CNRS Nantes University UFIP UFIP
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***    ***

elNémo ID: 190719103646101225

Job options:

ID        	=	 190719103646101225
JOBID     	=	 
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

ATOM      1  N   ALA A  15      17.242  86.193  48.898  1.00 63.48           N1+
ATOM      2  CA  ALA A  15      18.258  86.864  49.774  1.00 63.54           C  
ATOM      3  C   ALA A  15      19.000  87.902  48.895  1.00 64.58           C  
ATOM      4  O   ALA A  15      19.150  89.043  49.330  1.00 64.94           O  
ATOM      5  CB  ALA A  15      19.182  85.838  50.461  1.00  0.00           C  
ATOM      6  N   THR A  16      19.454  87.492  47.700  1.00 65.68           N  
ATOM      7  CA  THR A  16      20.187  88.244  46.689  1.00 67.45           C  
ATOM      8  C   THR A  16      21.600  88.640  47.159  1.00 68.38           C  
ATOM      9  O   THR A  16      21.764  89.514  48.013  1.00 68.05           O  
ATOM     10  CB  THR A  16      19.397  89.465  46.149  1.00  0.00           C  
ATOM     11  OG1 THR A  16      18.158  88.988  45.643  1.00  0.00           O  
ATOM     12  CG2 THR A  16      20.095  90.228  45.010  1.00  0.00           C  
ATOM     13  N   ALA A  17      22.596  87.948  46.589  1.00 69.49           N  
ATOM     14  CA  ALA A  17      24.017  88.179  46.817  1.00 70.57           C  
ATOM     15  C   ALA A  17      24.455  89.586  46.379  1.00 71.77           C  
ATOM     16  O   ALA A  17      23.913  90.128  45.413  1.00 71.40           O  
ATOM     17  CB  ALA A  17      24.810  87.117  46.039  1.00  0.00           C  
ATOM     18  N   MET A  18      25.452  90.132  47.082  1.00 73.14           N  
ATOM     19  CA  MET A  18      26.061  91.428  46.784  1.00 74.55           C  
ATOM     20  C   MET A  18      26.805  91.380  45.426  1.00 76.18           C  
ATOM     21  O   MET A  18      27.713  90.553  45.306  1.00 76.21           O  
ATOM     22  CB  MET A  18      27.036  91.757  47.942  1.00  0.00           C  
ATOM     23  CG  MET A  18      27.836  93.063  47.777  1.00  0.00           C  
ATOM     24  SD  MET A  18      26.817  94.561  47.685  1.00  0.00           S  
ATOM     25  CE  MET A  18      28.084  95.763  47.196  1.00  0.00           C  
ATOM     26  N   PRO A  19      26.438  92.232  44.438  1.00 77.77           N  
ATOM     27  CA  PRO A  19      27.207  92.326  43.183  1.00 79.11           C  
ATOM     28  C   PRO A  19      28.629  92.871  43.418  1.00 79.51           C  
ATOM     29  O   PRO A  19      28.811  93.775  44.235  1.00 79.29           O  
ATOM     30  CD  PRO A  19      25.324  93.188  44.452  1.00  0.00           C  
ATOM     31  CB  PRO A  19      26.358  93.258  42.302  1.00  0.00           C  
ATOM     32  CG  PRO A  19      25.589  94.129  43.282  1.00  0.00           C  
ATOM     33  N   ALA A  20      29.612  92.288  42.724  1.00 80.02           N  
ATOM     34  CA  ALA A  20      31.019  92.660  42.843  1.00 80.48           C  
ATOM     35  C   ALA A  20      31.311  94.069  42.300  1.00 81.00           C  
ATOM     36  O   ALA A  20      30.702  94.500  41.319  1.00 80.96           O  
ATOM     37  CB  ALA A  20      31.877  91.627  42.100  1.00  0.00           C  
ATOM     38  N   GLU A  21      32.291  94.726  42.926  1.00 81.59           N  
ATOM     39  CA  GLU A  21      32.905  95.959  42.446  1.00 82.12           C  
ATOM     40  C   GLU A  21      33.795  95.659  41.223  1.00 82.48           C  
ATOM     41  O   GLU A  21      34.377  94.578  41.151  1.00 82.61           O  
ATOM     42  CB  GLU A  21      33.693  96.565  43.631  1.00  0.00           C  
ATOM     43  CG  GLU A  21      34.493  97.855  43.368  1.00  0.00           C  
ATOM     44  CD  GLU A  21      33.623  99.000  42.863  1.00  0.00           C  
ATOM     45  OE1 GLU A  21      33.047  99.706  43.715  1.00  0.00           O  
ATOM     46  OE2 GLU A  21      33.536  99.133  41.626  1.00  0.00           O1-
ATOM     47  N   HIS A  22      33.894  96.621  40.301  1.00 83.03           N  
ATOM     48  CA  HIS A  22      34.672  96.518  39.065  1.00 83.47           C  
ATOM     49  C   HIS A  22      36.045  97.204  39.172  1.00 83.66           C  
ATOM     50  O   HIS A  22      36.913  96.910  38.352  1.00 83.50           O  
ATOM     51  CB  HIS A  22      33.860  97.126  37.902  1.00  0.00           C  
ATOM     52  CG  HIS A  22      33.441  98.566  38.099  1.00  0.00           C  
ATOM     53  ND1 HIS A  22      32.226  98.934  38.653  1.00  0.00           N  
ATOM     54  CD2 HIS A  22      34.086  99.749  37.811  1.00  0.00           C  
ATOM     55  CE1 HIS A  22      32.194 100.267  38.704  1.00  0.00           C  
ATOM     56  NE2 HIS A  22      33.292 100.827  38.207  1.00  0.00           N  
ATOM     57  N   VAL A  23      36.224  98.114  40.145  1.00 84.11           N  
ATOM     58  CA  VAL A  23      37.476  98.832  40.395  1.00 84.41           C  
ATOM     59  C   VAL A  23      38.640  97.859  40.682  1.00 84.12           C  
ATOM     60  O   VAL A  23      38.480  96.935  41.489  1.00 84.03           O  
ATOM     61  CB  VAL A  23      37.317  99.845  41.569  1.00  0.00           C  
ATOM     62  CG1 VAL A  23      38.628 100.421  42.151  1.00  0.00           C  
ATOM     63  CG2 VAL A  23      36.397 101.007  41.150  1.00  0.00           C  
ATOM     64  N   ALA A  24      39.788  98.097  40.023  1.00 83.70           N  
ATOM     65  CA  ALA A  24      40.858  97.115  39.898  1.00 83.31           C  
ATOM     66  C   ALA A  24      41.517  96.734  41.224  1.00 82.96           C  
ATOM     67  O   ALA A  24      42.209  95.716  41.304  1.00 82.70           O  
ATOM     68  CB  ALA A  24      41.914  97.622  38.919  1.00 83.50           C  
ATOM     69  N   VAL A  25      41.370  97.598  42.233  1.00 82.43           N  
ATOM     70  CA  VAL A  25      41.917  97.411  43.571  1.00 82.05           C  
ATOM     71  C   VAL A  25      41.058  96.421  44.386  1.00 81.62           C  
ATOM     72  O   VAL A  25      41.594  95.687  45.214  1.00 81.29           O  
ATOM     73  CB  VAL A  25      41.961  98.775  44.327  1.00  0.00           C  
ATOM     74  CG1 VAL A  25      42.507  98.691  45.768  1.00  0.00           C  
ATOM     75  CG2 VAL A  25      42.764  99.830  43.540  1.00  0.00           C  
ATOM     76  N   GLN A  26      39.740  96.421  44.139  1.00 81.35           N  
ATOM     77  CA  GLN A  26      38.777  95.668  44.932  1.00 81.09           C  
ATOM     78  C   GLN A  26      38.550  94.260  44.361  1.00 80.31           C  
ATOM     79  O   GLN A  26      38.361  93.329  45.145  1.00 80.15           O  
ATOM     80  CB  GLN A  26      37.468  96.483  45.029  1.00  0.00           C  
ATOM     81  CG  GLN A  26      36.364  95.883  45.926  1.00  0.00           C  
ATOM     82  CD  GLN A  26      36.803  95.692  47.375  1.00  0.00           C  
ATOM     83  OE1 GLN A  26      36.786  96.629  48.164  1.00  0.00           O  
ATOM     84  NE2 GLN A  26      37.211  94.484  47.732  1.00  0.00           N  
ATOM     85  N   VAL A  27      38.578  94.127  43.025  1.00 79.42           N  
ATOM     86  CA  VAL A  27      38.351  92.867  42.306  1.00 78.35           C  
ATOM     87  C   VAL A  27      39.183  91.648  42.803  1.00 78.07           C  
ATOM     88  O   VAL A  27      38.578  90.606  43.061  1.00 77.83           O  
ATOM     89  CB  VAL A  27      38.489  93.066  40.757  1.00  0.00           C  
ATOM     90  CG1 VAL A  27      38.766  91.792  39.934  1.00  0.00           C  
ATOM     91  CG2 VAL A  27      37.261  93.790  40.187  1.00  0.00           C  
ATOM     92  N   PRO A  28      40.520  91.776  42.985  1.00 77.72           N  
ATOM     93  CA  PRO A  28      41.341  90.647  43.453  1.00 77.68           C  
ATOM     94  C   PRO A  28      41.277  90.368  44.966  1.00 77.84           C  
ATOM     95  O   PRO A  28      41.932  89.427  45.395  1.00 77.81           O  
ATOM     96  CD  PRO A  28      41.382  92.892  42.603  1.00  0.00           C  
ATOM     97  CB  PRO A  28      42.780  91.021  43.024  1.00  0.00           C  
ATOM     98  CG  PRO A  28      42.640  92.212  42.089  1.00  0.00           C  
ATOM     99  N   ALA A  29      40.522  91.150  45.754  1.00 78.07           N  
ATOM    100  CA  ALA A  29      40.463  90.998  47.211  1.00 78.51           C  
ATOM    101  C   ALA A  29      39.860  89.689  47.787  1.00 78.61           C  
ATOM    102  O   ALA A  29      40.330  89.284  48.849  1.00 78.28           O  
ATOM    103  CB  ALA A  29      39.790  92.224  47.841  1.00  0.00           C  
ATOM    104  N   PRO A  30      38.890  89.011  47.123  1.00 79.01           N  
ATOM    105  CA  PRO A  30      38.381  87.705  47.603  1.00 79.39           C  
ATOM    106  C   PRO A  30      39.312  86.496  47.365  1.00 79.19           C  
ATOM    107  O   PRO A  30      38.844  85.364  47.491  1.00 79.57           O  
ATOM    108  CD  PRO A  30      38.047  89.506  46.037  1.00  0.00           C  
ATOM    109  CB  PRO A  30      37.034  87.529  46.867  1.00  0.00           C  
ATOM    110  CG  PRO A  30      36.681  88.901  46.318  1.00  0.00           C  
ATOM    111  N   GLU A  31      40.573  86.728  46.995  1.00 78.78           N  
ATOM    112  CA  GLU A  31      41.591  85.726  46.700  1.00 78.45           C  
ATOM    113  C   GLU A  31      42.869  86.156  47.451  1.00 78.22           C  
ATOM    114  O   GLU A  31      43.049  87.358  47.672  1.00 78.60           O  
ATOM    115  CB  GLU A  31      41.832  85.743  45.172  1.00  0.00           C  
ATOM    116  CG  GLU A  31      40.612  85.309  44.329  1.00  0.00           C  
ATOM    117  CD  GLU A  31      40.800  85.631  42.850  1.00  0.00           C  
ATOM    118  OE1 GLU A  31      41.690  85.012  42.230  1.00  0.00           O  
ATOM    119  OE2 GLU A  31      40.047  86.503  42.366  1.00  0.00           O1-
ATOM    120  N   PRO A  32      43.754  85.203  47.826  1.00 77.86           N  
ATOM    121  CA  PRO A  32      45.085  85.564  48.343  1.00 77.35           C  
ATOM    122  C   PRO A  32      45.940  86.260  47.274  1.00 77.32           C  
ATOM    123  O   PRO A  32      45.877  85.888  46.103  1.00 77.16           O  
ATOM    124  CD  PRO A  32      43.595  83.751  47.714  1.00  0.00           C  
ATOM    125  CB  PRO A  32      45.714  84.215  48.748  1.00  0.00           C  
ATOM    126  CG  PRO A  32      45.003  83.184  47.895  1.00  0.00           C  
ATOM    127  N   THR A  33      46.791  87.199  47.705  1.00 77.10           N  
ATOM    128  CA  THR A  33      47.951  87.594  46.910  1.00 77.29           C  
ATOM    129  C   THR A  33      48.920  86.378  46.887  1.00 77.40           C  
ATOM    130  O   THR A  33      49.265  85.890  47.969  1.00 77.28           O  
ATOM    131  CB  THR A  33      48.619  88.865  47.508  1.00  0.00           C  
ATOM    132  OG1 THR A  33      49.728  89.263  46.724  1.00  0.00           O  
ATOM    133  CG2 THR A  33      49.111  88.772  48.965  1.00  0.00           C  
ATOM    134  N   PRO A  34      49.174  85.786  45.697  1.00 77.56           N  
ATOM    135  CA  PRO A  34      49.719  84.421  45.611  1.00 77.87           C  
ATOM    136  C   PRO A  34      51.128  84.290  46.213  1.00 77.97           C  
ATOM    137  O   PRO A  34      52.040  85.010  45.811  1.00 77.90           O  
ATOM    138  CD  PRO A  34      48.852  86.318  44.371  1.00  0.00           C  
ATOM    139  CB  PRO A  34      49.673  84.100  44.113  1.00  0.00           C  
ATOM    140  CG  PRO A  34      49.631  85.442  43.401  1.00  0.00           C  
ATOM    141  N   GLY A  35      51.264  83.383  47.186  1.00 45.49           N  
ATOM    142  CA  GLY A  35      52.470  83.247  48.002  1.00 46.48           C  
ATOM    143  C   GLY A  35      52.591  84.413  49.003  1.00 46.57           C  
ATOM    144  O   GLY A  35      53.610  85.102  48.959  1.00 47.48           O  
ATOM    145  N   PRO A  36      51.585  84.675  49.876  1.00 46.56           N  
ATOM    146  CA  PRO A  36      51.592  85.858  50.760  1.00 46.60           C  
ATOM    147  C   PRO A  36      52.689  85.808  51.839  1.00 45.94           C  
ATOM    148  O   PRO A  36      53.230  86.844  52.217  1.00 45.45           O  
ATOM    149  CD  PRO A  36      50.449  83.795  50.176  1.00  0.00           C  
ATOM    150  CB  PRO A  36      50.181  85.851  51.374  1.00  0.00           C  
ATOM    151  CG  PRO A  36      49.784  84.382  51.420  1.00  0.00           C  
ATOM    152  N   VAL A  37      52.995  84.591  52.295  1.00 45.12           N  
ATOM    153  CA  VAL A  37      54.035  84.224  53.234  1.00 45.15           C  
ATOM    154  C   VAL A  37      54.091  82.680  53.206  1.00 44.68           C  
ATOM    155  O   VAL A  37      53.214  82.054  52.603  1.00 44.85           O  
ATOM    156  CB  VAL A  37      53.713  84.730  54.678  1.00  0.00           C  
ATOM    157  CG1 VAL A  37      52.590  83.940  55.385  1.00  0.00           C  
ATOM    158  CG2 VAL A  37      54.973  84.822  55.557  1.00  0.00           C  
ATOM    159  N   ARG A  38      55.091  82.099  53.886  1.00 43.43           N  
ATOM    160  CA  ARG A  38      55.243  80.673  54.222  1.00 42.93           C  
ATOM    161  C   ARG A  38      55.184  79.713  53.013  1.00 42.14           C  
ATOM    162  O   ARG A  38      54.854  78.543  53.180  1.00 42.83           O  
ATOM    163  CB  ARG A  38      54.325  80.291  55.427  1.00  0.00           C  
ATOM    164  CG  ARG A  38      52.849  79.922  55.146  1.00  0.00           C  
ATOM    165  CD  ARG A  38      51.968  79.806  56.406  1.00  0.00           C  
ATOM    166  NE  ARG A  38      51.628  81.117  56.980  1.00  0.00           N  
ATOM    167  CZ  ARG A  38      51.188  81.353  58.226  1.00  0.00           C  
ATOM    168  NH1 ARG A  38      51.047  80.356  59.107  1.00  0.00           N  
ATOM    169  NH2 ARG A  38      50.891  82.611  58.571  1.00  0.00           N1+
ATOM    170  N   ILE A  39      55.490  80.239  51.824  1.00 42.35           N  
ATOM    171  CA  ILE A  39      55.409  79.579  50.531  1.00 41.75           C  
ATOM    172  C   ILE A  39      56.744  78.883  50.210  1.00 41.87           C  
ATOM    173  O   ILE A  39      57.780  79.547  50.214  1.00 42.26           O  
ATOM    174  CB  ILE A  39      55.003  80.618  49.438  1.00  0.00           C  
ATOM    175  CG1 ILE A  39      54.868  80.027  48.020  1.00  0.00           C  
ATOM    176  CG2 ILE A  39      55.878  81.891  49.392  1.00  0.00           C  
ATOM    177  CD1 ILE A  39      53.886  78.855  47.936  1.00  0.00           C  
ATOM    178  N   LEU A  40      56.705  77.560  49.996  1.00 78.79           N  
ATOM    179  CA  LEU A  40      57.905  76.748  49.779  1.00 79.21           C  
ATOM    180  C   LEU A  40      57.657  75.624  48.765  1.00 79.18           C  
ATOM    181  O   LEU A  40      58.431  75.463  47.821  1.00 79.45           O  
ATOM    182  CB  LEU A  40      58.393  76.128  51.117  1.00  0.00           C  
ATOM    183  CG  LEU A  40      59.069  77.094  52.115  1.00  0.00           C  
ATOM    184  CD1 LEU A  40      59.400  76.368  53.433  1.00  0.00           C  
ATOM    185  CD2 LEU A  40      60.321  77.783  51.534  1.00  0.00           C  
ATOM    186  N   ARG A  41      56.611  74.820  48.999  1.00 78.85           N  
ATOM    187  CA  ARG A  41      56.448  73.505  48.376  1.00 78.16           C  
ATOM    188  C   ARG A  41      56.052  73.520  46.894  1.00 77.14           C  
ATOM    189  O   ARG A  41      56.032  72.453  46.285  1.00 76.61           O  
ATOM    190  CB  ARG A  41      55.522  72.609  49.225  1.00  0.00           C  
ATOM    191  CG  ARG A  41      56.034  72.302  50.645  1.00  0.00           C  
ATOM    192  CD  ARG A  41      57.383  71.573  50.616  1.00  0.00           C  
ATOM    193  NE  ARG A  41      57.774  71.024  51.917  1.00  0.00           N  
ATOM    194  CZ  ARG A  41      59.003  70.568  52.206  1.00  0.00           C  
ATOM    195  NH1 ARG A  41      59.988  70.610  51.298  1.00  0.00           N  
ATOM    196  NH2 ARG A  41      59.245  70.059  53.416  1.00  0.00           N1+
ATOM    197  N   THR A  42      55.845  74.700  46.303  1.00 76.09           N  
ATOM    198  CA  THR A  42      55.689  74.891  44.863  1.00 75.42           C  
ATOM    199  C   THR A  42      56.871  74.325  44.039  1.00 74.92           C  
ATOM    200  O   THR A  42      56.661  73.801  42.948  1.00 74.77           O  
ATOM    201  CB  THR A  42      55.563  76.397  44.519  1.00  0.00           C  
ATOM    202  OG1 THR A  42      54.956  77.089  45.597  1.00  0.00           O  
ATOM    203  CG2 THR A  42      54.739  76.660  43.250  1.00  0.00           C  
ATOM    204  N   ALA A  43      58.082  74.361  44.622  1.00 74.28           N  
ATOM    205  CA  ALA A  43      59.287  73.738  44.077  1.00 73.64           C  
ATOM    206  C   ALA A  43      59.177  72.206  43.966  1.00 72.77           C  
ATOM    207  O   ALA A  43      59.666  71.628  42.997  1.00 72.44           O  
ATOM    208  CB  ALA A  43      60.485  74.122  44.956  1.00  0.00           C  
ATOM    209  N   GLN A  44      58.503  71.578  44.939  1.00 71.84           N  
ATOM    210  CA  GLN A  44      58.197  70.153  44.911  1.00 71.02           C  
ATOM    211  C   GLN A  44      57.066  69.841  43.917  1.00 69.88           C  
ATOM    212  O   GLN A  44      57.159  68.835  43.218  1.00 69.33           O  
ATOM    213  CB  GLN A  44      57.921  69.602  46.329  1.00  0.00           C  
ATOM    214  CG  GLN A  44      59.188  69.340  47.175  1.00  0.00           C  
ATOM    215  CD  GLN A  44      59.938  70.603  47.594  1.00  0.00           C  
ATOM    216  OE1 GLN A  44      59.378  71.476  48.249  1.00  0.00           O  
ATOM    217  NE2 GLN A  44      61.214  70.711  47.256  1.00  0.00           N  
ATOM    218  N   ASP A  45      56.073  70.736  43.800  1.00 69.06           N  
ATOM    219  CA  ASP A  45      55.004  70.673  42.789  1.00 68.21           C  
ATOM    220  C   ASP A  45      55.563  70.704  41.355  1.00 67.51           C  
ATOM    221  O   ASP A  45      55.186  69.867  40.536  1.00 66.79           O  
ATOM    222  CB  ASP A  45      53.890  71.741  42.944  1.00  0.00           C  
ATOM    223  CG  ASP A  45      53.271  71.872  44.338  1.00  0.00           C  
ATOM    224  OD1 ASP A  45      53.493  70.978  45.182  1.00  0.00           O  
ATOM    225  OD2 ASP A  45      52.481  72.821  44.519  1.00  0.00           O1-
ATOM    226  N   LEU A  46      56.521  71.606  41.105  1.00 66.87           N  
ATOM    227  CA  LEU A  46      57.308  71.707  39.868  1.00 66.15           C  
ATOM    228  C   LEU A  46      58.135  70.444  39.541  1.00 65.17           C  
ATOM    229  O   LEU A  46      58.530  70.267  38.392  1.00 65.23           O  
ATOM    230  CB  LEU A  46      58.227  72.948  39.956  1.00  0.00           C  
ATOM    231  CG  LEU A  46      57.500  74.307  39.820  1.00  0.00           C  
ATOM    232  CD1 LEU A  46      58.315  75.453  40.458  1.00  0.00           C  
ATOM    233  CD2 LEU A  46      57.124  74.611  38.353  1.00  0.00           C  
ATOM    234  N   SER A  47      58.366  69.590  40.542  1.00 63.46           N  
ATOM    235  CA  SER A  47      59.089  68.326  40.445  1.00 61.88           C  
ATOM    236  C   SER A  47      58.141  67.114  40.614  1.00 59.93           C  
ATOM    237  O   SER A  47      58.626  65.996  40.794  1.00 60.05           O  
ATOM    238  CB  SER A  47      60.222  68.355  41.500  1.00  0.00           C  
ATOM    239  OG  SER A  47      61.114  67.262  41.373  1.00  0.00           O  
ATOM    240  N   SER A  48      56.815  67.305  40.540  1.00 57.47           N  
ATOM    241  CA  SER A  48      55.852  66.202  40.605  1.00 54.24           C  
ATOM    242  C   SER A  48      55.942  65.293  39.352  1.00 51.77           C  
ATOM    243  O   SER A  48      56.218  65.800  38.259  1.00 50.83           O  
ATOM    244  CB  SER A  48      54.426  66.779  40.774  1.00  0.00           C  
ATOM    245  OG  SER A  48      53.425  65.772  40.881  1.00  0.00           O  
ATOM    246  N   PRO A  49      55.585  63.993  39.506  1.00 49.90           N  
ATOM    247  CA  PRO A  49      55.029  63.183  38.404  1.00 47.94           C  
ATOM    248  C   PRO A  49      53.890  63.886  37.638  1.00 46.59           C  
ATOM    249  O   PRO A  49      53.179  64.722  38.207  1.00 46.46           O  
ATOM    250  CB  PRO A  49      54.555  61.893  39.089  1.00 48.22           C  
ATOM    251  CG  PRO A  49      55.399  61.788  40.349  1.00 48.69           C  
ATOM    252  CD  PRO A  49      55.599  63.241  40.762  1.00 49.54           C  
ATOM    253  N   ARG A  50      53.821  63.580  36.341  1.00 44.28           N  
ATOM    254  CA  ARG A  50      53.205  64.416  35.323  1.00 42.66           C  
ATOM    255  C   ARG A  50      52.707  63.490  34.206  1.00 41.40           C  
ATOM    256  O   ARG A  50      53.419  63.252  33.230  1.00 42.38           O  
ATOM    257  CB  ARG A  50      54.251  65.461  34.851  1.00  0.00           C  
ATOM    258  CG  ARG A  50      55.716  64.980  34.732  1.00  0.00           C  
ATOM    259  CD  ARG A  50      56.663  66.079  34.234  1.00  0.00           C  
ATOM    260  NE  ARG A  50      58.069  65.669  34.348  1.00  0.00           N  
ATOM    261  CZ  ARG A  50      59.127  66.332  33.857  1.00  0.00           C  
ATOM    262  NH1 ARG A  50      58.984  67.484  33.193  1.00  0.00           N  
ATOM    263  NH2 ARG A  50      60.351  65.831  34.039  1.00  0.00           N1+
ATOM    264  N   THR A  51      51.513  62.938  34.409  1.00 39.65           N  
ATOM    265  CA  THR A  51      50.930  61.888  33.585  1.00 37.59           C  
ATOM    266  C   THR A  51      49.886  62.487  32.617  1.00 36.75           C  
ATOM    267  O   THR A  51      49.128  63.371  33.019  1.00 35.20           O  
ATOM    268  CB  THR A  51      50.223  60.877  34.526  1.00  0.00           C  
ATOM    269  OG1 THR A  51      51.144  60.395  35.489  1.00  0.00           O  
ATOM    270  CG2 THR A  51      49.563  59.670  33.837  1.00  0.00           C  
ATOM    271  N   ARG A  52      49.818  62.010  31.365  1.00 36.68           N  
ATOM    272  CA  ARG A  52      48.747  62.401  30.437  1.00 37.36           C  
ATOM    273  C   ARG A  52      48.295  61.142  29.670  1.00 38.83           C  
ATOM    274  O   ARG A  52      49.150  60.298  29.398  1.00 38.50           O  
ATOM    275  CB  ARG A  52      49.286  63.435  29.417  1.00  0.00           C  
ATOM    276  CG  ARG A  52      49.447  64.884  29.921  1.00  0.00           C  
ATOM    277  CD  ARG A  52      50.703  65.588  29.379  1.00  0.00           C  
ATOM    278  NE  ARG A  52      51.917  65.046  30.018  1.00  0.00           N  
ATOM    279  CZ  ARG A  52      53.120  65.642  30.073  1.00  0.00           C  
ATOM    280  NH1 ARG A  52      53.353  66.807  29.464  1.00  0.00           N  
ATOM    281  NH2 ARG A  52      54.107  65.083  30.781  1.00  0.00           N1+
ATOM    282  N   THR A  53      47.010  61.068  29.286  1.00 39.73           N  
ATOM    283  CA  THR A  53      46.462  59.977  28.481  1.00 41.14           C  
ATOM    284  C   THR A  53      45.571  60.570  27.383  1.00 42.32           C  
ATOM    285  O   THR A  53      44.894  61.571  27.602  1.00 42.50           O  
ATOM    286  CB  THR A  53      45.611  59.031  29.368  1.00 41.30           C  
ATOM    287  OG1 THR A  53      46.406  58.578  30.466  1.00 42.73           O  
ATOM    288  CG2 THR A  53      45.133  57.824  28.600  1.00 41.37           C  
ATOM    289  N   GLY A  54      45.576  59.961  26.202  1.00 43.12           N  
ATOM    290  CA  GLY A  54      44.747  60.461  25.120  1.00 44.60           C  
ATOM    291  C   GLY A  54      45.472  60.485  23.789  1.00 45.86           C  
ATOM    292  O   GLY A  54      46.674  60.239  23.735  1.00 45.74           O  
ATOM    293  N   ASP A  55      44.761  60.907  22.741  1.00 47.56           N  
ATOM    294  CA  ASP A  55      45.365  61.406  21.506  1.00 49.51           C  
ATOM    295  C   ASP A  55      45.615  62.913  21.668  1.00 50.46           C  
ATOM    296  O   ASP A  55      44.813  63.601  22.301  1.00 50.67           O  
ATOM    297  CB  ASP A  55      44.504  61.156  20.242  1.00  0.00           C  
ATOM    298  CG  ASP A  55      44.093  59.703  19.992  1.00  0.00           C  
ATOM    299  OD1 ASP A  55      44.762  58.791  20.522  1.00  0.00           O  
ATOM    300  OD2 ASP A  55      43.166  59.517  19.176  1.00  0.00           O1-
ATOM    301  N   VAL A  56      46.699  63.397  21.049  1.00 51.21           N  
ATOM    302  CA  VAL A  56      47.079  64.812  20.940  1.00 52.28           C  
ATOM    303  C   VAL A  56      47.337  65.461  22.330  1.00 51.61           C  
ATOM    304  O   VAL A  56      46.979  66.612  22.566  1.00 51.31           O  
ATOM    305  CB  VAL A  56      46.058  65.649  20.086  1.00  0.00           C  
ATOM    306  CG1 VAL A  56      46.600  67.020  19.616  1.00  0.00           C  
ATOM    307  CG2 VAL A  56      45.576  64.888  18.830  1.00  0.00           C  
ATOM    308  N   LEU A  57      47.975  64.710  23.242  1.00 50.83           N  
ATOM    309  CA  LEU A  57      48.485  65.246  24.508  1.00 50.28           C  
ATOM    310  C   LEU A  57      49.773  66.069  24.267  1.00 50.30           C  
ATOM    311  O   LEU A  57      50.490  65.801  23.301  1.00 50.32           O  
ATOM    312  CB  LEU A  57      48.601  64.118  25.560  1.00  0.00           C  
ATOM    313  CG  LEU A  57      49.644  63.000  25.312  1.00  0.00           C  
ATOM    314  CD1 LEU A  57      51.085  63.428  25.678  1.00  0.00           C  
ATOM    315  CD2 LEU A  57      49.233  61.690  26.025  1.00  0.00           C  
ATOM    316  N   LEU A  58      50.029  67.069  25.122  1.00 49.81           N  
ATOM    317  CA  LEU A  58      51.051  68.101  24.917  1.00 49.52           C  
ATOM    318  C   LEU A  58      52.075  68.084  26.064  1.00 49.66           C  
ATOM    319  O   LEU A  58      51.820  67.488  27.114  1.00 49.17           O  
ATOM    320  CB  LEU A  58      50.327  69.471  24.759  1.00  0.00           C  
ATOM    321  CG  LEU A  58      51.125  70.673  24.181  1.00  0.00           C  
ATOM    322  CD1 LEU A  58      51.957  71.462  25.213  1.00  0.00           C  
ATOM    323  CD2 LEU A  58      51.915  70.342  22.901  1.00  0.00           C  
ATOM    324  N   ALA A  59      53.223  68.725  25.808  1.00 49.56           N  
ATOM    325  CA  ALA A  59      54.357  68.924  26.709  1.00 50.30           C  
ATOM    326  C   ALA A  59      54.077  69.979  27.806  1.00 49.54           C  
ATOM    327  O   ALA A  59      53.017  69.936  28.426  1.00 49.23           O  
ATOM    328  CB  ALA A  59      55.602  69.238  25.856  1.00  0.00           C  
ATOM    329  N   GLU A  60      55.044  70.872  28.077  1.00 49.49           N  
ATOM    330  CA  GLU A  60      55.015  71.771  29.236  1.00 49.58           C  
ATOM    331  C   GLU A  60      55.971  72.996  29.091  1.00 49.73           C  
ATOM    332  O   GLU A  60      57.007  73.037  29.755  1.00 50.32           O  
ATOM    333  CB  GLU A  60      55.174  70.933  30.542  1.00  0.00           C  
ATOM    334  CG  GLU A  60      56.356  69.927  30.560  1.00  0.00           C  
ATOM    335  CD  GLU A  60      56.142  68.783  31.552  1.00  0.00           C  
ATOM    336  OE1 GLU A  60      55.536  67.770  31.134  1.00  0.00           O  
ATOM    337  OE2 GLU A  60      56.603  68.910  32.706  1.00  0.00           O1-
ATOM    338  N   PRO A  61      55.656  73.963  28.192  1.00 31.02           N  
ATOM    339  CA  PRO A  61      56.649  74.942  27.675  1.00 32.28           C  
ATOM    340  C   PRO A  61      56.906  76.256  28.480  1.00 31.44           C  
ATOM    341  O   PRO A  61      57.026  77.318  27.874  1.00 32.07           O  
ATOM    342  CD  PRO A  61      54.405  74.023  27.422  1.00  0.00           C  
ATOM    343  CB  PRO A  61      56.113  75.195  26.252  1.00  0.00           C  
ATOM    344  CG  PRO A  61      54.606  75.153  26.422  1.00  0.00           C  
ATOM    345  N   ALA A  62      57.063  76.189  29.806  1.00 31.02           N  
ATOM    346  CA  ALA A  62      57.628  77.215  30.711  1.00 30.54           C  
ATOM    347  C   ALA A  62      56.940  78.592  30.973  1.00 30.29           C  
ATOM    348  O   ALA A  62      57.091  79.062  32.101  1.00 30.82           O  
ATOM    349  CB  ALA A  62      59.110  77.450  30.363  1.00  0.00           C  
ATOM    350  N   ASP A  63      56.258  79.259  30.025  1.00 27.98           N  
ATOM    351  CA  ASP A  63      55.762  80.652  30.201  1.00 27.56           C  
ATOM    352  C   ASP A  63      54.328  80.798  29.645  1.00 27.51           C  
ATOM    353  O   ASP A  63      53.876  79.858  29.014  1.00 28.08           O  
ATOM    354  CB  ASP A  63      56.733  81.681  29.564  1.00  0.00           C  
ATOM    355  CG  ASP A  63      56.659  83.102  30.142  1.00  0.00           C  
ATOM    356  OD1 ASP A  63      55.823  83.349  31.039  1.00  0.00           O  
ATOM    357  OD2 ASP A  63      57.470  83.929  29.678  1.00  0.00           O1-
ATOM    358  N   PHE A  64      53.616  81.924  29.881  1.00 20.52           N  
ANISOU  358  N   PHE A  64     2627   2681   2487     28    -68    -12
ATOM    359  CA  PHE A  64      52.194  82.107  29.407  1.00 19.30           C  
ANISOU  359  CA  PHE A  64     2439   2497   2398     26    -53    -28
ATOM    360  C   PHE A  64      52.196  82.379  27.901  1.00 18.36           C  
ANISOU  360  C   PHE A  64     2287   2424   2266     28   -103     16
ATOM    361  O   PHE A  64      51.380  81.831  27.181  1.00 17.27           O  
ANISOU  361  O   PHE A  64     2102   2330   2130     65   -108     43
ATOM    362  CB  PHE A  64      51.268  83.067  30.154  1.00 17.86           C  
ANISOU  362  CB  PHE A  64     2262   2316   2205      9    -37    -70
ATOM    363  CG  PHE A  64      50.748  82.534  31.479  1.00 17.40           C  
ANISOU  363  CG  PHE A  64     2303   2236   2069      7     61   -102
ATOM    364  CD1 PHE A  64      49.856  81.471  31.522  1.00 16.44           C  
ANISOU  364  CD1 PHE A  64     2018   2134   2093    -17    147    -84
ATOM    365  CD2 PHE A  64      51.109  83.140  32.677  1.00 17.53           C  
ANISOU  365  CD2 PHE A  64     2251   2204   2205    -84    111    -67
ATOM    366  CE1 PHE A  64      49.361  81.005  32.740  1.00 15.94           C  
ANISOU  366  CE1 PHE A  64     2025   2121   1910    -91    155    -33
ATOM    367  CE2 PHE A  64      50.624  82.675  33.894  1.00 16.56           C  
ANISOU  367  CE2 PHE A  64     2156   2103   2032    -53    132   -142
ATOM    368  CZ  PHE A  64      49.761  81.604  33.930  1.00 16.64           C  
ANISOU  368  CZ  PHE A  64     2012   2203   2108    -27    130     26
ATOM    369  N   GLU A  65      53.121  83.208  27.413  1.00 18.38           N  
ANISOU  369  N   GLU A  65     2275   2422   2283     31   -130    -26
ATOM    370  CA  GLU A  65      53.206  83.475  25.971  1.00 17.98           C  
ANISOU  370  CA  GLU A  65     2221   2412   2198     35   -120      3
ATOM    371  C   GLU A  65      53.375  82.226  25.123  1.00 17.14           C  
ANISOU  371  C   GLU A  65     2118   2360   2035     67   -165    -18
ATOM    372  O   GLU A  65      52.806  82.138  24.031  1.00 17.77           O  
ANISOU  372  O   GLU A  65     2149   2514   2086     90   -222    -55
ATOM    373  CB  GLU A  65      54.360  84.436  25.637  1.00 18.62           C  
ANISOU  373  CB  GLU A  65     2304   2493   2276     61   -141     17
ATOM    374  CG  GLU A  65      54.014  85.895  25.806  1.00 20.76           C  
ANISOU  374  CG  GLU A  65     2598   2706   2582    -41    -71     56
ATOM    375  CD  GLU A  65      54.024  86.341  27.247  1.00 23.84           C  
ANISOU  375  CD  GLU A  65     2999   2965   3093     34    -34      0
ATOM    376  OE1 GLU A  65      54.416  85.542  28.127  1.00 25.19           O  
ANISOU  376  OE1 GLU A  65     3011   3339   3221    -54    -79    -22
ATOM    377  OE2 GLU A  65      53.643  87.503  27.497  1.00 26.78           O1-
ANISOU  377  OE2 GLU A  65     3320   3338   3515   -143     15     60
ATOM    378  N   SER A  66      54.161  81.264  25.613  1.00 16.18           N  
ANISOU  378  N   SER A  66     2080   2247   1819     51   -145      8
ATOM    379  CA  SER A  66      54.402  80.034  24.866  1.00 16.08           C  
ANISOU  379  CA  SER A  66     2046   2196   1866     78    -86     26
ATOM    380  C   SER A  66      53.136  79.198  24.726  1.00 14.94           C  
ANISOU  380  C   SER A  66     1946   2039   1689     62    -74     55
ATOM    381  O   SER A  66      53.103  78.255  23.923  1.00 15.40           O  
ANISOU  381  O   SER A  66     2184   2046   1620    105   -114    159
ATOM    382  CB  SER A  66      55.490  79.187  25.523  1.00 16.38           C  
ANISOU  382  CB  SER A  66     2124   2248   1849     25    -55     39
ATOM    383  OG  SER A  66      55.019  78.604  26.719  1.00 18.54           O  
ANISOU  383  OG  SER A  66     2296   2588   2160    141    -40     38
ATOM    384  N   LEU A  67      52.110  79.528  25.520  1.00 14.28           N  
ANISOU  384  N   LEU A  67     1812   1976   1637     78    -41     41
ATOM    385  CA  LEU A  67      50.829  78.826  25.486  1.00 13.79           C  
ANISOU  385  CA  LEU A  67     1726   1875   1636     44    -14      2
ATOM    386  C   LEU A  67      49.844  79.457  24.481  1.00 13.41           C  
ANISOU  386  C   LEU A  67     1672   1789   1632     38     10     28
ATOM    387  O   LEU A  67      48.735  78.975  24.330  1.00 12.54           O  
ANISOU  387  O   LEU A  67     1648   1599   1514    -77     63     89
ATOM    388  CB  LEU A  67      50.230  78.789  26.895  1.00 13.50           C  
ANISOU  388  CB  LEU A  67     1680   1827   1623     51    -14    -51
ATOM    389  CG  LEU A  67      51.170  78.235  27.981  1.00 12.88           C  
ANISOU  389  CG  LEU A  67     1713   1664   1514     35      6     12
ATOM    390  CD1 LEU A  67      50.456  78.148  29.340  1.00 13.40           C  
ANISOU  390  CD1 LEU A  67     1599   1776   1715     22   -244     30
ATOM    391  CD2 LEU A  67      51.727  76.885  27.585  1.00 14.12           C  
ANISOU  391  CD2 LEU A  67     1798   1817   1751      1    -48    -57
ATOM    392  N   LEU A  68      50.280  80.529  23.810  1.00 13.20           N  
ANISOU  392  N   LEU A  68     1686   1777   1552     50    -59     25
ATOM    393  CA  LEU A  68      49.565  81.159  22.683  1.00 13.29           C  
ANISOU  393  CA  LEU A  68     1640   1802   1606     23    -28      2
ATOM    394  C   LEU A  68      48.227  81.802  23.079  1.00 13.12           C  
ANISOU  394  C   LEU A  68     1600   1798   1585     36    -37    -26
ATOM    395  O   LEU A  68      47.312  81.914  22.260  1.00 13.19           O  
ANISOU  395  O   LEU A  68     1649   1878   1484    113    -53     -6
ATOM    396  CB  LEU A  68      49.413  80.182  21.506  1.00 13.92           C  
ANISOU  396  CB  LEU A  68     1686   1887   1713     47    -34      4
ATOM    397  CG  LEU A  68      50.716  79.524  21.023  1.00 14.79           C  
ANISOU  397  CG  LEU A  68     1687   2000   1930    -17    -29      9
ATOM    398  CD1 LEU A  68      50.424  78.705  19.766  1.00 16.09           C  
ANISOU  398  CD1 LEU A  68     1897   2022   2192    177    -56     13
ATOM    399  CD2 LEU A  68      51.846  80.525  20.789  1.00 16.80           C  
ANISOU  399  CD2 LEU A  68     2039   2354   1988     70    -50     56
ATOM    400  N   LEU A  69      48.129  82.244  24.329  1.00 12.83           N  
ANISOU  400  N   LEU A  69     1577   1758   1538    -23     -4     -1
ATOM    401  CA  LEU A  69      46.930  82.911  24.810  1.00 12.43           C  
ANISOU  401  CA  LEU A  69     1465   1749   1507    -13    -49    -23
ATOM    402  C   LEU A  69      46.821  84.265  24.158  1.00 12.35           C  
ANISOU  402  C   LEU A  69     1427   1794   1471     19    -68     -8
ATOM    403  O   LEU A  69      47.831  84.861  23.757  1.00 13.53           O  
ANISOU  403  O   LEU A  69     1660   1975   1504     18   -102     -7
ATOM    404  CB  LEU A  69      46.969  83.078  26.332  1.00 12.16           C  
ANISOU  404  CB  LEU A  69     1461   1682   1476    -57     -1    -47
ATOM    405  CG  LEU A  69      46.820  81.764  27.094  1.00 12.02           C  
ANISOU  405  CG  LEU A  69     1467   1596   1503      8     26   -125
ATOM    406  CD1 LEU A  69      47.395  81.902  28.502  1.00 13.61           C  
ANISOU  406  CD1 LEU A  69     1506   1827   1837     76     54   -211
ATOM    407  CD2 LEU A  69      45.362  81.336  27.127  1.00 12.13           C  
ANISOU  407  CD2 LEU A  69     1471   1637   1498    -71     40     73
ATOM    408  N   SER A  70      45.594  84.762  24.057  1.00 12.23           N  
ANISOU  408  N   SER A  70     1402   1855   1389     27   -131     -8
ATOM    409  CA  SER A  70      45.349  86.087  23.495  1.00 12.33           C  
ANISOU  409  CA  SER A  70     1404   1804   1473     44    -75      0
ATOM    410  C   SER A  70      45.902  87.196  24.392  1.00 12.69           C  
ANISOU  410  C   SER A  70     1449   1866   1504     36    -92    -35
ATOM    411  O   SER A  70      46.054  87.033  25.598  1.00 12.57           O  
ANISOU  411  O   SER A  70     1550   1844   1380     13   -106    -21
ATOM    412  CB  SER A  70      43.858  86.295  23.287  1.00 12.88           C  
ANISOU  412  CB  SER A  70     1525   1863   1506     47    -59    -21
ATOM    413  OG  SER A  70      43.194  86.421  24.526  1.00 13.34           O  
ANISOU  413  OG  SER A  70     1574   1977   1518    128    -79    132
ATOM    414  N   ARG A  71      46.204  88.344  23.792  1.00 13.24           N  
ANISOU  414  N   ARG A  71     1506   1885   1640    128   -147    -15
ATOM    415  CA  ARG A  71      46.809  89.442  24.536  1.00 12.91           C  
ANISOU  415  CA  ARG A  71     1473   1823   1607     85   -114    -12
ATOM    416  C   ARG A  71      45.964  89.919  25.736  1.00 12.58           C  
ANISOU  416  C   ARG A  71     1428   1782   1569     78   -143    -45
ATOM    417  O   ARG A  71      46.503  90.132  26.820  1.00 13.19           O  
ANISOU  417  O   ARG A  71     1611   1905   1493    124   -283    -70
ATOM    418  CB  ARG A  71      47.144  90.607  23.584  1.00 13.47           C  
ANISOU  418  CB  ARG A  71     1547   1846   1725    101   -107     18
ATOM    419  CG  ARG A  71      47.971  91.707  24.227  1.00 16.41           C  
ANISOU  419  CG  ARG A  71     1939   2138   2155     62   -195    -39
ATOM    420  CD  ARG A  71      49.315  91.218  24.786  1.00 21.36           C  
ANISOU  420  CD  ARG A  71     2698   2726   2689     14     31    -42
ATOM    421  NE  ARG A  71      50.009  90.256  23.922  1.00 23.74           N  
ANISOU  421  NE  ARG A  71     3096   2894   3029    -50    137     22
ATOM    422  CZ  ARG A  71      51.147  89.639  24.241  1.00 23.56           C  
ANISOU  422  CZ  ARG A  71     3009   2928   3013    -36    162     20
ATOM    423  NH1 ARG A  71      51.758  89.885  25.400  1.00 26.32           N  
ANISOU  423  NH1 ARG A  71     3412   3167   3419    -69    138   -104
ATOM    424  NH2 ARG A  71      51.688  88.770  23.392  1.00 24.98           N1+
ANISOU  424  NH2 ARG A  71     3228   3013   3247      9    131     52
ATOM    425  N   PRO A  72      44.636  90.062  25.572  1.00 12.14           N  
ANISOU  425  N   PRO A  72     1369   1720   1521     19   -177    -25
ATOM    426  CA  PRO A  72      43.857  90.477  26.749  1.00 12.19           C  
ANISOU  426  CA  PRO A  72     1363   1756   1511     26   -132    -27
ATOM    427  C   PRO A  72      43.942  89.489  27.929  1.00 11.72           C  
ANISOU  427  C   PRO A  72     1349   1661   1441     33   -157      0
ATOM    428  O   PRO A  72      43.970  89.911  29.097  1.00 11.78           O  
ANISOU  428  O   PRO A  72     1316   1722   1436    -21   -203     45
ATOM    429  CB  PRO A  72      42.427  90.602  26.186  1.00 12.38           C  
ANISOU  429  CB  PRO A  72     1358   1820   1523     39    -93     -5
ATOM    430  CG  PRO A  72      42.623  90.843  24.694  1.00 13.11           C  
ANISOU  430  CG  PRO A  72     1536   1829   1616    -28    -84    -15
ATOM    431  CD  PRO A  72      43.797  89.979  24.358  1.00 12.45           C  
ANISOU  431  CD  PRO A  72     1450   1755   1522     26   -104     32
ATOM    432  N   VAL A  73      44.015  88.195  27.625  1.00 11.23           N  
ANISOU  432  N   VAL A  73     1297   1566   1403     39   -126    -48
ATOM    433  CA  VAL A  73      44.124  87.194  28.681  1.00 11.73           C  
ANISOU  433  CA  VAL A  73     1346   1632   1476     37   -106    -69
ATOM    434  C   VAL A  73      45.525  87.251  29.302  1.00 11.87           C  
ANISOU  434  C   VAL A  73     1379   1672   1456     50    -96    -27
ATOM    435  O   VAL A  73      45.672  87.210  30.528  1.00 11.88           O  
ANISOU  435  O   VAL A  73     1380   1673   1458     50   -156   -129
ATOM    436  CB  VAL A  73      43.767  85.785  28.170  1.00 11.34           C  
ANISOU  436  CB  VAL A  73     1299   1553   1455     34    -54    -55
ATOM    437  CG1 VAL A  73      44.100  84.712  29.231  1.00 12.11           C  
ANISOU  437  CG1 VAL A  73     1284   1630   1687     96     13      4
ATOM    438  CG2 VAL A  73      42.293  85.737  27.803  1.00 12.22           C  
ANISOU  438  CG2 VAL A  73     1305   1844   1493     59     -5    -63
ATOM    439  N   LEU A  74      46.556  87.397  28.470  1.00 11.59           N  
ANISOU  439  N   LEU A  74     1429   1625   1347    144   -131    -57
ATOM    440  CA  LEU A  74      47.928  87.526  28.991  1.00 12.53           C  
ANISOU  440  CA  LEU A  74     1572   1718   1470     34    -81    -46
ATOM    441  C   LEU A  74      48.056  88.713  29.942  1.00 12.77           C  
ANISOU  441  C   LEU A  74     1689   1733   1427     60   -110    -29
ATOM    442  O   LEU A  74      48.646  88.607  31.022  1.00 13.50           O  
ANISOU  442  O   LEU A  74     1767   1843   1517     12   -158    -76
ATOM    443  CB  LEU A  74      48.934  87.648  27.844  1.00 12.78           C  
ANISOU  443  CB  LEU A  74     1659   1751   1444     49    -48    -58
ATOM    444  CG  LEU A  74      49.137  86.393  26.991  1.00 13.52           C  
ANISOU  444  CG  LEU A  74     1711   1792   1632     40     -3    -41
ATOM    445  CD1 LEU A  74      49.952  86.693  25.736  1.00 15.28           C  
ANISOU  445  CD1 LEU A  74     2072   1959   1772    119     40     57
ATOM    446  CD2 LEU A  74      49.795  85.285  27.810  1.00 14.62           C  
ANISOU  446  CD2 LEU A  74     1745   1981   1827     -6    179     12
ATOM    447  N   GLU A  75      47.495  89.845  29.527  1.00 12.53           N  
ANISOU  447  N   GLU A  75     1631   1742   1387    -27   -156    -67
ATOM    448  CA  GLU A  75      47.546  91.060  30.339  1.00 13.80           C  
ANISOU  448  CA  GLU A  75     1752   1827   1664    -20    -99    -37
ATOM    449  C   GLU A  75      46.743  90.905  31.631  1.00 13.58           C  
ANISOU  449  C   GLU A  75     1754   1769   1634    -22   -121    -48
ATOM    450  O   GLU A  75      47.129  91.399  32.690  1.00 14.26           O  
ANISOU  450  O   GLU A  75     1897   1888   1633      0   -209   -156
ATOM    451  CB  GLU A  75      47.034  92.249  29.529  1.00 14.31           C  
ANISOU  451  CB  GLU A  75     1788   1889   1759    -54    -61    -34
ATOM    452  CG  GLU A  75      47.976  92.654  28.413  1.00 16.38           C  
ANISOU  452  CG  GLU A  75     2094   2127   2001      8   -134    -23
ATOM    453  CD  GLU A  75      47.459  93.832  27.607  1.00 18.20           C  
ANISOU  453  CD  GLU A  75     2220   2368   2324     60    -17     17
ATOM    454  OE1 GLU A  75      46.490  94.493  28.060  1.00 24.53           O  
ANISOU  454  OE1 GLU A  75     3157   3130   3033     44    189    243
ATOM    455  OE2 GLU A  75      48.026  94.117  26.524  1.00 23.09           O1-
ANISOU  455  OE2 GLU A  75     2916   2837   3017    133    -87    171
ATOM    456  N   GLY A  76      45.607  90.222  31.538  1.00 13.21           N  
ANISOU  456  N   GLY A  76     1736   1729   1554    -49   -145    -56
ATOM    457  CA  GLY A  76      44.784  89.955  32.708  1.00 12.94           C  
ANISOU  457  CA  GLY A  76     1675   1676   1564    -49   -108    -39
ATOM    458  C   GLY A  76      45.457  89.039  33.705  1.00 12.50           C  
ANISOU  458  C   GLY A  76     1662   1667   1420    -36   -182    -46
ATOM    459  O   GLY A  76      45.405  89.285  34.903  1.00 12.81           O  
ANISOU  459  O   GLY A  76     1706   1735   1424    -95   -237    -79
ATOM    460  N   LEU A  77      46.095  87.983  33.210  1.00 12.48           N  
ANISOU  460  N   LEU A  77     1628   1642   1471    -28   -186    -66
ATOM    461  CA  LEU A  77      46.840  87.079  34.080  1.00 13.71           C  
ANISOU  461  CA  LEU A  77     1773   1768   1665     -8    -69    -51
ATOM    462  C   LEU A  77      47.882  87.851  34.877  1.00 14.46           C  
ANISOU  462  C   LEU A  77     1884   1813   1797     14    -41    -48
ATOM    463  O   LEU A  77      47.956  87.745  36.097  1.00 14.68           O  
ANISOU  463  O   LEU A  77     1899   1824   1856     32    -50   -123
ATOM    464  CB  LEU A  77      47.519  85.969  33.269  1.00 12.68           C  
ANISOU  464  CB  LEU A  77     1645   1634   1537     45    -72    -81
ATOM    465  CG  LEU A  77      46.593  84.846  32.769  1.00 12.08           C  
ANISOU  465  CG  LEU A  77     1526   1616   1448     48    -70   -129
ATOM    466  CD1 LEU A  77      47.282  84.070  31.659  1.00 14.02           C  
ANISOU  466  CD1 LEU A  77     1802   1824   1700     17    -90    113
ATOM    467  CD2 LEU A  77      46.179  83.927  33.908  1.00 12.75           C  
ANISOU  467  CD2 LEU A  77     1389   1826   1629     94     54    -63
ATOM    468  N   ARG A  78      48.666  88.666  34.190  1.00 15.30           N  
ANISOU  468  N   ARG A  78     2031   1907   1874      6    -78   -114
ATOM    469  CA  ARG A  78      49.718  89.399  34.893  1.00 16.93           C  
ANISOU  469  CA  ARG A  78     2250   2105   2075    -30    -60    -89
ATOM    470  C   ARG A  78      49.110  90.401  35.879  1.00 16.46           C  
ANISOU  470  C   ARG A  78     2167   2077   2009    -25    -91    -84
ATOM    471  O   ARG A  78      49.581  90.510  37.015  1.00 16.59           O  
ANISOU  471  O   ARG A  78     2166   2065   2072    -53   -108    -91
ATOM    472  CB  ARG A  78      50.681  90.065  33.914  1.00 18.02           C  
ANISOU  472  CB  ARG A  78     2434   2202   2211    -32    -83    -76
ATOM    473  CG  ARG A  78      50.027  90.861  32.827  1.00 20.82           C  
ANISOU  473  CG  ARG A  78     2739   2541   2630     16     50    -14
ATOM    474  CD  ARG A  78      50.765  92.114  32.485  1.00 22.17           C  
ANISOU  474  CD  ARG A  78     2792   2730   2902     29      3     11
ATOM    475  NE  ARG A  78      49.921  93.058  31.751  1.00 24.68           N  
ANISOU  475  NE  ARG A  78     2994   3030   3350     12    189    -42
ATOM    476  CZ  ARG A  78      48.937  93.783  32.282  1.00 25.09           C  
ANISOU  476  CZ  ARG A  78     3223   3165   3143    -10     42     12
ATOM    477  NH1 ARG A  78      48.639  93.694  33.567  1.00 25.57           N  
ANISOU  477  NH1 ARG A  78     3187   3288   3237     -7    -80    -21
ATOM    478  NH2 ARG A  78      48.255  94.627  31.516  1.00 27.20           N1+
ANISOU  478  NH2 ARG A  78     3591   3333   3410     46    200     33
ATOM    479  N   ALA A  79      48.042  91.090  35.476  1.00 16.55           N  
ANISOU  479  N   ALA A  79     2177   2036   2074    -39    -88    -80
ATOM    480  CA  ALA A  79      47.373  92.047  36.364  1.00 16.98           C  
ANISOU  480  CA  ALA A  79     2233   2075   2144    -17    -43    -47
ATOM    481  C   ALA A  79      46.799  91.379  37.615  1.00 17.20           C  
ANISOU  481  C   ALA A  79     2251   2081   2202    -16    -53    -47
ATOM    482  O   ALA A  79      46.765  91.985  38.699  1.00 17.22           O  
ANISOU  482  O   ALA A  79     2267   2020   2255    -14    -55    -56
ATOM    483  CB  ALA A  79      46.286  92.809  35.616  1.00 17.36           C  
ANISOU  483  CB  ALA A  79     2324   2094   2175      0    -23    -37
ATOM    484  N   ALA A  80      46.363  90.129  37.462  1.00 16.91           N  
ANISOU  484  N   ALA A  80     2194   2047   2183      2    -35    -66
ATOM    485  CA  ALA A  80      45.786  89.338  38.548  1.00 17.58           C  
ANISOU  485  CA  ALA A  80     2278   2174   2228     12    -35    -46
ATOM    486  C   ALA A  80      46.836  88.656  39.431  1.00 17.82           C  
ANISOU  486  C   ALA A  80     2277   2211   2283      8    -22    -43
ATOM    487  O   ALA A  80      46.483  87.949  40.374  1.00 18.32           O  
ANISOU  487  O   ALA A  80     2396   2239   2322     24    -67    -45
ATOM    488  CB  ALA A  80      44.821  88.298  37.979  1.00 17.64           C  
ANISOU  488  CB  ALA A  80     2293   2205   2204     31    -61    -28
ATOM    489  N   GLY A  81      48.120  88.874  39.134  1.00 17.70           N  
ANISOU  489  N   GLY A  81     2275   2188   2259    -26    -21    -50
ATOM    490  CA  GLY A  81      49.215  88.318  39.939  1.00 18.62           C  
ANISOU  490  CA  GLY A  81     2375   2320   2379      7     13    -31
ATOM    491  C   GLY A  81      49.723  86.953  39.495  1.00 19.04           C  
ANISOU  491  C   GLY A  81     2411   2376   2448     10     32     -5
ATOM    492  O   GLY A  81      50.444  86.283  40.234  1.00 20.00           O  
ANISOU  492  O   GLY A  81     2562   2461   2575     58     73    -18
ATOM    493  N   PHE A  82      49.349  86.526  38.293  1.00 19.47           N  
ANISOU  493  N   PHE A  82     2467   2422   2507     -3     26      9
ATOM    494  CA  PHE A  82      49.804  85.242  37.769  1.00 19.84           C  
ANISOU  494  CA  PHE A  82     2473   2492   2570     -6     17     14
ATOM    495  C   PHE A  82      50.920  85.476  36.768  1.00 20.22           C  
ANISOU  495  C   PHE A  82     2535   2529   2615    -17     10     23
ATOM    496  O   PHE A  82      50.676  85.754  35.593  1.00 20.11           O  
ANISOU  496  O   PHE A  82     2503   2521   2617     26     17     27
ATOM    497  CB  PHE A  82      48.638  84.477  37.164  1.00 20.37           C  
ANISOU  497  CB  PHE A  82     2544   2564   2630     -8      2     48
ATOM    498  CG  PHE A  82      47.479  84.327  38.105  1.00 20.41           C  
ANISOU  498  CG  PHE A  82     2493   2569   2692     44    -27     97
ATOM    499  CD1 PHE A  82      47.677  83.832  39.399  1.00 22.08           C  
ANISOU  499  CD1 PHE A  82     2677   2815   2895     87     30    137
ATOM    500  CD2 PHE A  82      46.214  84.728  37.738  1.00 20.40           C  
ANISOU  500  CD2 PHE A  82     2598   2493   2661     90    -63    -21
ATOM    501  CE1 PHE A  82      46.613  83.705  40.275  1.00 21.66           C  
ANISOU  501  CE1 PHE A  82     2666   2729   2833     47    -14    127
ATOM    502  CE2 PHE A  82      45.138  84.581  38.603  1.00 21.38           C  
ANISOU  502  CE2 PHE A  82     2858   2610   2654     76     48     36
ATOM    503  CZ  PHE A  82      45.334  84.058  39.869  1.00 21.81           C  
ANISOU  503  CZ  PHE A  82     2639   2850   2797     44    -41    156
ATOM    504  N   GLU A  83      52.157  85.380  37.254  1.00 20.47           N  
ANISOU  504  N   GLU A  83     2570   2565   2641    -18      1     -2
ATOM    505  CA  GLU A  83      53.322  85.735  36.453  1.00 20.12           C  
ANISOU  505  CA  GLU A  83     2527   2549   2567    -35    -30     -3
ATOM    506  C   GLU A  83      53.758  84.605  35.524  1.00 19.78           C  
ANISOU  506  C   GLU A  83     2472   2507   2535    -28    -63      5
ATOM    507  O   GLU A  83      54.072  84.855  34.358  1.00 20.09           O  
ANISOU  507  O   GLU A  83     2473   2541   2618    -54   -165     13
ATOM    508  CB  GLU A  83      54.489  86.166  37.354  1.00 20.96           C  
ANISOU  508  CB  GLU A  83     2648   2630   2684    -37    -19    -15
ATOM    509  CG  GLU A  83      55.652  86.815  36.616  1.00 22.45           C  
ANISOU  509  CG  GLU A  83     2866   2832   2830      9    -15     39
ATOM    510  CD  GLU A  83      55.304  88.146  35.936  1.00 26.30           C  
ANISOU  510  CD  GLU A  83     3182   3424   3384    -32     15     58
ATOM    511  OE1 GLU A  83      54.282  88.782  36.292  1.00 27.99           O  
ANISOU  511  OE1 GLU A  83     3563   3654   3415    -33     86     88
ATOM    512  OE2 GLU A  83      56.080  88.565  35.045  1.00 29.38           O1-
ANISOU  512  OE2 GLU A  83     3636   3729   3798     52    -36    175
ATOM    513  N   ARG A  84      53.782  83.372  36.036  1.00 18.52           N  
ANISOU  513  N   ARG A  84     2349   2392   2293    -70   -124     -2
ATOM    514  CA  ARG A  84      54.222  82.210  35.254  1.00 17.77           C  
ANISOU  514  CA  ARG A  84     2244   2348   2156    -61   -143    -31
ATOM    515  C   ARG A  84      53.248  81.049  35.452  1.00 16.37           C  
ANISOU  515  C   ARG A  84     2062   2193   1966    -89   -133    -34
ATOM    516  O   ARG A  84      52.715  80.895  36.539  1.00 15.96           O  
ANISOU  516  O   ARG A  84     2083   2191   1788   -226   -218    -89
ATOM    517  CB  ARG A  84      55.616  81.769  35.691  1.00 19.59           C  
ANISOU  517  CB  ARG A  84     2480   2507   2455    -71    -22     40
ATOM    518  CG  ARG A  84      56.677  82.848  35.612  1.00 21.79           C  
ANISOU  518  CG  ARG A  84     2712   2831   2735    -48    -61      4
ATOM    519  CD  ARG A  84      57.054  83.189  34.174  1.00 25.34           C  
ANISOU  519  CD  ARG A  84     3190   3167   3268     56     11     34
ATOM    520  NE  ARG A  84      58.054  84.256  34.136  1.00 26.01           N  
ANISOU  520  NE  ARG A  84     3181   3357   3342     15   -111     88
ATOM    521  CZ  ARG A  84      57.833  85.529  33.789  1.00 27.88           C  
ANISOU  521  CZ  ARG A  84     3406   3581   3604     -8     22     32
ATOM    522  NH1 ARG A  84      56.628  85.944  33.403  1.00 28.70           N  
ANISOU  522  NH1 ARG A  84     3613   3634   3655     -8     63     23
ATOM    523  NH2 ARG A  84      58.837  86.395  33.813  1.00 27.97           N1+
ANISOU  523  NH2 ARG A  84     3449   3516   3661    -33     48    -34
ATOM    524  N   PRO A  85      53.062  80.219  34.420  1.00 14.56           N  
ANISOU  524  N   PRO A  85     1875   2010   1648    -34   -133     21
ATOM    525  CA  PRO A  85      52.142  79.078  34.591  1.00 13.41           C  
ANISOU  525  CA  PRO A  85     1716   1874   1503    -29    -71    -39
ATOM    526  C   PRO A  85      52.658  78.012  35.564  1.00 12.75           C  
ANISOU  526  C   PRO A  85     1648   1791   1402    -44    -51    -40
ATOM    527  O   PRO A  85      53.859  77.685  35.569  1.00 13.32           O  
ANISOU  527  O   PRO A  85     1732   2021   1308    -36    -48    -80
ATOM    528  CB  PRO A  85      52.023  78.500  33.167  1.00 13.42           C  
ANISOU  528  CB  PRO A  85     1723   1887   1486      3    -56     -6
ATOM    529  CG  PRO A  85      53.212  78.987  32.438  1.00 14.67           C  
ANISOU  529  CG  PRO A  85     1874   1954   1746    -13   -100     87
ATOM    530  CD  PRO A  85      53.652  80.261  33.070  1.00 14.98           C  
ANISOU  530  CD  PRO A  85     1897   1987   1805    -14    -52     22
ATOM    531  N   SER A  86      51.750  77.462  36.364  1.00 11.25           N  
ANISOU  531  N   SER A  86     1564   1548   1163    -27     16    -95
ATOM    532  CA  SER A  86      52.038  76.272  37.159  1.00 11.08           C  
ANISOU  532  CA  SER A  86     1505   1495   1208      9     26   -119
ATOM    533  C   SER A  86      52.146  75.037  36.253  1.00 10.31           C  
ANISOU  533  C   SER A  86     1366   1421   1129     52     43    -99
ATOM    534  O   SER A  86      51.736  75.075  35.092  1.00  9.50           O  
ANISOU  534  O   SER A  86     1287   1255   1065     25    170   -148
ATOM    535  CB  SER A  86      50.937  76.055  38.192  1.00 10.58           C  
ANISOU  535  CB  SER A  86     1353   1407   1260      2     -5   -137
ATOM    536  OG  SER A  86      49.759  75.591  37.547  1.00 11.08           O  
ANISOU  536  OG  SER A  86     1565   1483   1162     10     44   -148
ATOM    537  N   PRO A  87      52.668  73.895  36.777  1.00  9.99           N  
ANISOU  537  N   PRO A  87     1306   1421   1069     90     82   -151
ATOM    538  CA  PRO A  87      52.825  72.663  35.971  1.00 10.22           C  
ANISOU  538  CA  PRO A  87     1326   1384   1172     87     19    -89
ATOM    539  C   PRO A  87      51.545  72.142  35.303  1.00  9.31           C  
ANISOU  539  C   PRO A  87     1253   1187   1095     77     23    -97
ATOM    540  O   PRO A  87      51.603  71.733  34.144  1.00  9.97           O  
ANISOU  540  O   PRO A  87     1369   1296   1123     62    -41    -52
ATOM    541  CB  PRO A  87      53.406  71.631  36.953  1.00 10.37           C  
ANISOU  541  CB  PRO A  87     1268   1427   1245     13     25    -81
ATOM    542  CG  PRO A  87      54.104  72.471  38.003  1.00 11.48           C  
ANISOU  542  CG  PRO A  87     1441   1574   1346    128     55   -164
ATOM    543  CD  PRO A  87      53.202  73.688  38.126  1.00 11.23           C  
ANISOU  543  CD  PRO A  87     1464   1475   1327    141     43   -139
ATOM    544  N   VAL A  88      50.417  72.187  36.026  1.00  9.42           N  
ANISOU  544  N   VAL A  88     1346   1154   1078     76      1   -172
ATOM    545  CA  VAL A  88      49.114  71.811  35.487  1.00  9.35           C  
ANISOU  545  CA  VAL A  88     1304   1168   1080     30    -79   -141
ATOM    546  C   VAL A  88      48.629  72.811  34.414  1.00  8.47           C  
ANISOU  546  C   VAL A  88     1234   1077    905    -13    -49    -54
ATOM    547  O   VAL A  88      48.033  72.376  33.430  1.00  8.84           O  
ANISOU  547  O   VAL A  88     1288   1112    957    158     -1    -60
ATOM    548  CB  VAL A  88      48.055  71.608  36.614  1.00  9.74           C  
ANISOU  548  CB  VAL A  88     1407   1249   1042    130     -3   -149
ATOM    549  CG1 VAL A  88      47.729  72.868  37.438  1.00 12.40           C  
ANISOU  549  CG1 VAL A  88     1815   1428   1466     10    -28    -45
ATOM    550  CG2 VAL A  88      46.754  70.956  36.110  1.00 12.01           C  
ANISOU  550  CG2 VAL A  88     1654   1459   1449    126   -204   -217
ATOM    551  N   GLN A  89      48.954  74.108  34.561  1.00  8.15           N  
ANISOU  551  N   GLN A  89     1146   1074    873     19     15   -101
ATOM    552  CA  GLN A  89      48.597  75.110  33.564  1.00  7.99           C  
ANISOU  552  CA  GLN A  89     1159   1043    831     31     41    -55
ATOM    553  C   GLN A  89      49.396  74.958  32.269  1.00  8.04           C  
ANISOU  553  C   GLN A  89     1120   1062    870     80     85    -39
ATOM    554  O   GLN A  89      48.847  75.056  31.175  1.00  7.80           O  
ANISOU  554  O   GLN A  89     1037   1035    890     82     29     84
ATOM    555  CB  GLN A  89      48.751  76.491  34.189  1.00  8.66           C  
ANISOU  555  CB  GLN A  89     1273   1071    944     20     35   -107
ATOM    556  CG  GLN A  89      47.689  76.743  35.264  1.00  8.47           C  
ANISOU  556  CG  GLN A  89     1200   1000   1016      9     14   -112
ATOM    557  CD  GLN A  89      48.043  77.816  36.285  1.00  8.57           C  
ANISOU  557  CD  GLN A  89     1255   1090    911     55    -34    -79
ATOM    558  OE1 GLN A  89      49.047  78.531  36.170  1.00  9.60           O  
ANISOU  558  OE1 GLN A  89     1446   1221    978    -65   -207    -75
ATOM    559  NE2 GLN A  89      47.190  77.919  37.320  1.00 10.03           N  
ANISOU  559  NE2 GLN A  89     1606   1121   1081     19      5    170
ATOM    560  N   LEU A  90      50.699  74.682  32.391  1.00  8.44           N  
ANISOU  560  N   LEU A  90     1211   1145    848    110     90     -4
ATOM    561  CA  LEU A  90      51.501  74.358  31.203  1.00  8.24           C  
ANISOU  561  CA  LEU A  90     1151   1124    854     79     68     70
ATOM    562  C   LEU A  90      50.930  73.233  30.384  1.00  8.25           C  
ANISOU  562  C   LEU A  90     1155   1061    917    112     97     97
ATOM    563  O   LEU A  90      50.887  73.284  29.145  1.00  8.75           O  
ANISOU  563  O   LEU A  90     1134   1102   1088    130    106    174
ATOM    564  CB  LEU A  90      52.947  73.998  31.557  1.00  9.41           C  
ANISOU  564  CB  LEU A  90     1355   1221    998    118    103     41
ATOM    565  CG  LEU A  90      53.837  75.122  32.035  1.00 10.83           C  
ANISOU  565  CG  LEU A  90     1444   1480   1190     -3     74     32
ATOM    566  CD1 LEU A  90      55.139  74.572  32.606  1.00 12.82           C  
ANISOU  566  CD1 LEU A  90     1610   1965   1294     25    200    -74
ATOM    567  CD2 LEU A  90      54.119  76.092  30.898  1.00 13.28           C  
ANISOU  567  CD2 LEU A  90     1580   1993   1470     94    -74   -108
ATOM    568  N   LYS A  91      50.484  72.175  31.069  1.00  8.06           N  
ANISOU  568  N   LYS A  91     1098   1040    924     36     25    105
ATOM    569  CA  LYS A  91      49.954  70.980  30.420  1.00  8.77           C  
ANISOU  569  CA  LYS A  91     1294   1065    973     46    -18    105
ATOM    570  C   LYS A  91      48.537  71.182  29.872  1.00  7.56           C  
ANISOU  570  C   LYS A  91     1093    878    902    137     -8    113
ATOM    571  O   LYS A  91      48.260  70.737  28.758  1.00  8.71           O  
ANISOU  571  O   LYS A  91     1391    929    989    184    -84    142
ATOM    572  CB  LYS A  91      49.998  69.807  31.414  1.00  9.81           C  
ANISOU  572  CB  LYS A  91     1406   1173   1148     29      5    115
ATOM    573  CG  LYS A  91      51.439  69.412  31.768  1.00 13.14           C  
ANISOU  573  CG  LYS A  91     1715   1684   1594     -9     36     54
ATOM    574  CD  LYS A  91      51.537  68.650  33.097  1.00 13.58           C  
ANISOU  574  CD  LYS A  91     1712   1766   1682     10     26     77
ATOM    575  CE  LYS A  91      52.985  68.418  33.544  1.00 17.01           C  
ANISOU  575  CE  LYS A  91     2061   2236   2163     38    174     -4
ATOM    576  NZ  LYS A  91      53.753  69.667  33.678  1.00 19.80           N1+
ANISOU  576  NZ  LYS A  91     2259   2624   2639     50      1     98
ATOM    577  N   ALA A  92      47.652  71.811  30.662  1.00  7.25           N  
ANISOU  577  N   ALA A  92     1055    815    884     96    -15     90
ATOM    578  CA  ALA A  92      46.237  71.823  30.323  1.00  7.56           C  
ANISOU  578  CA  ALA A  92     1113    909    849      5    -26    115
ATOM    579  C   ALA A  92      45.833  72.952  29.371  1.00  7.32           C  
ANISOU  579  C   ALA A  92     1074    903    802      2      2     52
ATOM    580  O   ALA A  92      44.889  72.781  28.592  1.00  8.07           O  
ANISOU  580  O   ALA A  92     1223   1068    773     79    -23      0
ATOM    581  CB  ALA A  92      45.368  71.881  31.598  1.00  7.77           C  
ANISOU  581  CB  ALA A  92     1171    901    878     74    -36    151
ATOM    582  N   ILE A  93      46.473  74.121  29.440  1.00  7.84           N  
ANISOU  582  N   ILE A  93     1080   1087    811    -38     72     22
ATOM    583  CA  ILE A  93      45.984  75.273  28.662  1.00  8.26           C  
ANISOU  583  CA  ILE A  93     1152   1085    902    -52    115    -14
ATOM    584  C   ILE A  93      46.039  74.996  27.154  1.00  8.00           C  
ANISOU  584  C   ILE A  93     1090   1067    883    -68     75     67
ATOM    585  O   ILE A  93      45.048  75.202  26.477  1.00  7.64           O  
ANISOU  585  O   ILE A  93     1032   1031    839    -48    166     -1
ATOM    586  CB  ILE A  93      46.673  76.585  29.071  1.00  8.92           C  
ANISOU  586  CB  ILE A  93     1131   1255   1000   -128    147     19
ATOM    587  CG1 ILE A  93      46.154  77.011  30.454  1.00 10.02           C  
ANISOU  587  CG1 ILE A  93     1301   1336   1167   -167    282   -103
ATOM    588  CG2 ILE A  93      46.461  77.639  28.021  1.00 10.16           C  
ANISOU  588  CG2 ILE A  93     1234   1366   1259    -21    115   -160
ATOM    589  CD1 ILE A  93      46.920  78.175  31.129  1.00 11.12           C  
ANISOU  589  CD1 ILE A  93     1507   1322   1393   -239    263   -158
ATOM    590  N   PRO A  94      47.171  74.495  26.618  1.00  7.63           N  
ANISOU  590  N   PRO A  94     1089    974    834     18    118     65
ATOM    591  CA  PRO A  94      47.162  74.225  25.166  1.00  7.66           C  
ANISOU  591  CA  PRO A  94     1066    989    855     77     51    104
ATOM    592  C   PRO A  94      46.131  73.191  24.730  1.00  7.37           C  
ANISOU  592  C   PRO A  94     1025    925    849    104      0    154
ATOM    593  O   PRO A  94      45.510  73.332  23.663  1.00  7.84           O  
ANISOU  593  O   PRO A  94     1122    914    940    182    -18    167
ATOM    594  CB  PRO A  94      48.597  73.745  24.889  1.00  8.45           C  
ANISOU  594  CB  PRO A  94     1180   1090    940     -1     30    164
ATOM    595  CG  PRO A  94      49.391  74.319  25.982  1.00  9.00           C  
ANISOU  595  CG  PRO A  94     1258   1251    909     29    128    143
ATOM    596  CD  PRO A  94      48.499  74.259  27.202  1.00  8.09           C  
ANISOU  596  CD  PRO A  94     1105   1128    840     86      1     47
ATOM    597  N   LEU A  95      45.946  72.162  25.552  1.00  7.37           N  
ANISOU  597  N   LEU A  95     1023    954    824    165    -18    122
ATOM    598  CA  LEU A  95      44.971  71.117  25.253  1.00  7.17           C  
ANISOU  598  CA  LEU A  95      969    857    896     81     13     98
ATOM    599  C   LEU A  95      43.551  71.690  25.297  1.00  6.66           C  
ANISOU  599  C   LEU A  95      910    808    809     51    -37     74
ATOM    600  O   LEU A  95      42.702  71.329  24.494  1.00  7.56           O  
ANISOU  600  O   LEU A  95     1044    839    988     -6   -115     57
ATOM    601  CB  LEU A  95      45.126  69.956  26.238  1.00  7.40           C  
ANISOU  601  CB  LEU A  95      966    933    909     42     21     66
ATOM    602  CG  LEU A  95      46.483  69.236  26.181  1.00  8.06           C  
ANISOU  602  CG  LEU A  95     1119    916   1026     39      9    219
ATOM    603  CD1 LEU A  95      46.584  68.235  27.322  1.00  8.32           C  
ANISOU  603  CD1 LEU A  95      980   1024   1155    122    -73     14
ATOM    604  CD2 LEU A  95      46.712  68.563  24.834  1.00  9.91           C  
ANISOU  604  CD2 LEU A  95     1269    967   1529    123     78    224
ATOM    605  N   GLY A  96      43.293  72.601  26.235  1.00  6.60           N  
ANISOU  605  N   GLY A  96      980    719    806    110    -10     84
ATOM    606  CA  GLY A  96      42.014  73.311  26.283  1.00  6.42           C  
ANISOU  606  CA  GLY A  96      920    739    778      7    -28     98
ATOM    607  C   GLY A  96      41.786  74.165  25.058  1.00  6.58           C  
ANISOU  607  C   GLY A  96      921    827    749     31    -28     48
ATOM    608  O   GLY A  96      40.691  74.153  24.477  1.00  6.83           O  
ANISOU  608  O   GLY A  96      877    983    732     78    -76     66
ATOM    609  N   ARG A  97      42.808  74.914  24.647  1.00  7.58           N  
ANISOU  609  N   ARG A  97     1078   1048    754    158    -21     69
ATOM    610  CA  ARG A  97      42.701  75.741  23.440  1.00  8.15           C  
ANISOU  610  CA  ARG A  97     1069   1136    892     93    -68     94
ATOM    611  C   ARG A  97      42.474  74.896  22.183  1.00  8.53           C  
ANISOU  611  C   ARG A  97     1142   1178    921    189   -135     48
ATOM    612  O   ARG A  97      41.856  75.365  21.227  1.00 10.25           O  
ANISOU  612  O   ARG A  97     1213   1539   1141    319     -5    -47
ATOM    613  CB  ARG A  97      43.939  76.623  23.266  1.00  7.88           C  
ANISOU  613  CB  ARG A  97     1049   1158    785     82    -40     49
ATOM    614  CG  ARG A  97      44.128  77.647  24.366  1.00  8.39           C  
ANISOU  614  CG  ARG A  97     1063   1229    894     36     24     54
ATOM    615  CD  ARG A  97      45.243  78.657  24.074  1.00  9.34           C  
ANISOU  615  CD  ARG A  97     1183   1292   1072    -51    -96    178
ATOM    616  NE  ARG A  97      44.906  79.524  22.947  1.00 10.05           N  
ANISOU  616  NE  ARG A  97     1092   1422   1303   -101   -117    232
ATOM    617  CZ  ARG A  97      45.295  79.367  21.679  1.00 11.05           C  
ANISOU  617  CZ  ARG A  97     1295   1510   1392    -30    -95    183
ATOM    618  NH1 ARG A  97      46.118  78.396  21.313  1.00 11.59           N  
ANISOU  618  NH1 ARG A  97     1236   1645   1521    117    -75    389
ATOM    619  NH2 ARG A  97      44.859  80.224  20.766  1.00 12.40           N1+
ANISOU  619  NH2 ARG A  97     1500   1681   1531     77      7    311
ATOM    620  N   CYS A  98      42.963  73.658  22.190  1.00  8.86           N  
ANISOU  620  N   CYS A  98     1208   1110   1045    167    -19    110
ATOM    621  CA  CYS A  98      42.770  72.725  21.092  0.50  9.28           C  
ANISOU  621  CA  CYS A  98     1271   1110   1144    149    -65    106
ATOM    622  C   CYS A  98      41.312  72.246  20.941  1.00  9.13           C  
ANISOU  622  C   CYS A  98     1275   1014   1179    146    -17    119
ATOM    623  O   CYS A  98      40.953  71.645  19.930  1.00 10.62           O  
ANISOU  623  O   CYS A  98     1488   1119   1428    101    -14     81
ATOM    624  CB  CYS A  98      43.705  71.531  21.323  0.50  9.89           C  
ANISOU  624  CB  CYS A  98     1414   1152   1191    169    -73    121
ATOM    625  SG  CYS A  98      43.958  70.479  19.923  0.50 10.78           S  
ANISOU  625  SG  CYS A  98     1503   1180   1410     83    -14    295
ATOM    626  N   GLY A  99      40.491  72.479  21.965  1.00  7.93           N  
ANISOU  626  N   GLY A  99     1051    873   1088    198   -116    149
ATOM    627  CA  GLY A  99      39.100  72.099  21.907  1.00  8.16           C  
ANISOU  627  CA  GLY A  99     1043    990   1068    156    -49     48
ATOM    628  C   GLY A  99      38.777  70.720  22.453  1.00  7.60           C  
ANISOU  628  C   GLY A  99      984    905    997    120    -44    130
ATOM    629  O   GLY A  99      37.637  70.278  22.340  1.00  8.56           O  
ANISOU  629  O   GLY A  99     1022   1114   1115    159    -81    -38
ATOM    630  N   LEU A 100      39.772  70.055  23.034  1.00  7.16           N  
ANISOU  630  N   LEU A 100     1019    818    881    113    -24    188
ATOM    631  CA  LEU A 100      39.609  68.689  23.519  1.00  7.06           C  
ANISOU  631  CA  LEU A 100     1003    823    857     94      0    104
ATOM    632  C   LEU A 100      38.809  68.636  24.815  1.00  6.18           C  
ANISOU  632  C   LEU A 100      876    702    769     45     15    155
ATOM    633  O   LEU A 100      38.885  69.542  25.652  1.00  6.38           O  
ANISOU  633  O   LEU A 100      813    718    894     19     32    104
ATOM    634  CB  LEU A 100      40.976  68.056  23.782  1.00  7.81           C  
ANISOU  634  CB  LEU A 100     1019   1027    921     32     11    190
ATOM    635  CG  LEU A 100      41.889  67.922  22.558  1.00  8.55           C  
ANISOU  635  CG  LEU A 100     1364    969    912     66    -79    153
ATOM    636  CD1 LEU A 100      43.321  67.637  22.945  1.00 10.82           C  
ANISOU  636  CD1 LEU A 100     1484   1466   1159    145     97    213
ATOM    637  CD2 LEU A 100      41.361  66.815  21.658  1.00 11.48           C  
ANISOU  637  CD2 LEU A 100     1971   1057   1334    -28   -172    114
ATOM    638  N   ASP A 101      38.054  67.563  24.993  1.00  5.26           N  
ANISOU  638  N   ASP A 101      749    528    722     63     19     91
ATOM    639  CA  ASP A 101      37.476  67.256  26.298  1.00  5.26           C  
ANISOU  639  CA  ASP A 101      686    567    744      0     64    138
ATOM    640  C   ASP A 101      38.610  66.885  27.256  1.00  4.88           C  
ANISOU  640  C   ASP A 101      630    541    684    -30     55    105
ATOM    641  O   ASP A 101      39.426  66.031  26.929  1.00  6.00           O  
ANISOU  641  O   ASP A 101      938    528    811     26    222    165
ATOM    642  CB  ASP A 101      36.498  66.088  26.253  1.00  5.66           C  
ANISOU  642  CB  ASP A 101      795    516    839    -76     38    163
ATOM    643  CG  ASP A 101      35.219  66.374  25.498  1.00  6.81           C  
ANISOU  643  CG  ASP A 101     1024    694    868   -143    -57    101
ATOM    644  OD1 ASP A 101      34.884  67.556  25.231  1.00  7.05           O  
ANISOU  644  OD1 ASP A 101     1143    559    974   -116    243    -44
ATOM    645  OD2 ASP A 101      34.523  65.364  25.205  1.00  9.56           O1-
ANISOU  645  OD2 ASP A 101     1225   1302   1103   -227     52    -96
ATOM    646  N   LEU A 102      38.655  67.537  28.421  1.00  4.79           N  
ANISOU  646  N   LEU A 102      639    513    667    -50    156    115
ATOM    647  CA  LEU A 102      39.705  67.319  29.416  1.00  5.12           C  
ANISOU  647  CA  LEU A 102      637    590    717     29     83     96
ATOM    648  C   LEU A 102      39.168  66.840  30.744  1.00  5.15           C  
ANISOU  648  C   LEU A 102      567    669    721    -15     16     92
ATOM    649  O   LEU A 102      38.166  67.356  31.240  1.00  5.67           O  
ANISOU  649  O   LEU A 102      582    777    796     61    145    199
ATOM    650  CB  LEU A 102      40.510  68.591  29.708  1.00  6.09           C  
ANISOU  650  CB  LEU A 102      754    760    799    -48     81     25
ATOM    651  CG  LEU A 102      41.135  69.320  28.523  1.00  6.47           C  
ANISOU  651  CG  LEU A 102      638    799   1022      6     49     53
ATOM    652  CD1 LEU A 102      41.973  70.450  29.087  1.00  8.44           C  
ANISOU  652  CD1 LEU A 102     1087   1133    986    -26   -135    -68
ATOM    653  CD2 LEU A 102      41.976  68.396  27.693  1.00  9.01           C  
ANISOU  653  CD2 LEU A 102     1164   1037   1222     84     11    350
ATOM    654  N   ILE A 103      39.881  65.883  31.326  1.00  5.19           N  
ANISOU  654  N   ILE A 103      593    545    830     -6    109    155
ATOM    655  CA  ILE A 103      39.753  65.535  32.733  1.00  5.71           C  
ANISOU  655  CA  ILE A 103      699    603    865     -2     73    103
ATOM    656  C   ILE A 103      41.081  65.899  33.395  1.00  5.80           C  
ANISOU  656  C   ILE A 103      737    573    893     84    148     89
ATOM    657  O   ILE A 103      42.102  65.296  33.102  1.00  6.80           O  
ANISOU  657  O   ILE A 103      932    759    892     34    172    161
ATOM    658  CB  ILE A 103      39.403  64.056  32.953  1.00  6.00           C  
ANISOU  658  CB  ILE A 103      767    579    932     -6     88    110
ATOM    659  CG1 ILE A 103      38.039  63.765  32.307  1.00  6.31           C  
ANISOU  659  CG1 ILE A 103      717    773    908   -194    -26     73
ATOM    660  CG2 ILE A 103      39.448  63.728  34.457  1.00  7.23           C  
ANISOU  660  CG2 ILE A 103      826    757   1163     37    122     18
ATOM    661  CD1 ILE A 103      37.663  62.293  32.247  1.00  7.51           C  
ANISOU  661  CD1 ILE A 103      767    948   1136   -226     -1     80
ATOM    662  N   VAL A 104      41.058  66.948  34.224  1.00  6.06           N  
ANISOU  662  N   VAL A 104      828    633    839     23    147     54
ATOM    663  CA  VAL A 104      42.232  67.447  34.933  1.00  6.91           C  
ANISOU  663  CA  VAL A 104      933    766    923     42     69     33
ATOM    664  C   VAL A 104      42.162  66.936  36.382  1.00  7.17           C  
ANISOU  664  C   VAL A 104     1015    737    972     88    152     -3
ATOM    665  O   VAL A 104      41.134  67.099  37.044  1.00  7.32           O  
ANISOU  665  O   VAL A 104     1043    670   1068     97    240     54
ATOM    666  CB  VAL A 104      42.299  68.999  34.951  1.00  7.16           C  
ANISOU  666  CB  VAL A 104      984    795    942     19    -16     -9
ATOM    667  CG1 VAL A 104      43.573  69.550  35.624  1.00  9.15           C  
ANISOU  667  CG1 VAL A 104     1402    885   1189     31    -23   -216
ATOM    668  CG2 VAL A 104      42.166  69.597  33.535  1.00  8.38           C  
ANISOU  668  CG2 VAL A 104     1110    954   1120     94    -93    111
ATOM    669  N   GLN A 105      43.245  66.311  36.841  1.00  7.53           N  
ANISOU  669  N   GLN A 105     1006    850   1004     -4    134     30
ATOM    670  CA  GLN A 105      43.309  65.627  38.120  1.00  7.64           C  
ANISOU  670  CA  GLN A 105      975    888   1037    -11    129    -48
ATOM    671  C   GLN A 105      44.618  66.047  38.800  1.00  7.15           C  
ANISOU  671  C   GLN A 105      806    932    975     17    207    -59
ATOM    672  O   GLN A 105      45.686  65.596  38.387  1.00  7.20           O  
ANISOU  672  O   GLN A 105      847    810   1078    -12    192    -35
ATOM    673  CB  GLN A 105      43.148  64.117  37.839  1.00  8.37           C  
ANISOU  673  CB  GLN A 105     1117   1016   1044    -92     58    -82
ATOM    674  CG  GLN A 105      43.027  63.215  39.078  1.00  9.41           C  
ANISOU  674  CG  GLN A 105     1223   1045   1305    -64     24   -104
ATOM    675  CD  GLN A 105      44.373  62.839  39.681  1.00 10.53           C  
ANISOU  675  CD  GLN A 105     1336   1211   1454     53     97     64
ATOM    676  OE1 GLN A 105      45.236  62.287  39.003  1.00 11.61           O  
ANISOU  676  OE1 GLN A 105     1339   1410   1659   -102     61    -34
ATOM    677  NE2 GLN A 105      44.557  63.096  40.966  1.00 10.60           N  
ANISOU  677  NE2 GLN A 105     1050   1280   1695    176    156   -195
ATOM    678  N   ALA A 106      44.528  66.918  39.811  1.00  7.35           N  
ANISOU  678  N   ALA A 106      829    979    982     -6    168   -196
ATOM    679  CA  ALA A 106      45.678  67.435  40.548  1.00  8.03           C  
ANISOU  679  CA  ALA A 106      935   1068   1046    -11    165   -136
ATOM    680  C   ALA A 106      45.234  67.923  41.928  1.00  8.37           C  
ANISOU  680  C   ALA A 106      962   1080   1135    -19    140   -141
ATOM    681  O   ALA A 106      44.082  68.312  42.086  1.00  7.67           O  
ANISOU  681  O   ALA A 106      893    900   1120    -97     25   -200
ATOM    682  CB  ALA A 106      46.358  68.568  39.754  1.00  8.69           C  
ANISOU  682  CB  ALA A 106     1015   1156   1128     11     54   -158
ATOM    683  N   LYS A 107      46.156  67.905  42.898  1.00  9.47           N  
ANISOU  683  N   LYS A 107     1121   1206   1270     31    223   -172
ATOM    684  CA  LYS A 107      45.908  68.279  44.295  1.00 10.59           C  
ANISOU  684  CA  LYS A 107     1280   1307   1437     49    129   -104
ATOM    685  C   LYS A 107      45.434  69.735  44.465  1.00  9.88           C  
ANISOU  685  C   LYS A 107     1250   1170   1334     45     76   -158
ATOM    686  O   LYS A 107      45.624  70.570  43.574  1.00  9.32           O  
ANISOU  686  O   LYS A 107     1243   1022   1274    190    112   -227
ATOM    687  CB  LYS A 107      47.180  67.986  45.122  1.00 11.43           C  
ANISOU  687  CB  LYS A 107     1330   1388   1622     67    142   -137
ATOM    688  CG  LYS A 107      48.367  68.912  44.818  1.00 14.39           C  
ANISOU  688  CG  LYS A 107     1774   1816   1879     45    138    -36
ATOM    689  CD  LYS A 107      49.690  68.411  45.408  1.00 14.84           C  
ANISOU  689  CD  LYS A 107     1887   1963   1788     74    146   -117
ATOM    690  CE  LYS A 107      50.850  69.381  45.158  1.00 17.03           C  
ANISOU  690  CE  LYS A 107     2256   2267   1947     33     76   -116
ATOM    691  NZ  LYS A 107      50.641  70.676  45.832  1.00 20.40           N1+
ANISOU  691  NZ  LYS A 107     2685   2763   2300    124    219   -206
ATOM    692  N   SER A 108      44.846  70.008  45.629  1.00 10.38           N  
ANISOU  692  N   SER A 108     1236   1242   1465     84     68    -98
ATOM    693  CA  SER A 108      44.258  71.286  45.991  1.00 10.98           C  
ANISOU  693  CA  SER A 108     1361   1289   1520     62     65    -77
ATOM    694  C   SER A 108      45.250  72.457  45.951  1.00  9.88           C  
ANISOU  694  C   SER A 108     1265   1072   1417     29    106   -103
ATOM    695  O   SER A 108      46.352  72.363  46.494  1.00 10.92           O  
ANISOU  695  O   SER A 108     1403   1179   1564    -21     90   -153
ATOM    696  CB  SER A 108      43.583  71.116  47.365  1.00 12.83           C  
ANISOU  696  CB  SER A 108     1625   1526   1723      0     18     47
ATOM    697  OG  SER A 108      44.493  70.545  48.292  1.00 18.03           O  
ANISOU  697  OG  SER A 108     2282   2315   2252     68    111    -60
ATOM    698  N   GLY A 109      44.826  73.554  45.322  1.00  9.30           N  
ANISOU  698  N   GLY A 109     1204    945   1383     75     76   -102
ATOM    699  CA  GLY A 109      45.570  74.805  45.300  1.00  9.61           C  
ANISOU  699  CA  GLY A 109     1264   1074   1313     69     90   -176
ATOM    700  C   GLY A 109      46.668  74.813  44.228  1.00 10.05           C  
ANISOU  700  C   GLY A 109     1348   1196   1274    -19     69   -135
ATOM    701  O   GLY A 109      47.512  75.703  44.272  1.00 11.49           O  
ANISOU  701  O   GLY A 109     1541   1312   1513     -4      8   -291
ATOM    702  N   THR A 110      46.674  73.867  43.277  1.00  9.11           N  
ANISOU  702  N   THR A 110     1229   1055   1175     67     76   -239
ATOM    703  CA  THR A 110      47.586  73.864  42.123  1.00  9.34           C  
ANISOU  703  CA  THR A 110     1242   1153   1154    -21    105   -156
ATOM    704  C   THR A 110      47.147  74.851  41.013  1.00  9.05           C  
ANISOU  704  C   THR A 110     1190   1143   1105      4     88    -73
ATOM    705  O   THR A 110      47.919  75.103  40.081  1.00 10.80           O  
ANISOU  705  O   THR A 110     1265   1427   1408     97    171    110
ATOM    706  CB  THR A 110      47.676  72.446  41.501  1.00  9.27           C  
ANISOU  706  CB  THR A 110     1191   1173   1155    -69    156   -107
ATOM    707  OG1 THR A 110      46.388  71.879  41.313  1.00  9.27           O  
ANISOU  707  OG1 THR A 110     1261   1030   1228    -83    175   -201
ATOM    708  CG2 THR A 110      48.489  71.489  42.378  1.00 10.52           C  
ANISOU  708  CG2 THR A 110     1135   1517   1345    -10    310   -150
ATOM    709  N   GLY A 111      45.945  75.428  41.148  1.00  8.24           N  
ANISOU  709  N   GLY A 111     1165   1034    928     25     65   -101
ATOM    710  CA  GLY A 111      45.433  76.431  40.231  1.00  8.09           C  
ANISOU  710  CA  GLY A 111     1061   1095    916    -23     65    -70
ATOM    711  C   GLY A 111      44.584  75.773  39.143  1.00  7.16           C  
ANISOU  711  C   GLY A 111      909    965    845     20     69    -34
ATOM    712  O   GLY A 111      44.585  76.278  38.020  1.00  7.11           O  
ANISOU  712  O   GLY A 111      865    944    891     38     46    -61
ATOM    713  N   LYS A 112      43.865  74.680  39.459  1.00  6.76           N  
ANISOU  713  N   LYS A 112      820    939    809     74     60   -137
ATOM    714  CA  LYS A 112      42.884  74.034  38.578  1.00  6.73           C  
ANISOU  714  CA  LYS A 112      835    903    819     55     98   -103
ATOM    715  C   LYS A 112      41.742  74.979  38.186  1.00  6.32           C  
ANISOU  715  C   LYS A 112      824    822    754     20     82   -104
ATOM    716  O   LYS A 112      41.343  74.979  37.022  1.00  6.38           O  
ANISOU  716  O   LYS A 112      794    722    905    135     57    -41
ATOM    717  CB  LYS A 112      42.271  72.787  39.238  1.00  6.77           C  
ANISOU  717  CB  LYS A 112      825    889    856    -30     83   -124
ATOM    718  CG  LYS A 112      43.240  71.610  39.413  1.00  6.81           C  
ANISOU  718  CG  LYS A 112      901    760    927     99    119    -77
ATOM    719  CD  LYS A 112      42.544  70.341  39.944  1.00  7.50           C  
ANISOU  719  CD  LYS A 112      814   1023   1011     98    193   -177
ATOM    720  CE  LYS A 112      41.831  70.506  41.301  1.00  8.12           C  
ANISOU  720  CE  LYS A 112      756   1100   1227     16    -32   -128
ATOM    721  NZ  LYS A 112      42.727  71.048  42.330  1.00  7.60           N1+
ANISOU  721  NZ  LYS A 112      884    967   1036     38     10   -263
ATOM    722  N   THR A 113      41.262  75.792  39.136  1.00  6.88           N  
ANISOU  722  N   THR A 113      782    897    935    -50    155    -83
ATOM    723  CA  THR A 113      40.293  76.831  38.818  1.00  7.00           C  
ANISOU  723  CA  THR A 113      802    925    931    -32    104    -55
ATOM    724  C   THR A 113      40.902  77.936  37.931  1.00  7.73           C  
ANISOU  724  C   THR A 113      871   1119    944    -60     71    -86
ATOM    725  O   THR A 113      40.212  78.367  37.016  1.00  7.78           O  
ANISOU  725  O   THR A 113      849   1114    990    -55    112    -98
ATOM    726  CB  THR A 113      39.525  77.354  40.067  1.00  6.97           C  
ANISOU  726  CB  THR A 113      794    904    951    -17    153    -43
ATOM    727  OG1 THR A 113      39.160  76.224  40.864  1.00  8.65           O  
ANISOU  727  OG1 THR A 113     1061   1020   1205    142     41     50
ATOM    728  CG2 THR A 113      38.383  78.354  39.831  1.00  8.06           C  
ANISOU  728  CG2 THR A 113      895   1115   1051   -222    200   -103
ATOM    729  N   CYS A 114      42.209  78.271  38.061  1.00  8.14           N  
ANISOU  729  N   CYS A 114      919   1251    923      4     63   -151
ATOM    730  CA  CYS A 114      42.792  79.210  37.157  0.50  8.41           C  
ANISOU  730  CA  CYS A 114      899   1331    962    -27     27   -108
ATOM    731  C   CYS A 114      42.929  78.604  35.738  1.00  8.08           C  
ANISOU  731  C   CYS A 114      840   1329    901     55    -14   -117
ATOM    732  O   CYS A 114      42.682  79.313  34.745  1.00  9.33           O  
ANISOU  732  O   CYS A 114      818   1669   1055    275    -38   -201
ATOM    733  CB  CYS A 114      44.096  79.751  37.762  0.50  8.71           C  
ANISOU  733  CB  CYS A 114      867   1401   1041    -53      3   -200
ATOM    734  SG  CYS A 114      43.805  80.804  39.251  0.50 13.05           S  
ANISOU  734  SG  CYS A 114     1346   1817   1794   -240    150   -224
ATOM    735  N   VAL A 115      43.273  77.300  35.626  0.50  7.37           N  
ANISOU  735  N   VAL A 115      828   1196    776     50     12    -46
ATOM    736  CA  VAL A 115      43.296  76.569  34.321  0.50  7.07           C  
ANISOU  736  CA  VAL A 115      783   1094    809     61     31     36
ATOM    737  C   VAL A 115      42.011  76.828  33.564  0.50  6.19           C  
ANISOU  737  C   VAL A 115      719    895    738     10     24     78
ATOM    738  O   VAL A 115      42.015  77.418  32.484  0.50  6.13           O  
ANISOU  738  O   VAL A 115      753    826    747     56     60    157
ATOM    739  CB  VAL A 115      43.500  74.990  34.437  0.50  6.28           C  
ANISOU  739  CB  VAL A 115      777    928    678     17    -13     17
ATOM    740  CG1 VAL A 115      43.136  74.236  33.118  0.50  6.53           C  
ANISOU  740  CG1 VAL A 115      659    930    889     23    173    172
ATOM    741  CG2 VAL A 115      44.924  74.654  34.872  0.50  7.08           C  
ANISOU  741  CG2 VAL A 115      877   1011    800    101    140    101
ATOM    742  N   PHE A 116      40.898  76.393  34.137  1.00  5.92           N  
ANISOU  742  N   PHE A 116      693    800    754     69      2     81
ATOM    743  CA  PHE A 116      39.655  76.437  33.381  1.00  6.13           C  
ANISOU  743  CA  PHE A 116      734    831    762     28    -21     49
ATOM    744  C   PHE A 116      39.159  77.846  33.158  1.00  5.61           C  
ANISOU  744  C   PHE A 116      658    775    696     16    -77    -15
ATOM    745  O   PHE A 116      38.545  78.112  32.131  1.00  5.75           O  
ANISOU  745  O   PHE A 116      731    700    753    158    -69    -26
ATOM    746  CB  PHE A 116      38.572  75.475  33.898  1.00  5.87           C  
ANISOU  746  CB  PHE A 116      661    728    839    -26    -55      8
ATOM    747  CG  PHE A 116      37.920  75.849  35.211  1.00  5.22           C  
ANISOU  747  CG  PHE A 116      625    660    700    -47   -141    -79
ATOM    748  CD1 PHE A 116      37.084  76.935  35.328  1.00  4.70           C  
ANISOU  748  CD1 PHE A 116      489    608    687     48   -116    -63
ATOM    749  CD2 PHE A 116      38.058  75.028  36.317  1.00  6.69           C  
ANISOU  749  CD2 PHE A 116      657    918    964   -132    146     78
ATOM    750  CE1 PHE A 116      36.431  77.203  36.527  1.00  5.29           C  
ANISOU  750  CE1 PHE A 116      709    695    603   -164     -7     -2
ATOM    751  CE2 PHE A 116      37.408  75.278  37.499  1.00  6.38           C  
ANISOU  751  CE2 PHE A 116      523    856   1042    -39    -45     25
ATOM    752  CZ  PHE A 116      36.600  76.389  37.611  1.00  5.68           C  
ANISOU  752  CZ  PHE A 116      646    650    862   -202    -79     14
ATOM    753  N   SER A 117      39.456  78.746  34.089  1.00  5.90           N  
ANISOU  753  N   SER A 117      663    855    723      3    -44   -113
ATOM    754  CA  SER A 117      39.056  80.136  33.926  1.00  6.01           C  
ANISOU  754  CA  SER A 117      631    908    741      7    -38    -25
ATOM    755  C   SER A 117      39.811  80.771  32.761  1.00  5.89           C  
ANISOU  755  C   SER A 117      648    941    645      8    -48    -56
ATOM    756  O   SER A 117      39.248  81.568  32.009  1.00  6.03           O  
ANISOU  756  O   SER A 117      661    945    683     67    -30   -147
ATOM    757  CB  SER A 117      39.313  80.920  35.220  1.00  6.04           C  
ANISOU  757  CB  SER A 117      622    974    698    -80      8    -51
ATOM    758  OG  SER A 117      38.500  80.435  36.290  1.00  6.67           O  
ANISOU  758  OG  SER A 117      676    893    964     12    -59     -2
ATOM    759  N   THR A 118      41.091  80.418  32.617  1.00  6.31           N  
ANISOU  759  N   THR A 118      692   1054    649     38    -61    -57
ATOM    760  CA  THR A 118      41.934  80.944  31.531  1.00  6.62           C  
ANISOU  760  CA  THR A 118      764   1029    720     12    -52    -18
ATOM    761  C   THR A 118      41.507  80.377  30.178  1.00  6.65           C  
ANISOU  761  C   THR A 118      730   1026    769     63    -81     26
ATOM    762  O   THR A 118      41.389  81.101  29.191  1.00  7.01           O  
ANISOU  762  O   THR A 118      798   1060    804    104   -106     24
ATOM    763  CB  THR A 118      43.414  80.633  31.835  1.00  6.98           C  
ANISOU  763  CB  THR A 118      863   1073    716     65    -80    -79
ATOM    764  OG1 THR A 118      43.791  81.269  33.067  1.00  8.51           O  
ANISOU  764  OG1 THR A 118     1217   1217    800     13    -63    -91
ATOM    765  CG2 THR A 118      44.325  81.121  30.741  1.00  7.99           C  
ANISOU  765  CG2 THR A 118      869   1305    859     42   -127     71
ATOM    766  N   ILE A 119      41.273  79.066  30.130  1.00  5.79           N  
ANISOU  766  N   ILE A 119      609    894    697     30    -18     30
ATOM    767  CA  ILE A 119      40.769  78.459  28.903  1.00  5.86           C  
ANISOU  767  CA  ILE A 119      705    847    671     44    -68    105
ATOM    768  C   ILE A 119      39.448  79.107  28.509  1.00  5.66           C  
ANISOU  768  C   ILE A 119      597    807    747     58    -64     45
ATOM    769  O   ILE A 119      39.228  79.443  27.334  1.00  6.35           O  
ANISOU  769  O   ILE A 119      645    955    811    104      3     59
ATOM    770  CB  ILE A 119      40.630  76.926  29.071  1.00  6.07           C  
ANISOU  770  CB  ILE A 119      688    876    740     56    -25    104
ATOM    771  CG1 ILE A 119      42.006  76.254  29.242  1.00  7.11           C  
ANISOU  771  CG1 ILE A 119      844    898    959    112     57    142
ATOM    772  CG2 ILE A 119      39.870  76.306  27.898  1.00  7.49           C  
ANISOU  772  CG2 ILE A 119      926   1017    903    -98      2    -53
ATOM    773  CD1 ILE A 119      41.931  74.812  29.794  1.00  7.85           C  
ANISOU  773  CD1 ILE A 119      751   1099   1131      3    -48    175
ATOM    774  N   ALA A 120      38.551  79.259  29.480  1.00  5.65           N  
ANISOU  774  N   ALA A 120      624    802    720     87     -4     10
ATOM    775  CA  ALA A 120      37.271  79.893  29.223  1.00  5.38           C  
ANISOU  775  CA  ALA A 120      604    764    673     54    -35     -4
ATOM    776  C   ALA A 120      37.411  81.303  28.646  1.00  5.16           C  
ANISOU  776  C   ALA A 120      605    622    732     70    -21     40
ATOM    777  O   ALA A 120      36.834  81.629  27.607  1.00  5.14           O  
ANISOU  777  O   ALA A 120      523    589    840    107   -138    -46
ATOM    778  CB  ALA A 120      36.431  79.923  30.511  1.00  5.91           C  
ANISOU  778  CB  ALA A 120      658    814    773    120   -112     98
ATOM    779  N   LEU A 121      38.154  82.162  29.337  1.00  4.98           N  
ANISOU  779  N   LEU A 121      461    757    674     31    -91    -84
ATOM    780  CA  LEU A 121      38.309  83.541  28.866  1.00  5.10           C  
ANISOU  780  CA  LEU A 121      524    776    635      8    -38    -15
ATOM    781  C   LEU A 121      38.946  83.615  27.484  1.00  5.70           C  
ANISOU  781  C   LEU A 121      535    817    813     19    -19    -13
ATOM    782  O   LEU A 121      38.517  84.427  26.650  1.00  6.19           O  
ANISOU  782  O   LEU A 121      456    928    966     60    -23     14
ATOM    783  CB  LEU A 121      39.089  84.371  29.880  1.00  5.23           C  
ANISOU  783  CB  LEU A 121      529    760    696    -13    -98   -121
ATOM    784  CG  LEU A 121      38.277  84.740  31.116  1.00  5.85           C  
ANISOU  784  CG  LEU A 121      707    748    765     60   -105    -23
ATOM    785  CD1 LEU A 121      39.207  85.257  32.175  1.00  8.18           C  
ANISOU  785  CD1 LEU A 121     1083    865   1160     36   -153    -86
ATOM    786  CD2 LEU A 121      37.183  85.753  30.844  1.00  6.71           C  
ANISOU  786  CD2 LEU A 121      683    896    969   -137    -75    354
ATOM    787  N   ASP A 122      39.939  82.768  27.217  1.00  5.95           N  
ANISOU  787  N   ASP A 122      534    890    836     87     -8     39
ATOM    788  CA  ASP A 122      40.603  82.795  25.916  1.00  5.72           C  
ANISOU  788  CA  ASP A 122      537    857    776     54    -50     53
ATOM    789  C   ASP A 122      39.682  82.360  24.794  1.00  6.14           C  
ANISOU  789  C   ASP A 122      609    874    847     81     12    110
ATOM    790  O   ASP A 122      39.862  82.771  23.656  1.00  7.90           O  
ANISOU  790  O   ASP A 122      933   1070    997    233   -117    134
ATOM    791  CB  ASP A 122      41.880  81.957  25.930  1.00  6.49           C  
ANISOU  791  CB  ASP A 122      761    858    844    107     -8     63
ATOM    792  CG  ASP A 122      42.793  82.277  24.776  1.00  8.49           C  
ANISOU  792  CG  ASP A 122      970   1142   1113    170     93    -14
ATOM    793  OD1 ASP A 122      43.278  83.421  24.739  1.00 11.88           O  
ANISOU  793  OD1 ASP A 122     1209   2082   1223    213    -73     -8
ATOM    794  OD2 ASP A 122      42.997  81.391  23.950  1.00 12.63           O1-
ANISOU  794  OD2 ASP A 122     1482   1642   1673    104    464    203
ATOM    795  N   SER A 123      38.690  81.525  25.112  1.00  6.13           N  
ANISOU  795  N   SER A 123      606    946    775     51      0     32
ATOM    796  CA  SER A 123      37.761  81.010  24.114  1.00  6.08           C  
ANISOU  796  CA  SER A 123      673    892    745     21      9     16
ATOM    797  C   SER A 123      36.639  81.978  23.771  1.00  6.21           C  
ANISOU  797  C   SER A 123      705    960    693     75     -9     43
ATOM    798  O   SER A 123      35.918  81.761  22.786  1.00  7.22           O  
ANISOU  798  O   SER A 123     1006    951    787    209     71     87
ATOM    799  CB  SER A 123      37.128  79.698  24.587  1.00  7.04           C  
ANISOU  799  CB  SER A 123      827   1040    806    -32    -28    -74
ATOM    800  OG  SER A 123      36.136  79.929  25.584  1.00  7.08           O  
ANISOU  800  OG  SER A 123      788   1050    848    109   -135   -127
ATOM    801  N   LEU A 124      36.429  82.988  24.611  1.00  5.94           N  
ANISOU  801  N   LEU A 124      639    838    777    134     36    -15
ATOM    802  CA  LEU A 124      35.245  83.847  24.481  1.00  6.68           C  
ANISOU  802  CA  LEU A 124      795    910    833     85      4     33
ATOM    803  C   LEU A 124      35.310  84.719  23.238  1.00  6.58           C  
ANISOU  803  C   LEU A 124      697    974    825    103    -36     30
ATOM    804  O   LEU A 124      36.361  85.259  22.927  1.00  8.54           O  
ANISOU  804  O   LEU A 124      840   1468    933    220    -37     34
ATOM    805  CB  LEU A 124      35.140  84.755  25.703  1.00  7.43           C  
ANISOU  805  CB  LEU A 124      891    989    942     46     19    -55
ATOM    806  CG  LEU A 124      33.779  85.385  25.984  1.00  8.79           C  
ANISOU  806  CG  LEU A 124     1044   1045   1248     -9     79     -6
ATOM    807  CD1 LEU A 124      32.754  84.313  26.327  1.00 10.07           C  
ANISOU  807  CD1 LEU A 124     1852   1012    961    -81   -307    162
ATOM    808  CD2 LEU A 124      33.936  86.356  27.147  1.00  9.95           C  
ANISOU  808  CD2 LEU A 124     1493   1003   1283   -240   -146     35
ATOM    809  N   VAL A 125      34.158  84.877  22.581  1.00  6.16           N  
ANISOU  809  N   VAL A 125      546    998    794    172    -36     77
ATOM    810  CA  VAL A 125      33.965  85.877  21.524  1.00  6.48           C  
ANISOU  810  CA  VAL A 125      622    981    858    172    -17     37
ATOM    811  C   VAL A 125      33.292  87.055  22.244  1.00  6.24           C  
ANISOU  811  C   VAL A 125      612    931    828    207     30     19
ATOM    812  O   VAL A 125      32.084  87.071  22.473  1.00  6.30           O  
ANISOU  812  O   VAL A 125      570   1023    800    240     50     78
ATOM    813  CB  VAL A 125      33.123  85.348  20.356  1.00  6.87           C  
ANISOU  813  CB  VAL A 125      659    909   1040    170     24     67
ATOM    814  CG1 VAL A 125      32.985  86.443  19.311  1.00  8.38           C  
ANISOU  814  CG1 VAL A 125      778   1128   1276    323     69     44
ATOM    815  CG2 VAL A 125      33.775  84.100  19.739  1.00  9.33           C  
ANISOU  815  CG2 VAL A 125     1187    993   1364     76    125    130
ATOM    816  N   LEU A 126      34.106  88.007  22.673  1.00  6.83           N  
ANISOU  816  N   LEU A 126      733   1061    800    161     73      3
ATOM    817  CA  LEU A 126      33.665  89.065  23.568  1.00  6.58           C  
ANISOU  817  CA  LEU A 126      662    974    864    122    -32    -21
ATOM    818  C   LEU A 126      32.563  89.932  22.947  1.00  6.32           C  
ANISOU  818  C   LEU A 126      667    906    828    154    -23    -24
ATOM    819  O   LEU A 126      31.651  90.398  23.626  1.00  5.88           O  
ANISOU  819  O   LEU A 126      539    826    867     84   -111     12
ATOM    820  CB  LEU A 126      34.860  89.918  23.988  1.00  7.50           C  
ANISOU  820  CB  LEU A 126      855   1027    968    206     50   -136
ATOM    821  CG  LEU A 126      34.651  90.993  25.055  1.00  9.28           C  
ANISOU  821  CG  LEU A 126     1176   1247   1101     53      0    -12
ATOM    822  CD1 LEU A 126      34.201  90.434  26.412  1.00 11.97           C  
ANISOU  822  CD1 LEU A 126     1478   1550   1518    234   -126    -40
ATOM    823  CD2 LEU A 126      35.942  91.810  25.202  1.00 10.23           C  
ANISOU  823  CD2 LEU A 126     1280   1350   1256     32   -138   -170
ATOM    824  N   GLU A 127      32.679  90.193  21.649  1.00  5.98           N  
ANISOU  824  N   GLU A 127      619    874    779    130    -29     64
ATOM    825  CA  GLU A 127      31.709  91.015  20.940  1.00  6.04           C  
ANISOU  825  CA  GLU A 127      576    886    830    151    -25    -22
ATOM    826  C   GLU A 127      30.345  90.352  20.732  1.00  5.70           C  
ANISOU  826  C   GLU A 127      564    831    771    131     34     18
ATOM    827  O   GLU A 127      29.401  91.030  20.315  1.00  5.79           O  
ANISOU  827  O   GLU A 127      559    885    756    267     75      4
ATOM    828  CB  GLU A 127      32.267  91.523  19.601  1.00  6.80           C  
ANISOU  828  CB  GLU A 127      616   1092    874    205    -56     12
ATOM    829  CG  GLU A 127      32.510  90.458  18.564  1.00  8.75           C  
ANISOU  829  CG  GLU A 127      916   1184   1225    229   -166     -1
ATOM    830  CD  GLU A 127      33.893  89.803  18.616  1.00 12.49           C  
ANISOU  830  CD  GLU A 127     1661   1503   1581    163    -16    215
ATOM    831  OE1 GLU A 127      34.602  89.861  19.663  1.00 12.00           O  
ANISOU  831  OE1 GLU A 127     1599   1485   1474    359   -145    449
ATOM    832  OE2 GLU A 127      34.295  89.230  17.557  1.00 14.80           O1-
ANISOU  832  OE2 GLU A 127     1946   1544   2133    273     94    360
ATOM    833  N   ASN A 128      30.238  89.054  21.019  1.00  5.37           N  
ANISOU  833  N   ASN A 128      475    812    752    161     39    -14
ATOM    834  CA  ASN A 128      28.962  88.346  20.954  1.00  5.57           C  
ANISOU  834  CA  ASN A 128      482    809    823    163     11     13
ATOM    835  C   ASN A 128      28.413  88.223  22.377  1.00  4.97           C  
ANISOU  835  C   ASN A 128      323    786    779    168    -74    -21
ATOM    836  O   ASN A 128      28.946  87.439  23.191  1.00  5.79           O  
ANISOU  836  O   ASN A 128      349    932    917    217     32     12
ATOM    837  CB  ASN A 128      29.149  86.939  20.377  1.00  5.98           C  
ANISOU  837  CB  ASN A 128      637    790    843    129    -22     43
ATOM    838  CG  ASN A 128      29.497  86.906  18.921  1.00  8.87           C  
ANISOU  838  CG  ASN A 128      958   1118   1292     54      6     68
ATOM    839  OD1 ASN A 128      29.612  87.931  18.266  1.00 10.04           O  
ANISOU  839  OD1 ASN A 128      996   1358   1459    175   -136     17
ATOM    840  ND2 ASN A 128      29.630  85.691  18.393  1.00 12.60           N  
ANISOU  840  ND2 ASN A 128     1577   1376   1835    -56    -53    -28
ATOM    841  N   LEU A 129      27.409  89.034  22.695  1.00  4.89           N  
ANISOU  841  N   LEU A 129      476    588    791    167    -21    -22
ATOM    842  CA  LEU A 129      26.880  89.086  24.063  1.00  5.72           C  
ANISOU  842  CA  LEU A 129      547    769    854    118     12     30
ATOM    843  C   LEU A 129      25.845  87.956  24.197  1.00  5.85           C  
ANISOU  843  C   LEU A 129      581    802    839    110    -17     55
ATOM    844  O   LEU A 129      24.641  88.171  24.178  1.00  6.95           O  
ANISOU  844  O   LEU A 129      602   1088    950     65    -11    134
ATOM    845  CB  LEU A 129      26.334  90.478  24.419  1.00  6.23           C  
ANISOU  845  CB  LEU A 129      687    795    883    112    -31    121
ATOM    846  CG  LEU A 129      25.984  90.668  25.892  1.00  7.47           C  
ANISOU  846  CG  LEU A 129      952    812   1074     30      3    -26
ATOM    847  CD1 LEU A 129      27.101  90.232  26.836  1.00  9.37           C  
ANISOU  847  CD1 LEU A 129     1431    787   1342    296    142      1
ATOM    848  CD2 LEU A 129      25.650  92.124  26.131  1.00  8.71           C  
ANISOU  848  CD2 LEU A 129      962   1025   1320    -76     75      7
ATOM    849  N   SER A 130      26.371  86.756  24.361  0.60  5.53           N  
ANISOU  849  N   SER A 130      521    789    791    100    -15     44
ATOM    850  CA  SER A 130      25.594  85.531  24.425  0.60  5.81           C  
ANISOU  850  CA  SER A 130      570    795    840     73     -8     49
ATOM    851  C   SER A 130      26.301  84.603  25.391  0.60  5.47           C  
ANISOU  851  C   SER A 130      571    684    820     84    -16      5
ATOM    852  O   SER A 130      27.514  84.709  25.577  0.60  5.44           O  
ANISOU  852  O   SER A 130      485    684    897    172    -41     36
ATOM    853  CB  SER A 130      25.529  84.886  23.049  0.60  6.39           C  
ANISOU  853  CB  SER A 130      583    906    936    177     -6    -89
ATOM    854  OG  SER A 130      26.833  84.509  22.645  0.60  6.38           O  
ANISOU  854  OG  SER A 130      862    396   1165    152   -110     -7
ATOM    855  N   THR A 131      25.549  83.690  25.996  1.00  5.40           N  
ANISOU  855  N   THR A 131      522    760    770     59     -5     66
ATOM    856  CA  THR A 131      26.131  82.807  27.007  1.00  5.29           C  
ANISOU  856  CA  THR A 131      604    612    795     56     17     72
ATOM    857  C   THR A 131      26.835  81.652  26.302  1.00  4.63           C  
ANISOU  857  C   THR A 131      505    516    738    101     -2     52
ATOM    858  O   THR A 131      26.205  80.707  25.812  1.00  6.63           O  
ANISOU  858  O   THR A 131      980    735    800    -49    -46     97
ATOM    859  CB  THR A 131      25.086  82.306  28.009  1.00  5.20           C  
ANISOU  859  CB  THR A 131      591    609    776    -48    -47     89
ATOM    860  OG1 THR A 131      24.371  83.428  28.561  1.00  7.13           O  
ANISOU  860  OG1 THR A 131      636    904   1166   -131    -90    382
ATOM    861  CG2 THR A 131      25.755  81.537  29.130  1.00  6.50           C  
ANISOU  861  CG2 THR A 131      581    839   1048     96    -60    105
ATOM    862  N   GLN A 132      28.152  81.757  26.221  1.00  4.13           N  
ANISOU  862  N   GLN A 132      462    409    696    143     33     13
ATOM    863  CA  GLN A 132      28.994  80.818  25.490  1.00  4.55           C  
ANISOU  863  CA  GLN A 132      538    487    700    108     20     36
ATOM    864  C   GLN A 132      29.580  79.729  26.389  1.00  4.36           C  
ANISOU  864  C   GLN A 132      490    438    728    102     53     79
ATOM    865  O   GLN A 132      29.998  78.687  25.881  1.00  4.22           O  
ANISOU  865  O   GLN A 132      460    362    781    148     34     59
ATOM    866  CB  GLN A 132      30.132  81.588  24.819  1.00  4.48           C  
ANISOU  866  CB  GLN A 132      553    399    746    163    -20     33
ATOM    867  CG  GLN A 132      29.632  82.531  23.692  1.00  5.25           C  
ANISOU  867  CG  GLN A 132      538    714    740    203     20     -1
ATOM    868  CD  GLN A 132      30.617  83.611  23.376  1.00  5.47           C  
ANISOU  868  CD  GLN A 132      580    661    839    136     43     47
ATOM    869  OE1 GLN A 132      31.810  83.342  23.215  1.00  5.92           O  
ANISOU  869  OE1 GLN A 132      404    996    850    146      2    137
ATOM    870  NE2 GLN A 132      30.144  84.858  23.328  1.00  5.69           N  
ANISOU  870  NE2 GLN A 132      352    700   1109    139    116    136
ATOM    871  N   ILE A 133      29.606  79.994  27.698  1.00  4.25           N  
ANISOU  871  N   ILE A 133      353    436    825     41     71     23
ATOM    872  CA  ILE A 133      30.292  79.148  28.663  1.00  3.91           C  
ANISOU  872  CA  ILE A 133      369    489    625     22     22     53
ATOM    873  C   ILE A 133      29.411  78.990  29.876  1.00  3.57           C  
ANISOU  873  C   ILE A 133      362    336    656     35     31    -10
ATOM    874  O   ILE A 133      28.891  79.969  30.400  1.00  4.28           O  
ANISOU  874  O   ILE A 133      351    459    817     -1     51     43
ATOM    875  CB  ILE A 133      31.674  79.736  29.058  1.00  4.65           C  
ANISOU  875  CB  ILE A 133      435    512    818      0     33     -4
ATOM    876  CG1 ILE A 133      32.481  80.105  27.793  1.00  5.52           C  
ANISOU  876  CG1 ILE A 133      519    797    779    122   -119      3
ATOM    877  CG2 ILE A 133      32.417  78.784  29.998  1.00  4.89           C  
ANISOU  877  CG2 ILE A 133      535    523    796    127    150    -85
ATOM    878  CD1 ILE A 133      33.762  80.820  28.028  1.00  8.04           C  
ANISOU  878  CD1 ILE A 133     1222    949    883     64   -254     90
ATOM    879  N   LEU A 134      29.272  77.738  30.329  1.00  2.87           N  
ANISOU  879  N   LEU A 134      300    273    516      0     36     49
ATOM    880  CA  LEU A 134      28.505  77.374  31.519  1.00  2.96           C  
ANISOU  880  CA  LEU A 134      360    292    473    -28     14      8
ATOM    881  C   LEU A 134      29.420  76.601  32.464  1.00  2.93           C  
ANISOU  881  C   LEU A 134      337    309    465    -50     47     41
ATOM    882  O   LEU A 134      30.036  75.605  32.049  1.00  3.36           O  
ANISOU  882  O   LEU A 134      436    274    566    -35    159     18
ATOM    883  CB  LEU A 134      27.307  76.532  31.156  1.00  3.44           C  
ANISOU  883  CB  LEU A 134      393    400    511     35     44     21
ATOM    884  CG  LEU A 134      26.458  75.971  32.278  1.00  3.41           C  
ANISOU  884  CG  LEU A 134      458    371    466     27    -59     68
ATOM    885  CD1 LEU A 134      25.872  77.085  33.133  1.00  5.89           C  
ANISOU  885  CD1 LEU A 134      855    539    843    -44     -9    200
ATOM    886  CD2 LEU A 134      25.348  75.083  31.747  1.00  4.64           C  
ANISOU  886  CD2 LEU A 134      641    559    561     19   -193    -98
ATOM    887  N   ILE A 135      29.504  77.080  33.716  1.00  3.13           N  
ANISOU  887  N   ILE A 135      352    259    578     11    132     40
ATOM    888  CA  ILE A 135      30.392  76.488  34.714  1.00  3.08           C  
ANISOU  888  CA  ILE A 135      366    320    485    -24     43     51
ATOM    889  C   ILE A 135      29.549  76.112  35.934  1.00  3.09           C  
ANISOU  889  C   ILE A 135      368    277    527     -4     12     20
ATOM    890  O   ILE A 135      28.825  76.943  36.482  1.00  4.02           O  
ANISOU  890  O   ILE A 135      487    347    693     15     -1    179
ATOM    891  CB  ILE A 135      31.530  77.439  35.132  1.00  3.35           C  
ANISOU  891  CB  ILE A 135      463    285    523    -29     66    -13
ATOM    892  CG1 ILE A 135      32.202  78.071  33.899  1.00  3.48           C  
ANISOU  892  CG1 ILE A 135      398    345    575     28     43    -20
ATOM    893  CG2 ILE A 135      32.524  76.742  36.078  1.00  4.50           C  
ANISOU  893  CG2 ILE A 135      480    582    647    -33    244    -27
ATOM    894  CD1 ILE A 135      33.379  78.978  34.199  1.00  4.76           C  
ANISOU  894  CD1 ILE A 135      590    670    548    -55    -24    -69
ATOM    895  N   LEU A 136      29.656  74.844  36.352  1.00  3.05           N  
ANISOU  895  N   LEU A 136      299    298    558    -33    -17     93
ATOM    896  CA  LEU A 136      28.944  74.356  37.542  1.00  3.63           C  
ANISOU  896  CA  LEU A 136      397    388    593      0      8     63
ATOM    897  C   LEU A 136      29.891  74.156  38.715  1.00  3.92           C  
ANISOU  897  C   LEU A 136      468    470    550    -13      2     64
ATOM    898  O   LEU A 136      31.018  73.688  38.567  1.00  4.28           O  
ANISOU  898  O   LEU A 136      475    455    695    120     45     43
ATOM    899  CB  LEU A 136      28.228  73.038  37.229  1.00  3.86           C  
ANISOU  899  CB  LEU A 136      467    481    517    -44      2     43
ATOM    900  CG  LEU A 136      27.203  73.105  36.073  1.00  4.13           C  
ANISOU  900  CG  LEU A 136      483    514    570    -38     31     24
ATOM    901  CD1 LEU A 136      26.497  71.745  35.932  1.00  5.34           C  
ANISOU  901  CD1 LEU A 136      618    691    716   -130   -100     16
ATOM    902  CD2 LEU A 136      26.191  74.224  36.286  1.00  5.84           C  
ANISOU  902  CD2 LEU A 136      619    883    717   -190    236    -72
ATOM    903  N   ALA A 137      29.423  74.621  39.867  1.00  4.50           N  
ANISOU  903  N   ALA A 137      514    486    707     88     55    139
ATOM    904  CA  ALA A 137      30.135  74.619  41.131  1.00  4.55           C  
ANISOU  904  CA  ALA A 137      561    386    779     52      4    112
ATOM    905  C   ALA A 137      29.253  73.858  42.127  1.00  4.82           C  
ANISOU  905  C   ALA A 137      568    426    838     92     59     92
ATOM    906  O   ALA A 137      28.030  74.015  42.040  1.00  4.84           O  
ANISOU  906  O   ALA A 137      590    415    832     48     31    106
ATOM    907  CB  ALA A 137      30.239  76.075  41.574  1.00  6.64           C  
ANISOU  907  CB  ALA A 137      743    744   1035    -36   -138    -62
ATOM    908  N   PRO A 138      29.846  73.052  43.037  1.00  5.38           N  
ANISOU  908  N   PRO A 138      592    434   1018     52     40     46
ATOM    909  CA  PRO A 138      29.049  72.306  44.017  1.00  5.78           C  
ANISOU  909  CA  PRO A 138      582    510   1104     15    -21     84
ATOM    910  C   PRO A 138      28.179  73.189  44.915  1.00  6.39           C  
ANISOU  910  C   PRO A 138      680    538   1209    -69   -119    192
ATOM    911  O   PRO A 138      26.958  73.079  44.843  1.00  7.96           O  
ANISOU  911  O   PRO A 138      804    598   1620    -71   -319    310
ATOM    912  CB  PRO A 138      30.070  71.439  44.783  1.00  6.82           C  
ANISOU  912  CB  PRO A 138      649    624   1316    152     52     94
ATOM    913  CG  PRO A 138      31.340  71.445  43.946  1.00  7.08           C  
ANISOU  913  CG  PRO A 138      788    688   1213    105    173     89
ATOM    914  CD  PRO A 138      31.272  72.760  43.180  1.00  6.56           C  
ANISOU  914  CD  PRO A 138      895    504   1091    121     71     21
ATOM    915  N   THR A 139      28.811  74.057  45.705  1.00  5.79           N  
ANISOU  915  N   THR A 139      569    500   1130     -4   -148    148
ATOM    916  CA  THR A 139      28.114  74.896  46.661  1.00  6.25           C  
ANISOU  916  CA  THR A 139      688    586   1101     -2    -19    120
ATOM    917  C   THR A 139      28.028  76.337  46.138  1.00  5.71           C  
ANISOU  917  C   THR A 139      608    613    945    -19    -30    130
ATOM    918  O   THR A 139      28.845  76.769  45.312  1.00  5.88           O  
ANISOU  918  O   THR A 139      563    547   1124     89     12     73
ATOM    919  CB  THR A 139      28.813  74.849  48.052  1.00  6.51           C  
ANISOU  919  CB  THR A 139      683    583   1206    -60     41     12
ATOM    920  OG1 THR A 139      29.973  75.659  48.195  1.00  7.62           O  
ANISOU  920  OG1 THR A 139      714    841   1339     74    162     28
ATOM    921  CG2 THR A 139      29.142  73.414  48.484  1.00  8.16           C  
ANISOU  921  CG2 THR A 139      667    898   1534    108     11    127
ATOM    922  N   ARG A 140      27.048  77.058  46.692  1.00  6.29           N  
ANISOU  922  N   ARG A 140      666    705   1016   -118    -83    154
ATOM    923  CA  ARG A 140      26.764  78.479  46.524  1.00  7.54           C  
ANISOU  923  CA  ARG A 140      795    918   1153   -112     19    130
ATOM    924  C   ARG A 140      28.005  79.368  46.755  1.00  6.29           C  
ANISOU  924  C   ARG A 140      702    618   1070    -53     -6    197
ATOM    925  O   ARG A 140      28.109  80.425  46.136  1.00  5.65           O  
ANISOU  925  O   ARG A 140      636    489   1020    -44    -32    148
ATOM    926  CB  ARG A 140      25.640  78.854  47.525  1.00 10.18           C  
ANISOU  926  CB  ARG A 140     1070   1424   1373   -363     -1    234
ATOM    927  CG  ARG A 140      24.227  78.304  47.199  1.00 13.13           C  
ANISOU  927  CG  ARG A 140     1590   1722   1677   -243      5    133
ATOM    928  CD  ARG A 140      23.331  78.187  48.446  1.00  9.39           C  
ANISOU  928  CD  ARG A 140      967   1202   1398    -60     -3    199
ATOM    929  NE  ARG A 140      21.902  78.010  48.140  1.00  8.81           N  
ANISOU  929  NE  ARG A 140     1207    879   1261   -134      9     -6
ATOM    930  CZ  ARG A 140      21.029  77.143  48.686  1.00  7.91           C  
ANISOU  930  CZ  ARG A 140     1259    749    996     16   -104     -2
ATOM    931  NH1 ARG A 140      21.408  76.144  49.495  1.00  9.99           N  
ANISOU  931  NH1 ARG A 140     1614    965   1214   -129    -14   -131
ATOM    932  NH2 ARG A 140      19.728  77.285  48.418  1.00  9.57           N1+
ANISOU  932  NH2 ARG A 140     1425    883   1327    -92    118     56
ATOM    933  N   GLU A 141      28.923  78.926  47.629  1.00  6.79           N  
ANISOU  933  N   GLU A 141      842    697   1038     28     -3    129
ATOM    934  CA  GLU A 141      30.162  79.627  47.948  1.00  7.09           C  
ANISOU  934  CA  GLU A 141      819    735   1137     -3     65     63
ATOM    935  C   GLU A 141      31.224  79.460  46.844  1.00  6.19           C  
ANISOU  935  C   GLU A 141      677    639   1035     52     44     15
ATOM    936  O   GLU A 141      31.840  80.447  46.439  1.00  6.15           O  
ANISOU  936  O   GLU A 141      663    534   1139     90     46     36
ATOM    937  CB  GLU A 141      30.697  79.158  49.319  1.00  8.07           C  
ANISOU  937  CB  GLU A 141      932    832   1300     -2     37     61
ATOM    938  CG  GLU A 141      29.679  79.294  50.472  1.00  9.72           C  
ANISOU  938  CG  GLU A 141     1331   1036   1324    121     88    -39
ATOM    939  CD  GLU A 141      30.295  79.058  51.853  1.00 11.26           C  
ANISOU  939  CD  GLU A 141     1450   1162   1666     94     69    -52
ATOM    940  OE1 GLU A 141      31.167  78.169  51.973  1.00 16.14           O  
ANISOU  940  OE1 GLU A 141     1763   1813   2554    385     -6   -492
ATOM    941  OE2 GLU A 141      29.862  79.773  52.781  1.00 14.97           O1-
ANISOU  941  OE2 GLU A 141     2040   1692   1956    -18    148   -168
ATOM    942  N   ILE A 142      31.418  78.226  46.359  1.00  5.72           N  
ANISOU  942  N   ILE A 142      645    553    973     77     55     98
ATOM    943  CA  ILE A 142      32.460  77.875  45.382  1.00  5.98           C  
ANISOU  943  CA  ILE A 142      710    639    921     74    106     49
ATOM    944  C   ILE A 142      32.274  78.596  44.035  1.00  4.83           C  
ANISOU  944  C   ILE A 142      540    484    810      6     49     68
ATOM    945  O   ILE A 142      33.236  79.104  43.460  1.00  4.89           O  
ANISOU  945  O   ILE A 142      688    431    738     32    119    -12
ATOM    946  CB  ILE A 142      32.500  76.341  45.131  1.00  5.99           C  
ANISOU  946  CB  ILE A 142      640    706    927    111    107     75
ATOM    947  CG1 ILE A 142      32.878  75.612  46.432  1.00  7.16           C  
ANISOU  947  CG1 ILE A 142      741    850   1127    -29    195     58
ATOM    948  CG2 ILE A 142      33.450  75.907  43.988  1.00  6.57           C  
ANISOU  948  CG2 ILE A 142      802    657   1034    -76    -14    170
ATOM    949  CD1 ILE A 142      32.507  74.126  46.445  1.00 10.24           C  
ANISOU  949  CD1 ILE A 142      968   1341   1582    -96    176     46
ATOM    950  N   ALA A 143      31.007  78.690  43.619  1.00  4.65           N  
ANISOU  950  N   ALA A 143      503    408    853     26     31     27
ATOM    951  CA  ALA A 143      30.523  79.443  42.458  1.00  4.82           C  
ANISOU  951  CA  ALA A 143      599    374    857     95    108     14
ATOM    952  C   ALA A 143      31.035  80.867  42.470  1.00  4.67           C  
ANISOU  952  C   ALA A 143      642    347    784     76    187     -4
ATOM    953  O   ALA A 143      31.497  81.380  41.435  1.00  4.90           O  
ANISOU  953  O   ALA A 143      524    467    870     46    110     30
ATOM    954  CB  ALA A 143      29.013  79.422  42.400  1.00  5.68           C  
ANISOU  954  CB  ALA A 143      743    565    847    145    101    -17
ATOM    955  N   VAL A 144      30.952  81.531  43.633  1.00  4.89           N  
ANISOU  955  N   VAL A 144      648    368    842     54     30     29
ATOM    956  CA  VAL A 144      31.384  82.917  43.816  1.00  5.00           C  
ANISOU  956  CA  VAL A 144      592    449    856     70     60     32
ATOM    957  C   VAL A 144      32.921  83.060  43.750  1.00  5.17           C  
ANISOU  957  C   VAL A 144      610    398    955     35     36     46
ATOM    958  O   VAL A 144      33.412  84.064  43.228  1.00  5.91           O  
ANISOU  958  O   VAL A 144      681    619    942      9     32    -16
ATOM    959  CB  VAL A 144      30.839  83.509  45.152  1.00  4.73           C  
ANISOU  959  CB  VAL A 144      536    372    888     61     26     52
ATOM    960  CG1 VAL A 144      31.376  84.909  45.519  1.00  6.48           C  
ANISOU  960  CG1 VAL A 144      776    668   1016    -64    -47     52
ATOM    961  CG2 VAL A 144      29.299  83.552  45.146  1.00  5.65           C  
ANISOU  961  CG2 VAL A 144      792    491    863   -105    103    233
ATOM    962  N   GLN A 145      33.659  82.036  44.209  1.00  5.09           N  
ANISOU  962  N   GLN A 145      671    411    851     28     86     24
ATOM    963  CA  GLN A 145      35.117  81.983  44.094  1.00  6.10           C  
ANISOU  963  CA  GLN A 145      819    643    852     30     26      0
ATOM    964  C   GLN A 145      35.542  81.907  42.612  1.00  5.11           C  
ANISOU  964  C   GLN A 145      705    549    686    -39     26      5
ATOM    965  O   GLN A 145      36.431  82.657  42.210  1.00  6.17           O  
ANISOU  965  O   GLN A 145      925    639    781    -76    -68     41
ATOM    966  CB  GLN A 145      35.686  80.810  44.927  1.00  6.64           C  
ANISOU  966  CB  GLN A 145      881    794    847     66     40     55
ATOM    967  CG  GLN A 145      37.197  80.923  45.223  1.00 11.80           C  
ANISOU  967  CG  GLN A 145     1578   1277   1626     21     44    -97
ATOM    968  CD  GLN A 145      37.501  81.968  46.296  1.00 12.55           C  
ANISOU  968  CD  GLN A 145     1605   1488   1674    156    196    -93
ATOM    969  OE1 GLN A 145      37.162  81.772  47.461  1.00 18.46           O  
ANISOU  969  OE1 GLN A 145     2053   2321   2640   -249    353    -99
ATOM    970  NE2 GLN A 145      38.146  83.068  45.931  1.00 17.93           N  
ANISOU  970  NE2 GLN A 145     2227   2025   2557    353    184    295
ATOM    971  N   ILE A 146      34.845  81.082  41.812  1.00  5.04           N  
ANISOU  971  N   ILE A 146      694    494    727     24      3    -58
ATOM    972  CA  ILE A 146      35.022  80.990  40.357  1.00  5.46           C  
ANISOU  972  CA  ILE A 146      712    594    768    -16    -53    -17
ATOM    973  C   ILE A 146      34.783  82.344  39.656  1.00  5.23           C  
ANISOU  973  C   ILE A 146      664    542    780    -46    -69    -17
ATOM    974  O   ILE A 146      35.628  82.762  38.861  1.00  5.65           O  
ANISOU  974  O   ILE A 146      701    517    926    -85   -111     -7
ATOM    975  CB  ILE A 146      34.094  79.918  39.708  1.00  5.04           C  
ANISOU  975  CB  ILE A 146      608    551    756    -36      7    -82
ATOM    976  CG1 ILE A 146      34.409  78.499  40.222  1.00  5.43           C  
ANISOU  976  CG1 ILE A 146      623    505    933   -116   -108     69
ATOM    977  CG2 ILE A 146      34.080  79.936  38.161  1.00  5.91           C  
ANISOU  977  CG2 ILE A 146      809    417   1018     96    -45   -104
ATOM    978  CD1 ILE A 146      33.349  77.458  39.823  1.00  6.58           C  
ANISOU  978  CD1 ILE A 146      828    721    950      5   -139    -97
ATOM    979  N   HIS A 147      33.673  83.027  39.999  1.00  5.01           N  
ANISOU  979  N   HIS A 147      571    585    747     17    -62     21
ATOM    980  CA  HIS A 147      33.381  84.359  39.498  1.00  5.47           C  
ANISOU  980  CA  HIS A 147      652    612    814     11    -40    -28
ATOM    981  C   HIS A 147      34.488  85.360  39.817  1.00  5.59           C  
ANISOU  981  C   HIS A 147      654    635    832     21     22    -24
ATOM    982  O   HIS A 147      34.859  86.178  38.966  1.00  6.43           O  
ANISOU  982  O   HIS A 147      686    786    969     -3   -126    -68
ATOM    983  CB  HIS A 147      32.045  84.825  40.090  1.00  5.79           C  
ANISOU  983  CB  HIS A 147      644    754    800    -16     51    -92
ATOM    984  CG  HIS A 147      31.663  86.221  39.732  1.00  5.40           C  
ANISOU  984  CG  HIS A 147      630    563    857    -12     64    -37
ATOM    985  ND1 HIS A 147      31.975  87.305  40.527  1.00  7.87           N  
ANISOU  985  ND1 HIS A 147      738   1048   1201   -181     68   -181
ATOM    986  CD2 HIS A 147      30.988  86.714  38.665  1.00  6.96           C  
ANISOU  986  CD2 HIS A 147      785    535   1322    170    107   -111
ATOM    987  CE1 HIS A 147      31.497  88.401  39.968  1.00  8.08           C  
ANISOU  987  CE1 HIS A 147      615   1012   1440    -91    -13    -29
ATOM    988  NE2 HIS A 147      30.898  88.071  38.837  1.00  8.81           N  
ANISOU  988  NE2 HIS A 147      951   1007   1389    -43     64     78
ATOM    989  N   SER A 148      35.045  85.286  41.029  1.00  5.54           N  
ANISOU  989  N   SER A 148      659    549    897     29    -10    -38
ATOM    990  CA  SER A 148      36.115  86.199  41.412  0.50  6.24           C  
ANISOU  990  CA  SER A 148      793    697    878      2    -25    -58
ATOM    991  C   SER A 148      37.352  85.997  40.532  1.00  6.60           C  
ANISOU  991  C   SER A 148      859    782    866    -20    -20   -102
ATOM    992  O   SER A 148      37.983  86.974  40.117  1.00  7.14           O  
ANISOU  992  O   SER A 148      856    878    977   -118   -183    -67
ATOM    993  CB  SER A 148      36.474  86.032  42.900  0.50  6.22           C  
ANISOU  993  CB  SER A 148      857    617    888     15    -79    -59
ATOM    994  OG  SER A 148      37.333  87.046  43.396  0.50  7.39           O  
ANISOU  994  OG  SER A 148     1126    618   1063   -135     44    -90
ATOM    995  N   VAL A 149      37.716  84.729  40.266  1.00  6.05           N  
ANISOU  995  N   VAL A 149      808    638    849     22     33    -33
ATOM    996  CA  VAL A 149      38.883  84.377  39.454  1.00  6.42           C  
ANISOU  996  CA  VAL A 149      802    835    802     -9      5    -18
ATOM    997  C   VAL A 149      38.706  84.848  37.996  1.00  6.24           C  
ANISOU  997  C   VAL A 149      748    850    774    -58     -5      5
ATOM    998  O   VAL A 149      39.621  85.458  37.440  1.00  7.40           O  
ANISOU  998  O   VAL A 149      991    988    830    -43    -94     52
ATOM    999  CB  VAL A 149      39.183  82.844  39.488  1.00  6.93           C  
ANISOU  999  CB  VAL A 149      878    934    818     49     44     55
ATOM   1000  CG1 VAL A 149      40.266  82.365  38.495  1.00  7.96           C  
ANISOU 1000  CG1 VAL A 149     1102    989    933    -25     55     62
ATOM   1001  CG2 VAL A 149      39.596  82.392  40.901  1.00  8.81           C  
ANISOU 1001  CG2 VAL A 149      931   1264   1151     96     81     13
ATOM   1002  N   ILE A 150      37.518  84.606  37.416  1.00  5.59           N  
ANISOU 1002  N   ILE A 150      620    765    739      0    -32    -26
ATOM   1003  CA  ILE A 150      37.211  85.024  36.045  1.00  6.34           C  
ANISOU 1003  CA  ILE A 150      687    781    937     25    -34     16
ATOM   1004  C   ILE A 150      37.219  86.549  35.913  1.00  6.82           C  
ANISOU 1004  C   ILE A 150      699    902    987     36    -44    -29
ATOM   1005  O   ILE A 150      37.736  87.094  34.935  1.00  7.09           O  
ANISOU 1005  O   ILE A 150      750    993    950     19    -60     -2
ATOM   1006  CB  ILE A 150      35.883  84.385  35.588  1.00  5.72           C  
ANISOU 1006  CB  ILE A 150      654    641    878    137    -21     39
ATOM   1007  CG1 ILE A 150      36.120  82.857  35.438  1.00  7.91           C  
ANISOU 1007  CG1 ILE A 150      962    849   1194    -10    -54    -31
ATOM   1008  CG2 ILE A 150      35.354  85.082  34.319  1.00  6.98           C  
ANISOU 1008  CG2 ILE A 150      696    929   1028    218    -36    -67
ATOM   1009  CD1 ILE A 150      34.914  82.062  35.107  1.00  8.87           C  
ANISOU 1009  CD1 ILE A 150     1208   1008   1152    137     -2   -142
ATOM   1010  N   THR A 151      36.620  87.214  36.895  1.00  7.09           N  
ANISOU 1010  N   THR A 151      639    980   1072    -56    -85    -30
ATOM   1011  CA  THR A 151      36.559  88.670  36.846  0.50  7.89           C  
ANISOU 1011  CA  THR A 151      791   1057   1150    -78    -57    -42
ATOM   1012  C   THR A 151      37.972  89.260  36.959  1.00  8.43           C  
ANISOU 1012  C   THR A 151      870   1140   1192    -96    -89    -55
ATOM   1013  O   THR A 151      38.285  90.234  36.246  1.00  9.28           O  
ANISOU 1013  O   THR A 151      839   1339   1346   -169   -188   -143
ATOM   1014  CB  THR A 151      35.575  89.209  37.905  0.50  8.29           C  
ANISOU 1014  CB  THR A 151      829   1173   1146   -163    -29      4
ATOM   1015  OG1 THR A 151      34.260  88.768  37.562  0.50  9.02           O  
ANISOU 1015  OG1 THR A 151      970   1126   1329   -114    -77    -28
ATOM   1016  CG2 THR A 151      35.594  90.743  37.981  0.50  8.44           C  
ANISOU 1016  CG2 THR A 151      862   1074   1269    -89    -23    -64
ATOM   1017  N   ALA A 152      38.832  88.685  37.797  1.00  8.27           N  
ANISOU 1017  N   ALA A 152      942   1134   1064    -99   -186   -149
ATOM   1018  CA  ALA A 152      40.214  89.167  37.936  1.00  8.53           C  
ANISOU 1018  CA  ALA A 152     1002   1145   1093    -72   -143   -112
ATOM   1019  C   ALA A 152      41.039  88.970  36.666  1.00  8.64           C  
ANISOU 1019  C   ALA A 152      997   1223   1062    -57   -157   -117
ATOM   1020  O   ALA A 152      41.708  89.905  36.196  1.00  9.53           O  
ANISOU 1020  O   ALA A 152     1062   1430   1128      3   -301   -113
ATOM   1021  CB  ALA A 152      40.894  88.475  39.127  1.00  9.55           C  
ANISOU 1021  CB  ALA A 152     1197   1300   1129    -44    -50   -192
ATOM   1022  N   ILE A 153      41.017  87.759  36.119  1.00  8.31           N  
ANISOU 1022  N   ILE A 153      984   1179    991    -35   -129   -162
ATOM   1023  CA  ILE A 153      41.806  87.474  34.928  1.00  8.79           C  
ANISOU 1023  CA  ILE A 153     1082   1245   1011    -34   -134    -86
ATOM   1024  C   ILE A 153      41.221  88.182  33.703  1.00  8.80           C  
ANISOU 1024  C   ILE A 153     1044   1251   1049    -10   -128    -46
ATOM   1025  O   ILE A 153      41.952  88.519  32.761  1.00  9.54           O  
ANISOU 1025  O   ILE A 153     1093   1416   1114    -45   -207    -41
ATOM   1026  CB  ILE A 153      41.920  85.949  34.670  1.00  8.62           C  
ANISOU 1026  CB  ILE A 153     1094   1155   1023    -31   -101    -30
ATOM   1027  CG1 ILE A 153      42.593  85.246  35.858  1.00  8.77           C  
ANISOU 1027  CG1 ILE A 153      934   1385   1011      7   -169    -18
ATOM   1028  CG2 ILE A 153      42.643  85.628  33.348  1.00  9.59           C  
ANISOU 1028  CG2 ILE A 153     1241   1307   1093    -20   -185     40
ATOM   1029  CD1 ILE A 153      42.632  83.711  35.764  1.00  9.70           C  
ANISOU 1029  CD1 ILE A 153     1069   1377   1240   -167   -144    -39
ATOM   1030  N   GLY A 154      39.914  88.424  33.725  1.00  8.70           N  
ANISOU 1030  N   GLY A 154     1006   1281   1016     46   -145    -81
ATOM   1031  CA  GLY A 154      39.220  89.082  32.630  1.00  9.41           C  
ANISOU 1031  CA  GLY A 154     1085   1308   1183     13    -80    -89
ATOM   1032  C   GLY A 154      39.167  90.579  32.743  1.00  9.25           C  
ANISOU 1032  C   GLY A 154     1053   1276   1186     61    -98   -101
ATOM   1033  O   GLY A 154      38.427  91.207  31.990  1.00 10.40           O  
ANISOU 1033  O   GLY A 154      917   1652   1383     52    -56   -140
ATOM   1034  N   ILE A 155      39.963  91.156  33.645  1.00 10.63           N  
ANISOU 1034  N   ILE A 155     1076   1539   1423    -73    -82   -136
ATOM   1035  CA  ILE A 155      39.901  92.589  33.941  1.00 11.44           C  
ANISOU 1035  CA  ILE A 155     1152   1579   1613    -49    -80    -85
ATOM   1036  C   ILE A 155      40.240  93.492  32.740  1.00 11.87           C  
ANISOU 1036  C   ILE A 155     1157   1669   1683    -90   -115    -90
ATOM   1037  O   ILE A 155      39.805  94.639  32.719  1.00 13.37           O  
ANISOU 1037  O   ILE A 155     1236   1892   1949   -231    -12   -105
ATOM   1038  CB  ILE A 155      40.781  92.904  35.177  1.00 12.12           C  
ANISOU 1038  CB  ILE A 155     1186   1669   1750    -43    -49    -83
ATOM   1039  CG1 ILE A 155      40.389  94.255  35.792  1.00 15.09           C  
ANISOU 1039  CG1 ILE A 155     1725   1888   2120   -144     14    -62
ATOM   1040  CG2 ILE A 155      42.266  92.831  34.825  1.00 12.71           C  
ANISOU 1040  CG2 ILE A 155     1234   1865   1729    -23   -105   -140
ATOM   1041  CD1 ILE A 155      39.036  94.267  36.433  1.00 17.79           C  
ANISOU 1041  CD1 ILE A 155     2206   2177   2373     11    -25    -11
ATOM   1042  N   LYS A 156      40.975  92.983  31.753  1.00 11.78           N  
ANISOU 1042  N   LYS A 156     1102   1713   1658    -39   -199   -107
ATOM   1043  CA  LYS A 156      41.299  93.776  30.551  1.00 12.73           C  
ANISOU 1043  CA  LYS A 156     1285   1839   1712      3   -173    -47
ATOM   1044  C   LYS A 156      40.295  93.572  29.408  1.00 13.34           C  
ANISOU 1044  C   LYS A 156     1354   1937   1774     87   -220    -70
ATOM   1045  O   LYS A 156      40.436  94.174  28.323  1.00 15.49           O  
ANISOU 1045  O   LYS A 156     1557   2343   1984    237   -237    -71
ATOM   1046  CB  LYS A 156      42.723  93.453  30.080  1.00 13.90           C  
ANISOU 1046  CB  LYS A 156     1445   2023   1813    -31   -200    -14
ATOM   1047  CG  LYS A 156      43.783  93.606  31.161  1.00 15.69           C  
ANISOU 1047  CG  LYS A 156     1765   2196   1998    -35    -92    -22
ATOM   1048  CD  LYS A 156      43.827  95.036  31.731  1.00 17.51           C  
ANISOU 1048  CD  LYS A 156     2192   2342   2118   -114     -8    -51
ATOM   1049  CE  LYS A 156      44.874  95.153  32.813  1.00 17.90           C  
ANISOU 1049  CE  LYS A 156     2177   2310   2314    -61    -39    -77
ATOM   1050  NZ  LYS A 156      45.153  96.568  33.187  1.00 20.06           N1+
ANISOU 1050  NZ  LYS A 156     2558   2504   2559   -186   -117   -131
ATOM   1051  N   MET A 157      39.263  92.769  29.652  1.00 12.28           N  
ANISOU 1051  N   MET A 157     1222   1838   1606     57   -199    -58
ATOM   1052  CA  MET A 157      38.264  92.453  28.640  1.00 12.05           C  
ANISOU 1052  CA  MET A 157     1171   1765   1640     87   -198    -27
ATOM   1053  C   MET A 157      37.055  93.328  28.893  1.00 11.64           C  
ANISOU 1053  C   MET A 157     1116   1683   1623     73   -155    -33
ATOM   1054  O   MET A 157      36.201  93.039  29.722  1.00 11.40           O  
ANISOU 1054  O   MET A 157     1062   1615   1654    246    -69    -27
ATOM   1055  CB  MET A 157      37.933  90.956  28.690  1.00 11.30           C  
ANISOU 1055  CB  MET A 157     1063   1712   1516    133   -240    -67
ATOM   1056  CG  MET A 157      39.141  90.115  28.284  1.00 11.69           C  
ANISOU 1056  CG  MET A 157     1179   1698   1562     69   -299    -63
ATOM   1057  SD  MET A 157      39.025  88.312  28.503  1.00 14.04           S  
ANISOU 1057  SD  MET A 157     1260   2306   1766    -17   -401   -140
ATOM   1058  CE  MET A 157      37.656  87.894  27.421  1.00 13.75           C  
ANISOU 1058  CE  MET A 157     1547   2155   1523    168   -118    -64
ATOM   1059  N   GLU A 158      37.014  94.445  28.177  1.00 12.11           N  
ANISOU 1059  N   GLU A 158     1195   1752   1653     83   -228    -57
ATOM   1060  CA  GLU A 158      35.970  95.417  28.334  1.00 12.35           C  
ANISOU 1060  CA  GLU A 158     1266   1702   1725     55   -174    -49
ATOM   1061  C   GLU A 158      34.596  94.825  28.008  1.00 11.40           C  
ANISOU 1061  C   GLU A 158     1042   1609   1678     66   -137    -66
ATOM   1062  O   GLU A 158      34.419  94.202  26.969  1.00 13.01           O  
ANISOU 1062  O   GLU A 158     1273   1680   1990    103   -206    -16
ATOM   1063  CB  GLU A 158      36.270  96.630  27.435  1.00 13.85           C  
ANISOU 1063  CB  GLU A 158     1436   1986   1841     85   -164     14
ATOM   1064  CG  GLU A 158      35.974  96.493  25.927  1.00 19.00           C  
ANISOU 1064  CG  GLU A 158     2364   2410   2445     93    -75    -27
ATOM   1065  CD  GLU A 158      36.985  95.683  25.093  1.00 22.71           C  
ANISOU 1065  CD  GLU A 158     2825   2852   2952     85     78    118
ATOM   1066  OE1 GLU A 158      37.915  95.004  25.637  1.00 21.78           O  
ANISOU 1066  OE1 GLU A 158     2247   3026   2999    253   -191    115
ATOM   1067  OE2 GLU A 158      36.836  95.753  23.833  1.00 26.78           O1-
ANISOU 1067  OE2 GLU A 158     3235   3307   3632    245     54     12
ATOM   1068  N   GLY A 159      33.638  94.993  28.904  1.00 10.23           N  
ANISOU 1068  N   GLY A 159      891   1380   1614     73   -146   -142
ATOM   1069  CA  GLY A 159      32.285  94.498  28.689  1.00  9.46           C  
ANISOU 1069  CA  GLY A 159      842   1237   1514     91   -123    -89
ATOM   1070  C   GLY A 159      32.079  93.025  29.012  1.00  8.38           C  
ANISOU 1070  C   GLY A 159      716   1083   1383    107    -43    -80
ATOM   1071  O   GLY A 159      31.011  92.489  28.741  1.00  8.56           O  
ANISOU 1071  O   GLY A 159      777    988   1487    217    -54   -116
ATOM   1072  N   LEU A 160      33.079  92.362  29.586  1.00  7.78           N  
ANISOU 1072  N   LEU A 160      703   1009   1243    143   -124   -123
ATOM   1073  CA  LEU A 160      32.901  90.986  30.024  1.00  7.21           C  
ANISOU 1073  CA  LEU A 160      671    885   1180     62    -95    -80
ATOM   1074  C   LEU A 160      31.762  90.898  31.029  1.00  7.11           C  
ANISOU 1074  C   LEU A 160      744    794   1161    152    -37   -119
ATOM   1075  O   LEU A 160      31.725  91.645  32.014  1.00  7.61           O  
ANISOU 1075  O   LEU A 160      801    807   1282      1    -47    -73
ATOM   1076  CB  LEU A 160      34.189  90.460  30.659  1.00  7.11           C  
ANISOU 1076  CB  LEU A 160      701    906   1092     95   -104    -68
ATOM   1077  CG  LEU A 160      34.139  89.087  31.348  1.00  6.77           C  
ANISOU 1077  CG  LEU A 160      630    814   1127     35   -104    -30
ATOM   1078  CD1 LEU A 160      33.880  87.996  30.312  1.00  7.95           C  
ANISOU 1078  CD1 LEU A 160      753    997   1270   -208    -63   -133
ATOM   1079  CD2 LEU A 160      35.413  88.828  32.112  1.00  8.05           C  
ANISOU 1079  CD2 LEU A 160      779   1049   1230     14    -57    -60
ATOM   1080  N   GLU A 161      30.856  89.947  30.803  1.00  5.97           N  
ANISOU 1080  N   GLU A 161      528    593   1145     68    -19   -126
ATOM   1081  CA  GLU A 161      29.724  89.715  31.686  1.00  6.11           C  
ANISOU 1081  CA  GLU A 161      560    654   1106     76     -1    -56
ATOM   1082  C   GLU A 161      29.764  88.277  32.213  1.00  5.19           C  
ANISOU 1082  C   GLU A 161      467    445   1058     14     20    -80
ATOM   1083  O   GLU A 161      29.486  87.323  31.478  1.00  6.97           O  
ANISOU 1083  O   GLU A 161      529    563   1557     30     -8   -146
ATOM   1084  CB  GLU A 161      28.414  89.944  30.943  1.00  6.53           C  
ANISOU 1084  CB  GLU A 161      619    710   1150     50     22    -47
ATOM   1085  CG  GLU A 161      28.188  91.395  30.497  1.00  7.37           C  
ANISOU 1085  CG  GLU A 161      638    931   1229    -23     12    -41
ATOM   1086  CD  GLU A 161      27.809  92.349  31.607  1.00  8.34           C  
ANISOU 1086  CD  GLU A 161      521   1099   1547   -138    -16    139
ATOM   1087  OE1 GLU A 161      27.697  91.939  32.775  1.00 10.39           O  
ANISOU 1087  OE1 GLU A 161      740   1083   2122    -26   -179    178
ATOM   1088  OE2 GLU A 161      27.602  93.548  31.299  1.00 11.78           O1-
ANISOU 1088  OE2 GLU A 161      652   1281   2540   -162     14    320
ATOM   1089  N   CYS A 162      30.151  88.131  33.469  1.00  5.24           N  
ANISOU 1089  N   CYS A 162      455    480   1056     55     10    -25
ATOM   1090  CA  CYS A 162      30.168  86.834  34.157  1.00  5.10           C  
ANISOU 1090  CA  CYS A 162      491    479    966     63    -59     -4
ATOM   1091  C   CYS A 162      29.295  86.974  35.396  1.00  5.39           C  
ANISOU 1091  C   CYS A 162      566    511    969     19    -36     69
ATOM   1092  O   CYS A 162      29.460  87.929  36.159  1.00  5.65           O  
ANISOU 1092  O   CYS A 162      565    451   1128    -73   -104     45
ATOM   1093  CB  CYS A 162      31.594  86.458  34.523  1.00  5.88           C  
ANISOU 1093  CB  CYS A 162      578    596   1057     -5    -19     10
ATOM   1094  SG  CYS A 162      31.716  84.924  35.469  1.00  6.29           S  
ANISOU 1094  SG  CYS A 162      578    741   1071     28     27    -16
ATOM   1095  N   HIS A 163      28.356  86.053  35.591  1.00  4.95           N  
ANISOU 1095  N   HIS A 163      484    434    961     56    -54     13
ATOM   1096  CA  HIS A 163      27.353  86.148  36.646  1.00  4.89           C  
ANISOU 1096  CA  HIS A 163      450    461    947     39    -10     32
ATOM   1097  C   HIS A 163      27.124  84.827  37.324  1.00  4.51           C  
ANISOU 1097  C   HIS A 163      410    427    876      2      4     73
ATOM   1098  O   HIS A 163      27.335  83.768  36.729  1.00  4.38           O  
ANISOU 1098  O   HIS A 163      404    393    865    -11      7     87
ATOM   1099  CB  HIS A 163      26.060  86.750  36.085  1.00  6.22           C  
ANISOU 1099  CB  HIS A 163      611    686   1066     69    -38     82
ATOM   1100  CG  HIS A 163      26.292  88.129  35.564  1.00  6.94           C  
ANISOU 1100  CG  HIS A 163      568    731   1338     52    -54    174
ATOM   1101  ND1 HIS A 163      26.421  89.203  36.418  1.00  7.97           N  
ANISOU 1101  ND1 HIS A 163      312    849   1865   -113   -106    110
ATOM   1102  CD2 HIS A 163      26.592  88.593  34.328  1.00  7.64           C  
ANISOU 1102  CD2 HIS A 163      667    719   1516     34    -37    165
ATOM   1103  CE1 HIS A 163      26.717  90.289  35.721  1.00 10.06           C  
ANISOU 1103  CE1 HIS A 163      573   1203   2043   -193   -125     60
ATOM   1104  NE2 HIS A 163      26.841  89.941  34.451  1.00  9.33           N  
ANISOU 1104  NE2 HIS A 163      829    906   1809    -30   -136     55
ATOM   1105  N   VAL A 164      26.742  84.924  38.607  1.00  4.29           N  
ANISOU 1105  N   VAL A 164      399    376    853    130    -22     41
ATOM   1106  CA  VAL A 164      26.543  83.807  39.520  1.00  4.65           C  
ANISOU 1106  CA  VAL A 164      505    495    767     19     -1     43
ATOM   1107  C   VAL A 164      25.031  83.539  39.663  1.00  4.24           C  
ANISOU 1107  C   VAL A 164      467    443    700    -27     18     42
ATOM   1108  O   VAL A 164      24.283  84.461  39.991  1.00  4.71           O  
ANISOU 1108  O   VAL A 164      485    481    824    -63    135     38
ATOM   1109  CB  VAL A 164      27.141  84.103  40.928  1.00  4.39           C  
ANISOU 1109  CB  VAL A 164      511    433    721     20     62     26
ATOM   1110  CG1 VAL A 164      26.882  82.989  41.964  1.00  5.66           C  
ANISOU 1110  CG1 VAL A 164      517    727    904    247    -51    -29
ATOM   1111  CG2 VAL A 164      28.656  84.351  40.845  1.00  6.09           C  
ANISOU 1111  CG2 VAL A 164      833    855    623    132    -77    108
ATOM   1112  N   PHE A 165      24.624  82.291  39.419  1.00  3.92           N  
ANISOU 1112  N   PHE A 165      450    282    754    -39     58     25
ATOM   1113  CA  PHE A 165      23.238  81.852  39.358  1.00  4.30           C  
ANISOU 1113  CA  PHE A 165      475    436    723    -40     19     56
ATOM   1114  C   PHE A 165      23.044  80.711  40.358  1.00  4.59           C  
ANISOU 1114  C   PHE A 165      540    443    759     11     71    102
ATOM   1115  O   PHE A 165      23.225  79.541  40.020  1.00  5.04           O  
ANISOU 1115  O   PHE A 165      472    544    899     65     28     68
ATOM   1116  CB  PHE A 165      22.915  81.413  37.920  1.00  5.05           C  
ANISOU 1116  CB  PHE A 165      652    522    745    -35     38    -12
ATOM   1117  CG  PHE A 165      22.994  82.536  36.905  1.00  4.53           C  
ANISOU 1117  CG  PHE A 165      503    401    817    -16     71     82
ATOM   1118  CD1 PHE A 165      21.997  83.531  36.876  1.00  4.79           C  
ANISOU 1118  CD1 PHE A 165      717    499    603     32    149    104
ATOM   1119  CD2 PHE A 165      24.150  82.701  36.115  1.00  5.17           C  
ANISOU 1119  CD2 PHE A 165      528    559    875    162    151     80
ATOM   1120  CE1 PHE A 165      22.134  84.632  36.045  1.00  6.21           C  
ANISOU 1120  CE1 PHE A 165      674    929    754    117    268     67
ATOM   1121  CE2 PHE A 165      24.259  83.799  35.276  1.00  5.21           C  
ANISOU 1121  CE2 PHE A 165      658    559    761    177    135     47
ATOM   1122  CZ  PHE A 165      23.257  84.761  35.239  1.00  5.62           C  
ANISOU 1122  CZ  PHE A 165      665    698    771    131     64     -8
ATOM   1123  N   ILE A 166      22.716  81.087  41.588  1.00  4.74           N  
ANISOU 1123  N   ILE A 166      480    397    924     -9    -28    102
ATOM   1124  CA  ILE A 166      22.571  80.187  42.720  1.00  5.29           C  
ANISOU 1124  CA  ILE A 166      616    570    822     43    -17     39
ATOM   1125  C   ILE A 166      21.188  80.408  43.355  1.00  5.65           C  
ANISOU 1125  C   ILE A 166      644    656    846     68    -55     11
ATOM   1126  O   ILE A 166      20.614  81.495  43.216  1.00  6.26           O  
ANISOU 1126  O   ILE A 166      654    754    970    118     29    177
ATOM   1127  CB  ILE A 166      23.681  80.492  43.763  1.00  5.67           C  
ANISOU 1127  CB  ILE A 166      740    580    835     15    -41    -10
ATOM   1128  CG1 ILE A 166      23.712  81.962  44.268  1.00  6.29           C  
ANISOU 1128  CG1 ILE A 166     1068    453    865    150    -88     17
ATOM   1129  CG2 ILE A 166      25.054  80.032  43.228  1.00  8.00           C  
ANISOU 1129  CG2 ILE A 166      966   1120    953    170      4    203
ATOM   1130  CD1 ILE A 166      24.736  82.225  45.381  1.00  8.54           C  
ANISOU 1130  CD1 ILE A 166     1369    866   1007    164    -16   -169
ATOM   1131  N   GLY A 167      20.665  79.377  44.023  1.00  5.88           N  
ANISOU 1131  N   GLY A 167      683    616    934    119    -89     15
ATOM   1132  CA  GLY A 167      19.373  79.394  44.694  1.00  7.01           C  
ANISOU 1132  CA  GLY A 167      969    755    937     79   -100      1
ATOM   1133  C   GLY A 167      19.409  80.326  45.906  1.00  7.02           C  
ANISOU 1133  C   GLY A 167     1052    681    933    141   -145     -8
ATOM   1134  O   GLY A 167      19.656  79.882  47.027  1.00  6.99           O  
ANISOU 1134  O   GLY A 167      917    715   1024     65   -201   -104
ATOM   1135  N   GLY A 168      19.158  81.621  45.688  1.00  8.13           N  
ANISOU 1135  N   GLY A 168     1308    663   1118     52    -38     12
ATOM   1136  CA  GLY A 168      19.141  82.592  46.774  1.00  8.54           C  
ANISOU 1136  CA  GLY A 168     1415    771   1056    -14     13     27
ATOM   1137  C   GLY A 168      18.736  83.985  46.291  1.00  9.69           C  
ANISOU 1137  C   GLY A 168     1545    972   1162    -24    -13    -11
ATOM   1138  O   GLY A 168      19.118  84.956  46.934  1.00 10.28           O  
ANISOU 1138  O   GLY A 168     1749    970   1186    -18     47    114
ATOM   1139  N   THR A 169      17.995  84.131  45.187  1.00  9.09           N  
ANISOU 1139  N   THR A 169     1439    903   1111    -19     52     16
ATOM   1140  CA  THR A 169      17.622  85.420  44.583  1.00  9.34           C  
ANISOU 1140  CA  THR A 169     1461    970   1116    -20     20    -59
ATOM   1141  C   THR A 169      16.368  85.166  43.699  1.00  9.06           C  
ANISOU 1141  C   THR A 169     1333    999   1109    -29     31    -22
ATOM   1142  O   THR A 169      16.173  84.000  43.334  1.00  8.49           O  
ANISOU 1142  O   THR A 169     1137    957   1130    -76    124   -125
ATOM   1143  CB  THR A 169      18.845  85.957  43.762  1.00  9.45           C  
ANISOU 1143  CB  THR A 169     1574    995   1020    -51    129   -121
ATOM   1144  OG1 THR A 169      18.726  87.312  43.371  1.00 11.66           O  
ANISOU 1144  OG1 THR A 169     2402    852   1176    -29    103   -307
ATOM   1145  CG2 THR A 169      19.182  85.151  42.497  1.00 10.43           C  
ANISOU 1145  CG2 THR A 169     1571   1138   1252      3     -9    -42
ATOM   1146  N   PRO A 170      15.505  86.176  43.396  1.00  9.62           N  
ANISOU 1146  N   PRO A 170     1355   1100   1200   -117     32    -10
ATOM   1147  CA  PRO A 170      14.329  85.921  42.574  1.00  9.36           C  
ANISOU 1147  CA  PRO A 170     1277   1151   1127    -23     69     23
ATOM   1148  C   PRO A 170      14.675  85.516  41.153  1.00  8.51           C  
ANISOU 1148  C   PRO A 170     1136   1071   1024     17     18    -32
ATOM   1149  O   PRO A 170      15.566  86.102  40.520  1.00  8.20           O  
ANISOU 1149  O   PRO A 170     1187   1059    869     49     32     51
ATOM   1150  CB  PRO A 170      13.583  87.266  42.577  1.00 10.69           C  
ANISOU 1150  CB  PRO A 170     1454   1345   1258    -27    131     89
ATOM   1151  CG  PRO A 170      14.485  88.227  43.118  1.00 12.61           C  
ANISOU 1151  CG  PRO A 170     1581   1601   1607   -112    102     44
ATOM   1152  CD  PRO A 170      15.482  87.532  43.973  1.00 10.47           C  
ANISOU 1152  CD  PRO A 170     1386   1215   1375   -126     36     22
ATOM   1153  N   LEU A 171      13.950  84.521  40.624  1.00  8.07           N  
ANISOU 1153  N   LEU A 171     1075   1100    888     53      8    -48
ATOM   1154  CA  LEU A 171      14.098  84.052  39.240  1.00  8.43           C  
ANISOU 1154  CA  LEU A 171     1057   1133   1012     22     -4    -28
ATOM   1155  C   LEU A 171      13.902  85.168  38.198  1.00  8.63           C  
ANISOU 1155  C   LEU A 171     1083   1170   1023    -13     -4    -21
ATOM   1156  O   LEU A 171      14.491  85.079  37.120  1.00  8.02           O  
ANISOU 1156  O   LEU A 171      994   1055    997    172    -41    -74
ATOM   1157  CB  LEU A 171      13.125  82.880  38.970  1.00  8.96           C  
ANISOU 1157  CB  LEU A 171     1094   1214   1095     22     -2    -93
ATOM   1158  CG  LEU A 171      13.599  81.524  39.537  1.00  9.63           C  
ANISOU 1158  CG  LEU A 171     1139   1161   1357    121   -123   -181
ATOM   1159  CD1 LEU A 171      12.469  80.475  39.502  1.00 11.82           C  
ANISOU 1159  CD1 LEU A 171     1423   1696   1369    -31   -187   -266
ATOM   1160  CD2 LEU A 171      14.859  81.018  38.807  1.00 11.78           C  
ANISOU 1160  CD2 LEU A 171     1380   1497   1598     62   -139   -110
ATOM   1161  N   SER A 172      13.129  86.216  38.536  1.00  9.07           N  
ANISOU 1161  N   SER A 172     1135   1277   1033      4    -42     29
ATOM   1162  CA  SER A 172      12.950  87.335  37.619  1.00  9.48           C  
ANISOU 1162  CA  SER A 172     1129   1379   1093    -88     58     88
ATOM   1163  C   SER A 172      14.231  88.167  37.459  1.00  9.54           C  
ANISOU 1163  C   SER A 172     1097   1370   1158   -106     66     63
ATOM   1164  O   SER A 172      14.482  88.744  36.398  1.00  8.96           O  
ANISOU 1164  O   SER A 172      954   1245   1204   -135     -6     26
ATOM   1165  CB  SER A 172      11.788  88.213  38.105  1.00 10.53           C  
ANISOU 1165  CB  SER A 172     1216   1584   1201    -61    151    125
ATOM   1166  OG  SER A 172      12.093  88.813  39.341  1.00 13.10           O  
ANISOU 1166  OG  SER A 172     1685   1829   1461   -208    157     80
ATOM   1167  N   GLN A 173      15.036  88.232  38.507  1.00  8.31           N  
ANISOU 1167  N   GLN A 173     1047   1100   1007   -178      8    128
ATOM   1168  CA  GLN A 173      16.292  88.950  38.442  1.00  9.26           C  
ANISOU 1168  CA  GLN A 173     1128   1250   1137   -119     10     96
ATOM   1169  C   GLN A 173      17.348  88.162  37.698  1.00  8.23           C  
ANISOU 1169  C   GLN A 173     1004   1078   1043   -108    -46     50
ATOM   1170  O   GLN A 173      18.085  88.720  36.905  1.00  8.00           O  
ANISOU 1170  O   GLN A 173      878    976   1183   -105    -89    155
ATOM   1171  CB  GLN A 173      16.735  89.346  39.835  1.00  9.71           C  
ANISOU 1171  CB  GLN A 173     1306   1264   1117   -196     -2     79
ATOM   1172  CG  GLN A 173      15.808  90.426  40.391  1.00 12.83           C  
ANISOU 1172  CG  GLN A 173     1665   1556   1653    -76     98    193
ATOM   1173  CD  GLN A 173      16.301  91.069  41.652  1.00 13.51           C  
ANISOU 1173  CD  GLN A 173     1811   1602   1720    -82      2    137
ATOM   1174  OE1 GLN A 173      17.427  90.864  42.102  1.00 17.13           O  
ANISOU 1174  OE1 GLN A 173     2454   1799   2252     52    358    111
ATOM   1175  NE2 GLN A 173      15.431  91.878  42.244  1.00 20.04           N  
ANISOU 1175  NE2 GLN A 173     2814   2242   2555   -247    200    458
ATOM   1176  N   ASP A 174      17.384  86.848  37.903  1.00  7.75           N  
ANISOU 1176  N   ASP A 174      878    973   1091    -79    -56     46
ATOM   1177  CA  ASP A 174      18.259  85.996  37.093  1.00  7.32           C  
ANISOU 1177  CA  ASP A 174      843    880   1056     -8     21     21
ATOM   1178  C   ASP A 174      17.891  86.171  35.618  1.00  7.10           C  
ANISOU 1178  C   ASP A 174      798    830   1068      1     20     39
ATOM   1179  O   ASP A 174      18.772  86.239  34.771  1.00  8.02           O  
ANISOU 1179  O   ASP A 174      916    881   1249    120    102    192
ATOM   1180  CB  ASP A 174      18.101  84.508  37.455  1.00  7.36           C  
ANISOU 1180  CB  ASP A 174      841    854   1100    -60     57     17
ATOM   1181  CG  ASP A 174      18.801  84.092  38.745  1.00  8.51           C  
ANISOU 1181  CG  ASP A 174      998   1019   1215     -9    -12    -29
ATOM   1182  OD1 ASP A 174      19.525  84.866  39.387  1.00  9.16           O  
ANISOU 1182  OD1 ASP A 174     1235    845   1398     56    195    -86
ATOM   1183  OD2 ASP A 174      18.597  82.924  39.101  1.00 10.71           O1-
ANISOU 1183  OD2 ASP A 174      997   1261   1808     33      9    -92
ATOM   1184  N   LYS A 175      16.591  86.185  35.304  1.00  8.00           N  
ANISOU 1184  N   LYS A 175      858    989   1190     66     11     28
ATOM   1185  CA  LYS A 175      16.148  86.339  33.896  1.00  8.44           C  
ANISOU 1185  CA  LYS A 175      884   1060   1261     42     39     12
ATOM   1186  C   LYS A 175      16.780  87.585  33.267  1.00  8.17           C  
ANISOU 1186  C   LYS A 175      847   1061   1195     46     49     24
ATOM   1187  O   LYS A 175      17.332  87.532  32.168  1.00  8.09           O  
ANISOU 1187  O   LYS A 175      628   1071   1375    161    148    112
ATOM   1188  CB  LYS A 175      14.623  86.436  33.809  1.00  9.27           C  
ANISOU 1188  CB  LYS A 175      938   1259   1326     46    -11    -58
ATOM   1189  CG  LYS A 175      14.064  86.480  32.380  1.00 10.26           C  
ANISOU 1189  CG  LYS A 175     1074   1340   1482     60     66    -59
ATOM   1190  CD  LYS A 175      12.551  86.698  32.325  1.00 11.24           C  
ANISOU 1190  CD  LYS A 175     1409   1391   1469    117     22    -74
ATOM   1191  CE  LYS A 175      11.983  86.591  30.911  1.00 13.49           C  
ANISOU 1191  CE  LYS A 175     1793   1673   1659     99    135   -160
ATOM   1192  NZ  LYS A 175      10.523  86.923  30.834  1.00 16.60           N1+
ANISOU 1192  NZ  LYS A 175     1982   2334   1988     55    229   -123
ATOM   1193  N   THR A 176      16.684  88.710  33.967  1.00  8.29           N  
ANISOU 1193  N   THR A 176      850   1150   1148     -9     63    163
ATOM   1194  CA  THR A 176      17.241  89.971  33.480  1.00  8.23           C  
ANISOU 1194  CA  THR A 176      777   1104   1245     19     79    154
ATOM   1195  C   THR A 176      18.754  89.883  33.306  1.00  7.81           C  
ANISOU 1195  C   THR A 176      720   1027   1220     54     66    119
ATOM   1196  O   THR A 176      19.294  90.279  32.266  1.00  8.65           O  
ANISOU 1196  O   THR A 176      721   1232   1333    125    159    278
ATOM   1197  CB  THR A 176      16.872  91.126  34.423  1.00  9.25           C  
ANISOU 1197  CB  THR A 176      916   1298   1300    -96    115    194
ATOM   1198  OG1 THR A 176      15.440  91.207  34.499  1.00 11.27           O  
ANISOU 1198  OG1 THR A 176     1100   1738   1442    -74    176    246
ATOM   1199  CG2 THR A 176      17.451  92.443  33.916  1.00 11.53           C  
ANISOU 1199  CG2 THR A 176     1182   1769   1428   -168    -53    292
ATOM   1200  N   ARG A 177      19.440  89.313  34.283  1.00  7.27           N  
ANISOU 1200  N   ARG A 177      674    943   1143     47     99    151
ATOM   1201  CA  ARG A 177      20.893  89.220  34.231  1.00  7.70           C  
ANISOU 1201  CA  ARG A 177      826    956   1142     30     14    114
ATOM   1202  C   ARG A 177      21.352  88.336  33.063  1.00  7.23           C  
ANISOU 1202  C   ARG A 177      763    896   1089     40     39    147
ATOM   1203  O   ARG A 177      22.374  88.627  32.442  1.00  8.33           O  
ANISOU 1203  O   ARG A 177      970   1044   1150    -34    -85    226
ATOM   1204  CB  ARG A 177      21.442  88.676  35.562  1.00  8.00           C  
ANISOU 1204  CB  ARG A 177      893   1004   1142     63     10     82
ATOM   1205  CG  ARG A 177      21.215  89.604  36.759  1.00  9.91           C  
ANISOU 1205  CG  ARG A 177     1112   1227   1424    112     68    -11
ATOM   1206  CD  ARG A 177      21.425  88.924  38.120  1.00 10.37           C  
ANISOU 1206  CD  ARG A 177     1246   1215   1479     69    -67     32
ATOM   1207  NE  ARG A 177      20.880  89.751  39.202  1.00 10.04           N  
ANISOU 1207  NE  ARG A 177     1371    952   1490    112    132     61
ATOM   1208  CZ  ARG A 177      20.977  89.467  40.499  1.00 11.76           C  
ANISOU 1208  CZ  ARG A 177     1502   1282   1682    123      8    109
ATOM   1209  NH1 ARG A 177      21.615  88.389  40.918  1.00 11.50           N  
ANISOU 1209  NH1 ARG A 177     1582   1339   1447     53     12    160
ATOM   1210  NH2 ARG A 177      20.430  90.289  41.390  1.00 13.54           N1+
ANISOU 1210  NH2 ARG A 177     1709   1470   1964   -124    160    -16
ATOM   1211  N   LEU A 178      20.578  87.304  32.738  1.00  6.95           N  
ANISOU 1211  N   LEU A 178      744    814   1081     86    102    173
ATOM   1212  CA  LEU A 178      20.927  86.393  31.653  1.00  7.71           C  
ANISOU 1212  CA  LEU A 178      794    885   1248    116    126    128
ATOM   1213  C   LEU A 178      20.811  87.025  30.270  1.00  9.15           C  
ANISOU 1213  C   LEU A 178      944   1023   1507    161    159    167
ATOM   1214  O   LEU A 178      21.297  86.446  29.305  1.00 10.16           O  
ANISOU 1214  O   LEU A 178      995    973   1890     78    281    258
ATOM   1215  CB  LEU A 178      20.107  85.104  31.770  1.00  7.26           C  
ANISOU 1215  CB  LEU A 178      861    756   1142    109    193     76
ATOM   1216  CG  LEU A 178      20.612  84.162  32.869  1.00  6.50           C  
ANISOU 1216  CG  LEU A 178      636    806   1027     22    165   -191
ATOM   1217  CD1 LEU A 178      19.512  83.194  33.315  1.00  7.57           C  
ANISOU 1217  CD1 LEU A 178      905    922   1047   -171     39     15
ATOM   1218  CD2 LEU A 178      21.860  83.399  32.413  1.00  7.79           C  
ANISOU 1218  CD2 LEU A 178      838   1067   1055     67     92     10
ATOM   1219  N   LYS A 179      20.196  88.211  30.172  1.00  9.72           N  
ANISOU 1219  N   LYS A 179     1020   1115   1555    186    188    237
ATOM   1220  CA  LYS A 179      20.161  88.951  28.897  1.00 10.84           C  
ANISOU 1220  CA  LYS A 179     1087   1362   1667    144    184    175
ATOM   1221  C   LYS A 179      21.506  89.563  28.531  1.00 10.86           C  
ANISOU 1221  C   LYS A 179     1119   1336   1670    219    137    239
ATOM   1222  O   LYS A 179      21.694  90.013  27.396  1.00 13.14           O  
ANISOU 1222  O   LYS A 179     1416   1525   2049    539    155    394
ATOM   1223  CB  LYS A 179      19.101  90.051  28.961  1.00 11.24           C  
ANISOU 1223  CB  LYS A 179     1037   1433   1800    182    254    187
ATOM   1224  CG  LYS A 179      17.697  89.535  29.145  1.00 12.80           C  
ANISOU 1224  CG  LYS A 179     1217   1682   1963     90    209    128
ATOM   1225  CD  LYS A 179      16.688  90.689  29.202  1.00 14.28           C  
ANISOU 1225  CD  LYS A 179     1461   2003   1960     76    254    140
ATOM   1226  CE  LYS A 179      15.275  90.153  29.281  1.00 17.72           C  
ANISOU 1226  CE  LYS A 179     2094   2471   2167      8    185     66
ATOM   1227  NZ  LYS A 179      14.234  91.219  29.136  1.00 20.40           N1+
ANISOU 1227  NZ  LYS A 179     2351   2841   2559    -14    345     99
ATOM   1228  N   LYS A 180      22.433  89.651  29.480  1.00 10.40           N  
ANISOU 1228  N   LYS A 180     1052   1324   1573    159    133    210
ATOM   1229  CA  LYS A 180      23.771  90.178  29.243  1.00 11.06           C  
ANISOU 1229  CA  LYS A 180     1181   1418   1599     92     77    189
ATOM   1230  C   LYS A 180      24.743  89.315  30.024  1.00  8.94           C  
ANISOU 1230  C   LYS A 180      871   1183   1340     93     19    216
ATOM   1231  O   LYS A 180      25.181  89.673  31.105  1.00  9.41           O  
ANISOU 1231  O   LYS A 180      785   1278   1512   -163    -49    242
ATOM   1232  CB  LYS A 180      23.933  91.639  29.726  1.00 12.68           C  
ANISOU 1232  CB  LYS A 180     1391   1705   1719     71    -23    179
ATOM   1233  CG  LYS A 180      23.026  92.677  29.125  1.00 14.53           C  
ANISOU 1233  CG  LYS A 180     1682   1900   1937      9     25    105
ATOM   1234  CD  LYS A 180      23.250  94.064  29.773  1.00 15.63           C  
ANISOU 1234  CD  LYS A 180     1750   2066   2122    -92      3     51
ATOM   1235  CE  LYS A 180      22.198  95.055  29.317  1.00 18.43           C  
ANISOU 1235  CE  LYS A 180     2243   2371   2386    -73    156     94
ATOM   1236  NZ  LYS A 180      22.479  95.594  27.957  1.00 23.12           N1+
ANISOU 1236  NZ  LYS A 180     2720   3073   2992    151      8    103
ATOM   1237  N   CYS A 181      25.087  88.160  29.462  1.00  7.31           N  
ANISOU 1237  N   CYS A 181      719    801   1256    107     13    218
ATOM   1238  CA  CYS A 181      25.879  87.182  30.220  1.00  6.94           C  
ANISOU 1238  CA  CYS A 181      789    805   1040     90     47     95
ATOM   1239  C   CYS A 181      26.703  86.314  29.283  1.00  5.45           C  
ANISOU 1239  C   CYS A 181      645    485    938    132    -16     42
ATOM   1240  O   CYS A 181      26.141  85.489  28.561  1.00  7.39           O  
ANISOU 1240  O   CYS A 181     1111    788    908   -134    -44     33
ATOM   1241  CB  CYS A 181      24.962  86.303  31.078  1.00  6.41           C  
ANISOU 1241  CB  CYS A 181      660    748   1026     24    106     93
ATOM   1242  SG  CYS A 181      25.861  85.236  32.223  1.00  7.83           S  
ANISOU 1242  SG  CYS A 181      648   1140   1186    283     44    118
ATOM   1243  N   HIS A 182      28.019  86.523  29.266  1.00  4.75           N  
ANISOU 1243  N   HIS A 182      420    472    910    125     23    -41
ATOM   1244  CA  HIS A 182      28.923  85.679  28.490  1.00  4.87           C  
ANISOU 1244  CA  HIS A 182      541    460    849     66     -2    -56
ATOM   1245  C   HIS A 182      29.179  84.323  29.156  1.00  5.00           C  
ANISOU 1245  C   HIS A 182      633    381    886     79    -51    -44
ATOM   1246  O   HIS A 182      29.309  83.300  28.481  1.00  4.32           O  
ANISOU 1246  O   HIS A 182      443    291    907     79     -3    -55
ATOM   1247  CB  HIS A 182      30.300  86.337  28.357  1.00  4.29           C  
ANISOU 1247  CB  HIS A 182      384    406    838     63    -26    -98
ATOM   1248  CG  HIS A 182      30.354  87.565  27.509  1.00  4.45           C  
ANISOU 1248  CG  HIS A 182      355    440    895     98    -62   -174
ATOM   1249  ND1 HIS A 182      30.563  88.826  28.031  1.00  5.14           N  
ANISOU 1249  ND1 HIS A 182      484    442   1027    169   -112   -226
ATOM   1250  CD2 HIS A 182      30.310  87.711  26.161  1.00  5.27           C  
ANISOU 1250  CD2 HIS A 182      641    438    923    112    110   -175
ATOM   1251  CE1 HIS A 182      30.632  89.695  27.032  1.00  5.48           C  
ANISOU 1251  CE1 HIS A 182      378    664   1038     22   -155   -202
ATOM   1252  NE2 HIS A 182      30.483  89.043  25.889  1.00  5.68           N  
ANISOU 1252  NE2 HIS A 182      621    640    895     46     30   -181
ATOM   1253  N   ILE A 183      29.360  84.352  30.485  1.00  4.22           N  
ANISOU 1253  N   ILE A 183      393    364    843    110     12    -78
ATOM   1254  CA  ILE A 183      29.761  83.184  31.264  1.00  4.10           C  
ANISOU 1254  CA  ILE A 183      452    397    706     73      7    -49
ATOM   1255  C   ILE A 183      28.823  83.064  32.465  1.00  4.22           C  
ANISOU 1255  C   ILE A 183      466    396    740     46    -41     -8
ATOM   1256  O   ILE A 183      28.787  83.950  33.328  1.00  4.88           O  
ANISOU 1256  O   ILE A 183      496    447    910    -11   -134     29
ATOM   1257  CB  ILE A 183      31.224  83.278  31.755  1.00  4.55           C  
ANISOU 1257  CB  ILE A 183      553    428    745     58    -13    -84
ATOM   1258  CG1 ILE A 183      32.189  83.557  30.607  1.00  5.13           C  
ANISOU 1258  CG1 ILE A 183      612    623    712     26     11    -10
ATOM   1259  CG2 ILE A 183      31.607  82.027  32.536  1.00  5.63           C  
ANISOU 1259  CG2 ILE A 183      560    762    816     58    178     13
ATOM   1260  CD1 ILE A 183      33.622  83.717  31.019  1.00  6.68           C  
ANISOU 1260  CD1 ILE A 183      950    779    809    116   -104    -43
ATOM   1261  N   ALA A 184      28.053  81.974  32.489  1.00  4.03           N  
ANISOU 1261  N   ALA A 184      472    305    752     29    -14     68
ATOM   1262  CA  ALA A 184      27.148  81.676  33.587  1.00  3.97           C  
ANISOU 1262  CA  ALA A 184      391    438    677     51     33      8
ATOM   1263  C   ALA A 184      27.836  80.683  34.508  1.00  3.68           C  
ANISOU 1263  C   ALA A 184      402    322    672     20    -20    -16
ATOM   1264  O   ALA A 184      28.280  79.635  34.058  1.00  4.22           O  
ANISOU 1264  O   ALA A 184      343    379    882    -41    126    -39
ATOM   1265  CB  ALA A 184      25.842  81.102  33.051  1.00  4.50           C  
ANISOU 1265  CB  ALA A 184      549    537    621    -43     -5      6
ATOM   1266  N   VAL A 185      27.897  81.014  35.797  1.00  4.02           N  
ANISOU 1266  N   VAL A 185      349    319    859     43     88     64
ATOM   1267  CA  VAL A 185      28.472  80.156  36.831  1.00  3.95           C  
ANISOU 1267  CA  VAL A 185      318    384    797    -12     23     22
ATOM   1268  C   VAL A 185      27.369  79.880  37.830  1.00  3.87           C  
ANISOU 1268  C   VAL A 185      258    429    782    -26    -35     44
ATOM   1269  O   VAL A 185      26.709  80.821  38.278  1.00  5.86           O  
ANISOU 1269  O   VAL A 185      515    654   1058    -47      0    279
ATOM   1270  CB  VAL A 185      29.651  80.848  37.546  1.00  4.19           C  
ANISOU 1270  CB  VAL A 185      424    402    764     64     12     19
ATOM   1271  CG1 VAL A 185      30.316  79.871  38.524  1.00  6.10           C  
ANISOU 1271  CG1 VAL A 185      574    744   1000    231     77    -56
ATOM   1272  CG2 VAL A 185      30.671  81.416  36.524  1.00  5.58           C  
ANISOU 1272  CG2 VAL A 185      654    710    753     33   -130    -21
ATOM   1273  N   GLY A 186      27.127  78.634  38.213  1.00  4.61           N  
ANISOU 1273  N   GLY A 186      416    440    895      7      6    144
ATOM   1274  CA  GLY A 186      26.100  78.403  39.195  1.00  5.18           C  
ANISOU 1274  CA  GLY A 186      530    654    782     -8    -26     99
ATOM   1275  C   GLY A 186      26.045  77.010  39.735  1.00  4.90           C  
ANISOU 1275  C   GLY A 186      528    579    752     65     18    130
ATOM   1276  O   GLY A 186      26.862  76.152  39.419  1.00  5.32           O  
ANISOU 1276  O   GLY A 186      413    711    898     60     37    203
ATOM   1277  N   SER A 187      25.073  76.795  40.623  1.00  5.92           N  
ANISOU 1277  N   SER A 187      690    670    889     89    -72    128
ATOM   1278  CA  SER A 187      24.804  75.505  41.250  0.50  6.95           C  
ANISOU 1278  CA  SER A 187      770    904    965    116   -106    105
ATOM   1279  C   SER A 187      23.724  74.776  40.416  1.00  6.56           C  
ANISOU 1279  C   SER A 187      716    879    897     70    -69    116
ATOM   1280  O   SER A 187      22.830  75.454  39.891  1.00  7.32           O  
ANISOU 1280  O   SER A 187      744   1173    863     58    -42     44
ATOM   1281  CB  SER A 187      24.359  75.753  42.702  0.50  8.15           C  
ANISOU 1281  CB  SER A 187      959    973   1163    168   -193    105
ATOM   1282  OG  SER A 187      25.459  76.221  43.472  0.50 12.06           O  
ANISOU 1282  OG  SER A 187     1278   1694   1610     27   -127    418
ATOM   1283  N   PRO A 188      23.835  73.434  40.235  1.00  6.32           N  
ANISOU 1283  N   PRO A 188      557    973    870     51     10      6
ATOM   1284  CA  PRO A 188      22.966  72.691  39.296  1.00  6.45           C  
ANISOU 1284  CA  PRO A 188      682    946    820     50    -24     41
ATOM   1285  C   PRO A 188      21.442  72.829  39.479  1.00  7.01           C  
ANISOU 1285  C   PRO A 188      877    927    859     36    -22    100
ATOM   1286  O   PRO A 188      20.735  72.758  38.474  1.00  6.63           O  
ANISOU 1286  O   PRO A 188      748    903    866      4   -108      7
ATOM   1287  CB  PRO A 188      23.426  71.230  39.421  1.00  7.30           C  
ANISOU 1287  CB  PRO A 188      757    973   1043    -51     15     -9
ATOM   1288  CG  PRO A 188      24.870  71.335  39.870  1.00  8.00           C  
ANISOU 1288  CG  PRO A 188      857   1248    934     47    -65     11
ATOM   1289  CD  PRO A 188      24.856  72.539  40.799  1.00  7.18           C  
ANISOU 1289  CD  PRO A 188      763   1167    799     95     58     30
ATOM   1290  N   GLY A 189      20.961  73.027  40.718  1.00  7.15           N  
ANISOU 1290  N   GLY A 189      860    964    890     99     14    116
ATOM   1291  CA  GLY A 189      19.545  73.229  41.041  1.00  6.95           C  
ANISOU 1291  CA  GLY A 189      857    964    817     73    -58    101
ATOM   1292  C   GLY A 189      18.999  74.479  40.345  1.00  6.48           C  
ANISOU 1292  C   GLY A 189      816    872    772    113    -78     89
ATOM   1293  O   GLY A 189      18.062  74.382  39.546  1.00  6.92           O  
ANISOU 1293  O   GLY A 189      849   1023    755    125    -80     84
ATOM   1294  N   ARG A 190      19.612  75.643  40.605  1.00  6.62           N  
ANISOU 1294  N   ARG A 190      932    831    750    112    -53     32
ATOM   1295  CA  ARG A 190      19.231  76.894  39.964  1.00  6.27           C  
ANISOU 1295  CA  ARG A 190      876    782    725     95     -8     37
ATOM   1296  C   ARG A 190      19.486  76.903  38.448  1.00  5.68           C  
ANISOU 1296  C   ARG A 190      855    644    657     -1     24     41
ATOM   1297  O   ARG A 190      18.611  77.367  37.716  1.00  5.63           O  
ANISOU 1297  O   ARG A 190      790    699    650     80     89     45
ATOM   1298  CB  ARG A 190      19.867  78.093  40.698  1.00  7.23           C  
ANISOU 1298  CB  ARG A 190     1119    827    800    178    -26     -2
ATOM   1299  CG  ARG A 190      19.591  79.484  40.090  1.00  7.41           C  
ANISOU 1299  CG  ARG A 190     1188    729    898    -20    -14    -19
ATOM   1300  CD  ARG A 190      18.103  79.842  39.962  1.00 10.16           C  
ANISOU 1300  CD  ARG A 190     1459   1231   1166    -36    -88     25
ATOM   1301  NE  ARG A 190      17.442  79.972  41.266  1.00 10.73           N  
ANISOU 1301  NE  ARG A 190     1625   1092   1360     71      9    -71
ATOM   1302  CZ  ARG A 190      17.107  81.089  41.920  1.00  9.37           C  
ANISOU 1302  CZ  ARG A 190     1343    934   1282     56     43    -94
ATOM   1303  NH1 ARG A 190      17.396  82.298  41.440  1.00 11.28           N  
ANISOU 1303  NH1 ARG A 190     1491   1312   1481     53     -4     73
ATOM   1304  NH2 ARG A 190      16.445  80.985  43.077  1.00 10.35           N1+
ANISOU 1304  NH2 ARG A 190     1604    816   1512     41     37     64
ATOM   1305  N   ILE A 191      20.636  76.384  37.992  1.00  5.53           N  
ANISOU 1305  N   ILE A 191      792    606    702     84    100     67
ATOM   1306  CA  ILE A 191      20.973  76.343  36.564  1.00  5.59           C  
ANISOU 1306  CA  ILE A 191      767    651    704     28     12     48
ATOM   1307  C   ILE A 191      19.976  75.512  35.732  1.00  5.40           C  
ANISOU 1307  C   ILE A 191      658    729    664     20      0     33
ATOM   1308  O   ILE A 191      19.551  75.981  34.674  1.00  5.69           O  
ANISOU 1308  O   ILE A 191      868    606    687     34     16     18
ATOM   1309  CB  ILE A 191      22.429  75.858  36.293  1.00  5.42           C  
ANISOU 1309  CB  ILE A 191      717    653    687     42     37     33
ATOM   1310  CG1 ILE A 191      23.474  76.882  36.803  1.00  5.65           C  
ANISOU 1310  CG1 ILE A 191      827    735    583    -67    -70    152
ATOM   1311  CG2 ILE A 191      22.722  75.456  34.825  1.00  5.75           C  
ANISOU 1311  CG2 ILE A 191      928    577    678     15    -35    131
ATOM   1312  CD1 ILE A 191      23.535  78.211  36.028  1.00  6.33           C  
ANISOU 1312  CD1 ILE A 191      753    739    913   -109    -20     -8
ATOM   1313  N   LYS A 192      19.581  74.329  36.235  1.00  6.17           N  
ANISOU 1313  N   LYS A 192      759    825    761    -18     -4     57
ATOM   1314  CA  LYS A 192      18.566  73.491  35.597  0.50  6.42           C  
ANISOU 1314  CA  LYS A 192      833    825    779    -35     27     36
ATOM   1315  C   LYS A 192      17.234  74.242  35.426  1.00  6.05           C  
ANISOU 1315  C   LYS A 192      788    781    727      1     25     -5
ATOM   1316  O   LYS A 192      16.714  74.279  34.313  1.00  6.51           O  
ANISOU 1316  O   LYS A 192      881    838    751    -99     -8    -45
ATOM   1317  CB  LYS A 192      18.419  72.142  36.340  0.50  7.14           C  
ANISOU 1317  CB  LYS A 192      910    960    843    -48      9     37
ATOM   1318  CG  LYS A 192      17.234  71.284  35.853  0.50  7.24           C  
ANISOU 1318  CG  LYS A 192      925    988    838    -53    -39      0
ATOM   1319  CD  LYS A 192      17.232  69.849  36.394  0.50  8.17           C  
ANISOU 1319  CD  LYS A 192      958   1133   1012    -84     20     37
ATOM   1320  CE  LYS A 192      15.971  69.064  35.988  0.50  9.56           C  
ANISOU 1320  CE  LYS A 192     1123   1343   1163    -93    -47    -28
ATOM   1321  NZ  LYS A 192      14.755  69.596  36.627  0.50 10.83           N1+
ANISOU 1321  NZ  LYS A 192     1397   1462   1255    -18    -81    -32
ATOM   1322  N   GLN A 193      16.762  74.882  36.506  1.00  6.40           N  
ANISOU 1322  N   GLN A 193      883    746    802    -19     83     26
ATOM   1323  CA  GLN A 193      15.533  75.678  36.511  1.00  6.96           C  
ANISOU 1323  CA  GLN A 193      945    883    815    -49     69     -5
ATOM   1324  C   GLN A 193      15.582  76.839  35.496  1.00  5.94           C  
ANISOU 1324  C   GLN A 193      845    678    730   -115     57    -60
ATOM   1325  O   GLN A 193      14.624  77.044  34.754  1.00  6.97           O  
ANISOU 1325  O   GLN A 193      997    957    691   -165     61    -94
ATOM   1326  CB  GLN A 193      15.246  76.158  37.955  1.00  8.18           C  
ANISOU 1326  CB  GLN A 193     1194   1001    911    -60     53    -21
ATOM   1327  CG  GLN A 193      13.936  76.948  38.165  1.00 10.27           C  
ANISOU 1327  CG  GLN A 193     1371   1303   1228    -57    103     36
ATOM   1328  CD  GLN A 193      12.688  76.149  37.785  1.00 12.29           C  
ANISOU 1328  CD  GLN A 193     1711   1462   1496    -23    105     81
ATOM   1329  OE1 GLN A 193      12.244  76.166  36.645  1.00 17.36           O  
ANISOU 1329  OE1 GLN A 193     2676   1602   2315    121     56   -178
ATOM   1330  NE2 GLN A 193      12.109  75.435  38.736  1.00 16.92           N  
ANISOU 1330  NE2 GLN A 193     2184   2322   1921     88    141    250
ATOM   1331  N   LEU A 194      16.719  77.546  35.424  1.00  5.29           N  
ANISOU 1331  N   LEU A 194      767    618    625    -60     29     38
ATOM   1332  CA  LEU A 194      16.918  78.611  34.441  1.00  5.72           C  
ANISOU 1332  CA  LEU A 194      801    610    762    -43    107     -5
ATOM   1333  C   LEU A 194      16.879  78.114  32.991  1.00  5.64           C  
ANISOU 1333  C   LEU A 194      800    557    786    -47     44    -54
ATOM   1334  O   LEU A 194      16.365  78.851  32.148  1.00  6.37           O  
ANISOU 1334  O   LEU A 194      892    641    887     30    173    -45
ATOM   1335  CB  LEU A 194      18.228  79.377  34.698  1.00  5.86           C  
ANISOU 1335  CB  LEU A 194      740    704    781    -66    129     48
ATOM   1336  CG  LEU A 194      18.247  80.201  35.996  1.00  6.11           C  
ANISOU 1336  CG  LEU A 194      762    675    883   -100     98    -41
ATOM   1337  CD1 LEU A 194      19.680  80.648  36.311  1.00  7.03           C  
ANISOU 1337  CD1 LEU A 194      845    927    896    -16     51   -165
ATOM   1338  CD2 LEU A 194      17.277  81.394  35.964  1.00  6.75           C  
ANISOU 1338  CD2 LEU A 194      812    660   1092   -191    163    -96
ATOM   1339  N   ILE A 195      17.390  76.902  32.720  1.00  6.09           N  
ANISOU 1339  N   ILE A 195      814    693    807    -14     96    -47
ATOM   1340  CA  ILE A 195      17.304  76.337  31.375  1.00  6.69           C  
ANISOU 1340  CA  ILE A 195      901    708    929    -11     80     -2
ATOM   1341  C   ILE A 195      15.875  75.866  31.087  1.00  6.86           C  
ANISOU 1341  C   ILE A 195      973    696    935    -32     96    -31
ATOM   1342  O   ILE A 195      15.339  76.114  30.002  1.00  8.16           O  
ANISOU 1342  O   ILE A 195     1283    696   1118    -12    175   -176
ATOM   1343  CB  ILE A 195      18.341  75.217  31.148  1.00  6.65           C  
ANISOU 1343  CB  ILE A 195      918    651    954    -15    167    -37
ATOM   1344  CG1 ILE A 195      19.765  75.796  31.220  1.00  6.85           C  
ANISOU 1344  CG1 ILE A 195      826    724   1051     -5    140     54
ATOM   1345  CG2 ILE A 195      18.138  74.555  29.777  1.00  7.36           C  
ANISOU 1345  CG2 ILE A 195     1001    635   1160    -42    197    -40
ATOM   1346  CD1 ILE A 195      20.868  74.756  31.251  1.00  7.38           C  
ANISOU 1346  CD1 ILE A 195      908    845   1052    -99    140    168
ATOM   1347  N   GLU A 196      15.241  75.228  32.059  1.00  7.38           N  
ANISOU 1347  N   GLU A 196     1047    757    999    -36      5   -120
ATOM   1348  CA  GLU A 196      13.863  74.741  31.879  1.00  9.19           C  
ANISOU 1348  CA  GLU A 196     1298   1062   1131    -24     -3    -88
ATOM   1349  C   GLU A 196      12.908  75.897  31.565  1.00  8.47           C  
ANISOU 1349  C   GLU A 196     1196   1008   1012      3    -48   -124
ATOM   1350  O   GLU A 196      11.974  75.742  30.765  1.00 10.14           O  
ANISOU 1350  O   GLU A 196     1445   1257   1151    -75     25   -287
ATOM   1351  CB  GLU A 196      13.380  74.061  33.160  1.00 10.38           C  
ANISOU 1351  CB  GLU A 196     1424   1289   1228     -1    -59   -122
ATOM   1352  CG  GLU A 196      13.954  72.648  33.352  1.00 12.97           C  
ANISOU 1352  CG  GLU A 196     1776   1614   1536   -100    -30    -60
ATOM   1353  CD  GLU A 196      13.516  71.979  34.651  1.00 14.90           C  
ANISOU 1353  CD  GLU A 196     1790   1851   2018    -13   -109     -7
ATOM   1354  OE1 GLU A 196      13.869  72.501  35.729  1.00 17.63           O  
ANISOU 1354  OE1 GLU A 196     1974   2122   2600   -135   -114    -86
ATOM   1355  OE2 GLU A 196      12.882  70.907  34.559  1.00 22.39           O1-
ANISOU 1355  OE2 GLU A 196     2440   2836   3231   -225   -426    -23
ATOM   1356  N   LEU A 197      13.122  77.041  32.218  1.00  8.07           N  
ANISOU 1356  N   LEU A 197     1114    999    952    -17     22    -64
ATOM   1357  CA  LEU A 197      12.301  78.221  31.979  1.00  8.81           C  
ANISOU 1357  CA  LEU A 197     1172   1162   1013    -24     -5    -89
ATOM   1358  C   LEU A 197      12.659  78.974  30.693  1.00  8.80           C  
ANISOU 1358  C   LEU A 197     1207   1121   1015      6     23   -161
ATOM   1359  O   LEU A 197      11.998  79.946  30.329  1.00  9.71           O  
ANISOU 1359  O   LEU A 197     1315   1244   1127     79     74   -140
ATOM   1360  CB  LEU A 197      12.458  79.176  33.157  1.00  8.96           C  
ANISOU 1360  CB  LEU A 197     1240   1171    990     11     66    -93
ATOM   1361  CG  LEU A 197      11.711  78.757  34.426  1.00  7.70           C  
ANISOU 1361  CG  LEU A 197     1036   1050    837   -106     56      6
ATOM   1362  CD1 LEU A 197      12.271  79.465  35.664  1.00  8.08           C  
ANISOU 1362  CD1 LEU A 197      954   1059   1056    -54    120     35
ATOM   1363  CD2 LEU A 197      10.198  79.017  34.254  1.00 10.16           C  
ANISOU 1363  CD2 LEU A 197     1444   1414    999     36    129    137
ATOM   1364  N   ASP A 198      13.735  78.550  30.043  1.00  8.91           N  
ANISOU 1364  N   ASP A 198     1198   1076   1110     26     68    -86
ATOM   1365  CA  ASP A 198      14.310  79.245  28.887  1.00  9.22           C  
ANISOU 1365  CA  ASP A 198     1200   1162   1138     69     49    -92
ATOM   1366  C   ASP A 198      14.794  80.653  29.225  1.00  8.90           C  
ANISOU 1366  C   ASP A 198     1083   1121   1179     67     61    -24
ATOM   1367  O   ASP A 198      14.915  81.497  28.340  1.00 10.61           O  
ANISOU 1367  O   ASP A 198     1139   1349   1541    147     34   -202
ATOM   1368  CB  ASP A 198      13.361  79.265  27.671  1.00 10.22           C  
ANISOU 1368  CB  ASP A 198     1298   1183   1402    121     22   -173
ATOM   1369  CG  ASP A 198      14.108  79.427  26.331  1.00 11.78           C  
ANISOU 1369  CG  ASP A 198     1515   1489   1469    183    112    -47
ATOM   1370  OD1 ASP A 198      15.228  78.880  26.153  1.00 14.12           O  
ANISOU 1370  OD1 ASP A 198     2036   1524   1805    358    246     17
ATOM   1371  OD2 ASP A 198      13.532  80.060  25.413  1.00 16.95           O1-
ANISOU 1371  OD2 ASP A 198     2035   2001   2402    568    299    -91
ATOM   1372  N   TYR A 199      15.135  80.881  30.491  1.00  7.60           N  
ANISOU 1372  N   TYR A 199      952    946    988      9     67    -10
ATOM   1373  CA  TYR A 199      15.810  82.119  30.895  1.00  7.89           C  
ANISOU 1373  CA  TYR A 199      997   1002    997      3     80     26
ATOM   1374  C   TYR A 199      17.286  82.084  30.510  1.00  7.71           C  
ANISOU 1374  C   TYR A 199      981    983    962     49     75     30
ATOM   1375  O   TYR A 199      17.863  83.104  30.116  1.00  7.92           O  
ANISOU 1375  O   TYR A 199      856   1109   1042    -20    186    -54
ATOM   1376  CB  TYR A 199      15.647  82.372  32.389  1.00  7.84           C  
ANISOU 1376  CB  TYR A 199     1027    983    969     69    170     71
ATOM   1377  CG  TYR A 199      14.222  82.675  32.843  1.00  8.40           C  
ANISOU 1377  CG  TYR A 199     1037   1132   1020     91     72    131
ATOM   1378  CD1 TYR A 199      13.155  82.770  31.940  1.00  8.92           C  
ANISOU 1378  CD1 TYR A 199     1332   1076    979    -41    111    119
ATOM   1379  CD2 TYR A 199      13.954  82.896  34.187  1.00  7.23           C  
ANISOU 1379  CD2 TYR A 199      873    937    936     99    188    104
ATOM   1380  CE1 TYR A 199      11.867  83.031  32.385  1.00  8.49           C  
ANISOU 1380  CE1 TYR A 199     1214   1182    830     89    169     47
ATOM   1381  CE2 TYR A 199      12.679  83.196  34.636  1.00  8.33           C  
ANISOU 1381  CE2 TYR A 199     1069   1076   1018     11     64    140
ATOM   1382  CZ  TYR A 199      11.634  83.244  33.739  1.00  8.98           C  
ANISOU 1382  CZ  TYR A 199     1141   1268   1002    149    113    133
ATOM   1383  OH  TYR A 199      10.356  83.548  34.177  1.00 10.54           O  
ANISOU 1383  OH  TYR A 199     1453   1435   1116    156     83    241
ATOM   1384  N   LEU A 200      17.886  80.903  30.634  1.00  7.63           N  
ANISOU 1384  N   LEU A 200      927   1054    918      2     38    116
ATOM   1385  CA  LEU A 200      19.178  80.606  30.014  1.00  8.68           C  
ANISOU 1385  CA  LEU A 200     1082   1167   1047     30     29     47
ATOM   1386  C   LEU A 200      18.871  79.714  28.824  1.00  8.16           C  
ANISOU 1386  C   LEU A 200      972   1055   1074     41     73     84
ATOM   1387  O   LEU A 200      18.560  78.538  29.003  1.00  9.50           O  
ANISOU 1387  O   LEU A 200     1207   1063   1337    -11    -41    -26
ATOM   1388  CB  LEU A 200      20.088  79.877  30.996  1.00  8.72           C  
ANISOU 1388  CB  LEU A 200     1120   1175   1018    -46     22     23
ATOM   1389  CG  LEU A 200      21.410  79.339  30.422  1.00  9.81           C  
ANISOU 1389  CG  LEU A 200     1158   1513   1057     45     25     61
ATOM   1390  CD1 LEU A 200      22.165  80.320  29.514  1.00 11.13           C  
ANISOU 1390  CD1 LEU A 200     1222   1750   1256     -8    -59    150
ATOM   1391  CD2 LEU A 200      22.301  78.773  31.517  1.00 11.00           C  
ANISOU 1391  CD2 LEU A 200     1297   1689   1191     77    153     35
ATOM   1392  N   ASN A 201      18.935  80.255  27.604  1.00  9.31           N  
ANISOU 1392  N   ASN A 201     1130   1210   1196     98    138     46
ATOM   1393  CA  ASN A 201      18.792  79.408  26.433  1.00  9.71           C  
ANISOU 1393  CA  ASN A 201     1277   1259   1151     95    101     38
ATOM   1394  C   ASN A 201      20.179  78.836  26.149  1.00  9.50           C  
ANISOU 1394  C   ASN A 201     1344   1163   1101    199     78     29
ATOM   1395  O   ASN A 201      21.127  79.587  26.004  1.00 11.38           O  
ANISOU 1395  O   ASN A 201     1576   1545   1202     93     84     91
ATOM   1396  CB  ASN A 201      18.222  80.145  25.220  1.00 10.75           C  
ANISOU 1396  CB  ASN A 201     1464   1383   1237     56    148     30
ATOM   1397  CG  ASN A 201      18.088  79.233  24.037  1.00 11.80           C  
ANISOU 1397  CG  ASN A 201     1707   1376   1400    206    213   -101
ATOM   1398  OD1 ASN A 201      19.067  78.952  23.375  1.00 15.40           O  
ANISOU 1398  OD1 ASN A 201     2574   1653   1622    252    498      1
ATOM   1399  ND2 ASN A 201      16.887  78.700  23.807  1.00 17.86           N  
ANISOU 1399  ND2 ASN A 201     2666   2323   1796    -11    131    -75
ATOM   1400  N   PRO A 202      20.303  77.514  26.146  1.00  9.60           N  
ANISOU 1400  N   PRO A 202     1456   1164   1027    143     93     52
ATOM   1401  CA  PRO A 202      21.645  76.932  26.056  1.00  9.68           C  
ANISOU 1401  CA  PRO A 202     1405   1133   1138     92    158     34
ATOM   1402  C   PRO A 202      22.229  76.864  24.645  1.00  9.27           C  
ANISOU 1402  C   PRO A 202     1361   1086   1072     95    155     30
ATOM   1403  O   PRO A 202      23.324  76.338  24.465  1.00  8.56           O  
ANISOU 1403  O   PRO A 202     1383   1059    811     77    170     39
ATOM   1404  CB  PRO A 202      21.437  75.540  26.627  1.00 10.90           C  
ANISOU 1404  CB  PRO A 202     1502   1316   1320     90    157     99
ATOM   1405  CG  PRO A 202      20.034  75.194  26.331  1.00 11.57           C  
ANISOU 1405  CG  PRO A 202     1529   1370   1496     17     -2     59
ATOM   1406  CD  PRO A 202      19.262  76.483  26.342  1.00 10.16           C  
ANISOU 1406  CD  PRO A 202     1510   1239   1111    133     84      5
ATOM   1407  N   GLY A 203      21.525  77.393  23.647  1.00  8.86           N  
ANISOU 1407  N   GLY A 203     1340   1026   1000     54    220     40
ATOM   1408  CA  GLY A 203      21.931  77.231  22.254  1.00  8.73           C  
ANISOU 1408  CA  GLY A 203     1262    972   1081     80    146    -46
ATOM   1409  C   GLY A 203      23.262  77.825  21.850  1.00  8.39           C  
ANISOU 1409  C   GLY A 203     1113    987   1088     19    172   -101
ATOM   1410  O   GLY A 203      23.836  77.386  20.851  1.00  9.66           O  
ANISOU 1410  O   GLY A 203     1277   1111   1279     37    -13    -67
ATOM   1411  N   SER A 204      23.773  78.809  22.596  1.00  8.54           N  
ANISOU 1411  N   SER A 204     1082    943   1218     83    256   -143
ATOM   1412  CA  SER A 204      25.094  79.341  22.296  1.00  9.35           C  
ANISOU 1412  CA  SER A 204     1116   1161   1274     86    107   -214
ATOM   1413  C   SER A 204      26.208  78.786  23.148  1.00  7.63           C  
ANISOU 1413  C   SER A 204     1031    863   1003    131     85   -194
ATOM   1414  O   SER A 204      27.357  79.195  22.974  1.00  8.14           O  
ANISOU 1414  O   SER A 204     1145    869   1077    223    -46   -340
ATOM   1415  CB  SER A 204      25.168  80.858  22.346  1.00 11.98           C  
ANISOU 1415  CB  SER A 204     1350   1613   1589     -8    210   -249
ATOM   1416  OG  SER A 204      24.488  81.407  21.242  1.00 15.99           O  
ANISOU 1416  OG  SER A 204     1797   2076   2200    165    205   -225
ATOM   1417  N   ILE A 205      25.899  77.851  24.042  1.00  5.92           N  
ANISOU 1417  N   ILE A 205      797    711    741     58     61   -144
ATOM   1418  CA  ILE A 205      26.950  77.301  24.897  1.00  6.00           C  
ANISOU 1418  CA  ILE A 205      849    717    712    -28     51   -101
ATOM   1419  C   ILE A 205      27.827  76.365  24.068  1.00  5.72           C  
ANISOU 1419  C   ILE A 205      841    561    770    -74      1    -86
ATOM   1420  O   ILE A 205      27.327  75.417  23.453  1.00  7.77           O  
ANISOU 1420  O   ILE A 205     1339    777    834   -224    -47   -146
ATOM   1421  CB  ILE A 205      26.368  76.539  26.108  1.00  5.75           C  
ANISOU 1421  CB  ILE A 205      820    666    696    -83     46    -83
ATOM   1422  CG1 ILE A 205      25.586  77.503  26.998  1.00  7.26           C  
ANISOU 1422  CG1 ILE A 205     1080    845    832    -19      2     42
ATOM   1423  CG2 ILE A 205      27.493  75.848  26.916  1.00  6.81           C  
ANISOU 1423  CG2 ILE A 205      845   1011    729    108    121    -22
ATOM   1424  CD1 ILE A 205      24.792  76.846  28.076  1.00  7.91           C  
ANISOU 1424  CD1 ILE A 205     1334    901    771    127    -54     57
ATOM   1425  N   ARG A 206      29.133  76.619  24.076  1.00  5.19           N  
ANISOU 1425  N   ARG A 206      729    502    737    -31     83    -90
ATOM   1426  CA  ARG A 206      30.095  75.716  23.439  1.00  5.79           C  
ANISOU 1426  CA  ARG A 206      791    617    791     59     49     11
ATOM   1427  C   ARG A 206      31.107  75.117  24.408  1.00  4.99           C  
ANISOU 1427  C   ARG A 206      651    514    731    -15     71     19
ATOM   1428  O   ARG A 206      31.879  74.274  24.008  1.00  5.51           O  
ANISOU 1428  O   ARG A 206      704    426    963     84     78     21
ATOM   1429  CB  ARG A 206      30.828  76.361  22.255  1.00  6.27           C  
ANISOU 1429  CB  ARG A 206      789    703    890    107    129     43
ATOM   1430  CG  ARG A 206      31.797  77.432  22.664  1.00  6.29           C  
ANISOU 1430  CG  ARG A 206      693    744    951    114     41     -9
ATOM   1431  CD  ARG A 206      32.947  77.610  21.666  1.00  6.85           C  
ANISOU 1431  CD  ARG A 206      916    719    967     87     46    -36
ATOM   1432  NE  ARG A 206      33.785  76.416  21.571  1.00  7.00           N  
ANISOU 1432  NE  ARG A 206     1036    747    875    125    -46     -5
ATOM   1433  CZ  ARG A 206      34.751  76.080  22.428  1.00  6.99           C  
ANISOU 1433  CZ  ARG A 206      920    807    929     25     26     54
ATOM   1434  NH1 ARG A 206      35.063  76.871  23.446  1.00  7.52           N  
ANISOU 1434  NH1 ARG A 206     1091    855    910    -55     73     33
ATOM   1435  NH2 ARG A 206      35.451  74.966  22.230  1.00  7.47           N1+
ANISOU 1435  NH2 ARG A 206     1048    833    955    -37     94     48
ATOM   1436  N   LEU A 207      31.129  75.587  25.663  1.00  4.56           N  
ANISOU 1436  N   LEU A 207      580    487    665     73     80    -11
ATOM   1437  CA  LEU A 207      32.091  75.115  26.653  1.00  4.36           C  
ANISOU 1437  CA  LEU A 207      642    408    605     69     -3     -7
ATOM   1438  C   LEU A 207      31.360  74.897  27.982  1.00  3.66           C  
ANISOU 1438  C   LEU A 207      502    270    619     64     18    -13
ATOM   1439  O   LEU A 207      30.723  75.813  28.488  1.00  4.08           O  
ANISOU 1439  O   LEU A 207      484    347    716    -11    -17     58
ATOM   1440  CB  LEU A 207      33.231  76.127  26.802  1.00  4.04           C  
ANISOU 1440  CB  LEU A 207      484    394    654     14     20     22
ATOM   1441  CG  LEU A 207      34.347  75.801  27.809  1.00  4.41           C  
ANISOU 1441  CG  LEU A 207      593    530    551     26      8    -15
ATOM   1442  CD1 LEU A 207      35.033  74.481  27.452  1.00  6.31           C  
ANISOU 1442  CD1 LEU A 207      747    810    838   -128    122    -44
ATOM   1443  CD2 LEU A 207      35.373  76.938  27.832  1.00  5.36           C  
ANISOU 1443  CD2 LEU A 207      809    646    579    -25    -68   -174
ATOM   1444  N   PHE A 208      31.432  73.676  28.490  1.00  3.76           N  
ANISOU 1444  N   PHE A 208      455    351    622     12     20     -9
ATOM   1445  CA  PHE A 208      30.715  73.269  29.693  1.00  3.57           C  
ANISOU 1445  CA  PHE A 208      471    334    552     -1      0     -4
ATOM   1446  C   PHE A 208      31.754  72.745  30.674  1.00  3.61           C  
ANISOU 1446  C   PHE A 208      438    354    577      0      4      7
ATOM   1447  O   PHE A 208      32.507  71.831  30.349  1.00  4.43           O  
ANISOU 1447  O   PHE A 208      541    269    870      9    234     56
ATOM   1448  CB  PHE A 208      29.706  72.187  29.298  1.00  4.02           C  
ANISOU 1448  CB  PHE A 208      522    396    607   -152    -13    -32
ATOM   1449  CG  PHE A 208      28.810  71.673  30.411  1.00  4.30           C  
ANISOU 1449  CG  PHE A 208      555    471    606   -134    -67    -35
ATOM   1450  CD1 PHE A 208      28.336  72.477  31.406  1.00  4.62           C  
ANISOU 1450  CD1 PHE A 208      468    656    630   -183   -242     47
ATOM   1451  CD2 PHE A 208      28.389  70.353  30.398  1.00  7.53           C  
ANISOU 1451  CD2 PHE A 208      855    732   1271   -180   -288    258
ATOM   1452  CE1 PHE A 208      27.475  71.985  32.366  1.00  5.38           C  
ANISOU 1452  CE1 PHE A 208      631    586    827   -182    -26     57
ATOM   1453  CE2 PHE A 208      27.536  69.871  31.335  1.00  7.80           C  
ANISOU 1453  CE2 PHE A 208      727    991   1245   -359   -405     45
ATOM   1454  CZ  PHE A 208      27.072  70.696  32.326  1.00  5.32           C  
ANISOU 1454  CZ  PHE A 208      510    745    763      8   -104     72
ATOM   1455  N   ILE A 209      31.821  73.329  31.868  1.00  3.41           N  
ANISOU 1455  N   ILE A 209      320    378    597     16     75     32
ATOM   1456  CA  ILE A 209      32.891  73.077  32.832  1.00  3.91           C  
ANISOU 1456  CA  ILE A 209      443    410    631    -17     22     39
ATOM   1457  C   ILE A 209      32.320  72.611  34.161  1.00  3.56           C  
ANISOU 1457  C   ILE A 209      313    436    601    -65      0     38
ATOM   1458  O   ILE A 209      31.405  73.230  34.689  1.00  4.12           O  
ANISOU 1458  O   ILE A 209      527    289    748     35     60    117
ATOM   1459  CB  ILE A 209      33.746  74.357  33.050  1.00  3.77           C  
ANISOU 1459  CB  ILE A 209      523    347    559    -12     -8     89
ATOM   1460  CG1 ILE A 209      34.364  74.812  31.726  1.00  4.49           C  
ANISOU 1460  CG1 ILE A 209      586    528    589    -27    -14      4
ATOM   1461  CG2 ILE A 209      34.820  74.146  34.140  1.00  4.87           C  
ANISOU 1461  CG2 ILE A 209      602    664    583    -36     81   -127
ATOM   1462  CD1 ILE A 209      35.008  76.211  31.755  1.00  5.39           C  
ANISOU 1462  CD1 ILE A 209      475    679    892      2    -79    -28
ATOM   1463  N   LEU A 210      32.873  71.516  34.676  1.00  3.90           N  
ANISOU 1463  N   LEU A 210      290    421    768    -66     60     34
ATOM   1464  CA  LEU A 210      32.525  70.986  35.973  1.00  4.58           C  
ANISOU 1464  CA  LEU A 210      495    515    728    -23     41     72
ATOM   1465  C   LEU A 210      33.690  71.204  36.930  1.00  4.53           C  
ANISOU 1465  C   LEU A 210      466    535    719     16     29     81
ATOM   1466  O   LEU A 210      34.755  70.627  36.741  1.00  6.18           O  
ANISOU 1466  O   LEU A 210      907    534    907     91    321     85
ATOM   1467  CB  LEU A 210      32.217  69.491  35.873  1.00  5.01           C  
ANISOU 1467  CB  LEU A 210      600    622    682    -41    -65    148
ATOM   1468  CG  LEU A 210      31.120  69.090  34.888  1.00  5.78           C  
ANISOU 1468  CG  LEU A 210      600    812    782   -145    -16     70
ATOM   1469  CD1 LEU A 210      30.885  67.553  34.971  1.00  9.76           C  
ANISOU 1469  CD1 LEU A 210      934   1529   1245   -529   -113   -117
ATOM   1470  CD2 LEU A 210      29.827  69.833  35.090  1.00  6.65           C  
ANISOU 1470  CD2 LEU A 210      842    874    810   -156    163     33
ATOM   1471  N   ASP A 211      33.525  72.113  37.914  1.00  4.65           N  
ANISOU 1471  N   ASP A 211      449    592    723    -38     76     68
ATOM   1472  CA  ASP A 211      34.530  72.439  38.948  1.00  4.76           C  
ANISOU 1472  CA  ASP A 211      539    549    719    -11    -13     31
ATOM   1473  C   ASP A 211      34.345  71.485  40.138  1.00  5.42           C  
ANISOU 1473  C   ASP A 211      610    662    785     23    -11     58
ATOM   1474  O   ASP A 211      33.244  71.412  40.680  1.00  7.11           O  
ANISOU 1474  O   ASP A 211      748    967    983    321    -42    162
ATOM   1475  CB  ASP A 211      34.463  73.919  39.426  1.00  5.31           C  
ANISOU 1475  CB  ASP A 211      637    539    842   -107     -8     64
ATOM   1476  CG  ASP A 211      35.496  74.352  40.495  1.00  5.85           C  
ANISOU 1476  CG  ASP A 211      629    767    826    -34    -41    126
ATOM   1477  OD1 ASP A 211      36.676  73.936  40.431  1.00  6.82           O  
ANISOU 1477  OD1 ASP A 211      909    788    893    -92      0    -31
ATOM   1478  OD2 ASP A 211      35.132  75.216  41.317  1.00  7.76           O1-
ANISOU 1478  OD2 ASP A 211     1150    577   1219   -143     18    -50
ATOM   1479  N   GLU A 212      35.422  70.783  40.509  1.00  5.57           N  
ANISOU 1479  N   GLU A 212      612    703    801     14    -82      5
ATOM   1480  CA  GLU A 212      35.503  69.759  41.556  1.00  5.77           C  
ANISOU 1480  CA  GLU A 212      631    644    914     -7    -41     22
ATOM   1481  C   GLU A 212      34.421  68.677  41.363  1.00  5.51           C  
ANISOU 1481  C   GLU A 212      587    652    852     49    -31     37
ATOM   1482  O   GLU A 212      33.536  68.470  42.197  1.00  5.72           O  
ANISOU 1482  O   GLU A 212      593    630    950    -37   -100     91
ATOM   1483  CB  GLU A 212      35.622  70.380  42.968  1.00  7.13           C  
ANISOU 1483  CB  GLU A 212      851    809   1046     13    -77      7
ATOM   1484  CG  GLU A 212      36.628  71.561  43.101  1.00  8.62           C  
ANISOU 1484  CG  GLU A 212     1069    975   1231    -31    -12     -6
ATOM   1485  CD  GLU A 212      38.017  71.377  42.461  1.00 10.60           C  
ANISOU 1485  CD  GLU A 212     1514   1012   1498   -111   -104    -80
ATOM   1486  OE1 GLU A 212      38.496  70.227  42.364  1.00 16.25           O  
ANISOU 1486  OE1 GLU A 212     2001   1690   2483      3   -232     45
ATOM   1487  OE2 GLU A 212      38.590  72.419  42.060  1.00 15.42           O1-
ANISOU 1487  OE2 GLU A 212     2297   1590   1970   -102   -226   -326
ATOM   1488  N   ALA A 213      34.548  68.037  40.192  1.00  5.44           N  
ANISOU 1488  N   ALA A 213      627    592    848     82    -23     54
ATOM   1489  CA  ALA A 213      33.633  67.089  39.572  1.00  5.33           C  
ANISOU 1489  CA  ALA A 213      546    662    814     39    -45     40
ATOM   1490  C   ALA A 213      33.334  65.896  40.480  1.00  5.90           C  
ANISOU 1490  C   ALA A 213      598    684    957    -57      0     56
ATOM   1491  O   ALA A 213      32.247  65.347  40.420  1.00  5.89           O  
ANISOU 1491  O   ALA A 213      492    716   1029    -47    -67     42
ATOM   1492  CB  ALA A 213      34.153  66.649  38.206  1.00  5.64           C  
ANISOU 1492  CB  ALA A 213      626    585    929    120    -43     61
ATOM   1493  N   ASP A 214      34.271  65.466  41.348  1.00  5.54           N  
ANISOU 1493  N   ASP A 214      581    604    917     -3    -70     39
ATOM   1494  CA  ASP A 214      34.004  64.382  42.312  1.00  5.88           C  
ANISOU 1494  CA  ASP A 214      590    676    968    -18    -78     12
ATOM   1495  C   ASP A 214      32.830  64.737  43.250  1.00  6.45           C  
ANISOU 1495  C   ASP A 214      630    780   1038    -20    -97     32
ATOM   1496  O   ASP A 214      31.872  63.975  43.344  1.00  7.94           O  
ANISOU 1496  O   ASP A 214      888    926   1199   -129   -229    122
ATOM   1497  CB  ASP A 214      35.229  63.854  43.112  1.00  6.35           C  
ANISOU 1497  CB  ASP A 214      662    675   1073    -89     -5    -72
ATOM   1498  CG  ASP A 214      36.143  64.881  43.789  1.00  7.90           C  
ANISOU 1498  CG  ASP A 214      818    941   1242     29    -11    -36
ATOM   1499  OD1 ASP A 214      35.733  66.050  43.943  1.00  7.60           O  
ANISOU 1499  OD1 ASP A 214      843    675   1368   -138   -140   -129
ATOM   1500  OD2 ASP A 214      37.224  64.448  44.241  1.00  8.11           O1-
ANISOU 1500  OD2 ASP A 214      745    967   1369      1     66   -118
ATOM   1501  N   LYS A 215      32.868  65.936  43.836  1.00  6.14           N  
ANISOU 1501  N   LYS A 215      694    641    998    -44   -137     60
ATOM   1502  CA  LYS A 215      31.811  66.469  44.692  1.00  6.74           C  
ANISOU 1502  CA  LYS A 215      656    775   1128      2   -101    105
ATOM   1503  C   LYS A 215      30.584  67.004  43.932  1.00  6.47           C  
ANISOU 1503  C   LYS A 215      729    759    970    -37   -176    101
ATOM   1504  O   LYS A 215      29.562  67.252  44.576  1.00  8.62           O  
ANISOU 1504  O   LYS A 215     1034   1085   1154    127   -191    183
ATOM   1505  CB  LYS A 215      32.411  67.468  45.711  1.00  8.01           C  
ANISOU 1505  CB  LYS A 215      875    940   1229    -97   -103    103
ATOM   1506  CG  LYS A 215      32.562  66.860  47.124  1.00 12.03           C  
ANISOU 1506  CG  LYS A 215     1514   1373   1683    -98     29    -88
ATOM   1507  CD  LYS A 215      33.480  65.632  47.224  1.00 15.91           C  
ANISOU 1507  CD  LYS A 215     1960   1904   2181     48    -22    -70
ATOM   1508  CE  LYS A 215      34.967  65.985  47.246  1.00 17.74           C  
ANISOU 1508  CE  LYS A 215     2189   2243   2307    159     69   -167
ATOM   1509  NZ  LYS A 215      35.787  64.776  47.101  1.00 20.60           N1+
ANISOU 1509  NZ  LYS A 215     2433   2611   2780    225     41   -101
ATOM   1510  N   LEU A 216      30.668  67.126  42.600  1.00  5.93           N  
ANISOU 1510  N   LEU A 216      623    706    924      3   -125     91
ATOM   1511  CA  LEU A 216      29.498  67.344  41.747  1.00  6.21           C  
ANISOU 1511  CA  LEU A 216      698    713    947    -36    -94     72
ATOM   1512  C   LEU A 216      28.731  66.047  41.453  1.00  6.58           C  
ANISOU 1512  C   LEU A 216      726    848    926     -3    -85     42
ATOM   1513  O   LEU A 216      27.536  66.139  41.170  1.00  7.46           O  
ANISOU 1513  O   LEU A 216      855    947   1031    -71   -122     81
ATOM   1514  CB  LEU A 216      29.882  67.982  40.393  1.00  5.72           C  
ANISOU 1514  CB  LEU A 216      601    691    880    -29    -40    103
ATOM   1515  CG  LEU A 216      30.349  69.448  40.443  1.00  6.00           C  
ANISOU 1515  CG  LEU A 216      559    841    880    -68    -11    -31
ATOM   1516  CD1 LEU A 216      30.829  69.908  39.064  1.00  6.41           C  
ANISOU 1516  CD1 LEU A 216      663    696   1076     18    -27     78
ATOM   1517  CD2 LEU A 216      29.235  70.376  40.939  1.00  7.24           C  
ANISOU 1517  CD2 LEU A 216      922    939    889   -360   -146    118
ATOM   1518  N   LEU A 217      29.423  64.895  41.435  1.00  6.77           N  
ANISOU 1518  N   LEU A 217      713    849   1010    -92   -121    -36
ATOM   1519  CA  LEU A 217      28.864  63.669  40.874  1.00  7.89           C  
ANISOU 1519  CA  LEU A 217      796   1039   1161    -85   -100    -19
ATOM   1520  C   LEU A 217      28.813  62.508  41.876  1.00  9.50           C  
ANISOU 1520  C   LEU A 217      939   1279   1389    -66   -195     30
ATOM   1521  O   LEU A 217      28.304  61.440  41.537  1.00 10.86           O  
ANISOU 1521  O   LEU A 217      932   1569   1625    -92   -322   -144
ATOM   1522  CB  LEU A 217      29.620  63.304  39.580  1.00  7.88           C  
ANISOU 1522  CB  LEU A 217      823   1035   1132   -114   -137    -40
ATOM   1523  CG  LEU A 217      29.528  64.316  38.408  1.00  7.61           C  
ANISOU 1523  CG  LEU A 217      926    874   1090     13    -31    -12
ATOM   1524  CD1 LEU A 217      30.531  63.969  37.296  1.00  7.94           C  
ANISOU 1524  CD1 LEU A 217     1091    757   1166   -228    -93    115
ATOM   1525  CD2 LEU A 217      28.107  64.419  37.830  1.00  9.03           C  
ANISOU 1525  CD2 LEU A 217     1298    987   1144    -81     59    -57
ATOM   1526  N   GLU A 218      29.277  62.698  43.117  1.00  9.54           N  
ANISOU 1526  N   GLU A 218      764   1408   1450    -74   -220     33
ATOM   1527  CA  GLU A 218      29.172  61.708  44.194  1.00 11.54           C  
ANISOU 1527  CA  GLU A 218     1127   1641   1617     90   -132     54
ATOM   1528  C   GLU A 218      27.719  61.306  44.545  1.00 12.77           C  
ANISOU 1528  C   GLU A 218     1258   1860   1731     73   -134     64
ATOM   1529  O   GLU A 218      26.758  61.992  44.186  1.00 12.62           O  
ANISOU 1529  O   GLU A 218     1360   1938   1495     75   -211    213
ATOM   1530  CB  GLU A 218      29.921  62.243  45.434  1.00 11.24           C  
ANISOU 1530  CB  GLU A 218     1008   1662   1601    158   -208     50
ATOM   1531  CG  GLU A 218      29.314  63.528  46.038  1.00 12.80           C  
ANISOU 1531  CG  GLU A 218     1330   1753   1780    213   -168     22
ATOM   1532  CD  GLU A 218      30.053  64.059  47.261  1.00 14.95           C  
ANISOU 1532  CD  GLU A 218     1701   1884   2093    215    -45     20
ATOM   1533  OE1 GLU A 218      31.127  63.513  47.588  1.00 20.75           O  
ANISOU 1533  OE1 GLU A 218     2929   2530   2424    379    110    -58
ATOM   1534  OE2 GLU A 218      29.535  65.043  47.830  1.00 21.07           O1-
ANISOU 1534  OE2 GLU A 218     2711   2176   3115     97     63    -33
ATOM   1535  N   GLU A 219      27.588  60.206  45.297  1.00 14.47           N  
ANISOU 1535  N   GLU A 219     1451   2133   1914    120    -99    100
ATOM   1536  CA  GLU A 219      26.326  59.770  45.887  1.00 15.18           C  
ANISOU 1536  CA  GLU A 219     1605   2176   1984    129   -147     71
ATOM   1537  C   GLU A 219      25.806  60.822  46.888  1.00 14.34           C  
ANISOU 1537  C   GLU A 219     1460   2097   1891    190   -223     89
ATOM   1538  O   GLU A 219      26.576  61.298  47.723  1.00 15.45           O  
ANISOU 1538  O   GLU A 219     1619   2186   2062    223   -241    135
ATOM   1539  CB  GLU A 219      26.531  58.382  46.529  1.00 15.69           C  
ANISOU 1539  CB  GLU A 219     1620   2277   2065    110   -138     64
ATOM   1540  CG  GLU A 219      25.252  57.749  47.123  1.00 17.25           C  
ANISOU 1540  CG  GLU A 219     1995   2395   2163    105   -166     90
ATOM   1541  CD  GLU A 219      25.460  56.347  47.698  1.00 19.95           C  
ANISOU 1541  CD  GLU A 219     2220   2773   2584     85    -89     47
ATOM   1542  OE1 GLU A 219      26.620  55.886  47.751  1.00 26.17           O  
ANISOU 1542  OE1 GLU A 219     3210   3613   3119     53    171     92
ATOM   1543  OE2 GLU A 219      24.439  55.745  48.087  1.00 25.89           O1-
ANISOU 1543  OE2 GLU A 219     3299   3540   2995    108   -179     77
ATOM   1544  N   GLY A 220      24.523  61.180  46.769  1.00 14.61           N  
ANISOU 1544  N   GLY A 220     1547   2083   1921    149   -240     60
ATOM   1545  CA  GLY A 220      23.934  62.273  47.545  1.00 14.60           C  
ANISOU 1545  CA  GLY A 220     1631   2021   1892    160   -194    104
ATOM   1546  C   GLY A 220      24.233  63.635  46.894  1.00 14.00           C  
ANISOU 1546  C   GLY A 220     1574   1876   1867    148   -171    147
ATOM   1547  O   GLY A 220      24.184  64.651  47.587  1.00 15.90           O  
ANISOU 1547  O   GLY A 220     1772   2135   2132    228   -203    272
ATOM   1548  N   SER A 221      24.614  63.684  45.602  1.00 12.90           N  
ANISOU 1548  N   SER A 221     1444   1763   1693    124   -183    199
ATOM   1549  CA  SER A 221      24.964  64.905  44.863  1.00 12.14           C  
ANISOU 1549  CA  SER A 221     1406   1672   1531    102   -126     88
ATOM   1550  C   SER A 221      24.413  64.854  43.414  1.00 11.20           C  
ANISOU 1550  C   SER A 221     1293   1605   1357     93   -130    117
ATOM   1551  O   SER A 221      23.668  63.937  43.058  1.00 11.97           O  
ANISOU 1551  O   SER A 221     1476   1757   1313    194   -254    198
ATOM   1552  CB  SER A 221      26.485  65.180  44.981  1.00 11.79           C  
ANISOU 1552  CB  SER A 221     1310   1639   1529     74    -69     85
ATOM   1553  OG  SER A 221      26.848  66.457  44.494  1.00 11.80           O  
ANISOU 1553  OG  SER A 221     1426   1515   1541    125   -146    132
ATOM   1554  N   PHE A 222      24.708  65.896  42.627  1.00 10.14           N  
ANISOU 1554  N   PHE A 222     1216   1375   1261     80   -132    135
ATOM   1555  CA  PHE A 222      23.871  66.423  41.539  1.00 10.13           C  
ANISOU 1555  CA  PHE A 222     1171   1414   1264     20   -114     72
ATOM   1556  C   PHE A 222      23.987  65.714  40.174  1.00  9.32           C  
ANISOU 1556  C   PHE A 222     1004   1348   1189     33   -100     65
ATOM   1557  O   PHE A 222      23.698  66.359  39.162  1.00  8.47           O  
ANISOU 1557  O   PHE A 222      869   1154   1192    -13   -112      0
ATOM   1558  CB  PHE A 222      24.106  67.948  41.349  1.00 10.77           C  
ANISOU 1558  CB  PHE A 222     1293   1460   1337     11    -88     22
ATOM   1559  CG  PHE A 222      24.778  68.694  42.478  1.00 11.71           C  
ANISOU 1559  CG  PHE A 222     1441   1614   1393     33   -150     95
ATOM   1560  CD1 PHE A 222      24.071  69.043  43.643  1.00 14.60           C  
ANISOU 1560  CD1 PHE A 222     2109   1688   1748   -113    -52    112
ATOM   1561  CD2 PHE A 222      26.171  68.886  42.432  1.00 11.82           C  
ANISOU 1561  CD2 PHE A 222     1513   1389   1586    -43   -312    124
ATOM   1562  CE1 PHE A 222      24.754  69.631  44.697  1.00 16.49           C  
ANISOU 1562  CE1 PHE A 222     2475   1801   1987   -153    -77    109
ATOM   1563  CE2 PHE A 222      26.825  69.473  43.501  1.00 13.71           C  
ANISOU 1563  CE2 PHE A 222     1804   1573   1830    -87   -219    -48
ATOM   1564  CZ  PHE A 222      26.116  69.869  44.619  1.00 16.05           C  
ANISOU 1564  CZ  PHE A 222     2322   1745   2028   -140    -78     38
ATOM   1565  N   GLN A 223      24.345  64.420  40.116  1.00  9.36           N  
ANISOU 1565  N   GLN A 223      912   1359   1283    -18   -121     31
ATOM   1566  CA  GLN A 223      24.404  63.674  38.844  1.00  9.80           C  
ANISOU 1566  CA  GLN A 223      970   1436   1317    -52   -146    -12
ATOM   1567  C   GLN A 223      23.119  63.768  38.028  1.00  9.60           C  
ANISOU 1567  C   GLN A 223      927   1426   1291   -118   -170      2
ATOM   1568  O   GLN A 223      23.174  63.947  36.823  1.00  9.01           O  
ANISOU 1568  O   GLN A 223      944   1220   1258   -173   -265    -63
ATOM   1569  CB  GLN A 223      24.785  62.202  39.059  1.00  9.87           C  
ANISOU 1569  CB  GLN A 223      986   1388   1375   -104    -74     31
ATOM   1570  CG  GLN A 223      24.944  61.426  37.757  1.00 10.74           C  
ANISOU 1570  CG  GLN A 223     1208   1431   1441    -83    -73     -5
ATOM   1571  CD  GLN A 223      25.388  59.991  37.936  1.00 11.58           C  
ANISOU 1571  CD  GLN A 223     1207   1631   1561    -71   -148     82
ATOM   1572  OE1 GLN A 223      25.006  59.347  38.901  1.00 14.48           O  
ANISOU 1572  OE1 GLN A 223     1233   1955   2314     85   -126    152
ATOM   1573  NE2 GLN A 223      26.164  59.473  36.983  1.00 13.28           N  
ANISOU 1573  NE2 GLN A 223     1554   1773   1716   -165    -76    106
ATOM   1574  N   GLU A 224      21.955  63.703  38.655  1.00  9.82           N  
ANISOU 1574  N   GLU A 224      948   1476   1305    -37   -185     -8
ATOM   1575  CA  GLU A 224      20.723  63.775  37.866  1.00 10.58           C  
ANISOU 1575  CA  GLU A 224     1124   1563   1333      8   -149    -22
ATOM   1576  C   GLU A 224      20.555  65.141  37.182  1.00  9.59           C  
ANISOU 1576  C   GLU A 224     1062   1370   1209     20   -129      6
ATOM   1577  O   GLU A 224      20.238  65.216  35.987  1.00  9.35           O  
ANISOU 1577  O   GLU A 224     1001   1291   1261     26   -196   -135
ATOM   1578  CB  GLU A 224      19.501  63.416  38.719  1.00 12.60           C  
ANISOU 1578  CB  GLU A 224     1538   1742   1506     57    -60     24
ATOM   1579  CG  GLU A 224      19.493  61.936  39.163  1.00 16.32           C  
ANISOU 1579  CG  GLU A 224     1930   2268   2002     47   -183    -41
ATOM   1580  CD  GLU A 224      19.611  60.929  38.011  1.00 20.46           C  
ANISOU 1580  CD  GLU A 224     2494   2628   2652     55   -139    -19
ATOM   1581  OE1 GLU A 224      18.698  60.894  37.166  1.00 23.68           O  
ANISOU 1581  OE1 GLU A 224     2938   3075   2985     31   -198   -239
ATOM   1582  OE2 GLU A 224      20.608  60.172  37.948  1.00 23.46           O1-
ANISOU 1582  OE2 GLU A 224     2756   2948   3208   -140   -172     -9
ATOM   1583  N   GLN A 225      20.781  66.224  37.939  1.00  9.43           N  
ANISOU 1583  N   GLN A 225     1119   1383   1081     13   -132      0
ATOM   1584  CA  GLN A 225      20.737  67.597  37.445  1.00  9.07           C  
ANISOU 1584  CA  GLN A 225     1073   1261   1110    -13    -80     24
ATOM   1585  C   GLN A 225      21.736  67.824  36.304  1.00  7.91           C  
ANISOU 1585  C   GLN A 225      944   1086    974    -18   -103      4
ATOM   1586  O   GLN A 225      21.379  68.446  35.306  1.00  8.00           O  
ANISOU 1586  O   GLN A 225      933   1095   1012    -59    -77    -11
ATOM   1587  CB  GLN A 225      20.985  68.618  38.579  1.00  9.48           C  
ANISOU 1587  CB  GLN A 225     1199   1250   1152    -41   -110     62
ATOM   1588  CG  GLN A 225      19.869  68.725  39.640  1.00 12.00           C  
ANISOU 1588  CG  GLN A 225     1551   1636   1372      3   -127    166
ATOM   1589  CD  GLN A 225      19.998  67.738  40.803  1.00 14.01           C  
ANISOU 1589  CD  GLN A 225     1893   1900   1527    125    -39    157
ATOM   1590  OE1 GLN A 225      20.556  66.654  40.667  1.00 12.80           O  
ANISOU 1590  OE1 GLN A 225     1664   1735   1463    285   -158    193
ATOM   1591  NE2 GLN A 225      19.470  68.093  41.966  1.00 18.51           N  
ANISOU 1591  NE2 GLN A 225     2536   2212   2284    208    -44    359
ATOM   1592  N   ILE A 226      22.949  67.276  36.451  1.00  6.95           N  
ANISOU 1592  N   ILE A 226      709    963    968    -58   -120    -49
ATOM   1593  CA  ILE A 226      24.012  67.479  35.479  1.00  7.13           C  
ANISOU 1593  CA  ILE A 226      711   1022    974   -111   -102    -30
ATOM   1594  C   ILE A 226      23.730  66.664  34.211  1.00  6.92           C  
ANISOU 1594  C   ILE A 226      663   1074    892   -116    -95    -63
ATOM   1595  O   ILE A 226      23.954  67.153  33.098  1.00  6.94           O  
ANISOU 1595  O   ILE A 226      711    991    934   -179    -61   -145
ATOM   1596  CB  ILE A 226      25.405  67.208  36.089  1.00  6.21           C  
ANISOU 1596  CB  ILE A 226      522    943    893   -203   -139     37
ATOM   1597  CG1 ILE A 226      25.667  68.213  37.226  1.00  6.78           C  
ANISOU 1597  CG1 ILE A 226      669    946    959   -271    -67     39
ATOM   1598  CG2 ILE A 226      26.506  67.304  35.024  1.00  7.47           C  
ANISOU 1598  CG2 ILE A 226      804    954   1077   -173   -125     55
ATOM   1599  CD1 ILE A 226      26.916  67.964  38.029  1.00  7.78           C  
ANISOU 1599  CD1 ILE A 226      920    979   1053   -136    -77   -141
ATOM   1600  N   ASN A 227      23.213  65.438  34.364  1.00  7.58           N  
ANISOU 1600  N   ASN A 227      769   1043   1067    -77   -147    -59
ATOM   1601  CA  ASN A 227      22.792  64.669  33.188  1.00  7.53           C  
ANISOU 1601  CA  ASN A 227      804   1003   1053    -87   -138    -90
ATOM   1602  C   ASN A 227      21.763  65.481  32.373  1.00  7.74           C  
ANISOU 1602  C   ASN A 227      878   1075    987   -142   -167   -122
ATOM   1603  O   ASN A 227      21.830  65.552  31.147  1.00  8.64           O  
ANISOU 1603  O   ASN A 227      970   1168   1143   -190   -161   -201
ATOM   1604  CB  ASN A 227      22.140  63.349  33.591  1.00  8.40           C  
ANISOU 1604  CB  ASN A 227      962   1104   1126   -124   -190   -119
ATOM   1605  CG  ASN A 227      23.137  62.248  34.022  1.00  9.45           C  
ANISOU 1605  CG  ASN A 227      842   1389   1357   -100   -197   -112
ATOM   1606  OD1 ASN A 227      22.697  61.166  34.480  1.00 15.48           O  
ANISOU 1606  OD1 ASN A 227     1305   2380   2195   -364   -448   -231
ATOM   1607  ND2 ASN A 227      24.420  62.460  33.848  1.00  8.53           N  
ANISOU 1607  ND2 ASN A 227      617   1163   1458   -395     15    -56
ATOM   1608  N   TRP A 228      20.795  66.066  33.070  1.00  7.71           N  
ANISOU 1608  N   TRP A 228      932   1046    950   -160   -164   -159
ATOM   1609  CA  TRP A 228      19.738  66.847  32.430  1.00  7.98           C  
ANISOU 1609  CA  TRP A 228     1014   1086    931   -101   -141   -126
ATOM   1610  C   TRP A 228      20.315  68.067  31.717  1.00  7.65           C  
ANISOU 1610  C   TRP A 228      972   1044    890    -57    -77   -116
ATOM   1611  O   TRP A 228      20.005  68.332  30.550  1.00  7.60           O  
ANISOU 1611  O   TRP A 228     1095    939    850    -88   -114    -69
ATOM   1612  CB  TRP A 228      18.680  67.266  33.465  1.00  9.17           C  
ANISOU 1612  CB  TRP A 228     1128   1295   1059   -105   -104   -114
ATOM   1613  CG  TRP A 228      17.438  67.810  32.863  1.00  9.36           C  
ANISOU 1613  CG  TRP A 228     1122   1455    979   -108   -119    -72
ATOM   1614  CD1 TRP A 228      16.274  67.146  32.670  1.00 11.05           C  
ANISOU 1614  CD1 TRP A 228     1245   1727   1226   -235   -139   -163
ATOM   1615  CD2 TRP A 228      17.238  69.136  32.355  1.00  9.34           C  
ANISOU 1615  CD2 TRP A 228     1130   1449    968    -63    -28    -69
ATOM   1616  NE1 TRP A 228      15.355  67.970  32.072  1.00 11.21           N  
ANISOU 1616  NE1 TRP A 228     1352   1801   1103   -180    -73   -173
ATOM   1617  CE2 TRP A 228      15.923  69.198  31.867  1.00 11.50           C  
ANISOU 1617  CE2 TRP A 228     1279   1787   1302   -165     13   -124
ATOM   1618  CE3 TRP A 228      18.044  70.282  32.280  1.00  9.25           C  
ANISOU 1618  CE3 TRP A 228     1062   1331   1122   -204    -77     48
ATOM   1619  CZ2 TRP A 228      15.397  70.350  31.302  1.00 11.74           C  
ANISOU 1619  CZ2 TRP A 228     1375   1861   1224   -151    111   -148
ATOM   1620  CZ3 TRP A 228      17.520  71.418  31.720  1.00 10.29           C  
ANISOU 1620  CZ3 TRP A 228     1181   1475   1253   -198    -47    -49
ATOM   1621  CH2 TRP A 228      16.214  71.442  31.225  1.00 11.42           C  
ANISOU 1621  CH2 TRP A 228     1151   1747   1439   -156     24    -42
ATOM   1622  N   ILE A 229      21.171  68.809  32.415  1.00  6.78           N  
ANISOU 1622  N   ILE A 229      775    940    860    -98   -130    -64
ATOM   1623  CA  ILE A 229      21.784  70.006  31.831  1.00  6.52           C  
ANISOU 1623  CA  ILE A 229      761    890    826    -78    -71    -85
ATOM   1624  C   ILE A 229      22.582  69.613  30.589  1.00  6.36           C  
ANISOU 1624  C   ILE A 229      704    886    823   -124    -93    -83
ATOM   1625  O   ILE A 229      22.469  70.243  29.524  1.00  6.83           O  
ANISOU 1625  O   ILE A 229      826    954    813   -155     18    -89
ATOM   1626  CB  ILE A 229      22.656  70.744  32.861  1.00  6.09           C  
ANISOU 1626  CB  ILE A 229      721    834    758   -119    -46    -63
ATOM   1627  CG1 ILE A 229      21.805  71.359  33.973  1.00  6.22           C  
ANISOU 1627  CG1 ILE A 229      743    877    741    -70    -16    -42
ATOM   1628  CG2 ILE A 229      23.489  71.810  32.179  1.00  6.27           C  
ANISOU 1628  CG2 ILE A 229      550    891    940    -20    -97    -39
ATOM   1629  CD1 ILE A 229      22.577  71.681  35.222  1.00  6.84           C  
ANISOU 1629  CD1 ILE A 229      743    802   1054   -208    -14    -81
ATOM   1630  N   TYR A 230      23.384  68.554  30.720  1.00  6.60           N  
ANISOU 1630  N   TYR A 230      689    933    883    -88    -27    -35
ATOM   1631  CA  TYR A 230      24.214  68.102  29.608  1.00  7.08           C  
ANISOU 1631  CA  TYR A 230      793    965    930    -85     -6    -75
ATOM   1632  C   TYR A 230      23.355  67.844  28.368  1.00  7.05           C  
ANISOU 1632  C   TYR A 230      755    954    971   -150     15    -91
ATOM   1633  O   TYR A 230      23.682  68.234  27.249  1.00  8.35           O  
ANISOU 1633  O   TYR A 230      948   1164   1059    -81     93   -192
ATOM   1634  CB  TYR A 230      24.975  66.828  29.998  1.00  7.21           C  
ANISOU 1634  CB  TYR A 230      732   1032    973    -86    -48    -37
ATOM   1635  CG  TYR A 230      25.726  66.220  28.846  1.00  7.77           C  
ANISOU 1635  CG  TYR A 230      765   1082   1102    -93    104     41
ATOM   1636  CD1 TYR A 230      26.992  66.677  28.482  1.00  9.63           C  
ANISOU 1636  CD1 TYR A 230     1033   1320   1304     59    146     82
ATOM   1637  CD2 TYR A 230      25.172  65.189  28.106  1.00  9.59           C  
ANISOU 1637  CD2 TYR A 230     1315    949   1377    -61    164     62
ATOM   1638  CE1 TYR A 230      27.664  66.128  27.393  1.00 10.48           C  
ANISOU 1638  CE1 TYR A 230     1026   1553   1401    270    207    231
ATOM   1639  CE2 TYR A 230      25.851  64.615  27.023  1.00 11.06           C  
ANISOU 1639  CE2 TYR A 230     1374   1128   1697     36    242     84
ATOM   1640  CZ  TYR A 230      27.085  65.104  26.675  1.00 10.79           C  
ANISOU 1640  CZ  TYR A 230     1264   1164   1670    250    242    298
ATOM   1641  OH  TYR A 230      27.765  64.540  25.602  1.00 13.62           O  
ANISOU 1641  OH  TYR A 230     1689   1347   2136    356    339    461
ATOM   1642  N   SER A 231      22.243  67.160  28.582  1.00  7.85           N  
ANISOU 1642  N   SER A 231      948   1106    925    -47     24   -113
ATOM   1643  CA  SER A 231      21.360  66.770  27.486  1.00  9.00           C  
ANISOU 1643  CA  SER A 231     1152   1114   1150   -106     -5   -145
ATOM   1644  C   SER A 231      20.688  67.976  26.812  1.00  8.48           C  
ANISOU 1644  C   SER A 231     1095   1029   1097    -95     15   -157
ATOM   1645  O   SER A 231      20.296  67.896  25.636  1.00 10.68           O  
ANISOU 1645  O   SER A 231     1516   1085   1456   -200    284   -218
ATOM   1646  CB  SER A 231      20.318  65.771  27.994  1.00 10.44           C  
ANISOU 1646  CB  SER A 231     1334   1375   1257    -81    -15   -145
ATOM   1647  OG  SER A 231      20.944  64.520  28.244  1.00 15.85           O  
ANISOU 1647  OG  SER A 231     1821   2161   2040   -271    -18   -194
ATOM   1648  N   SER A 232      20.545  69.092  27.538  1.00  7.55           N  
ANISOU 1648  N   SER A 232     1015    920    934    -64    -22   -150
ATOM   1649  CA  SER A 232      19.927  70.313  26.979  1.00  7.66           C  
ANISOU 1649  CA  SER A 232     1070    925    914     54     27   -132
ATOM   1650  C   SER A 232      20.864  71.110  26.077  1.00  8.01           C  
ANISOU 1650  C   SER A 232     1083   1003    956     51    -15   -138
ATOM   1651  O   SER A 232      20.423  71.973  25.337  1.00  8.86           O  
ANISOU 1651  O   SER A 232     1177   1205    982     24    -70   -199
ATOM   1652  CB  SER A 232      19.438  71.230  28.111  1.00  8.13           C  
ANISOU 1652  CB  SER A 232     1146    938   1004    -44     -3   -117
ATOM   1653  OG  SER A 232      20.498  71.972  28.698  1.00  8.91           O  
ANISOU 1653  OG  SER A 232     1204   1077   1102   -156     61   -141
ATOM   1654  N   LEU A 233      22.166  70.856  26.193  1.00  7.95           N  
ANISOU 1654  N   LEU A 233     1095   1027    898    207    -26   -140
ATOM   1655  CA  LEU A 233      23.177  71.637  25.491  1.00  8.62           C  
ANISOU 1655  CA  LEU A 233     1173   1151    950    126    -34   -115
ATOM   1656  C   LEU A 233      23.277  71.238  24.036  1.00  8.26           C  
ANISOU 1656  C   LEU A 233      993   1114   1032    125     -4    -89
ATOM   1657  O   LEU A 233      22.847  70.153  23.671  1.00  9.16           O  
ANISOU 1657  O   LEU A 233     1286   1136   1058     47   -178   -157
ATOM   1658  CB  LEU A 233      24.548  71.422  26.134  1.00  9.80           C  
ANISOU 1658  CB  LEU A 233     1242   1397   1081    205    -18   -101
ATOM   1659  CG  LEU A 233      24.682  71.748  27.598  1.00 11.05           C  
ANISOU 1659  CG  LEU A 233     1382   1580   1235    183     -8   -212
ATOM   1660  CD1 LEU A 233      26.115  71.547  28.076  1.00 13.94           C  
ANISOU 1660  CD1 LEU A 233     1954   1969   1373    412    -35   -360
ATOM   1661  CD2 LEU A 233      24.231  73.184  27.778  1.00 11.45           C  
ANISOU 1661  CD2 LEU A 233     1220   1466   1662    -23     52   -632
ATOM   1662  N   PRO A 234      23.872  72.097  23.198  1.00  8.17           N  
ANISOU 1662  N   PRO A 234     1051   1032   1022     99    -63   -103
ATOM   1663  CA  PRO A 234      24.111  71.702  21.808  1.00  9.47           C  
ANISOU 1663  CA  PRO A 234     1258   1221   1116     67     24    -57
ATOM   1664  C   PRO A 234      24.953  70.435  21.684  1.00 10.15           C  
ANISOU 1664  C   PRO A 234     1357   1352   1146     23      3    -30
ATOM   1665  O   PRO A 234      25.782  70.130  22.552  1.00 10.56           O  
ANISOU 1665  O   PRO A 234     1112   1551   1347    112      0    124
ATOM   1666  CB  PRO A 234      24.868  72.902  21.232  1.00  9.19           C  
ANISOU 1666  CB  PRO A 234     1188   1221   1079    144     53    -29
ATOM   1667  CG  PRO A 234      24.410  74.070  22.079  1.00  8.40           C  
ANISOU 1667  CG  PRO A 234      939   1133   1117    204    -35   -115
ATOM   1668  CD  PRO A 234      24.336  73.470  23.463  1.00  7.82           C  
ANISOU 1668  CD  PRO A 234      933   1020   1016    166   -138    -89
ATOM   1669  N   ALA A 235      24.742  69.722  20.582  1.00 12.05           N  
ANISOU 1669  N   ALA A 235     1691   1546   1338   -145     25    -74
ATOM   1670  CA  ALA A 235      25.528  68.528  20.274  1.00 12.53           C  
ANISOU 1670  CA  ALA A 235     1748   1607   1403   -128     56      4
ATOM   1671  C   ALA A 235      27.039  68.788  20.238  1.00 12.61           C  
ANISOU 1671  C   ALA A 235     1795   1559   1437   -100     93    -68
ATOM   1672  O   ALA A 235      27.847  68.007  20.784  1.00 15.45           O  
ANISOU 1672  O   ALA A 235     2022   2116   1730   -174    119     93
ATOM   1673  CB  ALA A 235      25.061  67.918  18.949  1.00 14.56           C  
ANISOU 1673  CB  ALA A 235     2079   1843   1607   -184     15    -59
ATOM   1674  N   SER A 236      27.407  69.888  19.608  1.00 11.29           N  
ANISOU 1674  N   SER A 236     1691   1245   1353    -34     96     -7
ATOM   1675  CA  SER A 236      28.809  70.262  19.404  1.00 11.34           C  
ANISOU 1675  CA  SER A 236     1669   1261   1378     11     91    -71
ATOM   1676  C   SER A 236      29.256  71.195  20.519  1.00 10.36           C  
ANISOU 1676  C   SER A 236     1463   1113   1357     29    126    -93
ATOM   1677  O   SER A 236      28.844  72.349  20.577  1.00 10.74           O  
ANISOU 1677  O   SER A 236     1376   1168   1534    145    235   -196
ATOM   1678  CB  SER A 236      28.982  70.976  18.067  1.00 13.24           C  
ANISOU 1678  CB  SER A 236     1883   1527   1620     72     84   -102
ATOM   1679  OG  SER A 236      30.343  71.245  17.814  1.00 17.24           O  
ANISOU 1679  OG  SER A 236     2569   1937   2042    180   -148     42
ATOM   1680  N   LYS A 237      30.117  70.697  21.394  1.00  8.76           N  
ANISOU 1680  N   LYS A 237     1283    959   1085     11    142    -99
ATOM   1681  CA  LYS A 237      30.616  71.469  22.531  1.00  7.95           C  
ANISOU 1681  CA  LYS A 237     1099    913   1006      1    110    -91
ATOM   1682  C   LYS A 237      31.837  70.778  23.090  1.00  6.61           C  
ANISOU 1682  C   LYS A 237      994    681    836    -29    108    -23
ATOM   1683  O   LYS A 237      32.087  69.606  22.827  1.00  8.30           O  
ANISOU 1683  O   LYS A 237     1279    762   1109   -251    162   -319
ATOM   1684  CB  LYS A 237      29.554  71.593  23.630  1.00  8.48           C  
ANISOU 1684  CB  LYS A 237     1141   1074   1004     14    101   -177
ATOM   1685  CG  LYS A 237      29.127  70.256  24.172  1.00 10.50           C  
ANISOU 1685  CG  LYS A 237     1244   1424   1318     54    -63   -146
ATOM   1686  CD  LYS A 237      27.939  70.275  25.060  1.00 12.05           C  
ANISOU 1686  CD  LYS A 237     1325   1815   1438    103     33    -11
ATOM   1687  CE  LYS A 237      27.422  68.839  25.295  1.00 14.78           C  
ANISOU 1687  CE  LYS A 237     1371   2238   2007     96    -85    -10
ATOM   1688  NZ  LYS A 237      27.000  68.092  24.076  1.00 17.08           N1+
ANISOU 1688  NZ  LYS A 237     1899   2510   2080     49   -146    -16
ATOM   1689  N   GLN A 238      32.573  71.523  23.893  1.00  5.06           N  
ANISOU 1689  N   GLN A 238      769    453    700    -16     20    -10
ATOM   1690  CA  GLN A 238      33.749  71.044  24.617  1.00  5.28           C  
ANISOU 1690  CA  GLN A 238      810    496    699      0     64     44
ATOM   1691  C   GLN A 238      33.413  70.945  26.113  1.00  4.59           C  
ANISOU 1691  C   GLN A 238      704    406    634    -41     29     20
ATOM   1692  O   GLN A 238      32.748  71.832  26.658  1.00  4.78           O  
ANISOU 1692  O   GLN A 238      660    425    730    -64     82    181
ATOM   1693  CB  GLN A 238      34.886  72.027  24.397  1.00  4.66           C  
ANISOU 1693  CB  GLN A 238      802    341    627    -30     -8     32
ATOM   1694  CG  GLN A 238      36.158  71.718  25.186  1.00  5.47           C  
ANISOU 1694  CG  GLN A 238      941    572    564     -9     42     67
ATOM   1695  CD  GLN A 238      37.276  72.706  24.911  1.00  5.45           C  
ANISOU 1695  CD  GLN A 238      836    606    627    -12    -14    144
ATOM   1696  OE1 GLN A 238      37.032  73.798  24.401  1.00  6.85           O  
ANISOU 1696  OE1 GLN A 238      791   1222    587    -98     53    -36
ATOM   1697  NE2 GLN A 238      38.512  72.338  25.260  1.00  6.02           N  
ANISOU 1697  NE2 GLN A 238      901    913    473     63      5     70
ATOM   1698  N   MET A 239      33.895  69.889  26.762  1.00  5.19           N  
ANISOU 1698  N   MET A 239      813    526    632     34    136    131
ATOM   1699  CA  MET A 239      33.708  69.801  28.182  0.50  6.23           C  
ANISOU 1699  CA  MET A 239      823    714    830     29     76    110
ATOM   1700  C   MET A 239      35.036  69.680  28.907  1.00  5.46           C  
ANISOU 1700  C   MET A 239      718    580    774    101    140    153
ATOM   1701  O   MET A 239      35.997  69.054  28.446  1.00  6.51           O  
ANISOU 1701  O   MET A 239      963    583    927    205    307    230
ATOM   1702  CB  MET A 239      32.781  68.644  28.493  0.50  6.69           C  
ANISOU 1702  CB  MET A 239      860    817    864    -33     50    103
ATOM   1703  CG  MET A 239      32.275  68.608  29.898  0.50  8.19           C  
ANISOU 1703  CG  MET A 239      811   1050   1249      8   -105     70
ATOM   1704  SD  MET A 239      31.038  67.325  30.049  0.50  9.53           S  
ANISOU 1704  SD  MET A 239     1171   1199   1248   -172   -186     12
ATOM   1705  CE  MET A 239      30.614  67.527  31.765  0.50 10.39           C  
ANISOU 1705  CE  MET A 239     1467   1337   1142    -90   -104    257
ATOM   1706  N   LEU A 240      35.095  70.338  30.055  1.00  5.12           N  
ANISOU 1706  N   LEU A 240      539    533    871     94    255    211
ATOM   1707  CA  LEU A 240      36.219  70.249  30.961  1.00  5.38           C  
ANISOU 1707  CA  LEU A 240      672    584    787     19    172    192
ATOM   1708  C   LEU A 240      35.702  69.826  32.313  1.00  5.10           C  
ANISOU 1708  C   LEU A 240      642    501    794     80    187    213
ATOM   1709  O   LEU A 240      34.719  70.378  32.797  1.00  7.16           O  
ANISOU 1709  O   LEU A 240      663    823   1235    258    344    546
ATOM   1710  CB  LEU A 240      36.927  71.590  31.163  1.00  6.14           C  
ANISOU 1710  CB  LEU A 240      748    647    938     56    203    161
ATOM   1711  CG  LEU A 240      37.285  72.411  29.936  1.00  6.93           C  
ANISOU 1711  CG  LEU A 240      778    800   1054     75    125    155
ATOM   1712  CD1 LEU A 240      37.913  73.735  30.371  1.00  8.12           C  
ANISOU 1712  CD1 LEU A 240      811   1196   1078     34    -94    126
ATOM   1713  CD2 LEU A 240      38.247  71.659  29.019  1.00  9.00           C  
ANISOU 1713  CD2 LEU A 240     1239    945   1233    163     39    252
ATOM   1714  N   ALA A 241      36.380  68.872  32.929  1.00  4.28           N  
ANISOU 1714  N   ALA A 241      600    332    694     16    141    124
ATOM   1715  CA  ALA A 241      36.072  68.470  34.295  1.00  4.94           C  
ANISOU 1715  CA  ALA A 241      596    503    775     12    116    113
ATOM   1716  C   ALA A 241      37.368  68.537  35.067  1.00  5.23           C  
ANISOU 1716  C   ALA A 241      514    592    880     14    194     76
ATOM   1717  O   ALA A 241      38.367  67.962  34.636  1.00  6.32           O  
ANISOU 1717  O   ALA A 241      880    567    952    -12    446     24
ATOM   1718  CB  ALA A 241      35.495  67.060  34.333  1.00  5.56           C  
ANISOU 1718  CB  ALA A 241      520    655    935     57    -62     90
ATOM   1719  N   VAL A 242      37.366  69.232  36.203  1.00  4.96           N  
ANISOU 1719  N   VAL A 242      548    566    768    -15    130     91
ATOM   1720  CA  VAL A 242      38.547  69.281  37.061  1.00  5.53           C  
ANISOU 1720  CA  VAL A 242      628    571    900      0     75     92
ATOM   1721  C   VAL A 242      38.158  68.724  38.425  1.00  5.49           C  
ANISOU 1721  C   VAL A 242      618    634    832     16     65     59
ATOM   1722  O   VAL A 242      37.028  68.899  38.904  1.00  5.75           O  
ANISOU 1722  O   VAL A 242      706    613    865      8     54     20
ATOM   1723  CB  VAL A 242      39.191  70.696  37.170  1.00  6.17           C  
ANISOU 1723  CB  VAL A 242      652    735    955     50     43     59
ATOM   1724  CG1 VAL A 242      39.403  71.341  35.784  1.00  7.23           C  
ANISOU 1724  CG1 VAL A 242      525    809   1413     92    -56    238
ATOM   1725  CG2 VAL A 242      38.481  71.706  38.090  1.00  8.24           C  
ANISOU 1725  CG2 VAL A 242     1062    825   1243   -138     -6    212
ATOM   1726  N   SER A 243      39.084  67.995  39.043  1.00  5.75           N  
ANISOU 1726  N   SER A 243      660    684    838     62     53     33
ATOM   1727  CA  SER A 243      38.820  67.287  40.284  1.00  5.80           C  
ANISOU 1727  CA  SER A 243      701    606    897     68     19    -38
ATOM   1728  C   SER A 243      40.145  67.113  41.030  1.00  5.75           C  
ANISOU 1728  C   SER A 243      696    616    872     52     -5    -48
ATOM   1729  O   SER A 243      41.200  67.071  40.392  1.00  6.91           O  
ANISOU 1729  O   SER A 243      884    693   1048    196     70    -34
ATOM   1730  CB  SER A 243      38.131  65.949  39.926  1.00  5.95           C  
ANISOU 1730  CB  SER A 243      634    686    937     31    -14   -139
ATOM   1731  OG  SER A 243      37.476  65.380  41.036  1.00  8.55           O  
ANISOU 1731  OG  SER A 243     1058    863   1327     55    -78   -143
ATOM   1732  N   ALA A 244      40.094  67.023  42.365  1.00  6.19           N  
ANISOU 1732  N   ALA A 244      731    647    972     99    -51    -64
ATOM   1733  CA  ALA A 244      41.273  66.667  43.153  1.00  6.38           C  
ANISOU 1733  CA  ALA A 244      690    709   1024     10     26   -132
ATOM   1734  C   ALA A 244      41.537  65.159  43.055  1.00  7.00           C  
ANISOU 1734  C   ALA A 244      709    820   1130      9     15   -152
ATOM   1735  O   ALA A 244      42.641  64.737  42.701  1.00  8.43           O  
ANISOU 1735  O   ALA A 244      820   1141   1242   -107     76   -143
ATOM   1736  CB  ALA A 244      41.128  67.131  44.609  1.00  7.37           C  
ANISOU 1736  CB  ALA A 244      794    633   1370     60      5   -101
ATOM   1737  N   THR A 245      40.489  64.378  43.338  1.00  6.84           N  
ANISOU 1737  N   THR A 245      582    905   1112    -93     39   -199
ATOM   1738  CA  THR A 245      40.533  62.926  43.330  1.00  6.50           C  
ANISOU 1738  CA  THR A 245      555    799   1115    -26     36   -171
ATOM   1739  C   THR A 245      39.737  62.399  42.120  1.00  6.72           C  
ANISOU 1739  C   THR A 245      633    805   1113    -27     60   -193
ATOM   1740  O   THR A 245      38.880  63.113  41.588  1.00  7.28           O  
ANISOU 1740  O   THR A 245      553    829   1384   -144    137   -265
ATOM   1741  CB  THR A 245      39.979  62.348  44.670  1.00  6.88           C  
ANISOU 1741  CB  THR A 245      631    795   1186     42     67   -160
ATOM   1742  OG1 THR A 245      38.582  62.134  44.721  1.00  8.07           O  
ANISOU 1742  OG1 THR A 245      928    747   1390      7    -47   -114
ATOM   1743  CG2 THR A 245      40.398  63.146  45.916  1.00  9.04           C  
ANISOU 1743  CG2 THR A 245      949    937   1548    185     27   -323
ATOM   1744  N   TYR A 246      40.037  61.171  41.693  1.00  7.14           N  
ANISOU 1744  N   TYR A 246      729    821   1162    -71     60   -176
ATOM   1745  CA  TYR A 246      39.337  60.497  40.603  1.00  6.97           C  
ANISOU 1745  CA  TYR A 246      755    795   1098    -67     10   -155
ATOM   1746  C   TYR A 246      39.060  59.036  41.023  1.00  7.24           C  
ANISOU 1746  C   TYR A 246      833    784   1132   -106      8   -120
ATOM   1747  O   TYR A 246      39.917  58.178  40.791  1.00  7.85           O  
ANISOU 1747  O   TYR A 246      907    875   1200   -273     30     -3
ATOM   1748  CB  TYR A 246      40.164  60.666  39.313  1.00  7.08           C  
ANISOU 1748  CB  TYR A 246      720    882   1089    -17      7   -152
ATOM   1749  CG  TYR A 246      39.548  60.130  38.033  1.00  6.73           C  
ANISOU 1749  CG  TYR A 246      708    759   1091   -172     -7   -136
ATOM   1750  CD1 TYR A 246      38.748  60.963  37.223  1.00  6.99           C  
ANISOU 1750  CD1 TYR A 246      595    867   1191    -59     -5    -57
ATOM   1751  CD2 TYR A 246      39.812  58.809  37.621  1.00  6.63           C  
ANISOU 1751  CD2 TYR A 246      600    888   1031    -42     29    -31
ATOM   1752  CE1 TYR A 246      38.233  60.478  36.006  1.00  7.01           C  
ANISOU 1752  CE1 TYR A 246      634    887   1140     59     19     20
ATOM   1753  CE2 TYR A 246      39.339  58.342  36.382  1.00  7.21           C  
ANISOU 1753  CE2 TYR A 246      834    770   1132   -108     36    -70
ATOM   1754  CZ  TYR A 246      38.550  59.179  35.572  1.00  7.17           C  
ANISOU 1754  CZ  TYR A 246      619    941   1160     26    -85    -83
ATOM   1755  OH  TYR A 246      38.100  58.736  34.364  1.00  7.60           O  
ANISOU 1755  OH  TYR A 246      731    876   1278     23     63    -65
ATOM   1756  N   PRO A 247      37.917  58.794  41.708  1.00  7.38           N  
ANISOU 1756  N   PRO A 247      822    809   1173    -82    -78   -145
ATOM   1757  CA  PRO A 247      37.432  57.436  42.026  1.00  7.81           C  
ANISOU 1757  CA  PRO A 247      888    872   1208    -32    -98   -152
ATOM   1758  C   PRO A 247      36.599  56.827  40.878  1.00  7.12           C  
ANISOU 1758  C   PRO A 247      763    766   1174    -77   -111   -175
ATOM   1759  O   PRO A 247      36.314  57.525  39.899  1.00  6.86           O  
ANISOU 1759  O   PRO A 247      632    777   1195   -136   -120   -195
ATOM   1760  CB  PRO A 247      36.582  57.681  43.283  1.00  8.63           C  
ANISOU 1760  CB  PRO A 247     1045    938   1295    -40   -179   -181
ATOM   1761  CG  PRO A 247      35.989  59.066  43.080  1.00 10.80           C  
ANISOU 1761  CG  PRO A 247     1433   1131   1538   -166   -169    -41
ATOM   1762  CD  PRO A 247      37.070  59.821  42.326  1.00  7.94           C  
ANISOU 1762  CD  PRO A 247      932    849   1233     62    -69    -92
ATOM   1763  N   GLU A 248      36.175  55.552  41.030  1.00  6.84           N  
ANISOU 1763  N   GLU A 248      646    773   1180    -20   -136   -154
ATOM   1764  CA  GLU A 248      35.401  54.860  40.005  1.00  7.16           C  
ANISOU 1764  CA  GLU A 248      721    821   1177    -29   -139   -115
ATOM   1765  C   GLU A 248      34.081  55.570  39.717  1.00  6.63           C  
ANISOU 1765  C   GLU A 248      631    738   1150    -85   -150   -107
ATOM   1766  O   GLU A 248      33.660  55.656  38.564  1.00  6.57           O  
ANISOU 1766  O   GLU A 248      596    606   1291   -103   -160   -145
ATOM   1767  CB  GLU A 248      35.131  53.404  40.410  1.00  7.12           C  
ANISOU 1767  CB  GLU A 248      681    908   1114      6    -51   -140
ATOM   1768  CG  GLU A 248      34.483  52.641  39.261  1.00  7.81           C  
ANISOU 1768  CG  GLU A 248      761    863   1343    105   -173   -142
ATOM   1769  CD  GLU A 248      34.134  51.207  39.548  1.00  8.74           C  
ANISOU 1769  CD  GLU A 248      901    892   1528    -69   -188    -82
ATOM   1770  OE1 GLU A 248      34.633  50.668  40.564  1.00 11.01           O  
ANISOU 1770  OE1 GLU A 248      761   1220   2203   -121   -294   -292
ATOM   1771  OE2 GLU A 248      33.388  50.633  38.724  1.00  7.97           O1-
ANISOU 1771  OE2 GLU A 248      833    772   1424   -157   -336     94
ATOM   1772  N   PHE A 249      33.389  56.087  40.749  1.00  6.87           N  
ANISOU 1772  N   PHE A 249      758    685   1164    -86   -173    -87
ATOM   1773  CA  PHE A 249      32.087  56.738  40.532  1.00  7.09           C  
ANISOU 1773  CA  PHE A 249      752    767   1173    -65   -133    -90
ATOM   1774  C   PHE A 249      32.187  57.927  39.561  1.00  7.06           C  
ANISOU 1774  C   PHE A 249      790    755   1136    -27   -119    -98
ATOM   1775  O   PHE A 249      31.260  58.158  38.785  1.00  6.41           O  
ANISOU 1775  O   PHE A 249      768    640   1027   -144   -131   -204
ATOM   1776  CB  PHE A 249      31.374  57.090  41.858  1.00  8.97           C  
ANISOU 1776  CB  PHE A 249     1036    951   1419     22    -98     -5
ATOM   1777  CG  PHE A 249      31.952  58.192  42.737  1.00  9.17           C  
ANISOU 1777  CG  PHE A 249     1086    989   1409    -49    -39     37
ATOM   1778  CD1 PHE A 249      31.829  59.550  42.366  1.00 10.34           C  
ANISOU 1778  CD1 PHE A 249     1316   1062   1549    -75    144    -33
ATOM   1779  CD2 PHE A 249      32.660  57.867  43.914  1.00 10.18           C  
ANISOU 1779  CD2 PHE A 249     1180   1078   1610   -115     69      5
ATOM   1780  CE1 PHE A 249      32.373  60.542  43.167  1.00 10.36           C  
ANISOU 1780  CE1 PHE A 249     1211   1059   1665    -81    -52     12
ATOM   1781  CE2 PHE A 249      33.161  58.880  44.723  1.00 11.10           C  
ANISOU 1781  CE2 PHE A 249     1477   1123   1614    -33     28   -158
ATOM   1782  CZ  PHE A 249      33.020  60.211  44.350  1.00 11.70           C  
ANISOU 1782  CZ  PHE A 249     1481   1252   1710   -154     83    -94
ATOM   1783  N   LEU A 250      33.347  58.599  39.569  1.00  6.18           N  
ANISOU 1783  N   LEU A 250      587    710   1048     -2    -36   -167
ATOM   1784  CA  LEU A 250      33.563  59.765  38.714  1.00  6.30           C  
ANISOU 1784  CA  LEU A 250      631    698   1064    -95    -74   -143
ATOM   1785  C   LEU A 250      33.982  59.311  37.320  1.00  5.81           C  
ANISOU 1785  C   LEU A 250      565    667    973   -101    -41    -83
ATOM   1786  O   LEU A 250      33.482  59.845  36.319  1.00  6.59           O  
ANISOU 1786  O   LEU A 250      551    676   1277   -136     18   -102
ATOM   1787  CB  LEU A 250      34.589  60.715  39.333  1.00  6.86           C  
ANISOU 1787  CB  LEU A 250      779    685   1142   -120    -44   -142
ATOM   1788  CG  LEU A 250      34.904  62.006  38.545  1.00  6.06           C  
ANISOU 1788  CG  LEU A 250      653    664    984    -74    -40   -138
ATOM   1789  CD1 LEU A 250      33.641  62.842  38.317  1.00  7.19           C  
ANISOU 1789  CD1 LEU A 250      775    881   1075   -171     89     96
ATOM   1790  CD2 LEU A 250      35.991  62.842  39.246  1.00  6.45           C  
ANISOU 1790  CD2 LEU A 250      691    749   1008   -299    -14   -237
ATOM   1791  N   ALA A 251      34.914  58.361  37.239  1.00  5.71           N  
ANISOU 1791  N   ALA A 251      574    594   1000   -106      1   -103
ATOM   1792  CA  ALA A 251      35.282  57.782  35.946  1.00  5.43           C  
ANISOU 1792  CA  ALA A 251      593    605    863    -87    -55    -61
ATOM   1793  C   ALA A 251      34.018  57.339  35.212  1.00  5.17           C  
ANISOU 1793  C   ALA A 251      616    496    851    -81    -11    -29
ATOM   1794  O   ALA A 251      33.831  57.628  34.033  1.00  5.35           O  
ANISOU 1794  O   ALA A 251      488    579    963      2   -118    -13
ATOM   1795  CB  ALA A 251      36.227  56.605  36.139  1.00  6.50           C  
ANISOU 1795  CB  ALA A 251      636    837    993   -121     -3      5
ATOM   1796  N   ASN A 252      33.155  56.614  35.912  1.00  5.26           N  
ANISOU 1796  N   ASN A 252      691    409    896    -16    -44     20
ATOM   1797  CA  ASN A 252      31.942  56.072  35.295  1.00  4.88           C  
ANISOU 1797  CA  ASN A 252      558    447    846   -104    -43     26
ATOM   1798  C   ASN A 252      30.975  57.198  34.902  1.00  4.90           C  
ANISOU 1798  C   ASN A 252      550    436    876   -175     -8     -2
ATOM   1799  O   ASN A 252      30.467  57.224  33.780  1.00  5.49           O  
ANISOU 1799  O   ASN A 252      614    432   1038    -59    -17    -20
ATOM   1800  CB  ASN A 252      31.259  55.089  36.239  1.00  4.98           C  
ANISOU 1800  CB  ASN A 252      685    315    890    -58    -82     87
ATOM   1801  CG  ASN A 252      32.040  53.807  36.402  1.00  4.90           C  
ANISOU 1801  CG  ASN A 252      686    311    861    -42    -51     -2
ATOM   1802  OD1 ASN A 252      33.057  53.595  35.759  1.00  5.49           O  
ANISOU 1802  OD1 ASN A 252      569    583    931    -97      4     16
ATOM   1803  ND2 ASN A 252      31.552  52.935  37.272  1.00  7.13           N  
ANISOU 1803  ND2 ASN A 252      786    716   1205    -30   -179     17
ATOM   1804  N   ALA A 253      30.780  58.179  35.782  1.00  5.82           N  
ANISOU 1804  N   ALA A 253      683    473   1053   -157     32    -26
ATOM   1805  CA  ALA A 253      29.851  59.257  35.469  1.00  5.70           C  
ANISOU 1805  CA  ALA A 253      656    569    938    -20     53     53
ATOM   1806  C   ALA A 253      30.255  60.062  34.236  1.00  5.88           C  
ANISOU 1806  C   ALA A 253      527    665   1039    -72     42      2
ATOM   1807  O   ALA A 253      29.402  60.477  33.421  1.00  6.34           O  
ANISOU 1807  O   ALA A 253      553    845   1011   -184    106     45
ATOM   1808  CB  ALA A 253      29.685  60.167  36.666  1.00  7.42           C  
ANISOU 1808  CB  ALA A 253      823    734   1262   -168     38     69
ATOM   1809  N   LEU A 254      31.552  60.316  34.097  1.00  5.62           N  
ANISOU 1809  N   LEU A 254      432    696   1005    -30    114    -17
ATOM   1810  CA  LEU A 254      32.014  61.183  33.017  1.00  5.90           C  
ANISOU 1810  CA  LEU A 254      509    681   1052    -54     38     42
ATOM   1811  C   LEU A 254      31.934  60.511  31.648  1.00  5.90           C  
ANISOU 1811  C   LEU A 254      405    710   1127   -106    -37    -66
ATOM   1812  O   LEU A 254      32.025  61.201  30.620  1.00  6.66           O  
ANISOU 1812  O   LEU A 254      406    880   1242    -24   -104     37
ATOM   1813  CB  LEU A 254      33.421  61.709  33.293  1.00  6.22           C  
ANISOU 1813  CB  LEU A 254      479    743   1139    -59      0     54
ATOM   1814  CG  LEU A 254      33.541  62.657  34.489  1.00  6.24           C  
ANISOU 1814  CG  LEU A 254      522    740   1106   -142    -26     59
ATOM   1815  CD1 LEU A 254      35.017  63.050  34.682  1.00  7.82           C  
ANISOU 1815  CD1 LEU A 254      953    908   1110   -239      9     59
ATOM   1816  CD2 LEU A 254      32.697  63.932  34.311  1.00  7.60           C  
ANISOU 1816  CD2 LEU A 254      611   1042   1233   -331     84     31
ATOM   1817  N   THR A 255      31.758  59.188  31.604  1.00  6.07           N  
ANISOU 1817  N   THR A 255      396    759   1149   -157    -34    -52
ATOM   1818  CA  THR A 255      31.534  58.535  30.316  1.00  6.43           C  
ANISOU 1818  CA  THR A 255      539    779   1122    -36    -19    -61
ATOM   1819  C   THR A 255      30.232  58.978  29.633  1.00  6.49           C  
ANISOU 1819  C   THR A 255      484    787   1194    -89      8    -48
ATOM   1820  O   THR A 255      30.074  58.798  28.428  1.00  7.74           O  
ANISOU 1820  O   THR A 255      748    808   1382    -12    190      0
ATOM   1821  CB  THR A 255      31.520  56.989  30.412  1.00  5.70           C  
ANISOU 1821  CB  THR A 255      489    625   1050    -41    -16    -13
ATOM   1822  OG1 THR A 255      30.363  56.541  31.124  1.00  6.00           O  
ANISOU 1822  OG1 THR A 255      511    692   1075    -55   -101    110
ATOM   1823  CG2 THR A 255      32.819  56.434  31.008  1.00  5.81           C  
ANISOU 1823  CG2 THR A 255      390    803   1011    -51     49     -5
ATOM   1824  N   LYS A 256      29.297  59.548  30.381  1.00  6.98           N  
ANISOU 1824  N   LYS A 256      641    899   1110     37      5    -30
ATOM   1825  CA  LYS A 256      28.066  60.066  29.801  1.00  8.04           C  
ANISOU 1825  CA  LYS A 256      834   1043   1175    -29     35     -4
ATOM   1826  C   LYS A 256      28.345  61.300  28.949  1.00  7.71           C  
ANISOU 1826  C   LYS A 256      763    944   1222    -10     86    -56
ATOM   1827  O   LYS A 256      27.596  61.607  28.008  1.00  9.51           O  
ANISOU 1827  O   LYS A 256      924   1241   1446     -9    141   -233
ATOM   1828  CB  LYS A 256      27.087  60.422  30.913  1.00  9.44           C  
ANISOU 1828  CB  LYS A 256     1041   1193   1351    -26     -9     44
ATOM   1829  CG  LYS A 256      25.698  60.831  30.446  1.00 12.17           C  
ANISOU 1829  CG  LYS A 256     1403   1590   1628     -7     68     45
ATOM   1830  CD  LYS A 256      24.939  59.635  29.939  1.00 17.41           C  
ANISOU 1830  CD  LYS A 256     2216   2167   2231   -127      1    -70
ATOM   1831  CE  LYS A 256      23.485  59.602  30.317  1.00 20.99           C  
ANISOU 1831  CE  LYS A 256     2741   2643   2588    -59    -25     32
ATOM   1832  NZ  LYS A 256      23.032  58.184  30.330  1.00 22.75           N1+
ANISOU 1832  NZ  LYS A 256     2810   2952   2880   -153    -39     13
ATOM   1833  N   TYR A 257      29.408  62.025  29.291  1.00  6.88           N  
ANISOU 1833  N   TYR A 257      614    925   1073    103     87      4
ATOM   1834  CA  TYR A 257      29.625  63.364  28.753  1.00  7.04           C  
ANISOU 1834  CA  TYR A 257      647    976   1051    -34     85    -32
ATOM   1835  C   TYR A 257      30.807  63.483  27.808  1.00  7.05           C  
ANISOU 1835  C   TYR A 257      699    877   1102    -39     63      3
ATOM   1836  O   TYR A 257      30.849  64.417  26.994  1.00  9.26           O  
ANISOU 1836  O   TYR A 257      829   1268   1421    -58     25    140
ATOM   1837  CB  TYR A 257      29.877  64.372  29.877  1.00  7.95           C  
ANISOU 1837  CB  TYR A 257      824   1013   1182    -59    171     -4
ATOM   1838  CG  TYR A 257      28.951  64.282  31.056  1.00  7.52           C  
ANISOU 1838  CG  TYR A 257      835    904   1117   -104    226     37
ATOM   1839  CD1 TYR A 257      27.576  64.091  30.896  1.00  8.15           C  
ANISOU 1839  CD1 TYR A 257      916    962   1219   -145    114    -35
ATOM   1840  CD2 TYR A 257      29.445  64.404  32.356  1.00  8.49           C  
ANISOU 1840  CD2 TYR A 257      996   1002   1225   -131    245    119
ATOM   1841  CE1 TYR A 257      26.729  64.028  32.000  1.00  8.62           C  
ANISOU 1841  CE1 TYR A 257      896   1224   1154   -181    257    106
ATOM   1842  CE2 TYR A 257      28.609  64.339  33.455  1.00  9.34           C  
ANISOU 1842  CE2 TYR A 257     1172   1133   1244     47    276     44
ATOM   1843  CZ  TYR A 257      27.264  64.130  33.284  1.00  8.76           C  
ANISOU 1843  CZ  TYR A 257     1106   1042   1178   -107    143    195
ATOM   1844  OH  TYR A 257      26.487  64.071  34.413  1.00  9.50           O  
ANISOU 1844  OH  TYR A 257     1206    932   1469    -73     99    107
ATOM   1845  N   MET A 258      31.783  62.579  27.925  1.00  6.50           N  
ANISOU 1845  N   MET A 258      695    824    951    -50     20     -7
ATOM   1846  CA  MET A 258      33.032  62.680  27.158  1.00  7.86           C  
ANISOU 1846  CA  MET A 258      939    961   1084    -92     18   -104
ATOM   1847  C   MET A 258      33.326  61.344  26.509  1.00  7.76           C  
ANISOU 1847  C   MET A 258      862    943   1143    -70     14    -39
ATOM   1848  O   MET A 258      33.582  60.357  27.202  1.00  8.10           O  
ANISOU 1848  O   MET A 258      856    965   1253   -110    -54    -53
ATOM   1849  CB  MET A 258      34.188  63.054  28.073  1.00  7.85           C  
ANISOU 1849  CB  MET A 258      885    996   1099   -102    -56   -104
ATOM   1850  CG  MET A 258      34.013  64.351  28.834  1.00  8.82           C  
ANISOU 1850  CG  MET A 258     1324    870   1157   -236   -159   -169
ATOM   1851  SD  MET A 258      35.394  64.551  30.010  1.00 12.08           S  
ANISOU 1851  SD  MET A 258     2020   1126   1441   -463    102   -255
ATOM   1852  CE  MET A 258      35.058  66.163  30.722  1.00 11.20           C  
ANISOU 1852  CE  MET A 258     1293   1265   1696   -190   -212   -102
ATOM   1853  N   ARG A 259      33.344  61.335  25.190  1.00  9.05           N  
ANISOU 1853  N   ARG A 259      956   1118   1361   -152     41    -40
ATOM   1854  CA  ARG A 259      33.549  60.102  24.445  1.00 10.56           C  
ANISOU 1854  CA  ARG A 259     1371   1135   1505   -116     35    -52
ATOM   1855  C   ARG A 259      34.953  59.551  24.585  1.00  9.88           C  
ANISOU 1855  C   ARG A 259     1219   1036   1499    -58     81    -94
ATOM   1856  O   ARG A 259      35.123  58.329  24.690  1.00 11.14           O  
ANISOU 1856  O   ARG A 259     1313   1288   1631   -292     87   -298
ATOM   1857  CB  ARG A 259      33.260  60.342  22.957  1.00 11.55           C  
ANISOU 1857  CB  ARG A 259     1489   1334   1565    -47    116     -5
ATOM   1858  CG  ARG A 259      33.287  59.096  22.109  1.00 14.76           C  
ANISOU 1858  CG  ARG A 259     1870   1688   2050   -101     19    -49
ATOM   1859  CD  ARG A 259      32.992  59.424  20.664  1.00 17.94           C  
ANISOU 1859  CD  ARG A 259     2344   1937   2533     20     74    -85
ATOM   1860  NE  ARG A 259      34.021  60.309  20.133  1.00 23.88           N  
ANISOU 1860  NE  ARG A 259     3107   2942   3022     -5   -136    -15
ATOM   1861  CZ  ARG A 259      35.249  59.923  19.786  1.00 25.71           C  
ANISOU 1861  CZ  ARG A 259     3282   3266   3220    -16    -25     70
ATOM   1862  NH1 ARG A 259      35.620  58.646  19.871  1.00 27.02           N  
ANISOU 1862  NH1 ARG A 259     3335   3463   3466    -28    -54     53
ATOM   1863  NH2 ARG A 259      36.113  60.823  19.335  1.00 27.08           N1+
ANISOU 1863  NH2 ARG A 259     3423   3545   3319    -54   -112     60
ATOM   1864  N   ASP A 260      35.957  60.421  24.546  1.00  9.94           N  
ANISOU 1864  N   ASP A 260     1382    875   1517    -78     45    -43
ATOM   1865  CA  ASP A 260      37.351  59.981  24.573  1.00 10.08           C  
ANISOU 1865  CA  ASP A 260     1415    968   1446    -29      0      4
ATOM   1866  C   ASP A 260      38.212  61.090  25.155  1.00  9.29           C  
ANISOU 1866  C   ASP A 260     1249   1008   1270      2     -7     21
ATOM   1867  O   ASP A 260      38.974  61.764  24.449  1.00 10.66           O  
ANISOU 1867  O   ASP A 260     1518   1113   1417     31   -106     72
ATOM   1868  CB  ASP A 260      37.830  59.605  23.163  1.00 11.92           C  
ANISOU 1868  CB  ASP A 260     1718   1087   1723    -34    -45    -25
ATOM   1869  CG  ASP A 260      39.252  59.022  23.148  1.00 13.70           C  
ANISOU 1869  CG  ASP A 260     1910   1397   1897      4     69     28
ATOM   1870  OD1 ASP A 260      39.701  58.464  24.175  1.00 18.80           O  
ANISOU 1870  OD1 ASP A 260     2573   2045   2525    -40    329     -6
ATOM   1871  OD2 ASP A 260      39.895  59.069  22.075  1.00 20.58           O1-
ANISOU 1871  OD2 ASP A 260     2889   2391   2537    -17    -25    259
ATOM   1872  N   PRO A 261      38.051  61.328  26.451  1.00  8.24           N  
ANISOU 1872  N   PRO A 261     1179    856   1094    -10    -20      0
ATOM   1873  CA  PRO A 261      38.725  62.479  27.059  1.00  7.86           C  
ANISOU 1873  CA  PRO A 261     1080    852   1053    -54     27     32
ATOM   1874  C   PRO A 261      40.236  62.365  27.093  1.00  7.05           C  
ANISOU 1874  C   PRO A 261      960    687   1031    -87     53     49
ATOM   1875  O   PRO A 261      40.783  61.245  27.135  1.00  8.80           O  
ANISOU 1875  O   PRO A 261     1018   1050   1274   -223    105    122
ATOM   1876  CB  PRO A 261      38.171  62.488  28.488  1.00  8.89           C  
ANISOU 1876  CB  PRO A 261     1340    916   1120    -88     41      0
ATOM   1877  CG  PRO A 261      37.774  61.081  28.753  1.00  9.12           C  
ANISOU 1877  CG  PRO A 261     1264   1131   1070     83    -27    -10
ATOM   1878  CD  PRO A 261      37.252  60.572  27.437  1.00  8.33           C  
ANISOU 1878  CD  PRO A 261     1089    941   1133    -58      0     78
ATOM   1879  N   THR A 262      40.889  63.521  27.096  1.00  6.70           N  
ANISOU 1879  N   THR A 262     1003    553    988    -26     37     97
ATOM   1880  CA  THR A 262      42.307  63.615  27.384  1.00  6.82           C  
ANISOU 1880  CA  THR A 262     1026    608    955     11     78    113
ATOM   1881  C   THR A 262      42.492  63.894  28.875  1.00  6.58           C  
ANISOU 1881  C   THR A 262      935    616    948    -33    109    120
ATOM   1882  O   THR A 262      41.849  64.787  29.435  1.00  7.13           O  
ANISOU 1882  O   THR A 262     1036    640   1034    -41    333    224
ATOM   1883  CB  THR A 262      42.940  64.727  26.542  1.00  7.22           C  
ANISOU 1883  CB  THR A 262     1023    682   1036    111     31     42
ATOM   1884  OG1 THR A 262      42.814  64.372  25.155  1.00  8.66           O  
ANISOU 1884  OG1 THR A 262     1367    603   1319    207   -143    113
ATOM   1885  CG2 THR A 262      44.408  64.924  26.866  1.00  9.23           C  
ANISOU 1885  CG2 THR A 262     1395   1000   1109     95    -91     43
ATOM   1886  N   PHE A 263      43.352  63.103  29.503  1.00  7.42           N  
ANISOU 1886  N   PHE A 263     1063    783    971     56    151    248
ATOM   1887  CA  PHE A 263      43.650  63.224  30.928  1.00  7.67           C  
ANISOU 1887  CA  PHE A 263     1021    891   1002     68    171    134
ATOM   1888  C   PHE A 263      44.867  64.082  31.135  1.00  8.45           C  
ANISOU 1888  C   PHE A 263     1192    987   1030    102    133    138
ATOM   1889  O   PHE A 263      45.864  63.944  30.410  1.00  9.51           O  
ANISOU 1889  O   PHE A 263     1613    971   1030    177    169    187
ATOM   1890  CB  PHE A 263      43.867  61.836  31.546  1.00  7.71           C  
ANISOU 1890  CB  PHE A 263      910    888   1132    135    224    166
ATOM   1891  CG  PHE A 263      42.623  61.038  31.593  1.00  7.98           C  
ANISOU 1891  CG  PHE A 263      719   1118   1193     43    155    163
ATOM   1892  CD1 PHE A 263      41.832  61.007  32.741  1.00  8.74           C  
ANISOU 1892  CD1 PHE A 263      877   1058   1383     -4    168    110
ATOM   1893  CD2 PHE A 263      42.209  60.314  30.489  1.00  8.99           C  
ANISOU 1893  CD2 PHE A 263      987   1137   1291   -104    168    195
ATOM   1894  CE1 PHE A 263      40.648  60.272  32.762  1.00  8.59           C  
ANISOU 1894  CE1 PHE A 263      647   1178   1437     13     90    222
ATOM   1895  CE2 PHE A 263      41.034  59.602  30.511  1.00  9.80           C  
ANISOU 1895  CE2 PHE A 263      850   1334   1538     17    145     74
ATOM   1896  CZ  PHE A 263      40.253  59.583  31.653  1.00  9.08           C  
ANISOU 1896  CZ  PHE A 263      723   1319   1408    -95    115     81
ATOM   1897  N   VAL A 264      44.804  64.963  32.134  1.00  7.91           N  
ANISOU 1897  N   VAL A 264     1106    920    979    157    151    151
ATOM   1898  CA  VAL A 264      45.943  65.713  32.647  1.00  8.90           C  
ANISOU 1898  CA  VAL A 264     1171   1130   1078    107     98    150
ATOM   1899  C   VAL A 264      46.010  65.339  34.136  1.00  8.85           C  
ANISOU 1899  C   VAL A 264     1187   1144   1029    122     95    141
ATOM   1900  O   VAL A 264      45.272  65.897  34.948  1.00  8.17           O  
ANISOU 1900  O   VAL A 264     1181    871   1050    201    195    120
ATOM   1901  CB  VAL A 264      45.767  67.250  32.463  1.00  9.20           C  
ANISOU 1901  CB  VAL A 264     1223   1144   1126    154     45    183
ATOM   1902  CG1 VAL A 264      46.929  68.070  33.066  1.00 12.02           C  
ANISOU 1902  CG1 VAL A 264     1548   1537   1481    -30     -6     54
ATOM   1903  CG2 VAL A 264      45.587  67.623  30.978  1.00 11.24           C  
ANISOU 1903  CG2 VAL A 264     1412   1320   1538    245     51    146
ATOM   1904  N   ARG A 265      46.809  64.316  34.444  1.00  9.48           N  
ANISOU 1904  N   ARG A 265     1203   1356   1042     81     87    133
ATOM   1905  CA  ARG A 265      46.919  63.736  35.773  1.00 10.26           C  
ANISOU 1905  CA  ARG A 265     1286   1379   1232     25     73     23
ATOM   1906  C   ARG A 265      48.250  64.161  36.399  1.00 11.10           C  
ANISOU 1906  C   ARG A 265     1335   1588   1293     68     86      8
ATOM   1907  O   ARG A 265      49.279  64.205  35.724  1.00 12.99           O  
ANISOU 1907  O   ARG A 265     1763   1834   1337    234     79   -138
ATOM   1908  CB  ARG A 265      46.861  62.202  35.651  1.00  9.59           C  
ANISOU 1908  CB  ARG A 265     1195   1255   1192     64     16      5
ATOM   1909  CG  ARG A 265      45.450  61.601  35.599  1.00  9.18           C  
ANISOU 1909  CG  ARG A 265     1176   1139   1173    -51     -1    -54
ATOM   1910  CD  ARG A 265      45.536  60.080  35.409  1.00 10.88           C  
ANISOU 1910  CD  ARG A 265     1325   1468   1338   -131    -21    -49
ATOM   1911  NE  ARG A 265      44.293  59.373  35.733  1.00 11.27           N  
ANISOU 1911  NE  ARG A 265     1377   1544   1361   -154    -92    -39
ATOM   1912  CZ  ARG A 265      43.876  59.067  36.972  1.00 11.00           C  
ANISOU 1912  CZ  ARG A 265     1287   1588   1303   -207     52     31
ATOM   1913  NH1 ARG A 265      44.473  59.549  38.067  1.00 10.91           N  
ANISOU 1913  NH1 ARG A 265     1217   1561   1366   -257     99   -208
ATOM   1914  NH2 ARG A 265      42.842  58.245  37.131  1.00 12.29           N1+
ANISOU 1914  NH2 ARG A 265     1597   1634   1438   -346   -183   -147
ATOM   1915  N   LEU A 266      48.208  64.411  37.705  1.00 31.02           N  
ATOM   1916  CA  LEU A 266      49.372  64.698  38.527  1.00 32.28           C  
ATOM   1917  C   LEU A 266      50.109  63.380  38.864  1.00 31.44           C  
ATOM   1918  O   LEU A 266      50.677  62.752  37.966  1.00 32.07           O  
ATOM   1919  CB  LEU A 266      48.882  65.538  39.734  1.00  0.00           C  
ATOM   1920  CG  LEU A 266      49.983  66.306  40.495  1.00  0.00           C  
ATOM   1921  CD1 LEU A 266      50.616  67.419  39.633  1.00  0.00           C  
ATOM   1922  CD2 LEU A 266      49.454  66.854  41.835  1.00  0.00           C  
ATOM   1923  N   ASN A 267      50.094  62.988  40.145  1.00 31.02           N  
ATOM   1924  CA  ASN A 267      50.797  61.823  40.675  1.00 30.54           C  
ATOM   1925  C   ASN A 267      49.778  60.740  41.062  1.00 30.29           C  
ATOM   1926  O   ASN A 267      49.459  59.895  40.228  1.00 30.82           O  
ATOM   1927  CB  ASN A 267      51.804  62.260  41.779  1.00  0.00           C  
ATOM   1928  CG  ASN A 267      51.288  63.260  42.819  1.00  0.00           C  
ATOM   1929  OD1 ASN A 267      50.322  62.975  43.516  1.00  0.00           O  
ATOM   1930  ND2 ASN A 267      51.891  64.437  42.940  1.00  0.00           N  
ATOM   1931  N   SER A 268      49.278  60.765  42.300  1.00 27.98           N  
ATOM   1932  CA  SER A 268      48.225  59.879  42.784  1.00 27.56           C  
ATOM   1933  C   SER A 268      46.852  60.310  42.232  1.00 27.51           C  
ATOM   1934  O   SER A 268      46.619  61.503  42.025  1.00 28.08           O  
ATOM   1935  CB  SER A 268      48.252  59.898  44.329  1.00  0.00           C  
ATOM   1936  OG  SER A 268      47.204  59.140  44.915  1.00  0.00           O  
ATOM   1937  N   SER A 269      45.939  59.335  42.112  1.00 34.32           N  
ATOM   1938  CA  SER A 269      44.520  59.538  41.806  1.00 33.87           C  
ATOM   1939  C   SER A 269      43.731  60.083  43.026  1.00 34.25           C  
ATOM   1940  O   SER A 269      42.543  60.376  42.893  1.00 33.82           O  
ATOM   1941  CB  SER A 269      43.937  58.219  41.236  1.00  0.00           C  
ATOM   1942  OG  SER A 269      42.860  58.431  40.334  1.00  0.00           O  
ATOM   1943  N   ASP A 270      44.406  60.230  44.177  1.00 34.46           N  
ATOM   1944  CA  ASP A 270      43.963  60.960  45.365  1.00 35.26           C  
ATOM   1945  C   ASP A 270      45.241  61.593  45.983  1.00 35.90           C  
ATOM   1946  O   ASP A 270      45.888  60.953  46.820  1.00 35.39           O  
ATOM   1947  CB  ASP A 270      43.169  60.043  46.326  1.00  0.00           C  
ATOM   1948  CG  ASP A 270      42.469  60.766  47.478  1.00  0.00           C  
ATOM   1949  OD1 ASP A 270      42.807  61.933  47.770  1.00  0.00           O  
ATOM   1950  OD2 ASP A 270      41.649  60.091  48.133  1.00  0.00           O1-
ATOM   1951  N   PRO A 271      45.678  62.758  45.450  1.00 36.09           N  
ATOM   1952  CA  PRO A 271      46.994  63.337  45.766  1.00 36.60           C  
ATOM   1953  C   PRO A 271      46.947  64.307  46.961  1.00 37.26           C  
ATOM   1954  O   PRO A 271      46.311  65.354  46.862  1.00 36.30           O  
ATOM   1955  CD  PRO A 271      45.022  63.497  44.368  1.00  0.00           C  
ATOM   1956  CB  PRO A 271      47.360  64.024  44.440  1.00  0.00           C  
ATOM   1957  CG  PRO A 271      46.037  64.524  43.878  1.00  0.00           C  
ATOM   1958  N   SER A 272      47.638  63.957  48.055  1.00 37.60           N  
ATOM   1959  CA  SER A 272      47.757  64.796  49.250  1.00 38.89           C  
ATOM   1960  C   SER A 272      48.549  66.097  48.981  1.00 39.55           C  
ATOM   1961  O   SER A 272      49.456  66.113  48.143  1.00 39.91           O  
ATOM   1962  CB  SER A 272      48.344  63.952  50.402  1.00  0.00           C  
ATOM   1963  OG  SER A 272      48.336  64.647  51.636  1.00  0.00           O  
ATOM   1964  N   LEU A 273      48.198  67.169  49.705  1.00 41.13           N  
ATOM   1965  CA  LEU A 273      48.850  68.470  49.603  1.00 42.93           C  
ATOM   1966  C   LEU A 273      50.124  68.484  50.468  1.00 43.57           C  
ATOM   1967  O   LEU A 273      50.050  68.568  51.694  1.00 43.67           O  
ATOM   1968  CB  LEU A 273      47.868  69.599  49.991  1.00  0.00           C  
ATOM   1969  CG  LEU A 273      48.026  70.928  49.217  1.00  0.00           C  
ATOM   1970  CD1 LEU A 273      47.033  71.965  49.761  1.00  0.00           C  
ATOM   1971  CD2 LEU A 273      49.446  71.514  49.230  1.00  0.00           C  
ATOM   1972  N   ILE A 274      51.283  68.444  49.808  1.00 44.71           N  
ATOM   1973  CA  ILE A 274      52.625  68.478  50.403  1.00 45.57           C  
ATOM   1974  C   ILE A 274      52.930  69.705  51.311  1.00 45.44           C  
ATOM   1975  O   ILE A 274      53.855  69.654  52.118  1.00 45.58           O  
ATOM   1976  CB  ILE A 274      53.684  68.370  49.264  1.00  0.00           C  
ATOM   1977  CG1 ILE A 274      55.143  68.273  49.766  1.00  0.00           C  
ATOM   1978  CG2 ILE A 274      53.528  69.468  48.188  1.00  0.00           C  
ATOM   1979  CD1 ILE A 274      56.072  67.520  48.807  1.00  0.00           C  
ATOM   1980  N   GLY A 275      52.145  70.782  51.183  1.00 46.07           N  
ATOM   1981  CA  GLY A 275      52.250  71.982  52.015  1.00 46.17           C  
ATOM   1982  C   GLY A 275      51.548  71.815  53.374  1.00 45.83           C  
ATOM   1983  O   GLY A 275      51.811  72.586  54.294  1.00 46.24           O  
ATOM   1984  N   LEU A 276      50.655  70.831  53.525  1.00 44.96           N  
ATOM   1985  CA  LEU A 276      49.874  70.647  54.742  1.00 44.35           C  
ATOM   1986  C   LEU A 276      50.570  69.710  55.710  1.00 43.78           C  
ATOM   1987  O   LEU A 276      50.703  68.519  55.401  1.00 42.94           O  
ATOM   1988  CB  LEU A 276      48.518  70.033  54.383  1.00  0.00           C  
ATOM   1989  CG  LEU A 276      47.540  71.089  53.888  1.00  0.00           C  
ATOM   1990  CD1 LEU A 276      46.379  70.402  53.183  1.00  0.00           C  
ATOM   1991  CD2 LEU A 276      47.081  71.990  55.055  1.00  0.00           C  
ATOM   1992  N   LYS A 277      50.918  70.228  56.896  1.00 43.26           N  
ATOM   1993  CA  LYS A 277      51.382  69.338  57.942  1.00 43.53           C  
ATOM   1994  C   LYS A 277      50.115  68.824  58.626  1.00 42.88           C  
ATOM   1995  O   LYS A 277      49.332  69.591  59.179  1.00 42.11           O  
ATOM   1996  CB  LYS A 277      52.275  70.102  58.921  1.00 44.70           C  
ATOM   1997  CG  LYS A 277      53.292  69.240  59.661  1.00 47.14           C  
ATOM   1998  CD  LYS A 277      52.920  69.065  61.123  1.00 49.63           C  
ATOM   1999  CE  LYS A 277      54.057  68.429  61.927  1.00 50.96           C  
ATOM   2000  NZ  LYS A 277      54.387  67.038  61.491  1.00 51.43           N1+
ATOM   2001  N   GLN A 278      49.909  67.520  58.559  1.00 42.09           N  
ATOM   2002  CA  GLN A 278      48.731  66.919  59.145  1.00 42.48           C  
ATOM   2003  C   GLN A 278      49.032  66.202  60.450  1.00 43.23           C  
ATOM   2004  O   GLN A 278      50.001  65.447  60.557  1.00 43.21           O  
ATOM   2005  CB  GLN A 278      48.124  65.930  58.157  1.00 40.77           C  
ATOM   2006  CG  GLN A 278      47.818  66.548  56.821  1.00 40.18           C  
ATOM   2007  CD  GLN A 278      47.631  65.513  55.741  1.00 39.15           C  
ATOM   2008  OE1 GLN A 278      46.787  64.625  55.852  1.00 39.81           O  
ATOM   2009  NE2 GLN A 278      48.421  65.619  54.687  1.00 37.56           N  
ATOM   2010  N   TYR A 279      48.196  66.470  61.453  1.00 43.38           N  
ATOM   2011  CA  TYR A 279      48.225  65.824  62.753  1.00 43.99           C  
ATOM   2012  C   TYR A 279      46.897  65.090  62.966  1.00 44.21           C  
ATOM   2013  O   TYR A 279      45.833  65.618  62.632  1.00 44.02           O  
ATOM   2014  CB  TYR A 279      48.494  66.884  63.841  1.00  0.00           C  
ATOM   2015  CG  TYR A 279      48.553  66.347  65.262  1.00  0.00           C  
ATOM   2016  CD1 TYR A 279      49.443  65.300  65.587  1.00  0.00           C  
ATOM   2017  CD2 TYR A 279      47.716  66.885  66.263  1.00  0.00           C  
ATOM   2018  CE1 TYR A 279      49.483  64.784  66.896  1.00  0.00           C  
ATOM   2019  CE2 TYR A 279      47.764  66.375  67.574  1.00  0.00           C  
ATOM   2020  CZ  TYR A 279      48.646  65.325  67.891  1.00  0.00           C  
ATOM   2021  OH  TYR A 279      48.695  64.839  69.163  1.00  0.00           O  
ATOM   2022  N   TYR A 280      46.989  63.884  63.525  1.00 44.81           N  
ATOM   2023  CA  TYR A 280      45.877  62.975  63.740  1.00 45.54           C  
ATOM   2024  C   TYR A 280      45.972  62.578  65.214  1.00 46.40           C  
ATOM   2025  O   TYR A 280      46.993  62.015  65.612  1.00 46.03           O  
ATOM   2026  CB  TYR A 280      45.988  61.732  62.815  1.00  0.00           C  
ATOM   2027  CG  TYR A 280      46.582  61.962  61.433  1.00  0.00           C  
ATOM   2028  CD1 TYR A 280      47.985  62.023  61.259  1.00  0.00           C  
ATOM   2029  CD2 TYR A 280      45.741  62.121  60.316  1.00  0.00           C  
ATOM   2030  CE1 TYR A 280      48.534  62.293  59.991  1.00  0.00           C  
ATOM   2031  CE2 TYR A 280      46.299  62.340  59.044  1.00  0.00           C  
ATOM   2032  CZ  TYR A 280      47.687  62.456  58.880  1.00  0.00           C  
ATOM   2033  OH  TYR A 280      48.205  62.723  57.647  1.00  0.00           O  
ATOM   2034  N   LYS A 281      44.945  62.897  66.003  1.00 46.87           N  
ATOM   2035  CA  LYS A 281      44.875  62.563  67.420  1.00 47.83           C  
ATOM   2036  C   LYS A 281      43.626  61.705  67.626  1.00 49.17           C  
ATOM   2037  O   LYS A 281      42.581  62.034  67.067  1.00 49.46           O  
ATOM   2038  CB  LYS A 281      44.815  63.876  68.239  1.00  0.00           C  
ATOM   2039  CG  LYS A 281      44.650  63.718  69.767  1.00  0.00           C  
ATOM   2040  CD  LYS A 281      45.854  63.083  70.482  1.00  0.00           C  
ATOM   2041  CE  LYS A 281      45.580  62.832  71.972  1.00  0.00           C  
ATOM   2042  NZ  LYS A 281      46.768  62.281  72.645  1.00  0.00           N1+
ATOM   2043  N   VAL A 282      43.724  60.659  68.453  1.00 50.65           N  
ATOM   2044  CA  VAL A 282      42.553  59.928  68.922  1.00 51.93           C  
ATOM   2045  C   VAL A 282      41.959  60.677  70.126  1.00 52.48           C  
ATOM   2046  O   VAL A 282      42.527  60.659  71.219  1.00 53.00           O  
ATOM   2047  CB  VAL A 282      42.867  58.452  69.284  1.00  0.00           C  
ATOM   2048  CG1 VAL A 282      41.701  57.705  69.969  1.00  0.00           C  
ATOM   2049  CG2 VAL A 282      43.289  57.684  68.022  1.00  0.00           C  
ATOM   2050  N   VAL A 283      40.848  61.356  69.852  1.00 53.48           N  
ATOM   2051  CA  VAL A 283      39.984  62.013  70.825  1.00 54.06           C  
ATOM   2052  C   VAL A 283      38.588  61.403  70.886  1.00 55.35           C  
ATOM   2053  O   VAL A 283      38.035  60.968  69.870  1.00 55.43           O  
ATOM   2054  CB  VAL A 283      39.833  63.514  70.508  1.00 53.24           C  
ATOM   2055  CG1 VAL A 283      39.134  64.215  71.663  1.00 52.42           C  
ATOM   2056  CG2 VAL A 283      41.195  64.130  70.225  1.00 51.46           C  
ATOM   2057  N   ASN A 284      38.021  61.370  72.087  1.00 56.54           N  
ATOM   2058  CA  ASN A 284      36.687  60.829  72.261  1.00 57.40           C  
ATOM   2059  C   ASN A 284      35.687  61.959  72.183  1.00 56.79           C  
ATOM   2060  O   ASN A 284      36.010  63.110  72.483  1.00 56.52           O  
ATOM   2061  CB  ASN A 284      36.568  60.104  73.598  1.00 59.49           C  
ATOM   2062  CG  ASN A 284      37.412  58.844  73.649  1.00 61.76           C  
ATOM   2063  OD1 ASN A 284      37.310  57.967  72.774  1.00 62.28           O  
ATOM   2064  ND2 ASN A 284      38.255  58.743  74.679  1.00 62.58           N  
ATOM   2065  N   SER A 285      34.450  61.593  71.844  1.00 56.57           N  
ATOM   2066  CA  SER A 285      33.290  62.453  71.627  1.00 56.76           C  
ATOM   2067  C   SER A 285      33.127  63.630  72.610  1.00 55.88           C  
ATOM   2068  O   SER A 285      32.890  64.750  72.158  1.00 55.64           O  
ATOM   2069  CB  SER A 285      32.051  61.539  71.555  1.00  0.00           C  
ATOM   2070  OG  SER A 285      32.045  60.605  72.627  1.00  0.00           O  
ATOM   2071  N   TYR A 286      33.319  63.382  73.915  1.00 55.47           N  
ATOM   2072  CA  TYR A 286      33.191  64.423  74.920  1.00 54.74           C  
ATOM   2073  C   TYR A 286      34.498  65.072  75.326  1.00 53.11           C  
ATOM   2074  O   TYR A 286      34.520  66.001  76.132  1.00 53.05           O  
ATOM   2075  CB  TYR A 286      32.431  63.872  76.128  1.00 56.77           C  
ATOM   2076  CG  TYR A 286      31.059  63.383  75.722  1.00 58.82           C  
ATOM   2077  CD1 TYR A 286      30.870  62.076  75.266  1.00 60.07           C  
ATOM   2078  CD2 TYR A 286      29.971  64.260  75.678  1.00 59.62           C  
ATOM   2079  CE1 TYR A 286      29.635  61.653  74.768  1.00 61.16           C  
ATOM   2080  CE2 TYR A 286      28.731  63.850  75.182  1.00 60.90           C  
ATOM   2081  CZ  TYR A 286      28.572  62.549  74.727  1.00 61.65           C  
ATOM   2082  OH  TYR A 286      27.359  62.147  74.211  1.00 62.63           O  
ATOM   2083  N   PRO A 287      35.662  64.463  75.043  1.00 51.43           N  
ATOM   2084  CA  PRO A 287      36.920  65.231  75.040  1.00 49.11           C  
ATOM   2085  C   PRO A 287      37.088  66.300  73.944  1.00 47.12           C  
ATOM   2086  O   PRO A 287      37.796  67.273  74.215  1.00 45.73           O  
ATOM   2087  CD  PRO A 287      35.911  63.145  75.643  1.00  0.00           C  
ATOM   2088  CB  PRO A 287      37.994  64.144  75.039  1.00  0.00           C  
ATOM   2089  CG  PRO A 287      37.406  63.103  75.971  1.00  0.00           C  
ATOM   2090  N   LEU A 288      36.431  66.132  72.780  1.00 45.73           N  
ATOM   2091  CA  LEU A 288      36.521  66.989  71.582  1.00 44.13           C  
ATOM   2092  C   LEU A 288      36.605  68.503  71.859  1.00 43.74           C  
ATOM   2093  O   LEU A 288      37.618  69.122  71.537  1.00 43.62           O  
ATOM   2094  CB  LEU A 288      35.330  66.730  70.624  1.00  0.00           C  
ATOM   2095  CG  LEU A 288      35.281  65.387  69.862  1.00  0.00           C  
ATOM   2096  CD1 LEU A 288      34.036  65.336  68.951  1.00  0.00           C  
ATOM   2097  CD2 LEU A 288      36.557  65.060  69.068  1.00  0.00           C  
ATOM   2098  N   ALA A 289      35.547  69.064  72.463  1.00 43.87           N  
ATOM   2099  CA  ALA A 289      35.404  70.504  72.697  1.00 44.69           C  
ATOM   2100  C   ALA A 289      36.521  71.100  73.568  1.00 43.87           C  
ATOM   2101  O   ALA A 289      36.981  72.204  73.299  1.00 42.58           O  
ATOM   2102  CB  ALA A 289      34.031  70.789  73.320  1.00  0.00           C  
ATOM   2103  N   HIS A 290      36.976  70.338  74.566  1.00 44.12           N  
ATOM   2104  CA  HIS A 290      38.042  70.746  75.477  1.00 45.02           C  
ATOM   2105  C   HIS A 290      39.386  70.883  74.746  1.00 44.20           C  
ATOM   2106  O   HIS A 290      40.054  71.904  74.893  1.00 44.69           O  
ATOM   2107  CB  HIS A 290      38.108  69.765  76.662  1.00  0.00           C  
ATOM   2108  CG  HIS A 290      36.786  69.611  77.379  1.00  0.00           C  
ATOM   2109  ND1 HIS A 290      35.920  68.542  77.186  1.00  0.00           N  
ATOM   2110  CD2 HIS A 290      36.164  70.422  78.302  1.00  0.00           C  
ATOM   2111  CE1 HIS A 290      34.852  68.747  77.959  1.00  0.00           C  
ATOM   2112  NE2 HIS A 290      34.933  69.870  78.663  1.00  0.00           N  
ATOM   2113  N   LYS A 291      39.697  69.879  73.913  1.00 43.29           N  
ATOM   2114  CA  LYS A 291      40.836  69.807  72.997  1.00 43.01           C  
ATOM   2115  C   LYS A 291      40.807  71.005  72.041  1.00 41.60           C  
ATOM   2116  O   LYS A 291      41.827  71.636  71.806  1.00 40.48           O  
ATOM   2117  CB  LYS A 291      40.802  68.521  72.176  1.00 44.41           C  
ATOM   2118  CG  LYS A 291      42.170  67.867  72.006  1.00 47.24           C  
ATOM   2119  CD  LYS A 291      43.238  68.886  71.659  1.00 48.87           C  
ATOM   2120  CE  LYS A 291      44.650  68.300  71.803  1.00 51.33           C  
ATOM   2121  NZ  LYS A 291      45.023  67.933  73.215  1.00 52.15           N1+
ATOM   2122  N   VAL A 292      39.614  71.326  71.486  1.00 40.85           N  
ATOM   2123  CA  VAL A 292      39.362  72.480  70.597  1.00 40.42           C  
ATOM   2124  C   VAL A 292      39.697  73.811  71.285  1.00 40.78           C  
ATOM   2125  O   VAL A 292      40.440  74.619  70.721  1.00 40.94           O  
ATOM   2126  CB  VAL A 292      37.884  72.572  70.073  1.00  0.00           C  
ATOM   2127  CG1 VAL A 292      37.443  73.927  69.461  1.00  0.00           C  
ATOM   2128  CG2 VAL A 292      37.582  71.481  69.050  1.00  0.00           C  
ATOM   2129  N   PHE A 293      39.170  74.003  72.506  1.00 41.13           N  
ATOM   2130  CA  PHE A 293      39.466  75.173  73.334  1.00 41.84           C  
ATOM   2131  C   PHE A 293      40.977  75.275  73.602  1.00 41.27           C  
ATOM   2132  O   PHE A 293      41.507  76.376  73.598  1.00 40.15           O  
ATOM   2133  CB  PHE A 293      38.710  75.130  74.684  1.00  0.00           C  
ATOM   2134  CG  PHE A 293      37.203  74.910  74.670  1.00  0.00           C  
ATOM   2135  CD1 PHE A 293      36.386  75.354  73.605  1.00  0.00           C  
ATOM   2136  CD2 PHE A 293      36.584  74.365  75.817  1.00  0.00           C  
ATOM   2137  CE1 PHE A 293      35.012  75.150  73.656  1.00  0.00           C  
ATOM   2138  CE2 PHE A 293      35.208  74.183  75.852  1.00  0.00           C  
ATOM   2139  CZ  PHE A 293      34.427  74.565  74.771  1.00  0.00           C  
ATOM   2140  N   GLU A 294      41.637  74.126  73.780  1.00 41.53           N  
ATOM   2141  CA  GLU A 294      43.055  73.949  74.105  1.00 42.68           C  
ATOM   2142  C   GLU A 294      43.846  74.476  72.904  1.00 41.51           C  
ATOM   2143  O   GLU A 294      44.720  75.343  73.034  1.00 40.90           O  
ATOM   2144  CB  GLU A 294      43.373  72.458  74.295  1.00 45.59           C  
ATOM   2145  CG  GLU A 294      44.478  72.144  75.306  1.00 49.77           C  
ATOM   2146  CD  GLU A 294      45.206  70.833  74.994  1.00 52.33           C  
ATOM   2147  OE1 GLU A 294      46.086  70.848  74.101  1.00 53.72           O  
ATOM   2148  OE2 GLU A 294      44.896  69.791  75.625  1.00 53.12           O1-
ATOM   2149  N   GLU A 295      43.503  74.048  71.685  1.00 39.66           N  
ATOM   2150  CA  GLU A 295      44.200  74.494  70.478  1.00 38.16           C  
ATOM   2151  C   GLU A 295      43.953  75.976  70.125  1.00 38.46           C  
ATOM   2152  O   GLU A 295      44.896  76.654  69.715  1.00 39.28           O  
ATOM   2153  CB  GLU A 295      43.918  73.509  69.335  1.00  0.00           C  
ATOM   2154  CG  GLU A 295      44.549  72.132  69.647  1.00  0.00           C  
ATOM   2155  CD  GLU A 295      44.291  71.057  68.603  1.00  0.00           C  
ATOM   2156  OE1 GLU A 295      43.554  71.333  67.633  1.00  0.00           O  
ATOM   2157  OE2 GLU A 295      44.818  69.945  68.816  1.00  0.00           O1-
ATOM   2158  N   LYS A 296      42.734  76.482  70.356  1.00 38.41           N  
ATOM   2159  CA  LYS A 296      42.409  77.897  70.141  1.00 39.50           C  
ATOM   2160  C   LYS A 296      42.910  78.833  71.263  1.00 40.68           C  
ATOM   2161  O   LYS A 296      43.205  79.991  70.978  1.00 40.05           O  
ATOM   2162  CB  LYS A 296      40.895  78.061  69.886  1.00  0.00           C  
ATOM   2163  CG  LYS A 296      40.379  77.398  68.590  1.00  0.00           C  
ATOM   2164  CD  LYS A 296      41.008  77.961  67.296  1.00  0.00           C  
ATOM   2165  CE  LYS A 296      40.353  77.446  66.003  1.00  0.00           C  
ATOM   2166  NZ  LYS A 296      40.485  75.987  65.862  1.00  0.00           N1+
ATOM   2167  N   THR A 297      43.019  78.348  72.508  1.00 41.98           N  
ATOM   2168  CA  THR A 297      43.593  79.111  73.623  1.00 44.30           C  
ATOM   2169  C   THR A 297      45.132  79.121  73.570  1.00 45.86           C  
ATOM   2170  O   THR A 297      45.734  80.106  73.993  1.00 46.36           O  
ATOM   2171  CB  THR A 297      43.161  78.567  75.014  1.00  0.00           C  
ATOM   2172  OG1 THR A 297      41.750  78.546  75.090  1.00  0.00           O  
ATOM   2173  CG2 THR A 297      43.648  79.367  76.235  1.00  0.00           C  
ATOM   2174  N   GLN A 298      45.742  78.054  73.021  1.00 47.94           N  
ATOM   2175  CA  GLN A 298      47.173  77.980  72.731  1.00 49.40           C  
ATOM   2176  C   GLN A 298      47.615  79.140  71.825  1.00 50.11           C  
ATOM   2177  O   GLN A 298      48.526  79.876  72.197  1.00 49.99           O  
ATOM   2178  CB  GLN A 298      47.529  76.583  72.159  1.00  0.00           C  
ATOM   2179  CG  GLN A 298      48.964  76.389  71.619  1.00  0.00           C  
ATOM   2180  CD  GLN A 298      50.051  76.724  72.640  1.00  0.00           C  
ATOM   2181  OE1 GLN A 298      49.953  76.341  73.803  1.00  0.00           O  
ATOM   2182  NE2 GLN A 298      51.102  77.423  72.229  1.00  0.00           N  
ATOM   2183  N   HIS A 299      46.915  79.317  70.698  1.00 50.82           N  
ATOM   2184  CA  HIS A 299      47.096  80.460  69.816  1.00 51.68           C  
ATOM   2185  C   HIS A 299      45.760  80.767  69.131  1.00 51.67           C  
ATOM   2186  O   HIS A 299      45.198  79.871  68.500  1.00 52.07           O  
ATOM   2187  CB  HIS A 299      48.172  80.167  68.747  1.00  0.00           C  
ATOM   2188  CG  HIS A 299      49.569  79.845  69.215  1.00  0.00           C  
ATOM   2189  ND1 HIS A 299      50.372  80.741  69.904  1.00  0.00           N  
ATOM   2190  CD2 HIS A 299      50.337  78.714  69.058  1.00  0.00           C  
ATOM   2191  CE1 HIS A 299      51.532  80.133  70.154  1.00  0.00           C  
ATOM   2192  NE2 HIS A 299      51.577  78.892  69.675  1.00  0.00           N  
ATOM   2193  N   LEU A 300      45.335  82.035  69.179  1.00 50.75           N  
ATOM   2194  CA  LEU A 300      44.278  82.595  68.333  1.00 49.73           C  
ATOM   2195  C   LEU A 300      44.947  83.551  67.322  1.00 49.50           C  
ATOM   2196  O   LEU A 300      46.096  83.949  67.535  1.00 49.35           O  
ATOM   2197  CB  LEU A 300      43.220  83.300  69.223  1.00  0.00           C  
ATOM   2198  CG  LEU A 300      41.960  83.839  68.492  1.00  0.00           C  
ATOM   2199  CD1 LEU A 300      41.179  82.715  67.775  1.00  0.00           C  
ATOM   2200  CD2 LEU A 300      41.064  84.654  69.450  1.00  0.00           C  
ATOM   2201  N   GLN A 301      44.236  83.807  66.218  1.00 22.11           N  
ATOM   2202  CA  GLN A 301      44.568  84.547  64.993  1.00 22.50           C  
ATOM   2203  C   GLN A 301      45.648  85.649  65.069  1.00 22.96           C  
ATOM   2204  O   GLN A 301      45.660  86.448  66.004  1.00 22.53           O  
ATOM   2205  CB  GLN A 301      43.232  85.061  64.410  1.00  0.00           C  
ATOM   2206  CG  GLN A 301      43.334  86.070  63.242  1.00  0.00           C  
ATOM   2207  CD  GLN A 301      42.059  86.208  62.421  1.00  0.00           C  
ATOM   2208  OE1 GLN A 301      41.471  87.278  62.358  1.00  0.00           O  
ATOM   2209  NE2 GLN A 301      41.605  85.145  61.769  1.00  0.00           N  
ATOM   2210  N   GLU A 302      46.485  85.692  64.028  1.00 21.51           N  
ATOM   2211  CA  GLU A 302      47.536  86.671  63.805  1.00 20.51           C  
ATOM   2212  C   GLU A 302      47.193  87.468  62.529  1.00 22.04           C  
ATOM   2213  O   GLU A 302      46.051  87.907  62.387  1.00 19.06           O  
ATOM   2214  CB  GLU A 302      48.914  85.949  63.869  1.00  0.00           C  
ATOM   2215  CG  GLU A 302      49.134  84.701  62.958  1.00  0.00           C  
ATOM   2216  CD  GLU A 302      49.858  84.929  61.636  1.00  0.00           C  
ATOM   2217  OE1 GLU A 302      50.471  86.007  61.497  1.00  0.00           O  
ATOM   2218  OE2 GLU A 302      49.803  84.025  60.772  1.00  0.00           O1-
ATOM   2219  N   LEU A 303      48.169  87.669  61.642  1.00 23.09           N  
ATOM   2220  CA  LEU A 303      48.018  88.334  60.354  1.00 25.76           C  
ATOM   2221  C   LEU A 303      48.427  87.303  59.292  1.00 25.15           C  
ATOM   2222  O   LEU A 303      47.665  86.378  59.011  1.00 23.78           O  
ATOM   2223  CB  LEU A 303      48.847  89.645  60.311  1.00  0.00           C  
ATOM   2224  CG  LEU A 303      48.363  90.752  61.281  1.00  0.00           C  
ATOM   2225  CD1 LEU A 303      48.897  90.554  62.719  1.00  0.00           C  
ATOM   2226  CD2 LEU A 303      48.682  92.161  60.731  1.00  0.00           C  
ATOM   2227  N   PHE A 304      49.644  87.435  58.764  1.00 23.84           N  
ATOM   2228  CA  PHE A 304      50.309  86.442  57.932  1.00 23.16           C  
ATOM   2229  C   PHE A 304      51.823  86.541  58.175  1.00 24.76           C  
ATOM   2230  O   PHE A 304      52.619  86.625  57.248  1.00 23.77           O  
ATOM   2231  CB  PHE A 304      49.821  86.485  56.461  1.00  0.00           C  
ATOM   2232  CG  PHE A 304      49.883  87.820  55.738  1.00  0.00           C  
ATOM   2233  CD1 PHE A 304      48.855  88.771  55.917  1.00  0.00           C  
ATOM   2234  CD2 PHE A 304      51.018  88.173  54.977  1.00  0.00           C  
ATOM   2235  CE1 PHE A 304      48.944  90.014  55.306  1.00  0.00           C  
ATOM   2236  CE2 PHE A 304      51.085  89.419  54.369  1.00  0.00           C  
ATOM   2237  CZ  PHE A 304      50.052  90.334  54.531  1.00  0.00           C  
ATOM   2238  N   SER A 305      52.206  86.501  59.454  1.00 26.10           N  
ATOM   2239  CA  SER A 305      53.573  86.582  59.960  1.00 29.00           C  
ATOM   2240  C   SER A 305      54.236  85.186  59.997  1.00 29.52           C  
ATOM   2241  O   SER A 305      54.917  84.852  60.964  1.00 29.13           O  
ATOM   2242  CB  SER A 305      53.531  87.286  61.339  1.00  0.00           C  
ATOM   2243  OG  SER A 305      54.823  87.591  61.832  1.00  0.00           O  
ATOM   2244  N   ARG A 306      54.016  84.386  58.945  1.00 31.69           N  
ATOM   2245  CA  ARG A 306      54.567  83.051  58.673  1.00 34.09           C  
ATOM   2246  C   ARG A 306      54.087  81.910  59.598  1.00 33.99           C  
ATOM   2247  O   ARG A 306      54.117  80.760  59.165  1.00 35.54           O  
ATOM   2248  CB  ARG A 306      56.118  83.109  58.595  1.00  0.00           C  
ATOM   2249  CG  ARG A 306      56.785  81.847  58.011  1.00  0.00           C  
ATOM   2250  CD  ARG A 306      58.284  82.013  57.733  1.00  0.00           C  
ATOM   2251  NE  ARG A 306      58.889  80.736  57.328  1.00  0.00           N  
ATOM   2252  CZ  ARG A 306      60.053  80.575  56.679  1.00  0.00           C  
ATOM   2253  NH1 ARG A 306      60.803  81.624  56.324  1.00  0.00           N  
ATOM   2254  NH2 ARG A 306      60.467  79.341  56.379  1.00  0.00           N1+
ATOM   2255  N   ILE A 307      53.682  82.217  60.831  1.00 32.44           N  
ATOM   2256  CA  ILE A 307      53.484  81.261  61.918  1.00 30.29           C  
ATOM   2257  C   ILE A 307      52.616  81.969  62.996  1.00 28.19           C  
ATOM   2258  O   ILE A 307      52.663  83.204  63.054  1.00 26.98           O  
ATOM   2259  CB  ILE A 307      54.911  80.892  62.486  1.00  0.00           C  
ATOM   2260  CG1 ILE A 307      55.009  79.609  63.339  1.00  0.00           C  
ATOM   2261  CG2 ILE A 307      55.608  82.049  63.240  1.00  0.00           C  
ATOM   2262  CD1 ILE A 307      54.731  78.309  62.563  1.00  0.00           C  
ATOM   2263  N   PRO A 308      51.897  81.231  63.876  1.00 25.37           N  
ATOM   2264  CA  PRO A 308      51.609  79.788  63.836  1.00 25.14           C  
ATOM   2265  C   PRO A 308      50.357  79.442  63.001  1.00 22.36           C  
ATOM   2266  O   PRO A 308      50.181  79.980  61.908  1.00 21.95           O  
ATOM   2267  CD  PRO A 308      51.403  81.823  65.124  1.00  0.00           C  
ATOM   2268  CB  PRO A 308      51.529  79.445  65.340  1.00  0.00           C  
ATOM   2269  CG  PRO A 308      50.871  80.664  65.961  1.00  0.00           C  
ATOM   2270  N   PHE A 309      49.566  78.485  63.501  1.00 20.65           N  
ATOM   2271  CA  PHE A 309      48.376  77.919  62.877  1.00 19.77           C  
ATOM   2272  C   PHE A 309      47.156  78.824  63.092  1.00 19.41           C  
ATOM   2273  O   PHE A 309      46.784  79.535  62.175  1.00 18.49           O  
ATOM   2274  CB  PHE A 309      48.208  76.459  63.354  1.00  0.00           C  
ATOM   2275  CG  PHE A 309      48.291  76.183  64.854  1.00  0.00           C  
ATOM   2276  CD1 PHE A 309      47.130  76.178  65.657  1.00  0.00           C  
ATOM   2277  CD2 PHE A 309      49.547  76.017  65.478  1.00  0.00           C  
ATOM   2278  CE1 PHE A 309      47.224  75.977  67.026  1.00  0.00           C  
ATOM   2279  CE2 PHE A 309      49.619  75.795  66.846  1.00  0.00           C  
ATOM   2280  CZ  PHE A 309      48.462  75.774  67.616  1.00  0.00           C  
ATOM   2281  N   ASN A 310      46.600  78.820  64.303  1.00 16.18           N  
ATOM   2282  CA  ASN A 310      45.811  79.854  64.990  1.00 18.94           C  
ATOM   2283  C   ASN A 310      44.592  80.560  64.340  1.00 18.31           C  
ATOM   2284  O   ASN A 310      43.834  81.173  65.094  1.00 20.44           O  
ATOM   2285  CB  ASN A 310      46.780  80.862  65.650  1.00  0.00           C  
ATOM   2286  CG  ASN A 310      47.438  81.949  64.793  1.00  0.00           C  
ATOM   2287  OD1 ASN A 310      47.797  81.751  63.643  1.00  0.00           O  
ATOM   2288  ND2 ASN A 310      47.693  83.112  65.373  1.00  0.00           N  
ATOM   2289  N   GLN A 311      44.374  80.493  63.024  1.00 18.02           N  
ATOM   2290  CA  GLN A 311      43.300  81.211  62.325  1.00 19.00           C  
ATOM   2291  C   GLN A 311      42.507  80.306  61.376  1.00 19.24           C  
ATOM   2292  O   GLN A 311      43.108  79.654  60.517  1.00 19.21           O  
ATOM   2293  CB  GLN A 311      43.831  82.495  61.649  1.00  0.00           C  
ATOM   2294  CG  GLN A 311      45.163  82.362  60.886  1.00  0.00           C  
ATOM   2295  CD  GLN A 311      45.828  83.709  60.624  1.00  0.00           C  
ATOM   2296  OE1 GLN A 311      45.905  84.547  61.515  1.00  0.00           O  
ATOM   2297  NE2 GLN A 311      46.347  83.938  59.427  1.00  0.00           N  
ATOM   2298  N   ALA A 312      41.172  80.321  61.573  1.00 18.66           N  
ATOM   2299  CA  ALA A 312      40.169  79.412  60.997  1.00 19.77           C  
ATOM   2300  C   ALA A 312      40.430  77.945  61.430  1.00 19.73           C  
ATOM   2301  O   ALA A 312      41.156  77.736  62.403  1.00 17.88           O  
ATOM   2302  CB  ALA A 312      40.093  79.631  59.477  1.00  0.00           C  
ATOM   2303  N   LEU A 313      39.868  76.908  60.801  1.00 33.01           N  
ATOM   2304  CA  LEU A 313      38.561  76.717  60.176  1.00 30.28           C  
ATOM   2305  C   LEU A 313      38.154  75.371  60.799  1.00 29.26           C  
ATOM   2306  O   LEU A 313      38.944  74.434  60.641  1.00 28.35           O  
ATOM   2307  CB  LEU A 313      38.716  76.568  58.631  1.00  0.00           C  
ATOM   2308  CG  LEU A 313      37.425  76.791  57.803  1.00  0.00           C  
ATOM   2309  CD1 LEU A 313      37.738  76.844  56.292  1.00  0.00           C  
ATOM   2310  CD2 LEU A 313      36.306  75.770  58.103  1.00  0.00           C  
ATOM   2311  N   VAL A 314      37.037  75.267  61.542  1.00 28.01           N  
ATOM   2312  CA  VAL A 314      36.728  74.006  62.196  1.00 26.63           C  
ATOM   2313  C   VAL A 314      35.576  73.373  61.436  1.00 26.70           C  
ATOM   2314  O   VAL A 314      34.526  74.001  61.268  1.00 26.20           O  
ATOM   2315  CB  VAL A 314      36.300  74.230  63.658  1.00 25.58           C  
ATOM   2316  CG1 VAL A 314      36.079  72.904  64.342  1.00 24.37           C  
ATOM   2317  CG2 VAL A 314      37.362  75.043  64.385  1.00 25.44           C  
ATOM   2318  N   PHE A 315      35.803  72.148  60.962  1.00 25.33           N  
ATOM   2319  CA  PHE A 315      34.824  71.375  60.205  1.00 25.69           C  
ATOM   2320  C   PHE A 315      34.080  70.430  61.150  1.00 26.60           C  
ATOM   2321  O   PHE A 315      34.702  69.675  61.903  1.00 27.64           O  
ATOM   2322  CB  PHE A 315      35.525  70.563  59.086  1.00 22.28           C  
ATOM   2323  CG  PHE A 315      35.871  71.385  57.858  1.00 22.09           C  
ATOM   2324  CD1 PHE A 315      34.867  71.865  57.011  1.00 22.73           C  
ATOM   2325  CD2 PHE A 315      37.197  71.715  57.561  1.00 21.32           C  
ATOM   2326  CE1 PHE A 315      35.181  72.670  55.886  1.00 21.19           C  
ATOM   2327  CE2 PHE A 315      37.519  72.517  56.441  1.00 19.94           C  
ATOM   2328  CZ  PHE A 315      36.510  72.989  55.613  1.00 21.53           C  
ATOM   2329  N   SER A 316      32.754  70.527  61.115  1.00 26.62           N  
ATOM   2330  CA  SER A 316      31.777  69.739  61.851  1.00 28.63           C  
ATOM   2331  C   SER A 316      31.059  68.775  60.889  1.00 28.93           C  
ATOM   2332  O   SER A 316      31.192  68.905  59.670  1.00 28.43           O  
ATOM   2333  CB  SER A 316      30.752  70.733  62.436  1.00  0.00           C  
ATOM   2334  OG  SER A 316      31.364  71.546  63.422  1.00  0.00           O  
ATOM   2335  N   ASN A 317      30.295  67.833  61.455  1.00 29.67           N  
ATOM   2336  CA  ASN A 317      29.354  66.979  60.726  1.00 30.16           C  
ATOM   2337  C   ASN A 317      28.075  67.750  60.335  1.00 29.86           C  
ATOM   2338  O   ASN A 317      27.996  68.241  59.211  1.00 30.80           O  
ATOM   2339  CB  ASN A 317      29.113  65.619  61.451  1.00  0.00           C  
ATOM   2340  CG  ASN A 317      28.671  65.631  62.924  1.00  0.00           C  
ATOM   2341  OD1 ASN A 317      28.211  66.636  63.459  1.00  0.00           O  
ATOM   2342  ND2 ASN A 317      28.775  64.496  63.602  1.00  0.00           N  
ATOM   2343  N   LEU A 318      27.098  67.833  61.246  1.00 27.80           N  
ATOM   2344  CA  LEU A 318      25.778  68.401  60.984  1.00 27.01           C  
ATOM   2345  C   LEU A 318      25.764  69.938  61.038  1.00 26.10           C  
ATOM   2346  O   LEU A 318      26.575  70.554  61.736  1.00 25.55           O  
ATOM   2347  CB  LEU A 318      24.737  67.843  61.986  1.00  0.00           C  
ATOM   2348  CG  LEU A 318      24.381  66.349  61.785  1.00  0.00           C  
ATOM   2349  CD1 LEU A 318      25.171  65.414  62.721  1.00  0.00           C  
ATOM   2350  CD2 LEU A 318      22.862  66.118  61.913  1.00  0.00           C  
ATOM   2351  N   HIS A 319      24.749  70.516  60.387  1.00 24.87           N  
ATOM   2352  CA  HIS A 319      24.364  71.933  60.450  1.00 25.19           C  
ATOM   2353  C   HIS A 319      24.173  72.426  61.898  1.00 25.04           C  
ATOM   2354  O   HIS A 319      24.712  73.459  62.300  1.00 25.18           O  
ATOM   2355  CB  HIS A 319      23.068  72.153  59.629  1.00  0.00           C  
ATOM   2356  CG  HIS A 319      21.794  71.542  60.186  1.00  0.00           C  
ATOM   2357  ND1 HIS A 319      21.526  70.191  60.120  1.00  0.00           N  
ATOM   2358  CD2 HIS A 319      20.725  72.080  60.869  1.00  0.00           C  
ATOM   2359  CE1 HIS A 319      20.362  69.962  60.722  1.00  0.00           C  
ATOM   2360  NE2 HIS A 319      19.823  71.071  61.216  1.00  0.00           N  
ATOM   2361  N   SER A 320      23.442  71.622  62.676  1.00 24.80           N  
ATOM   2362  CA  SER A 320      23.121  71.838  64.074  1.00 26.46           C  
ATOM   2363  C   SER A 320      24.368  71.800  64.970  1.00 26.26           C  
ATOM   2364  O   SER A 320      24.452  72.592  65.911  1.00 27.17           O  
ATOM   2365  CB  SER A 320      22.054  70.797  64.461  1.00  0.00           C  
ATOM   2366  OG  SER A 320      22.493  69.479  64.164  1.00  0.00           O  
ATOM   2367  N   ARG A 321      25.336  70.935  64.632  1.00 26.56           N  
ATOM   2368  CA  ARG A 321      26.636  70.866  65.288  1.00 27.10           C  
ATOM   2369  C   ARG A 321      27.452  72.144  65.048  1.00 27.50           C  
ATOM   2370  O   ARG A 321      28.064  72.619  66.008  1.00 28.04           O  
ATOM   2371  CB  ARG A 321      27.383  69.570  64.887  1.00  0.00           C  
ATOM   2372  CG  ARG A 321      28.831  69.419  65.412  1.00  0.00           C  
ATOM   2373  CD  ARG A 321      28.980  69.274  66.933  1.00  0.00           C  
ATOM   2374  NE  ARG A 321      28.376  68.040  67.458  1.00  0.00           N  
ATOM   2375  CZ  ARG A 321      28.889  66.801  67.393  1.00  0.00           C  
ATOM   2376  NH1 ARG A 321      30.026  66.539  66.744  1.00  0.00           N  
ATOM   2377  NH2 ARG A 321      28.246  65.801  68.001  1.00  0.00           N1+
ATOM   2378  N   ALA A 322      27.404  72.705  63.822  1.00 27.96           N  
ATOM   2379  CA  ALA A 322      28.166  73.917  63.532  1.00 29.15           C  
ATOM   2380  C   ALA A 322      27.605  75.096  64.310  1.00 30.42           C  
ATOM   2381  O   ALA A 322      28.354  75.882  64.902  1.00 31.83           O  
ATOM   2382  CB  ALA A 322      28.141  74.229  62.032  1.00 28.14           C  
ATOM   2383  N   GLN A 323      26.273  75.221  64.282  1.00 31.68           N  
ATOM   2384  CA  GLN A 323      25.537  76.281  64.957  1.00 33.66           C  
ATOM   2385  C   GLN A 323      25.855  76.317  66.460  1.00 31.76           C  
ATOM   2386  O   GLN A 323      26.330  77.335  66.957  1.00 31.85           O  
ATOM   2387  CB  GLN A 323      24.037  76.122  64.646  1.00  0.00           C  
ATOM   2388  CG  GLN A 323      23.132  77.195  65.284  1.00  0.00           C  
ATOM   2389  CD  GLN A 323      21.672  77.027  64.863  1.00  0.00           C  
ATOM   2390  OE1 GLN A 323      21.385  76.620  63.740  1.00  0.00           O  
ATOM   2391  NE2 GLN A 323      20.730  77.359  65.741  1.00  0.00           N  
ATOM   2392  N   HIS A 324      25.673  75.173  67.132  1.00 30.31           N  
ATOM   2393  CA  HIS A 324      25.916  75.069  68.568  1.00 29.26           C  
ATOM   2394  C   HIS A 324      27.388  75.251  68.956  1.00 27.77           C  
ATOM   2395  O   HIS A 324      27.631  75.909  69.966  1.00 27.27           O  
ATOM   2396  CB  HIS A 324      25.315  73.783  69.158  1.00  0.00           C  
ATOM   2397  CG  HIS A 324      23.804  73.782  69.163  1.00  0.00           C  
ATOM   2398  ND1 HIS A 324      23.054  73.367  68.080  1.00  0.00           N  
ATOM   2399  CD2 HIS A 324      22.886  74.153  70.121  1.00  0.00           C  
ATOM   2400  CE1 HIS A 324      21.766  73.510  68.393  1.00  0.00           C  
ATOM   2401  NE2 HIS A 324      21.591  73.982  69.623  1.00  0.00           N  
ATOM   2402  N   LEU A 325      28.351  74.742  68.163  1.00 26.71           N  
ATOM   2403  CA  LEU A 325      29.755  75.002  68.480  1.00 27.45           C  
ATOM   2404  C   LEU A 325      30.141  76.460  68.297  1.00 27.90           C  
ATOM   2405  O   LEU A 325      30.907  77.001  69.087  1.00 26.96           O  
ATOM   2406  CB  LEU A 325      30.677  74.089  67.649  1.00 27.35           C  
ATOM   2407  CG  LEU A 325      32.201  74.249  67.755  1.00 28.40           C  
ATOM   2408  CD1 LEU A 325      32.629  74.180  69.216  1.00 28.46           C  
ATOM   2409  CD2 LEU A 325      32.899  73.145  66.968  1.00 27.44           C  
ATOM   2410  N   ALA A 326      29.610  77.103  67.265  1.00 29.07           N  
ATOM   2411  CA  ALA A 326      29.924  78.505  67.043  1.00 31.23           C  
ATOM   2412  C   ALA A 326      29.414  79.338  68.217  1.00 32.98           C  
ATOM   2413  O   ALA A 326      30.117  80.212  68.723  1.00 33.67           O  
ATOM   2414  CB  ALA A 326      29.288  78.989  65.745  1.00 31.23           C  
ATOM   2415  N   ASP A 327      28.186  79.044  68.682  1.00 34.86           N  
ATOM   2416  CA  ASP A 327      27.567  79.665  69.865  1.00 37.72           C  
ATOM   2417  C   ASP A 327      28.373  79.432  71.156  1.00 38.59           C  
ATOM   2418  O   ASP A 327      28.585  80.372  71.923  1.00 38.32           O  
ATOM   2419  CB  ASP A 327      26.093  79.246  70.104  1.00  0.00           C  
ATOM   2420  CG  ASP A 327      25.136  79.471  68.932  1.00  0.00           C  
ATOM   2421  OD1 ASP A 327      25.408  80.372  68.110  1.00  0.00           O  
ATOM   2422  OD2 ASP A 327      24.084  78.797  68.929  1.00  0.00           O1-
ATOM   2423  N   ILE A 328      28.825  78.187  71.370  1.00 39.27           N  
ATOM   2424  CA  ILE A 328      29.697  77.805  72.482  1.00 40.92           C  
ATOM   2425  C   ILE A 328      31.011  78.610  72.485  1.00 41.24           C  
ATOM   2426  O   ILE A 328      31.369  79.179  73.518  1.00 41.36           O  
ATOM   2427  CB  ILE A 328      29.990  76.269  72.482  1.00  0.00           C  
ATOM   2428  CG1 ILE A 328      28.738  75.484  72.935  1.00  0.00           C  
ATOM   2429  CG2 ILE A 328      31.217  75.803  73.301  1.00  0.00           C  
ATOM   2430  CD1 ILE A 328      28.759  73.995  72.548  1.00  0.00           C  
ATOM   2431  N   LEU A 329      31.684  78.660  71.326  1.00 40.73           N  
ATOM   2432  CA  LEU A 329      32.945  79.347  71.195  1.00 40.44           C  
ATOM   2433  C   LEU A 329      32.841  80.843  71.407  1.00 41.42           C  
ATOM   2434  O   LEU A 329      33.630  81.401  72.166  1.00 41.68           O  
ATOM   2435  CB  LEU A 329      33.577  79.052  69.831  1.00 39.01           C  
ATOM   2436  CG  LEU A 329      34.089  77.622  69.653  1.00 37.66           C  
ATOM   2437  CD1 LEU A 329      34.734  77.475  68.295  1.00 36.59           C  
ATOM   2438  CD2 LEU A 329      35.090  77.297  70.747  1.00 37.92           C  
ATOM   2439  N   SER A 330      31.883  81.505  70.765  1.00 41.86           N  
ATOM   2440  CA  SER A 330      31.794  82.947  70.936  1.00 43.88           C  
ATOM   2441  C   SER A 330      31.466  83.370  72.373  1.00 44.97           C  
ATOM   2442  O   SER A 330      31.871  84.446  72.810  1.00 43.86           O  
ATOM   2443  CB  SER A 330      30.798  83.562  69.943  1.00 43.36           C  
ATOM   2444  OG  SER A 330      29.486  83.118  70.179  1.00 46.56           O  
ATOM   2445  N   SER A 331      30.676  82.533  73.063  1.00 47.41           N  
ATOM   2446  CA  SER A 331      30.356  82.689  74.473  1.00 50.33           C  
ATOM   2447  C   SER A 331      31.625  82.599  75.345  1.00 51.39           C  
ATOM   2448  O   SER A 331      31.542  82.894  76.538  1.00 51.97           O  
ATOM   2449  CB  SER A 331      29.277  81.656  74.871  1.00  0.00           C  
ATOM   2450  OG  SER A 331      28.766  81.889  76.174  1.00  0.00           O  
ATOM   2451  N   LYS A 332      32.761  82.210  74.740  1.00 51.19           N  
ATOM   2452  CA  LYS A 332      34.029  82.066  75.423  1.00 50.25           C  
ATOM   2453  C   LYS A 332      35.111  82.975  74.872  1.00 50.19           C  
ATOM   2454  O   LYS A 332      36.296  82.657  74.917  1.00 50.27           O  
ATOM   2455  CB  LYS A 332      34.484  80.610  75.386  1.00 50.83           C  
ATOM   2456  CG  LYS A 332      33.813  79.777  76.445  1.00 51.82           C  
ATOM   2457  CD  LYS A 332      34.470  78.429  76.602  1.00 52.63           C  
ATOM   2458  CE  LYS A 332      34.022  77.791  77.913  1.00 53.70           C  
ATOM   2459  NZ  LYS A 332      32.534  77.793  78.032  1.00 53.04           N1+
ATOM   2460  N   GLY A 333      34.696  84.107  74.278  1.00 50.26           N  
ATOM   2461  CA  GLY A 333      35.595  85.183  73.849  1.00 50.76           C  
ATOM   2462  C   GLY A 333      36.431  84.836  72.606  1.00 49.90           C  
ATOM   2463  O   GLY A 333      37.571  85.286  72.506  1.00 49.87           O  
ATOM   2464  N   PHE A 334      35.876  84.072  71.656  1.00 48.11           N  
ATOM   2465  CA  PHE A 334      36.540  83.686  70.433  1.00 45.36           C  
ATOM   2466  C   PHE A 334      35.629  84.287  69.392  1.00 44.31           C  
ATOM   2467  O   PHE A 334      34.458  83.918  69.314  1.00 44.53           O  
ATOM   2468  CB  PHE A 334      36.591  82.173  70.285  1.00 44.90           C  
ATOM   2469  CG  PHE A 334      37.624  81.521  71.149  1.00 44.42           C  
ATOM   2470  CD1 PHE A 334      37.250  80.729  72.227  1.00 44.75           C  
ATOM   2471  CD2 PHE A 334      38.976  81.700  70.884  1.00 44.06           C  
ATOM   2472  CE1 PHE A 334      38.212  80.120  73.031  1.00 45.19           C  
ATOM   2473  CE2 PHE A 334      39.947  81.099  71.678  1.00 43.94           C  
ATOM   2474  CZ  PHE A 334      39.568  80.308  72.751  1.00 44.90           C  
ATOM   2475  N   PRO A 335      36.128  85.274  68.622  1.00 43.38           N  
ATOM   2476  CA  PRO A 335      35.310  85.908  67.581  1.00 41.91           C  
ATOM   2477  C   PRO A 335      34.991  84.799  66.582  1.00 40.95           C  
ATOM   2478  O   PRO A 335      35.801  84.481  65.716  1.00 39.38           O  
ATOM   2479  CB  PRO A 335      36.248  86.958  66.994  1.00 42.51           C  
ATOM   2480  CG  PRO A 335      37.191  87.250  68.120  1.00 43.18           C  
ATOM   2481  CD  PRO A 335      37.464  85.888  68.680  1.00 43.02           C  
ATOM   2482  N   ALA A 336      33.809  84.181  66.681  1.00 40.21           N  
ATOM   2483  CA  ALA A 336      33.459  82.938  65.993  1.00 39.79           C  
ATOM   2484  C   ALA A 336      32.100  83.071  65.303  1.00 38.98           C  
ATOM   2485  O   ALA A 336      31.268  83.867  65.739  1.00 39.27           O  
ATOM   2486  CB  ALA A 336      33.451  81.775  67.003  1.00  0.00           C  
ATOM   2487  N   GLU A 337      31.913  82.285  64.240  1.00 37.54           N  
ATOM   2488  CA  GLU A 337      30.738  82.301  63.377  1.00 36.97           C  
ATOM   2489  C   GLU A 337      30.548  80.898  62.780  1.00 36.20           C  
ATOM   2490  O   GLU A 337      31.529  80.159  62.660  1.00 35.77           O  
ATOM   2491  CB  GLU A 337      30.966  83.400  62.311  1.00  0.00           C  
ATOM   2492  CG  GLU A 337      29.945  83.553  61.169  1.00  0.00           C  
ATOM   2493  CD  GLU A 337      28.568  84.032  61.618  1.00  0.00           C  
ATOM   2494  OE1 GLU A 337      28.186  85.140  61.177  1.00  0.00           O  
ATOM   2495  OE2 GLU A 337      27.921  83.289  62.385  1.00  0.00           O1-
ATOM   2496  N   CYS A 338      29.306  80.567  62.417  1.00 35.26           N  
ATOM   2497  CA  CYS A 338      28.920  79.328  61.745  1.00 34.55           C  
ATOM   2498  C   CYS A 338      28.447  79.638  60.321  1.00 33.07           C  
ATOM   2499  O   CYS A 338      27.764  80.641  60.109  1.00 33.45           O  
ATOM   2500  CB  CYS A 338      27.807  78.562  62.499  1.00  0.00           C  
ATOM   2501  SG  CYS A 338      26.394  79.617  62.963  1.00  0.00           S  
ATOM   2502  N   ILE A 339      28.724  78.712  59.404  1.00 31.33           N  
ATOM   2503  CA  ILE A 339      28.101  78.646  58.090  1.00 30.75           C  
ATOM   2504  C   ILE A 339      27.683  77.197  57.813  1.00 31.00           C  
ATOM   2505  O   ILE A 339      28.340  76.269  58.280  1.00 31.32           O  
ATOM   2506  CB  ILE A 339      29.040  79.159  56.968  1.00 29.51           C  
ATOM   2507  CG1 ILE A 339      30.422  78.469  56.930  1.00 28.38           C  
ATOM   2508  CG2 ILE A 339      29.187  80.672  57.104  1.00 29.21           C  
ATOM   2509  CD1 ILE A 339      31.457  79.158  56.031  1.00 29.44           C  
ATOM   2510  N   SER A 340      26.565  77.047  57.102  1.00 30.13           N  
ATOM   2511  CA  SER A 340      25.936  75.789  56.732  1.00 30.97           C  
ATOM   2512  C   SER A 340      24.702  76.142  55.882  1.00 31.36           C  
ATOM   2513  O   SER A 340      24.247  77.290  55.893  1.00 30.53           O  
ATOM   2514  CB  SER A 340      25.575  74.958  57.995  1.00  0.00           C  
ATOM   2515  OG  SER A 340      24.801  73.807  57.706  1.00  0.00           O  
ATOM   2516  N   GLY A 341      24.175  75.132  55.189  1.00 32.09           N  
ATOM   2517  CA  GLY A 341      22.932  75.091  54.431  1.00 33.42           C  
ATOM   2518  C   GLY A 341      21.690  75.466  55.257  1.00 34.38           C  
ATOM   2519  O   GLY A 341      20.680  75.840  54.665  1.00 35.12           O  
ATOM   2520  N   ASN A 342      21.739  75.394  56.600  1.00 36.13           N  
ATOM   2521  CA  ASN A 342      20.636  75.846  57.457  1.00 37.27           C  
ATOM   2522  C   ASN A 342      20.643  77.372  57.694  1.00 37.19           C  
ATOM   2523  O   ASN A 342      19.621  77.908  58.123  1.00 37.65           O  
ATOM   2524  CB  ASN A 342      20.569  75.044  58.782  1.00  0.00           C  
ATOM   2525  CG  ASN A 342      21.433  75.577  59.932  1.00  0.00           C  
ATOM   2526  OD1 ASN A 342      22.611  75.857  59.743  1.00  0.00           O  
ATOM   2527  ND2 ASN A 342      20.854  75.710  61.121  1.00  0.00           N  
ATOM   2528  N   MET A 343      21.776  78.040  57.443  1.00 36.16           N  
ATOM   2529  CA  MET A 343      21.883  79.493  57.525  1.00 36.82           C  
ATOM   2530  C   MET A 343      21.307  80.110  56.245  1.00 37.02           C  
ATOM   2531  O   MET A 343      21.437  79.524  55.165  1.00 36.75           O  
ATOM   2532  CB  MET A 343      23.356  79.923  57.699  1.00  0.00           C  
ATOM   2533  CG  MET A 343      24.044  79.414  58.976  1.00  0.00           C  
ATOM   2534  SD  MET A 343      23.462  80.182  60.513  1.00  0.00           S  
ATOM   2535  CE  MET A 343      22.461  78.839  61.206  1.00  0.00           C  
ATOM   2536  N   ASN A 344      20.802  81.351  56.293  1.00 37.02           N  
ATOM   2537  CA  ASN A 344      20.445  82.098  55.071  1.00 37.01           C  
ATOM   2538  C   ASN A 344      21.691  82.320  54.188  1.00 36.06           C  
ATOM   2539  O   ASN A 344      22.769  82.575  54.721  1.00 36.14           O  
ATOM   2540  CB  ASN A 344      19.764  83.438  55.442  1.00  0.00           C  
ATOM   2541  CG  ASN A 344      19.340  84.284  54.233  1.00  0.00           C  
ATOM   2542  OD1 ASN A 344      20.164  84.957  53.616  1.00  0.00           O  
ATOM   2543  ND2 ASN A 344      18.059  84.273  53.883  1.00  0.00           N  
ATOM   2544  N   GLN A 345      21.522  82.246  52.864  1.00 35.55           N  
ATOM   2545  CA  GLN A 345      22.551  82.408  51.837  1.00 34.78           C  
ATOM   2546  C   GLN A 345      23.454  83.634  52.060  1.00 34.79           C  
ATOM   2547  O   GLN A 345      24.675  83.505  51.995  1.00 35.07           O  
ATOM   2548  CB  GLN A 345      21.899  82.465  50.435  1.00 34.33           C  
ATOM   2549  CG  GLN A 345      21.152  81.184  49.995  1.00 35.13           C  
ATOM   2550  CD  GLN A 345      19.676  81.130  50.410  1.00 34.87           C  
ATOM   2551  OE1 GLN A 345      19.284  81.658  51.447  1.00 34.43           O  
ATOM   2552  NE2 GLN A 345      18.839  80.474  49.622  1.00 34.17           N  
ATOM   2553  N   ASN A 346      22.848  84.777  52.405  1.00 34.30           N  
ATOM   2554  CA  ASN A 346      23.582  86.025  52.635  1.00 34.02           C  
ATOM   2555  C   ASN A 346      24.297  86.023  53.994  1.00 33.32           C  
ATOM   2556  O   ASN A 346      25.314  86.698  54.103  1.00 34.13           O  
ATOM   2557  CB  ASN A 346      22.665  87.261  52.483  1.00  0.00           C  
ATOM   2558  CG  ASN A 346      22.336  87.642  51.033  1.00  0.00           C  
ATOM   2559  OD1 ASN A 346      22.461  86.847  50.103  1.00  0.00           O  
ATOM   2560  ND2 ASN A 346      21.883  88.872  50.816  1.00  0.00           N  
ATOM   2561  N   GLN A 347      23.840  85.235  54.981  1.00 32.75           N  
ATOM   2562  CA  GLN A 347      24.582  85.029  56.233  1.00 33.37           C  
ATOM   2563  C   GLN A 347      25.884  84.250  55.994  1.00 32.59           C  
ATOM   2564  O   GLN A 347      26.890  84.564  56.624  1.00 31.20           O  
ATOM   2565  CB  GLN A 347      23.726  84.320  57.301  1.00 35.41           C  
ATOM   2566  CG  GLN A 347      22.518  85.144  57.783  1.00 37.62           C  
ATOM   2567  CD  GLN A 347      21.595  84.328  58.691  1.00 38.98           C  
ATOM   2568  OE1 GLN A 347      21.294  83.168  58.410  1.00 39.69           O  
ATOM   2569  NE2 GLN A 347      21.097  84.931  59.766  1.00 39.63           N  
ATOM   2570  N   ARG A 348      25.862  83.297  55.048  1.00 33.21           N  
ATOM   2571  CA  ARG A 348      27.058  82.587  54.585  1.00 32.92           C  
ATOM   2572  C   ARG A 348      28.055  83.558  53.929  1.00 33.88           C  
ATOM   2573  O   ARG A 348      29.231  83.563  54.287  1.00 35.03           O  
ATOM   2574  CB  ARG A 348      26.712  81.426  53.625  1.00 31.73           C  
ATOM   2575  CG  ARG A 348      25.531  80.538  54.057  1.00 30.36           C  
ATOM   2576  CD  ARG A 348      25.137  79.537  52.963  1.00 29.42           C  
ATOM   2577  NE  ARG A 348      23.760  79.053  53.133  1.00 29.38           N  
ATOM   2578  CZ  ARG A 348      23.195  78.054  52.442  1.00 29.71           C  
ATOM   2579  NH1 ARG A 348      23.920  77.307  51.599  1.00 28.07           N  
ATOM   2580  NH2 ARG A 348      21.891  77.823  52.611  1.00 29.44           N1+
ATOM   2581  N   LEU A 349      27.539  84.420  53.040  1.00 34.65           N  
ATOM   2582  CA  LEU A 349      28.307  85.483  52.392  1.00 35.61           C  
ATOM   2583  C   LEU A 349      28.893  86.482  53.405  1.00 35.93           C  
ATOM   2584  O   LEU A 349      30.091  86.759  53.327  1.00 35.03           O  
ATOM   2585  CB  LEU A 349      27.454  86.202  51.327  1.00  0.00           C  
ATOM   2586  CG  LEU A 349      27.003  85.306  50.150  1.00  0.00           C  
ATOM   2587  CD1 LEU A 349      25.910  86.001  49.312  1.00  0.00           C  
ATOM   2588  CD2 LEU A 349      28.191  84.819  49.289  1.00  0.00           C  
ATOM   2589  N   ASP A 350      28.083  86.951  54.373  1.00 36.71           N  
ATOM   2590  CA  ASP A 350      28.575  87.805  55.456  1.00 37.45           C  
ATOM   2591  C   ASP A 350      29.616  87.105  56.338  1.00 37.47           C  
ATOM   2592  O   ASP A 350      30.562  87.764  56.765  1.00 37.37           O  
ATOM   2593  CB  ASP A 350      27.472  88.418  56.354  1.00  0.00           C  
ATOM   2594  CG  ASP A 350      26.428  89.274  55.634  1.00  0.00           C  
ATOM   2595  OD1 ASP A 350      26.711  89.742  54.511  1.00  0.00           O  
ATOM   2596  OD2 ASP A 350      25.379  89.519  56.265  1.00  0.00           O1-
ATOM   2597  N   ALA A 351      29.433  85.823  56.656  1.00 36.04           N  
ATOM   2598  CA  ALA A 351      30.376  85.061  57.469  1.00 36.44           C  
ATOM   2599  C   ALA A 351      31.743  84.900  56.788  1.00 37.05           C  
ATOM   2600  O   ALA A 351      32.770  85.132  57.428  1.00 36.14           O  
ATOM   2601  CB  ALA A 351      29.764  83.708  57.795  1.00 36.92           C  
ATOM   2602  N   MET A 352      31.723  84.589  55.486  1.00 38.58           N  
ATOM   2603  CA  MET A 352      32.917  84.549  54.645  1.00 40.08           C  
ATOM   2604  C   MET A 352      33.592  85.930  54.536  1.00 41.32           C  
ATOM   2605  O   MET A 352      34.804  86.013  54.734  1.00 41.04           O  
ATOM   2606  CB  MET A 352      32.589  83.947  53.262  1.00  0.00           C  
ATOM   2607  CG  MET A 352      32.242  82.443  53.284  1.00  0.00           C  
ATOM   2608  SD  MET A 352      33.508  81.339  53.974  1.00  0.00           S  
ATOM   2609  CE  MET A 352      34.882  81.600  52.830  1.00  0.00           C  
ATOM   2610  N   ALA A 353      32.809  87.000  54.307  1.00 43.59           N  
ATOM   2611  CA  ALA A 353      33.286  88.382  54.307  1.00 46.09           C  
ATOM   2612  C   ALA A 353      33.955  88.779  55.635  1.00 46.44           C  
ATOM   2613  O   ALA A 353      35.054  89.334  55.607  1.00 46.73           O  
ATOM   2614  CB  ALA A 353      32.137  89.337  53.957  1.00  0.00           C  
ATOM   2615  N   LYS A 354      33.324  88.432  56.765  1.00 46.26           N  
ATOM   2616  CA  LYS A 354      33.886  88.613  58.100  1.00 46.00           C  
ATOM   2617  C   LYS A 354      35.202  87.847  58.327  1.00 45.99           C  
ATOM   2618  O   LYS A 354      36.114  88.415  58.924  1.00 45.51           O  
ATOM   2619  CB  LYS A 354      32.855  88.243  59.188  1.00  0.00           C  
ATOM   2620  CG  LYS A 354      31.747  89.289  59.420  1.00  0.00           C  
ATOM   2621  CD  LYS A 354      30.903  89.022  60.684  1.00  0.00           C  
ATOM   2622  CE  LYS A 354      30.115  87.696  60.712  1.00  0.00           C  
ATOM   2623  NZ  LYS A 354      29.032  87.658  59.718  1.00  0.00           N1+
ATOM   2624  N   LEU A 355      35.294  86.590  57.874  1.00 45.83           N  
ATOM   2625  CA  LEU A 355      36.500  85.768  58.033  1.00 45.89           C  
ATOM   2626  C   LEU A 355      37.685  86.312  57.211  1.00 46.04           C  
ATOM   2627  O   LEU A 355      38.798  86.377  57.733  1.00 46.16           O  
ATOM   2628  CB  LEU A 355      36.162  84.285  57.730  1.00  0.00           C  
ATOM   2629  CG  LEU A 355      37.224  83.223  58.123  1.00  0.00           C  
ATOM   2630  CD1 LEU A 355      38.421  83.121  57.157  1.00  0.00           C  
ATOM   2631  CD2 LEU A 355      37.656  83.301  59.600  1.00  0.00           C  
ATOM   2632  N   LYS A 356      37.410  86.700  55.957  1.00 46.38           N  
ATOM   2633  CA  LYS A 356      38.403  87.233  55.024  1.00 47.30           C  
ATOM   2634  C   LYS A 356      39.031  88.558  55.501  1.00 47.32           C  
ATOM   2635  O   LYS A 356      40.221  88.773  55.283  1.00 47.36           O  
ATOM   2636  CB  LYS A 356      37.773  87.374  53.618  1.00 47.87           C  
ATOM   2637  CG  LYS A 356      37.508  86.023  52.919  1.00 49.03           C  
ATOM   2638  CD  LYS A 356      36.896  86.164  51.513  1.00 51.01           C  
ATOM   2639  CE  LYS A 356      36.987  84.868  50.685  1.00 52.01           C  
ATOM   2640  NZ  LYS A 356      38.368  84.605  50.252  1.00 52.91           N1+
ATOM   2641  N   HIS A 357      38.240  89.402  56.178  1.00 47.75           N  
ATOM   2642  CA  HIS A 357      38.680  90.713  56.670  1.00 47.81           C  
ATOM   2643  C   HIS A 357      39.152  90.692  58.136  1.00 48.66           C  
ATOM   2644  O   HIS A 357      39.350  91.762  58.705  1.00 49.71           O  
ATOM   2645  CB  HIS A 357      37.581  91.771  56.440  1.00  0.00           C  
ATOM   2646  CG  HIS A 357      37.259  92.035  54.990  1.00  0.00           C  
ATOM   2647  ND1 HIS A 357      36.331  91.295  54.284  1.00  0.00           N  
ATOM   2648  CD2 HIS A 357      37.723  92.980  54.102  1.00  0.00           C  
ATOM   2649  CE1 HIS A 357      36.275  91.781  53.044  1.00  0.00           C  
ATOM   2650  NE2 HIS A 357      37.097  92.808  52.863  1.00  0.00           N  
ATOM   2651  N   PHE A 358      39.349  89.502  58.727  1.00 48.72           N  
ATOM   2652  CA  PHE A 358      39.872  89.283  60.089  1.00 48.37           C  
ATOM   2653  C   PHE A 358      38.846  89.680  61.183  1.00 48.66           C  
ATOM   2654  O   PHE A 358      39.223  89.847  62.341  1.00 49.33           O  
ATOM   2655  CB  PHE A 358      41.232  90.015  60.352  1.00  0.00           C  
ATOM   2656  CG  PHE A 358      42.474  89.788  59.485  1.00  0.00           C  
ATOM   2657  CD1 PHE A 358      42.430  89.337  58.144  1.00  0.00           C  
ATOM   2658  CD2 PHE A 358      43.713  90.248  59.987  1.00  0.00           C  
ATOM   2659  CE1 PHE A 358      43.581  89.324  57.366  1.00  0.00           C  
ATOM   2660  CE2 PHE A 358      44.853  90.231  59.194  1.00  0.00           C  
ATOM   2661  CZ  PHE A 358      44.789  89.765  57.888  1.00  0.00           C  
ATOM   2662  N   HIS A 359      37.562  89.847  60.830  1.00 49.10           N  
ATOM   2663  CA  HIS A 359      36.496  90.196  61.776  1.00 49.05           C  
ATOM   2664  C   HIS A 359      36.095  88.956  62.589  1.00 49.05           C  
ATOM   2665  O   HIS A 359      36.051  89.010  63.817  1.00 49.54           O  
ATOM   2666  CB  HIS A 359      35.257  90.780  61.059  1.00  0.00           C  
ATOM   2667  CG  HIS A 359      35.477  91.928  60.099  1.00  0.00           C  
ATOM   2668  ND1 HIS A 359      34.489  92.362  59.227  1.00  0.00           N  
ATOM   2669  CD2 HIS A 359      36.555  92.753  59.865  1.00  0.00           C  
ATOM   2670  CE1 HIS A 359      34.986  93.385  58.528  1.00  0.00           C  
ATOM   2671  NE2 HIS A 359      36.236  93.674  58.864  1.00  0.00           N  
ATOM   2672  N   CYS A 360      35.871  87.840  61.887  1.00 48.39           N  
ATOM   2673  CA  CYS A 360      35.766  86.519  62.496  1.00 46.94           C  
ATOM   2674  C   CYS A 360      37.175  85.933  62.505  1.00 45.45           C  
ATOM   2675  O   CYS A 360      37.873  85.990  61.493  1.00 45.49           O  
ATOM   2676  CB  CYS A 360      34.796  85.587  61.753  1.00  0.00           C  
ATOM   2677  SG  CYS A 360      33.107  86.152  62.084  1.00  0.00           S  
ATOM   2678  N   ARG A 361      37.576  85.410  63.663  1.00 43.36           N  
ATOM   2679  CA  ARG A 361      38.883  84.796  63.849  1.00 42.05           C  
ATOM   2680  C   ARG A 361      38.807  83.280  63.594  1.00 40.02           C  
ATOM   2681  O   ARG A 361      39.797  82.673  63.176  1.00 39.51           O  
ATOM   2682  CB  ARG A 361      39.372  85.114  65.273  1.00  0.00           C  
ATOM   2683  CG  ARG A 361      39.953  86.532  65.494  1.00  0.00           C  
ATOM   2684  CD  ARG A 361      39.226  87.763  64.918  1.00  0.00           C  
ATOM   2685  NE  ARG A 361      39.881  88.991  65.394  1.00  0.00           N  
ATOM   2686  CZ  ARG A 361      39.326  90.199  65.573  1.00  0.00           C  
ATOM   2687  NH1 ARG A 361      38.027  90.423  65.350  1.00  0.00           N  
ATOM   2688  NH2 ARG A 361      40.093  91.206  65.999  1.00  0.00           N1+
ATOM   2689  N   VAL A 362      37.629  82.714  63.877  1.00 37.87           N  
ATOM   2690  CA  VAL A 362      37.320  81.302  63.778  1.00 35.57           C  
ATOM   2691  C   VAL A 362      36.058  81.098  62.956  1.00 35.09           C  
ATOM   2692  O   VAL A 362      35.061  81.784  63.169  1.00 34.69           O  
ATOM   2693  CB  VAL A 362      37.131  80.717  65.180  1.00 35.71           C  
ATOM   2694  CG1 VAL A 362      36.762  79.245  65.106  1.00 34.62           C  
ATOM   2695  CG2 VAL A 362      38.412  80.915  65.985  1.00 35.37           C  
ATOM   2696  N   LEU A 363      36.079  80.172  62.000  1.00 33.87           N  
ATOM   2697  CA  LEU A 363      34.920  79.875  61.167  1.00 32.38           C  
ATOM   2698  C   LEU A 363      34.567  78.417  61.429  1.00 30.74           C  
ATOM   2699  O   LEU A 363      35.452  77.571  61.286  1.00 30.23           O  
ATOM   2700  CB  LEU A 363      35.309  80.143  59.701  1.00 32.83           C  
ATOM   2701  CG  LEU A 363      34.188  79.961  58.657  1.00 33.97           C  
ATOM   2702  CD1 LEU A 363      33.005  80.930  58.891  1.00 32.56           C  
ATOM   2703  CD2 LEU A 363      34.773  80.072  57.233  1.00 33.16           C  
ATOM   2704  N   ILE A 364      33.328  78.158  61.858  1.00 29.49           N  
ATOM   2705  CA  ILE A 364      32.869  76.788  62.084  1.00 27.88           C  
ATOM   2706  C   ILE A 364      32.069  76.423  60.845  1.00 27.16           C  
ATOM   2707  O   ILE A 364      31.240  77.212  60.397  1.00 27.43           O  
ATOM   2708  CB  ILE A 364      31.970  76.674  63.338  1.00 27.74           C  
ATOM   2709  CG1 ILE A 364      32.698  77.249  64.556  1.00 25.87           C  
ATOM   2710  CG2 ILE A 364      31.609  75.211  63.580  1.00 25.99           C  
ATOM   2711  CD1 ILE A 364      34.058  76.601  64.836  1.00 22.88           C  
ATOM   2712  N   SER A 365      32.257  75.243  60.239  1.00 25.26           N  
ATOM   2713  CA  SER A 365      31.514  74.870  59.021  1.00 24.81           C  
ATOM   2714  C   SER A 365      31.168  73.370  58.963  1.00 24.51           C  
ATOM   2715  O   SER A 365      31.696  72.577  59.739  1.00 25.39           O  
ATOM   2716  CB  SER A 365      32.267  75.389  57.766  1.00  0.00           C  
ATOM   2717  OG  SER A 365      31.487  75.254  56.588  1.00  0.00           O  
ATOM   2718  N   THR A 366      30.271  73.031  58.038  1.00 23.66           N  
ATOM   2719  CA  THR A 366      29.971  71.717  57.492  1.00 23.16           C  
ATOM   2720  C   THR A 366      30.805  71.533  56.195  1.00 23.83           C  
ATOM   2721  O   THR A 366      31.703  72.330  55.899  1.00 23.50           O  
ATOM   2722  CB  THR A 366      28.460  71.695  57.121  1.00 23.05           C  
ATOM   2723  OG1 THR A 366      28.158  72.768  56.234  1.00 22.32           O  
ATOM   2724  CG2 THR A 366      27.553  71.790  58.353  1.00 22.13           C  
ATOM   2725  N   ASP A 367      30.506  70.523  55.364  1.00 24.00           N  
ATOM   2726  CA  ASP A 367      31.148  70.372  54.051  1.00 25.16           C  
ATOM   2727  C   ASP A 367      30.726  71.399  52.979  1.00 25.32           C  
ATOM   2728  O   ASP A 367      31.247  71.330  51.864  1.00 25.96           O  
ATOM   2729  CB  ASP A 367      31.247  68.917  53.542  1.00  0.00           C  
ATOM   2730  CG  ASP A 367      32.101  68.063  54.468  1.00  0.00           C  
ATOM   2731  OD1 ASP A 367      33.337  68.195  54.354  1.00  0.00           O  
ATOM   2732  OD2 ASP A 367      31.538  67.320  55.299  1.00  0.00           O1-
ATOM   2733  N   LEU A 368      29.907  72.397  53.341  1.00 24.75           N  
ATOM   2734  CA  LEU A 368      29.609  73.599  52.554  1.00 23.32           C  
ATOM   2735  C   LEU A 368      30.883  74.328  52.060  1.00 23.01           C  
ATOM   2736  O   LEU A 368      30.965  74.717  50.893  1.00 23.67           O  
ATOM   2737  CB  LEU A 368      28.731  74.533  53.422  1.00  0.00           C  
ATOM   2738  CG  LEU A 368      28.272  75.863  52.775  1.00  0.00           C  
ATOM   2739  CD1 LEU A 368      27.240  75.653  51.649  1.00  0.00           C  
ATOM   2740  CD2 LEU A 368      27.782  76.856  53.842  1.00  0.00           C  
ATOM   2741  N   THR A 369      31.862  74.468  52.959  1.00 24.75           N  
ATOM   2742  CA  THR A 369      33.098  75.224  52.734  1.00 25.22           C  
ATOM   2743  C   THR A 369      34.325  74.297  52.562  1.00 26.01           C  
ATOM   2744  O   THR A 369      35.464  74.758  52.572  1.00 25.69           O  
ATOM   2745  CB  THR A 369      33.348  76.187  53.929  1.00  0.00           C  
ATOM   2746  OG1 THR A 369      32.104  76.715  54.355  1.00  0.00           O  
ATOM   2747  CG2 THR A 369      34.242  77.400  53.627  1.00  0.00           C  
ATOM   2748  N   SER A 370      34.083  72.986  52.429  1.00 26.50           N  
ATOM   2749  CA  SER A 370      35.120  71.958  52.311  1.00 27.64           C  
ATOM   2750  C   SER A 370      35.868  72.003  50.974  1.00 26.69           C  
ATOM   2751  O   SER A 370      37.043  71.656  50.938  1.00 27.27           O  
ATOM   2752  CB  SER A 370      34.474  70.588  52.611  1.00 28.85           C  
ATOM   2753  OG  SER A 370      35.154  69.430  52.172  1.00 32.91           O  
ATOM   2754  N   ARG A 371      35.192  72.417  49.899  1.00 26.02           N  
ATOM   2755  CA  ARG A 371      35.713  72.353  48.539  1.00 26.03           C  
ATOM   2756  C   ARG A 371      35.783  73.770  47.959  1.00 27.38           C  
ATOM   2757  O   ARG A 371      35.077  74.642  48.462  1.00 27.24           O  
ATOM   2758  CB  ARG A 371      34.811  71.426  47.680  1.00 25.57           C  
ATOM   2759  CG  ARG A 371      34.353  70.136  48.398  1.00 29.98           C  
ATOM   2760  CD  ARG A 371      32.954  70.206  49.061  1.00 29.97           C  
ATOM   2761  NE  ARG A 371      31.867  69.981  48.090  1.00 34.26           N  
ATOM   2762  CZ  ARG A 371      30.548  69.972  48.352  1.00 33.11           C  
ATOM   2763  NH1 ARG A 371      30.058  70.375  49.527  1.00 32.49           N  
ATOM   2764  NH2 ARG A 371      29.689  69.532  47.428  1.00 33.61           N1+
ATOM   2765  N   GLY A 372      36.601  73.944  46.911  1.00 28.38           N  
ATOM   2766  CA  GLY A 372      36.718  75.077  45.974  1.00 30.23           C  
ATOM   2767  C   GLY A 372      36.947  76.495  46.540  1.00 30.72           C  
ATOM   2768  O   GLY A 372      37.496  77.333  45.830  1.00 31.53           O  
ATOM   2769  N   ILE A 373      36.550  76.789  47.781  1.00 30.89           N  
ATOM   2770  CA  ILE A 373      36.750  78.068  48.458  1.00 31.66           C  
ATOM   2771  C   ILE A 373      38.239  78.336  48.746  1.00 32.36           C  
ATOM   2772  O   ILE A 373      38.923  77.451  49.267  1.00 32.42           O  
ATOM   2773  CB  ILE A 373      35.902  78.129  49.774  1.00  0.00           C  
ATOM   2774  CG1 ILE A 373      34.454  78.562  49.456  1.00  0.00           C  
ATOM   2775  CG2 ILE A 373      36.465  78.957  50.954  1.00  0.00           C  
ATOM   2776  CD1 ILE A 373      34.320  80.033  49.016  1.00  0.00           C  
ATOM   2777  N   ASP A 374      38.690  79.558  48.446  1.00 33.36           N  
ATOM   2778  CA  ASP A 374      40.064  80.005  48.634  1.00 34.49           C  
ATOM   2779  C   ASP A 374      40.028  81.189  49.608  1.00 35.41           C  
ATOM   2780  O   ASP A 374      40.239  82.347  49.244  1.00 34.20           O  
ATOM   2781  CB  ASP A 374      40.756  80.335  47.294  1.00 35.82           C  
ATOM   2782  CG  ASP A 374      42.267  80.142  47.391  1.00 37.33           C  
ATOM   2783  OD1 ASP A 374      42.801  79.485  46.477  1.00 38.87           O  
ATOM   2784  OD2 ASP A 374      42.871  80.572  48.395  1.00 37.92           O1-
ATOM   2785  N   ALA A 375      39.733  80.860  50.868  1.00 36.68           N  
ATOM   2786  CA  ALA A 375      39.868  81.773  51.987  1.00 37.65           C  
ATOM   2787  C   ALA A 375      41.352  81.899  52.365  1.00 38.87           C  
ATOM   2788  O   ALA A 375      41.862  81.098  53.143  1.00 38.60           O  
ATOM   2789  CB  ALA A 375      38.972  81.295  53.134  1.00  0.00           C  
ATOM   2790  N   GLU A 376      42.002  82.918  51.791  1.00 40.87           N  
ATOM   2791  CA  GLU A 376      43.383  83.374  51.995  1.00 42.59           C  
ATOM   2792  C   GLU A 376      43.907  83.311  53.444  1.00 42.60           C  
ATOM   2793  O   GLU A 376      45.080  83.019  53.663  1.00 43.11           O  
ATOM   2794  CB  GLU A 376      43.505  84.823  51.443  1.00  0.00           C  
ATOM   2795  CG  GLU A 376      42.790  85.985  52.180  1.00  0.00           C  
ATOM   2796  CD  GLU A 376      41.278  85.825  52.277  1.00  0.00           C  
ATOM   2797  OE1 GLU A 376      40.596  86.143  51.281  1.00  0.00           O  
ATOM   2798  OE2 GLU A 376      40.834  85.296  53.318  1.00  0.00           O1-
ATOM   2799  N   LYS A 377      43.021  83.619  54.393  1.00 42.12           N  
ATOM   2800  CA  LYS A 377      43.288  83.742  55.817  1.00 41.87           C  
ATOM   2801  C   LYS A 377      43.432  82.390  56.554  1.00 41.92           C  
ATOM   2802  O   LYS A 377      43.828  82.376  57.720  1.00 42.75           O  
ATOM   2803  CB  LYS A 377      42.139  84.613  56.383  1.00  0.00           C  
ATOM   2804  CG  LYS A 377      42.273  85.062  57.844  1.00  0.00           C  
ATOM   2805  CD  LYS A 377      43.578  85.824  58.103  1.00  0.00           C  
ATOM   2806  CE  LYS A 377      43.658  86.336  59.534  1.00  0.00           C  
ATOM   2807  NZ  LYS A 377      44.890  87.085  59.776  1.00  0.00           N1+
ATOM   2808  N   VAL A 378      43.076  81.285  55.890  1.00 40.75           N  
ATOM   2809  CA  VAL A 378      43.007  79.945  56.477  1.00 40.16           C  
ATOM   2810  C   VAL A 378      44.415  79.307  56.562  1.00 40.57           C  
ATOM   2811  O   VAL A 378      44.882  78.665  55.622  1.00 41.57           O  
ATOM   2812  CB  VAL A 378      42.008  79.030  55.704  1.00  0.00           C  
ATOM   2813  CG1 VAL A 378      41.930  77.580  56.223  1.00  0.00           C  
ATOM   2814  CG2 VAL A 378      40.588  79.627  55.719  1.00  0.00           C  
ATOM   2815  N   ASN A 379      45.075  79.515  57.705  1.00 40.32           N  
ATOM   2816  CA  ASN A 379      46.340  78.858  58.059  1.00 40.31           C  
ATOM   2817  C   ASN A 379      46.089  77.433  58.582  1.00 38.91           C  
ATOM   2818  O   ASN A 379      46.912  76.542  58.355  1.00 39.95           O  
ATOM   2819  CB  ASN A 379      46.998  79.603  59.233  1.00  0.00           C  
ATOM   2820  CG  ASN A 379      47.655  80.955  59.001  1.00  0.00           C  
ATOM   2821  OD1 ASN A 379      47.574  81.555  57.935  1.00  0.00           O  
ATOM   2822  ND2 ASN A 379      48.261  81.487  60.060  1.00  0.00           N  
ATOM   2823  N   LEU A 380      45.015  77.290  59.372  1.00 37.31           N  
ATOM   2824  CA  LEU A 380      44.696  76.111  60.163  1.00 35.41           C  
ATOM   2825  C   LEU A 380      43.370  75.532  59.688  1.00 34.35           C  
ATOM   2826  O   LEU A 380      42.438  76.288  59.421  1.00 33.70           O  
ATOM   2827  CB  LEU A 380      44.579  76.533  61.648  1.00  0.00           C  
ATOM   2828  CG  LEU A 380      44.088  75.459  62.654  1.00  0.00           C  
ATOM   2829  CD1 LEU A 380      45.032  74.238  62.752  1.00  0.00           C  
ATOM   2830  CD2 LEU A 380      43.768  76.085  64.025  1.00  0.00           C  
ATOM   2831  N   VAL A 381      43.298  74.202  59.678  1.00 33.01           N  
ATOM   2832  CA  VAL A 381      42.075  73.474  59.425  1.00 31.16           C  
ATOM   2833  C   VAL A 381      41.933  72.420  60.481  1.00 31.50           C  
ATOM   2834  O   VAL A 381      42.824  71.586  60.683  1.00 31.56           O  
ATOM   2835  CB  VAL A 381      42.080  72.782  58.051  1.00 30.44           C  
ATOM   2836  CG1 VAL A 381      40.873  71.884  57.937  1.00 28.95           C  
ATOM   2837  CG2 VAL A 381      42.069  73.826  56.928  1.00 29.11           C  
ATOM   2838  N   VAL A 382      40.845  72.465  61.256  1.00 30.77           N  
ATOM   2839  CA  VAL A 382      40.593  71.495  62.320  1.00 30.28           C  
ATOM   2840  C   VAL A 382      39.389  70.643  61.905  1.00 29.81           C  
ATOM   2841  O   VAL A 382      38.304  71.178  61.685  1.00 28.96           O  
ATOM   2842  CB  VAL A 382      40.292  72.172  63.686  1.00  0.00           C  
ATOM   2843  CG1 VAL A 382      39.938  71.184  64.820  1.00  0.00           C  
ATOM   2844  CG2 VAL A 382      41.469  73.056  64.135  1.00  0.00           C  
ATOM   2845  N   ASN A 383      39.572  69.326  61.826  1.00 30.02           N  
ATOM   2846  CA  ASN A 383      38.473  68.414  61.606  1.00 30.23           C  
ATOM   2847  C   ASN A 383      38.000  68.040  63.009  1.00 31.41           C  
ATOM   2848  O   ASN A 383      38.539  67.121  63.640  1.00 31.95           O  
ATOM   2849  CB  ASN A 383      38.925  67.172  60.847  1.00 30.08           C  
ATOM   2850  CG  ASN A 383      39.147  67.444  59.365  1.00 29.69           C  
ATOM   2851  OD1 ASN A 383      38.233  67.869  58.663  1.00 30.24           O  
ATOM   2852  ND2 ASN A 383      40.360  67.198  58.889  1.00 28.58           N  
ATOM   2853  N   LEU A 384      37.066  68.849  63.525  1.00 30.93           N  
ATOM   2854  CA  LEU A 384      36.418  68.593  64.808  1.00 31.95           C  
ATOM   2855  C   LEU A 384      35.679  67.252  64.756  1.00 32.48           C  
ATOM   2856  O   LEU A 384      35.734  66.489  65.718  1.00 31.71           O  
ATOM   2857  CB  LEU A 384      35.577  69.821  65.229  1.00  0.00           C  
ATOM   2858  CG  LEU A 384      34.570  69.714  66.396  1.00  0.00           C  
ATOM   2859  CD1 LEU A 384      33.205  69.134  65.978  1.00  0.00           C  
ATOM   2860  CD2 LEU A 384      35.149  69.059  67.659  1.00  0.00           C  
ATOM   2861  N   ASP A 385      35.116  66.969  63.575  1.00 33.30           N  
ATOM   2862  CA  ASP A 385      34.476  65.697  63.275  1.00 33.95           C  
ATOM   2863  C   ASP A 385      35.142  65.240  61.973  1.00 35.08           C  
ATOM   2864  O   ASP A 385      35.219  66.020  61.006  1.00 35.35           O  
ATOM   2865  CB  ASP A 385      32.969  65.856  63.012  1.00 34.26           C  
ATOM   2866  CG  ASP A 385      32.181  66.233  64.250  1.00 33.90           C  
ATOM   2867  OD1 ASP A 385      32.509  65.729  65.346  1.00 35.18           O  
ATOM   2868  OD2 ASP A 385      31.220  67.018  64.115  1.00 32.01           O1-
ATOM   2869  N   VAL A 386      35.690  64.025  61.949  1.00 35.13           N  
ATOM   2870  CA  VAL A 386      36.307  63.473  60.741  1.00 35.08           C  
ATOM   2871  C   VAL A 386      35.162  63.131  59.763  1.00 34.72           C  
ATOM   2872  O   VAL A 386      34.103  62.695  60.227  1.00 34.60           O  
ATOM   2873  CB  VAL A 386      37.116  62.197  61.104  1.00  0.00           C  
ATOM   2874  CG1 VAL A 386      37.886  61.510  59.962  1.00  0.00           C  
ATOM   2875  CG2 VAL A 386      38.083  62.510  62.254  1.00  0.00           C  
ATOM   2876  N   PRO A 387      35.334  63.404  58.447  1.00 34.79           N  
ATOM   2877  CA  PRO A 387      34.246  63.188  57.491  1.00 34.15           C  
ATOM   2878  C   PRO A 387      34.134  61.675  57.325  1.00 34.12           C  
ATOM   2879  O   PRO A 387      35.004  60.939  57.784  1.00 33.49           O  
ATOM   2880  CB  PRO A 387      34.771  63.851  56.230  1.00 34.38           C  
ATOM   2881  CG  PRO A 387      36.220  63.504  56.294  1.00 33.87           C  
ATOM   2882  CD  PRO A 387      36.563  63.817  57.751  1.00 34.93           C  
ATOM   2883  N   LEU A 388      33.068  61.234  56.652  1.00 34.83           N  
ATOM   2884  CA  LEU A 388      32.804  59.821  56.366  1.00 35.84           C  
ATOM   2885  C   LEU A 388      33.215  59.461  54.925  1.00 36.04           C  
ATOM   2886  O   LEU A 388      32.742  58.464  54.383  1.00 37.37           O  
ATOM   2887  CB  LEU A 388      31.314  59.515  56.647  1.00  0.00           C  
ATOM   2888  CG  LEU A 388      30.858  59.803  58.099  1.00  0.00           C  
ATOM   2889  CD1 LEU A 388      29.340  59.574  58.257  1.00  0.00           C  
ATOM   2890  CD2 LEU A 388      31.679  59.021  59.149  1.00  0.00           C  
ATOM   2891  N   ASP A 389      34.098  60.282  54.347  1.00 35.06           N  
ATOM   2892  CA  ASP A 389      34.559  60.256  52.967  1.00 34.83           C  
ATOM   2893  C   ASP A 389      35.974  60.853  52.950  1.00 33.18           C  
ATOM   2894  O   ASP A 389      36.181  61.993  53.371  1.00 33.71           O  
ATOM   2895  CB  ASP A 389      33.622  60.933  51.921  1.00  0.00           C  
ATOM   2896  CG  ASP A 389      32.760  62.137  52.343  1.00  0.00           C  
ATOM   2897  OD1 ASP A 389      32.786  62.558  53.519  1.00  0.00           O  
ATOM   2898  OD2 ASP A 389      32.091  62.671  51.436  1.00  0.00           O1-
ATOM   2899  N   TRP A 390      36.949  60.065  52.493  1.00 30.74           N  
ATOM   2900  CA  TRP A 390      38.372  60.393  52.576  1.00 29.10           C  
ATOM   2901  C   TRP A 390      38.814  61.371  51.476  1.00 28.52           C  
ATOM   2902  O   TRP A 390      39.739  62.156  51.687  1.00 26.75           O  
ATOM   2903  CB  TRP A 390      39.183  59.095  52.538  1.00  0.00           C  
ATOM   2904  CG  TRP A 390      39.171  58.324  51.250  1.00  0.00           C  
ATOM   2905  CD1 TRP A 390      40.122  58.414  50.297  1.00  0.00           C  
ATOM   2906  CD2 TRP A 390      38.171  57.396  50.727  1.00  0.00           C  
ATOM   2907  NE1 TRP A 390      39.789  57.614  49.230  1.00  0.00           N  
ATOM   2908  CE2 TRP A 390      38.594  56.961  49.434  1.00  0.00           C  
ATOM   2909  CE3 TRP A 390      36.945  56.877  51.205  1.00  0.00           C  
ATOM   2910  CZ2 TRP A 390      37.842  56.063  48.658  1.00  0.00           C  
ATOM   2911  CZ3 TRP A 390      36.182  55.973  50.439  1.00  0.00           C  
ATOM   2912  CH2 TRP A 390      36.629  55.566  49.167  1.00  0.00           C  
ATOM   2913  N   GLU A 391      38.097  61.363  50.349  1.00 28.21           N  
ATOM   2914  CA  GLU A 391      38.195  62.342  49.276  1.00 29.79           C  
ATOM   2915  C   GLU A 391      37.810  63.751  49.778  1.00 28.81           C  
ATOM   2916  O   GLU A 391      38.308  64.755  49.266  1.00 30.60           O  
ATOM   2917  CB  GLU A 391      37.281  61.923  48.099  1.00  0.00           C  
ATOM   2918  CG  GLU A 391      37.314  60.429  47.690  1.00  0.00           C  
ATOM   2919  CD  GLU A 391      36.231  59.562  48.347  1.00  0.00           C  
ATOM   2920  OE1 GLU A 391      35.999  59.729  49.565  1.00  0.00           O  
ATOM   2921  OE2 GLU A 391      35.646  58.737  47.615  1.00  0.00           O1-
ATOM   2922  N   THR A 392      36.939  63.792  50.789  1.00 28.14           N  
ATOM   2923  CA  THR A 392      36.440  64.999  51.421  1.00 28.31           C  
ATOM   2924  C   THR A 392      37.312  65.437  52.619  1.00 27.42           C  
ATOM   2925  O   THR A 392      37.462  66.645  52.792  1.00 26.67           O  
ATOM   2926  CB  THR A 392      34.964  64.801  51.826  1.00  0.00           C  
ATOM   2927  OG1 THR A 392      34.263  64.417  50.652  1.00  0.00           O  
ATOM   2928  CG2 THR A 392      34.273  66.036  52.401  1.00  0.00           C  
ATOM   2929  N   TYR A 393      37.999  64.508  53.329  1.00 26.26           N  
ATOM   2930  CA  TYR A 393      39.127  64.846  54.192  1.00 25.95           C  
ATOM   2931  C   TYR A 393      40.178  65.588  53.372  1.00 24.79           C  
ATOM   2932  O   TYR A 393      40.695  66.606  53.804  1.00 24.22           O  
ATOM   2933  CB  TYR A 393      39.771  63.590  54.775  1.00 26.94           C  
ATOM   2934  CG  TYR A 393      41.075  63.857  55.498  1.00 29.67           C  
ATOM   2935  CD1 TYR A 393      41.091  64.275  56.829  1.00 31.19           C  
ATOM   2936  CD2 TYR A 393      42.299  63.667  54.858  1.00 31.17           C  
ATOM   2937  CE1 TYR A 393      42.293  64.488  57.510  1.00 31.10           C  
ATOM   2938  CE2 TYR A 393      43.506  63.880  55.532  1.00 31.85           C  
ATOM   2939  CZ  TYR A 393      43.490  64.287  56.857  1.00 31.51           C  
ATOM   2940  OH  TYR A 393      44.678  64.475  57.525  1.00 32.24           O  
ATOM   2941  N   MET A 394      40.486  65.078  52.166  1.00 24.71           N  
ATOM   2942  CA  MET A 394      41.470  65.675  51.258  1.00 25.50           C  
ATOM   2943  C   MET A 394      41.127  67.127  50.859  1.00 26.33           C  
ATOM   2944  O   MET A 394      41.992  68.000  50.913  1.00 26.68           O  
ATOM   2945  CB  MET A 394      41.697  64.732  50.051  1.00  0.00           C  
ATOM   2946  CG  MET A 394      42.553  65.308  48.913  1.00  0.00           C  
ATOM   2947  SD  MET A 394      44.196  65.826  49.464  1.00  0.00           S  
ATOM   2948  CE  MET A 394      44.406  67.304  48.439  1.00  0.00           C  
ATOM   2949  N   HIS A 395      39.858  67.374  50.510  1.00 26.07           N  
ATOM   2950  CA  HIS A 395      39.379  68.721  50.188  1.00 26.53           C  
ATOM   2951  C   HIS A 395      39.440  69.677  51.389  1.00 26.25           C  
ATOM   2952  O   HIS A 395      39.913  70.801  51.236  1.00 27.40           O  
ATOM   2953  CB  HIS A 395      37.964  68.675  49.585  1.00 26.63           C  
ATOM   2954  CG  HIS A 395      37.926  68.270  48.135  1.00 27.89           C  
ATOM   2955  ND1 HIS A 395      38.146  66.977  47.695  1.00 28.05           N  
ATOM   2956  CD2 HIS A 395      37.705  69.013  46.997  1.00 28.16           C  
ATOM   2957  CE1 HIS A 395      38.065  66.992  46.364  1.00 28.89           C  
ATOM   2958  NE2 HIS A 395      37.781  68.190  45.876  1.00 27.87           N  
ATOM   2959  N   ARG A 396      38.994  69.192  52.554  1.00 26.44           N  
ATOM   2960  CA  ARG A 396      38.924  69.933  53.818  1.00 27.37           C  
ATOM   2961  C   ARG A 396      40.279  70.485  54.271  1.00 27.27           C  
ATOM   2962  O   ARG A 396      40.372  71.689  54.514  1.00 27.95           O  
ATOM   2963  CB  ARG A 396      38.368  69.040  54.936  1.00 27.51           C  
ATOM   2964  CG  ARG A 396      36.843  68.901  54.977  1.00 26.00           C  
ATOM   2965  CD  ARG A 396      36.493  68.109  56.231  1.00 25.30           C  
ATOM   2966  NE  ARG A 396      35.077  67.795  56.389  1.00 27.08           N  
ATOM   2967  CZ  ARG A 396      34.527  67.377  57.532  1.00 27.70           C  
ATOM   2968  NH1 ARG A 396      35.306  67.184  58.598  1.00 28.10           N  
ATOM   2969  NH2 ARG A 396      33.212  67.161  57.602  1.00 28.08           N1+
ATOM   2970  N   ILE A 397      41.276  69.602  54.357  1.00 27.50           N  
ATOM   2971  CA  ILE A 397      42.631  70.002  54.704  1.00 27.82           C  
ATOM   2972  C   ILE A 397      43.168  71.003  53.654  1.00 27.53           C  
ATOM   2973  O   ILE A 397      43.778  72.004  54.022  1.00 27.98           O  
ATOM   2974  CB  ILE A 397      43.547  68.757  54.889  1.00 28.33           C  
ATOM   2975  CG1 ILE A 397      43.902  67.960  53.607  1.00 29.71           C  
ATOM   2976  CG2 ILE A 397      42.964  67.827  55.968  1.00 28.21           C  
ATOM   2977  CD1 ILE A 397      45.076  66.989  53.780  1.00 31.22           C  
ATOM   2978  N   GLY A 398      42.800  70.780  52.383  1.00 26.83           N  
ATOM   2979  CA  GLY A 398      43.113  71.592  51.214  1.00 26.41           C  
ATOM   2980  C   GLY A 398      42.633  73.049  51.274  1.00 27.34           C  
ATOM   2981  O   GLY A 398      43.014  73.820  50.393  1.00 27.96           O  
ATOM   2982  N   ARG A 399      41.838  73.464  52.277  1.00 28.44           N  
ATOM   2983  CA  ARG A 399      41.567  74.884  52.522  1.00 31.68           C  
ATOM   2984  C   ARG A 399      42.803  75.635  53.062  1.00 33.37           C  
ATOM   2985  O   ARG A 399      42.892  76.841  52.843  1.00 32.91           O  
ATOM   2986  CB  ARG A 399      40.343  75.106  53.441  1.00 30.84           C  
ATOM   2987  CG  ARG A 399      38.965  74.582  52.968  1.00 30.89           C  
ATOM   2988  CD  ARG A 399      38.626  74.764  51.473  1.00 29.76           C  
ATOM   2989  NE  ARG A 399      39.162  73.657  50.677  1.00 29.75           N  
ATOM   2990  CZ  ARG A 399      39.434  73.621  49.370  1.00 30.13           C  
ATOM   2991  NH1 ARG A 399      39.324  74.692  48.580  1.00 29.36           N  
ATOM   2992  NH2 ARG A 399      39.833  72.462  48.849  1.00 32.19           N1+
ATOM   2993  N   ALA A 400      43.743  74.924  53.699  1.00 35.38           N  
ATOM   2994  CA  ALA A 400      45.050  75.443  54.088  1.00 38.10           C  
ATOM   2995  C   ALA A 400      46.139  74.831  53.190  1.00 39.37           C  
ATOM   2996  O   ALA A 400      45.892  73.873  52.461  1.00 38.34           O  
ATOM   2997  CB  ALA A 400      45.309  75.107  55.567  1.00  0.00           C  
ATOM   2998  N   GLY A 401      47.348  75.402  53.255  1.00 41.04           N  
ATOM   2999  CA  GLY A 401      48.564  74.867  52.624  1.00 43.50           C  
ATOM   3000  C   GLY A 401      48.593  75.006  51.090  1.00 45.02           C  
ATOM   3001  O   GLY A 401      49.506  74.506  50.428  1.00 45.73           O  
ATOM   3002  N   ARG A 402      47.597  75.700  50.527  1.00 46.08           N  
ATOM   3003  CA  ARG A 402      47.368  75.969  49.109  1.00 47.57           C  
ATOM   3004  C   ARG A 402      48.603  76.567  48.416  1.00 48.41           C  
ATOM   3005  O   ARG A 402      49.386  77.264  49.067  1.00 48.60           O  
ATOM   3006  CB  ARG A 402      46.138  76.890  48.985  1.00 48.32           C  
ATOM   3007  CG  ARG A 402      44.884  76.273  49.640  1.00 48.97           C  
ATOM   3008  CD  ARG A 402      43.614  77.130  49.545  1.00 49.88           C  
ATOM   3009  NE  ARG A 402      43.085  77.224  48.182  1.00 52.61           N  
ATOM   3010  CZ  ARG A 402      42.464  76.263  47.490  1.00 53.24           C  
ATOM   3011  NH1 ARG A 402      42.374  75.017  47.954  1.00 55.34           N  
ATOM   3012  NH2 ARG A 402      41.917  76.557  46.311  1.00 53.14           N1+
ATOM   3013  N   PHE A 403      48.790  76.216  47.135  1.00 49.12           N  
ATOM   3014  CA  PHE A 403      49.939  76.552  46.280  1.00 50.03           C  
ATOM   3015  C   PHE A 403      51.338  76.166  46.813  1.00 50.61           C  
ATOM   3016  O   PHE A 403      52.346  76.525  46.202  1.00 50.09           O  
ATOM   3017  CB  PHE A 403      49.827  77.955  45.612  1.00  0.00           C  
ATOM   3018  CG  PHE A 403      49.338  79.109  46.474  1.00  0.00           C  
ATOM   3019  CD1 PHE A 403      47.957  79.373  46.576  1.00  0.00           C  
ATOM   3020  CD2 PHE A 403      50.225  79.805  47.317  1.00  0.00           C  
ATOM   3021  CE1 PHE A 403      47.490  80.347  47.447  1.00  0.00           C  
ATOM   3022  CE2 PHE A 403      49.735  80.757  48.200  1.00  0.00           C  
ATOM   3023  CZ  PHE A 403      48.377  81.040  48.257  1.00  0.00           C  
ATOM   3024  N   GLY A 404      51.387  75.378  47.896  1.00 51.29           N  
ATOM   3025  CA  GLY A 404      52.618  74.908  48.513  1.00 52.51           C  
ATOM   3026  C   GLY A 404      53.022  75.799  49.694  1.00 53.50           C  
ATOM   3027  O   GLY A 404      54.209  75.852  50.032  1.00 54.51           O  
ATOM   3028  N   THR A 405      52.072  76.506  50.320  1.00 53.24           N  
ATOM   3029  CA  THR A 405      52.290  77.162  51.607  1.00 53.10           C  
ATOM   3030  C   THR A 405      52.317  76.127  52.752  1.00 52.78           C  
ATOM   3031  O   THR A 405      51.732  75.055  52.631  1.00 52.66           O  
ATOM   3032  CB  THR A 405      51.213  78.246  51.892  1.00  0.00           C  
ATOM   3033  OG1 THR A 405      49.890  77.772  51.749  1.00  0.00           O  
ATOM   3034  CG2 THR A 405      51.349  79.461  50.973  1.00  0.00           C  
ATOM   3035  N   LEU A 406      53.048  76.443  53.825  1.00 52.24           N  
ATOM   3036  CA  LEU A 406      53.133  75.645  55.046  1.00 52.07           C  
ATOM   3037  C   LEU A 406      51.852  75.831  55.887  1.00 50.81           C  
ATOM   3038  O   LEU A 406      51.774  76.786  56.661  1.00 50.76           O  
ATOM   3039  CB  LEU A 406      54.391  76.076  55.835  1.00  0.00           C  
ATOM   3040  CG  LEU A 406      55.737  75.874  55.101  1.00  0.00           C  
ATOM   3041  CD1 LEU A 406      56.870  76.605  55.854  1.00  0.00           C  
ATOM   3042  CD2 LEU A 406      56.049  74.385  54.835  1.00  0.00           C  
ATOM   3043  N   GLY A 407      50.862  74.956  55.698  1.00 48.92           N  
ATOM   3044  CA  GLY A 407      49.610  74.962  56.460  1.00 46.23           C  
ATOM   3045  C   GLY A 407      49.681  73.895  57.561  1.00 44.33           C  
ATOM   3046  O   GLY A 407      50.517  72.989  57.493  1.00 44.34           O  
ATOM   3047  N   LEU A 408      48.778  73.972  58.549  1.00 42.04           N  
ATOM   3048  CA  LEU A 408      48.587  72.929  59.562  1.00 40.43           C  
ATOM   3049  C   LEU A 408      47.162  72.378  59.444  1.00 38.02           C  
ATOM   3050  O   LEU A 408      46.224  73.129  59.171  1.00 37.19           O  
ATOM   3051  CB  LEU A 408      48.853  73.479  60.992  1.00  0.00           C  
ATOM   3052  CG  LEU A 408      48.684  72.448  62.150  1.00  0.00           C  
ATOM   3053  CD1 LEU A 408      49.665  71.263  62.039  1.00  0.00           C  
ATOM   3054  CD2 LEU A 408      48.797  73.098  63.534  1.00  0.00           C  
ATOM   3055  N   THR A 409      47.026  71.082  59.718  1.00 36.92           N  
ATOM   3056  CA  THR A 409      45.765  70.416  59.944  1.00 36.42           C  
ATOM   3057  C   THR A 409      45.843  69.623  61.251  1.00 36.01           C  
ATOM   3058  O   THR A 409      46.857  68.970  61.507  1.00 36.72           O  
ATOM   3059  CB  THR A 409      45.499  69.457  58.766  1.00  0.00           C  
ATOM   3060  OG1 THR A 409      45.020  70.281  57.729  1.00  0.00           O  
ATOM   3061  CG2 THR A 409      44.524  68.287  59.000  1.00  0.00           C  
ATOM   3062  N   VAL A 410      44.745  69.638  62.010  1.00 35.46           N  
ATOM   3063  CA  VAL A 410      44.521  68.732  63.127  1.00 34.58           C  
ATOM   3064  C   VAL A 410      43.212  67.969  62.857  1.00 34.41           C  
ATOM   3065  O   VAL A 410      42.272  68.543  62.307  1.00 35.22           O  
ATOM   3066  CB  VAL A 410      44.388  69.483  64.476  1.00  0.00           C  
ATOM   3067  CG1 VAL A 410      44.100  68.523  65.647  1.00  0.00           C  
ATOM   3068  CG2 VAL A 410      45.641  70.329  64.777  1.00  0.00           C  
ATOM   3069  N   THR A 411      43.174  66.685  63.219  1.00 33.77           N  
ATOM   3070  CA  THR A 411      42.020  65.823  63.016  1.00 34.62           C  
ATOM   3071  C   THR A 411      41.808  64.918  64.242  1.00 35.38           C  
ATOM   3072  O   THR A 411      42.704  64.151  64.606  1.00 34.78           O  
ATOM   3073  CB  THR A 411      42.233  64.986  61.726  1.00  0.00           C  
ATOM   3074  OG1 THR A 411      42.317  65.900  60.647  1.00  0.00           O  
ATOM   3075  CG2 THR A 411      41.150  63.959  61.371  1.00  0.00           C  
ATOM   3076  N   TYR A 412      40.631  65.044  64.869  1.00 36.21           N  
ATOM   3077  CA  TYR A 412      40.233  64.301  66.064  1.00 37.15           C  
ATOM   3078  C   TYR A 412      39.583  62.974  65.653  1.00 38.84           C  
ATOM   3079  O   TYR A 412      38.361  62.841  65.613  1.00 38.73           O  
ATOM   3080  CB  TYR A 412      39.277  65.159  66.902  1.00  0.00           C  
ATOM   3081  CG  TYR A 412      39.784  66.527  67.321  1.00  0.00           C  
ATOM   3082  CD1 TYR A 412      41.137  66.794  67.637  1.00  0.00           C  
ATOM   3083  CD2 TYR A 412      38.850  67.570  67.358  1.00  0.00           C  
ATOM   3084  CE1 TYR A 412      41.544  68.111  67.939  1.00  0.00           C  
ATOM   3085  CE2 TYR A 412      39.268  68.885  67.592  1.00  0.00           C  
ATOM   3086  CZ  TYR A 412      40.611  69.165  67.887  1.00  0.00           C  
ATOM   3087  OH  TYR A 412      40.984  70.456  68.108  1.00  0.00           O  
ATOM   3088  N   CYS A 413      40.433  62.012  65.302  1.00 40.42           N  
ATOM   3089  CA  CYS A 413      40.059  60.731  64.732  1.00 42.94           C  
ATOM   3090  C   CYS A 413      39.628  59.763  65.849  1.00 44.95           C  
ATOM   3091  O   CYS A 413      40.421  58.932  66.288  1.00 45.84           O  
ATOM   3092  CB  CYS A 413      41.192  60.221  63.812  1.00  0.00           C  
ATOM   3093  SG  CYS A 413      40.521  59.300  62.399  1.00  0.00           S  
ATOM   3094  N   CYS A 414      38.386  59.932  66.327  1.00 46.65           N  
ATOM   3095  CA  CYS A 414      37.733  59.110  67.349  1.00 48.82           C  
ATOM   3096  C   CYS A 414      37.725  57.623  66.952  1.00 50.44           C  
ATOM   3097  O   CYS A 414      36.938  57.202  66.103  1.00 49.79           O  
ATOM   3098  CB  CYS A 414      36.318  59.628  67.710  1.00  0.00           C  
ATOM   3099  SG  CYS A 414      35.572  58.688  69.083  1.00  0.00           S  
ATOM   3100  N   ARG A 415      38.629  56.854  67.569  1.00 52.55           N  
ATOM   3101  CA  ARG A 415      38.942  55.469  67.226  1.00 54.31           C  
ATOM   3102  C   ARG A 415      37.758  54.489  67.337  1.00 55.80           C  
ATOM   3103  O   ARG A 415      37.812  53.425  66.727  1.00 56.03           O  
ATOM   3104  CB  ARG A 415      40.176  55.038  68.059  1.00  0.00           C  
ATOM   3105  CG  ARG A 415      40.732  53.622  67.803  1.00  0.00           C  
ATOM   3106  CD  ARG A 415      41.203  53.433  66.355  1.00  0.00           C  
ATOM   3107  NE  ARG A 415      41.611  52.063  66.036  1.00  0.00           N  
ATOM   3108  CZ  ARG A 415      40.763  51.064  65.746  1.00  0.00           C  
ATOM   3109  NH1 ARG A 415      39.445  51.208  65.916  1.00  0.00           N  
ATOM   3110  NH2 ARG A 415      41.230  49.917  65.250  1.00  0.00           N1+
ATOM   3111  N   GLY A 416      36.711  54.867  68.078  1.00 57.52           N  
ATOM   3112  CA  GLY A 416      35.507  54.062  68.253  1.00 59.38           C  
ATOM   3113  C   GLY A 416      34.499  54.238  67.105  1.00 58.85           C  
ATOM   3114  O   GLY A 416      33.497  53.526  67.102  1.00 59.34           O  
ATOM   3115  N   GLU A 417      34.715  55.165  66.155  1.00 57.68           N  
ATOM   3116  CA  GLU A 417      33.730  55.470  65.110  1.00 56.29           C  
ATOM   3117  C   GLU A 417      34.360  55.878  63.768  1.00 54.92           C  
ATOM   3118  O   GLU A 417      33.868  55.448  62.727  1.00 55.02           O  
ATOM   3119  CB  GLU A 417      32.697  56.493  65.638  1.00  0.00           C  
ATOM   3120  CG  GLU A 417      33.292  57.827  66.143  1.00  0.00           C  
ATOM   3121  CD  GLU A 417      32.270  58.727  66.838  1.00  0.00           C  
ATOM   3122  OE1 GLU A 417      31.079  58.665  66.465  1.00  0.00           O  
ATOM   3123  OE2 GLU A 417      32.696  59.463  67.753  1.00  0.00           O1-
ATOM   3124  N   GLU A 418      35.459  56.644  63.786  1.00 53.35           N  
ATOM   3125  CA  GLU A 418      36.101  57.168  62.573  1.00 52.35           C  
ATOM   3126  C   GLU A 418      37.006  56.126  61.878  1.00 52.12           C  
ATOM   3127  O   GLU A 418      37.575  56.427  60.826  1.00 51.24           O  
ATOM   3128  CB  GLU A 418      36.889  58.457  62.915  1.00  0.00           C  
ATOM   3129  CG  GLU A 418      36.176  59.511  63.802  1.00  0.00           C  
ATOM   3130  CD  GLU A 418      34.915  60.169  63.238  1.00  0.00           C  
ATOM   3131  OE1 GLU A 418      34.095  59.458  62.623  1.00  0.00           O  
ATOM   3132  OE2 GLU A 418      34.794  61.396  63.449  1.00  0.00           O1-
ATOM   3133  N   GLU A 419      37.113  54.923  62.469  1.00 51.94           N  
ATOM   3134  CA  GLU A 419      37.924  53.779  62.043  1.00 51.41           C  
ATOM   3135  C   GLU A 419      37.849  53.477  60.538  1.00 49.90           C  
ATOM   3136  O   GLU A 419      38.888  53.279  59.918  1.00 50.10           O  
ATOM   3137  CB  GLU A 419      37.589  52.546  62.917  1.00  0.00           C  
ATOM   3138  CG  GLU A 419      38.273  51.224  62.484  1.00  0.00           C  
ATOM   3139  CD  GLU A 419      38.048  50.056  63.445  1.00  0.00           C  
ATOM   3140  OE1 GLU A 419      37.099  50.124  64.253  1.00  0.00           O  
ATOM   3141  OE2 GLU A 419      38.897  49.140  63.438  1.00  0.00           O1-
ATOM   3142  N   ASN A 420      36.639  53.515  59.968  1.00 47.89           N  
ATOM   3143  CA  ASN A 420      36.362  53.228  58.553  1.00 46.34           C  
ATOM   3144  C   ASN A 420      37.118  54.142  57.573  1.00 45.02           C  
ATOM   3145  O   ASN A 420      37.343  53.728  56.437  1.00 44.89           O  
ATOM   3146  CB  ASN A 420      34.844  53.325  58.273  1.00  0.00           C  
ATOM   3147  CG  ASN A 420      34.020  52.233  58.958  1.00  0.00           C  
ATOM   3148  OD1 ASN A 420      33.762  52.302  60.155  1.00  0.00           O  
ATOM   3149  ND2 ASN A 420      33.583  51.222  58.217  1.00  0.00           N  
ATOM   3150  N   MET A 421      37.492  55.353  58.006  1.00 43.81           N  
ATOM   3151  CA  MET A 421      38.295  56.277  57.208  1.00 43.22           C  
ATOM   3152  C   MET A 421      39.778  56.239  57.584  1.00 43.78           C  
ATOM   3153  O   MET A 421      40.584  56.754  56.810  1.00 44.37           O  
ATOM   3154  CB  MET A 421      37.744  57.711  57.339  1.00  0.00           C  
ATOM   3155  CG  MET A 421      36.385  57.907  56.658  1.00  0.00           C  
ATOM   3156  SD  MET A 421      36.409  57.601  54.870  1.00  0.00           S  
ATOM   3157  CE  MET A 421      35.253  56.209  54.744  1.00  0.00           C  
ATOM   3158  N   MET A 422      40.147  55.626  58.718  1.00 42.62           N  
ATOM   3159  CA  MET A 422      41.524  55.615  59.213  1.00 42.30           C  
ATOM   3160  C   MET A 422      42.519  54.958  58.248  1.00 42.07           C  
ATOM   3161  O   MET A 422      43.630  55.464  58.121  1.00 41.44           O  
ATOM   3162  CB  MET A 422      41.628  54.981  60.605  1.00  0.00           C  
ATOM   3163  CG  MET A 422      41.141  55.885  61.736  1.00  0.00           C  
ATOM   3164  SD  MET A 422      41.325  55.119  63.364  1.00  0.00           S  
ATOM   3165  CE  MET A 422      41.203  56.573  64.429  1.00  0.00           C  
ATOM   3166  N   MET A 423      42.106  53.903  57.532  1.00 42.25           N  
ATOM   3167  CA  MET A 423      42.937  53.262  56.507  1.00 43.17           C  
ATOM   3168  C   MET A 423      43.195  54.177  55.295  1.00 43.14           C  
ATOM   3169  O   MET A 423      44.261  54.102  54.691  1.00 43.48           O  
ATOM   3170  CB  MET A 423      42.325  51.926  56.033  1.00  0.00           C  
ATOM   3171  CG  MET A 423      41.724  51.044  57.136  1.00  0.00           C  
ATOM   3172  SD  MET A 423      39.973  51.394  57.448  1.00  0.00           S  
ATOM   3173  CE  MET A 423      39.707  50.386  58.931  1.00  0.00           C  
ATOM   3174  N   ARG A 424      42.224  55.039  54.974  1.00 42.82           N  
ATOM   3175  CA  ARG A 424      42.322  56.004  53.885  1.00 42.64           C  
ATOM   3176  C   ARG A 424      43.146  57.230  54.307  1.00 42.00           C  
ATOM   3177  O   ARG A 424      43.995  57.694  53.549  1.00 41.70           O  
ATOM   3178  CB  ARG A 424      40.918  56.438  53.435  1.00  0.00           C  
ATOM   3179  CG  ARG A 424      39.900  55.330  53.086  1.00  0.00           C  
ATOM   3180  CD  ARG A 424      40.184  54.590  51.766  1.00  0.00           C  
ATOM   3181  NE  ARG A 424      41.328  53.676  51.868  1.00  0.00           N  
ATOM   3182  CZ  ARG A 424      41.325  52.450  52.407  1.00  0.00           C  
ATOM   3183  NH1 ARG A 424      40.201  51.903  52.883  1.00  0.00           N  
ATOM   3184  NH2 ARG A 424      42.471  51.769  52.466  1.00  0.00           N1+
ATOM   3185  N   ILE A 425      42.912  57.704  55.536  1.00 41.82           N  
ATOM   3186  CA  ILE A 425      43.679  58.760  56.192  1.00 42.07           C  
ATOM   3187  C   ILE A 425      45.158  58.344  56.378  1.00 42.66           C  
ATOM   3188  O   ILE A 425      46.050  59.151  56.121  1.00 42.83           O  
ATOM   3189  CB  ILE A 425      43.007  59.146  57.545  1.00  0.00           C  
ATOM   3190  CG1 ILE A 425      41.648  59.845  57.291  1.00  0.00           C  
ATOM   3191  CG2 ILE A 425      43.854  60.016  58.489  1.00  0.00           C  
ATOM   3192  CD1 ILE A 425      40.749  59.938  58.532  1.00  0.00           C  
ATOM   3193  N   ALA A 426      45.399  57.065  56.707  1.00 42.96           N  
ATOM   3194  CA  ALA A 426      46.718  56.436  56.724  1.00 43.43           C  
ATOM   3195  C   ALA A 426      47.420  56.474  55.357  1.00 43.31           C  
ATOM   3196  O   ALA A 426      48.622  56.730  55.314  1.00 42.71           O  
ATOM   3197  CB  ALA A 426      46.617  54.986  57.218  1.00  0.00           C  
ATOM   3198  N   GLN A 427      46.677  56.257  54.262  1.00 43.96           N  
ATOM   3199  CA  GLN A 427      47.195  56.426  52.904  1.00 44.03           C  
ATOM   3200  C   GLN A 427      47.576  57.886  52.611  1.00 43.30           C  
ATOM   3201  O   GLN A 427      48.685  58.118  52.135  1.00 42.96           O  
ATOM   3202  CB  GLN A 427      46.224  55.859  51.852  1.00  0.00           C  
ATOM   3203  CG  GLN A 427      46.136  54.321  51.875  1.00  0.00           C  
ATOM   3204  CD  GLN A 427      44.981  53.783  51.031  1.00  0.00           C  
ATOM   3205  OE1 GLN A 427      43.926  54.400  50.921  1.00  0.00           O  
ATOM   3206  NE2 GLN A 427      45.140  52.599  50.458  1.00  0.00           N  
ATOM   3207  N   LYS A 428      46.704  58.838  52.971  1.00 42.35           N  
ATOM   3208  CA  LYS A 428      46.965  60.276  52.834  1.00 41.63           C  
ATOM   3209  C   LYS A 428      48.217  60.714  53.623  1.00 42.10           C  
ATOM   3210  O   LYS A 428      49.083  61.394  53.074  1.00 41.76           O  
ATOM   3211  CB  LYS A 428      45.703  61.083  53.238  1.00  0.00           C  
ATOM   3212  CG  LYS A 428      45.332  62.238  52.281  1.00  0.00           C  
ATOM   3213  CD  LYS A 428      45.116  61.838  50.802  1.00  0.00           C  
ATOM   3214  CE  LYS A 428      44.100  60.707  50.569  1.00  0.00           C  
ATOM   3215  NZ  LYS A 428      42.714  61.177  50.714  1.00  0.00           N1+
ATOM   3216  N   CYS A 429      48.320  60.216  54.862  1.00 42.75           N  
ATOM   3217  CA  CYS A 429      49.448  60.376  55.774  1.00 44.02           C  
ATOM   3218  C   CYS A 429      50.769  59.894  55.149  1.00 45.22           C  
ATOM   3219  O   CYS A 429      51.746  60.642  55.148  1.00 45.20           O  
ATOM   3220  CB  CYS A 429      49.161  59.672  57.120  1.00  0.00           C  
ATOM   3221  SG  CYS A 429      50.459  59.923  58.357  1.00  0.00           S  
ATOM   3222  N   ASN A 430      50.763  58.671  54.598  1.00 46.06           N  
ATOM   3223  CA  ASN A 430      51.924  58.053  53.952  1.00 47.02           C  
ATOM   3224  C   ASN A 430      52.317  58.769  52.656  1.00 46.64           C  
ATOM   3225  O   ASN A 430      53.504  59.019  52.475  1.00 47.04           O  
ATOM   3226  CB  ASN A 430      51.665  56.553  53.709  1.00  0.00           C  
ATOM   3227  CG  ASN A 430      51.965  55.712  54.947  1.00  0.00           C  
ATOM   3228  OD1 ASN A 430      53.114  55.376  55.206  1.00  0.00           O  
ATOM   3229  ND2 ASN A 430      50.957  55.369  55.734  1.00  0.00           N  
ATOM   3230  N   ILE A 431      51.344  59.152  51.812  1.00 46.65           N  
ATOM   3231  CA  ILE A 431      51.580  59.922  50.579  1.00 45.84           C  
ATOM   3232  C   ILE A 431      52.295  61.266  50.852  1.00 45.54           C  
ATOM   3233  O   ILE A 431      53.197  61.640  50.106  1.00 45.45           O  
ATOM   3234  CB  ILE A 431      50.255  60.171  49.782  1.00  0.00           C  
ATOM   3235  CG1 ILE A 431      49.696  58.848  49.205  1.00  0.00           C  
ATOM   3236  CG2 ILE A 431      50.338  61.208  48.633  1.00  0.00           C  
ATOM   3237  CD1 ILE A 431      48.205  58.913  48.833  1.00  0.00           C  
ATOM   3238  N   ASN A 432      51.906  61.934  51.943  1.00 45.70           N  
ATOM   3239  CA  ASN A 432      52.510  63.181  52.400  1.00 46.35           C  
ATOM   3240  C   ASN A 432      53.728  62.999  53.326  1.00 47.04           C  
ATOM   3241  O   ASN A 432      54.327  64.007  53.697  1.00 47.06           O  
ATOM   3242  CB  ASN A 432      51.425  64.005  53.119  1.00  0.00           C  
ATOM   3243  CG  ASN A 432      51.247  65.379  52.502  1.00  0.00           C  
ATOM   3244  OD1 ASN A 432      50.993  65.458  51.308  1.00  0.00           O  
ATOM   3245  ND2 ASN A 432      51.265  66.460  53.271  1.00  0.00           N  
ATOM   3246  N   LEU A 433      54.064  61.756  53.707  1.00 47.47           N  
ATOM   3247  CA  LEU A 433      55.158  61.375  54.605  1.00 48.39           C  
ATOM   3248  C   LEU A 433      55.051  61.995  56.021  1.00 49.18           C  
ATOM   3249  O   LEU A 433      56.075  62.307  56.630  1.00 49.43           O  
ATOM   3250  CB  LEU A 433      56.537  61.643  53.938  1.00  0.00           C  
ATOM   3251  CG  LEU A 433      56.779  60.909  52.596  1.00  0.00           C  
ATOM   3252  CD1 LEU A 433      57.996  61.501  51.851  1.00  0.00           C  
ATOM   3253  CD2 LEU A 433      56.886  59.378  52.777  1.00  0.00           C  
ATOM   3254  N   LEU A 434      53.825  62.139  56.545  1.00 50.03           N  
ATOM   3255  CA  LEU A 434      53.593  62.506  57.950  1.00 50.23           C  
ATOM   3256  C   LEU A 434      53.803  61.269  58.867  1.00 51.20           C  
ATOM   3257  O   LEU A 434      53.739  60.137  58.374  1.00 51.04           O  
ATOM   3258  CB  LEU A 434      52.174  63.117  58.124  1.00  0.00           C  
ATOM   3259  CG  LEU A 434      52.005  64.647  57.932  1.00  0.00           C  
ATOM   3260  CD1 LEU A 434      52.939  65.535  58.778  1.00  0.00           C  
ATOM   3261  CD2 LEU A 434      52.007  65.093  56.468  1.00  0.00           C  
ATOM   3262  N   PRO A 435      54.043  61.482  60.185  1.00 52.48           N  
ATOM   3263  CA  PRO A 435      54.215  60.372  61.131  1.00 53.74           C  
ATOM   3264  C   PRO A 435      52.864  59.730  61.497  1.00 54.33           C  
ATOM   3265  O   PRO A 435      52.153  60.240  62.362  1.00 55.11           O  
ATOM   3266  CD  PRO A 435      54.189  62.776  60.860  1.00  0.00           C  
ATOM   3267  CB  PRO A 435      54.929  61.029  62.324  1.00  0.00           C  
ATOM   3268  CG  PRO A 435      54.426  62.463  62.335  1.00  0.00           C  
ATOM   3269  N   LEU A 436      52.541  58.627  60.816  1.00 54.89           N  
ATOM   3270  CA  LEU A 436      51.353  57.795  61.027  1.00 55.94           C  
ATOM   3271  C   LEU A 436      51.257  57.318  62.498  1.00 57.70           C  
ATOM   3272  O   LEU A 436      52.121  56.528  62.890  1.00 58.19           O  
ATOM   3273  CB  LEU A 436      51.467  56.617  60.031  1.00  0.00           C  
ATOM   3274  CG  LEU A 436      50.308  55.599  60.062  1.00  0.00           C  
ATOM   3275  CD1 LEU A 436      48.940  56.278  59.870  1.00  0.00           C  
ATOM   3276  CD2 LEU A 436      50.556  54.481  59.027  1.00  0.00           C  
ATOM   3277  N   PRO A 437      50.280  57.812  63.306  1.00 59.03           N  
ATOM   3278  CA  PRO A 437      50.242  57.463  64.732  1.00 59.62           C  
ATOM   3279  C   PRO A 437      49.790  56.017  64.852  1.00 60.29           C  
ATOM   3280  O   PRO A 437      48.921  55.581  64.094  1.00 60.57           O  
ATOM   3281  CB  PRO A 437      49.202  58.427  65.305  1.00 60.08           C  
ATOM   3282  CG  PRO A 437      49.134  59.550  64.282  1.00 60.24           C  
ATOM   3283  CD  PRO A 437      49.229  58.793  62.992  1.00 59.62           C  
ATOM   3284  N   ASP A 438      50.362  55.282  65.803  1.00 60.88           N  
ATOM   3285  CA  ASP A 438      50.022  53.871  65.981  1.00 61.55           C  
ATOM   3286  C   ASP A 438      48.541  53.558  66.098  1.00 61.33           C  
ATOM   3287  O   ASP A 438      48.068  52.576  65.525  1.00 61.44           O  
ATOM   3288  CB  ASP A 438      50.735  53.286  67.207  1.00 62.88           C  
ATOM   3289  CG  ASP A 438      52.231  53.126  66.996  1.00 64.28           C  
ATOM   3290  OD1 ASP A 438      53.002  53.904  67.603  1.00 65.43           O  
ATOM   3291  OD2 ASP A 438      52.633  52.226  66.220  1.00 64.69           O1-
ATOM   3292  N   PRO A 439      47.713  54.388  66.789  1.00 61.00           N  
ATOM   3293  CA  PRO A 439      46.262  54.114  66.856  1.00 60.73           C  
ATOM   3294  C   PRO A 439      45.480  54.112  65.527  1.00 61.27           C  
ATOM   3295  O   PRO A 439      44.421  53.488  65.488  1.00 61.94           O  
ATOM   3296  CD  PRO A 439      48.058  55.498  67.688  1.00  0.00           C  
ATOM   3297  CB  PRO A 439      45.721  55.190  67.804  1.00  0.00           C  
ATOM   3298  CG  PRO A 439      46.901  55.579  68.671  1.00  0.00           C  
ATOM   3299  N   ILE A 440      45.962  54.822  64.495  1.00 61.66           N  
ATOM   3300  CA  ILE A 440      45.234  54.993  63.234  1.00 61.61           C  
ATOM   3301  C   ILE A 440      45.176  53.696  62.375  1.00 62.21           C  
ATOM   3302  O   ILE A 440      44.072  53.279  62.031  1.00 61.68           O  
ATOM   3303  CB  ILE A 440      45.697  56.278  62.454  1.00  0.00           C  
ATOM   3304  CG1 ILE A 440      45.004  57.567  62.971  1.00  0.00           C  
ATOM   3305  CG2 ILE A 440      45.526  56.248  60.920  1.00  0.00           C  
ATOM   3306  CD1 ILE A 440      45.108  57.833  64.480  1.00  0.00           C  
ATOM   3307  N   PRO A 441      46.311  53.006  62.099  1.00 62.80           N  
ATOM   3308  CA  PRO A 441      46.297  51.648  61.505  1.00 63.33           C  
ATOM   3309  C   PRO A 441      45.558  50.556  62.259  1.00 64.13           C  
ATOM   3310  O   PRO A 441      45.553  49.381  61.890  1.00 64.75           O  
ATOM   3311  CD  PRO A 441      47.677  53.516  62.186  1.00  0.00           C  
ATOM   3312  CB  PRO A 441      47.794  51.313  61.334  1.00  0.00           C  
ATOM   3313  CG  PRO A 441      48.473  52.662  61.215  1.00  0.00           C  
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.