082  10.263  1.00 21.55      A    C  
ANISOU 2039  C   GLY A 276     2608   2652   2929   -327   -442    -90  A    C  
ATOM   2040  O   GLY A 276     -27.918 -12.203  10.372  1.00 23.96      A    O  
ANISOU 2040  O   GLY A 276     2957   2932   3217   -348   -436    -94  A    O  
ATOM   2041  N   ALA A 277     -28.078 -10.100  11.080  1.00 19.49      A    N  
ANISOU 2041  N   ALA A 277     2315   2407   2683   -297   -408    -86  A    N  
ATOM   2042  CA  ALA A 277     -27.207 -10.339  12.225  1.00 16.89      A    C  
ANISOU 2042  CA  ALA A 277     1998   2071   2348   -290   -362    -86  A    C  
ATOM   2043  C   ALA A 277     -27.871 -11.142  13.327  1.00 16.42      A    C  
ANISOU 2043  C   ALA A 277     1912   2023   2306   -329   -348    -81  A    C  
ATOM   2044  O   ALA A 277     -29.091 -11.136  13.501  1.00 19.54      A    O  
ANISOU 2044  O   ALA A 277     2257   2443   2726   -355   -360    -78  A    O  
ATOM   2045  CB  ALA A 277     -26.694  -9.019  12.778  1.00 16.62      A    C  
ANISOU 2045  CB  ALA A 277     1939   2052   2323   -249   -331    -86  A    C  
ATOM   2046  N   ASN A 278     -27.032 -11.818  14.108  1.00 15.08      A    N  
ANISOU 2046  N   ASN A 278     1774   1836   2121   -334   -319    -79  A    N  
ATOM   2047  CA  ASN A 278     -27.462 -12.519  15.306  1.00 14.81      A    C  
ANISOU 2047  CA  ASN A 278     1720   1810   2096   -370   -299    -72  A    C  
ATOM   2048  C   ASN A 278     -28.223 -11.499  16.208  1.00 15.65      A    C  
ANISOU 2048  C   ASN A 278     1756   1960   2230   -365   -274    -70  A    C  
ATOM   2049  O   ASN A 278     -27.708 -10.441  16.517  1.00 15.00      A    O  
ANISOU 2049  O   ASN A 278     1662   1888   2150   -328   -252    -74  A    O  
ATOM   2050  CB  ASN A 278     -26.206 -13.060  16.007  1.00 14.33      A    C  
ANISOU 2050  CB  ASN A 278     1705   1724   2013   -361   -272    -68  A    C  
ATOM   2051  CG  ASN A 278     -26.491 -13.881  17.259  1.00 16.31      A    C  
ANISOU 2051  CG  ASN A 278     1950   1979   2268   -400   -253    -55  A    C  
ATOM   2052  ND2 ASN A 278     -25.483 -14.625  17.689  1.00 16.57      A    N  
ANISOU 2052  ND2 ASN A 278     2031   1983   2282   -397   -243    -50  A    N  
ATOM   2053  OD1 ASN A 278     -27.513 -13.769  17.884  1.00 17.03      A    O  
ANISOU 2053  OD1 ASN A 278     1994   2101   2377   -428   -245    -51  A    O  
ATOM   2054  N   PRO A 279     -29.454 -11.800  16.601  1.00 17.24      A    N  
ANISOU 2054  N   PRO A 279     1911   2186   2452   -404   -278    -67  A    N  
ATOM   2055  CA  PRO A 279     -30.191 -10.897  17.472  1.00 17.69      A    C  
ANISOU 2055  CA  PRO A 279     1900   2284   2537   -399   -250    -70  A    C  
ATOM   2056  C   PRO A 279     -29.465 -10.528  18.767  1.00 16.56      A    C  
ANISOU 2056  C   PRO A 279     1759   2151   2384   -386   -201    -70  A    C  
ATOM   2057  O   PRO A 279     -29.674  -9.410  19.283  1.00 16.25      A    O  
ANISOU 2057  O   PRO A 279     1675   2138   2360   -360   -176    -79  A    O  
ATOM   2058  CB  PRO A 279     -31.495 -11.636  17.785  1.00 21.62      A    C  
ANISOU 2058  CB  PRO A 279     2356   2804   3053   -453   -257    -65  A    C  
ATOM   2059  CG  PRO A 279     -31.471 -12.837  16.974  1.00 25.34      A    C  
ANISOU 2059  CG  PRO A 279     2875   3243   3509   -486   -295    -59  A    C  
ATOM   2060  CD  PRO A 279     -30.229 -12.982  16.209  1.00 21.74      A    C  
ANISOU 2060  CD  PRO A 279     2489   2746   3025   -455   -308    -63  A    C  
ATOM   2061  N   LEU A 280     -28.608 -11.416  19.281  1.00 15.36      A    N  
ANISOU 2061  N   LEU A 280     1656   1974   2205   -400   -189    -61  A    N  
ATOM   2062  CA  LEU A 280     -27.843 -11.112  20.479  1.00 14.27      A    C  
ANISOU 2062  CA  LEU A 280     1525   1843   2053   -388   -149    -59  A    C  
ATOM   2063  C   LEU A 280     -26.767 -10.080  20.160  1.00 13.99      A    C  
ANISOU 2063  C   LEU A 280     1507   1798   2010   -333   -142    -67  A    C  
ATOM   2064  O   LEU A 280     -26.473  -9.230  21.011  1.00 15.25      A    O  
ANISOU 2064  O   LEU A 280     1647   1977   2171   -314   -109    -74  A    O  
ATOM   2065  CB  LEU A 280     -27.204 -12.351  21.065  1.00 15.32      A    C  
ANISOU 2065  CB  LEU A 280     1709   1950   2162   -417   -144    -44  A    C  
ATOM   2066  CG  LEU A 280     -28.171 -13.369  21.668  1.00 19.66      A    C  
ANISOU 2066  CG  LEU A 280     2244   2510   2715   -476   -143    -32  A    C  
ATOM   2067  CD1 LEU A 280     -27.378 -14.576  22.128  1.00 19.97      A    C  
ANISOU 2067  CD1 LEU A 280     2344   2514   2730   -499   -144    -15  A    C  
ATOM   2068  CD2 LEU A 280     -28.920 -12.747  22.836  1.00 22.71      A    C  
ANISOU 2068  CD2 LEU A 280     2573   2944   3112   -492   -103    -34  A    C  
ATOM   2069  N   ALA A 281     -26.224 -10.150  18.941  1.00 13.42      A    N  
ANISOU 2069  N   ALA A 281     1471   1698   1931   -312   -172    -70  A    N  
ATOM   2070  CA  ALA A 281     -25.264  -9.107  18.497  1.00 13.74      A    C  
ANISOU 2070  CA  ALA A 281     1526   1730   1964   -262   -166    -78  A    C  
ATOM   2071  C   ALA A 281     -25.934  -7.739  18.396  1.00 13.05      A    C  
ANISOU 2071  C   ALA A 281     1387   1669   1902   -238   -162    -87  A    C  
ATOM   2072  O   ALA A 281     -25.377  -6.731  18.862  1.00 13.37      A    O  
ANISOU 2072  O   ALA A 281     1420   1717   1945   -208   -139    -93  A    O  
ATOM   2073  CB  ALA A 281     -24.613  -9.457  17.177  1.00 14.63      A    C  
ANISOU 2073  CB  ALA A 281     1687   1811   2060   -248   -196    -79  A    C  
ATOM   2074  N   VAL A 282     -27.126  -7.708  17.814  1.00 13.64      A    N  
ANISOU 2074  N   VAL A 282     1426   1757   1998   -252   -188    -88  A    N  
ATOM   2075  CA  VAL A 282     -27.850  -6.457  17.677  1.00 14.18      A    C  
ANISOU 2075  CA  VAL A 282     1442   1848   2096   -227   -189    -96  A    C  
ATOM   2076  C   VAL A 282     -28.190  -5.906  19.067  1.00 13.82      A    C  
ANISOU 2076  C   VAL A 282     1353   1833   2067   -228   -146   -104  A    C  
ATOM   2077  O   VAL A 282     -28.039  -4.662  19.306  1.00 13.79      A    O  
ANISOU 2077  O   VAL A 282     1327   1837   2076   -192   -130   -114  A    O  
ATOM   2078  CB  VAL A 282     -29.085  -6.650  16.865  1.00 14.67      A    C  
ANISOU 2078  CB  VAL A 282     1474   1920   2181   -245   -227    -94  A    C  
ATOM   2079  CG1 VAL A 282     -29.867  -5.342  16.764  1.00 19.20      A    C  
ANISOU 2079  CG1 VAL A 282     1988   2515   2790   -215   -231   -101  A    C  
ATOM   2080  CG2 VAL A 282     -28.745  -7.179  15.484  1.00 17.81      A    C  
ANISOU 2080  CG2 VAL A 282     1920   2288   2558   -245   -269    -88  A    C  
ATOM   2081  N   ASP A 283     -28.593  -6.772  20.001  1.00 13.16      A    N  
ANISOU 2081  N   ASP A 283     1257   1764   1978   -268   -126   -100  A    N  
ATOM   2082  CA  ASP A 283     -28.932  -6.302  21.352  1.00 14.74      A    C  
ANISOU 2082  CA  ASP A 283     1419   1996   2188   -273    -81   -109  A    C  
ATOM   2083  C   ASP A 283     -27.688  -5.687  22.048  1.00 14.12      A    C  
ANISOU 2083  C   ASP A 283     1369   1909   2087   -245    -52   -114  A    C  
ATOM   2084  O   ASP A 283     -27.756  -4.597  22.661  1.00 15.01      A    O  
ANISOU 2084  O   ASP A 283     1451   2039   2211   -221    -25   -128  A    O  
ATOM   2085  CB  ASP A 283     -29.487  -7.468  22.215  1.00 15.40      A    C  
ANISOU 2085  CB  ASP A 283     1494   2095   2261   -328    -66   -100  A    C  
ATOM   2086  CG  ASP A 283     -29.875  -7.016  23.585  1.00 22.00      A    C  
ANISOU 2086  CG  ASP A 283     2290   2967   3102   -338    -18   -110  A    C  
ATOM   2087  OD1 ASP A 283     -30.925  -6.334  23.729  1.00 24.23      A    O  
ANISOU 2087  OD1 ASP A 283     2509   3281   3416   -333     -6   -124  A    O  
ATOM   2088  OD2 ASP A 283     -29.171  -7.276  24.514  1.00 19.21      A    O1-
ANISOU 2088  OD2 ASP A 283     1965   2613   2721   -348      8   -106  A    O1-
ATOM   2089  N   LEU A 284     -26.529  -6.341  21.918  1.00 13.17      A    N  
ANISOU 2089  N   LEU A 284     1308   1760   1937   -246    -59   -103  A    N  
ATOM   2090  CA  LEU A 284     -25.323  -5.818  22.509  1.00 12.31      A    C  
ANISOU 2090  CA  LEU A 284     1227   1643   1809   -222    -35   -105  A    C  
ATOM   2091  C   LEU A 284     -24.939  -4.472  21.876  1.00 12.32      A    C  
ANISOU 2091  C   LEU A 284     1221   1636   1822   -174    -40   -117  A    C  
ATOM   2092  O   LEU A 284     -24.570  -3.526  22.601  1.00 13.01      A    O  
ANISOU 2092  O   LEU A 284     1297   1734   1911   -154    -13   -128  A    O  
ATOM   2093  CB  LEU A 284     -24.218  -6.835  22.408  1.00 12.99      A    C  
ANISOU 2093  CB  LEU A 284     1371   1698   1865   -229    -45    -91  A    C  
ATOM   2094  CG  LEU A 284     -22.910  -6.380  22.995  1.00 12.44      A    C  
ANISOU 2094  CG  LEU A 284     1329   1623   1777   -207    -25    -93  A    C  
ATOM   2095  CD1 LEU A 284     -23.003  -6.062  24.516  1.00 14.83      A    C  
ANISOU 2095  CD1 LEU A 284     1610   1953   2071   -220     12    -97  A    C  
ATOM   2096  CD2 LEU A 284     -21.888  -7.458  22.743  1.00 14.58      A    C  
ANISOU 2096  CD2 LEU A 284     1653   1863   2024   -211    -40    -79  A    C  
ATOM   2097  N   LEU A 285     -25.033  -4.373  20.558  1.00 12.37      A    N  
ANISOU 2097  N   LEU A 285     1237   1626   1836   -159    -74   -114  A    N  
ATOM   2098  CA  LEU A 285     -24.745  -3.121  19.883  1.00 13.14      A    C  
ANISOU 2098  CA  LEU A 285     1333   1715   1946   -119    -82   -120  A    C  
ATOM   2099  C   LEU A 285     -25.614  -2.005  20.408  1.00 13.18      A    C  
ANISOU 2099  C   LEU A 285     1282   1745   1983   -103    -66   -135  A    C  
ATOM   2100  O   LEU A 285     -25.160  -0.902  20.626  1.00 13.89      A    O  
ANISOU 2100  O   LEU A 285     1369   1831   2079    -73    -52   -144  A    O  
ATOM   2101  CB  LEU A 285     -24.892  -3.263  18.374  1.00 11.84      A    C  
ANISOU 2101  CB  LEU A 285     1185   1531   1782   -112   -126   -112  A    C  
ATOM   2102  CG  LEU A 285     -23.785  -4.035  17.675  1.00 13.20      A    C  
ANISOU 2102  CG  LEU A 285     1417   1676   1922   -113   -138   -104  A    C  
ATOM   2103  CD1 LEU A 285     -24.176  -4.444  16.280  1.00 16.82      A    C  
ANISOU 2103  CD1 LEU A 285     1892   2121   2377   -118   -179    -99  A    C  
ATOM   2104  CD2 LEU A 285     -22.452  -3.269  17.673  1.00 14.58      A    C  
ANISOU 2104  CD2 LEU A 285     1620   1837   2082    -83   -122   -106  A    C  
ATOM   2105  N   GLU A 286     -26.906  -2.259  20.571  1.00 12.17      A    N  
ANISOU 2105  N   GLU A 286     1107   1639   1879   -123    -69   -138  A    N  
ATOM   2106  CA  GLU A 286     -27.813  -1.305  21.219  1.00 13.70      A    C  
ANISOU 2106  CA  GLU A 286     1242   1859   2106   -109    -48   -156  A    C  
ATOM   2107  C   GLU A 286     -27.326  -0.813  22.552  1.00 17.19      A    C  
ANISOU 2107  C   GLU A 286     1680   2313   2537   -105     -1   -170  A    C  
ATOM   2108  O   GLU A 286     -27.398   0.375  22.843  1.00 20.14      A    O  
ANISOU 2108  O   GLU A 286     2032   2692   2930    -74     15   -187  A    O  
ATOM   2109  CB  GLU A 286     -29.213  -1.894  21.375  1.00 18.43      A    C  
ANISOU 2109  CB  GLU A 286     1790   2487   2728   -140    -51   -157  A    C  
ATOM   2110  CG  GLU A 286     -29.981  -2.107  20.085  1.00 16.60      A    C  
ANISOU 2110  CG  GLU A 286     1543   2247   2516   -140   -100   -147  A    C  
ATOM   2111  CD  GLU A 286     -30.802  -0.933  19.656  1.00 27.27      A    C  
ANISOU 2111  CD  GLU A 286     2845   3608   3911   -105   -115   -157  A    C  
ATOM   2112  OE1 GLU A 286     -30.575   0.206  20.165  1.00 27.26      A    O  
ANISOU 2112  OE1 GLU A 286     2828   3606   3922    -70    -90   -172  A    O  
ATOM   2113  OE2 GLU A 286     -31.723  -1.159  18.811  1.00 24.85      A    O1-
ANISOU 2113  OE2 GLU A 286     2510   3305   3625   -112   -154   -151  A    O1-
ATOM   2114  N   LYS A 287     -26.764  -1.705  23.334  1.00 13.43      A    N  
ANISOU 2114  N   LYS A 287     1233   1840   2028   -135     19   -162  A    N  
ATOM   2115  CA ALYS A 287     -26.317  -1.361  24.680  0.50 13.56      A    C  
ANISOU 2115  CA ALYS A 287     1251   1874   2029   -138     62   -175  A    C  
ATOM   2116  CA BLYS A 287     -26.322  -1.339  24.670  0.50 13.63      A    C  
ANISOU 2116  CA BLYS A 287     1258   1881   2037   -138     62   -175  A    C  
ATOM   2117  C   LYS A 287     -24.989  -0.619  24.663  1.00 12.19      A    C  
ANISOU 2117  C   LYS A 287     1116   1677   1839   -108     65   -178  A    C  
ATOM   2118  O   LYS A 287     -24.683   0.167  25.574  1.00 14.41      A    O  
ANISOU 2118  O   LYS A 287     1391   1969   2117    -97     96   -194  A    O  
ATOM   2119  CB ALYS A 287     -26.241  -2.631  25.521  0.50 15.61      A    C  
ANISOU 2119  CB ALYS A 287     1527   2144   2259   -184     77   -162  A    C  
ATOM   2120  CB BLYS A 287     -26.294  -2.582  25.529  0.50 15.94      A    C  
ANISOU 2120  CB BLYS A 287     1567   2187   2303   -183     77   -163  A    C  
ATOM   2121  CG ALYS A 287     -27.627  -3.186  25.849  0.50 15.88      A    C  
ANISOU 2121  CG ALYS A 287     1516   2210   2310   -219     85   -164  A    C  
ATOM   2122  CG BLYS A 287     -27.707  -3.050  25.834  0.50 16.55      A    C  
ANISOU 2122  CG BLYS A 287     1595   2296   2398   -216     86   -166  A    C  
ATOM   2123  CD ALYS A 287     -27.575  -4.470  26.647  0.50 19.76      A    C  
ANISOU 2123  CD ALYS A 287     2028   2709   2771   -269     98   -147  A    C  
ATOM   2124  CD BLYS A 287     -27.772  -4.474  26.313  0.50 17.53      A    C  
ANISOU 2124  CD BLYS A 287     1739   2424   2497   -267     89   -147  A    C  
ATOM   2125  CE ALYS A 287     -28.950  -4.821  27.204  0.50 20.56      A    C  
ANISOU 2125  CE ALYS A 287     2077   2848   2888   -307    119   -152  A    C  
ATOM   2126  CE BLYS A 287     -29.174  -4.772  26.789  0.50 19.60      A    C  
ANISOU 2126  CE BLYS A 287     1946   2723   2777   -302    107   -152  A    C  
ATOM   2127  NZ ALYS A 287     -29.984  -4.902  26.131  0.50 21.29      A    N1+
ANISOU 2127  NZ ALYS A 287     2130   2941   3016   -306     87   -152  A    N1+
ATOM   2128  NZ BLYS A 287     -29.303  -6.201  27.134  0.50 20.37      A    N1+
ANISOU 2128  NZ BLYS A 287     2066   2821   2852   -356    103   -130  A    N1+
ATOM   2129  N   MET A 288     -24.173  -0.845  23.641  1.00 12.43      A    N  
ANISOU 2129  N   MET A 288     1187   1677   1859    -96     35   -163  A    N  
ATOM   2130  CA  MET A 288     -22.860  -0.140  23.489  1.00 12.39      A    C  
ANISOU 2130  CA  MET A 288     1217   1651   1840    -68     36   -165  A    C  
ATOM   2131  C   MET A 288     -22.978   1.242  22.871  1.00 16.24      A    C  
ANISOU 2131  C   MET A 288     1690   2128   2353    -31     28   -175  A    C  
ATOM   2132  O   MET A 288     -22.186   2.115  23.164  1.00 16.88      A    O  
ANISOU 2132  O   MET A 288     1783   2199   2431    -11     42   -183  A    O  
ATOM   2133  CB  MET A 288     -21.927  -0.971  22.668  1.00 14.05      A    C  
ANISOU 2133  CB  MET A 288     1474   1835   2028    -72     12   -146  A    C  
ATOM   2134  CG  MET A 288     -21.549  -2.247  23.324  1.00 12.79      A    C  
ANISOU 2134  CG  MET A 288     1339   1679   1842   -103     18   -135  A    C  
ATOM   2135  SD  MET A 288     -20.497  -3.150  22.151  1.00 21.57      A    S  
ANISOU 2135  SD  MET A 288     2504   2756   2934    -98    -12   -118  A    S  
ATOM   2136  CE  MET A 288     -19.731  -4.173  23.295  1.00 25.28      A    C  
ANISOU 2136  CE  MET A 288     3000   3227   3377   -122      4   -108  A    C  
ATOM   2137  N   LEU A 289     -23.923   1.438  21.989  1.00 12.40      A    N  
ANISOU 2137  N   LEU A 289     1178   1639   1894    -21      3   -173  A    N  
ATOM   2138  CA  LEU A 289     -24.035   2.654  21.181  1.00 12.00      A    C  
ANISOU 2138  CA  LEU A 289     1119   1573   1869     14    -15   -177  A    C  
ATOM   2139  C   LEU A 289     -25.145   3.580  21.684  1.00 15.71      A    C  
ANISOU 2139  C   LEU A 289     1534   2058   2376     32     -1   -197  A    C  
ATOM   2140  O   LEU A 289     -25.872   4.163  20.934  1.00 18.72      A    O  
ANISOU 2140  O   LEU A 289     1891   2432   2788     53    -26   -196  A    O  
ATOM   2141  CB  LEU A 289     -24.174   2.283  19.686  1.00 12.87      A    C  
ANISOU 2141  CB  LEU A 289     1248   1665   1979     17    -59   -158  A    C  
ATOM   2142  CG  LEU A 289     -22.976   1.564  19.062  1.00 14.72      A    C  
ANISOU 2142  CG  LEU A 289     1538   1879   2176      8    -70   -143  A    C  
ATOM   2143  CD1 LEU A 289     -23.290   1.131  17.648  1.00 15.03      A    C  
ANISOU 2143  CD1 LEU A 289     1593   1906   2212      6   -111   -128  A    C  
ATOM   2144  CD2 LEU A 289     -21.719   2.447  19.088  1.00 15.63      A    C  
ANISOU 2144  CD2 LEU A 289     1684   1977   2279     30    -57   -145  A    C  
ATOM   2145  N   VAL A 290     -25.357   3.572  22.983  1.00 20.57      A    N  
ANISOU 2145  N   VAL A 290     2128   2698   2991     20     38   -214  A    N  
ATOM   2146  CA  VAL A 290     -26.294   4.544  23.624  1.00 18.88      A    C  
ANISOU 2146  CA  VAL A 290     1861   2500   2812     40     61   -241  A    C  
ATOM   2147  C   VAL A 290     -25.680   5.889  23.606  1.00 16.06      A    C  
ANISOU 2147  C   VAL A 290     1518   2118   2467     76     65   -253  A    C  
ATOM   2148  O   VAL A 290     -24.498   6.110  23.939  1.00 16.70      A    O  
ANISOU 2148  O   VAL A 290     1640   2186   2520     76     77   -253  A    O  
ATOM   2149  CB  VAL A 290     -26.574   4.108  25.069  1.00 24.00      A    C  
ANISOU 2149  CB  VAL A 290     2489   3182   3447     11    107   -258  A    C  
ATOM   2150  CG1 VAL A 290     -27.633   4.994  25.679  1.00 27.37      A    C  
ANISOU 2150  CG1 VAL A 290     2860   3629   3912     30    133   -287  A    C  
ATOM   2151  CG2 VAL A 290     -27.134   2.702  25.087  1.00 31.96      A    C  
ANISOU 2151  CG2 VAL A 290     3490   4211   4442    -30    101   -241  A    C  
ATOM   2152  N   LEU A 291     -26.491   6.908  23.245  1.00 19.89      A    N  
ANISOU 2152  N   LEU A 291     1967   2596   2996    110     54   -265  A    N  
ATOM   2153  CA  LEU A 291     -26.002   8.205  23.200  1.00 19.62      A    C  
ANISOU 2153  CA  LEU A 291     1945   2534   2975    144     57   -276  A    C  
ATOM   2154  C   LEU A 291     -25.546   8.707  24.615  1.00 16.18      A    C  
ANISOU 2154  C   LEU A 291     1512   2109   2527    141    105   -305  A    C  
ATOM   2155  O   LEU A 291     -24.509   9.270  24.783  1.00 18.47      A    O  
ANISOU 2155  O   LEU A 291     1839   2378   2800    148    112   -308  A    O  
ATOM   2156  CB  LEU A 291     -27.082   9.143  22.612  1.00 21.20      A    C  
ANISOU 2156  CB  LEU A 291     2103   2724   3230    181     34   -284  A    C  
ATOM   2157  CG  LEU A 291     -26.617  10.579  22.504  1.00 21.53      A    C  
ANISOU 2157  CG  LEU A 291     2160   2729   3291    219     32   -295  A    C  
ATOM   2158  CD1 LEU A 291     -25.382  10.762  21.667  1.00 30.52      A    C  
ANISOU 2158  CD1 LEU A 291     3360   3835   4402    218      8   -269  A    C  
ATOM   2159  CD2 LEU A 291     -27.782  11.391  21.919  1.00 20.47      A    C  
ANISOU 2159  CD2 LEU A 291     1981   2584   3214    257      6   -300  A    C  
ATOM   2160  N   ASP A 292     -26.408   8.474  25.611  1.00 18.52      A    N  
ANISOU 2160  N   ASP A 292     1766   2440   2832    129    139   -329  A    N  
ATOM   2161  CA  ASP A 292     -26.098   8.881  26.992  1.00 19.45      A    C  
ANISOU 2161  CA  ASP A 292     1885   2573   2934    123    187   -359  A    C  
ATOM   2162  C   ASP A 292     -25.059   7.933  27.584  1.00 18.03      A    C  
ANISOU 2162  C   ASP A 292     1749   2403   2697     83    200   -344  A    C  
ATOM   2163  O   ASP A 292     -25.369   6.771  27.844  1.00 17.68      A    O  
ANISOU 2163  O   ASP A 292     1698   2386   2634     50    205   -332  A    O  
ATOM   2164  CB  ASP A 292     -27.378   8.834  27.808  1.00 15.65      A    C  
ANISOU 2164  CB  ASP A 292     1343   2128   2473    119    222   -386  A    C  
ATOM   2165  CG  ASP A 292     -27.189   9.377  29.251  1.00 16.96      A    C  
ANISOU 2165  CG  ASP A 292     1510   2311   2624    115    275   -423  A    C  
ATOM   2166  OD1 ASP A 292     -26.040   9.528  29.675  1.00 18.02      A    O  
ANISOU 2166  OD1 ASP A 292     1690   2433   2722    106    281   -422  A    O  
ATOM   2167  OD2 ASP A 292     -28.247   9.690  29.871  1.00 20.30      A    O1-
ANISOU 2167  OD2 ASP A 292     1880   2760   3073    123    306   -454  A    O1-
ATOM   2168  N   SER A 293     -23.868   8.422  27.795  1.00 16.15      A    N  
ANISOU 2168  N   SER A 293     1554   2145   2438     88    202   -346  A    N  
ATOM   2169  CA  SER A 293     -22.773   7.558  28.243  1.00 16.25      A    C  
ANISOU 2169  CA  SER A 293     1608   2165   2401     55    207   -329  A    C  
ATOM   2170  C   SER A 293     -23.026   6.989  29.630  1.00 20.35      A    C  
ANISOU 2170  C   SER A 293     2118   2722   2893     22    246   -343  A    C  
ATOM   2171  O   SER A 293     -22.415   5.960  29.960  1.00 20.89      A    O  
ANISOU 2171  O   SER A 293     2215   2800   2924     -9    244   -323  A    O  
ATOM   2172  CB  SER A 293     -21.486   8.290  28.219  1.00 18.45      A    C  
ANISOU 2172  CB  SER A 293     1928   2417   2666     67    202   -329  A    C  
ATOM   2173  OG  SER A 293     -21.466   9.283  29.190  1.00 20.60      A    O  
ANISOU 2173  OG  SER A 293     2194   2692   2942     76    232   -363  A    O  
ATOM   2174  N   ASP A 294     -23.869   7.612  30.450  1.00 16.87      A    N  
ANISOU 2174  N   ASP A 294     1641   2302   2468     29    280   -377  A    N  
ATOM   2175  CA  ASP A 294     -24.213   7.060  31.746  1.00 19.61      A    C  
ANISOU 2175  CA  ASP A 294     1979   2688   2786     -5    320   -391  A    C  
ATOM   2176  C   ASP A 294     -25.028   5.797  31.629  1.00 21.27      A    C  
ANISOU 2176  C   ASP A 294     2165   2923   2991    -36    317   -370  A    C  
ATOM   2177  O   ASP A 294     -25.208   5.065  32.601  1.00 23.12      A    O  
ANISOU 2177  O   ASP A 294     2400   3191   3195    -74    344   -371  A    O  
ATOM   2178  CB  ASP A 294     -25.073   8.036  32.548  1.00 19.64      A    C  
ANISOU 2178  CB  ASP A 294     1941   2709   2812     12    361   -435  A    C  
ATOM   2179  CG  ASP A 294     -24.317   9.261  33.038  1.00 27.15      A    C  
ANISOU 2179  CG  ASP A 294     2916   3639   3758     34    375   -463  A    C  
ATOM   2180  OD1 ASP A 294     -23.100   9.203  33.203  1.00 30.37      A    O  
ANISOU 2180  OD1 ASP A 294     3372   4034   4133     22    364   -451  A    O  
ATOM   2181  OD2 ASP A 294     -24.982  10.306  33.255  1.00 31.97      A    O1-
ANISOU 2181  OD2 ASP A 294     3495   4246   4403     64    396   -500  A    O1-
ATOM   2182  N   LYS A 295     -25.627   5.559  30.467  1.00 16.06      A    N  
ANISOU 2182  N   LYS A 295     1484   2251   2365    -22    285   -353  A    N  
ATOM   2183  CA  LYS A 295     -26.470   4.422  30.268  1.00 15.11      A    C  
ANISOU 2183  CA  LYS A 295     1341   2154   2247    -52    279   -336  A    C  
ATOM   2184  C   LYS A 295     -25.830   3.331  29.389  1.00 14.84      A    C  
ANISOU 2184  C   LYS A 295     1346   2099   2194    -70    237   -297  A    C  
ATOM   2185  O   LYS A 295     -26.433   2.301  29.167  1.00 20.35      A    O  
ANISOU 2185  O   LYS A 295     2032   2810   2890    -97    228   -279  A    O  
ATOM   2186  CB  LYS A 295     -27.743   4.864  29.601  1.00 19.95      A    C  
ANISOU 2186  CB  LYS A 295     1895   2771   2912    -28    269   -347  A    C  
ATOM   2187  CG  LYS A 295     -28.553   5.827  30.427  1.00 22.53      A    C  
ANISOU 2187  CG  LYS A 295     2175   3120   3265    -10    311   -388  A    C  
ATOM   2188  CD  LYS A 295     -29.151   5.193  31.625  1.00 32.78      A    C  
ANISOU 2188  CD  LYS A 295     3449   4465   4540    -51    358   -400  A    C  
ATOM   2189  CE  LYS A 295     -30.220   6.130  32.182  1.00 51.62      A    C  
ANISOU 2189  CE  LYS A 295     5774   6875   6964    -26    397   -444  A    C  
ATOM   2190  NZ  LYS A 295     -30.291   6.016  33.657  1.00 59.29      A    N1+
ANISOU 2190  NZ  LYS A 295     6745   7886   7900    -59    454   -469  A    N1+
ATOM   2191  N   ARG A 296     -24.611   3.593  28.955  1.00 15.10      A    N  
ANISOU 2191  N   ARG A 296     1425   2101   2212    -53    217   -286  A    N  
ATOM   2192  CA  ARG A 296     -23.901   2.680  28.100  1.00 16.63      A    C  
ANISOU 2192  CA  ARG A 296     1657   2273   2389    -63    182   -254  A    C  
ATOM   2193  C   ARG A 296     -23.386   1.527  28.940  1.00 16.08      A    C  
ANISOU 2193  C   ARG A 296     1616   2217   2277   -103    193   -238  A    C  
ATOM   2194  O   ARG A 296     -22.940   1.734  30.070  1.00 16.74      A    O  
ANISOU 2194  O   ARG A 296     1711   2314   2336   -114    220   -249  A    O  
ATOM   2195  CB  ARG A 296     -22.748   3.436  27.475  1.00 20.47      A    C  
ANISOU 2195  CB  ARG A 296     2177   2725   2873    -34    163   -250  A    C  
ATOM   2196  CG  ARG A 296     -22.373   3.079  26.060  1.00 25.16      A    C  
ANISOU 2196  CG  ARG A 296     2795   3292   3472    -23    122   -226  A    C  
ATOM   2197  CD  ARG A 296     -21.317   4.071  25.572  1.00 16.70      A    C  
ANISOU 2197  CD  ARG A 296     1751   2193   2401      7    113   -228  A    C  
ATOM   2198  NE  ARG A 296     -21.895   5.304  25.001  1.00 14.52      A    N  
ANISOU 2198  NE  ARG A 296     1451   1903   2162     40    104   -241  A    N  
ATOM   2199  CZ  ARG A 296     -21.257   6.468  24.935  1.00 14.42      A    C  
ANISOU 2199  CZ  ARG A 296     1452   1870   2157     65    107   -250  A    C  
ATOM   2200  NH1 ARG A 296     -20.001   6.547  25.311  1.00 14.74      A    N1+
ANISOU 2200  NH1 ARG A 296     1528   1904   2171     58    115   -248  A    N1+
ATOM   2201  NH2 ARG A 296     -21.861   7.527  24.470  1.00 14.76      A    N  
ANISOU 2201  NH2 ARG A 296     1473   1898   2235     94     98   -260  A    N  
ATOM   2202  N   ILE A 297     -23.382   0.338  28.359  1.00 14.26      A    N  
ANISOU 2202  N   ILE A 297     1403   1978   2038   -125    167   -212  A    N  
ATOM   2203  CA  ILE A 297     -22.911  -0.874  29.038  1.00 14.16      A    C  
ANISOU 2203  CA  ILE A 297     1421   1971   1988   -162    171   -193  A    C  
ATOM   2204  C   ILE A 297     -21.403  -0.758  29.333  1.00 12.77      A    C  
ANISOU 2204  C   ILE A 297     1291   1777   1784   -152    168   -186  A    C  
ATOM   2205  O   ILE A 297     -20.662  -0.168  28.598  1.00 13.41      A    O  
ANISOU 2205  O   ILE A 297     1387   1835   1873   -123    151   -187  A    O  
ATOM   2206  CB  ILE A 297     -23.226  -2.107  28.188  1.00 14.80      A    C  
ANISOU 2206  CB  ILE A 297     1512   2039   2071   -181    140   -168  A    C  
ATOM   2207  CG1 ILE A 297     -23.137  -3.404  29.021  1.00 15.14      A    C  
ANISOU 2207  CG1 ILE A 297     1579   2092   2084   -226    146   -148  A    C  
ATOM   2208  CG2 ILE A 297     -22.391  -2.173  26.903  1.00 15.49      A    C  
ANISOU 2208  CG2 ILE A 297     1633   2091   2163   -156    104   -155  A    C  
ATOM   2209  CD1 ILE A 297     -23.801  -4.583  28.398  1.00 17.79      A    C  
ANISOU 2209  CD1 ILE A 297     1914   2420   2425   -254    123   -129  A    C  
ATOM   2210  N   THR A 298     -20.999  -1.312  30.484  1.00 12.54      A    N  
ANISOU 2210  N   THR A 298     1281   1763   1720   -182    184   -179  A    N  
ATOM   2211  CA  THR A 298     -19.600  -1.331  30.801  1.00 12.11      A    C  
ANISOU 2211  CA  THR A 298     1266   1693   1639   -175    177   -171  A    C  
ATOM   2212  C   THR A 298     -18.909  -2.600  30.267  1.00 11.19      A    C  
ANISOU 2212  C   THR A 298     1187   1554   1511   -185    146   -141  A    C  
ATOM   2213  O   THR A 298     -19.575  -3.540  29.813  1.00 12.75      A    O  
ANISOU 2213  O   THR A 298     1382   1747   1715   -203    132   -126  A    O  
ATOM   2214  CB  THR A 298     -19.395  -1.313  32.301  1.00 13.84      A    C  
ANISOU 2214  CB  THR A 298     1493   1939   1825   -201    204   -177  A    C  
ATOM   2215  CG2 THR A 298     -20.105  -0.116  32.936  1.00 16.20      A    C  
ANISOU 2215  CG2 THR A 298     1758   2263   2135   -194    239   -211  A    C  
ATOM   2216  OG1 THR A 298     -19.821  -2.544  32.877  1.00 14.56      A    O  
ANISOU 2216  OG1 THR A 298     1594   2043   1895   -242    207   -155  A    O  
ATOM   2217  N   ALA A 299     -17.569  -2.597  30.322  1.00 10.53      A    N  
ANISOU 2217  N   ALA A 299     1135   1453   1411   -172    134   -132  A    N  
ATOM   2218  CA  ALA A 299     -16.875  -3.815  29.847  1.00 10.47      A    C  
ANISOU 2218  CA  ALA A 299     1161   1422   1396   -177    106   -106  A    C  
ATOM   2219  C   ALA A 299     -17.271  -5.051  30.669  1.00 10.93      A    C  
ANISOU 2219  C   ALA A 299     1233   1489   1433   -217    106    -86  A    C  
ATOM   2220  O   ALA A 299     -17.529  -6.108  30.111  1.00 12.02      A    O  
ANISOU 2220  O   ALA A 299     1384   1609   1575   -229     86    -70  A    O  
ATOM   2221  CB  ALA A 299     -15.360  -3.611  29.865  1.00 12.04      A    C  
ANISOU 2221  CB  ALA A 299     1386   1606   1584   -156     94   -102  A    C  
ATOM   2222  N   ALA A 300     -17.285  -4.935  31.990  1.00 11.72      A    N  
ANISOU 2222  N   ALA A 300     1333   1613   1506   -240    128    -88  A    N  
ATOM   2223  CA  ALA A 300     -17.629  -6.086  32.825  1.00 13.42      A    C  
ANISOU 2223  CA  ALA A 300     1565   1836   1696   -283    128    -65  A    C  
ATOM   2224  C   ALA A 300     -19.051  -6.555  32.544  1.00 13.73      A    C  
ANISOU 2224  C   ALA A 300     1581   1887   1751   -308    137    -65  A    C  
ATOM   2225  O   ALA A 300     -19.323  -7.760  32.435  1.00 14.90      A    O  
ANISOU 2225  O   ALA A 300     1746   2022   1894   -335    121    -42  A    O  
ATOM   2226  CB  ALA A 300     -17.460  -5.745  34.293  1.00 15.32      A    C  
ANISOU 2226  CB  ALA A 300     1811   2107   1903   -306    153    -69  A    C  
ATOM   2227  N   GLN A 301     -19.959  -5.614  32.392  1.00 13.32      A    N  
ANISOU 2227  N   GLN A 301     1485   1856   1720   -300    159    -90  A    N  
ATOM   2228  CA  GLN A 301     -21.356  -5.970  32.065  1.00 15.76      A    C  
ANISOU 2228  CA  GLN A 301     1762   2178   2048   -321    166    -92  A    C  
ATOM   2229  C   GLN A 301     -21.465  -6.658  30.715  1.00 13.22      A    C  
ANISOU 2229  C   GLN A 301     1449   1825   1750   -313    130    -80  A    C  
ATOM   2230  O   GLN A 301     -22.214  -7.642  30.536  1.00 16.14      A    O  
ANISOU 2230  O   GLN A 301     1817   2193   2123   -344    120    -65  A    O  
ATOM   2231  CB  GLN A 301     -22.268  -4.747  32.047  1.00 14.34      A    C  
ANISOU 2231  CB  GLN A 301     1530   2025   1892   -305    193   -124  A    C  
ATOM   2232  CG  GLN A 301     -22.573  -4.188  33.413  1.00 15.01      A    C  
ANISOU 2232  CG  GLN A 301     1600   2148   1956   -323    235   -142  A    C  
ATOM   2233  CD  GLN A 301     -23.146  -2.826  33.372  1.00 15.94      A    C  
ANISOU 2233  CD  GLN A 301     1673   2282   2100   -294    260   -178  A    C  
ATOM   2234  NE2 GLN A 301     -23.644  -2.396  34.560  1.00 26.02      A    N  
ANISOU 2234  NE2 GLN A 301     2930   3596   3360   -313    302   -198  A    N  
ATOM   2235  OE1 GLN A 301     -23.115  -2.108  32.397  1.00 16.99      A    O  
ANISOU 2235  OE1 GLN A 301     1794   2397   2266   -255    244   -189  A    O  
ATOM   2236  N   ALA A 302     -20.711  -6.140  29.746  1.00 12.46      A    N  
ANISOU 2236  N   ALA A 302     1362   1704   1667   -271    110    -86  A    N  
ATOM   2237  CA  ALA A 302     -20.757  -6.699  28.394  1.00 12.57      A    C  
ANISOU 2237  CA  ALA A 302     1387   1689   1701   -259     77    -78  A    C  
ATOM   2238  C   ALA A 302     -20.212  -8.139  28.348  1.00 13.20      A    C  
ANISOU 2238  C   ALA A 302     1510   1741   1763   -280     54    -52  A    C  
ATOM   2239  O   ALA A 302     -20.754  -8.977  27.601  1.00 13.51      A    O  
ANISOU 2239  O   ALA A 302     1556   1765   1813   -295     33    -43  A    O  
ATOM   2240  CB  ALA A 302     -20.071  -5.783  27.424  1.00 12.22      A    C  
ANISOU 2240  CB  ALA A 302     1345   1627   1670   -214     65    -90  A    C  
ATOM   2241  N   LEU A 303     -19.186  -8.438  29.152  1.00 12.30      A    N  
ANISOU 2241  N   LEU A 303     1427   1620   1624   -281     55    -39  A    N  
ATOM   2242  CA  LEU A 303     -18.633  -9.783  29.180  1.00 11.93      A    C  
ANISOU 2242  CA  LEU A 303     1424   1544   1565   -297     32    -15  A    C  
ATOM   2243  C   LEU A 303     -19.670 -10.821  29.601  1.00 14.61      A    C  
ANISOU 2243  C   LEU A 303     1765   1890   1898   -347     32      2  A    C  
ATOM   2244  O   LEU A 303     -19.560 -11.984  29.203  1.00 15.64      A    O  
ANISOU 2244  O   LEU A 303     1926   1988   2029   -360      6     20  A    O  
ATOM   2245  CB  LEU A 303     -17.415  -9.850  30.093  1.00 13.79      A    C  
ANISOU 2245  CB  LEU A 303     1688   1776   1776   -291     32     -3  A    C  
ATOM   2246  CG  LEU A 303     -16.184  -9.155  29.541  1.00 13.59      A    C  
ANISOU 2246  CG  LEU A 303     1669   1737   1756   -245     24    -14  A    C  
ATOM   2247  CD1 LEU A 303     -15.158  -8.994  30.662  1.00 14.55      A    C  
ANISOU 2247  CD1 LEU A 303     1807   1867   1854   -244     29     -5  A    C  
ATOM   2248  CD2 LEU A 303     -15.541  -9.917  28.381  1.00 12.11      A    C  
ANISOU 2248  CD2 LEU A 303     1509   1511   1582   -223     -5     -7  A    C  
ATOM   2249  N   ALA A 304     -20.660 -10.410  30.420  1.00 13.64      A    N  
ANISOU 2249  N   ALA A 304     1608   1805   1771   -376     62     -4  A    N  
ATOM   2250  CA  ALA A 304     -21.719 -11.268  30.898  1.00 15.20      A    C  
ANISOU 2250  CA  ALA A 304     1798   2014   1962   -428     68      9  A    C  
ATOM   2251  C   ALA A 304     -22.922 -11.336  29.958  1.00 14.52      A    C  
ANISOU 2251  C   ALA A 304     1677   1933   1906   -437     62      0  A    C  
ATOM   2252  O   ALA A 304     -23.884 -12.092  30.230  1.00 16.35      A    O  
ANISOU 2252  O   ALA A 304     1900   2174   2137   -484     65     12  A    O  
ATOM   2253  CB  ALA A 304     -22.177 -10.793  32.266  1.00 15.30      A    C  
ANISOU 2253  CB  ALA A 304     1790   2072   1953   -456    108      5  A    C  
ATOM   2254  N   HIS A 305     -22.900 -10.590  28.863  1.00 13.20      A    N  
ANISOU 2254  N   HIS A 305     1492   1758   1764   -397     51    -19  A    N  
ATOM   2255  CA  HIS A 305     -24.007 -10.630  27.908  1.00 14.75      A    C  
ANISOU 2255  CA  HIS A 305     1657   1958   1989   -404     38    -27  A    C  
ATOM   2256  C   HIS A 305     -24.036 -11.989  27.201  1.00 13.26      A    C  
ANISOU 2256  C   HIS A 305     1504   1732   1800   -426      3     -9  A    C  
ATOM   2257  O   HIS A 305     -23.004 -12.576  26.903  1.00 15.44      A    O  
ANISOU 2257  O   HIS A 305     1828   1972   2065   -412    -17      2  A    O  
ATOM   2258  CB  HIS A 305     -23.847  -9.477  26.945  1.00 15.67      A    C  
ANISOU 2258  CB  HIS A 305     1753   2073   2129   -354     31    -49  A    C  
ATOM   2259  CG  HIS A 305     -24.980  -9.268  26.018  1.00 14.68      A    C  
ANISOU 2259  CG  HIS A 305     1589   1956   2034   -355     17    -59  A    C  
ATOM   2260  CD2 HIS A 305     -25.957  -8.339  26.028  1.00 16.12      A    C  
ANISOU 2260  CD2 HIS A 305     1715   2169   2239   -349     32    -77  A    C  
ATOM   2261  ND1 HIS A 305     -25.208 -10.051  24.909  1.00 15.24      A    N  
ANISOU 2261  ND1 HIS A 305     1677   2002   2113   -363    -19    -52  A    N  
ATOM   2262  CE1 HIS A 305     -26.270  -9.609  24.273  1.00 15.65      A    C  
ANISOU 2262  CE1 HIS A 305     1686   2071   2192   -363    -28    -63  A    C  
ATOM   2263  NE2 HIS A 305     -26.716  -8.542  24.917  1.00 16.81      A    N  
ANISOU 2263  NE2 HIS A 305     1787   2251   2351   -350      2    -78  A    N  
ATOM   2264  N   ALA A 306     -25.232 -12.462  26.891  1.00 16.00      A    N  
ANISOU 2264  N   ALA A 306     1826   2089   2164   -462     -4     -7  A    N  
ATOM   2265  CA  ALA A 306     -25.414 -13.755  26.273  1.00 15.68      A    C  
ANISOU 2265  CA  ALA A 306     1819   2016   2125   -491    -36      8  A    C  
ATOM   2266  C   ALA A 306     -24.720 -13.975  24.944  1.00 14.57      A    C  
ANISOU 2266  C   ALA A 306     1712   1832   1989   -456    -72      3  A    C  
ATOM   2267  O   ALA A 306     -24.417 -15.123  24.582  1.00 16.52      A    O  
ANISOU 2267  O   ALA A 306     2005   2041   2231   -472    -97     15  A    O  
ATOM   2268  CB  ALA A 306     -26.910 -14.079  26.152  1.00 19.45      A    C  
ANISOU 2268  CB  ALA A 306     2254   2516   2620   -536    -36      9  A    C  
ATOM   2269  N   TYR A 307     -24.395 -12.870  24.250  1.00 13.59      A    N  
ANISOU 2269  N   TYR A 307     1573   1715   1877   -409    -72    -16  A    N  
ATOM   2270  CA  TYR A 307     -23.659 -12.952  23.002  1.00 14.59      A    C  
ANISOU 2270  CA  TYR A 307     1733   1808   2006   -375   -100    -22  A    C  
ATOM   2271  C   TYR A 307     -22.341 -13.721  23.185  1.00 13.69      A    C  
ANISOU 2271  C   TYR A 307     1675   1656   1871   -363   -107    -11  A    C  
ATOM   2272  O   TYR A 307     -21.878 -14.397  22.259  1.00 16.46      A    O  
ANISOU 2272  O   TYR A 307     2064   1970   2220   -353   -133    -13  A    O  
ATOM   2273  CB  TYR A 307     -23.427 -11.573  22.449  1.00 13.75      A    C  
ANISOU 2273  CB  TYR A 307     1601   1715   1908   -330    -94    -40  A    C  
ATOM   2274  CG  TYR A 307     -22.810 -11.574  21.063  1.00 14.06      A    C  
ANISOU 2274  CG  TYR A 307     1671   1725   1948   -299   -121    -48  A    C  
ATOM   2275  CD1 TYR A 307     -23.411 -12.210  20.017  1.00 15.26      A    C  
ANISOU 2275  CD1 TYR A 307     1833   1861   2104   -314   -153    -50  A    C  
ATOM   2276  CD2 TYR A 307     -21.619 -10.877  20.800  1.00 13.72      A    C  
ANISOU 2276  CD2 TYR A 307     1646   1672   1896   -255   -114    -56  A    C  
ATOM   2277  CE1 TYR A 307     -22.861 -12.212  18.708  1.00 13.49      A    C  
ANISOU 2277  CE1 TYR A 307     1641   1612   1875   -288   -176    -59  A    C  
ATOM   2278  CE2 TYR A 307     -21.106 -10.819  19.524  1.00 13.17      A    C  
ANISOU 2278  CE2 TYR A 307     1602   1580   1823   -230   -135    -63  A    C  
ATOM   2279  CZ  TYR A 307     -21.708 -11.489  18.477  1.00 13.40      A    C  
ANISOU 2279  CZ  TYR A 307     1645   1594   1855   -246   -164    -66  A    C  
ATOM   2280  OH  TYR A 307     -21.174 -11.395  17.198  1.00 16.40      A    O  
ANISOU 2280  OH  TYR A 307     2052   1953   2226   -221   -183    -74  A    O  
ATOM   2281  N   PHE A 308     -21.718 -13.639  24.367  1.00 13.48      A    N  
ANISOU 2281  N   PHE A 308     1656   1638   1829   -364    -85     -1  A    N  
ATOM   2282  CA  PHE A 308     -20.407 -14.260  24.608  1.00 12.16      A    C  
ANISOU 2282  CA  PHE A 308     1537   1437   1647   -346    -93     10  A    C  
ATOM   2283  C   PHE A 308     -20.491 -15.542  25.398  1.00 13.74      A    C  
ANISOU 2283  C   PHE A 308     1767   1618   1834   -387   -101     34  A    C  
ATOM   2284  O   PHE A 308     -19.467 -15.987  25.949  1.00 15.60      A    O  
ANISOU 2284  O   PHE A 308     2037   1832   2057   -376   -104     47  A    O  
ATOM   2285  CB  PHE A 308     -19.469 -13.303  25.344  1.00 13.80      A    C  
ANISOU 2285  CB  PHE A 308     1737   1664   1844   -316    -70      6  A    C  
ATOM   2286  CG  PHE A 308     -19.296 -12.002  24.626  1.00 11.51      A    C  
ANISOU 2286  CG  PHE A 308     1420   1389   1565   -277    -63    -16  A    C  
ATOM   2287  CD1 PHE A 308     -18.651 -11.957  23.389  1.00 12.77      A    C  
ANISOU 2287  CD1 PHE A 308     1599   1523   1730   -243    -80    -26  A    C  
ATOM   2288  CD2 PHE A 308     -19.778 -10.829  25.164  1.00 12.30      A    C  
ANISOU 2288  CD2 PHE A 308     1478   1526   1669   -274    -37    -27  A    C  
ATOM   2289  CE1 PHE A 308     -18.543 -10.753  22.686  1.00 13.17      A    C  
ANISOU 2289  CE1 PHE A 308     1628   1586   1790   -211    -75    -43  A    C  
ATOM   2290  CE2 PHE A 308     -19.659  -9.641  24.494  1.00 11.50      A    C  
ANISOU 2290  CE2 PHE A 308     1356   1435   1580   -238    -33    -45  A    C  
ATOM   2291  CZ  PHE A 308     -19.029  -9.580  23.261  1.00 12.00      A    C  
ANISOU 2291  CZ  PHE A 308     1439   1473   1648   -209    -53    -51  A    C  
ATOM   2292  N   ALA A 309     -21.658 -16.189  25.398  1.00 15.47      A    N  
ANISOU 2292  N   ALA A 309     1977   1840   2059   -434   -107     42  A    N  
ATOM   2293  CA  ALA A 309     -21.787 -17.390  26.177  1.00 19.51      A    C  
ANISOU 2293  CA  ALA A 309     2521   2333   2560   -477   -113     68  A    C  
ATOM   2294  C   ALA A 309     -20.737 -18.454  25.938  1.00 17.54      A    C  
ANISOU 2294  C   ALA A 309     2332   2028   2305   -463   -140     80  A    C  
ATOM   2295  O   ALA A 309     -20.397 -19.168  26.883  1.00 20.99      A    O  
ANISOU 2295  O   ALA A 309     2797   2450   2727   -485   -142    105  A    O  
ATOM   2296  CB  ALA A 309     -23.161 -17.973  26.017  1.00 18.16      A    C  
ANISOU 2296  CB  ALA A 309     2333   2170   2398   -531   -119     73  A    C  
ATOM   2297  N   GLN A 310     -20.261 -18.632  24.695  1.00 16.54      A    N  
ANISOU 2297  N   GLN A 310     2226   1869   2190   -430   -161     63  A    N  
ATOM   2298  CA  GLN A 310     -19.331 -19.700  24.433  1.00 16.01      A    C  
ANISOU 2298  CA  GLN A 310     2213   1747   2121   -416   -186     71  A    C  
ATOM   2299  C   GLN A 310     -17.915 -19.416  24.920  1.00 18.33      A    C  
ANISOU 2299  C   GLN A 310     2523   2034   2409   -372   -180     75  A    C  
ATOM   2300  O   GLN A 310     -17.095 -20.330  24.951  1.00 20.53      A    O  
ANISOU 2300  O   GLN A 310     2844   2269   2687   -359   -200     86  A    O  
ATOM   2301  CB  GLN A 310     -19.308 -20.093  22.955  1.00 21.75      A    C  
ANISOU 2301  CB  GLN A 310     2962   2442   2861   -398   -210     50  A    C  
ATOM   2302  CG  GLN A 310     -18.706 -19.133  21.981  1.00 25.42      A    C  
ANISOU 2302  CG  GLN A 310     3413   2917   3330   -347   -203     24  A    C  
ATOM   2303  CD  GLN A 310     -18.817 -19.658  20.519  1.00 26.75      A    C  
ANISOU 2303  CD  GLN A 310     3607   3051   3503   -339   -227      2  A    C  
ATOM   2304  NE2 GLN A 310     -19.261 -18.813  19.616  1.00 29.46      A    N  
ANISOU 2304  NE2 GLN A 310     3924   3419   3850   -328   -226    -17  A    N  
ATOM   2305  OE1 GLN A 310     -18.493 -20.829  20.230  1.00 30.93      A    O  
ANISOU 2305  OE1 GLN A 310     4184   3532   4035   -343   -248      4  A    O  
ATOM   2306  N   TYR A 311     -17.629 -18.154  25.275  1.00 14.62      A    N  
ANISOU 2306  N   TYR A 311     2016   1606   1933   -348   -156     66  A    N  
ATOM   2307  CA  TYR A 311     -16.309 -17.713  25.692  1.00 16.29      A    C  
ANISOU 2307  CA  TYR A 311     2234   1817   2138   -307   -149     66  A    C  
ATOM   2308  C   TYR A 311     -16.212 -17.211  27.129  1.00 15.25      A    C  
ANISOU 2308  C   TYR A 311     2086   1720   1989   -323   -131     83  A    C  
ATOM   2309  O   TYR A 311     -15.155 -17.268  27.744  1.00 18.28      A    O  
ANISOU 2309  O   TYR A 311     2485   2095   2363   -303   -135     94  A    O  
ATOM   2310  CB  TYR A 311     -15.787 -16.621  24.751  1.00 17.17      A    C  
ANISOU 2310  CB  TYR A 311     2324   1943   2257   -261   -140     39  A    C  
ATOM   2311  CG  TYR A 311     -15.671 -17.088  23.324  1.00 16.04      A    C  
ANISOU 2311  CG  TYR A 311     2202   1766   2126   -242   -158     21  A    C  
ATOM   2312  CD1 TYR A 311     -14.737 -18.080  23.017  1.00 22.23      A    C  
ANISOU 2312  CD1 TYR A 311     3028   2504   2914   -221   -177     24  A    C  
ATOM   2313  CD2 TYR A 311     -16.489 -16.654  22.366  1.00 15.84      A    C  
ANISOU 2313  CD2 TYR A 311     2159   1754   2108   -246   -159      5  A    C  
ATOM   2314  CE1 TYR A 311     -14.623 -18.565  21.749  1.00 21.40      A    C  
ANISOU 2314  CE1 TYR A 311     2946   2368   2816   -205   -191      5  A    C  
ATOM   2315  CE2 TYR A 311     -16.381 -17.098  21.064  1.00 22.38      A    C  
ANISOU 2315  CE2 TYR A 311     3010   2551   2941   -232   -175    -12  A    C  
ATOM   2316  CZ  TYR A 311     -15.441 -18.079  20.763  1.00 19.75      A    C  
ANISOU 2316  CZ  TYR A 311     2721   2174   2609   -212   -190    -14  A    C  
ATOM   2317  OH  TYR A 311     -15.390 -18.566  19.441  1.00 25.22      A    O  
ANISOU 2317  OH  TYR A 311     3440   2838   3304   -200   -206    -34  A    O  
ATOM   2318  N   HIS A 312     -17.314 -16.735  27.695  1.00 16.14      A    N  
ANISOU 2318  N   HIS A 312     2166   1871   2094   -358   -110     83  A    N  
ATOM   2319  CA  HIS A 312     -17.272 -16.072  28.973  1.00 14.83      A    C  
ANISOU 2319  CA  HIS A 312     1982   1744   1909   -371    -86     92  A    C  
ATOM   2320  C   HIS A 312     -16.909 -17.023  30.060  1.00 16.43      A    C  
ANISOU 2320  C   HIS A 312     2221   1929   2091   -398    -97    124  A    C  
ATOM   2321  O   HIS A 312     -17.495 -18.117  30.162  1.00 18.95      A    O  
ANISOU 2321  O   HIS A 312     2565   2226   2409   -437   -110    144  A    O  
ATOM   2322  CB  HIS A 312     -18.661 -15.431  29.229  1.00 15.21      A    C  
ANISOU 2322  CB  HIS A 312     1985   1835   1957   -404    -59     82  A    C  
ATOM   2323  CG  HIS A 312     -18.871 -14.837  30.607  1.00 14.18      A    C  
ANISOU 2323  CG  HIS A 312     1836   1748   1804   -427    -29     87  A    C  
ATOM   2324  CD2 HIS A 312     -19.932 -14.925  31.445  1.00 16.61      A    C  
ANISOU 2324  CD2 HIS A 312     2125   2088   2098   -476     -7     95  A    C  
ATOM   2325  ND1 HIS A 312     -17.995 -13.945  31.216  1.00 14.55      A    N  
ANISOU 2325  ND1 HIS A 312     1877   1813   1837   -400    -15     80  A    N  
ATOM   2326  CE1 HIS A 312     -18.508 -13.547  32.366  1.00 15.49      A    C  
ANISOU 2326  CE1 HIS A 312     1980   1973   1934   -431     12     82  A    C  
ATOM   2327  NE2 HIS A 312     -19.681 -14.123  32.535  1.00 17.81      A    N  
ANISOU 2327  NE2 HIS A 312     2264   2276   2227   -477     21     91  A    N  
ATOM   2328  N   ASP A 313     -15.981 -16.595  30.907  1.00 14.92      A    N  
ANISOU 2328  N   ASP A 313     2035   1750   1883   -382    -92    131  A    N  
ATOM   2329  CA  ASP A 313     -15.571 -17.333  32.088  1.00 15.84      A    C  
ANISOU 2329  CA  ASP A 313     2185   1858   1976   -406   -103    164  A    C  
ATOM   2330  C   ASP A 313     -15.356 -16.302  33.180  1.00 16.08      A    C  
ANISOU 2330  C   ASP A 313     2194   1935   1980   -410    -78    161  A    C  
ATOM   2331  O   ASP A 313     -14.349 -15.613  33.187  1.00 16.36      A    O  
ANISOU 2331  O   ASP A 313     2223   1976   2017   -371    -79    151  A    O  
ATOM   2332  CB  ASP A 313     -14.270 -18.122  31.868  1.00 19.75      A    C  
ANISOU 2332  CB  ASP A 313     2720   2304   2479   -372   -139    178  A    C  
ATOM   2333  CG  ASP A 313     -13.848 -18.914  33.114  1.00 24.07      A    C  
ANISOU 2333  CG  ASP A 313     3305   2838   3001   -398   -157    217  A    C  
ATOM   2334  OD1 ASP A 313     -14.422 -18.716  34.211  1.00 19.34      A    O  
ANISOU 2334  OD1 ASP A 313     2701   2275   2373   -441   -139    232  A    O  
ATOM   2335  OD2 ASP A 313     -12.942 -19.745  32.977  1.00 24.51      A    O1-
ANISOU 2335  OD2 ASP A 313     3396   2850   3068   -374   -189    234  A    O1-
ATOM   2336  N   PRO A 314     -16.313 -16.180  34.095  1.00 15.36      A    N  
ANISOU 2336  N   PRO A 314     2090   1879   1866   -458    -54    169  A    N  
ATOM   2337  CA  PRO A 314     -16.209 -15.153  35.130  1.00 17.33      A    C  
ANISOU 2337  CA  PRO A 314     2320   2176   2088   -464    -25    160  A    C  
ATOM   2338  C   PRO A 314     -15.018 -15.317  36.042  1.00 15.70      A    C  
ANISOU 2338  C   PRO A 314     2146   1963   1857   -456    -44    182  A    C  
ATOM   2339  O   PRO A 314     -14.641 -14.355  36.741  1.00 17.33      A    O  
ANISOU 2339  O   PRO A 314     2337   2203   2044   -449    -27    170  A    O  
ATOM   2340  CB  PRO A 314     -17.524 -15.304  35.909  1.00 21.60      A    C  
ANISOU 2340  CB  PRO A 314     2848   2750   2608   -524      3    167  A    C  
ATOM   2341  CG  PRO A 314     -17.870 -16.731  35.733  1.00 20.64      A    C  
ANISOU 2341  CG  PRO A 314     2761   2592   2491   -556    -22    198  A    C  
ATOM   2342  CD  PRO A 314     -17.490 -17.039  34.303  1.00 18.03      A    C  
ANISOU 2342  CD  PRO A 314     2435   2216   2199   -514    -50    187  A    C  
ATOM   2343  N   ASP A 315     -14.385 -16.490  36.035  1.00 16.66      A    N  
ANISOU 2343  N   ASP A 315     2310   2040   1980   -455    -82    212  A    N  
ATOM   2344  CA  ASP A 315     -13.195 -16.705  36.821  1.00 17.17      A    C  
ANISOU 2344  CA  ASP A 315     2404   2094   2026   -442   -107    235  A    C  
ATOM   2345  C   ASP A 315     -11.903 -16.527  36.093  1.00 17.24      A    C  
ANISOU 2345  C   ASP A 315     2412   2076   2062   -382   -131    225  A    C  
ATOM   2346  O   ASP A 315     -10.812 -16.747  36.693  1.00 18.68      A    O  
ANISOU 2346  O   ASP A 315     2615   2247   2233   -367   -157    244  A    O  
ATOM   2347  CB  ASP A 315     -13.246 -18.078  37.437  1.00 20.14      A    C  
ANISOU 2347  CB  ASP A 315     2827   2437   2386   -479   -135    280  A    C  
ATOM   2348  CG  ASP A 315     -14.456 -18.243  38.347  1.00 21.59      A    C  
ANISOU 2348  CG  ASP A 315     3015   2654   2536   -546   -109    295  A    C  
ATOM   2349  OD1 ASP A 315     -14.800 -17.258  39.081  1.00 22.62      A    O  
ANISOU 2349  OD1 ASP A 315     3119   2837   2639   -564    -73    279  A    O  
ATOM   2350  OD2 ASP A 315     -15.057 -19.287  38.234  1.00 23.78      A    O1-
ANISOU 2350  OD2 ASP A 315     3316   2904   2816   -580   -121    318  A    O1-
ATOM   2351  N   ASP A 316     -12.007 -16.064  34.855  1.00 15.20      A    N  
ANISOU 2351  N   ASP A 316     2127   1811   1835   -349   -121    193  A    N  
ATOM   2352  CA  ASP A 316     -10.792 -15.824  34.066  1.00 15.55      A    C  
ANISOU 2352  CA  ASP A 316     2167   1835   1906   -291   -137    179  A    C  
ATOM   2353  C   ASP A 316     -10.922 -14.550  33.285  1.00 13.95      A    C  
ANISOU 2353  C   ASP A 316     1924   1659   1719   -266   -110    141  A    C  
ATOM   2354  O   ASP A 316     -10.601 -14.485  32.110  1.00 15.84      A    O  
ANISOU 2354  O   ASP A 316     2155   1877   1985   -230   -114    123  A    O  
ATOM   2355  CB  ASP A 316     -10.413 -16.982  33.161  1.00 18.77      A    C  
ANISOU 2355  CB  ASP A 316     2603   2187   2342   -269   -167    188  A    C  
ATOM   2356  CG  ASP A 316      -8.956 -16.839  32.578  1.00 22.15      A    C  
ANISOU 2356  CG  ASP A 316     3028   2595   2792   -211   -185    177  A    C  
ATOM   2357  OD1 ASP A 316      -8.111 -16.081  33.087  1.00 24.52      A    O  
ANISOU 2357  OD1 ASP A 316     3313   2920   3086   -193   -183    174  A    O  
ATOM   2358  OD2 ASP A 316      -8.722 -17.467  31.523  1.00 29.09      A    O1-
ANISOU 2358  OD2 ASP A 316     3918   3437   3699   -183   -198    168  A    O1-
ATOM   2359  N   GLU A 317     -11.416 -13.526  33.968  1.00 14.24      A    N  
ANISOU 2359  N   GLU A 317     1936   1740   1736   -285    -81    128  A    N  
ATOM   2360  CA  GLU A 317     -11.576 -12.174  33.390  1.00 12.78      A    C  
ANISOU 2360  CA  GLU A 317     1711   1580   1563   -262    -54     93  A    C  
ATOM   2361  C   GLU A 317     -10.962 -11.219  34.410  1.00 12.82      A    C  
ANISOU 2361  C   GLU A 317     1707   1618   1545   -262    -43     88  A    C  
ATOM   2362  O   GLU A 317     -11.668 -10.485  35.089  1.00 15.03      A    O  
ANISOU 2362  O   GLU A 317     1970   1934   1807   -286    -15     76  A    O  
ATOM   2363  CB  GLU A 317     -13.048 -11.898  33.063  1.00 13.85      A    C  
ANISOU 2363  CB  GLU A 317     1824   1735   1705   -287    -29     79  A    C  
ATOM   2364  CG  GLU A 317     -13.492 -12.726  31.860  1.00 15.64      A    C  
ANISOU 2364  CG  GLU A 317     2059   1927   1956   -281    -44     79  A    C  
ATOM   2365  CD  GLU A 317     -15.005 -12.806  31.650  1.00 16.54      A    C  
ANISOU 2365  CD  GLU A 317     2153   2055   2075   -315    -28     73  A    C  
ATOM   2366  OE1 GLU A 317     -15.788 -12.269  32.451  1.00 16.59      A    O  
ANISOU 2366  OE1 GLU A 317     2138   2099   2068   -343     -1     69  A    O  
ATOM   2367  OE2 GLU A 317     -15.415 -13.472  30.696  1.00 15.86      A    O1-
ANISOU 2367  OE2 GLU A 317     2075   1944   2009   -315    -42     74  A    O1-
ATOM   2368  N   PRO A 318      -9.625 -11.250  34.531  1.00 14.11      A    N  
ANISOU 2368  N   PRO A 318     1882   1770   1711   -234    -66     95  A    N  
ATOM   2369  CA  PRO A 318      -9.056 -10.622  35.720  1.00 15.14      A    C  
ANISOU 2369  CA  PRO A 318     2013   1929   1813   -245    -63     99  A    C  
ATOM   2370  C   PRO A 318      -9.018  -9.094  35.700  1.00 11.99      A    C  
ANISOU 2370  C   PRO A 318     1581   1560   1414   -233    -36     65  A    C  
ATOM   2371  O   PRO A 318      -9.103  -8.463  34.630  1.00 13.97      A    O  
ANISOU 2371  O   PRO A 318     1809   1806   1693   -206    -24     41  A    O  
ATOM   2372  CB  PRO A 318      -7.637 -11.184  35.782  1.00 16.67      A    C  
ANISOU 2372  CB  PRO A 318     2223   2098   2013   -219   -100    118  A    C  
ATOM   2373  CG  PRO A 318      -7.347 -11.658  34.404  1.00 18.42      A    C  
ANISOU 2373  CG  PRO A 318     2442   2284   2272   -182   -111    112  A    C  
ATOM   2374  CD  PRO A 318      -8.638 -11.963  33.727  1.00 16.23      A    C  
ANISOU 2374  CD  PRO A 318     2164   1999   2004   -198    -95    104  A    C  
ATOM   2375  N   VAL A 319      -8.846  -8.521  36.865  1.00 12.62      A    N  
ANISOU 2375  N   VAL A 319     1662   1670   1463   -253    -27     63  A    N  
ATOM   2376  CA  VAL A 319      -8.630  -7.084  37.011  1.00 14.69      A    C  
ANISOU 2376  CA  VAL A 319     1900   1957   1723   -242     -6     32  A    C  
ATOM   2377  C   VAL A 319      -7.186  -6.749  37.353  1.00 13.70      A    C  
ANISOU 2377  C   VAL A 319     1779   1833   1593   -225    -29     36  A    C  
ATOM   2378  O   VAL A 319      -6.381  -7.622  37.645  1.00 13.79      A    O  
ANISOU 2378  O   VAL A 319     1811   1829   1600   -221    -62     64  A    O  
ATOM   2379  CB  VAL A 319      -9.570  -6.453  38.046  1.00 17.04      A    C  
ANISOU 2379  CB  VAL A 319     2192   2293   1988   -279     27     18  A    C  
ATOM   2380  CG1 VAL A 319     -11.030  -6.682  37.631  1.00 22.73      A    C  
ANISOU 2380  CG1 VAL A 319     2900   3016   2719   -295     52     11  A    C  
ATOM   2381  CG2 VAL A 319      -9.280  -6.966  39.447  1.00 21.68      A    C  
ANISOU 2381  CG2 VAL A 319     2810   2897   2531   -314     14     42  A    C  
ATOM   2382  N   ALA A 320      -6.890  -5.478  37.224  1.00 12.21      A    N  
ANISOU 2382  N   ALA A 320     1568   1659   1412   -211    -13      8  A    N  
ATOM   2383  CA  ALA A 320      -5.561  -4.958  37.408  1.00 10.72      A    C  
ANISOU 2383  CA  ALA A 320     1376   1474   1225   -195    -30      5  A    C  
ATOM   2384  C   ALA A 320      -5.269  -4.546  38.822  1.00 12.14      A    C  
ANISOU 2384  C   ALA A 320     1568   1682   1364   -223    -34      6  A    C  
ATOM   2385  O   ALA A 320      -6.150  -4.139  39.563  1.00 14.48      A    O  
ANISOU 2385  O   ALA A 320     1867   2001   1632   -252     -8     -6  A    O  
ATOM   2386  CB  ALA A 320      -5.361  -3.758  36.490  1.00 14.37      A    C  
ANISOU 2386  CB  ALA A 320     1810   1934   1714   -168    -12    -25  A    C  
ATOM   2387  N   ASP A 321      -3.971  -4.522  39.159  1.00 14.37      A    N  
ANISOU 2387  N   ASP A 321     1852   1964   1643   -213    -64     17  A    N  
ATOM   2388  CA  ASP A 321      -3.513  -3.860  40.372  1.00 17.83      A    C  
ANISOU 2388  CA  ASP A 321     2299   2431   2046   -238    -68     10  A    C  
ATOM   2389  C   ASP A 321      -3.771  -2.340  40.211  1.00 18.05      A    C  
ANISOU 2389  C   ASP A 321     2306   2473   2079   -236    -35    -31  A    C  
ATOM   2390  O   ASP A 321      -3.906  -1.815  39.104  1.00 15.70      A    O  
ANISOU 2390  O   ASP A 321     1985   2161   1818   -210    -19    -50  A    O  
ATOM   2391  CB  ASP A 321      -2.025  -4.144  40.589  1.00 19.46      A    C  
ANISOU 2391  CB  ASP A 321     2505   2632   2256   -223   -112     30  A    C  
ATOM   2392  CG  ASP A 321      -1.748  -5.579  41.035  1.00 25.60      A    C  
ANISOU 2392  CG  ASP A 321     3309   3395   3022   -229   -149     73  A    C  
ATOM   2393  OD1 ASP A 321      -2.659  -6.280  41.481  1.00 28.10      A    O  
ANISOU 2393  OD1 ASP A 321     3650   3713   3316   -255   -143     89  A    O  
ATOM   2394  OD2 ASP A 321      -0.605  -6.036  40.873  1.00 36.83      A    O1-
ANISOU 2394  OD2 ASP A 321     4726   4804   4463   -205   -187     91  A    O1-
ATOM   2395  N   PRO A 322      -3.859  -1.617  41.328  1.00 21.89      A    N  
ANISOU 2395  N   PRO A 322     2801   2988   2528   -264    -24    -48  A    N  
ATOM   2396  CA  PRO A 322      -4.115  -0.184  41.182  1.00 20.47      A    C  
ANISOU 2396  CA  PRO A 322     2605   2817   2356   -260      7    -89  A    C  
ATOM   2397  C   PRO A 322      -2.904   0.498  40.539  1.00 16.76      A    C  
ANISOU 2397  C   PRO A 322     2117   2335   1917   -236    -10    -97  A    C  
ATOM   2398  O   PRO A 322      -1.786   0.061  40.743  1.00 21.93      A    O  
ANISOU 2398  O   PRO A 322     2774   2989   2570   -232    -46    -76  A    O  
ATOM   2399  CB  PRO A 322      -4.274   0.281  42.625  1.00 22.87      A    C  
ANISOU 2399  CB  PRO A 322     2928   3152   2608   -299     16   -102  A    C  
ATOM   2400  CG  PRO A 322      -3.454  -0.680  43.404  1.00 25.29      A    C  
ANISOU 2400  CG  PRO A 322     3258   3465   2887   -315    -26    -64  A    C  
ATOM   2401  CD  PRO A 322      -3.693  -2.018  42.736  1.00 27.33      A    C  
ANISOU 2401  CD  PRO A 322     3519   3699   3165   -300    -41    -30  A    C  
ATOM   2402  N   TYR A 323      -3.163   1.478  39.743  1.00 17.50      A    N  
ANISOU 2402  N   TYR A 323     2191   2419   2038   -218     13   -124  A    N  
ATOM   2403  CA  TYR A 323      -2.132   2.178  38.986  1.00 19.08      A    C  
ANISOU 2403  CA  TYR A 323     2373   2606   2269   -196      3   -133  A    C  
ATOM   2404  C   TYR A 323      -2.106   3.623  39.525  1.00 19.88      A    C  
ANISOU 2404  C   TYR A 323     2473   2719   2360   -210     21   -168  A    C  
ATOM   2405  O   TYR A 323      -3.107   4.350  39.454  1.00 20.44      A    O  
ANISOU 2405  O   TYR A 323     2543   2790   2434   -211     53   -195  A    O  
ATOM   2406  CB  TYR A 323      -2.463   2.134  37.507  1.00 18.25      A    C  
ANISOU 2406  CB  TYR A 323     2250   2477   2206   -165     16   -134  A    C  
ATOM   2407  CG  TYR A 323      -1.620   3.009  36.580  1.00 17.76      A    C  
ANISOU 2407  CG  TYR A 323     2171   2402   2177   -145     15   -145  A    C  
ATOM   2408  CD1 TYR A 323      -0.264   2.735  36.336  1.00 21.74      A    C  
ANISOU 2408  CD1 TYR A 323     2664   2904   2692   -134    -12   -130  A    C  
ATOM   2409  CD2 TYR A 323      -2.162   4.106  35.970  1.00 21.04      A    C  
ANISOU 2409  CD2 TYR A 323     2577   2807   2610   -136     41   -171  A    C  
ATOM   2410  CE1 TYR A 323       0.488   3.586  35.514  1.00 19.53      A    C  
ANISOU 2410  CE1 TYR A 323     2365   2615   2439   -121     -9   -141  A    C  
ATOM   2411  CE2 TYR A 323      -1.410   4.943  35.136  1.00 25.68      A    C  
ANISOU 2411  CE2 TYR A 323     3151   3381   3224   -122     40   -179  A    C  
ATOM   2412  CZ  TYR A 323      -0.088   4.666  34.900  1.00 17.47      A    C  
ANISOU 2412  CZ  TYR A 323     2102   2343   2193   -117     17   -164  A    C  
ATOM   2413  OH  TYR A 323       0.609   5.575  34.064  1.00 20.02      A    O  
ANISOU 2413  OH  TYR A 323     2411   2656   2541   -108     22   -173  A    O  
ATOM   2414  N   ASP A 324      -0.948   4.023  39.986  1.00 21.21      A    N  
ANISOU 2414  N   ASP A 324     2642   2896   2521   -219     -3   -169  A    N  
ATOM   2415  CA  ASP A 324      -0.808   5.360  40.627  1.00 19.65      A    C  
ANISOU 2415  CA  ASP A 324     2448   2708   2309   -238      9   -202  A    C  
ATOM   2416  C   ASP A 324      -0.521   6.373  39.548  1.00 20.39      A    C  
ANISOU 2416  C   ASP A 324     2523   2780   2445   -217     21   -220  A    C  
ATOM   2417  O   ASP A 324       0.607   6.388  39.036  1.00 20.59      A    O  
ANISOU 2417  O   ASP A 324     2534   2799   2490   -207     -1   -208  A    O  
ATOM   2418  CB  ASP A 324       0.256   5.306  41.645  1.00 21.11      A    C  
ANISOU 2418  CB  ASP A 324     2643   2913   2465   -262    -23   -195  A    C  
ATOM   2419  CG  ASP A 324       0.488   6.694  42.344  1.00 19.70      A    C  
ANISOU 2419  CG  ASP A 324     2473   2743   2269   -285    -15   -231  A    C  
ATOM   2420  OD1 ASP A 324      -0.074   7.683  41.872  1.00 20.64      A    O  
ANISOU 2420  OD1 ASP A 324     2587   2848   2408   -276     15   -261  A    O  
ATOM   2421  OD2 ASP A 324       1.189   6.692  43.345  1.00 30.38      A    O1-
ANISOU 2421  OD2 ASP A 324     3838   4116   3589   -310    -40   -229  A    O1-
ATOM   2422  N   GLN A 325      -1.490   7.190  39.191  1.00 17.81      A    N  
ANISOU 2422  N   GLN A 325     2196   2442   2130   -210     53   -248  A    N  
ATOM   2423  CA  GLN A 325      -1.252   8.220  38.205  1.00 22.98      A    C  
ANISOU 2423  CA  GLN A 325     2837   3074   2822   -194     63   -262  A    C  
ATOM   2424  C   GLN A 325      -1.172   9.643  38.716  1.00 17.60      A    C  
ANISOU 2424  C   GLN A 325     2163   2389   2135   -208     75   -299  A    C  
ATOM   2425  O   GLN A 325      -1.341  10.624  37.960  1.00 20.82      A    O  
ANISOU 2425  O   GLN A 325     2565   2772   2573   -195     89   -316  A    O  
ATOM   2426  CB  GLN A 325      -2.107   8.084  36.987  1.00 36.43      A    C  
ANISOU 2426  CB  GLN A 325     4529   4755   4556   -165     80   -259  A    C  
ATOM   2427  CG  GLN A 325      -3.572   8.012  37.182  1.00 39.55      A    C  
ANISOU 2427  CG  GLN A 325     4929   5153   4947   -163    108   -272  A    C  
ATOM   2428  CD  GLN A 325      -4.212   7.581  35.877  1.00 61.27      A    C  
ANISOU 2428  CD  GLN A 325     7667   7884   7728   -136    113   -258  A    C  
ATOM   2429  NE2 GLN A 325      -5.366   6.965  35.959  1.00 42.68      A    N  
ANISOU 2429  NE2 GLN A 325     5311   5536   5369   -135    126   -256  A    N  
ATOM   2430  OE1 GLN A 325      -3.632   7.769  34.804  1.00 51.60      A    O  
ANISOU 2430  OE1 GLN A 325     6434   6641   6531   -119    104   -248  A    O  
ATOM   2431  N   SER A 326      -0.807   9.708  39.960  1.00 17.82      A    N  
ANISOU 2431  N   SER A 326     2205   2437   2126   -237     65   -308  A    N  
ATOM   2432  CA  SER A 326      -0.617  10.992  40.634  1.00 18.67      A    C  
ANISOU 2432  CA  SER A 326     2327   2545   2223   -257     72   -344  A    C  
ATOM   2433  C   SER A 326       0.489  11.789  39.989  1.00 18.51      A    C  
ANISOU 2433  C   SER A 326     2296   2507   2231   -256     57   -344  A    C  
ATOM   2434  O   SER A 326       0.445  12.989  40.065  1.00 17.34      A    O  
ANISOU 2434  O   SER A 326     2155   2343   2091   -263     68   -376  A    O  
ATOM   2435  CB  SER A 326      -0.393  10.817  42.104  1.00 17.40      A    C  
ANISOU 2435  CB  SER A 326     2187   2413   2010   -291     61   -352  A    C  
ATOM   2436  OG  SER A 326       0.758  10.085  42.431  1.00 18.65      A    O  
ANISOU 2436  OG  SER A 326     2342   2589   2155   -304     21   -321  A    O  
ATOM   2437  N   PHE A 327       1.465  11.130  39.344  1.00 16.79      A    N  
ANISOU 2437  N   PHE A 327     2058   2290   2030   -248     31   -312  A    N  
ATOM   2438  CA  PHE A 327       2.493  11.900  38.602  1.00 15.57      A    C  
ANISOU 2438  CA  PHE A 327     1890   2121   1906   -247     21   -313  A    C  
ATOM   2439  C   PHE A 327       1.951  12.861  37.573  1.00 16.18      A    C  
ANISOU 2439  C   PHE A 327     1965   2165   2017   -230     47   -328  A    C  
ATOM   2440  O   PHE A 327       2.569  13.861  37.202  1.00 14.37      A    O  
ANISOU 2440  O   PHE A 327     1734   1919   1807   -239     45   -338  A    O  
ATOM   2441  CB  PHE A 327       3.531  10.969  37.946  1.00 15.09      A    C  
ANISOU 2441  CB  PHE A 327     1804   2068   1862   -235     -3   -277  A    C  
ATOM   2442  CG  PHE A 327       3.072  10.276  36.703  1.00 15.90      A    C  
ANISOU 2442  CG  PHE A 327     1895   2156   1991   -202      9   -256  A    C  
ATOM   2443  CD1 PHE A 327       3.240  10.878  35.435  1.00 16.70      A    C  
ANISOU 2443  CD1 PHE A 327     1984   2234   2126   -188     22   -257  A    C  
ATOM   2444  CD2 PHE A 327       2.431   9.042  36.798  1.00 17.15      A    C  
ANISOU 2444  CD2 PHE A 327     2057   2322   2137   -189      8   -238  A    C  
ATOM   2445  CE1 PHE A 327       2.800  10.216  34.291  1.00 17.43      A    C  
ANISOU 2445  CE1 PHE A 327     2069   2314   2239   -159     32   -239  A    C  
ATOM   2446  CE2 PHE A 327       2.027   8.395  35.636  1.00 20.08      A    C  
ANISOU 2446  CE2 PHE A 327     2418   2679   2532   -160     17   -222  A    C  
ATOM   2447  CZ  PHE A 327       2.217   8.994  34.414  1.00 17.97      A    C  
ANISOU 2447  CZ  PHE A 327     2140   2391   2296   -146     30   -224  A    C  
ATOM   2448  N   GLU A 328       0.755  12.563  37.067  1.00 15.71      A    N  
ANISOU 2448  N   GLU A 328     1907   2094   1967   -207     69   -327  A    N  
ATOM   2449  CA  GLU A 328       0.221  13.351  36.004  1.00 16.07      A    C  
ANISOU 2449  CA  GLU A 328     1951   2107   2046   -187     87   -337  A    C  
ATOM   2450  C   GLU A 328      -0.084  14.759  36.430  1.00 16.48      A    C  
ANISOU 2450  C   GLU A 328     2019   2140   2101   -199    101   -373  A    C  
ATOM   2451  O   GLU A 328      -0.113  15.659  35.572  1.00 22.36      A    O  
ANISOU 2451  O   GLU A 328     2765   2855   2876   -189    109   -379  A    O  
ATOM   2452  CB  GLU A 328      -1.083  12.706  35.468  1.00 16.07      A    C  
ANISOU 2452  CB  GLU A 328     1949   2103   2054   -161    105   -329  A    C  
ATOM   2453  CG  GLU A 328      -0.876  11.381  34.719  1.00 18.05      A    C  
ANISOU 2453  CG  GLU A 328     2186   2362   2310   -145     93   -293  A    C  
ATOM   2454  CD  GLU A 328      -0.228  11.547  33.369  1.00 19.01      A    C  
ANISOU 2454  CD  GLU A 328     2296   2466   2461   -131     89   -276  A    C  
ATOM   2455  OE1 GLU A 328       0.203  12.661  32.963  1.00 19.84      A    O  
ANISOU 2455  OE1 GLU A 328     2403   2552   2583   -136     91   -287  A    O  
ATOM   2456  OE2 GLU A 328      -0.204  10.516  32.626  1.00 19.77      A    O1-
ANISOU 2456  OE2 GLU A 328     2383   2564   2563   -114     83   -252  A    O1-
ATOM   2457  N   SER A 329      -0.276  14.953  37.726  1.00 18.49      A    N  
ANISOU 2457  N   SER A 329     2289   2411   2324   -220    104   -398  A    N  
ATOM   2458  CA ASER A 329      -0.587  16.239  38.385  0.50 18.83      A    C  
ANISOU 2458  CA ASER A 329     2352   2438   2364   -232    119   -441  A    C  
ATOM   2459  CA BSER A 329      -0.566  16.311  38.233  0.50 21.33      A    C  
ANISOU 2459  CA BSER A 329     2668   2752   2686   -230    119   -439  A    C  
ATOM   2460  C   SER A 329       0.679  16.993  38.788  1.00 25.54      A    C  
ANISOU 2460  C   SER A 329     3209   3287   3209   -264     98   -450  A    C  
ATOM   2461  O   SER A 329       0.615  18.124  39.294  1.00 25.08      A    O  
ANISOU 2461  O   SER A 329     3170   3211   3149   -278    106   -485  A    O  
ATOM   2462  CB ASER A 329      -1.414  15.966  39.640  0.50 19.17      A    C  
ANISOU 2462  CB ASER A 329     2409   2506   2369   -242    135   -464  A    C  
ATOM   2463  CB BSER A 329      -1.689  16.275  39.237  0.50 23.78      A    C  
ANISOU 2463  CB BSER A 329     2991   3075   2971   -232    142   -469  A    C  
ATOM   2464  OG ASER A 329      -0.641  15.417  40.710  0.50 24.40      A    O  
ANISOU 2464  OG ASER A 329     3080   3202   2990   -273    114   -458  A    O  
ATOM   2465  OG BSER A 329      -2.871  15.855  38.584  0.50 24.64      A    O  
ANISOU 2465  OG BSER A 329     3088   3176   3098   -200    162   -462  A    O  
ATOM   2466  N   ARG A 330       1.828  16.350  38.626  1.00 18.02      A    N  
ANISOU 2466  N   ARG A 330     2242   2353   2253   -274     71   -419  A    N  
ATOM   2467  CA  ARG A 330       3.105  16.971  39.098  1.00 19.46      A    C  
ANISOU 2467  CA  ARG A 330     2425   2539   2428   -308     47   -426  A    C  
ATOM   2468  C   ARG A 330       3.858  17.823  38.104  1.00 18.50      A    C  
ANISOU 2468  C   ARG A 330     2295   2392   2344   -312     42   -421  A    C  
ATOM   2469  O   ARG A 330       3.755  17.599  36.924  1.00 20.60      A    O  
ANISOU 2469  O   ARG A 330     2547   2643   2638   -288     51   -399  A    O  
ATOM   2470  CB  ARG A 330       4.009  15.916  39.705  1.00 17.73      A    C  
ANISOU 2470  CB  ARG A 330     2194   2361   2184   -324     16   -400  A    C  
ATOM   2471  CG  ARG A 330       3.317  15.367  40.931  1.00 20.69      A    C  
ANISOU 2471  CG  ARG A 330     2587   2759   2512   -333     20   -412  A    C  
ATOM   2472  CD  ARG A 330       4.188  14.640  41.918  1.00 26.50      A    C  
ANISOU 2472  CD  ARG A 330     3323   3532   3213   -358    -15   -396  A    C  
ATOM   2473  NE  ARG A 330       3.271  14.071  42.890  1.00 28.81      A    N  
ANISOU 2473  NE  ARG A 330     3638   3846   3464   -363     -4   -404  A    N  
ATOM   2474  CZ  ARG A 330       2.816  12.799  42.876  1.00 23.40      A    C  
ANISOU 2474  CZ  ARG A 330     2947   3175   2768   -347     -5   -375  A    C  
ATOM   2475  NH1 ARG A 330       1.972  12.455  43.786  1.00 26.66      A    N1+
ANISOU 2475  NH1 ARG A 330     3382   3605   3141   -358      8   -385  A    N1+
ATOM   2476  NH2 ARG A 330       3.340  11.902  42.084  1.00 24.20      A    N  
ANISOU 2476  NH2 ARG A 330     3024   3277   2892   -327    -23   -337  A    N  
ATOM   2477  N   ASP A 331       4.603  18.796  38.640  1.00 20.06      A    N  
ANISOU 2477  N   ASP A 331     2503   2583   2537   -345     31   -442  A    N  
ATOM   2478  CA  ASP A 331       5.443  19.739  37.842  1.00 23.84      A    C  
ANISOU 2478  CA  ASP A 331     2975   3035   3047   -358     25   -439  A    C  
ATOM   2479  C   ASP A 331       6.843  19.555  38.337  1.00 18.26      A    C  
ANISOU 2479  C   ASP A 331     2251   2358   2329   -393     -7   -428  A    C  
ATOM   2480  O   ASP A 331       7.199  20.024  39.414  1.00 21.02      A    O  
ANISOU 2480  O   ASP A 331     2616   2717   2654   -424    -22   -452  A    O  
ATOM   2481  CB  ASP A 331       5.000  21.201  38.061  1.00 34.48      A    C  
ANISOU 2481  CB  ASP A 331     4353   4342   4404   -371     38   -478  A    C  
ATOM   2482  CG  ASP A 331       3.575  21.473  37.545  1.00 41.27      A    C  
ANISOU 2482  CG  ASP A 331     5229   5170   5283   -333     68   -490  A    C  
ATOM   2483  OD1 ASP A 331       3.278  21.113  36.401  1.00 41.88      A    O  
ANISOU 2483  OD1 ASP A 331     5292   5238   5385   -306     77   -463  A    O  
ATOM   2484  OD2 ASP A 331       2.757  22.042  38.295  1.00 66.89      A    O1-
ANISOU 2484  OD2 ASP A 331     8497   8401   8515   -332     84   -528  A    O1-
ATOM   2485  N   LEU A 332       7.606  18.800  37.528  1.00 16.61      A    N  
ANISOU 2485  N   LEU A 332     2009   2166   2137   -383    -17   -391  A    N  
ATOM   2486  CA  LEU A 332       8.946  18.399  37.940  1.00 16.38      A    C  
ANISOU 2486  CA  LEU A 332     1952   2169   2101   -408    -49   -376  A    C  
ATOM   2487  C   LEU A 332       9.931  18.928  36.927  1.00 16.73      A    C  
ANISOU 2487  C   LEU A 332     1972   2203   2180   -420    -50   -362  A    C  
ATOM   2488  O   LEU A 332       9.552  19.310  35.789  1.00 18.41      A    O  
ANISOU 2488  O   LEU A 332     2187   2386   2419   -403    -26   -355  A    O  
ATOM   2489  CB  LEU A 332       9.067  16.886  38.098  1.00 16.08      A    C  
ANISOU 2489  CB  LEU A 332     1894   2167   2050   -386    -64   -347  A    C  
ATOM   2490  CG  LEU A 332       8.060  16.228  39.031  1.00 17.53      A    C  
ANISOU 2490  CG  LEU A 332     2102   2363   2199   -375    -61   -356  A    C  
ATOM   2491  CD1 LEU A 332       8.269  14.741  39.025  1.00 17.65      A    C  
ANISOU 2491  CD1 LEU A 332     2094   2404   2205   -354    -77   -322  A    C  
ATOM   2492  CD2 LEU A 332       8.204  16.718  40.455  1.00 17.39      A    C  
ANISOU 2492  CD2 LEU A 332     2106   2358   2143   -411    -78   -382  A    C  
ATOM   2493  N   LEU A 333      11.182  18.930  37.334  1.00 16.91      A    N  
ANISOU 2493  N   LEU A 333     1970   2251   2202   -450    -78   -355  A    N  
ATOM   2494  CA  LEU A 333      12.260  19.352  36.448  1.00 17.86      A    C  
ANISOU 2494  CA  LEU A 333     2060   2371   2355   -467    -79   -341  A    C  
ATOM   2495  C   LEU A 333      12.618  18.227  35.493  1.00 17.71      A    C  
ANISOU 2495  C   LEU A 333     2003   2372   2354   -435    -74   -306  A    C  
ATOM   2496  O   LEU A 333      12.376  17.032  35.739  1.00 19.24      A    O  
ANISOU 2496  O   LEU A 333     2188   2588   2535   -406    -82   -292  A    O  
ATOM   2497  CB  LEU A 333      13.491  19.774  37.247  1.00 20.51      A    C  
ANISOU 2497  CB  LEU A 333     2377   2728   2686   -513   -113   -347  A    C  
ATOM   2498  CG  LEU A 333      13.210  20.873  38.231  1.00 20.66      A    C  
ANISOU 2498  CG  LEU A 333     2437   2728   2684   -549   -120   -385  A    C  
ATOM   2499  CD1 LEU A 333      14.477  21.136  39.018  1.00 28.76      A    C  
ANISOU 2499  CD1 LEU A 333     3442   3782   3703   -594   -160   -389  A    C  
ATOM   2500  CD2 LEU A 333      12.692  22.148  37.554  1.00 25.03      A    C  
ANISOU 2500  CD2 LEU A 333     3020   3231   3258   -556    -93   -402  A    C  
ATOM   2501  N   ILE A 334      13.235  18.599  34.393  1.00 18.09      A    N  
ANISOU 2501  N   ILE A 334     2029   2412   2431   -440    -61   -293  A    N  
ATOM   2502  CA  ILE A 334      13.587  17.657  33.399  1.00 16.65      A    C  
ANISOU 2502  CA  ILE A 334     1813   2246   2267   -411    -50   -266  A    C  
ATOM   2503  C   ILE A 334      14.472  16.499  33.940  1.00 15.83      A    C  
ANISOU 2503  C   ILE A 334     1669   2187   2161   -403    -78   -250  A    C  
ATOM   2504  O   ILE A 334      14.245  15.341  33.630  1.00 18.28      A    O  
ANISOU 2504  O   ILE A 334     1966   2507   2471   -366    -76   -233  A    O  
ATOM   2505  CB  ILE A 334      14.243  18.397  32.191  1.00 19.27      A    C  
ANISOU 2505  CB  ILE A 334     2128   2565   2626   -429    -29   -256  A    C  
ATOM   2506  CG1 ILE A 334      14.373  17.481  31.008  1.00 21.99      A    C  
ANISOU 2506  CG1 ILE A 334     2447   2921   2986   -395     -9   -232  A    C  
ATOM   2507  CG2 ILE A 334      15.583  19.027  32.596  1.00 22.46      A    C  
ANISOU 2507  CG2 ILE A 334     2502   2990   3042   -477    -50   -259  A    C  
ATOM   2508  CD1 ILE A 334      14.891  18.200  29.764  1.00 21.51      A    C  
ANISOU 2508  CD1 ILE A 334     2376   2850   2948   -414     17   -222  A    C  
ATOM   2509  N   ASP A 335      15.437  16.836  34.786  1.00 16.43      A    N  
ANISOU 2509  N   ASP A 335     1725   2284   2233   -440   -109   -255  A    N  
ATOM   2510  CA  ASP A 335      16.331  15.788  35.322  1.00 18.54      A    C  
ANISOU 2510  CA  ASP A 335     1951   2592   2502   -431   -142   -239  A    C  
ATOM   2511  C   ASP A 335      15.590  14.869  36.278  1.00 19.84      A    C  
ANISOU 2511  C   ASP A 335     2138   2764   2634   -409   -161   -237  A    C  
ATOM   2512  O   ASP A 335      15.997  13.719  36.490  1.00 18.09      A    O  
ANISOU 2512  O   ASP A 335     1891   2568   2414   -386   -183   -218  A    O  
ATOM   2513  CB  ASP A 335      17.600  16.335  35.938  1.00 20.53      A    C  
ANISOU 2513  CB  ASP A 335     2171   2870   2761   -475   -175   -243  A    C  
ATOM   2514  CG  ASP A 335      18.585  16.824  34.875  1.00 40.10      A    C  
ANISOU 2514  CG  ASP A 335     4608   5353   5277   -492   -157   -235  A    C  
ATOM   2515  OD1 ASP A 335      18.487  16.374  33.704  1.00 40.51      A    O  
ANISOU 2515  OD1 ASP A 335     4645   5401   5347   -462   -125   -221  A    O  
ATOM   2516  OD2 ASP A 335      19.456  17.638  35.211  1.00 46.62      A    O1-
ANISOU 2516  OD2 ASP A 335     5415   6189   6110   -537   -174   -244  A    O1-
ATOM   2517  N   GLU A 336      14.530  15.371  36.886  1.00 15.80      A    N  
ANISOU 2517  N   GLU A 336     1677   2232   2095   -417   -153   -258  A    N  
ATOM   2518  CA  GLU A 336      13.693  14.533  37.779  1.00 15.77      A    C  
ANISOU 2518  CA  GLU A 336     1700   2234   2057   -399   -165   -258  A    C  
ATOM   2519  C   GLU A 336      12.866  13.524  36.994  1.00 16.10      A    C  
ANISOU 2519  C   GLU A 336     1744   2266   2105   -352   -141   -240  A    C  
ATOM   2520  O   GLU A 336      12.844  12.342  37.302  1.00 16.32      A    O  
ANISOU 2520  O   GLU A 336     1766   2311   2125   -330   -158   -221  A    O  
ATOM   2521  CB  GLU A 336      12.818  15.409  38.668  1.00 15.76      A    C  
ANISOU 2521  CB  GLU A 336     1748   2217   2024   -423   -159   -289  A    C  
ATOM   2522  CG  GLU A 336      13.597  16.225  39.634  1.00 18.68      A    C  
ANISOU 2522  CG  GLU A 336     2120   2599   2380   -470   -188   -307  A    C  
ATOM   2523  CD  GLU A 336      12.729  17.160  40.493  1.00 23.62      A    C  
ANISOU 2523  CD  GLU A 336     2798   3205   2974   -494   -179   -345  A    C  
ATOM   2524  OE1 GLU A 336      11.889  17.942  39.960  1.00 20.60      A    O  
ANISOU 2524  OE1 GLU A 336     2441   2787   2602   -486   -144   -364  A    O  
ATOM   2525  OE2 GLU A 336      12.951  17.149  41.736  1.00 30.03      A    O1-
ANISOU 2525  OE2 GLU A 336     3623   4038   3749   -520   -208   -356  A    O1-
ATOM   2526  N   TRP A 337      12.207  13.957  35.940  1.00 14.72      A    N  
ANISOU 2526  N   TRP A 337     1582   2063   1947   -338   -105   -244  A    N  
ATOM   2527  CA  TRP A 337      11.552  13.015  35.094  1.00 14.95      A    C  
ANISOU 2527  CA  TRP A 337     1611   2084   1985   -297    -85   -228  A    C  
ATOM   2528  C   TRP A 337      12.514  11.960  34.551  1.00 14.45      A    C  
ANISOU 2528  C   TRP A 337     1504   2042   1944   -275    -97   -202  A    C  
ATOM   2529  O   TRP A 337      12.182  10.818  34.437  1.00 15.53      A    O  
ANISOU 2529  O   TRP A 337     1640   2184   2078   -244    -99   -187  A    O  
ATOM   2530  CB  TRP A 337      10.812  13.684  33.927  1.00 15.50      A    C  
ANISOU 2530  CB  TRP A 337     1697   2121   2071   -286    -47   -235  A    C  
ATOM   2531  CG  TRP A 337       9.637  14.515  34.340  1.00 14.39      A    C  
ANISOU 2531  CG  TRP A 337     1598   1955   1915   -293    -33   -259  A    C  
ATOM   2532  CD1 TRP A 337       9.501  15.858  34.167  1.00 16.13      A    C  
ANISOU 2532  CD1 TRP A 337     1836   2149   2142   -315    -20   -278  A    C  
ATOM   2533  CD2 TRP A 337       8.415  14.059  34.947  1.00 13.71      A    C  
ANISOU 2533  CD2 TRP A 337     1539   1865   1805   -278    -27   -266  A    C  
ATOM   2534  CE2 TRP A 337       7.597  15.202  35.125  1.00 13.13      A    C  
ANISOU 2534  CE2 TRP A 337     1496   1765   1728   -288    -10   -294  A    C  
ATOM   2535  CE3 TRP A 337       7.965  12.824  35.394  1.00 15.18      A    C  
ANISOU 2535  CE3 TRP A 337     1727   2067   1972   -258    -36   -254  A    C  
ATOM   2536  NE1 TRP A 337       8.275  16.287  34.636  1.00 17.63      A    N  
ANISOU 2536  NE1 TRP A 337     2062   2318   2318   -309     -6   -300  A    N  
ATOM   2537  CZ2 TRP A 337       6.344  15.129  35.733  1.00 14.04      A    C  
ANISOU 2537  CZ2 TRP A 337     1639   1872   1822   -279      2   -311  A    C  
ATOM   2538  CZ3 TRP A 337       6.706  12.760  35.966  1.00 16.10      A    C  
ANISOU 2538  CZ3 TRP A 337     1873   2177   2067   -252    -24   -267  A    C  
ATOM   2539  CH2 TRP A 337       5.945  13.894  36.159  1.00 14.35      A    C  
ANISOU 2539  CH2 TRP A 337     1676   1932   1842   -263     -5   -296  A    C  
ATOM   2540  N   LYS A 338      13.708  12.407  34.137  1.00 14.10      A    N  
ANISOU 2540  N   LYS A 338     1424   2012   1924   -292   -101   -199  A    N  
ATOM   2541  CA  LYS A 338      14.745  11.491  33.634  1.00 15.71      A    C  
ANISOU 2541  CA  LYS A 338     1579   2237   2151   -271   -110   -179  A    C  
ATOM   2542  C   LYS A 338      15.134  10.451  34.705  1.00 17.02      A    C  
ANISOU 2542  C   LYS A 338     1732   2429   2305   -262   -153   -166  A    C  
ATOM   2543  O   LYS A 338      15.220   9.247  34.445  1.00 15.80      A    O  
ANISOU 2543  O   LYS A 338     1562   2279   2160   -225   -158   -148  A    O  
ATOM   2544  CB  LYS A 338      15.974  12.283  33.175  1.00 19.23      A    C  
ANISOU 2544  CB  LYS A 338     1985   2697   2623   -298   -108   -181  A    C  
ATOM   2545  CG  LYS A 338      17.032  11.396  32.531  1.00 21.75      A    C  
ANISOU 2545  CG  LYS A 338     2250   3041   2972   -274   -110   -164  A    C  
ATOM   2546  CD  LYS A 338      18.186  12.207  31.905  1.00 26.38      A    C  
ANISOU 2546  CD  LYS A 338     2794   3641   3587   -303    -98   -166  A    C  
ATOM   2547  CE  LYS A 338      19.507  11.489  32.085  1.00 56.51      A    C  
ANISOU 2547  CE  LYS A 338     6548   7495   7429   -295   -124   -154  A    C  
ATOM   2548  NZ  LYS A 338      20.614  12.096  31.296  1.00 54.05      A    N1+
ANISOU 2548  NZ  LYS A 338     6187   7201   7147   -317   -104   -155  A    N1+
ATOM   2549  N   SER A 339      15.406  10.918  35.916  1.00 17.55      A    N  
ANISOU 2549  N   SER A 339     1808   2509   2352   -295   -184   -174  A    N  
ATOM   2550  CA  SER A 339      15.785  10.043  37.006  1.00 20.11      A    C  
ANISOU 2550  CA  SER A 339     2124   2856   2660   -291   -229   -160  A    C  
ATOM   2551  C   SER A 339      14.668   9.065  37.384  1.00 20.13      A    C  
ANISOU 2551  C   SER A 339     2165   2849   2637   -266   -229   -151  A    C  
ATOM   2552  O   SER A 339      14.909   7.900  37.581  1.00 18.35      A    O  
ANISOU 2552  O   SER A 339     1926   2632   2413   -240   -252   -129  A    O  
ATOM   2553  CB  SER A 339      16.161  10.884  38.226  1.00 22.22      A    C  
ANISOU 2553  CB  SER A 339     2402   3139   2903   -339   -259   -175  A    C  
ATOM   2554  OG  SER A 339      16.621  10.025  39.245  1.00 27.41      A    O  
ANISOU 2554  OG  SER A 339     3051   3820   3544   -337   -307   -157  A    O  
ATOM   2555  N   LEU A 340      13.420   9.529  37.442  1.00 16.50      A    N  
ANISOU 2555  N   LEU A 340     1749   2366   2153   -271   -201   -167  A    N  
ATOM   2556  CA  LEU A 340      12.279   8.624  37.666  1.00 15.45      A    C  
ANISOU 2556  CA  LEU A 340     1650   2223   1997   -248   -194   -159  A    C  
ATOM   2557  C   LEU A 340      12.207   7.524  36.607  1.00 15.92      A    C  
ANISOU 2557  C   LEU A 340     1691   2273   2084   -205   -182   -139  A    C  
ATOM   2558  O   LEU A 340      11.992   6.373  36.899  1.00 15.39      A    O  
ANISOU 2558  O   LEU A 340     1631   2208   2009   -183   -198   -119  A    O  
ATOM   2559  CB  LEU A 340      10.993   9.411  37.670  1.00 16.61      A    C  
ANISOU 2559  CB  LEU A 340     1837   2349   2126   -258   -161   -183  A    C  
ATOM   2560  CG  LEU A 340      10.802  10.255  38.931  1.00 18.42      A    C  
ANISOU 2560  CG  LEU A 340     2095   2585   2320   -298   -172   -205  A    C  
ATOM   2561  CD1 LEU A 340       9.703  11.264  38.714  1.00 16.40      A    C  
ANISOU 2561  CD1 LEU A 340     1870   2304   2057   -304   -135   -234  A    C  
ATOM   2562  CD2 LEU A 340      10.517   9.430  40.167  1.00 20.01      A    C  
ANISOU 2562  CD2 LEU A 340     2317   2805   2481   -305   -200   -194  A    C  
ATOM   2563  N   THR A 341      12.446   7.905  35.359  1.00 15.52      A    N  
ANISOU 2563  N   THR A 341     1621   2211   2064   -193   -153   -143  A    N  
ATOM   2564  CA  THR A 341      12.495   6.939  34.254  1.00 14.66      A    C  
ANISOU 2564  CA  THR A 341     1495   2095   1981   -153   -138   -129  A    C  
ATOM   2565  C   THR A 341      13.605   5.941  34.412  1.00 14.43      A    C  
ANISOU 2565  C   THR A 341     1427   2085   1971   -134   -170   -109  A    C  
ATOM   2566  O   THR A 341      13.375   4.728  34.252  1.00 14.93      A    O  
ANISOU 2566  O   THR A 341     1494   2141   2038   -100   -177    -93  A    O  
ATOM   2567  CB  THR A 341      12.566   7.654  32.883  1.00 15.03      A    C  
ANISOU 2567  CB  THR A 341     1530   2128   2052   -149    -99   -138  A    C  
ATOM   2568  CG2 THR A 341      12.524   6.662  31.757  1.00 15.77      A    C  
ANISOU 2568  CG2 THR A 341     1613   2214   2165   -110    -82   -126  A    C  
ATOM   2569  OG1 THR A 341      11.465   8.578  32.757  1.00 16.91      A    O  
ANISOU 2569  OG1 THR A 341     1806   2345   2275   -164    -74   -155  A    O  
ATOM   2570  N   TYR A 342      14.816   6.433  34.677  1.00 15.93      A    N  
ANISOU 2570  N   TYR A 342     1580   2298   2176   -152   -189   -110  A    N  
ATOM   2571  CA  TYR A 342      15.982   5.583  34.911  1.00 19.56      A    C  
ANISOU 2571  CA  TYR A 342     1995   2778   2658   -134   -224    -93  A    C  
ATOM   2572  C   TYR A 342      15.659   4.565  35.985  1.00 18.31      A    C  
ANISOU 2572  C   TYR A 342     1859   2621   2476   -124   -263    -74  A    C  
ATOM   2573  O   TYR A 342      15.875   3.345  35.821  1.00 19.77      A    O  
ANISOU 2573  O   TYR A 342     2033   2803   2678    -87   -279    -55  A    O  
ATOM   2574  CB  TYR A 342      17.187   6.449  35.244  1.00 18.98      A    C  
ANISOU 2574  CB  TYR A 342     1882   2731   2597   -167   -242    -99  A    C  
ATOM   2575  CG  TYR A 342      18.491   5.673  35.232  1.00 20.61      A    C  
ANISOU 2575  CG  TYR A 342     2032   2962   2839   -144   -273    -83  A    C  
ATOM   2576  CD1 TYR A 342      18.991   5.156  34.031  1.00 22.06      A    C  
ANISOU 2576  CD1 TYR A 342     2176   3145   3060   -109   -246    -81  A    C  
ATOM   2577  CD2 TYR A 342      19.158   5.419  36.394  1.00 24.47      A    C  
ANISOU 2577  CD2 TYR A 342     2505   3473   3321   -156   -326    -71  A    C  
ATOM   2578  CE1 TYR A 342      20.172   4.429  34.004  1.00 24.47      A    C  
ANISOU 2578  CE1 TYR A 342     2424   3471   3401    -84   -272    -69  A    C  
ATOM   2579  CE2 TYR A 342      20.332   4.695  36.385  1.00 24.62      A    C  
ANISOU 2579  CE2 TYR A 342     2466   3511   3374   -132   -357    -56  A    C  
ATOM   2580  CZ  TYR A 342      20.823   4.197  35.190  1.00 27.16      A    C  
ANISOU 2580  CZ  TYR A 342     2749   3833   3739    -94   -328    -56  A    C  
ATOM   2581  OH  TYR A 342      22.027   3.488  35.152  1.00 27.71      A    O  
ANISOU 2581  OH  TYR A 342     2756   3924   3850    -67   -357    -44  A    O  
ATOM   2582  N   ASP A 343      15.086   5.028  37.077  1.00 17.33      A    N  
ANISOU 2582  N   ASP A 343     1773   2500   2313   -156   -279    -79  A    N  
ATOM   2583  CA  ASP A 343      14.802   4.127  38.181  1.00 18.22      A    C  
ANISOU 2583  CA  ASP A 343     1910   2617   2396   -154   -317    -60  A    C  
ATOM   2584  C   ASP A 343      13.804   3.022  37.769  1.00 18.56      A    C  
ANISOU 2584  C   ASP A 343     1981   2634   2435   -121   -301    -47  A    C  
ATOM   2585  O   ASP A 343      13.920   1.862  38.167  1.00 21.51      A    O  
ANISOU 2585  O   ASP A 343     2358   3007   2809   -101   -332    -23  A    O  
ATOM   2586  CB  ASP A 343      14.308   4.880  39.395  1.00 26.30      A    C  
ANISOU 2586  CB  ASP A 343     2971   3649   3373   -198   -329    -72  A    C  
ATOM   2587  CG  ASP A 343      15.424   5.691  40.085  1.00 24.60      A    C  
ANISOU 2587  CG  ASP A 343     2729   3460   3156   -234   -363    -79  A    C  
ATOM   2588  OD1 ASP A 343      16.644   5.603  39.718  1.00 27.73      A    O  
ANISOU 2588  OD1 ASP A 343     3074   3871   3589   -224   -380    -71  A    O  
ATOM   2589  OD2 ASP A 343      15.057   6.462  40.956  1.00 32.89      A    O1-
ANISOU 2589  OD2 ASP A 343     3811   4517   4170   -271   -367    -95  A    O1-
ATOM   2590  N   GLU A 344      12.842   3.360  36.916  1.00 15.06      A    N  
ANISOU 2590  N   GLU A 344     1558   2171   1993   -116   -255    -62  A    N  
ATOM   2591  CA  GLU A 344      11.914   2.371  36.416  1.00 15.65      A    C  
ANISOU 2591  CA  GLU A 344     1657   2223   2067    -87   -239    -52  A    C  
ATOM   2592  C   GLU A 344      12.544   1.374  35.426  1.00 16.19      A    C  
ANISOU 2592  C   GLU A 344     1694   2281   2174    -43   -239    -40  A    C  
ATOM   2593  O   GLU A 344      12.103   0.217  35.339  1.00 17.20      A    O  
ANISOU 2593  O   GLU A 344     1839   2392   2304    -18   -246    -23  A    O  
ATOM   2594  CB  GLU A 344      10.684   3.064  35.767  1.00 14.18      A    C  
ANISOU 2594  CB  GLU A 344     1499   2019   1872    -94   -192    -73  A    C  
ATOM   2595  CG  GLU A 344       9.785   3.847  36.733  1.00 17.47      A    C  
ANISOU 2595  CG  GLU A 344     1952   2439   2248   -129   -186    -88  A    C  
ATOM   2596  CD  GLU A 344       8.852   2.967  37.532  1.00 19.56      A    C  
ANISOU 2596  CD  GLU A 344     2251   2700   2480   -131   -197    -74  A    C  
ATOM   2597  OE1 GLU A 344       8.590   1.805  37.142  1.00 18.74      A    O  
ANISOU 2597  OE1 GLU A 344     2152   2582   2386   -104   -201    -55  A    O  
ATOM   2598  OE2 GLU A 344       8.329   3.450  38.547  1.00 22.56      A    O1-
ANISOU 2598  OE2 GLU A 344     2658   3090   2824   -161   -200    -83  A    O1-
ATOM   2599  N   VAL A 345      13.559   1.808  34.691  1.00 17.86      A    N  
ANISOU 2599  N   VAL A 345     1862   2504   2419    -36   -230    -48  A    N  
ATOM   2600  CA  VAL A 345      14.321   0.883  33.828  1.00 17.13      A    C  
ANISOU 2600  CA  VAL A 345     1735   2408   2367      6   -230    -39  A    C  
ATOM   2601  C   VAL A 345      15.039  -0.109  34.740  1.00 18.07      A    C  
ANISOU 2601  C   VAL A 345     1839   2535   2491     21   -282    -15  A    C  
ATOM   2602  O   VAL A 345      14.965  -1.312  34.542  1.00 19.23      A    O  
ANISOU 2602  O   VAL A 345     1992   2664   2652     57   -293     -1  A    O  
ATOM   2603  CB  VAL A 345      15.290   1.623  32.880  1.00 17.77      A    C  
ANISOU 2603  CB  VAL A 345     1768   2503   2480      7   -205    -55  A    C  
ATOM   2604  CG1 VAL A 345      16.184   0.600  32.158  1.00 20.61      A    C  
ANISOU 2604  CG1 VAL A 345     2088   2864   2880     52   -208    -48  A    C  
ATOM   2605  CG2 VAL A 345      14.548   2.506  31.908  1.00 18.25      A    C  
ANISOU 2605  CG2 VAL A 345     1850   2551   2534     -5   -155    -74  A    C  
ATOM   2606  N   ILE A 346      15.718   0.411  35.767  1.00 19.64      A    N  
ANISOU 2606  N   ILE A 346     2023   2758   2681     -7   -317    -11  A    N  
ATOM   2607  CA  ILE A 346      16.570  -0.424  36.656  1.00 22.84      A    C  
ANISOU 2607  CA  ILE A 346     2408   3175   3094      7   -375     14  A    C  
ATOM   2608  C   ILE A 346      15.743  -1.463  37.387  1.00 23.27      A    C  
ANISOU 2608  C   ILE A 346     2511   3211   3121     13   -400     37  A    C  
ATOM   2609  O   ILE A 346      16.205  -2.600  37.603  1.00 27.03      A    O  
ANISOU 2609  O   ILE A 346     2977   3678   3614     45   -437     61  A    O  
ATOM   2610  CB  ILE A 346      17.328   0.466  37.686  1.00 26.18      A    C  
ANISOU 2610  CB  ILE A 346     2813   3630   3502    -35   -409     13  A    C  
ATOM   2611  CG1 ILE A 346      18.353   1.369  36.995  1.00 31.24      A    C  
ANISOU 2611  CG1 ILE A 346     3398   4292   4178    -42   -391     -5  A    C  
ATOM   2612  CG2 ILE A 346      18.019  -0.399  38.750  1.00 36.98      A    C  
ANISOU 2612  CG2 ILE A 346     4171   5009   4870    -26   -476     43  A    C  
ATOM   2613  CD1 ILE A 346      19.262   0.666  36.020  1.00 35.52      A    C  
ANISOU 2613  CD1 ILE A 346     3887   4836   4774      4   -384     -3  A    C  
ATOM   2614  N   SER A 347      14.553  -1.074  37.836  1.00 21.29      A    N  
ANISOU 2614  N   SER A 347     2311   2953   2825    -17   -384     32  A    N  
ATOM   2615  CA  SER A 347      13.676  -1.912  38.638  1.00 19.09      A    C  
ANISOU 2615  CA  SER A 347     2081   2660   2512    -22   -404     52  A    C  
ATOM   2616  C   SER A 347      12.836  -2.940  37.868  1.00 17.97      A    C  
ANISOU 2616  C   SER A 347     1963   2485   2381     10   -382     60  A    C  
ATOM   2617  O   SER A 347      12.144  -3.771  38.449  1.00 22.08      A    O  
ANISOU 2617  O   SER A 347     2523   2990   2876      7   -398     79  A    O  
ATOM   2618  CB  SER A 347      12.750  -1.045  39.486  1.00 22.17      A    C  
ANISOU 2618  CB  SER A 347     2513   3061   2851    -69   -391     40  A    C  
ATOM   2619  OG  SER A 347      11.764  -0.390  38.643  1.00 21.99      A    O  
ANISOU 2619  OG  SER A 347     2504   3024   2825    -73   -335     14  A    O  
ATOM   2620  N   PHE A 348      12.847  -2.862  36.535  1.00 20.46      A    N  
ANISOU 2620  N   PHE A 348     2258   2788   2729     36   -342     42  A    N  
ATOM   2621  CA  PHE A 348      12.089  -3.767  35.709  1.00 18.05      A    C  
ANISOU 2621  CA  PHE A 348     1974   2451   2434     64   -320     44  A    C  
ATOM   2622  C   PHE A 348      12.437  -5.223  35.990  1.00 18.36      A    C  
ANISOU 2622  C   PHE A 348     2017   2469   2488     96   -361     73  A    C  
ATOM   2623  O   PHE A 348      13.645  -5.567  36.048  1.00 19.19      A    O  
ANISOU 2623  O   PHE A 348     2084   2583   2626    121   -391     82  A    O  
ATOM   2624  CB  PHE A 348      12.345  -3.473  34.209  1.00 18.51      A    C  
ANISOU 2624  CB  PHE A 348     2004   2502   2527     89   -278     21  A    C  
ATOM   2625  CG  PHE A 348      11.623  -4.417  33.297  1.00 15.60      A    C  
ANISOU 2625  CG  PHE A 348     1657   2101   2168    119   -258     21  A    C  
ATOM   2626  CD1 PHE A 348      10.250  -4.324  33.151  1.00 17.43      A    C  
ANISOU 2626  CD1 PHE A 348     1932   2319   2374    102   -233     15  A    C  
ATOM   2627  CD2 PHE A 348      12.265  -5.454  32.669  1.00 16.60      A    C  
ANISOU 2627  CD2 PHE A 348     1765   2211   2331    162   -266     26  A    C  
ATOM   2628  CE1 PHE A 348       9.550  -5.198  32.348  1.00 17.55      A    C  
ANISOU 2628  CE1 PHE A 348     1968   2303   2396    124   -217     16  A    C  
ATOM   2629  CE2 PHE A 348      11.609  -6.324  31.868  1.00 17.44      A    C  
ANISOU 2629  CE2 PHE A 348     1895   2285   2445    187   -249     25  A    C  
ATOM   2630  CZ  PHE A 348      10.235  -6.202  31.675  1.00 17.54      A    C  
ANISOU 2630  CZ  PHE A 348     1950   2284   2429    166   -225     19  A    C  
ATOM   2631  N   VAL A 349      11.406  -6.021  36.192  1.00 17.89      A    N  
ANISOU 2631  N   VAL A 349     2004   2387   2408     94   -362     87  A    N  
ATOM   2632  CA  VAL A 349      11.495  -7.475  36.358  1.00 20.16      A    C  
ANISOU 2632  CA  VAL A 349     2307   2644   2709    123   -397    114  A    C  
ATOM   2633  C   VAL A 349      10.797  -8.121  35.179  1.00 17.71      A    C  
ANISOU 2633  C   VAL A 349     2012   2300   2416    150   -363    104  A    C  
ATOM   2634  O   VAL A 349       9.585  -7.872  34.949  1.00 22.27      A    O  
ANISOU 2634  O   VAL A 349     2622   2872   2969    127   -331     94  A    O  
ATOM   2635  CB  VAL A 349      10.812  -7.945  37.652  1.00 24.66      A    C  
ANISOU 2635  CB  VAL A 349     2924   3210   3234     92   -430    144  A    C  
ATOM   2636  CG1 VAL A 349      11.057  -9.436  37.824  1.00 27.79      A    C  
ANISOU 2636  CG1 VAL A 349     3337   3574   3649    123   -470    175  A    C  
ATOM   2637  CG2 VAL A 349      11.314  -7.150  38.850  1.00 27.93      A    C  
ANISOU 2637  CG2 VAL A 349     3332   3661   3620     57   -457    149  A    C  
ATOM   2638  N   PRO A 350      11.527  -8.934  34.432  1.00 24.96      A    N  
ANISOU 2638  N   PRO A 350     2907   3198   3378    196   -370    103  A    N  
ATOM   2639  CA  PRO A 350      10.906  -9.567  33.265  1.00 25.76      A    C  
ANISOU 2639  CA  PRO A 350     3026   3268   3495    220   -338     91  A    C  
ATOM   2640  C   PRO A 350       9.797 -10.535  33.622  1.00 30.00      A    C  
ANISOU 2640  C   PRO A 350     3617   3772   4010    210   -350    111  A    C  
ATOM   2641  O   PRO A 350       9.763 -11.059  34.740  1.00 27.36      A    O  
ANISOU 2641  O   PRO A 350     3305   3433   3657    196   -392    141  A    O  
ATOM   2642  CB  PRO A 350      12.068 -10.299  32.590  1.00 36.24      A    C  
ANISOU 2642  CB  PRO A 350     4317   4581   4873    274   -349     86  A    C  
ATOM   2643  CG  PRO A 350      13.149 -10.351  33.578  1.00 32.64      A    C  
ANISOU 2643  CG  PRO A 350     3832   4143   4429    279   -396    107  A    C  
ATOM   2644  CD  PRO A 350      12.963  -9.200  34.525  1.00 26.46      A    C  
ANISOU 2644  CD  PRO A 350     3051   3397   3606    228   -402    111  A    C  
ATOM   2645  N   PRO A 351       8.873 -10.755  32.690  1.00 27.74      A    N  
ANISOU 2645  N   PRO A 351     3353   3464   3722    213   -316     95  A    N  
ATOM   2646  CA  PRO A 351       7.852 -11.769  32.892  1.00 36.85      A    C  
ANISOU 2646  CA  PRO A 351     4557   4584   4861    204   -327    114  A    C  
ATOM   2647  C   PRO A 351       8.481 -13.169  32.853  1.00 32.96      A    C  
ANISOU 2647  C   PRO A 351     4069   4053   4400    245   -363    132  A    C  
ATOM   2648  O   PRO A 351       9.596 -13.313  32.360  1.00 35.44      A    O  
ANISOU 2648  O   PRO A 351     4346   4365   4753    285   -368    122  A    O  
ATOM   2649  CB  PRO A 351       6.885 -11.531  31.724  1.00 41.91      A    C  
ANISOU 2649  CB  PRO A 351     5209   5215   5500    201   -280     88  A    C  
ATOM   2650  CG  PRO A 351       7.713 -10.857  30.680  1.00 31.79      A    C  
ANISOU 2650  CG  PRO A 351     3885   3949   4245    226   -252     58  A    C  
ATOM   2651  CD  PRO A 351       8.708 -10.035  31.398  1.00 24.82      A    C  
ANISOU 2651  CD  PRO A 351     2967   3102   3364    219   -266     61  A    C  
TER   
END



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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.