CNRS Nantes University UFIP UFIP
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***  MutS_Ngo  ***

elNémo ID: 19100714172130534

Job options:

ID        	=	 19100714172130534
JOBID     	=	 MutS_Ngo
USERID    	=	 Peter
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:

HEADER MutS_Ngo

ATOM      1  N   GLN A  -1      81.034  90.271  15.807  1.00 75.87      A    N  
ATOM      2  CA  GLN A  -1      81.771  89.882  17.070  1.00 78.00      A    C  
ATOM      3  C   GLN A  -1      81.471  90.763  18.336  1.00 90.78      A    C  
ATOM      4  O   GLN A  -1      82.386  91.413  18.875  1.00 61.01      A    O  
ATOM      5  N   SER A   0      80.194  90.772  18.787  1.00102.91      A    N  
ATOM      6  CA  SER A   0      79.765  91.355  20.082  1.00 76.54      A    C  
ATOM      7  C   SER A   0      80.160  90.376  21.221  1.00 89.95      A    C  
ATOM      8  O   SER A   0      80.418  89.198  20.981  1.00111.63      A    O  
ATOM      9  N   MET A   1      80.236  90.862  22.454  1.00133.73      A    N  
ANISOU    9  N   MET A   1    14746  21688  14375   2640   1057   2456  A    N  
ATOM     10  CA  MET A   1      80.731  90.055  23.564  1.00123.29      A    C  
ANISOU   10  CA  MET A   1    13568  19975  13301   2262    892   2144  A    C  
ATOM     11  C   MET A   1      79.753  89.988  24.752  1.00125.97      A    C  
ANISOU   11  C   MET A   1    13949  20133  13778   2030    780   1999  A    C  
ATOM     12  O   MET A   1      78.527  90.034  24.585  1.00124.01      A    O  
ANISOU   12  O   MET A   1    13569  20177  13369   2104    718   1990  A    O  
ATOM     13  N   SER A   2      80.317  89.861  25.952  1.00122.26      A    N  
ANISOU   13  N   SER A   2    13652  19202  13596   1759    756   1881  A    N  
ATOM     14  CA  SER A   2      79.557  89.922  27.182  1.00108.40      A    C  
ANISOU   14  CA  SER A   2    11962  17226  11999   1554    689   1787  A    C  
ATOM     15  C   SER A   2      79.510  91.410  27.485  1.00113.67      A    C  
ANISOU   15  C   SER A   2    12699  17685  12803   1666    933   2085  A    C  
ATOM     16  O   SER A   2      78.804  92.148  26.792  1.00131.22      A    O  
ANISOU   16  O   SER A   2    14823  20153  14881   1906   1052   2311  A    O  
ATOM     17  N   LYS A   3      80.244  91.863  28.503  1.00100.78      A    N  
ANISOU   17  N   LYS A   3    11219  15624  11446   1504   1019   2078  A    N  
ATOM     18  CA  LYS A   3      81.006  90.983  29.344  1.00 94.83      A    C  
ANISOU   18  CA  LYS A   3    10563  14639  10830   1253    875   1829  A    C  
ATOM     19  C   LYS A   3      80.184  90.413  30.508  1.00 92.32      A    C  
ANISOU   19  C   LYS A   3    10272  14229  10574   1039    708   1640  A    C  
ATOM     20  O   LYS A   3      80.741  90.148  31.578  1.00100.32      A    O  
ANISOU   20  O   LYS A   3    11389  14968  11758    853    664   1514  A    O  
ATOM     21  N   SER A   4      78.878  90.214  30.321  1.00 85.21      A    N  
ANISOU   21  N   SER A   4     9267  13573   9534   1075    622   1620  A    N  
ATOM     22  CA  SER A   4      78.073  89.531  31.332  1.00 81.00      A    C  
ANISOU   22  CA  SER A   4     8744  12965   9064    877    475   1436  A    C  
ATOM     23  C   SER A   4      77.993  88.031  31.037  1.00 82.47      A    C  
ANISOU   23  C   SER A   4     8857  13302   9173    774    292   1174  A    C  
ATOM     24  O   SER A   4      77.481  87.264  31.843  1.00 88.37      A    O  
ANISOU   24  O   SER A   4     9613  13955  10007    600    190   1005  A    O  
ATOM     25  CB  SER A   4      76.672  90.144  31.448  1.00 77.15      A    C  
ANISOU   25  CB  SER A   4     8182  12615   8516    941    498   1533  A    C  
ATOM     26  OG  SER A   4      75.770  89.651  30.481  1.00 74.43      A    O  
ANISOU   26  OG  SER A   4     7662  12672   7946   1046    408   1473  A    O  
ATOM     27  N   ALA A   5      78.511  87.616  29.885  1.00 82.47      A    N  
ANISOU   27  N   ALA A   5     8778  13529   9024    885    273   1141  A    N  
ATOM     28  CA  ALA A   5      78.513  86.205  29.499  1.00 81.88      A    C  
ANISOU   28  CA  ALA A   5     8617  13604   8889    789    122    864  A    C  
ATOM     29  C   ALA A   5      79.729  85.494  30.077  1.00 80.72      A    C  
ANISOU   29  C   ALA A   5     8601  13158   8908    639     96    754  A    C  
ATOM     30  O   ALA A   5      79.837  84.259  30.000  1.00 85.47      A    O  
ANISOU   30  O   ALA A   5     9161  13783   9530    526     -4    518  A    O  
ATOM     31  CB  ALA A   5      78.487  86.070  27.973  1.00 82.04      A    C  
ANISOU   31  CB  ALA A   5     8467  14056   8646    994    109    857  A    C  
ATOM     32  N   VAL A   6      80.636  86.289  30.651  1.00 74.97      A    N  
ANISOU   32  N   VAL A   6     8017  12158   8308    644    202    915  A    N  
ATOM     33  CA  VAL A   6      81.930  85.823  31.106  1.00 69.08      A    C  
ANISOU   33  CA  VAL A   6     7384  11170   7691    547    197    848  A    C  
ATOM     34  C   VAL A   6      82.290  86.538  32.404  1.00 64.81      A    C  
ANISOU   34  C   VAL A   6     6973  10318   7334    462    267    929  A    C  
ATOM     35  O   VAL A   6      82.041  87.733  32.559  1.00 63.28      A    O  
ANISOU   35  O   VAL A   6     6795  10078   7168    533    382   1093  A    O  
ATOM     36  CB  VAL A   6      83.011  86.059  30.037  1.00 68.96      A    C  
ANISOU   36  CB  VAL A   6     7359  11246   7593    689    269    930  A    C  
ATOM     37  CG1 VAL A   6      83.074  87.511  29.621  1.00 67.40      A    C  
ANISOU   37  CG1 VAL A   6     7166  11064   7378    865    449   1196  A    C  
ATOM     38  CG2 VAL A   6      84.359  85.587  30.561  1.00 71.23      A    C  
ANISOU   38  CG2 VAL A   6     7758  11287   8019    584    261    852  A    C  
ATOM     39  N   SER A   7      82.847  85.782  33.349  1.00 63.35      A    N  
ANISOU   39  N   SER A   7     6865   9936   7269    321    205    805  A    N  
ATOM     40  CA  SER A   7      83.102  86.273  34.719  1.00 60.38      A    C  
ANISOU   40  CA  SER A   7     6581   9323   7034    238    242    836  A    C  
ATOM     41  C   SER A   7      84.271  87.207  34.678  1.00 58.08      A    C  
ANISOU   41  C   SER A   7     6337   8922   6807    287    359    916  A    C  
ATOM     42  O   SER A   7      85.122  87.044  33.845  1.00 64.28      A    O  
ANISOU   42  O   SER A   7     7114   9751   7557    345    382    916  A    O  
ATOM     43  CB  SER A   7      83.380  85.098  35.699  1.00 61.02      A    C  
ANISOU   43  CB  SER A   7     6712   9273   7198    113    155    701  A    C  
ATOM     44  OG  SER A   7      84.334  84.153  35.209  1.00 62.62      A    O  
ANISOU   44  OG  SER A   7     6919   9477   7393    104    114    604  A    O  
ATOM     45  N   PRO A   8      84.343  88.178  35.581  1.00 56.70      A    N  
ANISOU   45  N   PRO A   8     6201   8603   6738    260    444    962  A    N  
ATOM     46  CA  PRO A   8      85.547  89.008  35.660  1.00 57.82      A    C  
ANISOU   46  CA  PRO A   8     6366   8615   6986    272    570    977  A    C  
ATOM     47  C   PRO A   8      86.855  88.231  36.020  1.00 61.17      A    C  
ANISOU   47  C   PRO A   8     6825   8969   7448    209    507    845  A    C  
ATOM     48  O   PRO A   8      87.925  88.662  35.708  1.00 58.14      A    O  
ANISOU   48  O   PRO A   8     6438   8523   7128    230    599    839  A    O  
ATOM     49  CB  PRO A   8      85.206  90.012  36.745  1.00 55.75      A    C  
ANISOU   49  CB  PRO A   8     6115   8234   6832    226    649    984  A    C  
ATOM     50  CG  PRO A   8      83.732  89.977  36.835  1.00 55.86      A    C  
ANISOU   50  CG  PRO A   8     6110   8337   6775    238    599   1050  A    C  
ATOM     51  CD  PRO A   8      83.356  88.566  36.584  1.00 56.50      A    C  
ANISOU   51  CD  PRO A   8     6184   8531   6749    209    437    979  A    C  
ATOM     52  N   MET A   9      86.777  87.082  36.668  1.00 69.31      A    N  
ANISOU   52  N   MET A   9     7879  10006   8447    139    370    748  A    N  
ATOM     53  CA  MET A   9      87.990  86.334  36.925  1.00 72.20      A    C  
ANISOU   53  CA  MET A   9     8270  10326   8834    107    323    650  A    C  
ATOM     54  C   MET A   9      88.416  85.785  35.625  1.00 65.93      A    C  
ANISOU   54  C   MET A   9     7461   9610   7977    161    312    653  A    C  
ATOM     55  O   MET A   9      89.581  85.679  35.403  1.00 81.41      A    O  
ANISOU   55  O   MET A   9     9430  11537   9965    171    336    615  A    O  
ATOM     56  CB  MET A   9      87.805  85.212  37.974  1.00 87.05      A    C  
ANISOU   56  CB  MET A   9    10178  12184  10711     49    217    581  A    C  
ATOM     57  CG  MET A   9      87.360  85.774  39.341  1.00101.90      A    C  
ANISOU   57  CG  MET A   9    12064  14026  12628     21    229    588  A    C  
ATOM     58  SD  MET A   9      88.104  85.114  40.863  1.00115.53      A    S  
ANISOU   58  SD  MET A   9    13802  15739  14355     14    179    522  A    S  
ATOM     59  CE  MET A   9      89.864  85.194  40.471  1.00113.16      A    C  
ANISOU   59  CE  MET A   9    13484  15440  14070     29    201    431  A    C  
ATOM     60  N   MET A  10      87.481  85.406  34.777  1.00 61.12      A    N  
ANISOU   60  N   MET A  10     6813   9132   7275    200    274    681  A    N  
ATOM     61  CA  MET A  10      87.820  84.755  33.541  1.00 62.11      A    C  
ANISOU   61  CA  MET A  10     6903   9385   7310    258    246    652  A    C  
ATOM     62  C   MET A  10      88.218  85.812  32.553  1.00 62.63      A    C  
ANISOU   62  C   MET A  10     6941   9509   7346    383    378    785  A    C  
ATOM     63  O   MET A  10      89.069  85.602  31.721  1.00 66.88      A    O  
ANISOU   63  O   MET A  10     7469  10096   7847    445    404    787  A    O  
ATOM     64  CB  MET A  10      86.652  83.935  33.005  1.00 66.17      A    C  
ANISOU   64  CB  MET A  10     7350  10064   7727    254    158    587  A    C  
ATOM     65  CG  MET A  10      86.959  83.210  31.706  1.00 73.52      A    C  
ANISOU   65  CG  MET A  10     8215  11174   8544    317    121    514  A    C  
ATOM     66  SD  MET A  10      88.389  82.114  31.883  1.00 82.71      A    S  
ANISOU   66  SD  MET A  10     9439  12207   9780    255     82    390  A    S  
ATOM     67  CE  MET A  10      88.465  81.386  30.249  1.00 87.07      A    C  
ANISOU   67  CE  MET A  10     9887  13023  10172    341     43    291  A    C  
ATOM     68  N   GLN A  11      87.589  86.961  32.638  1.00 62.59      A    N  
ANISOU   68  N   GLN A  11     6921   9492   7365    432    482    913  A    N  
ATOM     69  CA  GLN A  11      87.850  88.042  31.716  1.00 63.31      A    C  
ANISOU   69  CA  GLN A  11     6981   9617   7455    575    658   1082  A    C  
ATOM     70  C   GLN A  11      89.281  88.512  31.847  1.00 59.77      A    C  
ANISOU   70  C   GLN A  11     6566   8991   7153    557    779   1073  A    C  
ATOM     71  O   GLN A  11      89.912  88.911  30.908  1.00 58.12      A    O  
ANISOU   71  O   GLN A  11     6333   8803   6942    670    909   1175  A    O  
ATOM     72  CB  GLN A  11      86.879  89.170  32.036  1.00 68.70      A    C  
ANISOU   72  CB  GLN A  11     7650  10270   8181    612    765   1211  A    C  
ATOM     73  CG  GLN A  11      87.108  90.428  31.254  1.00 78.26      A    C  
ANISOU   73  CG  GLN A  11     8832  11458   9444    770   1007   1418  A    C  
ATOM     74  CD  GLN A  11      86.852  90.227  29.762  1.00 87.71      A    C  
ANISOU   74  CD  GLN A  11     9954  12931  10441    973   1031   1557  A    C  
ATOM     75  NE2 GLN A  11      87.931  90.278  28.929  1.00 90.14      A    N  
ANISOU   75  NE2 GLN A  11    10254  13240  10754   1069   1137   1621  A    N  
ATOM     76  OE1 GLN A  11      85.696  90.046  29.357  1.00 89.60      A    O  
ANISOU   76  OE1 GLN A  11    10128  13404  10513   1052    958   1601  A    O  
ATOM     77  N   GLN A  12      89.790  88.443  33.053  1.00 60.96      A    N  
ANISOU   77  N   GLN A  12     6759   8980   7422    421    738    941  A    N  
ATOM     78  CA  GLN A  12      91.144  88.856  33.340  1.00 61.21      A    C  
ANISOU   78  CA  GLN A  12     6796   8861   7598    380    838    877  A    C  
ATOM     79  C   GLN A  12      92.125  87.859  32.767  1.00 59.12      A    C  
ANISOU   79  C   GLN A  12     6541   8648   7271    391    761    812  A    C  
ATOM     80  O   GLN A  12      93.209  88.250  32.300  1.00 58.77      A    O  
ANISOU   80  O   GLN A  12     6482   8537   7309    425    885    824  A    O  
ATOM     81  CB  GLN A  12      91.346  88.949  34.846  1.00 61.89      A    C  
ANISOU   81  CB  GLN A  12     6895   8839   7780    248    787    728  A    C  
ATOM     82  CG  GLN A  12      92.523  89.804  35.201  1.00 66.93      A    C  
ANISOU   82  CG  GLN A  12     7496   9337   8594    204    937    641  A    C  
ATOM     83  CD  GLN A  12      92.385  90.444  36.548  1.00 72.43      A    C  
ANISOU   83  CD  GLN A  12     8164   9967   9388    109    953    517  A    C  
ATOM     84  NE2 GLN A  12      93.310  91.376  36.875  1.00 76.22      A    N  
ANISOU   84  NE2 GLN A  12     8576  10331  10052     56   1115    397  A    N  
ATOM     85  OE1 GLN A  12      91.475  90.094  37.310  1.00 75.32      A    O  
ANISOU   85  OE1 GLN A  12     8554  10394   9671     80    829    509  A    O  
ATOM     86  N   TYR A  13      91.738  86.584  32.817  1.00 55.20      A    N  
ANISOU   86  N   TYR A  13     6063   8256   6653    360    576    734  A    N  
ATOM     87  CA  TYR A  13      92.519  85.518  32.225  1.00 55.43      A    C  
ANISOU   87  CA  TYR A  13     6099   8345   6617    374    499    664  A    C  
ATOM     88  C   TYR A  13      92.654  85.710  30.734  1.00 55.64      A    C  
ANISOU   88  C   TYR A  13     6084   8506   6552    514    581    774  A    C  
ATOM     89  O   TYR A  13      93.725  85.524  30.187  1.00 58.50      A    O  
ANISOU   89  O   TYR A  13     6445   8858   6924    551    623    764  A    O  
ATOM     90  CB  TYR A  13      91.910  84.141  32.467  1.00 55.29      A    C  
ANISOU   90  CB  TYR A  13     6092   8397   6517    316    328    558  A    C  
ATOM     91  CG  TYR A  13      92.571  83.067  31.647  1.00 55.95      A    C  
ANISOU   91  CG  TYR A  13     6168   8558   6533    342    270    481  A    C  
ATOM     92  CD1 TYR A  13      93.782  82.543  32.041  1.00 56.07      A    C  
ANISOU   92  CD1 TYR A  13     6217   8476   6610    303    252    405  A    C  
ATOM     93  CD2 TYR A  13      91.992  82.597  30.473  1.00 57.24      A    C  
ANISOU   93  CD2 TYR A  13     6271   8917   6559    414    234    473  A    C  
ATOM     94  CE1 TYR A  13      94.406  81.564  31.301  1.00 59.46      A    C  
ANISOU   94  CE1 TYR A  13     6640   8965   6985    327    207    333  A    C  
ATOM     95  CE2 TYR A  13      92.610  81.623  29.715  1.00 59.88      A    C  
ANISOU   95  CE2 TYR A  13     6586   9332   6831    437    186    378  A    C  
ATOM     96  CZ  TYR A  13      93.825  81.110  30.134  1.00 61.45      A    C  
ANISOU   96  CZ  TYR A  13     6837   9395   7114    389    177    315  A    C  
ATOM     97  OH  TYR A  13      94.481  80.135  29.418  1.00 63.74      A    O  
ANISOU   97  OH  TYR A  13     7112   9750   7354    409    137    218  A    O  
ATOM     98  N   LEU A  14      91.568  86.067  30.075  1.00 55.31      A    N  
ANISOU   98  N   LEU A  14     5996   8613   6405    611    607    886  A    N  
ATOM     99  CA  LEU A  14      91.606  86.316  28.649  1.00 55.84      A    C  
ANISOU   99  CA  LEU A  14     6003   8868   6347    791    698   1022  A    C  
ATOM    100  C   LEU A  14      92.469  87.538  28.300  1.00 57.79      A    C  
ANISOU  100  C   LEU A  14     6251   8980   6725    884    943   1187  A    C  
ATOM    101  O   LEU A  14      92.982  87.628  27.191  1.00 58.85      A    O  
ANISOU  101  O   LEU A  14     6350   9222   6788   1035   1042   1299  A    O  
ATOM    102  CB  LEU A  14      90.199  86.500  28.111  1.00 56.20      A    C  
ANISOU  102  CB  LEU A  14     5977   9140   6233    895    678   1110  A    C  
ATOM    103  CG  LEU A  14      89.309  85.279  28.260  1.00 56.30      A    C  
ANISOU  103  CG  LEU A  14     5953   9302   6133    806    468    923  A    C  
ATOM    104  CD1 LEU A  14      87.848  85.643  28.121  1.00 56.70      A    C  
ANISOU  104  CD1 LEU A  14     5933   9531   6080    865    453    985  A    C  
ATOM    105  CD2 LEU A  14      89.693  84.211  27.249  1.00 57.87      A    C  
ANISOU  105  CD2 LEU A  14     6092   9710   6183    860    381    807  A    C  
ATOM    106  N   GLY A  15      92.649  88.466  29.239  1.00 58.68      A    N  
ANISOU  106  N   GLY A  15     6396   8860   7041    797   1057   1191  A    N  
ATOM    107  CA  GLY A  15      93.594  89.566  29.032  1.00 61.65      A    C  
ANISOU  107  CA  GLY A  15     6759   9053   7609    844   1316   1290  A    C  
ATOM    108  C   GLY A  15      95.052  89.088  28.876  1.00 63.82      A    C  
ANISOU  108  C   GLY A  15     7043   9255   7947    803   1319   1187  A    C  
ATOM    109  O   GLY A  15      95.829  89.572  28.006  1.00 61.24      A    O  
ANISOU  109  O   GLY A  15     6690   8893   7685    918   1517   1310  A    O  
ATOM    110  N   ILE A  16      95.416  88.143  29.751  1.00 63.61      A    N  
ANISOU  110  N   ILE A  16     7052   9206   7909    651   1116    975  A    N  
ATOM    111  CA  ILE A  16      96.748  87.561  29.768  1.00 62.42      A    C  
ANISOU  111  CA  ILE A  16     6909   9003   7803    601   1084    854  A    C  
ATOM    112  C   ILE A  16      96.866  86.618  28.585  1.00 62.14      A    C  
ANISOU  112  C   ILE A  16     6869   9159   7579    714   1006    899  A    C  
ATOM    113  O   ILE A  16      97.848  86.647  27.888  1.00 65.05      A    O  
ANISOU  113  O   ILE A  16     7223   9516   7975    779   1104    937  A    O  
ATOM    114  CB  ILE A  16      97.046  86.825  31.111  1.00 61.00      A    C  
ANISOU  114  CB  ILE A  16     6757   8771   7648    439    903    642  A    C  
ATOM    115  CG1 ILE A  16      97.599  87.785  32.162  1.00 62.45      A    C  
ANISOU  115  CG1 ILE A  16     6906   8790   8033    339   1013    539  A    C  
ATOM    116  CG2 ILE A  16      98.070  85.727  30.941  1.00 59.97      A    C  
ANISOU  116  CG2 ILE A  16     6641   8679   7466    424    798    539  A    C  
ATOM    117  CD1 ILE A  16      96.637  88.902  32.487  1.00 66.00      A    C  
ANISOU  117  CD1 ILE A  16     7337   9173   8565    336   1131    615  A    C  
ATOM    118  N   LYS A  17      95.864  85.787  28.353  1.00 61.68      A    N  
ANISOU  118  N   LYS A  17     6812   9283   7338    733    839    877  A    N  
ATOM    119  CA  LYS A  17      95.985  84.705  27.379  1.00 63.26      A    C  
ANISOU  119  CA  LYS A  17     6990   9682   7362    806    734    836  A    C  
ATOM    120  C   LYS A  17      96.084  85.253  26.000  1.00 66.42      A    C  
ANISOU  120  C   LYS A  17     7332  10241   7663   1013    887   1025  A    C  
ATOM    121  O   LYS A  17      96.750  84.669  25.153  1.00 68.35      A    O  
ANISOU  121  O   LYS A  17     7555  10602   7812   1091    875   1011  A    O  
ATOM    122  CB  LYS A  17      94.784  83.759  27.458  1.00 64.26      A    C  
ANISOU  122  CB  LYS A  17     7099   9969   7347    766    548    731  A    C  
ATOM    123  CG  LYS A  17      94.751  82.617  26.450  1.00 63.29      A    C  
ANISOU  123  CG  LYS A  17     6922  10076   7046    827    442    632  A    C  
ATOM    124  CD  LYS A  17      95.950  81.718  26.584  1.00 62.08      A    C  
ANISOU  124  CD  LYS A  17     6811   9824   6950    759    390    502  A    C  
ATOM    125  CE  LYS A  17      95.938  80.618  25.543  1.00 62.27      A    C  
ANISOU  125  CE  LYS A  17     6771  10076   6811    817    303    383  A    C  
ATOM    126  NZ  LYS A  17      97.260  79.938  25.434  1.00 61.85      A    N1+
ANISOU  126  NZ  LYS A  17     6753   9937   6806    795    296    303  A    N1+
ATOM    127  N   ALA A  18      95.438  86.388  25.776  1.00 69.15      A    N  
ANISOU  127  N   ALA A  18     7650  10594   8028   1119   1047   1218  A    N  
ATOM    128  CA  ALA A  18      95.540  87.072  24.482  1.00 71.89      A    C  
ANISOU  128  CA  ALA A  18     7935  11086   8290   1363   1249   1460  A    C  
ATOM    129  C   ALA A  18      96.953  87.457  24.167  1.00 69.41      A    C  
ANISOU  129  C   ALA A  18     7634  10605   8131   1397   1435   1523  A    C  
ATOM    130  O   ALA A  18      97.302  87.486  23.035  1.00 71.98      A    O  
ANISOU  130  O   ALA A  18     7914  11089   8346   1589   1542   1669  A    O  
ATOM    131  CB  ALA A  18      94.680  88.325  24.450  1.00 76.18      A    C  
ANISOU  131  CB  ALA A  18     8451  11608   8883   1474   1437   1682  A    C  
ATOM    132  N   GLN A  19      97.762  87.792  25.155  1.00 68.97      A    N  
ANISOU  132  N   GLN A  19     7626  10251   8328   1222   1488   1410  A    N  
ATOM    133  CA  GLN A  19      99.158  88.124  24.879  1.00 72.71      A    C  
ANISOU  133  CA  GLN A  19     8092  10562   8969   1234   1668   1433  A    C  
ATOM    134  C   GLN A  19     100.070  86.892  24.614  1.00 72.39      A    C  
ANISOU  134  C   GLN A  19     8068  10610   8827   1197   1500   1280  A    C  
ATOM    135  O   GLN A  19     101.196  87.048  24.102  1.00 74.04      A    O  
ANISOU  135  O   GLN A  19     8260  10746   9123   1249   1645   1324  A    O  
ATOM    136  CB  GLN A  19      99.754  88.955  26.022  1.00 72.22      A    C  
ANISOU  136  CB  GLN A  19     8037  10182   9218   1056   1792   1319  A    C  
ATOM    137  CG  GLN A  19      99.150  90.331  26.258  1.00 70.97      A    C  
ANISOU  137  CG  GLN A  19     7854   9869   9241   1085   2034   1458  A    C  
ATOM    138  CD  GLN A  19      99.723  90.919  27.533  1.00 72.13      A    C  
ANISOU  138  CD  GLN A  19     7986   9750   9669    871   2094   1244  A    C  
ATOM    139  NE2 GLN A  19      98.869  91.540  28.344  1.00 75.91      A    N  
ANISOU  139  NE2 GLN A  19     8464  10154  10222    796   2105   1214  A    N  
ATOM    140  OE1 GLN A  19     100.911  90.749  27.826  1.00 69.94      A    O  
ANISOU  140  OE1 GLN A  19     7685   9368   9519    770   2109   1082  A    O  
ATOM    141  N   HIS A  20      99.595  85.697  24.985  1.00 69.23      A    N  
ANISOU  141  N   HIS A  20     7696  10338   8270   1104   1222   1102  A    N  
ATOM    142  CA  HIS A  20     100.388  84.446  24.901  1.00 66.70      A    C  
ANISOU  142  CA  HIS A  20     7394  10069   7878   1048   1060    934  A    C  
ATOM    143  C   HIS A  20      99.537  83.366  24.316  1.00 64.78      A    C  
ANISOU  143  C   HIS A  20     7128  10094   7390   1099    874    866  A    C  
ATOM    144  O   HIS A  20      99.232  82.342  24.924  1.00 60.17      A    O  
ANISOU  144  O   HIS A  20     6569   9515   6775    971    682    679  A    O  
ATOM    145  CB  HIS A  20     100.893  84.029  26.266  1.00 65.01      A    C  
ANISOU  145  CB  HIS A  20     7227   9668   7804    844    944    733  A    C  
ATOM    146  CG  HIS A  20     101.590  85.127  26.955  1.00 64.51      A    C  
ANISOU  146  CG  HIS A  20     7151   9380   7978    772   1114    737  A    C  
ATOM    147  CD2 HIS A  20     101.143  86.072  27.807  1.00 67.44      A    C  
ANISOU  147  CD2 HIS A  20     7514   9619   8490    697   1191    736  A    C  
ATOM    148  ND1 HIS A  20     102.889  85.445  26.676  1.00 66.81      A    N  
ANISOU  148  ND1 HIS A  20     7415   9566   8402    783   1259    734  A    N  
ATOM    149  CE1 HIS A  20     103.243  86.505  27.381  1.00 70.37      A    C  
ANISOU  149  CE1 HIS A  20     7831   9825   9082    699   1418    699  A    C  
ATOM    150  NE2 HIS A  20     102.197  86.907  28.076  1.00 70.68      A    N  
ANISOU  150  NE2 HIS A  20     7880   9847   9126    647   1378    697  A    N  
ATOM    151  N   THR A  21      99.157  83.649  23.092  1.00 67.81      A    N  
ANISOU  151  N   THR A  21     7444  10712   7606   1302    960   1024  A    N  
ATOM    152  CA  THR A  21      98.270  82.811  22.342  1.00 68.32      A    C  
ANISOU  152  CA  THR A  21     7439  11103   7413   1384    812    952  A    C  
ATOM    153  C   THR A  21      98.984  81.554  21.799  1.00 71.17      A    C  
ANISOU  153  C   THR A  21     7785  11583   7673   1376    694    778  A    C  
ATOM    154  O   THR A  21      98.341  80.575  21.485  1.00 71.54      A    O  
ANISOU  154  O   THR A  21     7774  11841   7565   1361    537    605  A    O  
ATOM    155  CB  THR A  21      97.674  83.613  21.199  1.00 66.71      A    C  
ANISOU  155  CB  THR A  21     7144  11168   7034   1645    958   1195  A    C  
ATOM    156  CG2 THR A  21      98.758  84.503  20.506  1.00 67.14      A    C  
ANISOU  156  CG2 THR A  21     7198  11140   7170   1814   1226   1440  A    C  
ATOM    157  OG1 THR A  21      97.136  82.690  20.274  1.00 68.25      A    O  
ANISOU  157  OG1 THR A  21     7237  11745   6948   1748    816   1083  A    O  
ATOM    158  N   ASP A  22     100.308  81.582  21.700  1.00 74.08      A    N  
ANISOU  158  N   ASP A  22     8192  11807   8145   1379    781    805  A    N  
ATOM    159  CA  ASP A  22     101.078  80.427  21.222  1.00 77.44      A    C  
ANISOU  159  CA  ASP A  22     8609  12319   8493   1372    685    648  A    C  
ATOM    160  C   ASP A  22     101.494  79.436  22.348  1.00 74.73      A    C  
ANISOU  160  C   ASP A  22     8341  11755   8295   1149    537    419  A    C  
ATOM    161  O   ASP A  22     101.703  78.260  22.121  1.00 74.12      A    O  
ANISOU  161  O   ASP A  22     8253  11752   8157   1112    425    242  A    O  
ATOM    162  CB  ASP A  22     102.313  80.927  20.462  1.00 83.22      A    C  
ANISOU  162  CB  ASP A  22     9334  13029   9254   1511    867    808  A    C  
ATOM    163  CG  ASP A  22     103.149  81.927  21.272  1.00 89.44      A    C  
ANISOU  163  CG  ASP A  22    10185  13475  10321   1426   1031    905  A    C  
ATOM    164  OD1 ASP A  22     102.564  82.788  21.974  1.00 91.69      A    O  
ANISOU  164  OD1 ASP A  22    10486  13623  10726   1369   1094    972  A    O  
ATOM    165  OD2 ASP A  22     104.401  81.873  21.185  1.00 97.16      A    O1-
ANISOU  165  OD2 ASP A  22    11177  14332  11404   1415   1108    897  A    O1-
ATOM    166  N   LYS A  23     101.598  79.937  23.568  1.00 73.88      A    N  
ANISOU  166  N   LYS A  23     8300  11389   8381   1016    556    429  A    N  
ATOM    167  CA  LYS A  23     102.121  79.197  24.700  1.00 67.79      A    C  
ANISOU  167  CA  LYS A  23     7592  10421   7741    852    458    274  A    C  
ATOM    168  C   LYS A  23     100.979  78.763  25.613  1.00 65.96      A    C  
ANISOU  168  C   LYS A  23     7380  10153   7525    738    337    179  A    C  
ATOM    169  O   LYS A  23      99.894  79.366  25.634  1.00 63.66      A    O  
ANISOU  169  O   LYS A  23     7067   9924   7196    755    347    247  A    O  
ATOM    170  CB  LYS A  23     103.080  80.087  25.531  1.00 65.50      A    C  
ANISOU  170  CB  LYS A  23     7333   9907   7643    794    566    330  A    C  
ATOM    171  CG  LYS A  23     104.099  80.853  24.722  1.00 66.60      A    C  
ANISOU  171  CG  LYS A  23     7443  10033   7829    898    746    453  A    C  
ATOM    172  CD  LYS A  23     104.436  82.204  25.307  1.00 68.84      A    C  
ANISOU  172  CD  LYS A  23     7714  10130   8311    859    918    535  A    C  
ATOM    173  CE  LYS A  23     105.069  83.053  24.223  1.00 76.49      A    C  
ANISOU  173  CE  LYS A  23     8639  11099   9322   1004   1151    709  A    C  
ATOM    174  NZ  LYS A  23     104.840  84.516  24.367  1.00 83.19      A    N1+
ANISOU  174  NZ  LYS A  23     9458  11805  10343   1023   1378    850  A    N1+
ATOM    175  N   LEU A  24     101.272  77.744  26.413  1.00 63.91      A    N  
ANISOU  175  N   LEU A  24     7163   9780   7339    632    245     41  A    N  
ATOM    176  CA  LEU A  24     100.452  77.406  27.553  1.00 59.64      A    C  
ANISOU  176  CA  LEU A  24     6653   9139   6869    523    172    -17  A    C  
ATOM    177  C   LEU A  24     100.614  78.503  28.604  1.00 58.71      A    C  
ANISOU  177  C   LEU A  24     6564   8884   6858    483    226     75  A    C  
ATOM    178  O   LEU A  24     101.700  79.063  28.770  1.00 60.75      A    O  
ANISOU  178  O   LEU A  24     6824   9070   7186    494    299    108  A    O  
ATOM    179  CB  LEU A  24     100.881  76.061  28.112  1.00 57.62      A    C  
ANISOU  179  CB  LEU A  24     6431   8784   6677    459    107   -148  A    C  
ATOM    180  CG  LEU A  24     100.622  74.830  27.246  1.00 57.44      A    C  
ANISOU  180  CG  LEU A  24     6367   8861   6594    464     63   -300  A    C  
ATOM    181  CD1 LEU A  24     101.313  73.579  27.789  1.00 57.29      A    C  
ANISOU  181  CD1 LEU A  24     6387   8700   6681    418     50   -400  A    C  
ATOM    182  CD2 LEU A  24      99.148  74.577  27.129  1.00 57.80      A    C  
ANISOU  182  CD2 LEU A  24     6362   8993   6606    421     20   -380  A    C  
ATOM    183  N   VAL A  25      99.534  78.820  29.300  1.00 57.13      A    N  
ANISOU  183  N   VAL A  25     6371   8658   6675    433    200     95  A    N  
ATOM    184  CA  VAL A  25      99.596  79.777  30.380  1.00 56.98      A    C  
ANISOU  184  CA  VAL A  25     6366   8529   6753    387    243    146  A    C  
ATOM    185  C   VAL A  25      99.161  79.103  31.652  1.00 58.61      A    C  
ANISOU  185  C   VAL A  25     6604   8663   7001    313    161     88  A    C  
ATOM    186  O   VAL A  25      98.018  78.643  31.739  1.00 62.22      A    O  
ANISOU  186  O   VAL A  25     7065   9141   7433    286    112     73  A    O  
ATOM    187  CB  VAL A  25      98.664  80.955  30.146  1.00 56.22      A    C  
ANISOU  187  CB  VAL A  25     6246   8467   6645    414    314    255  A    C  
ATOM    188  CG1 VAL A  25      98.645  81.854  31.376  1.00 54.84      A    C  
ANISOU  188  CG1 VAL A  25     6076   8176   6582    348    355    264  A    C  
ATOM    189  CG2 VAL A  25      99.100  81.700  28.900  1.00 57.23      A    C  
ANISOU  189  CG2 VAL A  25     6337   8665   6742    525    441    361  A    C  
ATOM    190  N   PHE A  26     100.101  79.015  32.600  1.00 59.07      A    N  
ANISOU  190  N   PHE A  26     6669   8654   7118    295    159     54  A    N  
ATOM    191  CA  PHE A  26      99.854  78.570  33.974  1.00 57.29      A    C  
ANISOU  191  CA  PHE A  26     6462   8384   6922    266    110     40  A    C  
ATOM    192  C   PHE A  26      99.334  79.731  34.733  1.00 55.34      A    C  
ANISOU  192  C   PHE A  26     6192   8134   6700    236    137     72  A    C  
ATOM    193  O   PHE A  26     100.109  80.595  35.115  1.00 58.63      A    O  
ANISOU  193  O   PHE A  26     6564   8553   7157    231    186     41  A    O  
ATOM    194  CB  PHE A  26     101.146  78.106  34.663  1.00 57.21      A    C  
ANISOU  194  CB  PHE A  26     6438   8369   6927    295    101     -4  A    C  
ATOM    195  CG  PHE A  26     101.463  76.655  34.435  1.00 57.90      A    C  
ANISOU  195  CG  PHE A  26     6558   8427   7011    327     73    -27  A    C  
ATOM    196  CD1 PHE A  26     100.937  75.976  33.326  1.00 57.40      A    C  
ANISOU  196  CD1 PHE A  26     6515   8356   6936    315     66    -57  A    C  
ATOM    197  CD2 PHE A  26     102.295  75.975  35.313  1.00 56.97      A    C  
ANISOU  197  CD2 PHE A  26     6436   8307   6900    379     66    -28  A    C  
ATOM    198  CE1 PHE A  26     101.213  74.641  33.131  1.00 58.67      A    C  
ANISOU  198  CE1 PHE A  26     6695   8470   7126    331     64   -108  A    C  
ATOM    199  CE2 PHE A  26     102.585  74.648  35.102  1.00 58.08      A    C  
ANISOU  199  CE2 PHE A  26     6607   8394   7064    415     72    -38  A    C  
ATOM    200  CZ  PHE A  26     102.040  73.977  34.017  1.00 59.16      A    C  
ANISOU  200  CZ  PHE A  26     6769   8484   7223    380     77    -87  A    C  
ATOM    201  N   TYR A  27      98.033  79.748  34.958  1.00 52.81      A    N  
ANISOU  201  N   TYR A  27     5889   7807   6366    212    114    114  A    N  
ATOM    202  CA  TYR A  27      97.416  80.841  35.673  1.00 51.69      A    C  
ANISOU  202  CA  TYR A  27     5729   7662   6248    185    143    146  A    C  
ATOM    203  C   TYR A  27      97.341  80.425  37.102  1.00 49.93      A    C  
ANISOU  203  C   TYR A  27     5507   7440   6022    186     99    136  A    C  
ATOM    204  O   TYR A  27      96.724  79.434  37.395  1.00 50.59      A    O  
ANISOU  204  O   TYR A  27     5626   7497   6098    193     62    163  A    O  
ATOM    205  CB  TYR A  27      96.035  81.058  35.121  1.00 52.03      A    C  
ANISOU  205  CB  TYR A  27     5782   7720   6264    173    142    206  A    C  
ATOM    206  CG  TYR A  27      95.422  82.419  35.343  1.00 52.74      A    C  
ANISOU  206  CG  TYR A  27     5850   7805   6382    160    207    260  A    C  
ATOM    207  CD1 TYR A  27      95.867  83.542  34.654  1.00 51.50      A    C  
ANISOU  207  CD1 TYR A  27     5662   7636   6268    185    321    296  A    C  
ATOM    208  CD2 TYR A  27      94.312  82.552  36.178  1.00 54.64      A    C  
ANISOU  208  CD2 TYR A  27     6099   8039   6622    129    178    288  A    C  
ATOM    209  CE1 TYR A  27      95.243  84.754  34.812  1.00 52.10      A    C  
ANISOU  209  CE1 TYR A  27     5716   7683   6395    179    411    353  A    C  
ATOM    210  CE2 TYR A  27      93.677  83.773  36.356  1.00 54.22      A    C  
ANISOU  210  CE2 TYR A  27     6026   7976   6599    119    245    337  A    C  
ATOM    211  CZ  TYR A  27      94.148  84.868  35.664  1.00 53.86      A    C  
ANISOU  211  CZ  TYR A  27     5948   7907   6606    144    365    367  A    C  
ATOM    212  OH  TYR A  27      93.510  86.074  35.829  1.00 55.11      A    O  
ANISOU  212  OH  TYR A  27     6085   8031   6821    139    461    422  A    O  
ATOM    213  N   ARG A  28      98.002  81.139  37.994  1.00 49.47      A    N  
ANISOU  213  N   ARG A  28     5397   7425   5974    189    118     87  A    N  
ATOM    214  CA  ARG A  28      97.920  80.778  39.388  1.00 50.52      A    C  
ANISOU  214  CA  ARG A  28     5512   7619   6065    227     78     90  A    C  
ATOM    215  C   ARG A  28      96.500  80.954  39.902  1.00 52.19      A    C  
ANISOU  215  C   ARG A  28     5749   7807   6271    208     70    162  A    C  
ATOM    216  O   ARG A  28      95.901  81.979  39.739  1.00 54.93      A    O  
ANISOU  216  O   ARG A  28     6083   8141   6645    161    102    161  A    O  
ATOM    217  CB  ARG A  28      98.861  81.609  40.233  1.00 50.12      A    C  
ANISOU  217  CB  ARG A  28     5361   7679   6002    236     93    -19  A    C  
ATOM    218  CG  ARG A  28      98.748  81.310  41.731  1.00 50.50      A    C  
ANISOU  218  CG  ARG A  28     5365   7859   5960    312     51    -10  A    C  
ATOM    219  CD  ARG A  28      99.590  80.151  42.219  1.00 50.88      A    C  
ANISOU  219  CD  ARG A  28     5402   7993   5936    425     19     21  A    C  
ATOM    220  NE  ARG A  28     100.786  80.680  42.864  1.00 51.92      A    N  
ANISOU  220  NE  ARG A  28     5401   8317   6009    462      9   -122  A    N  
ATOM    221  CZ  ARG A  28     100.980  80.740  44.177  1.00 54.10      A    C  
ANISOU  221  CZ  ARG A  28     5576   8814   6164    562    -19   -152  A    C  
ATOM    222  NH1 ARG A  28     100.088  80.277  45.021  1.00 55.93      A    N1+
ANISOU  222  NH1 ARG A  28     5841   9084   6324    650    -27    -12  A    N1+
ATOM    223  NH2 ARG A  28     102.094  81.251  44.665  1.00 56.69      A    N  
ANISOU  223  NH2 ARG A  28     5753   9351   6434    586    -31   -331  A    N  
ATOM    224  N   MET A  29      95.964  79.947  40.548  1.00 53.32      A    N  
ANISOU  224  N   MET A  29     5926   7936   6396    252     47    235  A    N  
ATOM    225  CA  MET A  29      94.656  80.056  41.066  1.00 56.05      A    C  
ANISOU  225  CA  MET A  29     6291   8256   6748    235     51    305  A    C  
ATOM    226  C   MET A  29      94.719  79.403  42.428  1.00 56.43      A    C  
ANISOU  226  C   MET A  29     6326   8361   6751    334     55    374  A    C  
ATOM    227  O   MET A  29      94.487  78.219  42.568  1.00 60.62      A    O  
ANISOU  227  O   MET A  29     6896   8817   7318    380     84    453  A    O  
ATOM    228  CB  MET A  29      93.712  79.299  40.115  1.00 63.46      A    C  
ANISOU  228  CB  MET A  29     7281   9088   7743    186     54    333  A    C  
ATOM    229  CG  MET A  29      92.327  79.892  39.945  1.00 66.40      A    C  
ANISOU  229  CG  MET A  29     7656   9442   8129    129     58    364  A    C  
ATOM    230  SD  MET A  29      92.459  81.584  39.416  1.00 68.12      A    S  
ANISOU  230  SD  MET A  29     7840   9716   8327     99     80    337  A    S  
ATOM    231  CE  MET A  29      90.819  81.762  38.679  1.00 77.95      A    C  
ANISOU  231  CE  MET A  29     9090  10951   9575     57     80    386  A    C  
ATOM    232  N   GLY A  30      95.047  80.166  43.444  1.00 56.86      A    N  
ANISOU  232  N   GLY A  30     6312   8562   6729    380     45    342  A    N  
ATOM    233  CA  GLY A  30      95.051  79.657  44.803  1.00 57.31      A    C  
ANISOU  233  CA  GLY A  30     6336   8736   6702    514     54    429  A    C  
ATOM    234  C   GLY A  30      96.313  78.911  45.023  1.00 59.23      A    C  
ANISOU  234  C   GLY A  30     6545   9070   6890    623     52    428  A    C  
ATOM    235  O   GLY A  30      97.349  79.451  44.850  1.00 59.13      A    O  
ANISOU  235  O   GLY A  30     6466   9160   6840    610     21    297  A    O  
ATOM    236  N   ASP A  31      96.204  77.641  45.377  1.00 64.75      A    N  
ANISOU  236  N   ASP A  31     7285   9711   7602    732    106    577  A    N  
ATOM    237  CA  ASP A  31      97.338  76.753  45.574  1.00 66.57      A    C  
ANISOU  237  CA  ASP A  31     7493  10010   7788    862    128    616  A    C  
ATOM    238  C   ASP A  31      97.594  75.930  44.328  1.00 64.13      A    C  
ANISOU  238  C   ASP A  31     7261   9494   7609    785    152    595  A    C  
ATOM    239  O   ASP A  31      98.287  74.926  44.366  1.00 66.60      A    O  
ANISOU  239  O   ASP A  31     7583   9784   7935    886    200    659  A    O  
ATOM    240  CB  ASP A  31      97.003  75.787  46.717  1.00 74.68      A    C  
ANISOU  240  CB  ASP A  31     8521  11071   8780   1057    222    831  A    C  
ATOM    241  CG  ASP A  31      97.342  76.348  48.067  1.00 81.12      A    C  
ANISOU  241  CG  ASP A  31     9217  12211   9394   1220    195    854  A    C  
ATOM    242  OD1 ASP A  31      98.482  76.887  48.206  1.00 90.78      A    O  
ANISOU  242  OD1 ASP A  31    10334  13663  10492   1252    121    708  A    O  
ATOM    243  OD2 ASP A  31      96.479  76.223  48.971  1.00 81.62      A    O1-
ANISOU  243  OD2 ASP A  31     9280  12308   9422   1319    254   1004  A    O1-
ATOM    244  N   PHE A  32      96.987  76.312  43.224  1.00 61.91      A    N  
ANISOU  244  N   PHE A  32     7030   9074   7419    624    127    510  A    N  
ATOM    245  CA  PHE A  32      97.153  75.591  41.982  1.00 61.19      A    C  
ANISOU  245  CA  PHE A  32     6990   8830   7426    553    141    461  A    C  
ATOM    246  C   PHE A  32      97.523  76.553  40.871  1.00 59.48      A    C  
ANISOU  246  C   PHE A  32     6762   8640   7196    444     80    328  A    C  
ATOM    247  O   PHE A  32      97.233  77.748  40.938  1.00 61.33      A    O  
ANISOU  247  O   PHE A  32     6966   8937   7398    391     53    285  A    O  
ATOM    248  CB  PHE A  32      95.865  74.873  41.603  1.00 60.90      A    C  
ANISOU  248  CB  PHE A  32     7008   8611   7518    484    199    496  A    C  
ATOM    249  CG  PHE A  32      95.446  73.860  42.603  1.00 64.26      A    C  
ANISOU  249  CG  PHE A  32     7448   8955   8010    590    310    645  A    C  
ATOM    250  CD1 PHE A  32      94.772  74.244  43.728  1.00 64.13      A    C  
ANISOU  250  CD1 PHE A  32     7416   9002   7948    655    333    757  A    C  
ATOM    251  CD2 PHE A  32      95.742  72.510  42.417  1.00 69.42      A    C  
ANISOU  251  CD2 PHE A  32     8128   9459   8786    637    416    683  A    C  
ATOM    252  CE1 PHE A  32      94.369  73.321  44.643  1.00 67.36      A    C  
ANISOU  252  CE1 PHE A  32     7836   9331   8425    777    467    928  A    C  
ATOM    253  CE2 PHE A  32      95.353  71.570  43.339  1.00 70.26      A    C  
ANISOU  253  CE2 PHE A  32     8247   9460   8990    754    568    850  A    C  
ATOM    254  CZ  PHE A  32      94.670  71.987  44.458  1.00 71.66      A    C  
ANISOU  254  CZ  PHE A  32     8407   9708   9111    831    595    984  A    C  
ATOM    255  N   TYR A  33      98.184  76.018  39.861  1.00 54.92      A    N  
ANISOU  255  N   TYR A  33     6204   8008   6653    423     80    270  A    N  
ATOM    256  CA  TYR A  33      98.200  76.656  38.615  1.00 52.12      A    C  
ANISOU  256  CA  TYR A  33     5851   7645   6306    336     55    188  A    C  
ATOM    257  C   TYR A  33      97.148  75.939  37.760  1.00 52.76      A    C  
ANISOU  257  C   TYR A  33     5969   7625   6451    274     69    172  A    C  
ATOM    258  O   TYR A  33      97.160  74.719  37.627  1.00 52.93      A    O  
ANISOU  258  O   TYR A  33     6011   7558   6539    288    105    163  A    O  
ATOM    259  CB  TYR A  33      99.574  76.523  38.040  1.00 51.88      A    C  
ANISOU  259  CB  TYR A  33     5804   7650   6258    363     51    127  A    C  
ATOM    260  CG  TYR A  33     100.612  77.361  38.723  1.00 50.78      A    C  
ANISOU  260  CG  TYR A  33     5592   7633   6065    399     42     85  A    C  
ATOM    261  CD1 TYR A  33     100.774  78.687  38.414  1.00 49.75      A    C  
ANISOU  261  CD1 TYR A  33     5417   7539   5944    338     54     18  A    C  
ATOM    262  CD2 TYR A  33     101.473  76.798  39.617  1.00 51.94      A    C  
ANISOU  262  CD2 TYR A  33     5702   7866   6165    501     37    100  A    C  
ATOM    263  CE1 TYR A  33     101.759  79.446  39.014  1.00 49.92      A    C  
ANISOU  263  CE1 TYR A  33     5346   7670   5950    349     64    -74  A    C  
ATOM    264  CE2 TYR A  33     102.462  77.535  40.229  1.00 52.19      A    C  
ANISOU  264  CE2 TYR A  33     5635   8057   6137    532     22     18  A    C  
ATOM    265  CZ  TYR A  33     102.609  78.866  39.934  1.00 51.04      A    C  
ANISOU  265  CZ  TYR A  33     5432   7937   6023    442     35    -93  A    C  
ATOM    266  OH  TYR A  33     103.627  79.578  40.569  1.00 51.05      A    O  
ANISOU  266  OH  TYR A  33     5303   8099   5992    456     36   -229  A    O  
ATOM    267  N   GLU A  34      96.229  76.694  37.185  1.00 53.22      A    N  
ANISOU  267  N   GLU A  34     6019   7704   6496    210     52    157  A    N  
ATOM    268  CA  GLU A  34      95.230  76.123  36.316  1.00 55.34      A    C  
ANISOU  268  CA  GLU A  34     6285   7940   6799    154     52    105  A    C  
ATOM    269  C   GLU A  34      95.429  76.582  34.895  1.00 55.20      A    C  
ANISOU  269  C   GLU A  34     6241   8017   6716    145     31     45  A    C  
ATOM    270  O   GLU A  34      96.105  77.561  34.653  1.00 54.11      A    O  
ANISOU  270  O   GLU A  34     6094   7934   6530    172     37     77  A    O  
ATOM    271  CB  GLU A  34      93.854  76.537  36.777  1.00 57.44      A    C  
ANISOU  271  CB  GLU A  34     6543   8197   7080    112     53    145  A    C  
ATOM    272  CG  GLU A  34      93.503  76.025  38.162  1.00 62.02      A    C  
ANISOU  272  CG  GLU A  34     7145   8692   7724    140     96    227  A    C  
ATOM    273  CD  GLU A  34      92.034  76.247  38.532  1.00 64.60      A    C  
ANISOU  273  CD  GLU A  34     7463   8994   8087     90    109    258  A    C  
ATOM    274  OE1 GLU A  34      91.349  76.969  37.778  1.00 68.14      A    O  
ANISOU  274  OE1 GLU A  34     7884   9513   8490     40     73    221  A    O  
ATOM    275  OE2 GLU A  34      91.563  75.686  39.556  1.00 65.72      A    O1-
ANISOU  275  OE2 GLU A  34     7619   9049   8301    115    169    335  A    O1-
ATOM    276  N   LEU A  35      94.865  75.826  33.964  1.00 57.81      A    N  
ANISOU  276  N   LEU A  35     6540   8371   7050    114     23    -50  A    N  
ATOM    277  CA  LEU A  35      94.843  76.174  32.550  1.00 60.06      A    C  
ANISOU  277  CA  LEU A  35     6776   8804   7236    134      4   -101  A    C  
ATOM    278  C   LEU A  35      93.395  76.115  32.063  1.00 58.89      A    C  
ANISOU  278  C   LEU A  35     6563   8750   7059     94    -18   -165  A    C  
ATOM    279  O   LEU A  35      92.608  75.324  32.553  1.00 57.98      A    O  
ANISOU  279  O   LEU A  35     6436   8552   7039     27     -9   -235  A    O  
ATOM    280  CB  LEU A  35      95.740  75.213  31.717  1.00 61.15      A    C  
ANISOU  280  CB  LEU A  35     6902   8960   7369    155      3   -207  A    C  
ATOM    281  CG  LEU A  35      97.218  75.147  32.093  1.00 59.92      A    C  
ANISOU  281  CG  LEU A  35     6796   8732   7238    199     22   -162  A    C  
ATOM    282  CD1 LEU A  35      97.471  73.995  33.022  1.00 59.97      A    C  
ANISOU  282  CD1 LEU A  35     6836   8588   7358    185     49   -180  A    C  
ATOM    283  CD2 LEU A  35      98.071  74.945  30.859  1.00 62.91      A    C  
ANISOU  283  CD2 LEU A  35     7148   9205   7547    246     22   -221  A    C  
ATOM    284  N   PHE A  36      93.061  76.932  31.074  1.00 59.60      A    N  
ANISOU  284  N   PHE A  36     6601   9022   7022    148    -29   -138  A    N  
ATOM    285  CA  PHE A  36      91.693  76.973  30.570  1.00 60.44      A    C  
ANISOU  285  CA  PHE A  36     6620   9276   7066    133    -55   -199  A    C  
ATOM    286  C   PHE A  36      91.565  76.771  29.078  1.00 60.18      A    C  
ANISOU  286  C   PHE A  36     6478   9504   6881    201    -82   -303  A    C  
ATOM    287  O   PHE A  36      92.510  76.945  28.293  1.00 60.94      A    O  
ANISOU  287  O   PHE A  36     6574   9686   6892    290    -67   -269  A    O  
ATOM    288  CB  PHE A  36      91.055  78.315  30.934  1.00 61.08      A    C  
ANISOU  288  CB  PHE A  36     6714   9384   7109    166    -34    -38  A    C  
ATOM    289  CG  PHE A  36      91.094  78.618  32.395  1.00 59.28      A    C  
ANISOU  289  CG  PHE A  36     6569   8955   7000    111    -14     48  A    C  
ATOM    290  CD1 PHE A  36      90.324  77.907  33.279  1.00 57.72      A    C  
ANISOU  290  CD1 PHE A  36     6379   8650   6901     32    -23     -2  A    C  
ATOM    291  CD2 PHE A  36      91.930  79.587  32.877  1.00 61.05      A    C  
ANISOU  291  CD2 PHE A  36     6847   9109   7239    147     29    164  A    C  
ATOM    292  CE1 PHE A  36      90.367  78.156  34.627  1.00 57.77      A    C  
ANISOU  292  CE1 PHE A  36     6450   8512   6986     12     -2     89  A    C  
ATOM    293  CE2 PHE A  36      91.989  79.850  34.234  1.00 61.67      A    C  
ANISOU  293  CE2 PHE A  36     6975   9058   7399    109     39    212  A    C  
ATOM    294  CZ  PHE A  36      91.196  79.133  35.113  1.00 59.42      A    C  
ANISOU  294  CZ  PHE A  36     6701   8697   7176     55     18    187  A    C  
ATOM    295  N   LEU A  37      90.361  76.420  28.690  1.00 60.52      A    N  
ANISOU  295  N   LEU A  37     6414   9699   6880    169   -117   -435  A    N  
ATOM    296  CA  LEU A  37      90.049  76.302  27.291  1.00 65.46      A    C  
ANISOU  296  CA  LEU A  37     6897  10656   7319    253   -152   -551  A    C  
ATOM    297  C   LEU A  37      90.970  75.266  26.569  1.00 70.17      A    C  
ANISOU  297  C   LEU A  37     7463  11294   7904    257   -163   -724  A    C  
ATOM    298  O   LEU A  37      91.137  74.129  27.033  1.00 67.22      A    O  
ANISOU  298  O   LEU A  37     7104  10735   7699    136   -154   -890  A    O  
ATOM    299  CB  LEU A  37      90.075  77.712  26.674  1.00 64.62      A    C  
ANISOU  299  CB  LEU A  37     6781  10734   7036    423   -118   -317  A    C  
ATOM    300  CG  LEU A  37      89.205  78.761  27.422  1.00 61.91      A    C  
ANISOU  300  CG  LEU A  37     6473  10324   6723    418    -90   -148  A    C  
ATOM    301  CD1 LEU A  37      89.461  80.182  26.951  1.00 62.70      A    C  
ANISOU  301  CD1 LEU A  37     6588  10514   6718    585     -1    111  A    C  
ATOM    302  CD2 LEU A  37      87.732  78.506  27.249  1.00 63.55      A    C  
ANISOU  302  CD2 LEU A  37     6552  10723   6871    384   -144   -279  A    C  
ATOM    303  N   ASP A  38      91.561  75.638  25.438  1.00 75.96      A    N  
ANISOU  303  N   ASP A  38     8147  12263   8449    403   -163   -675  A    N  
ATOM    304  CA  ASP A  38      92.368  74.690  24.697  1.00 78.80      A    C  
ANISOU  304  CA  ASP A  38     8464  12696   8780    415   -176   -848  A    C  
ATOM    305  C   ASP A  38      93.639  74.378  25.473  1.00 76.05      A    C  
ANISOU  305  C   ASP A  38     8269  12018   8605    360   -134   -772  A    C  
ATOM    306  O   ASP A  38      94.203  73.298  25.328  1.00 81.65      A    O  
ANISOU  306  O   ASP A  38     8972  12661   9388    308   -134   -943  A    O  
ATOM    307  CB  ASP A  38      92.631  75.198  23.269  1.00 84.46      A    C  
ANISOU  307  CB  ASP A  38     9076  13788   9225    616   -177   -793  A    C  
ATOM    308  CG  ASP A  38      91.346  75.259  22.433  1.00 90.45      A    C  
ANISOU  308  CG  ASP A  38     9636  14951   9776    687   -231   -922  A    C  
ATOM    309  OD1 ASP A  38      90.366  74.569  22.771  1.00 91.23      A    O  
ANISOU  309  OD1 ASP A  38     9653  15048   9960    546   -278  -1158  A    O  
ATOM    310  OD2 ASP A  38      91.302  76.008  21.434  1.00103.25      A    O1-
ANISOU  310  OD2 ASP A  38    11173  16908  11150    897   -213   -785  A    O1-
ATOM    311  N   ASP A  39      94.097  75.319  26.296  1.00 74.17      A    N  
ANISOU  311  N   ASP A  39     8154  11590   8433    376    -93   -535  A    N  
ATOM    312  CA  ASP A  39      95.274  75.069  27.125  1.00 73.32      A    C  
ANISOU  312  CA  ASP A  39     8169  11215   8473    334    -60   -475  A    C  
ATOM    313  C   ASP A  39      94.969  73.932  28.082  1.00 72.64      A    C  
ANISOU  313  C   ASP A  39     8112  10916   8571    202    -63   -605  A    C  
ATOM    314  O   ASP A  39      95.825  73.114  28.386  1.00 72.79      A    O  
ANISOU  314  O   ASP A  39     8180  10786   8692    178    -38   -653  A    O  
ATOM    315  CB  ASP A  39      95.695  76.311  27.912  1.00 73.36      A    C  
ANISOU  315  CB  ASP A  39     8263  11088   8519    360    -13   -250  A    C  
ATOM    316  CG  ASP A  39      96.519  77.297  27.079  1.00 74.80      A    C  
ANISOU  316  CG  ASP A  39     8441  11374   8604    489     51   -106  A    C  
ATOM    317  OD1 ASP A  39      96.520  77.180  25.847  1.00 82.93      A    O  
ANISOU  317  OD1 ASP A  39     9393  12628   9486    587     51   -136  A    O  
ATOM    318  OD2 ASP A  39      97.188  78.189  27.650  1.00 73.15      A    O1-
ANISOU  318  OD2 ASP A  39     8291  11030   8470    496    117     29  A    O1-
ATOM    319  N   ALA A  40      93.727  73.861  28.522  1.00 72.33      A    N  
ANISOU  319  N   ALA A  40     8035  10863   8581    130    -72   -654  A    N  
ATOM    320  CA  ALA A  40      93.305  72.769  29.369  1.00 74.27      A    C  
ANISOU  320  CA  ALA A  40     8293  10899   9026     17    -34   -766  A    C  
ATOM    321  C   ALA A  40      93.337  71.419  28.647  1.00 79.37      A    C  
ANISOU  321  C   ALA A  40     8850  11569   9738    -38    -13  -1035  A    C  
ATOM    322  O   ALA A  40      93.832  70.432  29.193  1.00 78.67      A    O  
ANISOU  322  O   ALA A  40     8808  11255   9826    -85     59  -1083  A    O  
ATOM    323  CB  ALA A  40      91.916  73.037  29.886  1.00 74.02      A    C  
ANISOU  323  CB  ALA A  40     8224  10863   9037    -47    -36   -768  A    C  
ATOM    324  N   VAL A  41      92.812  71.385  27.419  1.00 85.05      A    N  
ANISOU  324  N   VAL A  41     9428  12576  10307    -20    -64  -1213  A    N  
ATOM    325  CA  VAL A  41      92.712  70.145  26.632  1.00 83.78      A    C  
ANISOU  325  CA  VAL A  41     9141  12493  10197    -82    -46  -1534  A    C  
ATOM    326  C   VAL A  41      94.097  69.661  26.253  1.00 83.24      A    C  
ANISOU  326  C   VAL A  41     9128  12374  10124    -28    -28  -1537  A    C  
ATOM    327  O   VAL A  41      94.348  68.467  26.255  1.00 80.22      A    O  
ANISOU  327  O   VAL A  41     8719  11851   9909   -103     40  -1732  A    O  
ATOM    328  CB  VAL A  41      91.894  70.376  25.349  1.00 84.41      A    C  
ANISOU  328  CB  VAL A  41     9029  12990  10051    -37   -123  -1721  A    C  
ATOM    329  CG1 VAL A  41      91.865  69.124  24.486  1.00 90.25      A    C  
ANISOU  329  CG1 VAL A  41     9609  13853  10826   -101   -109  -2102  A    C  
ATOM    330  CG2 VAL A  41      90.492  70.839  25.698  1.00 83.01      A    C  
ANISOU  330  CG2 VAL A  41     8782  12883   9873    -88   -143  -1728  A    C  
ATOM    331  N   GLU A  42      94.975  70.600  25.913  1.00 85.42      A    N  
ANISOU  331  N   GLU A  42     9470  12756  10227    102    -67  -1325  A    N  
ATOM    332  CA  GLU A  42      96.356  70.296  25.598  1.00 93.58      A    C  
ANISOU  332  CA  GLU A  42    10562  13743  11249    164    -48  -1294  A    C  
ATOM    333  C   GLU A  42      97.056  69.684  26.826  1.00 91.74      A    C  
ANISOU  333  C   GLU A  42    10458  13153  11244    107     23  -1213  A    C  
ATOM    334  O   GLU A  42      97.669  68.617  26.757  1.00 90.99      A    O  
ANISOU  334  O   GLU A  42    10365  12941  11265     81     77  -1337  A    O  
ATOM    335  CB  GLU A  42      97.085  71.575  25.148  1.00100.96      A    C  
ANISOU  335  CB  GLU A  42    11543  14822  11995    308    -72  -1054  A    C  
ATOM    336  CG  GLU A  42      96.994  71.868  23.658  1.00107.65      A    C  
ANISOU  336  CG  GLU A  42    12263  16041  12595    433   -108  -1116  A    C  
ATOM    337  CD  GLU A  42      97.836  70.899  22.846  1.00115.86      A    C  
ANISOU  337  CD  GLU A  42    13257  17157  13606    457   -104  -1296  A    C  
ATOM    338  OE1 GLU A  42      99.059  70.766  23.118  1.00111.46      A    O  
ANISOU  338  OE1 GLU A  42    12802  16421  13123    474    -67  -1200  A    O  
ATOM    339  OE2 GLU A  42      97.266  70.271  21.931  1.00125.33      A    O1-
ANISOU  339  OE2 GLU A  42    14300  18615  14702    460   -138  -1552  A    O1-
ATOM    340  N   ALA A  43      96.960  70.369  27.955  1.00 87.82      A    N  
ANISOU  340  N   ALA A  43    10056  12506  10804    105     33  -1001  A    N  
ATOM    341  CA  ALA A  43      97.688  69.953  29.148  1.00 83.42      A    C  
ANISOU  341  CA  ALA A  43     9605  11683  10405    101     97   -881  A    C  
ATOM    342  C   ALA A  43      97.147  68.666  29.723  1.00 82.94      A    C  
ANISOU  342  C   ALA A  43     9531  11410  10572     15    196  -1006  A    C  
ATOM    343  O   ALA A  43      97.891  67.870  30.281  1.00 84.82      A    O  
ANISOU  343  O   ALA A  43     9824  11458  10944     37    280   -970  A    O  
ATOM    344  CB  ALA A  43      97.662  71.050  30.189  1.00 79.88      A    C  
ANISOU  344  CB  ALA A  43     9232  11184   9933    131     79   -653  A    C  
ATOM    345  N   ALA A  44      95.854  68.450  29.572  1.00 81.51      A    N  
ANISOU  345  N   ALA A  44     9265  11258  10446    -74    207  -1152  A    N  
ATOM    346  CA  ALA A  44      95.261  67.211  30.007  1.00 83.48      A    C  
ANISOU  346  CA  ALA A  44     9476  11285  10954   -170    339  -1301  A    C  
ATOM    347  C   ALA A  44      95.754  66.031  29.167  1.00 87.43      A    C  
ANISOU  347  C   ALA A  44     9908  11764  11548   -204    404  -1554  A    C  
ATOM    348  O   ALA A  44      95.882  64.931  29.692  1.00 89.18      A    O  
ANISOU  348  O   ALA A  44    10144  11717  12021   -243    561  -1605  A    O  
ATOM    349  CB  ALA A  44      93.771  67.303  29.898  1.00 88.16      A    C  
ANISOU  349  CB  ALA A  44     9966  11947  11584   -270    335  -1443  A    C  
ATOM    350  N   LYS A  45      96.005  66.242  27.869  1.00 88.36      A    N  
ANISOU  350  N   LYS A  45     9940  12163  11467   -180    304  -1709  A    N  
ATOM    351  CA  LYS A  45      96.590  65.188  27.014  1.00 91.43      A    C  
ANISOU  351  CA  LYS A  45    10258  12568  11912   -199    353  -1959  A    C  
ATOM    352  C   LYS A  45      98.019  64.947  27.434  1.00 88.85      A    C  
ANISOU  352  C   LYS A  45    10062  12072  11624   -110    398  -1774  A    C  
ATOM    353  O   LYS A  45      98.385  63.807  27.726  1.00 88.49      A    O  
ANISOU  353  O   LYS A  45    10028  11788  11806   -141    539  -1858  A    O  
ATOM    354  CB  LYS A  45      96.584  65.565  25.518  1.00 96.40      A    C  
ANISOU  354  CB  LYS A  45    10759  13599  12268   -153    227  -2137  A    C  
ATOM    355  CG  LYS A  45      95.475  64.932  24.681  1.00103.81      A    C  
ANISOU  355  CG  LYS A  45    11485  14732  13225   -258    231  -2533  A    C  
ATOM    356  CD  LYS A  45      94.991  65.841  23.540  1.00113.15      A    C  
ANISOU  356  CD  LYS A  45    12537  16391  14062   -168     80  -2587  A    C  
ATOM    357  CE  LYS A  45      96.095  66.668  22.859  1.00116.10      A    C  
ANISOU  357  CE  LYS A  45    12979  16972  14161     13     -4  -2365  A    C  
ATOM    358  NZ  LYS A  45      97.172  65.878  22.195  1.00119.91      A    N1+
ANISOU  358  NZ  LYS A  45    13447  17469  14642     47     25  -2502  A    N1+
ATOM    359  N   LEU A  46      98.811  66.028  27.460  1.00 83.76      A    N  
ANISOU  359  N   LEU A  46     9503  11548  10772      3    295  -1532  A    N  
ATOM    360  CA  LEU A  46     100.254  65.940  27.622  1.00 80.27      A    C  
ANISOU  360  CA  LEU A  46     9153  11033  10315     96    309  -1390  A    C  
ATOM    361  C   LEU A  46     100.663  65.403  28.977  1.00 82.78      A    C  
ANISOU  361  C   LEU A  46     9569  11055  10829    118    424  -1221  A    C  
ATOM    362  O   LEU A  46     101.624  64.632  29.081  1.00 87.11      A    O  
ANISOU  362  O   LEU A  46    10151  11478  11465    167    502  -1211  A    O  
ATOM    363  CB  LEU A  46     100.897  67.301  27.411  1.00 76.12      A    C  
ANISOU  363  CB  LEU A  46     8673  10688   9559    193    199  -1187  A    C  
ATOM    364  CG  LEU A  46     100.730  67.889  26.028  1.00 77.85      A    C  
ANISOU  364  CG  LEU A  46     8802  11218   9558    233    115  -1280  A    C  
ATOM    365  CD1 LEU A  46     101.309  69.287  26.011  1.00 79.26      A    C  
ANISOU  365  CD1 LEU A  46     9034  11500   9579    328     65  -1040  A    C  
ATOM    366  CD2 LEU A  46     101.429  67.038  24.983  1.00 80.46      A    C  
ANISOU  366  CD2 LEU A  46     9073  11640   9855    259    130  -1470  A    C  
ATOM    367  N   LEU A  47      99.953  65.803  30.023  1.00 83.95      A    N  
ANISOU  367  N   LEU A  47     9754  11107  11034    105    443  -1075  A    N  
ATOM    368  CA  LEU A  47     100.445  65.552  31.378  1.00 88.44      A    C  
ANISOU  368  CA  LEU A  47    10412  11476  11715    183    535   -850  A    C  
ATOM    369  C   LEU A  47      99.754  64.404  32.123  1.00 90.17      A    C  
ANISOU  369  C   LEU A  47    10625  11420  12215    145    727   -872  A    C  
ATOM    370  O   LEU A  47     100.123  64.070  33.281  1.00 85.39      A    O  
ANISOU  370  O   LEU A  47    10083  10654  11705    245    838   -658  A    O  
ATOM    371  CB  LEU A  47     100.345  66.833  32.187  1.00 90.43      A    C  
ANISOU  371  CB  LEU A  47    10710  11822  11826    231    443   -634  A    C  
ATOM    372  CG  LEU A  47     101.155  68.006  31.618  1.00 94.69      A    C  
ANISOU  372  CG  LEU A  47    11256  12577  12142    277    307   -583  A    C  
ATOM    373  CD1 LEU A  47     101.000  69.219  32.513  1.00 96.78      A    C  
ANISOU  373  CD1 LEU A  47    11551  12902  12319    307    250   -407  A    C  
ATOM    374  CD2 LEU A  47     102.630  67.662  31.435  1.00 97.32      A    C  
ANISOU  374  CD2 LEU A  47    11615  12912  12451    361    319   -556  A    C  
ATOM    375  N   ASP A  48      98.790  63.784  31.438  1.00 90.06      A    N  
ANISOU  375  N   ASP A  48    10518  11365  12334     14    784  -1135  A    N  
ATOM    376  CA  ASP A  48      97.994  62.713  32.001  1.00 90.74      A    C  
ANISOU  376  CA  ASP A  48    10573  11169  12734    -53    998  -1205  A    C  
ATOM    377  C   ASP A  48      97.432  63.177  33.340  1.00 84.76      A    C  
ANISOU  377  C   ASP A  48     9879  10314  12012      1   1043   -936  A    C  
ATOM    378  O   ASP A  48      97.559  62.500  34.354  1.00 81.50      A    O  
ANISOU  378  O   ASP A  48     9513   9662  11789     81   1232   -761  A    O  
ATOM    379  CB  ASP A  48      98.846  61.451  32.149  1.00102.14      A    C  
ANISOU  379  CB  ASP A  48    12039  12371  14396      2   1195  -1210  A    C  
ATOM    380  CG  ASP A  48      98.019  60.217  32.497  1.00111.18      A    C  
ANISOU  380  CG  ASP A  48    13128  13187  15929    -85   1472  -1339  A    C  
ATOM    381  OD1 ASP A  48      96.813  60.187  32.175  1.00113.34      A    O  
ANISOU  381  OD1 ASP A  48    13300  13463  16299   -236   1487  -1560  A    O  
ATOM    382  OD2 ASP A  48      98.587  59.267  33.075  1.00116.77      A    O1-
ANISOU  382  OD2 ASP A  48    13878  13629  16858      1   1694  -1221  A    O1-
ATOM    383  N   ILE A  49      96.852  64.376  33.321  1.00 82.64      A    N  
ANISOU  383  N   ILE A  49     9608  10250  11541    -23    873   -889  A    N  
ATOM    384  CA  ILE A  49      96.102  64.932  34.466  1.00 81.49      A    C  
ANISOU  384  CA  ILE A  49     9500  10053  11406      4    892   -682  A    C  
ATOM    385  C   ILE A  49      94.666  65.072  34.045  1.00 80.99      A    C  
ANISOU  385  C   ILE A  49     9346  10025  11401   -144    877   -874  A    C  
ATOM    386  O   ILE A  49      94.395  65.194  32.847  1.00 83.64      A    O  
ANISOU  386  O   ILE A  49     9591  10540  11648   -233    777  -1123  A    O  
ATOM    387  CB  ILE A  49      96.549  66.342  34.868  1.00 77.14      A    C  
ANISOU  387  CB  ILE A  49     9011   9718  10579     94    713   -478  A    C  
ATOM    388  CG1 ILE A  49      96.435  67.291  33.684  1.00 77.48      A    C  
ANISOU  388  CG1 ILE A  49     9008  10020  10411     31    528   -618  A    C  
ATOM    389  CG2 ILE A  49      97.982  66.311  35.334  1.00 77.60      A    C  
ANISOU  389  CG2 ILE A  49     9133   9791  10558    240    712   -309  A    C  
ATOM    390  CD1 ILE A  49      96.525  68.741  34.081  1.00 75.54      A    C  
ANISOU  390  CD1 ILE A  49     8801   9939   9959     83    397   -447  A    C  
ATOM    391  N   THR A  50      93.757  65.107  35.010  1.00 78.56      A    N  
ANISOU  391  N   THR A  50     9048   9585  11215   -154    971   -755  A    N  
ATOM    392  CA  THR A  50      92.346  65.048  34.673  1.00 80.41      A    C  
ANISOU  392  CA  THR A  50     9178   9817  11556   -303    994   -958  A    C  
ATOM    393  C   THR A  50      91.833  66.388  34.183  1.00 77.43      A    C  
ANISOU  393  C   THR A  50     8774   9743  10900   -327    770   -970  A    C  
ATOM    394  O   THR A  50      92.168  67.433  34.744  1.00 73.32      A    O  
ANISOU  394  O   THR A  50     8339   9326  10191   -232    663   -733  A    O  
ATOM    395  CB  THR A  50      91.465  64.565  35.838  1.00 83.93      A    C  
ANISOU  395  CB  THR A  50     9632   9996  12260   -311   1201   -832  A    C  
ATOM    396  CG2 THR A  50      92.081  63.317  36.537  1.00 87.67      A    C  
ANISOU  396  CG2 THR A  50    10152  10146  13010   -226   1469   -715  A    C  
ATOM    397  OG1 THR A  50      91.285  65.625  36.762  1.00 80.06      A    O  
ANISOU  397  OG1 THR A  50     9220   9601  11597   -218   1109   -558  A    O  
ATOM    398  N   LEU A  51      91.061  66.323  33.090  1.00 78.14      A    N  
ANISOU  398  N   LEU A  51     8730   9992  10967   -446    711  -1264  A    N  
ATOM    399  CA  LEU A  51      90.430  67.485  32.455  1.00 73.92      A    C  
ANISOU  399  CA  LEU A  51     8139   9765  10179   -457    527  -1296  A    C  
ATOM    400  C   LEU A  51      89.130  67.697  33.156  1.00 72.57      A    C  
ANISOU  400  C   LEU A  51     7937   9522  10113   -525    576  -1264  A    C  
ATOM    401  O   LEU A  51      88.552  66.763  33.639  1.00 76.72      A    O  
ANISOU  401  O   LEU A  51     8422   9810  10917   -605    750  -1352  A    O  
ATOM    402  CB  LEU A  51      90.185  67.222  30.969  1.00 73.45      A    C  
ANISOU  402  CB  LEU A  51     7920   9959  10026   -523    454  -1630  A    C  
ATOM    403  CG  LEU A  51      89.487  68.304  30.169  1.00 73.33      A    C  
ANISOU  403  CG  LEU A  51     7817  10304   9740   -504    288  -1671  A    C  
ATOM    404  CD1 LEU A  51      90.312  69.579  30.109  1.00 72.79      A    C  
ANISOU  404  CD1 LEU A  51     7863  10382   9409   -358    165  -1390  A    C  
ATOM    405  CD2 LEU A  51      89.329  67.794  28.753  1.00 78.55      A    C  
ANISOU  405  CD2 LEU A  51     8295  11237  10312   -543    241  -2021  A    C  
ATOM    406  N   THR A  52      88.662  68.915  33.239  1.00 70.22      A    N  
ANISOU  406  N   THR A  52     7655   9408   9614   -488    447  -1133  A    N  
ATOM    407  CA  THR A  52      87.399  69.158  33.916  1.00 72.37      A    C  
ANISOU  407  CA  THR A  52     7898   9620   9976   -548    490  -1095  A    C  
ATOM    408  C   THR A  52      86.781  70.469  33.420  1.00 76.15      A    C  
ANISOU  408  C   THR A  52     8337  10398  10198   -522    326  -1059  A    C  
ATOM    409  O   THR A  52      87.089  70.919  32.311  1.00 82.67      A    O  
ANISOU  409  O   THR A  52     9108  11487  10813   -481    209  -1142  A    O  
ATOM    410  CB  THR A  52      87.578  69.171  35.450  1.00 70.19      A    C  
ANISOU  410  CB  THR A  52     7756   9091   9819   -477    599   -801  A    C  
ATOM    411  CG2 THR A  52      88.411  70.355  35.889  1.00 68.35      A    C  
ANISOU  411  CG2 THR A  52     7643   8977   9351   -346    475   -540  A    C  
ATOM    412  OG1 THR A  52      86.310  69.258  36.095  1.00 68.57      A    O  
ANISOU  412  OG1 THR A  52     7513   8808   9731   -539    668   -779  A    O  
ATOM    413  N   THR A  53      85.905  71.068  34.218  1.00 76.05      A    N  
ANISOU  413  N   THR A  53     8347  10347  10202   -531    334   -924  A    N  
ATOM    414  CA  THR A  53      85.153  72.230  33.793  1.00 78.02      A    C  
ANISOU  414  CA  THR A  53     8547  10852  10246   -509    212   -892  A    C  
ATOM    415  C   THR A  53      84.949  73.181  34.953  1.00 77.81      A    C  
ANISOU  415  C   THR A  53     8632  10742  10188   -454    210   -614  A    C  
ATOM    416  O   THR A  53      84.564  72.756  36.034  1.00 80.99      A    O  
ANISOU  416  O   THR A  53     9075  10927  10769   -482    317   -532  A    O  
ATOM    417  CB  THR A  53      83.743  71.813  33.344  1.00 84.59      A    C  
ANISOU  417  CB  THR A  53     9203  11779  11158   -627    234  -1144  A    C  
ATOM    418  CG2 THR A  53      82.915  73.015  32.951  1.00 84.75      A    C  
ANISOU  418  CG2 THR A  53     9164  12078  10957   -583    118  -1086  A    C  
ATOM    419  OG1 THR A  53      83.818  70.904  32.242  1.00 92.65      A    O  
ANISOU  419  OG1 THR A  53    10078  12917  12207   -693    238  -1467  A    O  
ATOM    420  N   ARG A  54      85.162  74.469  34.721  1.00 77.56      A    N  
ANISOU  420  N   ARG A  54     8639  10888   9942   -369    108   -471  A    N  
ATOM    421  CA  ARG A  54      84.833  75.473  35.715  1.00 76.59      A    C  
ANISOU  421  CA  ARG A  54     8594  10723   9784   -328    104   -256  A    C  
ATOM    422  C   ARG A  54      84.157  76.681  35.116  1.00 72.75      A    C  
ANISOU  422  C   ARG A  54     8054  10462   9123   -291     27   -216  A    C  
ATOM    423  O   ARG A  54      84.759  77.385  34.315  1.00 70.46      A    O  
ANISOU  423  O   ARG A  54     7765  10329   8675   -213    -25   -177  A    O  
ATOM    424  CB  ARG A  54      86.092  75.941  36.395  1.00 84.17      A    C  
ANISOU  424  CB  ARG A  54     9676  11604  10699   -239    101    -79  A    C  
ATOM    425  CG  ARG A  54      85.870  77.183  37.241  1.00 94.24      A    C  
ANISOU  425  CG  ARG A  54    11006  12896  11902   -193     84    102  A    C  
ATOM    426  CD  ARG A  54      87.152  77.646  37.912  1.00 98.27      A    C  
ANISOU  426  CD  ARG A  54    11601  13366  12370   -116     82    221  A    C  
ATOM    427  NE  ARG A  54      87.606  76.657  38.883  1.00102.79      A    N  
ANISOU  427  NE  ARG A  54    12216  13786  13052    -93    149    261  A    N  
ATOM    428  CZ  ARG A  54      88.508  76.893  39.821  1.00104.94      A    C  
ANISOU  428  CZ  ARG A  54    12539  14043  13290    -12    159    368  A    C  
ATOM    429  NH1 ARG A  54      89.061  78.092  39.919  1.00108.86      A    N1+
ANISOU  429  NH1 ARG A  54    13044  14643  13673     23    108    406  A    N1+
ATOM    430  NH2 ARG A  54      88.856  75.928  40.661  1.00107.85      A    N  
ANISOU  430  NH2 ARG A  54    12932  14301  13743     43    236    431  A    N  
ATOM    431  N   GLY A  55      82.904  76.909  35.491  1.00 72.18      A    N  
ANISOU  431  N   GLY A  55     7934  10403   9086   -337     40   -213  A    N  
ATOM    432  CA  GLY A  55      82.167  78.104  35.067  1.00 72.65      A    C  
ANISOU  432  CA  GLY A  55     7947  10666   8988   -286    -15   -140  A    C  
ATOM    433  C   GLY A  55      81.777  78.113  33.600  1.00 73.08      A    C  
ANISOU  433  C   GLY A  55     7855  11018   8891   -255    -73   -289  A    C  
ATOM    434  O   GLY A  55      82.049  77.174  32.895  1.00 74.09      A    O  
ANISOU  434  O   GLY A  55     7908  11204   9036   -290    -83   -483  A    O  
ATOM    435  N   GLN A  56      81.147  79.189  33.144  1.00 74.36      A    N  
ANISOU  435  N   GLN A  56     7967  11389   8896   -172   -103   -194  A    N  
ATOM    436  CA  GLN A  56      80.648  79.292  31.784  1.00 76.91      A    C  
ANISOU  436  CA  GLN A  56     8127  12064   9032   -100   -155   -304  A    C  
ATOM    437  C   GLN A  56      81.199  80.521  31.074  1.00 75.80      A    C  
ANISOU  437  C   GLN A  56     8013  12089   8697     79   -148    -95  A    C  
ATOM    438  O   GLN A  56      81.540  81.535  31.700  1.00 77.90      A    O  
ANISOU  438  O   GLN A  56     8400  12208   8989    127    -96    127  A    O  
ATOM    439  CB  GLN A  56      79.125  79.371  31.797  1.00 84.91      A    C  
ANISOU  439  CB  GLN A  56     9005  13226  10029   -140   -172   -386  A    C  
ATOM    440  CG  GLN A  56      78.443  78.333  32.688  1.00 92.76      A    C  
ANISOU  440  CG  GLN A  56     9980  13998  11266   -318   -132   -550  A    C  
ATOM    441  CD  GLN A  56      77.166  77.730  32.058  1.00102.37      A    C  
ANISOU  441  CD  GLN A  56    10966  15454  12477   -395   -156   -832  A    C  
ATOM    442  NE2 GLN A  56      76.960  76.414  32.270  1.00103.40      A    N  
ANISOU  442  NE2 GLN A  56    11024  15429  12832   -556   -100  -1095  A    N  
ATOM    443  OE1 GLN A  56      76.386  78.424  31.377  1.00 99.84      A    O  
ANISOU  443  OE1 GLN A  56    10516  15458  11958   -304   -211   -827  A    O  
ATOM    444  N   MET A  57      81.304  80.418  29.754  1.00 74.45      A    N  
ANISOU  444  N   MET A  57     7716  12231   8338    187   -182   -174  A    N  
ATOM    445  CA  MET A  57      81.750  81.524  28.924  1.00 71.77      A    C  
ANISOU  445  CA  MET A  57     7377  12079   7813    390   -139     41  A    C  
ATOM    446  C   MET A  57      80.909  81.497  27.699  1.00 73.31      A    C  
ANISOU  446  C   MET A  57     7360  12723   7769    516   -185    -51  A    C  
ATOM    447  O   MET A  57      81.008  80.578  26.899  1.00 77.58      A    O  
ANISOU  447  O   MET A  57     7774  13478   8224    511   -248   -284  A    O  
ATOM    448  CB  MET A  57      83.210  81.374  28.524  1.00 70.06      A    C  
ANISOU  448  CB  MET A  57     7240  11786   7593    441   -113     77  A    C  
ATOM    449  CG  MET A  57      83.765  82.574  27.790  1.00 71.04      A    C  
ANISOU  449  CG  MET A  57     7381  12029   7581    649    -20    335  A    C  
ATOM    450  SD  MET A  57      85.556  82.411  27.515  1.00 72.75      A    S  
ANISOU  450  SD  MET A  57     7703  12090   7847    678     31    376  A    S  
ATOM    451  CE  MET A  57      85.510  81.521  25.935  1.00 80.83      A    C  
ANISOU  451  CE  MET A  57     8541  13544   8624    794    -44    191  A    C  
ATOM    452  N   ASP A  58      80.084  82.513  27.545  1.00 73.98      A    N  
ANISOU  452  N   ASP A  58     7395  12977   7737    643   -150    125  A    N  
ATOM    453  CA  ASP A  58      79.165  82.576  26.419  1.00 75.90      A    C  
ANISOU  453  CA  ASP A  58     7410  13711   7718    796   -192     58  A    C  
ATOM    454  C   ASP A  58      78.322  81.338  26.375  1.00 75.73      A    C  
ANISOU  454  C   ASP A  58     7218  13831   7724    632   -301   -324  A    C  
ATOM    455  O   ASP A  58      78.078  80.790  25.321  1.00 80.08      A    O  
ANISOU  455  O   ASP A  58     7563  14782   8083    703   -367   -538  A    O  
ATOM    456  CB  ASP A  58      79.921  82.752  25.108  1.00 77.37      A    C  
ANISOU  456  CB  ASP A  58     7521  14206   7671   1024   -166    135  A    C  
ATOM    457  CG  ASP A  58      80.638  84.072  25.048  1.00 76.34      A    C  
ANISOU  457  CG  ASP A  58     7525  13946   7531   1207    -11    524  A    C  
ATOM    458  OD1 ASP A  58      79.957  85.108  25.271  1.00 73.07      A    O  
ANISOU  458  OD1 ASP A  58     7120  13545   7099   1304     70    746  A    O  
ATOM    459  OD2 ASP A  58      81.867  84.063  24.791  1.00 75.70      A    O1-
ANISOU  459  OD2 ASP A  58     7538  13740   7484   1247     44    595  A    O1-
ATOM    460  N   GLY A  59      77.886  80.897  27.541  1.00 74.31      A    N  
ANISOU  460  N   GLY A  59     7116  13323   7796    413   -305   -419  A    N  
ATOM    461  CA  GLY A  59      76.986  79.761  27.637  1.00 74.94      A    C  
ANISOU  461  CA  GLY A  59     7032  13467   7973    233   -362   -778  A    C  
ATOM    462  C   GLY A  59      77.721  78.467  27.872  1.00 73.14      A    C  
ANISOU  462  C   GLY A  59     6845  12994   7951     58   -360  -1020  A    C  
ATOM    463  O   GLY A  59      77.251  77.597  28.584  1.00 70.86      A    O  
ANISOU  463  O   GLY A  59     6539  12481   7902   -141   -335  -1218  A    O  
ATOM    464  N   VAL A  60      78.891  78.353  27.270  1.00 72.86      A    N  
ANISOU  464  N   VAL A  60     6862  12987   7832    144   -363   -985  A    N  
ATOM    465  CA  VAL A  60      79.617  77.107  27.239  1.00 72.99      A    C  
ANISOU  465  CA  VAL A  60     6885  12845   8002     12   -359  -1230  A    C  
ATOM    466  C   VAL A  60      80.442  76.889  28.519  1.00 70.16      A    C  
ANISOU  466  C   VAL A  60     6774  11965   7918   -105   -288  -1083  A    C  
ATOM    467  O   VAL A  60      81.203  77.750  28.881  1.00 68.58      A    O  
ANISOU  467  O   VAL A  60     6743  11622   7690    -14   -261   -793  A    O  
ATOM    468  CB  VAL A  60      80.513  77.123  25.998  1.00 74.04      A    C  
ANISOU  468  CB  VAL A  60     6959  13271   7902    177   -395  -1243  A    C  
ATOM    469  CG1 VAL A  60      81.402  75.894  25.936  1.00 75.89      A    C  
ANISOU  469  CG1 VAL A  60     7215  13331   8289     56   -384  -1475  A    C  
ATOM    470  CG2 VAL A  60      79.635  77.229  24.748  1.00 77.26      A    C  
ANISOU  470  CG2 VAL A  60     7085  14260   8008    315   -467  -1413  A    C  
ATOM    471  N   PRO A  61      80.281  75.736  29.202  1.00 70.57      A    N  
ANISOU  471  N   PRO A  61     6826  11745   8241   -296   -237  -1289  A    N  
ATOM    472  CA  PRO A  61      81.193  75.296  30.227  1.00 69.68      A    C  
ANISOU  472  CA  PRO A  61     6910  11210   8355   -369   -163  -1179  A    C  
ATOM    473  C   PRO A  61      82.634  75.431  29.808  1.00 69.74      A    C  
ANISOU  473  C   PRO A  61     7023  11206   8268   -267   -178  -1068  A    C  
ATOM    474  O   PRO A  61      82.988  75.040  28.702  1.00 74.21      A    O  
ANISOU  474  O   PRO A  61     7479  12008   8707   -221   -219  -1236  A    O  
ATOM    475  CB  PRO A  61      80.880  73.804  30.368  1.00 71.54      A    C  
ANISOU  475  CB  PRO A  61     7046  11289   8844   -546    -90  -1501  A    C  
ATOM    476  CG  PRO A  61      79.465  73.718  30.050  1.00 74.52      A    C  
ANISOU  476  CG  PRO A  61     7219  11884   9212   -616   -107  -1718  A    C  
ATOM    477  CD  PRO A  61      79.327  74.667  28.887  1.00 76.14      A    C  
ANISOU  477  CD  PRO A  61     7315  12557   9055   -442   -229  -1674  A    C  
ATOM    478  N   ILE A  62      83.452  75.966  30.710  1.00 68.99      A    N  
ANISOU  478  N   ILE A  62     7125  10852   8236   -234   -143   -805  A    N  
ATOM    479  CA  ILE A  62      84.861  76.269  30.452  1.00 68.54      A    C  
ANISOU  479  CA  ILE A  62     7175  10760   8104   -138   -147   -672  A    C  
ATOM    480  C   ILE A  62      85.725  75.085  30.797  1.00 68.13      A    C  
ANISOU  480  C   ILE A  62     7181  10477   8228   -217   -102   -782  A    C  
ATOM    481  O   ILE A  62      85.697  74.612  31.913  1.00 66.24      A    O  
ANISOU  481  O   ILE A  62     7022   9961   8184   -294    -37   -743  A    O  
ATOM    482  CB  ILE A  62      85.327  77.473  31.294  1.00 66.34      A    C  
ANISOU  482  CB  ILE A  62     7050  10335   7816    -72   -122   -374  A    C  
ATOM    483  CG1 ILE A  62      84.547  78.730  30.866  1.00 66.41      A    C  
ANISOU  483  CG1 ILE A  62     7006  10561   7662     27   -136   -240  A    C  
ATOM    484  CG2 ILE A  62      86.819  77.670  31.126  1.00 66.06      A    C  
ANISOU  484  CG2 ILE A  62     7111  10234   7751     -0   -108   -277  A    C  
ATOM    485  CD1 ILE A  62      84.896  79.995  31.599  1.00 63.65      A    C  
ANISOU  485  CD1 ILE A  62     6781  10079   7324     84    -88     14  A    C  
ATOM    486  N   LYS A  63      86.469  74.582  29.820  1.00 70.99      A    N  
ANISOU  486  N   LYS A  63     7494  10964   8514   -179   -124   -912  A    N  
ATOM    487  CA  LYS A  63      87.318  73.446  30.076  1.00 73.15      A    C  
ANISOU  487  CA  LYS A  63     7816  11022   8955   -242    -70  -1015  A    C  
ATOM    488  C   LYS A  63      88.490  73.947  30.951  1.00 70.37      A    C  
ANISOU  488  C   LYS A  63     7646  10455   8633   -181    -46   -753  A    C  
ATOM    489  O   LYS A  63      88.946  75.101  30.830  1.00 66.12      A    O  
ANISOU  489  O   LYS A  63     7164  10005   7953    -82    -78   -566  A    O  
ATOM    490  CB  LYS A  63      87.734  72.738  28.758  1.00 79.05      A    C  
ANISOU  490  CB  LYS A  63     8442  11984   9608   -223   -102  -1257  A    C  
ATOM    491  CG  LYS A  63      86.695  71.713  28.272  1.00 85.31      A    C  
ANISOU  491  CG  LYS A  63     9039  12883  10490   -346    -84  -1617  A    C  
ATOM    492  CD  LYS A  63      87.067  71.019  26.962  1.00 92.78      A    C  
ANISOU  492  CD  LYS A  63     9837  14089  11327   -326   -120  -1898  A    C  
ATOM    493  CE  LYS A  63      86.494  71.727  25.725  1.00 98.65      A    C  
ANISOU  493  CE  LYS A  63    10406  15331  11744   -200   -226  -1964  A    C  
ATOM    494  NZ  LYS A  63      87.033  71.241  24.407  1.00 99.58      A    N1+
ANISOU  494  NZ  LYS A  63    10385  15765  11683   -125   -271  -2184  A    N1+
ATOM    495  N   MET A  64      88.939  73.076  31.853  1.00 68.64      A    N  
ANISOU  495  N   MET A  64     7503   9964   8611   -234     31   -750  A    N  
ATOM    496  CA  MET A  64      89.944  73.411  32.831  1.00 64.83      A    C  
ANISOU  496  CA  MET A  64     7161   9311   8160   -176     55   -537  A    C  
ATOM    497  C   MET A  64      90.726  72.203  33.250  1.00 63.75      A    C  
ANISOU  497  C   MET A  64     7068   8968   8186   -190    138   -580  A    C  
ATOM    498  O   MET A  64      90.233  71.095  33.261  1.00 65.88      A    O  
ANISOU  498  O   MET A  64     7282   9119   8628   -269    222   -734  A    O  
ATOM    499  CB  MET A  64      89.274  73.931  34.061  1.00 69.05      A    C  
ANISOU  499  CB  MET A  64     7749   9733   8753   -186     82   -380  A    C  
ATOM    500  CG  MET A  64      90.246  74.507  35.071  1.00 75.36      A    C  
ANISOU  500  CG  MET A  64     8658  10442   9532   -109     90   -179  A    C  
ATOM    501  SD  MET A  64      90.776  73.413  36.405  1.00 84.06      A    S  
ANISOU  501  SD  MET A  64     9829  11301  10808    -83    199    -97  A    S  
ATOM    502  CE  MET A  64      89.424  73.608  37.551  1.00 85.31      A    C  
ANISOU  502  CE  MET A  64     9987  11374  11051   -111    254      2  A    C  
ATOM    503  N   ALA A  65      91.975  72.420  33.593  1.00 62.70      A    N  
ANISOU  503  N   ALA A  65     7021   8789   8011   -110    133   -448  A    N  
ATOM    504  CA  ALA A  65      92.815  71.380  34.168  1.00 63.47      A    C  
ANISOU  504  CA  ALA A  65     7171   8698   8248    -86    221   -430  A    C  
ATOM    505  C   ALA A  65      93.892  72.126  34.954  1.00 60.26      A    C  
ANISOU  505  C   ALA A  65     6848   8296   7751     15    192   -230  A    C  
ATOM    506  O   ALA A  65      94.217  73.252  34.625  1.00 57.74      A    O  
ANISOU  506  O   ALA A  65     6533   8118   7286     46    114   -179  A    O  
ATOM    507  CB  ALA A  65      93.412  70.497  33.069  1.00 66.36      A    C  
ANISOU  507  CB  ALA A  65     7488   9091   8631   -104    231   -619  A    C  
ATOM    508  N   GLY A  66      94.437  71.510  35.992  1.00 60.19      A    N  
ANISOU  508  N   GLY A  66     6888   8145   7833     77    272   -124  A    N  
ATOM    509  CA  GLY A  66      95.375  72.220  36.869  1.00 58.04      A    C  
ANISOU  509  CA  GLY A  66     6662   7929   7461    178    241     35  A    C  
ATOM    510  C   GLY A  66      96.446  71.347  37.466  1.00 57.26      A    C  
ANISOU  510  C   GLY A  66     6591   7750   7414    279    314    105  A    C  
ATOM    511  O   GLY A  66      96.490  70.174  37.222  1.00 59.79      A    O  
ANISOU  511  O   GLY A  66     6911   7936   7871    271    407     50  A    O  
ATOM    512  N   VAL A  67      97.347  71.933  38.212  1.00 56.43      A    N  
ANISOU  512  N   VAL A  67     6494   7744   7200    375    278    211  A    N  
ATOM    513  CA  VAL A  67      98.369  71.178  38.888  1.00 59.32      A    C  
ANISOU  513  CA  VAL A  67     6869   8086   7581    503    345    302  A    C  
ATOM    514  C   VAL A  67      98.645  71.883  40.212  1.00 59.78      A    C  
ANISOU  514  C   VAL A  67     6906   8285   7520    616    322    436  A    C  
ATOM    515  O   VAL A  67      98.617  73.099  40.288  1.00 57.40      A    O  
ANISOU  515  O   VAL A  67     6577   8118   7112    579    231    401  A    O  
ATOM    516  CB  VAL A  67      99.697  71.079  38.065  1.00 61.16      A    C  
ANISOU  516  CB  VAL A  67     7097   8380   7762    520    300    218  A    C  
ATOM    517  CG1 VAL A  67      99.513  70.351  36.722  1.00 62.53      A    C  
ANISOU  517  CG1 VAL A  67     7275   8459   8024    425    319     66  A    C  
ATOM    518  CG2 VAL A  67     100.301  72.447  37.812  1.00 60.59      A    C  
ANISOU  518  CG2 VAL A  67     6994   8480   7544    499    188    177  A    C  
ATOM    519  N   PRO A  68      98.932  71.117  41.269  1.00 63.40      A    N  
ANISOU  519  N   PRO A  68     7363   8728   7996    770    421    589  A    N  
ATOM    520  CA  PRO A  68      99.286  71.738  42.538  1.00 63.30      A    C  
ANISOU  520  CA  PRO A  68     7299   8921   7830    909    394    701  A    C  
ATOM    521  C   PRO A  68     100.587  72.506  42.439  1.00 62.85      A    C  
ANISOU  521  C   PRO A  68     7181   9076   7622    936    285    607  A    C  
ATOM    522  O   PRO A  68     101.511  72.070  41.740  1.00 66.95      A    O  
ANISOU  522  O   PRO A  68     7704   9571   8160    935    282    545  A    O  
ATOM    523  CB  PRO A  68      99.451  70.547  43.479  1.00 65.51      A    C  
ANISOU  523  CB  PRO A  68     7584   9145   8161   1106    551    903  A    C  
ATOM    524  CG  PRO A  68      99.841  69.426  42.590  1.00 68.05      A    C  
ANISOU  524  CG  PRO A  68     7949   9266   8640   1074    637    857  A    C  
ATOM    525  CD  PRO A  68      99.136  69.656  41.282  1.00 67.45      A    C  
ANISOU  525  CD  PRO A  68     7903   9062   8662    846    575    658  A    C  
ATOM    526  N   PHE A  69     100.667  73.626  43.139  1.00 60.53      A    N  
ANISOU  526  N   PHE A  69     6815   8988   7192    953    210    576  A    N  
ATOM    527  CA  PHE A  69     101.871  74.454  43.161  1.00 59.59      A    C  
ANISOU  527  CA  PHE A  69     6606   9081   6955    963    127    447  A    C  
ATOM    528  C   PHE A  69     103.122  73.681  43.572  1.00 62.53      A    C  
ANISOU  528  C   PHE A  69     6925   9580   7254   1133    153    497  A    C  
ATOM    529  O   PHE A  69     104.189  73.911  43.016  1.00 60.93      A    O  
ANISOU  529  O   PHE A  69     6679   9440   7028   1103    108    376  A    O  
ATOM    530  CB  PHE A  69     101.640  75.589  44.154  1.00 59.38      A    C  
ANISOU  530  CB  PHE A  69     6486   9266   6809    983     77    404  A    C  
ATOM    531  CG  PHE A  69     102.757  76.588  44.249  1.00 56.95      A    C  
ANISOU  531  CG  PHE A  69     6050   9176   6412    963     11    217  A    C  
ATOM    532  CD1 PHE A  69     103.849  76.333  45.035  1.00 57.40      A    C  
ANISOU  532  CD1 PHE A  69     5990   9489   6331   1124     -4    203  A    C  
ATOM    533  CD2 PHE A  69     102.678  77.790  43.592  1.00 54.93      A    C  
ANISOU  533  CD2 PHE A  69     5774   8876   6218    793    -17     54  A    C  
ATOM    534  CE1 PHE A  69     104.877  77.230  45.130  1.00 57.51      A    C  
ANISOU  534  CE1 PHE A  69     5858   9710   6280   1091    -56    -13  A    C  
ATOM    535  CE2 PHE A  69     103.700  78.703  43.686  1.00 55.47      A    C  
ANISOU  535  CE2 PHE A  69     5709   9111   6253    760    -41   -142  A    C  
ATOM    536  CZ  PHE A  69     104.798  78.429  44.470  1.00 56.73      A    C  
ANISOU  536  CZ  PHE A  69     5740   9530   6284    897    -66   -196  A    C  
ATOM    537  N   HIS A  70     102.993  72.773  44.545  1.00 67.48      A    N  
ANISOU  537  N   HIS A  70     7549  10244   7846   1326    241    691  A    N  
ATOM    538  CA  HIS A  70     104.147  72.052  45.080  1.00 71.65      A    C  
ANISOU  538  CA  HIS A  70     8010  10936   8276   1536    280    776  A    C  
ATOM    539  C   HIS A  70     104.793  71.153  44.034  1.00 70.90      A    C  
ANISOU  539  C   HIS A  70     7984  10646   8305   1499    325    757  A    C  
ATOM    540  O   HIS A  70     105.918  70.703  44.227  1.00 72.87      A    O  
ANISOU  540  O   HIS A  70     8176  11032   8479   1639    338    785  A    O  
ATOM    541  CB  HIS A  70     103.779  71.242  46.345  1.00 78.71      A    C  
ANISOU  541  CB  HIS A  70     8889  11905   9112   1788    407   1042  A    C  
ATOM    542  CG  HIS A  70     102.908  70.049  46.090  1.00 84.90      A    C  
ANISOU  542  CG  HIS A  70     9799  12341  10117   1793    579   1216  A    C  
ATOM    543  CD2 HIS A  70     101.606  69.814  46.392  1.00 86.81      A    C  
ANISOU  543  CD2 HIS A  70    10104  12402  10479   1768    677   1332  A    C  
ATOM    544  ND1 HIS A  70     103.380  68.895  45.491  1.00 90.64      A    N  
ANISOU  544  ND1 HIS A  70    10585  12863  10988   1825    691   1269  A    N  
ATOM    545  CE1 HIS A  70     102.398  68.013  45.408  1.00 96.30      A    C  
ANISOU  545  CE1 HIS A  70    11389  13276  11924   1805    859   1386  A    C  
ATOM    546  NE2 HIS A  70     101.310  68.548  45.943  1.00 93.31      A    N  
ANISOU  546  NE2 HIS A  70    11012  12904  11535   1769    854   1428  A    N  
ATOM    547  N   ALA A  71     104.079  70.866  42.946  1.00 69.82      A    N  
ANISOU  547  N   ALA A  71     7957  10220   8348   1322    350    702  A    N  
ATOM    548  CA  ALA A  71     104.598  70.000  41.889  1.00 70.02      A    C  
ANISOU  548  CA  ALA A  71     8040  10068   8495   1277    395    655  A    C  
ATOM    549  C   ALA A  71     104.611  70.716  40.552  1.00 66.40      A    C  
ANISOU  549  C   ALA A  71     7606   9550   8071   1068    296    455  A    C  
ATOM    550  O   ALA A  71     104.529  70.111  39.503  1.00 67.22      A    O  
ANISOU  550  O   ALA A  71     7767   9482   8288    984    326    390  A    O  
ATOM    551  CB  ALA A  71     103.780  68.705  41.805  1.00 71.33      A    C  
ANISOU  551  CB  ALA A  71     8290   9953   8859   1296    561    772  A    C  
ATOM    552  N   ALA A  72     104.747  72.017  40.577  1.00 65.63      A    N  
ANISOU  552  N   ALA A  72     7451   9607   7877    996    194    352  A    N  
ATOM    553  CA  ALA A  72     104.668  72.745  39.330  1.00 65.69      A    C  
ANISOU  553  CA  ALA A  72     7479   9553   7924    827    137    208  A    C  
ATOM    554  C   ALA A  72     105.938  72.576  38.569  1.00 68.76      A    C  
ANISOU  554  C   ALA A  72     7846   9971   8305    834    126    128  A    C  
ATOM    555  O   ALA A  72     105.877  72.345  37.377  1.00 71.60      A    O  
ANISOU  555  O   ALA A  72     8257  10217   8731    752    131     68  A    O  
ATOM    556  CB  ALA A  72     104.393  74.213  39.565  1.00 65.17      A    C  
ANISOU  556  CB  ALA A  72     7358   9601   7802    749     77    134  A    C  
ATOM    557  N   GLU A  73     107.088  72.655  39.237  1.00 73.87      A    N  
ANISOU  557  N   GLU A  73     8409  10795   8863    943    111    122  A    N  
ATOM    558  CA  GLU A  73     108.358  72.529  38.529  1.00 78.24      A    C  
ANISOU  558  CA  GLU A  73     8931  11381   9412    948    102     40  A    C  
ATOM    559  C   GLU A  73     108.448  71.160  37.877  1.00 82.58      A    C  
ANISOU  559  C   GLU A  73     9566  11765  10044    986    166     97  A    C  
ATOM    560  O   GLU A  73     109.018  71.014  36.793  1.00 83.96      A    O  
ANISOU  560  O   GLU A  73     9761  11884  10256    934    164     19  A    O  
ATOM    561  CB  GLU A  73     109.540  72.734  39.451  1.00 84.24      A    C  
ANISOU  561  CB  GLU A  73     9561  12389  10055   1071     79     12  A    C  
ATOM    562  CG  GLU A  73     110.019  74.164  39.500  1.00 93.18      A    C  
ANISOU  562  CG  GLU A  73    10576  13669  11156    980     31   -162  A    C  
ATOM    563  CD  GLU A  73     110.864  74.460  40.734  1.00109.52      A    C  
ANISOU  563  CD  GLU A  73    12475  16050  13086   1103     -3   -226  A    C  
ATOM    564  OE1 GLU A  73     110.824  73.680  41.724  1.00113.44      A    O  
ANISOU  564  OE1 GLU A  73    12950  16675  13475   1285      5    -89  A    O  
ATOM    565  OE2 GLU A  73     111.576  75.487  40.715  1.00129.28      A    O1-
ANISOU  565  OE2 GLU A  73    14848  18682  15589   1026    -22   -419  A    O1-
ATOM    566  N   GLN A  74     107.866  70.150  38.512  1.00 81.75      A    N  
ANISOU  566  N   GLN A  74     9506  11569   9986   1078    243    232  A    N  
ATOM    567  CA  GLN A  74     107.906  68.832  37.937  1.00 80.76      A    C  
ANISOU  567  CA  GLN A  74     9449  11255   9980   1104    336    262  A    C  
ATOM    568  C   GLN A  74     107.150  68.778  36.630  1.00 76.50      A    C  
ANISOU  568  C   GLN A  74     8970  10555   9540    935    328    139  A    C  
ATOM    569  O   GLN A  74     107.661  68.268  35.633  1.00 86.99      A    O  
ANISOU  569  O   GLN A  74    10317  11825  10910    905    340     53  A    O  
ATOM    570  CB  GLN A  74     107.340  67.834  38.894  1.00 84.94      A    C  
ANISOU  570  CB  GLN A  74    10006  11683  10583   1231    465    434  A    C  
ATOM    571  CG  GLN A  74     107.983  67.919  40.247  1.00 92.87      A    C  
ANISOU  571  CG  GLN A  74    10930  12908  11446   1440    476    581  A    C  
ATOM    572  CD  GLN A  74     107.308  66.954  41.183  1.00106.02      A    C  
ANISOU  572  CD  GLN A  74    12627  14463  13193   1591    640    798  A    C  
ATOM    573  NE2 GLN A  74     107.385  67.236  42.480  1.00118.17      A    N  
ANISOU  573  NE2 GLN A  74    14090  16224  14582   1773    646    947  A    N  
ATOM    574  OE1 GLN A  74     106.710  65.960  40.745  1.00104.14      A    O  
ANISOU  574  OE1 GLN A  74    12465  13943  13159   1551    778    825  A    O  
ATOM    575  N   TYR A  75     105.935  69.286  36.617  1.00 70.32      A    N  
ANISOU  575  N   TYR A  75     8207   9732   8780    837    304    123  A    N  
ATOM    576  CA  TYR A  75     105.164  69.271  35.391  1.00 68.94      A    C  
ANISOU  576  CA  TYR A  75     8061   9466   8664    699    289     -3  A    C  
ATOM    577  C   TYR A  75     105.765  70.189  34.331  1.00 65.75      A    C  
ANISOU  577  C   TYR A  75     7632   9177   8169    640    206   -101  A    C  
ATOM    578  O   TYR A  75     105.659  69.919  33.116  1.00 62.81      A    O  
ANISOU  578  O   TYR A  75     7269   8783   7812    584    203   -204  A    O  
ATOM    579  CB  TYR A  75     103.728  69.692  35.663  1.00 70.24      A    C  
ANISOU  579  CB  TYR A  75     8236   9593   8857    621    281      9  A    C  
ATOM    580  CG  TYR A  75     102.878  68.642  36.333  1.00 70.74      A    C  
ANISOU  580  CG  TYR A  75     8325   9486   9065    645    400     75  A    C  
ATOM    581  CD1 TYR A  75     102.283  67.650  35.589  1.00 74.03      A    C  
ANISOU  581  CD1 TYR A  75     8751   9742   9632    568    479    -38  A    C  
ATOM    582  CD2 TYR A  75     102.652  68.667  37.691  1.00 70.10      A    C  
ANISOU  582  CD2 TYR A  75     8243   9414   8977    746    448    240  A    C  
ATOM    583  CE1 TYR A  75     101.500  66.685  36.188  1.00 79.31      A    C  
ANISOU  583  CE1 TYR A  75     9432  10217  10485    578    629     10  A    C  
ATOM    584  CE2 TYR A  75     101.874  67.718  38.309  1.00 72.56      A    C  
ANISOU  584  CE2 TYR A  75     8577   9549   9443    784    595    331  A    C  
ATOM    585  CZ  TYR A  75     101.296  66.726  37.562  1.00 77.98      A    C  
ANISOU  585  CZ  TYR A  75     9277  10031  10321    692    697    216  A    C  
ATOM    586  OH  TYR A  75     100.523  65.752  38.175  1.00 84.38      A    O  
ANISOU  586  OH  TYR A  75    10099  10623  11339    720    886    296  A    O  
ATOM    587  N   LEU A  76     106.390  71.276  34.787  1.00 63.54      A    N  
ANISOU  587  N   LEU A  76     7308   9029   7802    662    157    -76  A    N  
ATOM    588  CA  LEU A  76     107.053  72.205  33.867  1.00 62.89      A    C  
ANISOU  588  CA  LEU A  76     7195   9027   7673    620    125   -146  A    C  
ATOM    589  C   LEU A  76     108.192  71.513  33.177  1.00 65.96      A    C  
ANISOU  589  C   LEU A  76     7581   9414   8064    665    146   -189  A    C  
ATOM    590  O   LEU A  76     108.429  71.730  31.980  1.00 66.57      A    O  
ANISOU  590  O   LEU A  76     7659   9505   8126    633    146   -247  A    O  
ATOM    591  CB  LEU A  76     107.610  73.414  34.587  1.00 61.80      A    C  
ANISOU  591  CB  LEU A  76     6985   9006   7488    624    105   -149  A    C  
ATOM    592  CG  LEU A  76     106.663  74.553  34.983  1.00 61.47      A    C  
ANISOU  592  CG  LEU A  76     6927   8985   7441    557     90   -139  A    C  
ATOM    593  CD1 LEU A  76     107.442  75.662  35.695  1.00 59.94      A    C  
ANISOU  593  CD1 LEU A  76     6634   8911   7229    556     91   -197  A    C  
ATOM    594  CD2 LEU A  76     105.909  75.092  33.774  1.00 60.70      A    C  
ANISOU  594  CD2 LEU A  76     6860   8841   7360    483    104   -150  A    C  
ATOM    595  N   ALA A  77     108.896  70.680  33.948  1.00 67.30      A    N  
ANISOU  595  N   ALA A  77     7744   9581   8244    761    171   -143  A    N  
ATOM    596  CA  ALA A  77     109.988  69.872  33.423  1.00 67.86      A    C  
ANISOU  596  CA  ALA A  77     7815   9640   8326    820    201   -172  A    C  
ATOM    597  C   ALA A  77     109.517  68.943  32.311  1.00 66.09      A    C  
ANISOU  597  C   ALA A  77     7644   9298   8170    775    236   -243  A    C  
ATOM    598  O   ALA A  77     110.243  68.710  31.359  1.00 66.41      A    O  
ANISOU  598  O   ALA A  77     7679   9355   8196    780    241   -309  A    O  
ATOM    599  CB  ALA A  77     110.634  69.067  34.543  1.00 70.90      A    C  
ANISOU  599  CB  ALA A  77     8181  10047   8711    958    243    -78  A    C  
ATOM    600  N   ARG A  78     108.318  68.393  32.440  1.00 67.03      A    N  
ANISOU  600  N   ARG A  78     7797   9305   8363    732    269   -248  A    N  
ATOM    601  CA  ARG A  78     107.780  67.555  31.387  1.00 69.57      A    C  
ANISOU  601  CA  ARG A  78     8134   9543   8754    672    304   -374  A    C  
ATOM    602  C   ARG A  78     107.442  68.375  30.165  1.00 69.00      A    C  
ANISOU  602  C   ARG A  78     8037   9594   8586    604    236   -465  A    C  
ATOM    603  O   ARG A  78     107.717  67.965  29.025  1.00 70.62      A    O  
ANISOU  603  O   ARG A  78     8224   9840   8766    598    238   -577  A    O  
ATOM    604  CB  ARG A  78     106.518  66.875  31.828  1.00 73.17      A    C  
ANISOU  604  CB  ARG A  78     8606   9857   9336    625    369   -387  A    C  
ATOM    605  CG  ARG A  78     106.703  65.885  32.934  1.00 80.24      A    C  
ANISOU  605  CG  ARG A  78     9527  10603  10355    717    490   -273  A    C  
ATOM    606  CD  ARG A  78     105.428  65.083  33.037  1.00 87.74      A    C  
ANISOU  606  CD  ARG A  78    10482  11370  11482    646    596   -332  A    C  
ATOM    607  NE  ARG A  78     105.229  64.585  34.388  1.00 92.19      A    N  
ANISOU  607  NE  ARG A  78    11069  11807  12150    746    720   -146  A    N  
ATOM    608  CZ  ARG A  78     104.096  64.047  34.811  1.00100.95      A    C  
ANISOU  608  CZ  ARG A  78    12183  12743  13428    703    838   -139  A    C  
ATOM    609  NH1 ARG A  78     103.051  63.955  33.984  1.00105.95      A    N1+
ANISOU  609  NH1 ARG A  78    12785  13329  14141    544    830   -342  A    N1+
ATOM    610  NH2 ARG A  78     104.004  63.616  36.062  1.00104.09      A    N  
ANISOU  610  NH2 ARG A  78    12601  13039  13909    831    973     71  A    N  
ATOM    611  N   LEU A  79     106.843  69.539  30.389  1.00 63.60      A    N  
ANISOU  611  N   LEU A  79     7343   8981   7841    568    187   -410  A    N  
ATOM    612  CA  LEU A  79     106.344  70.293  29.281  1.00 61.82      A    C  
ANISOU  612  CA  LEU A  79     7089   8872   7527    532    150   -458  A    C  
ATOM    613  C   LEU A  79     107.461  70.804  28.382  1.00 63.43      A    C  
ANISOU  613  C   LEU A  79     7269   9177   7652    583    153   -453  A    C  
ATOM    614  O   LEU A  79     107.303  70.846  27.154  1.00 63.58      A    O  
ANISOU  614  O   LEU A  79     7259   9303   7593    597    151   -512  A    O  
ATOM    615  CB  LEU A  79     105.563  71.451  29.813  1.00 61.27      A    C  
ANISOU  615  CB  LEU A  79     7014   8834   7429    498    124   -376  A    C  
ATOM    616  CG  LEU A  79     104.197  71.139  30.354  1.00 61.64      A    C  
ANISOU  616  CG  LEU A  79     7071   8816   7530    439    120   -389  A    C  
ATOM    617  CD1 LEU A  79     103.553  72.447  30.748  1.00 60.94      A    C  
ANISOU  617  CD1 LEU A  79     6975   8780   7396    416     93   -303  A    C  
ATOM    618  CD2 LEU A  79     103.378  70.468  29.276  1.00 63.93      A    C  
ANISOU  618  CD2 LEU A  79     7325   9150   7812    398    117   -535  A    C  
ATOM    619  N   VAL A  80     108.572  71.222  29.000  1.00 63.45      A    N  
ANISOU  619  N   VAL A  80     7270   9168   7668    620    166   -386  A    N  
ATOM    620  CA  VAL A  80     109.730  71.664  28.257  1.00 63.11      A    C  
ANISOU  620  CA  VAL A  80     7198   9191   7588    664    194   -382  A    C  
ATOM    621  C   VAL A  80     110.508  70.493  27.622  1.00 68.08      A    C  
ANISOU  621  C   VAL A  80     7836   9812   8219    710    208   -455  A    C  
ATOM    622  O   VAL A  80     111.152  70.684  26.586  1.00 74.09      A    O  
ANISOU  622  O   VAL A  80     8575  10650   8926    750    233   -468  A    O  
ATOM    623  CB  VAL A  80     110.645  72.541  29.112  1.00 61.22      A    C  
ANISOU  623  CB  VAL A  80     6922   8959   7380    671    211   -333  A    C  
ATOM    624  CG1 VAL A  80     109.929  73.822  29.504  1.00 60.65      A    C  
ANISOU  624  CG1 VAL A  80     6827   8897   7317    620    219   -287  A    C  
ATOM    625  CG2 VAL A  80     111.184  71.801  30.319  1.00 60.05      A    C  
ANISOU  625  CG2 VAL A  80     6771   8779   7263    707    192   -329  A    C  
ATOM    626  N   LYS A  81     110.437  69.293  28.197  1.00 70.92      A    N  
ANISOU  626  N   LYS A  81     8224  10073   8647    716    215   -490  A    N  
ATOM    627  CA  LYS A  81     110.944  68.092  27.523  1.00 77.51      A    C  
ANISOU  627  CA  LYS A  81     9067  10876   9507    748    247   -583  A    C  
ATOM    628  C   LYS A  81     110.213  67.808  26.221  1.00 77.29      A    C  
ANISOU  628  C   LYS A  81     9013  10930   9424    717    238   -714  A    C  
ATOM    629  O   LYS A  81     110.725  67.105  25.341  1.00 79.71      A    O  
ANISOU  629  O   LYS A  81     9302  11274   9710    749    258   -815  A    O  
ATOM    630  CB  LYS A  81     110.807  66.851  28.391  1.00 87.24      A    C  
ANISOU  630  CB  LYS A  81    10330  11951  10863    762    300   -588  A    C  
ATOM    631  CG  LYS A  81     111.962  66.636  29.358  1.00102.42      A    C  
ANISOU  631  CG  LYS A  81    12255  13849  12809    854    328   -481  A    C  
ATOM    632  CD  LYS A  81     111.953  65.230  29.971  1.00114.91      A    C  
ANISOU  632  CD  LYS A  81    13867  15269  14522    910    428   -461  A    C  
ATOM    633  CE  LYS A  81     111.037  65.113  31.197  1.00118.26      A    C  
ANISOU  633  CE  LYS A  81    14311  15605  15018    919    468   -356  A    C  
ATOM    634  NZ  LYS A  81     111.599  65.693  32.461  1.00115.42      A    N1+
ANISOU  634  NZ  LYS A  81    13926  15344  14583   1020    443   -199  A    N1+
ATOM    635  N   LEU A  82     109.000  68.332  26.117  1.00 74.83      A    N  
ANISOU  635  N   LEU A  82     8684  10669   9076    666    206   -725  A    N  
ATOM    636  CA  LEU A  82     108.208  68.208  24.904  1.00 73.84      A    C  
ANISOU  636  CA  LEU A  82     8502  10694   8858    654    186   -857  A    C  
ATOM    637  C   LEU A  82     108.180  69.543  24.149  1.00 71.37      A    C  
ANISOU  637  C   LEU A  82     8157  10564   8394    712    169   -752  A    C  
ATOM    638  O   LEU A  82     107.237  69.839  23.417  1.00 71.45      A    O  
ANISOU  638  O   LEU A  82     8111  10736   8299    721    146   -797  A    O  
ATOM    639  CB  LEU A  82     106.789  67.755  25.247  1.00 73.05      A    C  
ANISOU  639  CB  LEU A  82     8383  10544   8826    567    177   -959  A    C  
ATOM    640  CG  LEU A  82     106.624  66.824  26.462  1.00 73.25      A    C  
ANISOU  640  CG  LEU A  82     8456  10326   9048    517    236   -959  A    C  
ATOM    641  CD1 LEU A  82     105.156  66.619  26.748  1.00 72.48      A    C  
ANISOU  641  CD1 LEU A  82     8331  10184   9024    427    242  -1043  A    C  
ATOM    642  CD2 LEU A  82     107.323  65.476  26.297  1.00 75.68      A    C  
ANISOU  642  CD2 LEU A  82     8768  10516   9470    532    313  -1072  A    C  
ATOM    643  N   GLY A  83     109.223  70.342  24.332  1.00 69.77      A    N  
ANISOU  643  N   GLY A  83     7975  10341   8194    759    202   -615  A    N  
ATOM    644  CA  GLY A  83     109.374  71.593  23.589  1.00 72.74      A    C  
ANISOU  644  CA  GLY A  83     8317  10844   8474    828    244   -495  A    C  
ATOM    645  C   GLY A  83     108.279  72.653  23.755  1.00 71.77      A    C  
ANISOU  645  C   GLY A  83     8183  10764   8323    812    246   -405  A    C  
ATOM    646  O   GLY A  83     108.133  73.535  22.911  1.00 68.37      A    O  
ANISOU  646  O   GLY A  83     7713  10465   7799    895    303   -305  A    O  
ATOM    647  N   LYS A  84     107.537  72.604  24.855  1.00 73.23      A    N  
ANISOU  647  N   LYS A  84     8399  10835   8590    723    203   -415  A    N  
ATOM    648  CA  LYS A  84     106.459  73.571  25.078  1.00 75.78      A    C  
ANISOU  648  CA  LYS A  84     8712  11188   8891    703    204   -335  A    C  
ATOM    649  C   LYS A  84     106.875  74.727  25.963  1.00 68.52      A    C  
ANISOU  649  C   LYS A  84     7810  10160   8062    678    256   -216  A    C  
ATOM    650  O   LYS A  84     107.609  74.528  26.911  1.00 69.51      A    O  
ANISOU  650  O   LYS A  84     7957  10175   8278    640    247   -234  A    O  
ATOM    651  CB  LYS A  84     105.253  72.884  25.719  1.00 81.25      A    C  
ANISOU  651  CB  LYS A  84     9414  11833   9621    618    137   -426  A    C  
ATOM    652  CG  LYS A  84     104.421  72.044  24.757  1.00 88.27      A    C  
ANISOU  652  CG  LYS A  84    10242  12871  10422    622     99   -584  A    C  
ATOM    653  CD  LYS A  84     103.675  72.939  23.756  1.00 95.23      A    C  
ANISOU  653  CD  LYS A  84    11054  13989  11139    704    105   -525  A    C  
ATOM    654  CE  LYS A  84     103.288  72.169  22.503  1.00103.86      A    C  
ANISOU  654  CE  LYS A  84    12047  15327  12085    757     71   -698  A    C  
ATOM    655  NZ  LYS A  84     104.460  71.478  21.863  1.00107.95      A    N1+
ANISOU  655  NZ  LYS A  84    12561  15872  12582    810     92   -768  A    N1+
ATOM    656  N   SER A  85     106.404  75.928  25.652  1.00 62.48      A    N  
ANISOU  656  N   SER A  85     7021   9443   7276    709    321   -105  A    N  
ATOM    657  CA  SER A  85     106.653  77.056  26.515  1.00 59.15      A    C  
ANISOU  657  CA  SER A  85     6597   8908   6967    666    386    -32  A    C  
ATOM    658  C   SER A  85     105.442  77.293  27.362  1.00 59.54      A    C  
ANISOU  658  C   SER A  85     6663   8925   7031    599    334    -28  A    C  
ATOM    659  O   SER A  85     104.302  77.047  26.966  1.00 59.32      A    O  
ANISOU  659  O   SER A  85     6633   8982   6920    608    287    -31  A    O  
ATOM    660  CB  SER A  85     106.944  78.317  25.737  1.00 59.12      A    C  
ANISOU  660  CB  SER A  85     6553   8926   6982    740    541     97  A    C  
ATOM    661  OG  SER A  85     108.196  78.212  25.141  1.00 61.97      A    O  
ANISOU  661  OG  SER A  85     6893   9284   7364    793    612    101  A    O  
ATOM    662  N   VAL A  86     105.698  77.806  28.545  1.00 59.33      A    N  
ANISOU  662  N   VAL A  86     6638   8797   7104    534    342    -35  A    N  
ATOM    663  CA  VAL A  86     104.647  78.085  29.480  1.00 57.25      A    C  
ANISOU  663  CA  VAL A  86     6389   8502   6861    475    298    -27  A    C  
ATOM    664  C   VAL A  86     104.888  79.461  30.059  1.00 56.89      A    C  
ANISOU  664  C   VAL A  86     6303   8397   6914    443    391      4  A    C  
ATOM    665  O   VAL A  86     105.993  79.752  30.484  1.00 60.38      A    O  
ANISOU  665  O   VAL A  86     6705   8804   7433    424    435    -52  A    O  
ATOM    666  CB  VAL A  86     104.702  77.067  30.602  1.00 56.69      A    C  
ANISOU  666  CB  VAL A  86     6346   8385   6808    437    207    -96  A    C  
ATOM    667  CG1 VAL A  86     103.549  77.289  31.557  1.00 56.75      A    C  
ANISOU  667  CG1 VAL A  86     6367   8365   6827    389    169    -74  A    C  
ATOM    668  CG2 VAL A  86     104.685  75.660  30.013  1.00 56.30      A    C  
ANISOU  668  CG2 VAL A  86     6325   8349   6714    460    157   -154  A    C  
ATOM    669  N   ALA A  87     103.871  80.313  30.040  1.00 55.29      A    N  
ANISOU  669  N   ALA A  87     6098   8191   6718    435    434     76  A    N  
ATOM    670  CA  ALA A  87     103.924  81.588  30.727  1.00 54.37      A    C  
ANISOU  670  CA  ALA A  87     5939   8000   6720    387    531     78  A    C  
ATOM    671  C   ALA A  87     103.332  81.393  32.117  1.00 53.04      A    C  
ANISOU  671  C   ALA A  87     5779   7826   6547    320    429     16  A    C  
ATOM    672  O   ALA A  87     102.267  80.800  32.274  1.00 52.66      A    O  
ANISOU  672  O   ALA A  87     5776   7806   6425    318    340     46  A    O  
ATOM    673  CB  ALA A  87     103.116  82.619  29.973  1.00 55.47      A    C  
ANISOU  673  CB  ALA A  87     6068   8133   6873    434    654    211  A    C  
ATOM    674  N   ILE A  88     104.012  81.900  33.132  1.00 51.70      A    N  
ANISOU  674  N   ILE A  88     5548   7637   6455    271    452    -81  A    N  
ATOM    675  CA  ILE A  88     103.530  81.738  34.455  1.00 51.01      A    C  
ANISOU  675  CA  ILE A  88     5455   7586   6338    238    364   -129  A    C  
ATOM    676  C   ILE A  88     102.821  83.007  34.834  1.00 52.24      A    C  
ANISOU  676  C   ILE A  88     5575   7703   6570    189    443   -127  A    C  
ATOM    677  O   ILE A  88     103.483  83.986  35.055  1.00 54.54      A    O  
ANISOU  677  O   ILE A  88     5782   7964   6976    148    552   -218  A    O  
ATOM    678  CB  ILE A  88     104.689  81.515  35.405  1.00 51.38      A    C  
ANISOU  678  CB  ILE A  88     5427   7705   6390    237    331   -257  A    C  
ATOM    679  CG1 ILE A  88     105.578  80.393  34.891  1.00 51.67      A    C  
ANISOU  679  CG1 ILE A  88     5491   7763   6379    292    287   -254  A    C  
ATOM    680  CG2 ILE A  88     104.156  81.155  36.785  1.00 52.43      A    C  
ANISOU  680  CG2 ILE A  88     5550   7922   6447    250    236   -273  A    C  
ATOM    681  CD1 ILE A  88     104.807  79.135  34.572  1.00 52.24      A    C  
ANISOU  681  CD1 ILE A  88     5664   7816   6369    334    204   -164  A    C  
ATOM    682  N   CYS A  89     101.488  82.997  34.921  1.00 52.26      A    N  
ANISOU  682  N   CYS A  89     5632   7701   6524    188    404    -39  A    N  
ATOM    683  CA  CYS A  89     100.744  84.160  35.399  1.00 52.05      A    C  
ANISOU  683  CA  CYS A  89     5574   7638   6564    146    475    -34  A    C  
ATOM    684  C   CYS A  89     100.468  84.117  36.895  1.00 52.79      A    C  
ANISOU  684  C   CYS A  89     5635   7797   6624    114    394   -116  A    C  
ATOM    685  O   CYS A  89      99.658  83.334  37.373  1.00 51.57      A    O  
ANISOU  685  O   CYS A  89     5535   7679   6380    136    291    -57  A    O  
ATOM    686  CB  CYS A  89      99.429  84.307  34.665  1.00 52.59      A    C  
ANISOU  686  CB  CYS A  89     5699   7690   6592    174    488    110  A    C  
ATOM    687  SG  CYS A  89      98.611  85.884  35.045  1.00 54.94      A    S  
ANISOU  687  SG  CYS A  89     5957   7917   6999    137    623    140  A    S  
ATOM    688  N   GLU A  90     101.160  84.978  37.629  1.00 56.59      A    N  
ANISOU  688  N   GLU A  90     6010   8301   7187     69    458   -264  A    N  
ATOM    689  CA  GLU A  90     100.941  85.165  39.052  1.00 59.94      A    C  
ANISOU  689  CA  GLU A  90     6370   8837   7567     55    399   -363  A    C  
ATOM    690  C   GLU A  90     100.235  86.474  39.250  1.00 64.76      A    C  
ANISOU  690  C   GLU A  90     6941   9380   8283     -8    509   -394  A    C  
ATOM    691  O   GLU A  90     100.042  87.214  38.299  1.00 69.45      A    O  
ANISOU  691  O   GLU A  90     7553   9836   8995    -30    644   -330  A    O  
ATOM    692  CB  GLU A  90     102.264  85.226  39.773  1.00 60.19      A    C  
ANISOU  692  CB  GLU A  90     6271   9000   7599     51    392   -559  A    C  
ATOM    693  CG  GLU A  90     103.046  83.928  39.680  1.00 63.22      A    C  
ANISOU  693  CG  GLU A  90     6684   9460   7875    130    294   -524  A    C  
ATOM    694  CD  GLU A  90     102.603  82.851  40.667  1.00 64.75      A    C  
ANISOU  694  CD  GLU A  90     6913   9780   7906    226    167   -442  A    C  
ATOM    695  OE1 GLU A  90     101.577  83.032  41.390  1.00 63.35      A    O  
ANISOU  695  OE1 GLU A  90     6752   9632   7686    233    141   -392  A    O  
ATOM    696  OE2 GLU A  90     103.303  81.808  40.704  1.00 66.04      A    O1-
ANISOU  696  OE2 GLU A  90     7088  10006   7997    306    113   -411  A    O1-
ATOM    697  N   GLN A  91      99.833  86.778  40.476  1.00 67.76      A    N  
ANISOU  697  N   GLN A  91     7261   9865   8619    -21    465   -482  A    N  
ATOM    698  CA  GLN A  91      99.329  88.120  40.736  1.00 70.93      A    C  
ANISOU  698  CA  GLN A  91     7599  10202   9148    -93    590   -559  A    C  
ATOM    699  C   GLN A  91     100.323  88.884  41.580  1.00 73.96      A    C  
ANISOU  699  C   GLN A  91     7802  10689   9610   -154    650   -847  A    C  
ATOM    700  O   GLN A  91     100.812  88.345  42.563  1.00 80.94      A    O  
ANISOU  700  O   GLN A  91     8607  11791  10354   -110    530   -961  A    O  
ATOM    701  CB  GLN A  91      97.962  88.107  41.400  1.00 71.97      A    C  
ANISOU  701  CB  GLN A  91     7785  10366   9192    -76    521   -461  A    C  
ATOM    702  CG  GLN A  91      97.695  86.984  42.374  1.00 76.27      A    C  
ANISOU  702  CG  GLN A  91     8354  11077   9544      4    353   -415  A    C  
ATOM    703  CD  GLN A  91      96.241  86.998  42.808  1.00 80.74      A    C  
ANISOU  703  CD  GLN A  91     8987  11630  10058     16    318   -287  A    C  
ATOM    704  NE2 GLN A  91      95.904  86.164  43.794  1.00 86.87      A    N  
ANISOU  704  NE2 GLN A  91     9775  12540  10691     95    212   -233  A    N  
ATOM    705  OE1 GLN A  91      95.417  87.721  42.228  1.00 75.90      A    O  
ANISOU  705  OE1 GLN A  91     8415  10888   9534    -27    399   -217  A    O  
ATOM    706  N   VAL A  92     100.605  90.132  41.195  1.00 73.66      A    N  
ANISOU  706  N   VAL A  92     7680  10504   9802   -244    854   -967  A    N  
ATOM    707  CA  VAL A  92     101.655  90.960  41.811  1.00 72.83      A    C  
ANISOU  707  CA  VAL A  92     7369  10467   9835   -334    959  -1300  A    C  
ATOM    708  C   VAL A  92     101.143  92.331  42.263  1.00 74.21      A    C  
ANISOU  708  C   VAL A  92     7444  10557  10195   -430   1127  -1458  A    C  
ATOM    709  O   VAL A  92     100.048  92.730  41.889  1.00 73.60      A    O  
ANISOU  709  O   VAL A  92     7472  10325  10165   -421   1194  -1270  A    O  
ATOM    710  CB  VAL A  92     102.810  91.170  40.814  1.00 70.44      A    C  
ANISOU  710  CB  VAL A  92     7025  10021   9717   -373   1111  -1351  A    C  
ATOM    711  CG1 VAL A  92     103.086  89.887  40.055  1.00 68.59      A    C  
ANISOU  711  CG1 VAL A  92     6928   9806   9325   -274    978  -1137  A    C  
ATOM    712  CG2 VAL A  92     102.495  92.282  39.852  1.00 69.15      A    C  
ANISOU  712  CG2 VAL A  92     6884   9562   9827   -423   1383  -1266  A    C  
ATOM    713  N   GLY A  93     101.918  93.049  43.070  1.00 79.37      A    N  
ANISOU  713  N   GLY A  93     7880  11324  10953   -521   1200  -1819  A    N  
ATOM    714  CA  GLY A  93     101.465  94.368  43.485  1.00 93.63      A    C  
ANISOU  714  CA  GLY A  93     9575  13031  12968   -625   1385  -2006  A    C  
ATOM    715  C   GLY A  93     102.265  95.206  44.488  1.00105.32      A    C  
ANISOU  715  C   GLY A  93    10772  14674  14569   -743   1469  -2483  A    C  
ATOM    716  O   GLY A  93     103.427  95.550  44.253  1.00 97.98      A    O  
ANISOU  716  O   GLY A  93     9690  13711  13826   -829   1601  -2727  A    O  
ATOM    717  N   GLU A  94     101.598  95.543  45.602  1.00113.81      A    N  
ANISOU  717  N   GLU A  94    11765  15938  15538   -748   1397  -2627  A    N  
ATOM    718  CA  GLU A  94     102.128  96.436  46.635  1.00117.95      A    C  
ANISOU  718  CA  GLU A  94    11998  16656  16159   -860   1475  -3113  A    C  
ATOM    719  C   GLU A  94     103.337  95.835  47.341  1.00115.66      A    C  
ANISOU  719  C   GLU A  94    11510  16756  15678   -825   1315  -3393  A    C  
ATOM    720  O   GLU A  94     104.280  96.541  47.674  1.00111.19      A    O  
ANISOU  720  O   GLU A  94    10677  16282  15285   -948   1440  -3829  A    O  
ATOM    721  CB  GLU A  94     101.007  96.758  47.655  1.00125.98      A    C  
ANISOU  721  CB  GLU A  94    13000  17830  17036   -833   1397  -3144  A    C  
ATOM    722  CG  GLU A  94     101.266  97.963  48.572  1.00124.74      A    C  
ANISOU  722  CG  GLU A  94    12548  17798  17048   -970   1543  -3651  A    C  
ATOM    723  CD  GLU A  94      99.994  98.765  48.917  1.00117.58      A    C  
ANISOU  723  CD  GLU A  94    11686  16769  16219  -1001   1635  -3610  A    C  
ATOM    724  OE1 GLU A  94     100.143  99.988  49.114  1.00110.70      A    O  
ANISOU  724  OE1 GLU A  94    10626  15778  15655  -1159   1881  -3964  A    O  
ATOM    725  OE2 GLU A  94      98.859  98.201  48.983  1.00103.39      A    O1-
ANISOU  725  OE2 GLU A  94    10099  14981  14202   -879   1483  -3245  A    O1-
ATOM    726  N   PRO A 101      95.784  97.237  44.632  1.00 77.49      A    N  
ANISOU  726  N   PRO A 101     7766  10600  11076   -644   1648  -1586  A    N  
ATOM    727  CA  PRO A 101      97.024  96.596  44.959  1.00 83.29      A    C  
ANISOU  727  CA  PRO A 101     8397  11532  11715   -654   1528  -1789  A    C  
ATOM    728  C   PRO A 101      97.404  95.345  44.153  1.00 80.45      A    C  
ANISOU  728  C   PRO A 101     8181  11190  11193   -558   1378  -1536  A    C  
ATOM    729  O   PRO A 101      98.490  94.837  44.380  1.00 86.66      A    O  
ANISOU  729  O   PRO A 101     8880  12131  11915   -560   1295  -1699  A    O  
ATOM    730  CB  PRO A 101      96.857  96.217  46.469  1.00 83.21      A    C  
ANISOU  730  CB  PRO A 101     8284  11890  11439   -620   1308  -1976  A    C  
ATOM    731  CG  PRO A 101      95.925  97.209  47.003  1.00 82.52      A    C  
ANISOU  731  CG  PRO A 101     8153  11749  11450   -671   1418  -2057  A    C  
ATOM    732  CD  PRO A 101      94.986  97.472  45.855  1.00 83.12      A    C  
ANISOU  732  CD  PRO A 101     8424  11495  11664   -648   1551  -1703  A    C  
ATOM    733  N   VAL A 102      96.557  94.806  43.285  1.00 73.62      A    N  
ANISOU  733  N   VAL A 102     7515  10207  10249   -472   1331  -1176  A    N  
ATOM    734  CA  VAL A 102      96.902  93.527  42.656  1.00 72.82      A    C  
ANISOU  734  CA  VAL A 102     7529  10162   9977   -388   1170   -988  A    C  
ATOM    735  C   VAL A 102      96.670  93.549  41.138  1.00 70.53      A    C  
ANISOU  735  C   VAL A 102     7365   9650   9782   -341   1292   -718  A    C  
ATOM    736  O   VAL A 102      95.636  93.991  40.645  1.00 68.30      A    O  
ANISOU  736  O   VAL A 102     7160   9248   9540   -307   1377   -525  A    O  
ATOM    737  CB  VAL A 102      96.169  92.334  43.352  1.00 74.51      A    C  
ANISOU  737  CB  VAL A 102     7835  10579   9896   -297    908   -852  A    C  
ATOM    738  CG1 VAL A 102      95.943  91.148  42.427  1.00 78.22      A    C  
ANISOU  738  CG1 VAL A 102     8465  11012  10243   -215    797   -586  A    C  
ATOM    739  CG2 VAL A 102      96.940  91.840  44.562  1.00 74.43      A    C  
ANISOU  739  CG2 VAL A 102     7701  10848   9730   -276    767  -1067  A    C  
ATOM    740  N   GLU A 103      97.651  93.037  40.412  1.00 68.99      A    N  
ANISOU  740  N   GLU A 103     7178   9435   9597   -321   1295   -702  A    N  
ATOM    741  CA  GLU A 103      97.556  92.920  38.979  1.00 69.56      A    C  
ANISOU  741  CA  GLU A 103     7354   9364   9712   -248   1391   -451  A    C  
ATOM    742  C   GLU A 103      97.997  91.551  38.483  1.00 67.63      A    C  
ANISOU  742  C   GLU A 103     7191   9228   9277   -180   1204   -354  A    C  
ATOM    743  O   GLU A 103      98.897  90.929  39.023  1.00 71.17      A    O  
ANISOU  743  O   GLU A 103     7588   9797   9656   -200   1090   -509  A    O  
ATOM    744  CB  GLU A 103      98.440  93.956  38.321  1.00 76.31      A    C  
ANISOU  744  CB  GLU A 103     8118  10017  10858   -290   1686   -526  A    C  
ATOM    745  CG  GLU A 103      98.513  93.835  36.787  1.00 81.04      A    C  
ANISOU  745  CG  GLU A 103     8806  10499  11486   -179   1809   -251  A    C  
ATOM    746  CD  GLU A 103      98.788  95.173  36.094  1.00 86.38      A    C  
ANISOU  746  CD  GLU A 103     9415  10916  12488   -179   2188   -207  A    C  
ATOM    747  OE1 GLU A 103      98.099  95.532  35.095  1.00 81.43      A    O  
ANISOU  747  OE1 GLU A 103     8860  10198  11881    -54   2337     86  A    O  
ATOM    748  OE2 GLU A 103      99.663  95.909  36.609  1.00 98.88      A    O1-
ANISOU  748  OE2 GLU A 103    10857  12397  14317   -301   2355   -478  A    O1-
ATOM    749  N   ARG A 104      97.352  91.080  37.440  1.00 63.68      A    N  
ANISOU  749  N   ARG A 104     6806   8703   8686    -88   1180   -104  A    N  
ATOM    750  CA  ARG A 104      97.661  89.804  36.924  1.00 60.89      A    C  
ANISOU  750  CA  ARG A 104     6522   8443   8167    -30   1020    -29  A    C  
ATOM    751  C   ARG A 104      98.832  89.948  35.984  1.00 63.82      A    C  
ANISOU  751  C   ARG A 104     6862   8736   8648    -10   1156    -34  A    C  
ATOM    752  O   ARG A 104      98.735  90.620  34.990  1.00 68.35      A    O  
ANISOU  752  O   ARG A 104     7442   9199   9327     45   1345    106  A    O  
ATOM    753  CB  ARG A 104      96.434  89.341  36.207  1.00 59.79      A    C  
ANISOU  753  CB  ARG A 104     6483   8338   7895     50    952    190  A    C  
ATOM    754  CG  ARG A 104      96.182  87.883  36.389  1.00 59.57      A    C  
ANISOU  754  CG  ARG A 104     6520   8435   7678     70    727    203  A    C  
ATOM    755  CD  ARG A 104      95.738  87.536  37.790  1.00 58.35      A    C  
ANISOU  755  CD  ARG A 104     6360   8348   7458     24    597    117  A    C  
ATOM    756  NE  ARG A 104      96.092  86.144  38.045  1.00 57.27      A    N  
ANISOU  756  NE  ARG A 104     6260   8294   7204     48    442     97  A    N  
ATOM    757  CZ  ARG A 104      95.464  85.372  38.898  1.00 56.60      A    C  
ANISOU  757  CZ  ARG A 104     6205   8269   7027     56    325    114  A    C  
ATOM    758  NH1 ARG A 104      94.429  85.840  39.599  1.00 57.78      A    N1+
ANISOU  758  NH1 ARG A 104     6354   8427   7171     39    323    142  A    N1+
ATOM    759  NH2 ARG A 104      95.883  84.137  39.054  1.00 56.67      A    N  
ANISOU  759  NH2 ARG A 104     6244   8321   6967     90    232    111  A    N  
ATOM    760  N   LYS A 105      99.964  89.344  36.305  1.00 68.57      A    N  
ANISOU  760  N   LYS A 105     7420   9402   9228    -40   1077   -183  A    N  
ATOM    761  CA  LYS A 105     101.205  89.526  35.509  1.00 69.05      A    C  
ANISOU  761  CA  LYS A 105     7434   9385   9415    -34   1218   -217  A    C  
ATOM    762  C   LYS A 105     101.781  88.200  35.015  1.00 65.63      A    C  
ANISOU  762  C   LYS A 105     7062   9052   8821     26   1061   -171  A    C  
ATOM    763  O   LYS A 105     101.417  87.134  35.497  1.00 65.61      A    O  
ANISOU  763  O   LYS A 105     7117   9172   8641     44    854   -165  A    O  
ATOM    764  CB  LYS A 105     102.262  90.197  36.388  1.00 72.64      A    C  
ANISOU  764  CB  LYS A 105     7735   9826  10038   -144   1307   -503  A    C  
ATOM    765  CG  LYS A 105     102.901  91.451  35.820  1.00 75.95      A    C  
ANISOU  765  CG  LYS A 105     8059  10039  10759   -190   1622   -558  A    C  
ATOM    766  CD  LYS A 105     102.043  92.686  36.097  1.00 77.82      A    C  
ANISOU  766  CD  LYS A 105     8261  10140  11168   -232   1806   -556  A    C  
ATOM    767  CE  LYS A 105     102.914  93.936  36.061  1.00 81.62      A    C  
ANISOU  767  CE  LYS A 105     8584  10419  12006   -330   2128   -749  A    C  
ATOM    768  NZ  LYS A 105     102.272  95.125  36.687  1.00 85.14      A    N1+
ANISOU  768  NZ  LYS A 105     8953  10747  12647   -410   2302   -859  A    N1+
ATOM    769  N   VAL A 106     102.724  88.261  34.096  1.00 65.24      A    N  
ANISOU  769  N   VAL A 106     6993   8940   8854     57   1181   -147  A    N  
ATOM    770  CA  VAL A 106     103.321  87.039  33.574  1.00 65.23      A    C  
ANISOU  770  CA  VAL A 106     7043   9028   8712    114   1048   -115  A    C  
ATOM    771  C   VAL A 106     104.694  86.710  34.153  1.00 66.88      A    C  
ANISOU  771  C   VAL A 106     7168   9285   8958     63   1010   -317  A    C  
ATOM    772  O   VAL A 106     105.112  85.576  34.103  1.00 81.95      A    O  
ANISOU  772  O   VAL A 106     9116  11286  10731    103    864   -316  A    O  
ATOM    773  CB  VAL A 106     103.324  87.039  32.040  1.00 64.66      A    C  
ANISOU  773  CB  VAL A 106     7019   8916   8630    223   1162     83  A    C  
ATOM    774  CG1 VAL A 106     104.258  86.023  31.456  1.00 63.80      A    C  
ANISOU  774  CG1 VAL A 106     6932   8872   8435    268   1084     72  A    C  
ATOM    775  CG2 VAL A 106     101.951  86.661  31.564  1.00 65.44      A    C  
ANISOU  775  CG2 VAL A 106     7204   9095   8566    299   1071    253  A    C  
ATOM    776  N   VAL A 107     105.384  87.657  34.738  1.00 65.26      A    N  
ANISOU  776  N   VAL A 107     6831   9030   8934    -24   1142   -507  A    N  
ATOM    777  CA  VAL A 107     106.574  87.355  35.567  1.00 64.58      A    C  
ANISOU  777  CA  VAL A 107     6627   9061   8848    -75   1073   -747  A    C  
ATOM    778  C   VAL A 107     107.738  86.559  34.888  1.00 65.48      A    C  
ANISOU  778  C   VAL A 107     6745   9204   8929    -29   1051   -740  A    C  
ATOM    779  O   VAL A 107     108.926  86.869  35.074  1.00 66.52      A    O  
ANISOU  779  O   VAL A 107     6744   9347   9182    -82   1132   -932  A    O  
ATOM    780  CB  VAL A 107     106.186  86.755  36.970  1.00 61.05      A    C  
ANISOU  780  CB  VAL A 107     6161   8817   8218    -74    857   -843  A    C  
ATOM    781  CG1 VAL A 107     104.957  87.429  37.547  1.00 61.17      A    C  
ANISOU  781  CG1 VAL A 107     6189   8808   8242   -106    869   -820  A    C  
ATOM    782  CG2 VAL A 107     105.936  85.277  36.932  1.00 59.70      A    C  
ANISOU  782  CG2 VAL A 107     6112   8745   7825     23    657   -698  A    C  
ATOM    783  N   ARG A 108     107.403  85.542  34.115  1.00 64.87      A    N  
ANISOU  783  N   ARG A 108     6803   9143   8698     65    946   -547  A    N  
ATOM    784  CA  ARG A 108     108.374  84.563  33.687  1.00 64.93      A    C  
ANISOU  784  CA  ARG A 108     6827   9210   8631    115    877   -550  A    C  
ATOM    785  C   ARG A 108     107.780  83.668  32.609  1.00 63.83      A    C  
ANISOU  785  C   ARG A 108     6830   9064   8356    211    810   -343  A    C  
ATOM    786  O   ARG A 108     106.650  83.201  32.696  1.00 61.18      A    O  
ANISOU  786  O   ARG A 108     6580   8762   7903    236    703   -247  A    O  
ATOM    787  CB  ARG A 108     108.787  83.715  34.879  1.00 68.53      A    C  
ANISOU  787  CB  ARG A 108     7240   9842   8954    122    695   -680  A    C  
ATOM    788  CG  ARG A 108     109.752  82.601  34.565  1.00 74.36      A    C  
ANISOU  788  CG  ARG A 108     7995  10649   9607    187    616   -677  A    C  
ATOM    789  CD  ARG A 108     109.629  81.466  35.588  1.00 83.03      A    C  
ANISOU  789  CD  ARG A 108     9114  11905  10527    251    432   -680  A    C  
ATOM    790  NE  ARG A 108     110.286  81.748  36.870  1.00 90.03      A    N  
ANISOU  790  NE  ARG A 108     9844  12972  11389    242    396   -869  A    N  
ATOM    791  CZ  ARG A 108     109.681  82.185  37.975  1.00 89.77      A    C  
ANISOU  791  CZ  ARG A 108     9751  13042  11313    227    356   -936  A    C  
ATOM    792  NH1 ARG A 108     108.373  82.390  37.983  1.00 87.16      A    N1+
ANISOU  792  NH1 ARG A 108     9518  12621  10974    211    347   -816  A    N1+
ATOM    793  NH2 ARG A 108     110.397  82.416  39.084  1.00 91.95      A    N  
ANISOU  793  NH2 ARG A 108     9852  13543  11539    239    321  -1135  A    N  
ATOM    794  N   ILE A 109     108.563  83.431  31.580  1.00 66.33      A    N  
ANISOU  794  N   ILE A 109     7154   9354   8694    261    881   -294  A    N  
ATOM    795  CA  ILE A 109     108.181  82.521  30.537  1.00 69.90      A    C  
ANISOU  795  CA  ILE A 109     7708   9844   9005    354    816   -148  A    C  
ATOM    796  C   ILE A 109     109.230  81.433  30.415  1.00 69.30      A    C  
ANISOU  796  C   ILE A 109     7635   9829   8865    385    730   -210  A    C  
ATOM    797  O   ILE A 109     110.377  81.714  30.086  1.00 76.07      A    O  
ANISOU  797  O   ILE A 109     8429  10657   9817    385    834   -261  A    O  
ATOM    798  CB  ILE A 109     108.094  83.243  29.205  1.00 77.22      A    C  
ANISOU  798  CB  ILE A 109     8639  10710   9988    428   1002      7  A    C  
ATOM    799  CG1 ILE A 109     106.990  84.286  29.260  1.00 80.28      A    C  
ANISOU  799  CG1 ILE A 109     9027  11040  10434    423   1102    100  A    C  
ATOM    800  CG2 ILE A 109     107.751  82.274  28.093  1.00 80.92      A    C  
ANISOU  800  CG2 ILE A 109     9182  11286  10278    537    924    122  A    C  
ATOM    801  CD1 ILE A 109     106.719  84.940  27.913  1.00 79.36      A    C  
ANISOU  801  CD1 ILE A 109     8917  10899  10336    547   1296    311  A    C  
ATOM    802  N   VAL A 110     108.831  80.195  30.689  1.00 65.35      A    N  
ANISOU  802  N   VAL A 110     7205   9399   8224    411    563   -206  A    N  
ATOM    803  CA  VAL A 110     109.729  79.054  30.688  1.00 63.33      A    C  
ANISOU  803  CA  VAL A 110     6958   9192   7910    448    485   -258  A    C  
ATOM    804  C   VAL A 110     109.745  78.449  29.304  1.00 62.94      A    C  
ANISOU  804  C   VAL A 110     6964   9155   7793    520    499   -180  A    C  
ATOM    805  O   VAL A 110     108.726  77.963  28.810  1.00 62.92      A    O  
ANISOU  805  O   VAL A 110     7020   9183   7701    546    445   -124  A    O  
ATOM    806  CB  VAL A 110     109.246  77.961  31.645  1.00 63.09      A    C  
ANISOU  806  CB  VAL A 110     6974   9206   7792    457    339   -275  A    C  
ATOM    807  CG1 VAL A 110     110.238  76.835  31.732  1.00 63.40      A    C  
ANISOU  807  CG1 VAL A 110     7014   9282   7793    511    290   -315  A    C  
ATOM    808  CG2 VAL A 110     109.030  78.512  33.029  1.00 65.64      A    C  
ANISOU  808  CG2 VAL A 110     7238   9565   8135    415    313   -332  A    C  
ATOM    809  N   THR A 111     110.918  78.482  28.691  1.00 62.08      A    N  
ANISOU  809  N   THR A 111     6817   9043   7724    553    576   -197  A    N  
ATOM    810  CA  THR A 111     111.109  77.949  27.365  1.00 61.66      A    C  
ANISOU  810  CA  THR A 111     6799   9031   7598    636    600   -134  A    C  
ATOM    811  C   THR A 111     112.243  76.944  27.425  1.00 61.66      A    C  
ANISOU  811  C   THR A 111     6795   9052   7581    658    548   -212  A    C  
ATOM    812  O   THR A 111     113.139  77.079  28.262  1.00 67.29      A    O  
ANISOU  812  O   THR A 111     7450   9751   8366    622    551   -294  A    O  
ATOM    813  CB  THR A 111     111.470  79.074  26.377  1.00 62.80      A    C  
ANISOU  813  CB  THR A 111     6898   9145   7818    685    793    -35  A    C  
ATOM    814  CG2 THR A 111     110.468  80.202  26.460  1.00 62.78      A    C  
ANISOU  814  CG2 THR A 111     6887   9100   7866    670    880     52  A    C  
ATOM    815  OG1 THR A 111     112.764  79.602  26.689  1.00 66.96      A    O  
ANISOU  815  OG1 THR A 111     7345   9601   8494    645    898   -107  A    O  
ATOM    816  N   PRO A 112     112.242  75.955  26.524  1.00 58.82      A    N  
ANISOU  816  N   PRO A 112     6480   8746   7121    724    507   -201  A    N  
ATOM    817  CA  PRO A 112     113.195  74.881  26.572  1.00 57.01      A    C  
ANISOU  817  CA  PRO A 112     6257   8527   6875    751    460   -271  A    C  
ATOM    818  C   PRO A 112     114.623  75.325  26.524  1.00 56.85      A    C  
ANISOU  818  C   PRO A 112     6169   8494   6937    761    546   -294  A    C  
ATOM    819  O   PRO A 112     115.490  74.583  27.000  1.00 56.13      A    O  
ANISOU  819  O   PRO A 112     6064   8414   6849    772    500   -360  A    O  
ATOM    820  CB  PRO A 112     112.863  74.094  25.333  1.00 58.22      A    C  
ANISOU  820  CB  PRO A 112     6447   8752   6921    818    443   -264  A    C  
ATOM    821  CG  PRO A 112     111.408  74.276  25.180  1.00 58.40      A    C  
ANISOU  821  CG  PRO A 112     6491   8814   6883    803    408   -236  A    C  
ATOM    822  CD  PRO A 112     111.256  75.733  25.462  1.00 59.48      A    C  
ANISOU  822  CD  PRO A 112     6595   8910   7092    780    497   -147  A    C  
ATOM    823  N   GLY A 113     114.876  76.530  26.006  1.00 56.96      A    N  
ANISOU  823  N   GLY A 113     6131   8476   7033    760    690   -239  A    N  
ATOM    824  CA  GLY A 113     116.258  77.036  25.847  1.00 58.44      A    C  
ANISOU  824  CA  GLY A 113     6235   8632   7337    759    813   -275  A    C  
ATOM    825  C   GLY A 113     116.746  78.156  26.760  1.00 58.54      A    C  
ANISOU  825  C   GLY A 113     6138   8583   7520    665    901   -366  A    C  
ATOM    826  O   GLY A 113     117.858  78.730  26.533  1.00 58.97      A    O  
ANISOU  826  O   GLY A 113     6098   8594   7711    648   1043   -416  A    O  
ATOM    827  N   THR A 114     115.954  78.480  27.780  1.00 57.32      A    N  
ANISOU  827  N   THR A 114     5979   8429   7369    598    834   -411  A    N  
ATOM    828  CA  THR A 114     116.348  79.540  28.666  1.00 60.37      A    C  
ANISOU  828  CA  THR A 114     6240   8786   7910    502    915   -540  A    C  
ATOM    829  C   THR A 114     116.335  79.077  30.104  1.00 58.76      A    C  
ANISOU  829  C   THR A 114     5996   8698   7632    471    755   -666  A    C  
ATOM    830  O   THR A 114     116.285  79.882  31.009  1.00 62.03      A    O  
ANISOU  830  O   THR A 114     6309   9134   8122    397    779   -788  A    O  
ATOM    831  CB  THR A 114     115.439  80.763  28.488  1.00 64.66      A    C  
ANISOU  831  CB  THR A 114     6782   9226   8559    461   1049   -471  A    C  
ATOM    832  CG2 THR A 114     115.615  81.414  27.090  1.00 65.37      A    C  
ANISOU  832  CG2 THR A 114     6879   9212   8745    526   1268   -320  A    C  
ATOM    833  OG1 THR A 114     114.077  80.341  28.659  1.00 71.69      A    O  
ANISOU  833  OG1 THR A 114     7780  10151   9306    483    917   -378  A    O  
ATOM    834  N   LEU A 115     116.471  77.785  30.326  1.00 58.07      A    N  
ANISOU  834  N   LEU A 115     5968   8693   7402    543    613   -645  A    N  
ATOM    835  CA  LEU A 115     116.431  77.223  31.678  1.00 57.67      A    C  
ANISOU  835  CA  LEU A 115     5882   8770   7259    563    480   -711  A    C  
ATOM    836  C   LEU A 115     117.652  77.532  32.513  1.00 58.57      A    C  
ANISOU  836  C   LEU A 115     5821   9026   7407    551    488   -889  A    C  
ATOM    837  O   LEU A 115     118.774  77.394  32.064  1.00 60.58      A    O  
ANISOU  837  O   LEU A 115     6015   9298   7703    567    538   -945  A    O  
ATOM    838  CB  LEU A 115     116.308  75.720  31.604  1.00 57.33      A    C  
ANISOU  838  CB  LEU A 115     5946   8747   7089    661    376   -618  A    C  
ATOM    839  CG  LEU A 115     115.180  75.266  30.685  1.00 57.05      A    C  
ANISOU  839  CG  LEU A 115     6053   8603   7019    668    365   -494  A    C  
ATOM    840  CD1 LEU A 115     115.199  73.759  30.670  1.00 58.76      A    C  
ANISOU  840  CD1 LEU A 115     6347   8820   7158    748    295   -454  A    C  
ATOM    841  CD2 LEU A 115     113.826  75.794  31.079  1.00 54.72      A    C  
ANISOU  841  CD2 LEU A 115     5797   8273   6721    618    344   -452  A    C  
ATOM    842  N   THR A 116     117.401  77.969  33.733  1.00 60.42      A    N  
ANISOU  842  N   THR A 116     5958   9385   7612    527    439   -992  A    N  
ATOM    843  CA  THR A 116     118.412  78.196  34.747  1.00 63.39      A    C  
ANISOU  843  CA  THR A 116     6134   9980   7968    534    415  -1193  A    C  
ATOM    844  C   THR A 116     118.064  77.506  36.062  1.00 66.82      A    C  
ANISOU  844  C   THR A 116     6546  10629   8212    646    275  -1168  A    C  
ATOM    845  O   THR A 116     118.902  77.444  36.933  1.00 68.87      A    O  
ANISOU  845  O   THR A 116     6637  11140   8391    705    231  -1308  A    O  
ATOM    846  CB  THR A 116     118.569  79.698  35.046  1.00 65.29      A    C  
ANISOU  846  CB  THR A 116     6205  10222   8378    394    531  -1412  A    C  
ATOM    847  CG2 THR A 116     119.375  80.372  33.963  1.00 67.23      A    C  
ANISOU  847  CG2 THR A 116     6404  10304   8835    311    713  -1473  A    C  
ATOM    848  OG1 THR A 116     117.295  80.350  35.119  1.00 64.29      A    O  
ANISOU  848  OG1 THR A 116     6156   9976   8292    333    556  -1345  A    O  
ATOM    849  N   ASP A 117     116.836  76.988  36.196  1.00 70.35      A    N  
ANISOU  849  N   ASP A 117     7150  10994   8586    687    217   -989  A    N  
ATOM    850  CA  ASP A 117     116.390  76.303  37.404  1.00 74.52      A    C  
ANISOU  850  CA  ASP A 117     7672  11691   8951    812    121   -915  A    C  
ATOM    851  C   ASP A 117     116.909  74.899  37.499  1.00 72.66      A    C  
ANISOU  851  C   ASP A 117     7484  11512   8610    975     82   -786  A    C  
ATOM    852  O   ASP A 117     116.683  74.114  36.616  1.00 71.12      A    O  
ANISOU  852  O   ASP A 117     7441  11125   8455    984    103   -657  A    O  
ATOM    853  CB  ASP A 117     114.876  76.195  37.424  1.00 81.22      A    C  
ANISOU  853  CB  ASP A 117     8674  12389   9797    792    103   -762  A    C  
ATOM    854  CG  ASP A 117     114.209  77.526  37.406  1.00 91.45      A    C  
ANISOU  854  CG  ASP A 117     9936  13623  11188    652    147   -855  A    C  
ATOM    855  OD1 ASP A 117     114.935  78.551  37.356  1.00 97.69      A    O  
ANISOU  855  OD1 ASP A 117    10581  14461  12075    563    213  -1048  A    O  
ATOM    856  OD2 ASP A 117     112.955  77.546  37.452  1.00108.75      A    O1-
ANISOU  856  OD2 ASP A 117    12235  15708  13374    631    132   -742  A    O1-
ATOM    857  N   SER A 118     117.521  74.557  38.619  1.00 75.53      A    N  
ANISOU  857  N   SER A 118     7711  12157   8829   1119     34   -815  A    N  
ATOM    858  CA  SER A 118     118.104  73.241  38.809  1.00 76.22      A    C  
ANISOU  858  CA  SER A 118     7825  12316   8818   1305     24   -675  A    C  
ATOM    859  C   SER A 118     117.055  72.163  38.664  1.00 73.61      A    C  
ANISOU  859  C   SER A 118     7696  11769   8500   1371     47   -433  A    C  
ATOM    860  O   SER A 118     117.353  71.027  38.387  1.00 72.24      A    O  
ANISOU  860  O   SER A 118     7600  11516   8330   1477     84   -307  A    O  
ATOM    861  CB  SER A 118     118.729  73.155  40.197  1.00 81.24      A    C  
ANISOU  861  CB  SER A 118     8260  13344   9261   1486    -26   -719  A    C  
ATOM    862  OG  SER A 118     119.362  71.902  40.372  1.00 89.67      A    O  
ANISOU  862  OG  SER A 118     9345  14487  10237   1691    -10   -560  A    O  
ATOM    863  N   ALA A 119     115.812  72.542  38.860  1.00 76.20      A    N  
ANISOU  863  N   ALA A 119     8098  11995   8858   1301     41   -386  A    N  
ATOM    864  CA  ALA A 119     114.705  71.613  38.836  1.00 78.29      A    C  
ANISOU  864  CA  ALA A 119     8527  12061   9157   1344     77   -191  A    C  
ATOM    865  C   ALA A 119     114.278  71.236  37.430  1.00 74.28      A    C  
ANISOU  865  C   ALA A 119     8173  11260   8789   1222    114   -176  A    C  
ATOM    866  O   ALA A 119     113.564  70.268  37.238  1.00 75.48      A    O  
ANISOU  866  O   ALA A 119     8443  11237   8997   1251    160    -57  A    O  
ATOM    867  CB  ALA A 119     113.533  72.237  39.591  1.00 81.57      A    C  
ANISOU  867  CB  ALA A 119     8943  12502   9545   1310     54   -165  A    C  
ATOM    868  N   LEU A 120     114.687  72.026  36.455  1.00 72.56      A    N  
ANISOU  868  N   LEU A 120     7939  10998   8630   1091    108   -306  A    N  
ATOM    869  CA  LEU A 120     114.289  71.811  35.069  1.00 73.37      A    C  
ANISOU  869  CA  LEU A 120     8161  10888   8826    995    138   -302  A    C  
ATOM    870  C   LEU A 120     115.453  71.349  34.177  1.00 76.31      A    C  
ANISOU  870  C   LEU A 120     8526  11247   9218   1019    166   -343  A    C  
ATOM    871  O   LEU A 120     115.310  71.189  32.971  1.00 74.45      A    O  
ANISOU  871  O   LEU A 120     8365  10887   9034    962    191   -355  A    O  
ATOM    872  CB  LEU A 120     113.733  73.128  34.523  1.00 72.33      A    C  
ANISOU  872  CB  LEU A 120     8022  10714   8745    852    141   -374  A    C  
ATOM    873  CG  LEU A 120     112.504  73.697  35.203  1.00 68.75      A    C  
ANISOU  873  CG  LEU A 120     7583  10253   8283    806    118   -341  A    C  
ATOM    874  CD1 LEU A 120     112.050  74.962  34.520  1.00 68.59      A    C  
ANISOU  874  CD1 LEU A 120     7557  10174   8329    680    150   -397  A    C  
ATOM    875  CD2 LEU A 120     111.443  72.653  35.077  1.00 69.89      A    C  
ANISOU  875  CD2 LEU A 120     7850  10264   8441    829    120   -232  A    C  
ATOM    876  N   LEU A 121     116.612  71.168  34.789  1.00 48.49      A    N  
ATOM    877  CA  LEU A 121     117.855  70.813  34.114  1.00 46.39      A    C  
ATOM    878  C   LEU A 121     118.490  69.570  34.790  1.00 53.14      A    C  
ATOM    879  O   LEU A 121     118.624  69.455  36.043  1.00 46.57      A    O  
ATOM    880  CB  LEU A 121     118.845  71.977  34.174  1.00 43.25      A    C  
ATOM    881  CG  LEU A 121     118.536  73.250  33.405  1.00 49.14      A    C  
ATOM    882  CD1 LEU A 121     119.556  74.369  33.656  1.00 50.54      A    C  
ATOM    883  CD2 LEU A 121     118.518  72.920  31.932  1.00 59.15      A    C  
ATOM    884  N   GLU A 122     118.901  68.640  33.944  1.00 60.93      A    N  
ATOM    885  CA  GLU A 122     119.769  67.567  34.373  1.00 63.52      A    C  
ATOM    886  C   GLU A 122     121.094  68.173  34.859  1.00 56.44      A    C  
ATOM    887  O   GLU A 122     121.440  69.305  34.489  1.00 64.74      A    O  
ATOM    888  CB  GLU A 122     120.034  66.649  33.199  1.00 78.35      A    C  
ATOM    889  CG  GLU A 122     120.111  65.208  33.616  1.00 95.78      A    C  
ATOM    890  CD  GLU A 122     118.735  64.666  33.842  1.00103.36      A    C  
ATOM    891  OE1 GLU A 122     118.034  64.493  32.824  1.00 97.08      A    O  
ATOM    892  OE2 GLU A 122     118.368  64.455  35.021  1.00111.97      A    O1-
ATOM    893  N   ASP A 123     121.851  67.438  35.664  1.00 85.00      A    N  
ANISOU  893  N   ASP A 123    11548  10495  10253   -949  -1056   1095  A    N  
ATOM    894  CA  ASP A 123     123.067  68.000  36.256  1.00 75.88      A    C  
ANISOU  894  CA  ASP A 123    10363   9301   9165   -771  -1178   1104  A    C  
ATOM    895  C   ASP A 123     124.162  68.282  35.239  1.00 68.34      A    C  
ANISOU  895  C   ASP A 123     9222   8342   8402   -589  -1188   1006  A    C  
ATOM    896  O   ASP A 123     124.933  69.183  35.416  1.00 66.80      A    O  
ANISOU  896  O   ASP A 123     8911   8211   8258   -484  -1236    986  A    O  
ATOM    897  CB  ASP A 123     123.615  67.081  37.327  1.00 81.65      A    C  
ANISOU  897  CB  ASP A 123    11319   9818   9882   -733  -1336   1204  A    C  
ATOM    898  CG  ASP A 123     122.668  66.906  38.481  1.00 87.41      A    C  
ANISOU  898  CG  ASP A 123    12253  10548  10408   -907  -1328   1316  A    C  
ATOM    899  OD1 ASP A 123     121.773  67.757  38.615  1.00 95.64      A    O  
ANISOU  899  OD1 ASP A 123    13225  11787  11326  -1021  -1210   1313  A    O  
ATOM    900  OD2 ASP A 123     122.804  65.917  39.240  1.00 93.67      A    O1-
ANISOU  900  OD2 ASP A 123    13283  11147  11161   -926  -1431   1411  A    O1-
ATOM    901  N   LYS A 124     124.256  67.524  34.170  1.00 65.44      A    N  
ANISOU  901  N   LYS A 124     8831   7900   8132   -561  -1140    944  A    N  
ATOM    902  CA  LYS A 124     125.282  67.796  33.170  1.00 63.67      A    C  
ANISOU  902  CA  LYS A 124     8430   7682   8078   -392  -1122    854  A    C  
ATOM    903  C   LYS A 124     124.698  68.272  31.846  1.00 64.45      A    C  
ANISOU  903  C   LYS A 124     8389   7926   8174   -438   -969    761  A    C  
ATOM    904  O   LYS A 124     125.324  68.133  30.809  1.00 63.70      A    O  
ANISOU  904  O   LYS A 124     8201   7807   8194   -332   -923    684  A    O  
ATOM    905  CB  LYS A 124     126.065  66.522  32.934  1.00 64.22      A    C  
ANISOU  905  CB  LYS A 124     8596   7534   8268   -272  -1188    846  A    C  
ATOM    906  CG  LYS A 124     126.817  66.085  34.161  1.00 64.45      A    C  
ANISOU  906  CG  LYS A 124     8745   7422   8321   -178  -1359    940  A    C  
ATOM    907  CD  LYS A 124     127.245  64.662  34.078  1.00 65.17      A    C  
ANISOU  907  CD  LYS A 124     9002   7272   8487    -79  -1418    954  A    C  
ATOM    908  CE  LYS A 124     127.945  64.255  35.345  1.00 66.52      A    C  
ANISOU  908  CE  LYS A 124     9298   7307   8667     28  -1606   1061  A    C  
ATOM    909  NZ  LYS A 124     128.269  62.805  35.235  1.00 68.46      A    N1+
ANISOU  909  NZ  LYS A 124     9741   7293   8976    138  -1654   1077  A    N1+
ATOM    910  N   GLU A 125     123.495  68.832  31.902  1.00 67.58      A    N  
ANISOU  910  N   GLU A 125     8768   8479   8429   -589   -887    773  A    N  
ATOM    911  CA  GLU A 125     122.744  69.259  30.733  1.00 69.69      A    C  
ANISOU  911  CA  GLU A 125     8913   8899   8666   -644   -760    702  A    C  
ATOM    912  C   GLU A 125     123.272  70.597  30.256  1.00 67.92      A    C  
ANISOU  912  C   GLU A 125     8508   8807   8489   -529   -712    652  A    C  
ATOM    913  O   GLU A 125     123.296  71.531  31.041  1.00 69.11      A    O  
ANISOU  913  O   GLU A 125     8635   9035   8589   -520   -732    687  A    O  
ATOM    914  CB  GLU A 125     121.267  69.448  31.119  1.00 74.85      A    C  
ANISOU  914  CB  GLU A 125     9587   9696   9153   -832   -699    748  A    C  
ATOM    915  CG  GLU A 125     120.294  68.767  30.170  1.00 81.86      A    C  
ANISOU  915  CG  GLU A 125    10476  10623  10001   -968   -634    708  A    C  
ATOM    916  CD  GLU A 125     118.832  69.077  30.458  1.00 83.78      A    C  
ANISOU  916  CD  GLU A 125    10673  11060  10098  -1152   -563    753  A    C  
ATOM    917  OE1 GLU A 125     118.165  68.208  31.074  1.00 84.02      A    O  
ANISOU  917  OE1 GLU A 125    10838  11028  10056  -1326   -582    817  A    O  
ATOM    918  OE2 GLU A 125     118.359  70.167  30.045  1.00 84.92      A    O1-
ANISOU  918  OE2 GLU A 125    10649  11416  10202  -1118   -484    726  A    O1-
ATOM    919  N   THR A 126     123.696  70.711  28.998  1.00 68.14      A    N  
ANISOU  919  N   THR A 126     8434   8853   8603   -447   -646    572  A    N  
ATOM    920  CA  THR A 126     124.046  72.024  28.477  1.00 69.92      A    C  
ANISOU  920  CA  THR A 126     8509   9203   8853   -366   -583    532  A    C  
ATOM    921  C   THR A 126     122.799  72.547  27.796  1.00 69.63      A    C  
ANISOU  921  C   THR A 126     8418   9341   8697   -445   -483    511  A    C  
ATOM    922  O   THR A 126     122.121  71.797  27.105  1.00 76.20      A    O  
ANISOU  922  O   THR A 126     9278  10181   9493   -521   -451    485  A    O  
ATOM    923  CB  THR A 126     125.265  72.015  27.527  1.00 74.13      A    C  
ANISOU  923  CB  THR A 126     8953   9674   9537   -228   -555    469  A    C  
ATOM    924  CG2 THR A 126     125.785  73.462  27.333  1.00 74.14      A    C  
ANISOU  924  CG2 THR A 126     8827   9775   9566   -165   -512    452  A    C  
ATOM    925  OG1 THR A 126     126.335  71.198  28.056  1.00 77.23      A    O  
ANISOU  925  OG1 THR A 126     9386   9905  10052   -145   -650    487  A    O  
ATOM    926  N   ASN A 127     122.471  73.820  28.007  1.00 67.59      A    N  
ANISOU  926  N   ASN A 127     8088   9219   8372   -427   -440    521  A    N  
ATOM    927  CA  ASN A 127     121.172  74.348  27.573  1.00 63.74      A    C  
ANISOU  927  CA  ASN A 127     7541   8915   7760   -487   -355    518  A    C  
ATOM    928  C   ASN A 127     121.380  75.592  26.739  1.00 61.16      A    C  
ANISOU  928  C   ASN A 127     7116   8682   7439   -376   -282    476  A    C  
ATOM    929  O   ASN A 127     121.731  76.644  27.267  1.00 59.87      A    O  
ANISOU  929  O   ASN A 127     6946   8534   7266   -314   -279    488  A    O  
ATOM    930  CB  ASN A 127     120.317  74.654  28.800  1.00 65.18      A    C  
ANISOU  930  CB  ASN A 127     7765   9180   7820   -567   -359    586  A    C  
ATOM    931  CG  ASN A 127     118.930  75.157  28.454  1.00 63.51      A    C  
ANISOU  931  CG  ASN A 127     7462   9182   7486   -618   -267    591  A    C  
ATOM    932  ND2 ASN A 127     117.982  74.246  28.268  1.00 61.02      A    N  
ANISOU  932  ND2 ASN A 127     7142   8920   7121   -760   -259    607  A    N  
ATOM    933  OD1 ASN A 127     118.726  76.363  28.354  1.00 65.68      A    O  
ANISOU  933  OD1 ASN A 127     7671   9571   7711   -528   -206    581  A    O  
ATOM    934  N   ARG A 128     121.181  75.458  25.424  1.00 61.26      A    N  
ANISOU  934  N   ARG A 128     7074   8742   7457   -355   -227    428  A    N  
ATOM    935  CA  ARG A 128     121.474  76.548  24.482  1.00 59.95      A    C  
ANISOU  935  CA  ARG A 128     6842   8638   7298   -245   -155    392  A    C  
ATOM    936  C   ARG A 128     120.285  76.998  23.682  1.00 58.77      A    C  
ANISOU  936  C   ARG A 128     6627   8667   7033   -245    -95    386  A    C  
ATOM    937  O   ARG A 128     119.448  76.201  23.284  1.00 57.53      A    O  
ANISOU  937  O   ARG A 128     6457   8575   6826   -334   -107    380  A    O  
ATOM    938  CB  ARG A 128     122.531  76.129  23.470  1.00 61.26      A    C  
ANISOU  938  CB  ARG A 128     7007   8695   7572   -183   -133    341  A    C  
ATOM    939  CG  ARG A 128     123.934  76.434  23.906  1.00 61.37      A    C  
ANISOU  939  CG  ARG A 128     7015   8587   7714   -116   -157    341  A    C  
ATOM    940  CD  ARG A 128     124.954  76.256  22.812  1.00 59.77      A    C  
ANISOU  940  CD  ARG A 128     6780   8315   7612    -42    -97    294  A    C  
ATOM    941  NE  ARG A 128     126.190  75.977  23.495  1.00 58.72      A    N  
ANISOU  941  NE  ARG A 128     6626   8062   7621    -10   -154    304  A    N  
ATOM    942  CZ  ARG A 128     126.740  74.798  23.528  1.00 60.16      A    C  
ANISOU  942  CZ  ARG A 128     6828   8138   7892     10   -187    289  A    C  
ATOM    943  NH1 ARG A 128     126.202  73.798  22.840  1.00 61.69      A    N1+
ANISOU  943  NH1 ARG A 128     7086   8309   8041    -11   -160    254  A    N1+
ATOM    944  NH2 ARG A 128     127.868  74.645  24.197  1.00 62.81      A    N  
ANISOU  944  NH2 ARG A 128     7119   8385   8360     58   -251    306  A    N  
ATOM    945  N   ILE A 129     120.263  78.292  23.412  1.00 57.64      A    N  
ANISOU  945  N   ILE A 129     6451   8596   6852   -142    -40    388  A    N  
ATOM    946  CA  ILE A 129     119.258  78.895  22.581  1.00 58.37      A    C  
ANISOU  946  CA  ILE A 129     6477   8858   6841    -94     12    386  A    C  
ATOM    947  C   ILE A 129     120.027  79.508  21.431  1.00 55.87      A    C  
ANISOU  947  C   ILE A 129     6177   8491   6558     15     61    355  A    C  
ATOM    948  O   ILE A 129     120.926  80.331  21.637  1.00 54.50      A    O  
ANISOU  948  O   ILE A 129     6042   8224   6437     82     86    355  A    O  
ATOM    949  CB  ILE A 129     118.413  79.956  23.371  1.00 63.26      A    C  
ANISOU  949  CB  ILE A 129     7066   9607   7362    -43     47    428  A    C  
ATOM    950  CG1 ILE A 129     117.472  80.696  22.437  1.00 64.99      A    C  
ANISOU  950  CG1 ILE A 129     7206  10003   7484     53     97    431  A    C  
ATOM    951  CG2 ILE A 129     119.251  80.984  24.152  1.00 63.89      A    C  
ANISOU  951  CG2 ILE A 129     7225   9580   7469     34     59    433  A    C  
ATOM    952  CD1 ILE A 129     116.201  79.920  22.230  1.00 68.80      A    C  
ANISOU  952  CD1 ILE A 129     7578  10663   7899    -47     74    444  A    C  
ATOM    953  N   VAL A 130     119.703  79.089  20.217  1.00 56.00      A    N  
ANISOU  953  N   VAL A 130     6175   8563   6538     16     73    327  A    N  
ATOM    954  CA  VAL A 130     120.366  79.628  19.015  1.00 56.69      A    C  
ANISOU  954  CA  VAL A 130     6296   8609   6633    114    134    303  A    C  
ATOM    955  C   VAL A 130     119.400  80.288  18.029  1.00 54.97      A    C  
ANISOU  955  C   VAL A 130     6047   8552   6286    193    155    314  A    C  
ATOM    956  O   VAL A 130     118.282  79.854  17.826  1.00 55.81      A    O  
ANISOU  956  O   VAL A 130     6088   8806   6311    146    110    318  A    O  
ATOM    957  CB  VAL A 130     121.117  78.545  18.266  1.00 59.63      A    C  
ANISOU  957  CB  VAL A 130     6712   8873   7070     75    138    252  A    C  
ATOM    958  CG1 VAL A 130     120.143  77.553  17.675  1.00 62.07      A    C  
ANISOU  958  CG1 VAL A 130     7015   9272   7296     -7     89    226  A    C  
ATOM    959  CG2 VAL A 130     121.947  79.159  17.158  1.00 63.69      A    C  
ANISOU  959  CG2 VAL A 130     7268   9335   7593    171    225    236  A    C  
ATOM    960  N   ALA A 131     119.831  81.376  17.445  1.00 53.92      A    N  
ANISOU  960  N   ALA A 131     5962   8390   6133    313    218    326  A    N  
ATOM    961  CA  ALA A 131     118.968  82.153  16.609  1.00 55.37      A    C  
ANISOU  961  CA  ALA A 131     6132   8713   6191    422    232    350  A    C  
ATOM    962  C   ALA A 131     119.673  82.230  15.249  1.00 58.19      A    C  
ANISOU  962  C   ALA A 131     6578   8999   6530    472    283    332  A    C  
ATOM    963  O   ALA A 131     120.888  82.547  15.161  1.00 57.06      A    O  
ANISOU  963  O   ALA A 131     6509   8698   6469    484    352    325  A    O  
ATOM    964  CB  ALA A 131     118.756  83.535  17.216  1.00 54.64      A    C  
ANISOU  964  CB  ALA A 131     6059   8637   6064    540    270    392  A    C  
ATOM    965  N   VAL A 132     118.922  81.909  14.195  1.00 58.68      A    N  
ANISOU  965  N   VAL A 132     6630   9183   6483    490    249    324  A    N  
ATOM    966  CA  VAL A 132     119.478  81.938  12.868  1.00 58.43      A    C  
ANISOU  966  CA  VAL A 132     6701   9097   6400    538    299    309  A    C  
ATOM    967  C   VAL A 132     118.770  82.987  12.060  1.00 60.28      A    C  
ANISOU  967  C   VAL A 132     6965   9443   6493    685    296    358  A    C  
ATOM    968  O   VAL A 132     117.560  82.976  11.969  1.00 59.93      A    O  
ANISOU  968  O   VAL A 132     6827   9583   6359    712    215    375  A    O  
ATOM    969  CB  VAL A 132     119.400  80.591  12.170  1.00 58.10      A    C  
ANISOU  969  CB  VAL A 132     6677   9066   6330    437    256    248  A    C  
ATOM    970  CG1 VAL A 132     119.728  79.491  13.152  1.00 58.20      A    C  
ANISOU  970  CG1 VAL A 132     6651   8996   6468    304    227    209  A    C  
ATOM    971  CG2 VAL A 132     118.042  80.390  11.579  1.00 59.64      A    C  
ANISOU  971  CG2 VAL A 132     6813   9463   6383    434    154    252  A    C  
ATOM    972  N   SER A 133     119.558  83.919  11.525  1.00 63.28      A    N  
ANISOU  972  N   SER A 133     7470   9710   6862    778    389    387  A    N  
ATOM    973  CA  SER A 133     119.065  84.986  10.697  1.00 67.43      A    C  
ANISOU  973  CA  SER A 133     8071  10295   7253    938    398    443  A    C  
ATOM    974  C   SER A 133     119.625  84.650   9.370  1.00 73.08      A    C  
ANISOU  974  C   SER A 133     8911  10957   7898    934    444    429  A    C  
ATOM    975  O   SER A 133     120.840  84.652   9.229  1.00 74.99      A    O  
ANISOU  975  O   SER A 133     9240  11035   8217    888    551    417  A    O  
ATOM    976  CB  SER A 133     119.596  86.353  11.157  1.00 66.65      A    C  
ANISOU  976  CB  SER A 133     8066  10068   7186   1032    479    492  A    C  
ATOM    977  OG  SER A 133     118.991  87.424  10.435  1.00 66.72      A    O  
ANISOU  977  OG  SER A 133     8164  10129   7056   1213    479    555  A    O  
ATOM    978  N   PRO A 134     118.759  84.337   8.390  1.00 82.21      A    N  
ANISOU  978  N   PRO A 134    10072  12261   8903    975    361    430  A    N  
ATOM    979  CA  PRO A 134     119.232  83.928   7.075  1.00 82.65      A    C  
ANISOU  979  CA  PRO A 134    10272  12273   8859    968    400    410  A    C  
ATOM    980  C   PRO A 134     119.210  85.066   6.120  1.00 83.89      A    C  
ANISOU  980  C   PRO A 134    10580  12416   8875   1127    439    487  A    C  
ATOM    981  O   PRO A 134     118.201  85.686   5.963  1.00 83.58      A    O  
ANISOU  981  O   PRO A 134    10509  12512   8733   1253    349    538  A    O  
ATOM    982  CB  PRO A 134     118.208  82.907   6.643  1.00 84.34      A    C  
ANISOU  982  CB  PRO A 134    10412  12659   8974    904    256    365  A    C  
ATOM    983  CG  PRO A 134     116.952  83.313   7.362  1.00 87.24      A    C  
ANISOU  983  CG  PRO A 134    10601  13211   9334    954    142    405  A    C  
ATOM    984  CD  PRO A 134     117.294  84.273   8.470  1.00 84.48      A    C  
ANISOU  984  CD  PRO A 134    10220  12775   9102   1017    222    448  A    C  
ATOM    985  N   ASP A 135     120.350  85.354   5.530  1.00 98.55      A    N  
ANISOU  985  N   ASP A 135    12602  14108  10734   1124    582    498  A    N  
ATOM    986  CA  ASP A 135     120.438  86.191   4.354  1.00116.94      A    C  
ANISOU  986  CA  ASP A 135    15129  16405  12897   1247    632    569  A    C  
ATOM    987  C   ASP A 135     119.932  85.298   3.213  1.00135.90      A    C  
ANISOU  987  C   ASP A 135    17584  18923  15128   1236    551    530  A    C  
ATOM    988  O   ASP A 135     118.726  85.237   2.956  1.00150.46      A    O  
ANISOU  988  O   ASP A 135    19361  20951  16853   1301    387    544  A    O  
ATOM    989  CB  ASP A 135     121.899  86.618   4.164  1.00122.47      A    C  
ANISOU  989  CB  ASP A 135    15969  16891  13670   1198    828    587  A    C  
ATOM    990  CG  ASP A 135     122.056  87.816   3.284  1.00131.97      A    C  
ANISOU  990  CG  ASP A 135    17394  18015  14731   1322    900    685  A    C  
ATOM    991  OD1 ASP A 135     121.036  88.456   2.950  1.00131.79      A    O  
ANISOU  991  OD1 ASP A 135    17415  18092  14567   1478    792    745  A    O  
ATOM    992  OD2 ASP A 135     123.220  88.117   2.946  1.00147.91      A    O1-
ANISOU  992  OD2 ASP A 135    19537  19873  16786   1261   1070    706  A    O1-
ATOM    993  N   LYS A 136     120.862  84.599   2.556  1.00146.72      A    N  
ANISOU  993  N   LYS A 136    19068  20194  16484   1150    663    481  A    N  
ATOM    994  CA  LYS A 136     120.578  83.447   1.687  1.00152.22      A    C  
ANISOU  994  CA  LYS A 136    19818  20967  17048   1091    600    407  A    C  
ATOM    995  C   LYS A 136     121.908  82.901   1.152  1.00157.31      A    C  
ANISOU  995  C   LYS A 136    20599  21454  17717   1020    795    359  A    C  
ATOM    996  O   LYS A 136     122.051  81.691   0.941  1.00151.31      A    O  
ANISOU  996  O   LYS A 136    19849  20692  16950    932    791    262  A    O  
ATOM    997  CB  LYS A 136     119.618  83.786   0.544  1.00157.31      A    C  
ANISOU  997  CB  LYS A 136    20579  21751  17439   1205    471    456  A    C  
ATOM    998  CG  LYS A 136     120.100  84.865  -0.418  1.00163.25      A    C  
ANISOU  998  CG  LYS A 136    21566  22414  18048   1334    584    553  A    C  
ATOM    999  CD  LYS A 136     119.883  86.273   0.127  1.00156.91      A    C  
ANISOU  999  CD  LYS A 136    20743  21580  17293   1468    588    660  A    C  
ATOM   1000  CE  LYS A 136     119.865  87.293  -0.990  1.00158.68      A    C  
ANISOU 1000  CE  LYS A 136    21217  21763  17308   1625    618    769  A    C  
ATOM   1001  NZ  LYS A 136     119.557  88.654  -0.494  1.00154.24      A    N1+
ANISOU 1001  NZ  LYS A 136    20667  21160  16777   1778    608    868  A    N1+
ATOM   1002  N   LYS A 137     122.872  83.809   0.948  1.00158.94      A    N  
ANISOU 1002  N   LYS A 137    20913  21525  17951   1060    972    426  A    N  
ATOM   1003  CA  LYS A 137     124.277  83.444   0.723  1.00156.23      A    C  
ANISOU 1003  CA  LYS A 137    20629  21036  17692    987   1191    393  A    C  
ATOM   1004  C   LYS A 137     124.881  83.089   2.058  1.00138.56      A    C  
ANISOU 1004  C   LYS A 137    18185  18734  15725    894   1220    349  A    C  
ATOM   1005  O   LYS A 137     125.400  81.995   2.246  1.00150.51      A    O  
ANISOU 1005  O   LYS A 137    19638  20215  17331    823   1266    262  A    O  
ATOM   1006  CB  LYS A 137     125.096  84.602   0.134  1.00169.29      A    C  
ANISOU 1006  CB  LYS A 137    22448  22575  19299   1030   1371    493  A    C  
ATOM   1007  CG  LYS A 137     124.612  85.142  -1.203  1.00181.77      A    C  
ANISOU 1007  CG  LYS A 137    24274  24191  20597   1138   1356    564  A    C  
ATOM   1008  CD  LYS A 137     123.551  86.225  -1.040  1.00189.16      A    C  
ANISOU 1008  CD  LYS A 137    25225  25193  21454   1267   1196    656  A    C  
ATOM   1009  CE  LYS A 137     124.047  87.415  -0.232  1.00192.00      A    C  
ANISOU 1009  CE  LYS A 137    25560  25425  21965   1274   1276    733  A    C  
ATOM   1010  NZ  LYS A 137     122.954  88.408  -0.026  1.00191.93      A    N1+
ANISOU 1010  NZ  LYS A 137    25568  25478  21877   1430   1123    810  A    N1+
ATOM   1011  N   TYR A 138     124.807  84.029   2.990  1.00120.73      A    N  
ANISOU 1011  N   TYR A 138    15835  16452  13585    908   1189    410  A    N  
ATOM   1012  CA  TYR A 138     125.273  83.787   4.335  1.00110.13      A    C  
ANISOU 1012  CA  TYR A 138    14304  15059  12481    825   1183    377  A    C  
ATOM   1013  C   TYR A 138     124.091  83.539   5.275  1.00100.47      A    C  
ANISOU 1013  C   TYR A 138    12937  13951  11285    828    985    356  A    C  
ATOM   1014  O   TYR A 138     122.950  83.736   4.900  1.00 98.97      A    O  
ANISOU 1014  O   TYR A 138    12772  13885  10945    899    862    379  A    O  
ATOM   1015  CB  TYR A 138     126.130  84.960   4.797  1.00111.02      A    C  
ANISOU 1015  CB  TYR A 138    14423  15049  12706    811   1293    447  A    C  
ATOM   1016  CG  TYR A 138     127.417  85.082   4.015  1.00116.24      A    C  
ANISOU 1016  CG  TYR A 138    15181  15603  13381    767   1508    465  A    C  
ATOM   1017  CD1 TYR A 138     128.302  84.004   3.900  1.00114.36      A    C  
ANISOU 1017  CD1 TYR A 138    14870  15341  13240    703   1616    392  A    C  
ATOM   1018  CD2 TYR A 138     127.749  86.270   3.384  1.00125.34      A    C  
ANISOU 1018  CD2 TYR A 138    16500  16677  14446    795   1616    558  A    C  
ATOM   1019  CE1 TYR A 138     129.482  84.118   3.187  1.00115.10      A    C  
ANISOU 1019  CE1 TYR A 138    15027  15358  13348    666   1836    412  A    C  
ATOM   1020  CE2 TYR A 138     128.926  86.392   2.673  1.00128.89      A    C  
ANISOU 1020  CE2 TYR A 138    17030  17035  14904    734   1830    583  A    C  
ATOM   1021  CZ  TYR A 138     129.784  85.313   2.577  1.00122.74      A    C  
ANISOU 1021  CZ  TYR A 138    16148  16259  14228    670   1945    509  A    C  
ATOM   1022  OH  TYR A 138     130.945  85.460   1.869  1.00129.81      A    O  
ANISOU 1022  OH  TYR A 138    17102  17085  15133    613   2180    538  A    O  
ATOM   1023  N   ILE A 139     124.381  83.086   6.493  1.00 93.47      A    N  
ANISOU 1023  N   ILE A 139    11895  13031  10587    748    956    319  A    N  
ATOM   1024  CA  ILE A 139     123.379  82.884   7.537  1.00 81.26      A    C  
ANISOU 1024  CA  ILE A 139    10210  11582   9081    731    797    308  A    C  
ATOM   1025  C   ILE A 139     123.975  83.308   8.862  1.00 72.91      A    C  
ANISOU 1025  C   ILE A 139     9053  10439   8212    686    814    324  A    C  
ATOM   1026  O   ILE A 139     125.068  82.885   9.201  1.00 70.63      A    O  
ANISOU 1026  O   ILE A 139     8723  10045   8066    618    892    294  A    O  
ATOM   1027  CB  ILE A 139     122.970  81.413   7.616  1.00 85.59      A    C  
ANISOU 1027  CB  ILE A 139    10699  12184   9634    648    712    226  A    C  
ATOM   1028  CG1 ILE A 139     121.965  81.103   6.513  1.00 92.36      A    C  
ANISOU 1028  CG1 ILE A 139    11636  13171  10284    680    626    212  A    C  
ATOM   1029  CG2 ILE A 139     122.384  81.084   8.981  1.00 86.25      A    C  
ANISOU 1029  CG2 ILE A 139    10629  12314   9825    584    596    216  A    C  
ATOM   1030  CD1 ILE A 139     121.376  79.717   6.620  1.00 98.56      A    C  
ANISOU 1030  CD1 ILE A 139    12378  14012  11056    575    516    131  A    C  
ATOM   1031  N   GLY A 140     123.281  84.168   9.594  1.00 69.44      A    N  
ANISOU 1031  N   GLY A 140     8575  10045   7762    734    743    368  A    N  
ATOM   1032  CA  GLY A 140     123.771  84.651  10.878  1.00 67.88      A    C  
ANISOU 1032  CA  GLY A 140     8311   9766   7711    692    743    380  A    C  
ATOM   1033  C   GLY A 140     123.371  83.678  11.953  1.00 65.13      A    C  
ANISOU 1033  C   GLY A 140     7828   9470   7449    614    642    336  A    C  
ATOM   1034  O   GLY A 140     122.218  83.418  12.120  1.00 69.40      A    O  
ANISOU 1034  O   GLY A 140     8314  10142   7911    629    547    335  A    O  
ATOM   1035  N   LEU A 141     124.333  83.119  12.665  1.00 64.42      A    N  
ANISOU 1035  N   LEU A 141     7677   9281   7517    527    660    306  A    N  
ATOM   1036  CA  LEU A 141     124.066  82.304  13.852  1.00 62.33      A    C  
ANISOU 1036  CA  LEU A 141     7310   9034   7337    453    563    279  A    C  
ATOM   1037  C   LEU A 141     124.468  83.057  15.092  1.00 59.17      A    C  
ANISOU 1037  C   LEU A 141     6880   8570   7031    433    541    306  A    C  
ATOM   1038  O   LEU A 141     125.547  83.661  15.155  1.00 59.24      A    O  
ANISOU 1038  O   LEU A 141     6910   8469   7127    419    605    318  A    O  
ATOM   1039  CB  LEU A 141     124.918  81.046  13.831  1.00 66.33      A    C  
ANISOU 1039  CB  LEU A 141     7782   9461   7956    388    583    226  A    C  
ATOM   1040  CG  LEU A 141     124.235  79.706  13.680  1.00 68.53      A    C  
ANISOU 1040  CG  LEU A 141     8055   9790   8193    342    513    177  A    C  
ATOM   1041  CD1 LEU A 141     123.357  79.744  12.456  1.00 72.86      A    C  
ANISOU 1041  CD1 LEU A 141     8673  10445   8565    381    511    171  A    C  
ATOM   1042  CD2 LEU A 141     125.303  78.649  13.534  1.00 70.81      A    C  
ANISOU 1042  CD2 LEU A 141     8345   9964   8594    319    566    126  A    C  
ATOM   1043  N   ALA A 142     123.630  82.991  16.102  1.00 55.80      A    N  
ANISOU 1043  N   ALA A 142     6405   8210   6584    418    451    315  A    N  
ATOM   1044  CA  ALA A 142     123.980  83.585  17.369  1.00 56.09      A    C  
ANISOU 1044  CA  ALA A 142     6434   8184   6691    392    417    331  A    C  
ATOM   1045  C   ALA A 142     123.439  82.682  18.445  1.00 57.38      A    C  
ANISOU 1045  C   ALA A 142     6531   8393   6875    324    322    321  A    C  
ATOM   1046  O   ALA A 142     122.248  82.396  18.436  1.00 64.39      A    O  
ANISOU 1046  O   ALA A 142     7388   9410   7666    330    287    328  A    O  
ATOM   1047  CB  ALA A 142     123.384  84.980  17.479  1.00 55.05      A    C  
ANISOU 1047  CB  ALA A 142     6375   8083   6458    483    436    368  A    C  
ATOM   1048  N   TRP A 143     124.273  82.229  19.375  1.00 55.49      A    N  
ANISOU 1048  N   TRP A 143     6264   8058   6760    254    278    313  A    N  
ATOM   1049  CA  TRP A 143     123.740  81.381  20.435  1.00 55.88      A    C  
ANISOU 1049  CA  TRP A 143     6280   8137   6814    187    188    316  A    C  
ATOM   1050  C   TRP A 143     124.127  81.814  21.841  1.00 56.38      A    C  
ANISOU 1050  C   TRP A 143     6360   8140   6920    155    125    337  A    C  
ATOM   1051  O   TRP A 143     125.089  82.556  21.995  1.00 56.61      A    O  
ANISOU 1051  O   TRP A 143     6411   8080   7017    162    135    337  A    O  
ATOM   1052  CB  TRP A 143     124.121  79.933  20.208  1.00 55.56      A    C  
ANISOU 1052  CB  TRP A 143     6213   8046   6850    134    162    286  A    C  
ATOM   1053  CG  TRP A 143     125.532  79.662  20.242  1.00 55.66      A    C  
ANISOU 1053  CG  TRP A 143     6203   7931   7011    134    173    270  A    C  
ATOM   1054  CD1 TRP A 143     126.245  79.261  21.307  1.00 56.01      A    C  
ANISOU 1054  CD1 TRP A 143     6222   7893   7165    100     97    281  A    C  
ATOM   1055  CD2 TRP A 143     126.432  79.716  19.145  1.00 58.34      A    C  
ANISOU 1055  CD2 TRP A 143     6531   8224   7410    176    270    246  A    C  
ATOM   1056  CE2 TRP A 143     127.692  79.357  19.629  1.00 58.40      A    C  
ANISOU 1056  CE2 TRP A 143     6477   8132   7578    165    254    241  A    C  
ATOM   1057  CE3 TRP A 143     126.295  80.037  17.793  1.00 61.78      A    C  
ANISOU 1057  CE3 TRP A 143     7004   8699   7771    224    371    232  A    C  
ATOM   1058  NE1 TRP A 143     127.546  79.091  20.958  1.00 57.47      A    N  
ANISOU 1058  NE1 TRP A 143     6353   7994   7487    124    134    264  A    N  
ATOM   1059  CZ2 TRP A 143     128.831  79.317  18.815  1.00 61.36      A    C  
ANISOU 1059  CZ2 TRP A 143     6804   8457   8053    198    354    221  A    C  
ATOM   1060  CZ3 TRP A 143     127.429  80.002  16.982  1.00 63.07      A    C  
ANISOU 1060  CZ3 TRP A 143     7151   8795   8016    250    475    214  A    C  
ATOM   1061  CH2 TRP A 143     128.680  79.644  17.501  1.00 62.31      A    C  
ANISOU 1061  CH2 TRP A 143     6972   8611   8090    234    474    208  A    C  
ATOM   1062  N   ALA A 144     123.345  81.389  22.843  1.00 56.19      A    N  
ANISOU 1062  N   ALA A 144     6337   8167   6843    108     61    356  A    N  
ATOM   1063  CA  ALA A 144     123.577  81.757  24.252  1.00 56.14      A    C  
ANISOU 1063  CA  ALA A 144     6375   8114   6841     77     -7    377  A    C  
ATOM   1064  C   ALA A 144     123.110  80.680  25.198  1.00 56.63      A    C  
ANISOU 1064  C   ALA A 144     6438   8187   6890     -4    -81    399  A    C  
ATOM   1065  O   ALA A 144     122.136  79.984  24.930  1.00 58.11      A    O  
ANISOU 1065  O   ALA A 144     6598   8466   7016    -40    -68    405  A    O  
ATOM   1066  CB  ALA A 144     122.853  83.044  24.605  1.00 56.63      A    C  
ANISOU 1066  CB  ALA A 144     6495   8242   6778    139     33    390  A    C  
ATOM   1067  N   SER A 145     123.800  80.554  26.321  1.00 56.08      A    N  
ANISOU 1067  N   SER A 145     6409   8025   6872    -43   -169    415  A    N  
ATOM   1068  CA  SER A 145     123.392  79.603  27.322  1.00 57.53      A    C  
ANISOU 1068  CA  SER A 145     6629   8201   7026   -118   -244    450  A    C  
ATOM   1069  C   SER A 145     123.220  80.368  28.574  1.00 59.83      A    C  
ANISOU 1069  C   SER A 145     7003   8498   7228   -128   -282    476  A    C  
ATOM   1070  O   SER A 145     124.218  80.780  29.166  1.00 63.83      A    O  
ANISOU 1070  O   SER A 145     7548   8910   7794   -124   -357    472  A    O  
ATOM   1071  CB  SER A 145     124.468  78.550  27.544  1.00 58.94      A    C  
ANISOU 1071  CB  SER A 145     6803   8245   7345   -141   -333    451  A    C  
ATOM   1072  OG  SER A 145     124.081  77.594  28.521  1.00 58.98      A    O  
ANISOU 1072  OG  SER A 145     6876   8219   7314   -212   -412    494  A    O  
ATOM   1073  N   LEU A 146     121.963  80.579  28.966  1.00 60.91      A    N  
ANISOU 1073  N   LEU A 146     7164   8757   7221   -141   -228    499  A    N  
ATOM   1074  CA  LEU A 146     121.660  81.335  30.163  1.00 59.07      A    C  
ANISOU 1074  CA  LEU A 146     7031   8542   6870   -139   -238    519  A    C  
ATOM   1075  C   LEU A 146     122.313  80.739  31.394  1.00 60.09      A    C  
ANISOU 1075  C   LEU A 146     7253   8561   7018   -210   -367    552  A    C  
ATOM   1076  O   LEU A 146     122.698  81.501  32.299  1.00 60.70      A    O  
ANISOU 1076  O   LEU A 146     7432   8590   7039   -199   -418    551  A    O  
ATOM   1077  CB  LEU A 146     120.161  81.448  30.368  1.00 58.24      A    C  
ANISOU 1077  CB  LEU A 146     6908   8605   6612   -143   -141    546  A    C  
ATOM   1078  CG  LEU A 146     119.480  82.525  29.516  1.00 56.53      A    C  
ANISOU 1078  CG  LEU A 146     6634   8511   6333    -26    -26    519  A    C  
ATOM   1079  CD1 LEU A 146     118.012  82.665  29.840  1.00 56.80      A    C  
ANISOU 1079  CD1 LEU A 146     6621   8737   6223    -15     70    550  A    C  
ATOM   1080  CD2 LEU A 146     120.127  83.871  29.735  1.00 57.01      A    C  
ANISOU 1080  CD2 LEU A 146     6800   8486   6374     69    -21    486  A    C  
ATOM   1081  N   GLN A 147     122.496  79.418  31.428  1.00 58.64      A    N  
ANISOU 1081  N   GLN A 147     7052   8320   6906   -274   -430    580  A    N  
ATOM   1082  CA  GLN A 147     123.111  78.862  32.610  1.00 61.33      A    C  
ANISOU 1082  CA  GLN A 147     7493   8550   7257   -321   -564    622  A    C  
ATOM   1083  C   GLN A 147     124.610  79.034  32.702  1.00 63.42      A    C  
ANISOU 1083  C   GLN A 147     7740   8691   7663   -280   -683    600  A    C  
ATOM   1084  O   GLN A 147     125.163  78.934  33.790  1.00 67.26      A    O  
ANISOU 1084  O   GLN A 147     8314   9104   8135   -302   -814    632  A    O  
ATOM   1085  CB  GLN A 147     122.780  77.412  32.760  1.00 63.34      A    C  
ANISOU 1085  CB  GLN A 147     7772   8764   7527   -397   -598    668  A    C  
ATOM   1086  CG  GLN A 147     123.846  76.507  32.241  1.00 66.61      A    C  
ANISOU 1086  CG  GLN A 147     8142   9048   8116   -365   -678    653  A    C  
ATOM   1087  CD  GLN A 147     123.469  75.055  32.393  1.00 71.21      A    C  
ANISOU 1087  CD  GLN A 147     8792   9561   8701   -436   -710    696  A    C  
ATOM   1088  NE2 GLN A 147     123.272  74.367  31.257  1.00 73.76      A    N  
ANISOU 1088  NE2 GLN A 147     9054   9881   9089   -439   -648    658  A    N  
ATOM   1089  OE1 GLN A 147     123.367  74.545  33.514  1.00 71.73      A    O  
ANISOU 1089  OE1 GLN A 147     8987   9564   8701   -490   -792    761  A    O  
ATOM   1090  N   SER A 148     125.282  79.299  31.583  1.00 64.72      A    N  
ANISOU 1090  N   SER A 148     7788   8842   7958   -227   -642    552  A    N  
ATOM   1091  CA  SER A 148     126.764  79.338  31.571  1.00 64.50      A    C  
ANISOU 1091  CA  SER A 148     7699   8715   8092   -200   -745    536  A    C  
ATOM   1092  C   SER A 148     127.338  80.667  31.124  1.00 64.80      A    C  
ANISOU 1092  C   SER A 148     7700   8759   8163   -178   -706    491  A    C  
ATOM   1093  O   SER A 148     128.552  80.863  31.157  1.00 67.21      A    O  
ANISOU 1093  O   SER A 148     7937   9000   8597   -180   -786    479  A    O  
ATOM   1094  CB  SER A 148     127.307  78.241  30.669  1.00 64.22      A    C  
ANISOU 1094  CB  SER A 148     7557   8632   8213   -164   -730    524  A    C  
ATOM   1095  OG  SER A 148     127.013  78.523  29.308  1.00 66.43      A    O  
ANISOU 1095  OG  SER A 148     7760   8971   8508   -132   -584    480  A    O  
ATOM   1096  N   GLY A 149     126.468  81.576  30.706  1.00 65.75      A    N  
ANISOU 1096  N   GLY A 149     7861   8955   8165   -158   -585    469  A    N  
ATOM   1097  CA  GLY A 149     126.871  82.924  30.303  1.00 65.18      A    C  
ANISOU 1097  CA  GLY A 149     7803   8866   8094   -137   -538    431  A    C  
ATOM   1098  C   GLY A 149     127.298  83.014  28.869  1.00 64.10      A    C  
ANISOU 1098  C   GLY A 149     7555   8731   8067   -101   -438    403  A    C  
ATOM   1099  O   GLY A 149     127.400  84.108  28.335  1.00 65.73      A    O  
ANISOU 1099  O   GLY A 149     7791   8927   8252    -80   -366    379  A    O  
ATOM   1100  N   GLU A 150     127.562  81.871  28.255  1.00 64.57      A    N  
ANISOU 1100  N   GLU A 150     7510   8789   8234    -92   -428    407  A    N  
ATOM   1101  CA  GLU A 150     128.016  81.816  26.865  1.00 67.85      A    C  
ANISOU 1101  CA  GLU A 150     7829   9205   8746    -55   -322    382  A    C  
ATOM   1102  C   GLU A 150     127.173  82.650  25.911  1.00 63.06      A    C  
ANISOU 1102  C   GLU A 150     7264   8667   8028     -7   -189    368  A    C  
ATOM   1103  O   GLU A 150     125.953  82.602  25.974  1.00 63.86      A    O  
ANISOU 1103  O   GLU A 150     7409   8853   8000     15   -155    378  A    O  
ATOM   1104  CB  GLU A 150     127.943  80.369  26.401  1.00 72.77      A    C  
ANISOU 1104  CB  GLU A 150     8390   9829   9430    -37   -315    382  A    C  
ATOM   1105  CG  GLU A 150     128.333  80.128  24.953  1.00 73.94      A    C  
ANISOU 1105  CG  GLU A 150     8460   9981   9653      7   -197    350  A    C  
ATOM   1106  CD  GLU A 150     128.068  78.694  24.565  1.00 73.63      A    C  
ANISOU 1106  CD  GLU A 150     8408   9931   9637     26   -191    340  A    C  
ATOM   1107  OE1 GLU A 150     129.043  77.940  24.298  1.00 82.44      A    O  
ANISOU 1107  OE1 GLU A 150     9453  10979  10890     61   -195    325  A    O  
ATOM   1108  OE2 GLU A 150     126.888  78.325  24.571  1.00 63.73      A    O1-
ANISOU 1108  OE2 GLU A 150     7216   8734   8264      2   -184    346  A    O1-
ATOM   1109  N   PHE A 151     127.823  83.387  25.018  1.00 56.84      A    N  
ANISOU 1109  N   PHE A 151     6454   7846   7293      8   -112    351  A    N  
ATOM   1110  CA  PHE A 151     127.105  84.210  24.086  1.00 55.69      A    C  
ANISOU 1110  CA  PHE A 151     6366   7750   7041     70      5    346  A    C  
ATOM   1111  C   PHE A 151     128.000  84.408  22.900  1.00 60.65      A    C  
ANISOU 1111  C   PHE A 151     6947   8333   7762     74     95    336  A    C  
ATOM   1112  O   PHE A 151     128.895  85.239  22.902  1.00 64.32      A    O  
ANISOU 1112  O   PHE A 151     7427   8722   8289     31    104    335  A    O  
ATOM   1113  CB  PHE A 151     126.777  85.551  24.728  1.00 55.50      A    C  
ANISOU 1113  CB  PHE A 151     6471   7703   6912     83     -3    348  A    C  
ATOM   1114  CG  PHE A 151     125.874  86.463  23.910  1.00 53.54      A    C  
ANISOU 1114  CG  PHE A 151     6303   7507   6533    183    107    352  A    C  
ATOM   1115  CD1 PHE A 151     124.907  85.975  23.069  1.00 52.63      A    C  
ANISOU 1115  CD1 PHE A 151     6139   7506   6349    252    168    360  A    C  
ATOM   1116  CD2 PHE A 151     125.962  87.827  24.067  1.00 53.84      A    C  
ANISOU 1116  CD2 PHE A 151     6476   7472   6507    210    133    346  A    C  
ATOM   1117  CE1 PHE A 151     124.071  86.827  22.366  1.00 52.02      A    C  
ANISOU 1117  CE1 PHE A 151     6125   7488   6151    362    249    370  A    C  
ATOM   1118  CE2 PHE A 151     125.144  88.679  23.376  1.00 53.38      A    C  
ANISOU 1118  CE2 PHE A 151     6506   7448   6326    329    225    356  A    C  
ATOM   1119  CZ  PHE A 151     124.191  88.180  22.523  1.00 52.88      A    C  
ANISOU 1119  CZ  PHE A 151     6371   7518   6202    414    280    371  A    C  
ATOM   1120  N   LYS A 152     127.748  83.644  21.859  1.00 65.53      A    N  
ANISOU 1120  N   LYS A 152     7516   9000   8380    114    167    327  A    N  
ATOM   1121  CA  LYS A 152     128.552  83.724  20.681  1.00 66.59      A    C  
ANISOU 1121  CA  LYS A 152     7615   9102   8583    123    274    319  A    C  
ATOM   1122  C   LYS A 152     127.705  83.924  19.461  1.00 66.67      A    C  
ANISOU 1122  C   LYS A 152     7689   9179   8464    196    373    321  A    C  
ATOM   1123  O   LYS A 152     126.511  83.638  19.462  1.00 61.91      A    O  
ANISOU 1123  O   LYS A 152     7108   8666   7746    237    347    322  A    O  
ATOM   1124  CB  LYS A 152     129.351  82.464  20.553  1.00 70.42      A    C  
ANISOU 1124  CB  LYS A 152     7986   9564   9206    108    266    300  A    C  
ATOM   1125  CG  LYS A 152     130.614  82.551  21.361  1.00 80.63      A    C  
ANISOU 1125  CG  LYS A 152     9189  10789  10659     47    197    306  A    C  
ATOM   1126  CD  LYS A 152     131.210  81.187  21.585  1.00 88.71      A    C  
ANISOU 1126  CD  LYS A 152    10101  11794  11809     66    151    293  A    C  
ATOM   1127  CE  LYS A 152     132.269  81.295  22.649  1.00103.01      A    C  
ANISOU 1127  CE  LYS A 152    11816  13561  13762     13     33    309  A    C  
ATOM   1128  NZ  LYS A 152     132.236  80.075  23.495  1.00115.83      A    N1+
ANISOU 1128  NZ  LYS A 152    13410  15166  15433     45    -90    313  A    N1+
ATOM   1129  N   THR A 153     128.347  84.460  18.431  1.00 70.78      A    N  
ANISOU 1129  N   THR A 153     8232   9658   9000    206    484    327  A    N  
ATOM   1130  CA  THR A 153     127.737  84.633  17.139  1.00 70.92      A    C  
ANISOU 1130  CA  THR A 153     8322   9728   8894    279    577    333  A    C  
ATOM   1131  C   THR A 153     128.676  84.103  16.111  1.00 71.40      A    C  
ANISOU 1131  C   THR A 153     8342   9756   9027    266    686    318  A    C  
ATOM   1132  O   THR A 153     129.898  84.163  16.300  1.00 74.14      A    O  
ANISOU 1132  O   THR A 153     8618  10032   9518    203    721    318  A    O  
ATOM   1133  CB  THR A 153     127.475  86.105  16.816  1.00 74.89      A    C  
ANISOU 1133  CB  THR A 153     8957  10199   9296    325    628    369  A    C  
ATOM   1134  CG2 THR A 153     128.790  86.932  16.742  1.00 78.94      A    C  
ANISOU 1134  CG2 THR A 153     9496  10584   9910    245    694    385  A    C  
ATOM   1135  OG1 THR A 153     126.812  86.180  15.557  1.00 80.17      A    O  
ANISOU 1135  OG1 THR A 153     9695  10930   9832    413    697    383  A    O  
ATOM   1136  N   LYS A 154     128.115  83.615  15.007  1.00 73.53      A    N  
ANISOU 1136  N   LYS A 154     8658  10086   9191    326    742    306  A    N  
ATOM   1137  CA  LYS A 154     128.916  83.100  13.891  1.00 76.36      A    C  
ANISOU 1137  CA  LYS A 154     9012  10421   9580    330    870    287  A    C  
ATOM   1138  C   LYS A 154     128.312  83.422  12.525  1.00 73.11      A    C  
ANISOU 1138  C   LYS A 154     8731  10054   8990    400    950    301  A    C  
ATOM   1139  O   LYS A 154     127.112  83.485  12.372  1.00 71.66      A    O  
ANISOU 1139  O   LYS A 154     8602   9955   8668    453    878    308  A    O  
ATOM   1140  CB  LYS A 154     129.088  81.590  14.042  1.00 77.38      A    C  
ANISOU 1140  CB  LYS A 154     9058  10557   9784    325    839    232  A    C  
ATOM   1141  CG  LYS A 154     129.943  80.952  12.974  1.00 80.09      A    C  
ANISOU 1141  CG  LYS A 154     9398  10872  10159    349    983    201  A    C  
ATOM   1142  CD  LYS A 154     130.306  79.526  13.309  1.00 81.13      A    C  
ANISOU 1142  CD  LYS A 154     9455  10976  10394    361    954    145  A    C  
ATOM   1143  CE  LYS A 154     131.464  79.082  12.437  1.00 90.07      A    C  
ANISOU 1143  CE  LYS A 154    10552  12071  11597    397   1125    117  A    C  
ATOM   1144  NZ  LYS A 154     131.995  77.764  12.867  1.00 95.58      A    N1+
ANISOU 1144  NZ  LYS A 154    11169  12723  12423    436   1105     66  A    N1+
ATOM   1145  N   LEU A 155     129.165  83.636  11.537  1.00 74.69      A    N  
ANISOU 1145  N   LEU A 155     8975  10208   9193    398   1100    313  A    N  
ATOM   1146  CA  LEU A 155     128.706  83.738  10.165  1.00 76.62      A    C  
ANISOU 1146  CA  LEU A 155     9360  10490   9258    464   1177    324  A    C  
ATOM   1147  C   LEU A 155     128.904  82.393   9.489  1.00 77.63      A    C  
ANISOU 1147  C   LEU A 155     9476  10643   9377    476   1228    258  A    C  
ATOM   1148  O   LEU A 155     129.994  81.818   9.582  1.00 86.17      A    O  
ANISOU 1148  O   LEU A 155    10467  11671  10600    444   1315    230  A    O  
ATOM   1149  CB  LEU A 155     129.497  84.813   9.404  1.00 76.97      A    C  
ANISOU 1149  CB  LEU A 155     9504  10457   9280    450   1332    383  A    C  
ATOM   1150  CG  LEU A 155     128.702  85.417   8.235  1.00 73.92      A    C  
ANISOU 1150  CG  LEU A 155     9311  10105   8668    541   1361    426  A    C  
ATOM   1151  CD1 LEU A 155     127.560  86.203   8.815  1.00 73.01      A    C  
ANISOU 1151  CD1 LEU A 155     9236  10031   8473    607   1222    460  A    C  
ATOM   1152  CD2 LEU A 155     129.569  86.327   7.394  1.00 76.21      A    C  
ANISOU 1152  CD2 LEU A 155     9727  10302   8926    515   1534    490  A    C  
ATOM   1153  N   THR A 156     127.882  81.900   8.795  1.00 74.13      A    N  
ANISOU 1153  N   THR A 156     9122  10277   8765    526   1173    233  A    N  
ATOM   1154  CA  THR A 156     127.973  80.592   8.165  1.00 76.21      A    C  
ANISOU 1154  CA  THR A 156     9411  10549   8994    532   1205    158  A    C  
ATOM   1155  C   THR A 156     127.174  80.569   6.874  1.00 79.28      A    C  
ANISOU 1155  C   THR A 156     9965  11007   9149    585   1206    153  A    C  
ATOM   1156  O   THR A 156     126.661  81.577   6.453  1.00 83.36      A    O  
ANISOU 1156  O   THR A 156    10562  11565   9543    629   1192    217  A    O  
ATOM   1157  CB  THR A 156     127.506  79.476   9.132  1.00 77.45      A    C  
ANISOU 1157  CB  THR A 156     9475  10717   9232    493   1064    101  A    C  
ATOM   1158  CG2 THR A 156     125.999  79.508   9.324  1.00 76.53      A    C  
ANISOU 1158  CG2 THR A 156     9378  10712   8986    486    899    109  A    C  
ATOM   1159  OG1 THR A 156     127.917  78.188   8.657  1.00 78.16      A    O  
ANISOU 1159  OG1 THR A 156     9600  10764   9332    500   1119     22  A    O  
ATOM   1160  N   THR A 157     127.107  79.410   6.232  1.00 86.90      A    N  
ANISOU 1160  N   THR A 157    10996  11976  10043    587   1219     75  A    N  
ATOM   1161  CA  THR A 157     126.438  79.257   4.950  1.00 86.82      A    C  
ANISOU 1161  CA  THR A 157    11159  12031   9798    626   1211     59  A    C  
ATOM   1162  C   THR A 157     125.219  78.407   5.163  1.00 89.97      A    C  
ANISOU 1162  C   THR A 157    11548  12514  10121    585   1019      5  A    C  
ATOM   1163  O   THR A 157     125.014  77.824   6.231  1.00 98.62      A    O  
ANISOU 1163  O   THR A 157    12524  13598  11346    526    925    -22  A    O  
ATOM   1164  CB  THR A 157     127.326  78.541   3.902  1.00 89.22      A    C  
ANISOU 1164  CB  THR A 157    11586  12268  10045    650   1390     -2  A    C  
ATOM   1165  CG2 THR A 157     128.781  79.046   3.931  1.00 93.16      A    C  
ANISOU 1165  CG2 THR A 157    12026  12679  10689    657   1606     36  A    C  
ATOM   1166  OG1 THR A 157     127.334  77.138   4.162  1.00 87.05      A    O  
ANISOU 1166  OG1 THR A 157    11298  11956   9819    622   1350   -103  A    O  
ATOM   1167  N   ALA A 158     124.418  78.309   4.123  1.00 92.47      A    N  
ANISOU 1167  N   ALA A 158    11999  12916  10219    606    958     -8  A    N  
ATOM   1168  CA  ALA A 158     123.187  77.564   4.200  1.00 93.73      A    C  
ANISOU 1168  CA  ALA A 158    12146  13177  10288    545    765    -56  A    C  
ATOM   1169  C   ALA A 158     123.392  76.050   4.356  1.00 92.42      A    C  
ANISOU 1169  C   ALA A 158    12017  12927  10170    464    752   -168  A    C  
ATOM   1170  O   ALA A 158     122.744  75.430   5.170  1.00100.76      A    O  
ANISOU 1170  O   ALA A 158    12987  14007  11289    378    618   -194  A    O  
ATOM   1171  CB  ALA A 158     122.354  77.866   2.974  1.00 99.79      A    C  
ANISOU 1171  CB  ALA A 158    13051  14061  10803    588    690    -40  A    C  
ATOM   1172  N   ASP A 159     124.275  75.444   3.585  1.00 94.74      A    N  
ANISOU 1172  N   ASP A 159    12452  13116  10426    498    899   -233  A    N  
ATOM   1173  CA  ASP A 159     124.431  73.999   3.657  1.00100.10      A    C  
ANISOU 1173  CA  ASP A 159    13205  13698  11127    446    888   -347  A    C  
ATOM   1174  C   ASP A 159     125.295  73.597   4.846  1.00100.64      A    C  
ANISOU 1174  C   ASP A 159    13137  13649  11453    446    948   -353  A    C  
ATOM   1175  O   ASP A 159     125.166  72.493   5.366  1.00103.34      A    O  
ANISOU 1175  O   ASP A 159    13494  13913  11855    391    880   -420  A    O  
ATOM   1176  CB  ASP A 159     124.975  73.421   2.341  1.00110.92      A    C  
ANISOU 1176  CB  ASP A 159    14804  15003  12336    499   1026   -428  A    C  
ATOM   1177  CG  ASP A 159     126.271  74.067   1.903  1.00119.31      A    C  
ANISOU 1177  CG  ASP A 159    15874  16008  13448    603   1275   -387  A    C  
ATOM   1178  OD1 ASP A 159     126.919  74.732   2.748  1.00134.45      A    O  
ANISOU 1178  OD1 ASP A 159    17610  17905  15570    620   1340   -315  A    O  
ATOM   1179  OD2 ASP A 159     126.640  73.902   0.710  1.00119.08      A    O1-
ANISOU 1179  OD2 ASP A 159    16039  15958  13248    656   1406   -427  A    O1-
ATOM   1180  N   LYS A 160     126.154  74.505   5.305  1.00102.34      A    N  
ANISOU 1180  N   LYS A 160    13221  13845  11816    502   1061   -277  A    N  
ATOM   1181  CA  LYS A 160     126.957  74.248   6.507  1.00103.55      A    C  
ANISOU 1181  CA  LYS A 160    13221  13909  12215    503   1088   -268  A    C  
ATOM   1182  C   LYS A 160     126.152  74.498   7.786  1.00 94.65      A    C  
ANISOU 1182  C   LYS A 160    11956  12833  11172    426    908   -218  A    C  
ATOM   1183  O   LYS A 160     126.705  74.586   8.871  1.00 98.81      A    O  
ANISOU 1183  O   LYS A 160    12350  13309  11884    423    903   -186  A    O  
ATOM   1184  CB  LYS A 160     128.228  75.116   6.516  1.00112.51      A    C  
ANISOU 1184  CB  LYS A 160    14259  15011  13477    567   1269   -210  A    C  
ATOM   1185  CG  LYS A 160     129.392  74.569   5.694  1.00119.45      A    C  
ANISOU 1185  CG  LYS A 160    15203  15811  14370    645   1485   -266  A    C  
ATOM   1186  CD  LYS A 160     130.570  75.536   5.653  1.00120.15      A    C  
ANISOU 1186  CD  LYS A 160    15176  15895  14578    676   1664   -195  A    C  
ATOM   1187  CE  LYS A 160     131.615  75.066   4.650  1.00126.18      A    C  
ANISOU 1187  CE  LYS A 160    16011  16615  15317    754   1906   -244  A    C  
ATOM   1188  NZ  LYS A 160     132.209  73.754   5.053  1.00125.93      A    N1+
ANISOU 1188  NZ  LYS A 160    15933  16495  15416    820   1940   -333  A    N1+
ATOM   1189  N   LEU A 161     124.839  74.583   7.668  1.00 86.99      A    N  
ANISOU 1189  N   LEU A 161    11015  11975  10062    363    758   -209  A    N  
ATOM   1190  CA  LEU A 161     124.014  74.968   8.787  1.00 78.69      A    C  
ANISOU 1190  CA  LEU A 161     9830  10999   9066    300    616   -152  A    C  
ATOM   1191  C   LEU A 161     123.766  73.815   9.729  1.00 78.32      A    C  
ANISOU 1191  C   LEU A 161     9763  10886   9109    209    517   -192  A    C  
ATOM   1192  O   LEU A 161     124.062  73.930  10.896  1.00 79.51      A    O  
ANISOU 1192  O   LEU A 161     9807  10994   9407    197    493   -153  A    O  
ATOM   1193  CB  LEU A 161     122.701  75.545   8.292  1.00 75.60      A    C  
ANISOU 1193  CB  LEU A 161     9446  10780   8499    279    505   -117  A    C  
ATOM   1194  CG  LEU A 161     121.658  75.842   9.350  1.00 75.19      A    C  
ANISOU 1194  CG  LEU A 161     9255  10838   8477    213    365    -66  A    C  
ATOM   1195  CD1 LEU A 161     122.202  76.821  10.376  1.00 76.52      A    C  
ANISOU 1195  CD1 LEU A 161     9312  10976   8787    263    414      5  A    C  
ATOM   1196  CD2 LEU A 161     120.409  76.398   8.700  1.00 75.18      A    C  
ANISOU 1196  CD2 LEU A 161     9239  11026   8300    221    267    -34  A    C  
ATOM   1197  N   ASN A 162     123.241  72.700   9.232  1.00 85.73      A    N  
ANISOU 1197  N   ASN A 162    10827  11798   9946    139    455   -271  A    N  
ATOM   1198  CA  ASN A 162     122.859  71.569  10.110  1.00 87.09      A    C  
ANISOU 1198  CA  ASN A 162    11014  11892  10181     30    348   -304  A    C  
ATOM   1199  C   ASN A 162     124.042  70.971  10.829  1.00 87.03      A    C  
ANISOU 1199  C   ASN A 162    11004  11705  10357     92    423   -321  A    C  
ATOM   1200  O   ASN A 162     123.861  70.319  11.839  1.00 87.32      A    O  
ANISOU 1200  O   ASN A 162    11029  11670  10478     24    338   -314  A    O  
ATOM   1201  CB  ASN A 162     122.118  70.468   9.352  1.00 90.75      A    C  
ANISOU 1201  CB  ASN A 162    11648  12339  10494    -73    268   -395  A    C  
ATOM   1202  CG  ASN A 162     120.718  70.904   8.911  1.00 99.73      A    C  
ANISOU 1202  CG  ASN A 162    12744  13681  11466   -172    134   -370  A    C  
ATOM   1203  ND2 ASN A 162     120.397  70.646   7.643  1.00101.01      A    N  
ANISOU 1203  ND2 ASN A 162    13048  13882  11447   -183    116   -435  A    N  
ATOM   1204  OD1 ASN A 162     119.934  71.471   9.700  1.00101.56      A    O  
ANISOU 1204  OD1 ASN A 162    12815  14044  11727   -231     48   -294  A    O  
ATOM   1205  N   ASP A 163     125.254  71.204  10.320  1.00 88.86      A    N  
ANISOU 1205  N   ASP A 163    11240  11871  10650    224    582   -336  A    N  
ATOM   1206  CA  ASP A 163     126.467  70.850  11.052  1.00 85.06      A    C  
ANISOU 1206  CA  ASP A 163    10693  11258  10366    306    653   -334  A    C  
ATOM   1207  C   ASP A 163     126.608  71.720  12.264  1.00 79.42      A    C  
ANISOU 1207  C   ASP A 163     9799  10589   9787    293    599   -239  A    C  
ATOM   1208  O   ASP A 163     126.929  71.240  13.343  1.00 75.28      A    O  
ANISOU 1208  O   ASP A 163     9227   9980   9394    289    538   -221  A    O  
ATOM   1209  CB  ASP A 163     127.708  71.015  10.191  1.00 88.97      A    C  
ANISOU 1209  CB  ASP A 163    11194  11710  10899    441    851   -362  A    C  
ATOM   1210  CG  ASP A 163     127.919  69.859   9.273  1.00 95.76      A    C  
ANISOU 1210  CG  ASP A 163    12246  12465  11672    491    928   -473  A    C  
ATOM   1211  OD1 ASP A 163     127.249  68.812   9.491  1.00 90.41      A    O  
ANISOU 1211  OD1 ASP A 163    11698  11709  10943    420    815   -528  A    O  
ATOM   1212  OD2 ASP A 163     128.760  70.006   8.346  1.00111.14      A    O1-
ANISOU 1212  OD2 ASP A 163    14226  14404  13596    595   1110   -502  A    O1-
ATOM   1213  N   GLU A 164     126.374  73.011  12.091  1.00 79.17      A    N  
ANISOU 1213  N   GLU A 164     9690  10681   9709    293    617   -177  A    N  
ATOM   1214  CA  GLU A 164     126.491  73.923  13.214  1.00 79.69      A    C  
ANISOU 1214  CA  GLU A 164     9614  10783   9880    278    567    -96  A    C  
ATOM   1215  C   GLU A 164     125.375  73.665  14.232  1.00 74.80      A    C  
ANISOU 1215  C   GLU A 164     8981  10206   9233    174    409    -68  A    C  
ATOM   1216  O   GLU A 164     125.593  73.718  15.431  1.00 80.21      A    O  
ANISOU 1216  O   GLU A 164     9594  10854  10026    155    347    -26  A    O  
ATOM   1217  CB  GLU A 164     126.524  75.373  12.746  1.00 79.64      A    C  
ANISOU 1217  CB  GLU A 164     9565  10871   9822    311    634    -42  A    C  
ATOM   1218  CG  GLU A 164     127.645  75.675  11.754  1.00 89.83      A    C  
ANISOU 1218  CG  GLU A 164    10872  12122  11135    390    808    -57  A    C  
ATOM   1219  CD  GLU A 164     129.057  75.498  12.316  1.00 99.11      A    C  
ANISOU 1219  CD  GLU A 164    11936  13203  12517    432    883    -55  A    C  
ATOM   1220  OE1 GLU A 164     129.618  74.372  12.264  1.00102.06      A    O  
ANISOU 1220  OE1 GLU A 164    12324  13490  12961    478    917   -112  A    O  
ATOM   1221  OE2 GLU A 164     129.630  76.507  12.788  1.00107.37      A    O1-
ANISOU 1221  OE2 GLU A 164    12879  14260  13655    424    904      4  A    O1-
ATOM   1222  N   LEU A 165     124.193  73.334  13.762  1.00 72.50      A    N  
ANISOU 1222  N   LEU A 165     8757   9995   8793     98    341    -90  A    N  
ATOM   1223  CA  LEU A 165     123.116  73.048  14.667  1.00 72.73      A    C  
ANISOU 1223  CA  LEU A 165     8760  10079   8792    -19    211    -61  A    C  
ATOM   1224  C   LEU A 165     123.367  71.809  15.516  1.00 76.05      A    C  
ANISOU 1224  C   LEU A 165     9239  10351   9305    -74    153    -81  A    C  
ATOM   1225  O   LEU A 165     123.034  71.777  16.724  1.00 76.48      A    O  
ANISOU 1225  O   LEU A 165     9249  10404   9405   -140     73    -27  A    O  
ATOM   1226  CB  LEU A 165     121.823  72.911  13.901  1.00 74.93      A    C  
ANISOU 1226  CB  LEU A 165     9076  10492   8899   -103    147    -82  A    C  
ATOM   1227  CG  LEU A 165     120.914  74.116  14.110  1.00 81.22      A    C  
ANISOU 1227  CG  LEU A 165     9752  11479   9625   -101    112    -11  A    C  
ATOM   1228  CD1 LEU A 165     121.621  75.480  14.061  1.00 83.58      A    C  
ANISOU 1228  CD1 LEU A 165     9997  11790   9966     33    204     38  A    C  
ATOM   1229  CD2 LEU A 165     119.824  74.038  13.064  1.00 86.46      A    C  
ANISOU 1229  CD2 LEU A 165    10437  12290  10121   -147     56    -35  A    C  
ATOM   1230  N   ALA A 166     123.962  70.788  14.914  1.00 74.02      A    N  
ANISOU 1230  N   ALA A 166     9102   9957   9066    -38    197   -155  A    N  
ATOM   1231  CA  ALA A 166     124.272  69.600  15.675  1.00 72.19      A    C  
ANISOU 1231  CA  ALA A 166     8952   9554   8920    -60    146   -172  A    C  
ATOM   1232  C   ALA A 166     125.425  69.904  16.612  1.00 73.14      A    C  
ANISOU 1232  C   ALA A 166     8970   9602   9217     46    169   -123  A    C  
ATOM   1233  O   ALA A 166     125.528  69.340  17.687  1.00 79.96      A    O  
ANISOU 1233  O   ALA A 166     9853  10369  10158     22     88    -90  A    O  
ATOM   1234  CB  ALA A 166     124.614  68.445  14.771  1.00 70.52      A    C  
ANISOU 1234  CB  ALA A 166     8914   9204   8674    -24    195   -273  A    C  
ATOM   1235  N   ARG A 167     126.306  70.804  16.236  1.00 71.85      A    N  
ANISOU 1235  N   ARG A 167     8700   9480   9117    154    269   -111  A    N  
ATOM   1236  CA  ARG A 167     127.415  71.065  17.113  1.00 72.53      A    C  
ANISOU 1236  CA  ARG A 167     8674   9507   9374    234    272    -68  A    C  
ATOM   1237  C   ARG A 167     126.893  71.731  18.348  1.00 70.47      A    C  
ANISOU 1237  C   ARG A 167     8345   9311   9118    155    160     11  A    C  
ATOM   1238  O   ARG A 167     127.319  71.396  19.450  1.00 76.65      A    O  
ANISOU 1238  O   ARG A 167     9108  10014  10000    164     81     49  A    O  
ATOM   1239  CB  ARG A 167     128.491  71.934  16.447  1.00 73.29      A    C  
ANISOU 1239  CB  ARG A 167     8660   9644   9542    335    408    -70  A    C  
ATOM   1240  CG  ARG A 167     129.575  72.388  17.424  1.00 74.76      A    C  
ANISOU 1240  CG  ARG A 167     8695   9804   9905    385    386    -17  A    C  
ATOM   1241  CD  ARG A 167     130.547  73.287  16.746  1.00 75.67      A    C  
ANISOU 1241  CD  ARG A 167     8697   9966  10085    443    523    -12  A    C  
ATOM   1242  NE  ARG A 167     129.859  74.435  16.189  1.00 76.80      A    N  
ANISOU 1242  NE  ARG A 167     8864  10219  10096    383    559     10  A    N  
ATOM   1243  CZ  ARG A 167     130.006  75.680  16.633  1.00 82.31      A    C  
ANISOU 1243  CZ  ARG A 167     9484  10971  10819    348    544     67  A    C  
ATOM   1244  NH1 ARG A 167     130.833  75.961  17.646  1.00 79.01      A    N1+
ANISOU 1244  NH1 ARG A 167     8949  10520  10549    344    484    104  A    N1+
ATOM   1245  NH2 ARG A 167     129.326  76.657  16.038  1.00 84.95      A    N  
ANISOU 1245  NH2 ARG A 167     9868  11387  11019    320    582     85  A    N  
ATOM   1246  N   LEU A 168     126.001  72.693  18.171  1.00 69.38      A    N  
ANISOU 1246  N   LEU A 168     8177   9317   8867     92    156     39  A    N  
ATOM   1247  CA  LEU A 168     125.539  73.487  19.294  1.00 72.16      A    C  
ANISOU 1247  CA  LEU A 168     8466   9738   9210     38     79    110  A    C  
ATOM   1248  C   LEU A 168     124.528  72.741  20.185  1.00 76.49      A    C  
ANISOU 1248  C   LEU A 168     9081  10282   9700    -80    -31    137  A    C  
ATOM   1249  O   LEU A 168     124.343  73.143  21.346  1.00 84.77      A    O  
ANISOU 1249  O   LEU A 168    10099  11351  10755   -117    -95    197  A    O  
ATOM   1250  CB  LEU A 168     124.947  74.795  18.814  1.00 68.78      A    C  
ANISOU 1250  CB  LEU A 168     7991   9458   8683     40    124    132  A    C  
ATOM   1251  CG  LEU A 168     125.906  75.590  17.970  1.00 69.15      A    C  
ANISOU 1251  CG  LEU A 168     7998   9500   8775    131    236    118  A    C  
ATOM   1252  CD1 LEU A 168     125.211  76.832  17.408  1.00 70.06      A    C  
ANISOU 1252  CD1 LEU A 168     8108   9742   8770    145    276    143  A    C  
ATOM   1253  CD2 LEU A 168     127.120  75.950  18.806  1.00 70.18      A    C  
ANISOU 1253  CD2 LEU A 168     8049   9552   9063    165    227    146  A    C  
ATOM   1254  N   GLN A 169     123.899  71.677  19.668  1.00 71.36      A    N  
ANISOU 1254  N   GLN A 169     8530   9598   8981   -148    -47     93  A    N  
ATOM   1255  CA  GLN A 169     123.011  70.834  20.464  1.00 72.33      A    C  
ANISOU 1255  CA  GLN A 169     8732   9693   9055   -286   -141    119  A    C  
ATOM   1256  C   GLN A 169     121.881  71.694  21.034  1.00 69.38      A    C  
ANISOU 1256  C   GLN A 169     8276   9498   8584   -376   -169    181  A    C  
ATOM   1257  O   GLN A 169     121.436  71.510  22.165  1.00 72.64      A    O  
ANISOU 1257  O   GLN A 169     8706   9907   8984   -462   -231    239  A    O  
ATOM   1258  CB  GLN A 169     123.768  70.162  21.624  1.00 79.11      A    C  
ANISOU 1258  CB  GLN A 169     9645  10383  10027   -260   -207    156  A    C  
ATOM   1259  CG  GLN A 169     124.816  69.128  21.257  1.00 88.22      A    C  
ANISOU 1259  CG  GLN A 169    10885  11349  11284   -154   -189    102  A    C  
ATOM   1260  CD  GLN A 169     125.855  68.883  22.381  1.00101.07      A    C  
ANISOU 1260  CD  GLN A 169    12501  12848  13052    -62   -253    152  A    C  
ATOM   1261  NE2 GLN A 169     125.647  67.797  23.126  1.00107.41      A    N  
ANISOU 1261  NE2 GLN A 169    13448  13506  13855   -110   -340    177  A    N  
ATOM   1262  OE1 GLN A 169     126.842  69.648  22.565  1.00100.62      A    O  
ANISOU 1262  OE1 GLN A 169    12312  12819  13098     47   -232    169  A    O  
ATOM   1263  N   ALA A 170     121.413  72.656  20.264  1.00 65.33      A    N  
ANISOU 1263  N   ALA A 170     7680   9145   7995   -345   -117    173  A    N  
ATOM   1264  CA  ALA A 170     120.496  73.657  20.811  1.00 62.04      A    C  
ANISOU 1264  CA  ALA A 170     7169   8901   7501   -374   -122    231  A    C  
ATOM   1265  C   ALA A 170     119.251  73.037  21.342  1.00 58.80      A    C  
ANISOU 1265  C   ALA A 170     6763   8570   7007   -538   -179    261  A    C  
ATOM   1266  O   ALA A 170     118.730  72.095  20.776  1.00 56.04      A    O  
ANISOU 1266  O   ALA A 170     6466   8212   6614   -644   -211    226  A    O  
ATOM   1267  CB  ALA A 170     120.131  74.685  19.750  1.00 65.05      A    C  
ANISOU 1267  CB  ALA A 170     7478   9432   7804   -295    -64    218  A    C  
ATOM   1268  N   ALA A 171     118.763  73.597  22.433  1.00 59.79      A    N  
ANISOU 1268  N   ALA A 171     6837   8777   7102   -567   -186    326  A    N  
ATOM   1269  CA  ALA A 171     117.492  73.157  23.022  1.00 59.53      A    C  
ANISOU 1269  CA  ALA A 171     6779   8855   6982   -735   -216    370  A    C  
ATOM   1270  C   ALA A 171     116.328  73.917  22.424  1.00 58.06      A    C  
ANISOU 1270  C   ALA A 171     6445   8921   6691   -735   -183    377  A    C  
ATOM   1271  O   ALA A 171     115.191  73.541  22.575  1.00 57.32      A    O  
ANISOU 1271  O   ALA A 171     6288   8964   6526   -881   -200    404  A    O  
ATOM   1272  CB  ALA A 171     117.530  73.354  24.522  1.00 60.10      A    C  
ANISOU 1272  CB  ALA A 171     6880   8897   7055   -760   -225    441  A    C  
ATOM   1273  N   GLU A 172     116.633  75.001  21.739  1.00 59.45      A    N  
ANISOU 1273  N   GLU A 172     6565   9160   6862   -571   -135    360  A    N  
ATOM   1274  CA  GLU A 172     115.621  75.858  21.181  1.00 63.07      A    C  
ANISOU 1274  CA  GLU A 172     6887   9850   7224   -520   -107    374  A    C  
ATOM   1275  C   GLU A 172     116.238  76.749  20.097  1.00 64.83      A    C  
ANISOU 1275  C   GLU A 172     7118  10063   7450   -342    -66    342  A    C  
ATOM   1276  O   GLU A 172     117.379  77.211  20.227  1.00 66.78      A    O  
ANISOU 1276  O   GLU A 172     7439  10162   7772   -239    -30    332  A    O  
ATOM   1277  CB  GLU A 172     114.994  76.715  22.282  1.00 64.76      A    C  
ANISOU 1277  CB  GLU A 172     7021  10192   7391   -490    -62    437  A    C  
ATOM   1278  CG  GLU A 172     113.713  77.412  21.847  1.00 68.51      A    C  
ANISOU 1278  CG  GLU A 172     7326  10938   7765   -448    -35    462  A    C  
ATOM   1279  CD  GLU A 172     113.171  78.372  22.878  1.00 69.53      A    C  
ANISOU 1279  CD  GLU A 172     7388  11188   7842   -372     38    516  A    C  
ATOM   1280  OE1 GLU A 172     113.534  78.223  24.059  1.00 71.46      A    O  
ANISOU 1280  OE1 GLU A 172     7718  11325   8107   -423     52    541  A    O  
ATOM   1281  OE2 GLU A 172     112.381  79.264  22.500  1.00 69.11      A    O1-
ANISOU 1281  OE2 GLU A 172     7208  11332   7718   -251     79    534  A    O1-
ATOM   1282  N   ILE A 173     115.472  76.996  19.035  1.00 65.15      A    N  
ANISOU 1282  N   ILE A 173     7082  10267   7404   -312    -77    331  A    N  
ATOM   1283  CA  ILE A 173     115.942  77.759  17.903  1.00 64.13      A    C  
ANISOU 1283  CA  ILE A 173     6983  10130   7251   -155    -42    308  A    C  
ATOM   1284  C   ILE A 173     115.016  78.934  17.656  1.00 64.12      A    C  
ANISOU 1284  C   ILE A 173     6867  10339   7154    -28    -23    352  A    C  
ATOM   1285  O   ILE A 173     113.805  78.787  17.699  1.00 65.21      A    O  
ANISOU 1285  O   ILE A 173     6871  10681   7224    -88    -63    375  A    O  
ATOM   1286  CB  ILE A 173     115.966  76.867  16.665  1.00 67.37      A    C  
ANISOU 1286  CB  ILE A 173     7451  10520   7624   -217    -88    249  A    C  
ATOM   1287  CG1 ILE A 173     116.958  75.720  16.866  1.00 68.30      A    C  
ANISOU 1287  CG1 ILE A 173     7700  10411   7839   -303    -91    199  A    C  
ATOM   1288  CG2 ILE A 173     116.328  77.669  15.423  1.00 70.20      A    C  
ANISOU 1288  CG2 ILE A 173     7852  10893   7926    -59    -48    237  A    C  
ATOM   1289  CD1 ILE A 173     116.639  74.511  16.009  1.00 72.09      A    C  
ANISOU 1289  CD1 ILE A 173     8250  10873   8266   -426   -155    136  A    C  
ATOM   1290  N   LEU A 174     115.584  80.107  17.410  1.00 64.85      A    N  
ANISOU 1290  N   LEU A 174     7010  10381   7245    148     41    366  A    N  
ATOM   1291  CA  LEU A 174     114.786  81.264  17.060  1.00 67.00      A    C  
ANISOU 1291  CA  LEU A 174     7208  10824   7422    309     61    407  A    C  
ATOM   1292  C   LEU A 174     114.925  81.525  15.569  1.00 71.06      A    C  
ANISOU 1292  C   LEU A 174     7777  11350   7870    405     51    393  A    C  
ATOM   1293  O   LEU A 174     116.023  81.812  15.081  1.00 72.50      A    O  
ANISOU 1293  O   LEU A 174     8097  11360   8087    462    103    375  A    O  
ATOM   1294  CB  LEU A 174     115.232  82.487  17.844  1.00 65.69      A    C  
ANISOU 1294  CB  LEU A 174     7101  10580   7278    445    140    436  A    C  
ATOM   1295  CG  LEU A 174     115.111  82.373  19.372  1.00 64.85      A    C  
ANISOU 1295  CG  LEU A 174     6971  10459   7210    369    155    452  A    C  
ATOM   1296  CD1 LEU A 174     115.505  83.695  20.010  1.00 67.47      A    C  
ANISOU 1296  CD1 LEU A 174     7388  10713   7533    517    225    470  A    C  
ATOM   1297  CD2 LEU A 174     113.731  81.992  19.836  1.00 63.39      A    C  
ANISOU 1297  CD2 LEU A 174     6620  10503   6962    298    135    482  A    C  
ATOM   1298  N   LEU A 175     113.800  81.443  14.863  1.00 74.34      A    N  
ANISOU 1298  N   LEU A 175     8079  11982   8184    420    -19    406  A    N  
ATOM   1299  CA  LEU A 175     113.725  81.720  13.431  1.00 76.17      A    C  
ANISOU 1299  CA  LEU A 175     8361  12262   8317    521    -52    404  A    C  
ATOM   1300  C   LEU A 175     112.874  82.945  13.066  1.00 75.78      A    C  
ANISOU 1300  C   LEU A 175     8233  12391   8167    735    -57    467  A    C  
ATOM   1301  O   LEU A 175     111.928  83.283  13.768  1.00 77.92      A    O  
ANISOU 1301  O   LEU A 175     8342  12836   8426    773    -63    504  A    O  
ATOM   1302  CB  LEU A 175     113.091  80.534  12.750  1.00 81.38      A    C  
ANISOU 1302  CB  LEU A 175     8965  13033   8922    360   -165    364  A    C  
ATOM   1303  CG  LEU A 175     114.046  79.473  12.250  1.00 85.97      A    C  
ANISOU 1303  CG  LEU A 175     9707  13418   9537    235   -164    291  A    C  
ATOM   1304  CD1 LEU A 175     113.254  78.286  11.738  1.00 88.18      A    C  
ANISOU 1304  CD1 LEU A 175     9941  13809   9751     54   -289    246  A    C  
ATOM   1305  CD2 LEU A 175     114.891  80.049  11.126  1.00 89.38      A    C  
ANISOU 1305  CD2 LEU A 175    10304  13740   9916    378   -106    286  A    C  
ATOM   1306  N   PRO A 176     113.195  83.609  11.948  1.00 74.20      A    N  
ANISOU 1306  N   PRO A 176     8155  12148   7886    886    -49    483  A    N  
ATOM   1307  CA  PRO A 176     112.322  84.689  11.522  1.00 75.95      A    C  
ANISOU 1307  CA  PRO A 176     8311  12541   8002   1107    -73    548  A    C  
ATOM   1308  C   PRO A 176     111.007  84.138  11.044  1.00 82.73      A    C  
ANISOU 1308  C   PRO A 176     8965  13689   8778   1063   -210    556  A    C  
ATOM   1309  O   PRO A 176     110.951  82.988  10.615  1.00 83.24      A    O  
ANISOU 1309  O   PRO A 176     9015  13776   8834    871   -293    505  A    O  
ATOM   1310  CB  PRO A 176     113.092  85.332  10.370  1.00 74.29      A    C  
ANISOU 1310  CB  PRO A 176     8319  12187   7720   1241    -38    564  A    C  
ATOM   1311  CG  PRO A 176     114.517  85.004  10.661  1.00 73.76      A    C  
ANISOU 1311  CG  PRO A 176     8413  11849   7761   1123     61    518  A    C  
ATOM   1312  CD  PRO A 176     114.473  83.624  11.226  1.00 72.79      A    C  
ANISOU 1312  CD  PRO A 176     8191  11743   7720    893     15    457  A    C  
ATOM   1313  N   ASP A 177     109.956  84.952  11.124  1.00 92.82      A    N  
ANISOU 1313  N   ASP A 177    10084  15186   9998   1243   -236    617  A    N  
ATOM   1314  CA  ASP A 177     108.639  84.555  10.616  1.00 96.86      A    C  
ANISOU 1314  CA  ASP A 177    10358  16014  10430   1221   -380    636  A    C  
ATOM   1315  C   ASP A 177     108.568  84.638   9.104  1.00 97.46      A    C  
ANISOU 1315  C   ASP A 177    10523  16134  10370   1310   -493    646  A    C  
ATOM   1316  O   ASP A 177     107.640  84.116   8.500  1.00102.54      A    O  
ANISOU 1316  O   ASP A 177    11003  17017  10940   1245   -645    647  A    O  
ATOM   1317  CB  ASP A 177     107.522  85.422  11.204  1.00101.24      A    C  
ANISOU 1317  CB  ASP A 177    10682  16814  10971   1410   -363    703  A    C  
ATOM   1318  CG  ASP A 177     106.141  84.735  11.122  1.00103.35      A    C  
ANISOU 1318  CG  ASP A 177    10622  17434  11210   1291   -496    715  A    C  
ATOM   1319  OD1 ASP A 177     106.090  83.486  11.078  1.00100.61      A    O  
ANISOU 1319  OD1 ASP A 177    10234  17102  10889    999   -574    662  A    O  
ATOM   1320  OD2 ASP A 177     105.103  85.432  11.111  1.00106.97      A    O1-
ANISOU 1320  OD2 ASP A 177    10862  18157  11623   1486   -522    777  A    O1-
ATOM   1321  N   SER A 178     109.554  85.298   8.504  1.00 97.85      A    N  
ANISOU 1321  N   SER A 178    10837  15958  10382   1448   -420    657  A    N  
ATOM   1322  CA  SER A 178     109.666  85.428   7.055  1.00103.24      A    C  
ANISOU 1322  CA  SER A 178    11668  16639  10919   1539   -502    673  A    C  
ATOM   1323  C   SER A 178     109.458  84.114   6.264  1.00103.88      A    C  
ANISOU 1323  C   SER A 178    11734  16801  10934   1314   -643    607  A    C  
ATOM   1324  O   SER A 178     109.718  83.017   6.759  1.00 99.63      A    O  
ANISOU 1324  O   SER A 178    11174  16197  10481   1064   -636    534  A    O  
ATOM   1325  CB  SER A 178     111.032  86.024   6.706  1.00105.93      A    C  
ANISOU 1325  CB  SER A 178    12322  16667  11260   1617   -363    677  A    C  
ATOM   1326  OG  SER A 178     111.195  86.097   5.306  1.00113.97      A    O  
ANISOU 1326  OG  SER A 178    13511  17670  12122   1689   -424    697  A    O  
ATOM   1327  N   LYS A 179     108.991  84.257   5.023  1.00112.73      A    N  
ANISOU 1327  N   LYS A 179    12892  18051  11889   1412   -777    636  A    N  
ATOM   1328  CA  LYS A 179     108.733  83.121   4.114  1.00113.72      A    C  
ANISOU 1328  CA  LYS A 179    13038  18259  11910   1219   -933    572  A    C  
ATOM   1329  C   LYS A 179     110.035  82.485   3.572  1.00111.79      A    C  
ANISOU 1329  C   LYS A 179    13103  17724  11646   1100   -840    498  A    C  
ATOM   1330  O   LYS A 179     110.016  81.371   3.021  1.00101.34      A    O  
ANISOU 1330  O   LYS A 179    11840  16404  10258    905   -932    418  A    O  
ATOM   1331  CB  LYS A 179     107.834  83.572   2.964  1.00116.26      A    C  
ANISOU 1331  CB  LYS A 179    13313  18815  12043   1385  -1117    633  A    C  
ATOM   1332  N   ASN A 180     111.151  83.203   3.738  1.00110.29      A    N  
ANISOU 1332  N   ASN A 180    13106  17286  11511   1217   -654    521  A    N  
ATOM   1333  CA  ASN A 180     112.476  82.691   3.409  1.00109.41      A    C  
ANISOU 1333  CA  ASN A 180    13248  16905  11419   1119   -524    459  A    C  
ATOM   1334  C   ASN A 180     113.235  82.185   4.647  1.00114.96      A    C  
ANISOU 1334  C   ASN A 180    13912  17436  12331    969   -393    406  A    C  
ATOM   1335  O   ASN A 180     114.473  82.234   4.706  1.00120.10      A    O  
ANISOU 1335  O   ASN A 180    14730  17851  13051    962   -236    386  A    O  
ATOM   1336  CB  ASN A 180     113.297  83.751   2.667  1.00106.55      A    C  
ANISOU 1336  CB  ASN A 180    13127  16383  10973   1314   -405    523  A    C  
ATOM   1337  CG  ASN A 180     113.482  85.020   3.468  1.00106.59      A    C  
ANISOU 1337  CG  ASN A 180    13105  16317  11076   1484   -294    602  A    C  
ATOM   1338  ND2 ASN A 180     112.999  86.126   2.928  1.00104.63      A    N  
ANISOU 1338  ND2 ASN A 180    12905  16141  10708   1718   -333    696  A    N  
ATOM   1339  OD1 ASN A 180     114.071  85.012   4.557  1.00117.11      A    O  
ANISOU 1339  OD1 ASN A 180    14394  17519  12581   1410   -179    579  A    O  
ATOM   1340  N   ALA A 181     112.495  81.693   5.635  1.00113.96      A    N  
ANISOU 1340  N   ALA A 181    13561  17437  12302    848   -458    389  A    N  
ATOM   1341  CA  ALA A 181     113.100  80.974   6.749  1.00111.70      A    C  
ANISOU 1341  CA  ALA A 181    13251  17000  12188    682   -372    334  A    C  
ATOM   1342  C   ALA A 181     113.756  79.665   6.225  1.00110.02      A    C  
ANISOU 1342  C   ALA A 181    13194  16645  11963    502   -374    235  A    C  
ATOM   1343  O   ALA A 181     113.203  79.001   5.344  1.00112.64      A    O  
ANISOU 1343  O   ALA A 181    13556  17078  12162    424   -501    193  A    O  
ATOM   1344  CB  ALA A 181     112.041  80.685   7.819  1.00111.33      A    C  
ANISOU 1344  CB  ALA A 181    12947  17137  12214    580   -448    346  A    C  
ATOM   1345  N   PRO A 182     114.933  79.290   6.757  1.00102.02      A    N  
ANISOU 1345  N   PRO A 182    12282  15398  11081    447   -239    194  A    N  
ATOM   1346  CA  PRO A 182     115.594  78.072   6.311  1.00103.33      A    C  
ANISOU 1346  CA  PRO A 182    12602  15416  11242    314   -220     99  A    C  
ATOM   1347  C   PRO A 182     114.822  76.804   6.624  1.00103.48      A    C  
ANISOU 1347  C   PRO A 182    12549  15504  11263    100   -353     34  A    C  
ATOM   1348  O   PRO A 182     114.490  76.555   7.771  1.00 98.89      A    O  
ANISOU 1348  O   PRO A 182    11828  14944  10800      5   -369     47  A    O  
ATOM   1349  CB  PRO A 182     116.913  78.079   7.094  1.00102.35      A    C  
ANISOU 1349  CB  PRO A 182    12530  15063  11294    323    -54     89  A    C  
ATOM   1350  CG  PRO A 182     117.142  79.505   7.446  1.00100.51      A    C  
ANISOU 1350  CG  PRO A 182    12255  14832  11102    484     25    177  A    C  
ATOM   1351  CD  PRO A 182     115.762  80.024   7.717  1.00100.62      A    C  
ANISOU 1351  CD  PRO A 182    12096  15078  11053    522    -99    233  A    C  
ATOM   1352  N   GLN A 183     114.541  76.012   5.594  1.00115.63      A    N  
ANISOU 1352  N   GLN A 183    14206  17069  12658     15   -446    -35  A    N  
ATOM   1353  CA  GLN A 183     113.972  74.684   5.788  1.00123.03      A    C  
ANISOU 1353  CA  GLN A 183    15139  18016  13589   -217   -565   -114  A    C  
ATOM   1354  C   GLN A 183     114.969  73.863   6.607  1.00121.49      A    C  
ANISOU 1354  C   GLN A 183    15036  17569  13554   -292   -449   -167  A    C  
ATOM   1355  O   GLN A 183     116.188  73.933   6.412  1.00107.15      A    O  
ANISOU 1355  O   GLN A 183    13362  15562  11787   -186   -298   -190  A    O  
ATOM   1356  CB  GLN A 183     113.661  74.010   4.451  1.00124.72      A    C  
ANISOU 1356  CB  GLN A 183    15519  18264  13602   -288   -678   -192  A    C  
ATOM   1357  N   LEU A 184     114.421  73.078   7.521  1.00129.76      A    N  
ANISOU 1357  N   LEU A 184    15997  18622  14681   -475   -522   -181  A    N  
ATOM   1358  CA  LEU A 184     115.189  72.526   8.614  1.00138.31      A    C  
ANISOU 1358  CA  LEU A 184    17113  19501  15935   -521   -431   -195  A    C  
ATOM   1359  C   LEU A 184     114.384  71.400   9.276  1.00156.66      A    C  
ANISOU 1359  C   LEU A 184    19408  21832  18281   -769   -548   -224  A    C  
ATOM   1360  O   LEU A 184     113.176  71.305   9.051  1.00181.62      A    O  
ANISOU 1360  O   LEU A 184    22456  25200  21350   -900   -687   -214  A    O  
ATOM   1361  CB  LEU A 184     115.444  73.659   9.600  1.00128.54      A    C  
ANISOU 1361  CB  LEU A 184    15718  18299  14821   -391   -342    -97  A    C  
ATOM   1362  CG  LEU A 184     116.597  73.487  10.559  1.00132.64      A    C  
ANISOU 1362  CG  LEU A 184    16283  18599  15513   -355   -224    -97  A    C  
ATOM   1363  CD1 LEU A 184     117.521  74.680  10.427  1.00135.99      A    C  
ANISOU 1363  CD1 LEU A 184    16707  18980  15982   -153    -94    -51  A    C  
ATOM   1364  CD2 LEU A 184     116.092  73.333  11.984  1.00144.43      A    C  
ANISOU 1364  CD2 LEU A 184    17646  20123  17106   -464   -263    -47  A    C  
ATOM   1365  N   GLN A 185     115.031  70.541  10.070  1.00157.85      A    N  
ANISOU 1365  N   GLN A 185    19659  21763  18550   -839   -496   -256  A    N  
ATOM   1366  CA  GLN A 185     114.303  69.516  10.841  1.00153.46      A    C  
ANISOU 1366  CA  GLN A 185    19096  21187  18023  -1083   -594   -267  A    C  
ATOM   1367  C   GLN A 185     113.507  70.214  11.963  1.00158.49      A    C  
ANISOU 1367  C   GLN A 185    19480  22012  18725  -1122   -610   -158  A    C  
ATOM   1368  O   GLN A 185     113.660  71.417  12.162  1.00182.31      A    O  
ANISOU 1368  O   GLN A 185    22363  25132  21772   -944   -540    -89  A    O  
ATOM   1369  CB  GLN A 185     115.278  68.476  11.413  1.00151.35      A    C  
ANISOU 1369  CB  GLN A 185    19026  20615  17863  -1108   -530   -318  A    C  
ATOM   1370  CG  GLN A 185     116.092  68.932  12.627  1.00155.09      A    C  
ANISOU 1370  CG  GLN A 185    19430  20989  18507   -988   -426   -246  A    C  
ATOM   1371  CD  GLN A 185     117.379  69.668  12.285  1.00149.73      A    C  
ANISOU 1371  CD  GLN A 185    18776  20224  17889   -742   -287   -247  A    C  
ATOM   1372  NE2 GLN A 185     117.957  70.344  13.287  1.00140.67      A    N  
ANISOU 1372  NE2 GLN A 185    17525  19048  16874   -643   -218   -175  A    N  
ATOM   1373  OE1 GLN A 185     117.852  69.630  11.145  1.00139.53      A    O  
ANISOU 1373  OE1 GLN A 185    17599  18891  16523   -654   -241   -311  A    O  
ATOM   1374  N   THR A 186     112.655  69.496  12.689  1.00149.39      A    N  
ANISOU 1374  N   THR A 186    18274  20902  17586  -1354   -690   -141  A    N  
ATOM   1375  CA  THR A 186     112.036  70.076  13.905  1.00143.51      A    C  
ANISOU 1375  CA  THR A 186    17312  20306  16907  -1387   -667    -36  A    C  
ATOM   1376  C   THR A 186     111.770  68.993  14.946  1.00150.43      A    C  
ANISOU 1376  C   THR A 186    18252  21062  17840  -1624   -695    -25  A    C  
ATOM   1377  O   THR A 186     110.636  68.514  15.025  1.00142.57      A    O  
ANISOU 1377  O   THR A 186    17165  20213  16789  -1860   -788    -13  A    O  
ATOM   1378  CB  THR A 186     110.704  70.823  13.622  1.00130.61      A    C  
ANISOU 1378  CB  THR A 186    15412  19024  15187  -1416   -740     19  A    C  
ATOM   1379  CG2 THR A 186     110.164  71.522  14.894  1.00120.83      A    C  
ANISOU 1379  CG2 THR A 186    13960  17936  14014  -1405   -677    124  A    C  
ATOM   1380  OG1 THR A 186     110.912  71.817  12.621  1.00123.33      A    O  
ANISOU 1380  OG1 THR A 186    14459  18201  14198  -1188   -726     16  A    O  
ATOM   1381  N   ALA A 187     112.748  68.585  15.773  1.00156.28      A    N  
ANISOU 1381  N   ALA A 187    19143  21546  18688  -1580   -624    -21  A    N  
ATOM   1382  CA  ALA A 187     114.140  69.091  15.952  1.00150.54      A    C  
ANISOU 1382  CA  ALA A 187    18496  20644  18057  -1330   -514    -23  A    C  
ATOM   1383  C   ALA A 187     114.259  69.217  17.456  1.00140.36      A    C  
ANISOU 1383  C   ALA A 187    17163  19306  16860  -1347   -475     62  A    C  
ATOM   1384  O   ALA A 187     114.280  68.220  18.173  1.00135.11      A    O  
ANISOU 1384  O   ALA A 187    16622  18482  16232  -1494   -505     68  A    O  
ATOM   1385  CB  ALA A 187     114.432  70.437  15.288  1.00150.45      A    C  
ANISOU 1385  CB  ALA A 187    18370  20769  18022  -1098   -453     -8  A    C  
ATOM   1386  N   SER A 188     114.335  70.460  17.920  1.00132.64      A    N  
ANISOU 1386  N   SER A 188    16031  18456  15909  -1194   -410    127  A    N  
ATOM   1387  CA  SER A 188     114.011  70.812  19.276  1.00129.08      A    C  
ANISOU 1387  CA  SER A 188    15493  18059  15493  -1232   -382    215  A    C  
ATOM   1388  C   SER A 188     112.765  71.697  19.140  1.00127.84      A    C  
ANISOU 1388  C   SER A 188    15103  18220  15249  -1244   -382    263  A    C  
ATOM   1389  O   SER A 188     112.057  71.624  18.131  1.00125.12      A    O  
ANISOU 1389  O   SER A 188    14686  18026  14826  -1296   -440    230  A    O  
ATOM   1390  CB  SER A 188     115.196  71.548  19.900  1.00126.99      A    C  
ANISOU 1390  CB  SER A 188    15263  17667  15321  -1029   -309    240  A    C  
ATOM   1391  OG  SER A 188     115.843  72.356  18.929  1.00118.21      A    O  
ANISOU 1391  OG  SER A 188    14135  16567  14212   -836   -263    201  A    O  
ATOM   1392  N   GLY A 189     112.474  72.527  20.134  1.00120.86      A    N  
ANISOU 1392  N   GLY A 189    14102  17446  14372  -1187   -321    339  A    N  
ATOM   1393  CA  GLY A 189     111.459  73.542  19.936  1.00112.16      A    C  
ANISOU 1393  CA  GLY A 189    12777  16639  13197  -1122   -298    379  A    C  
ATOM   1394  C   GLY A 189     111.981  74.572  18.942  1.00103.83      A    C  
ANISOU 1394  C   GLY A 189    11714  15608  12130   -875   -273    349  A    C  
ATOM   1395  O   GLY A 189     113.077  75.116  19.119  1.00102.03      A    O  
ANISOU 1395  O   GLY A 189    11587  15217  11961   -716   -215    342  A    O  
ATOM   1396  N   VAL A 190     111.216  74.852  17.893  1.00 96.22      A    N  
ANISOU 1396  N   VAL A 190    10631  14844  11084   -851   -323    337  A    N  
ATOM   1397  CA  VAL A 190     111.525  75.993  17.037  1.00 89.99      A    C  
ANISOU 1397  CA  VAL A 190     9826  14106  10259   -607   -292    333  A    C  
ATOM   1398  C   VAL A 190     110.549  77.135  17.277  1.00 88.59      A    C  
ANISOU 1398  C   VAL A 190     9440  14192  10026   -479   -258    400  A    C  
ATOM   1399  O   VAL A 190     109.334  76.944  17.211  1.00 94.81      A    O  
ANISOU 1399  O   VAL A 190    10039  15225  10759   -580   -311    426  A    O  
ATOM   1400  CB  VAL A 190     111.501  75.608  15.565  1.00 89.56      A    C  
ANISOU 1400  CB  VAL A 190     9825  14067  10134   -616   -373    274  A    C  
ATOM   1401  CG1 VAL A 190     111.862  76.815  14.707  1.00 85.48      A    C  
ANISOU 1401  CG1 VAL A 190     9322  13584   9570   -361   -333    284  A    C  
ATOM   1402  CG2 VAL A 190     112.498  74.487  15.343  1.00 97.38      A    C  
ANISOU 1402  CG2 VAL A 190    11037  14789  11175   -715   -384    201  A    C  
ATOM   1403  N   THR A 191     111.086  78.321  17.554  1.00 83.10      A    N  
ANISOU 1403  N   THR A 191     8780  13446   9346   -257   -169    426  A    N  
ATOM   1404  CA  THR A 191     110.269  79.461  17.945  1.00 82.47      A    C  
ANISOU 1404  CA  THR A 191     8541  13576   9217   -100   -114    485  A    C  
ATOM   1405  C   THR A 191     110.446  80.595  16.948  1.00 83.10      A    C  
ANISOU 1405  C   THR A 191     8646  13684   9242    153   -102    491  A    C  
ATOM   1406  O   THR A 191     111.572  81.077  16.766  1.00 83.05      A    O  
ANISOU 1406  O   THR A 191     8820  13463   9270    264    -53    472  A    O  
ATOM   1407  CB  THR A 191     110.677  79.950  19.344  1.00 81.40      A    C  
ANISOU 1407  CB  THR A 191     8462  13338   9128    -59    -12    515  A    C  
ATOM   1408  CG2 THR A 191     109.717  81.055  19.818  1.00 80.66      A    C  
ANISOU 1408  CG2 THR A 191     8207  13469   8968    103     61    570  A    C  
ATOM   1409  OG1 THR A 191     110.707  78.836  20.270  1.00 80.13      A    O  
ANISOU 1409  OG1 THR A 191     8331  13098   9015   -292    -25    515  A    O  
ATOM   1410  N   ARG A 192     109.351  81.016  16.306  1.00 84.13      A    N  
ANISOU 1410  N   ARG A 192     8600  14079   9287    241   -150    522  A    N  
ATOM   1411  CA  ARG A 192     109.424  82.008  15.226  1.00 84.65      A    C  
ANISOU 1411  CA  ARG A 192     8705  14175   9281    484   -161    536  A    C  
ATOM   1412  C   ARG A 192     109.196  83.430  15.724  1.00 82.19      A    C  
ANISOU 1412  C   ARG A 192     8364  13918   8944    744    -64    589  A    C  
ATOM   1413  O   ARG A 192     108.362  83.654  16.546  1.00 82.14      A    O  
ANISOU 1413  O   ARG A 192     8191  14083   8932    761    -21    624  A    O  
ATOM   1414  CB  ARG A 192     108.435  81.655  14.126  1.00 91.73      A    C  
ANISOU 1414  CB  ARG A 192     9448  15315  10087    455   -295    541  A    C  
ATOM   1415  CG  ARG A 192     108.934  80.527  13.242  1.00 97.68      A    C  
ANISOU 1415  CG  ARG A 192    10334  15948  10829    271   -390    474  A    C  
ATOM   1416  CD  ARG A 192     108.141  80.340  11.946  1.00107.01      A    C  
ANISOU 1416  CD  ARG A 192    11427  17337  11894    274   -539    471  A    C  
ATOM   1417  NE  ARG A 192     108.987  79.715  10.929  1.00110.24      A    N  
ANISOU 1417  NE  ARG A 192    12066  17556  12261    210   -584    405  A    N  
ATOM   1418  CZ  ARG A 192     109.351  78.429  10.929  1.00108.84      A    C  
ANISOU 1418  CZ  ARG A 192    11993  17245  12117    -32   -621    332  A    C  
ATOM   1419  NH1 ARG A 192     108.910  77.600  11.878  1.00101.34      A    N1+
ANISOU 1419  NH1 ARG A 192    10939  16327  11237   -255   -634    324  A    N1+
ATOM   1420  NH2 ARG A 192     110.152  77.970   9.962  1.00108.04      A    N  
ANISOU 1420  NH2 ARG A 192    12113  16971  11965    -47   -637    270  A    N  
ATOM   1421  N   LEU A 193     109.950  84.387  15.218  1.00 85.06      A    N  
ANISOU 1421  N   LEU A 193     8907  14124   9286    945    -19    593  A    N  
ATOM   1422  CA  LEU A 193     110.018  85.706  15.842  1.00 91.23      A    C  
ANISOU 1422  CA  LEU A 193     9744  14861  10055   1172     89    627  A    C  
ATOM   1423  C   LEU A 193     109.800  86.855  14.877  1.00100.25      A    C  
ANISOU 1423  C   LEU A 193    10939  16046  11105   1453     85    668  A    C  
ATOM   1424  O   LEU A 193     110.712  87.642  14.603  1.00106.45      A    O  
ANISOU 1424  O   LEU A 193    11949  16609  11885   1573    141    668  A    O  
ATOM   1425  CB  LEU A 193     111.392  85.921  16.512  1.00 89.66      A    C  
ANISOU 1425  CB  LEU A 193     9780  14349   9937   1133    171    595  A    C  
ATOM   1426  CG  LEU A 193     111.525  85.888  18.022  1.00 84.59      A    C  
ANISOU 1426  CG  LEU A 193     9141  13648   9350   1054    241    589  A    C  
ATOM   1427  CD1 LEU A 193     111.240  84.482  18.527  1.00 81.66      A    C  
ANISOU 1427  CD1 LEU A 193     8652  13343   9030    789    189    572  A    C  
ATOM   1428  CD2 LEU A 193     112.921  86.389  18.406  1.00 82.46      A    C  
ANISOU 1428  CD2 LEU A 193     9110  13078   9143   1067    296    563  A    C  
ATOM   1429  N   ASN A 194     108.601  86.977  14.360  1.00109.33      A    N  
ANISOU 1429  N   ASN A 194    11881  17480  12179   1558     15    708  A    N  
ATOM   1430  CA  ASN A 194     108.168  88.289  13.926  1.00125.08      A    C  
ANISOU 1430  CA  ASN A 194    13894  19541  14086   1884     38    763  A    C  
ATOM   1431  C   ASN A 194     109.262  89.170  13.249  1.00130.03      A    C  
ANISOU 1431  C   ASN A 194    14839  19881  14682   2035     82    769  A    C  
ATOM   1432  O   ASN A 194     109.417  90.352  13.577  1.00146.16      A    O  
ANISOU 1432  O   ASN A 194    17016  21816  16700   2255    173    795  A    O  
ATOM   1433  CB  ASN A 194     107.587  88.979  15.176  1.00126.31      A    C  
ANISOU 1433  CB  ASN A 194    13952  19785  14254   2011    155    782  A    C  
ATOM   1434  CG  ASN A 194     107.268  90.429  14.953  1.00133.82      A    C  
ANISOU 1434  CG  ASN A 194    14975  20744  15124   2376    211    830  A    C  
ATOM   1435  ND2 ASN A 194     106.447  90.709  13.943  1.00137.34      A    N  
ANISOU 1435  ND2 ASN A 194    15291  21404  15490   2559    118    882  A    N  
ATOM   1436  OD1 ASN A 194     107.758  91.297  15.678  1.00142.55      A    O  
ANISOU 1436  OD1 ASN A 194    16266  21660  16233   2497    330    821  A    O  
ATOM   1437  N   ALA A 195     110.025  88.579  12.326  1.00127.27      A    N  
ANISOU 1437  N   ALA A 195    14623  19402  14329   1907     27    745  A    N  
ATOM   1438  CA  ALA A 195     110.890  89.320  11.382  1.00127.19      A    C  
ANISOU 1438  CA  ALA A 195    14885  19178  14263   2039     55    765  A    C  
ATOM   1439  C   ALA A 195     111.846  90.371  11.959  1.00121.09      A    C  
ANISOU 1439  C   ALA A 195    14353  18124  13529   2133    190    770  A    C  
ATOM   1440  O   ALA A 195     113.018  90.094  12.119  1.00127.40      A    O  
ANISOU 1440  O   ALA A 195    15303  18694  14407   1974    244    730  A    O  
ATOM   1441  CB  ALA A 195     110.035  89.946  10.291  1.00135.79      A    C  
ANISOU 1441  CB  ALA A 195    15941  20441  15213   2284    -31    834  A    C  
ATOM   1442  N   TRP A 196     111.362  91.581  12.244  1.00122.02      A    N  
ANISOU 1442  N   TRP A 196    14512  18257  13592   2392    240    814  A    N  
ATOM   1443  CA  TRP A 196     112.249  92.729  12.515  1.00121.62      A    C  
ANISOU 1443  CA  TRP A 196    14748  17918  13544   2502    350    824  A    C  
ATOM   1444  C   TRP A 196     113.164  92.579  13.733  1.00113.88      A    C  
ANISOU 1444  C   TRP A 196    13843  16741  12682   2314    430    764  A    C  
ATOM   1445  O   TRP A 196     114.020  93.447  13.971  1.00112.92      A    O  
ANISOU 1445  O   TRP A 196    13963  16366  12573   2351    508    761  A    O  
ATOM   1446  CB  TRP A 196     111.448  94.037  12.659  1.00134.33      A    C  
ANISOU 1446  CB  TRP A 196    16399  19578  15061   2837    388    876  A    C  
ATOM   1447  CG  TRP A 196     110.280  93.975  13.628  1.00149.78      A    C  
ANISOU 1447  CG  TRP A 196    18094  21790  17022   2918    398    870  A    C  
ATOM   1448  CD1 TRP A 196     108.968  93.878  13.289  1.00162.21      A    C  
ANISOU 1448  CD1 TRP A 196    19405  23689  18535   3071    327    914  A    C  
ATOM   1449  CD2 TRP A 196     110.318  94.027  15.078  1.00151.94      A    C  
ANISOU 1449  CD2 TRP A 196    18343  22029  17358   2850    489    824  A    C  
ATOM   1450  CE2 TRP A 196     108.988  93.940  15.530  1.00163.61      A    C  
ANISOU 1450  CE2 TRP A 196    19537  23820  18805   2966    489    843  A    C  
ATOM   1451  CE3 TRP A 196     111.346  94.133  16.030  1.00146.22      A    C  
ANISOU 1451  CE3 TRP A 196    17803  21047  16704   2698    565    771  A    C  
ATOM   1452  NE1 TRP A 196     108.185  93.856  14.421  1.00170.95      A    N  
ANISOU 1452  NE1 TRP A 196    20310  24972  19670   3098    387    898  A    N  
ATOM   1453  CZ2 TRP A 196     108.653  93.957  16.896  1.00163.53      A    C  
ANISOU 1453  CZ2 TRP A 196    19445  23866  18822   2938    582    812  A    C  
ATOM   1454  CZ3 TRP A 196     111.009  94.143  17.390  1.00139.72      A    C  
ANISOU 1454  CZ3 TRP A 196    16907  20277  15901   2673    633    737  A    C  
ATOM   1455  CH2 TRP A 196     109.676  94.059  17.803  1.00148.24      A    C  
ANISOU 1455  CH2 TRP A 196    17725  21661  16937   2794    650    759  A    C  
ATOM   1456  N   GLN A 197     112.986  91.511  14.511  1.00101.01      A    N  
ANISOU 1456  N   GLN A 197    12021  15222  11132   2109    403    719  A    N  
ATOM   1457  CA  GLN A 197     113.787  91.319  15.708  1.00 93.44      A    C  
ANISOU 1457  CA  GLN A 197    11126  14100  10277   1941    457    669  A    C  
ATOM   1458  C   GLN A 197     115.198  90.904  15.349  1.00 86.01      A    C  
ANISOU 1458  C   GLN A 197    10331  12927   9422   1757    465    640  A    C  
ATOM   1459  O   GLN A 197     116.121  91.047  16.156  1.00 86.19      A    O  
ANISOU 1459  O   GLN A 197    10462  12761   9525   1651    506    608  A    O  
ATOM   1460  CB  GLN A 197     113.151  90.282  16.603  1.00 97.65      A    C  
ANISOU 1460  CB  GLN A 197    11429  14816  10857   1784    425    645  A    C  
ATOM   1461  CG  GLN A 197     111.675  90.521  16.806  1.00101.26      A    C  
ANISOU 1461  CG  GLN A 197    11679  15559  11236   1943    422    680  A    C  
ATOM   1462  CD  GLN A 197     111.222  90.149  18.181  1.00102.73      A    C  
ANISOU 1462  CD  GLN A 197    11739  15840  11453   1845    464    661  A    C  
ATOM   1463  NE2 GLN A 197     109.966  89.758  18.304  1.00105.05      A    N  
ANISOU 1463  NE2 GLN A 197    11773  16430  11711   1861    445    687  A    N  
ATOM   1464  OE1 GLN A 197     111.997  90.214  19.132  1.00110.56      A    O  
ANISOU 1464  OE1 GLN A 197    12867  16645  12494   1750    511    629  A    O  
ATOM   1465  N   PHE A 198     115.354  90.420  14.121  1.00 80.64      A    N  
ANISOU 1465  N   PHE A 198     9653  12271   8714   1726    423    651  A    N  
ATOM   1466  CA  PHE A 198     116.661  90.114  13.548  1.00 76.64      A    C  
ANISOU 1466  CA  PHE A 198     9286  11561   8271   1590    454    631  A    C  
ATOM   1467  C   PHE A 198     117.270  91.260  12.743  1.00 74.91      A    C  
ANISOU 1467  C   PHE A 198     9306  11164   7991   1720    521    675  A    C  
ATOM   1468  O   PHE A 198     118.206  91.039  11.977  1.00 71.23      A    O  
ANISOU 1468  O   PHE A 198     8945  10570   7546   1630    557    674  A    O  
ATOM   1469  CB  PHE A 198     116.541  88.920  12.622  1.00 75.09      A    C  
ANISOU 1469  CB  PHE A 198     8996  11474   8061   1481    389    613  A    C  
ATOM   1470  CG  PHE A 198     116.137  87.642  13.304  1.00 70.89      A    C  
ANISOU 1470  CG  PHE A 198     8269  11067   7598   1306    326    567  A    C  
ATOM   1471  CD1 PHE A 198     114.820  87.376  13.558  1.00 69.63      A    C  
ANISOU 1471  CD1 PHE A 198     7921  11150   7386   1339    257    580  A    C  
ATOM   1472  CD2 PHE A 198     117.088  86.694  13.647  1.00 69.46      A    C  
ANISOU 1472  CD2 PHE A 198     8098  10760   7534   1109    336    516  A    C  
ATOM   1473  CE1 PHE A 198     114.444  86.194  14.150  1.00 69.67      A    C  
ANISOU 1473  CE1 PHE A 198     7771  11255   7445   1154    202    544  A    C  
ATOM   1474  CE2 PHE A 198     116.728  85.507  14.229  1.00 68.56      A    C  
ANISOU 1474  CE2 PHE A 198     7844  10732   7472    953    276    479  A    C  
ATOM   1475  CZ  PHE A 198     115.399  85.261  14.488  1.00 70.74      A    C  
ANISOU 1475  CZ  PHE A 198     7954  11235   7688    964    210    496  A    C  
ATOM   1476  N   ALA A 199     116.733  92.465  12.927  1.00 77.05      A    N  
ANISOU 1476  N   ALA A 199     9671  11421   8181   1931    546    715  A    N  
ATOM   1477  CA  ALA A 199     117.267  93.683  12.328  1.00 78.55      A    C  
ANISOU 1477  CA  ALA A 199    10128  11408   8307   2061    614    764  A    C  
ATOM   1478  C   ALA A 199     118.678  93.920  12.795  1.00 74.16      A    C  
ANISOU 1478  C   ALA A 199     9726  10589   7862   1884    689    734  A    C  
ATOM   1479  O   ALA A 199     118.932  93.902  13.984  1.00 70.86      A    O  
ANISOU 1479  O   ALA A 199     9273  10120   7528   1794    693    688  A    O  
ATOM   1480  CB  ALA A 199     116.414  94.884  12.715  1.00 81.57      A    C  
ANISOU 1480  CB  ALA A 199    10587  11807   8596   2324    630    800  A    C  
ATOM   1481  N   ALA A 200     119.579  94.164  11.854  1.00 74.58      A    N  
ANISOU 1481  N   ALA A 200     9947  10484   7904   1834    745    764  A    N  
ATOM   1482  CA  ALA A 200     120.970  94.373  12.178  1.00 77.24      A    C  
ANISOU 1482  CA  ALA A 200    10402  10590   8356   1647    818    742  A    C  
ATOM   1483  C   ALA A 200     121.188  95.729  12.877  1.00 84.09      A    C  
ANISOU 1483  C   ALA A 200    11484  11257   9206   1714    860    751  A    C  
ATOM   1484  O   ALA A 200     121.898  95.813  13.895  1.00 84.18      A    O  
ANISOU 1484  O   ALA A 200    11505  11153   9326   1565    866    704  A    O  
ATOM   1485  CB  ALA A 200     121.815  94.269  10.920  1.00 77.78      A    C  
ANISOU 1485  CB  ALA A 200    10582  10562   8406   1574    889    779  A    C  
ATOM   1486  N   ASP A 201     120.592  96.789  12.334  1.00 90.06      A    N  
ANISOU 1486  N   ASP A 201    12430  11965   9822   1942    881    811  A    N  
ATOM   1487  CA  ASP A 201     120.772  98.127  12.892  1.00 94.60      A    C  
ANISOU 1487  CA  ASP A 201    13260  12320  10361   2024    926    819  A    C  
ATOM   1488  C   ASP A 201     120.160  98.240  14.311  1.00 93.55      A    C  
ANISOU 1488  C   ASP A 201    13044  12253  10245   2078    889    757  A    C  
ATOM   1489  O   ASP A 201     120.757  98.840  15.210  1.00 93.21      A    O  
ANISOU 1489  O   ASP A 201    13144  12025  10245   1991    910    717  A    O  
ATOM   1490  CB  ASP A 201     120.208  99.176  11.936  1.00100.32      A    C  
ANISOU 1490  CB  ASP A 201    14220  12975  10921   2288    954    902  A    C  
ATOM   1491  CG  ASP A 201     118.749  98.923  11.584  1.00109.76      A    C  
ANISOU 1491  CG  ASP A 201    15247  14446  12009   2549    883    932  A    C  
ATOM   1492  OD1 ASP A 201     118.255  97.797  11.831  1.00111.78      A    O  
ANISOU 1492  OD1 ASP A 201    15203  14950  12319   2480    818    894  A    O  
ATOM   1493  OD2 ASP A 201     118.090  99.854  11.069  1.00118.25      A    O1-
ANISOU 1493  OD2 ASP A 201    16492  15489  12949   2822    887    997  A    O1-
ATOM   1494  N   ALA A 202     118.987  97.647  14.510  1.00 93.42      A    N  
ANISOU 1494  N   ALA A 202    12798  12505  10192   2205    835    751  A    N  
ATOM   1495  CA  ALA A 202     118.354  97.603  15.840  1.00 91.44      A    C  
ANISOU 1495  CA  ALA A 202    12440  12351   9952   2244    818    697  A    C  
ATOM   1496  C   ALA A 202     119.061  96.608  16.763  1.00 85.81      A    C  
ANISOU 1496  C   ALA A 202    11574  11649   9379   1962    782    633  A    C  
ATOM   1497  O   ALA A 202     119.119  96.809  17.968  1.00 82.40      A    O  
ANISOU 1497  O   ALA A 202    11171  11169   8966   1920    779    585  A    O  
ATOM   1498  CB  ALA A 202     116.879  97.244  15.708  1.00 94.97      A    C  
ANISOU 1498  CB  ALA A 202    12662  13102  10319   2446    781    721  A    C  
ATOM   1499  N   GLY A 203     119.582  95.533  16.175  1.00 83.26      A    N  
ANISOU 1499  N   GLY A 203    11106  11385   9145   1787    753    634  A    N  
ATOM   1500  CA  GLY A 203     120.374  94.548  16.888  1.00 78.93      A    C  
ANISOU 1500  CA  GLY A 203    10426  10826   8738   1536    716    583  A    C  
ATOM   1501  C   GLY A 203     121.690  95.139  17.344  1.00 80.08      A    C  
ANISOU 1501  C   GLY A 203    10745  10716   8964   1383    741    559  A    C  
ATOM   1502  O   GLY A 203     122.215  94.760  18.390  1.00 80.40      A    O  
ANISOU 1502  O   GLY A 203    10728  10723   9096   1228    697    513  A    O  
ATOM   1503  N   GLU A 204     122.226  96.093  16.587  1.00 80.61      A    N  
ANISOU 1503  N   GLU A 204    11031  10602   8994   1417    802    595  A    N  
ATOM   1504  CA  GLU A 204     123.453  96.759  17.013  1.00 83.42      A    C  
ANISOU 1504  CA  GLU A 204    11558  10712   9425   1250    822    575  A    C  
ATOM   1505  C   GLU A 204     123.194  97.730  18.181  1.00 80.20      A    C  
ANISOU 1505  C   GLU A 204    11324  10191   8955   1314    805    537  A    C  
ATOM   1506  O   GLU A 204     124.043  97.868  19.060  1.00 80.92      A    O  
ANISOU 1506  O   GLU A 204    11464  10154   9125   1135    767    492  A    O  
ATOM   1507  CB  GLU A 204     124.150  97.461  15.834  1.00 89.01      A    C  
ANISOU 1507  CB  GLU A 204    12461  11247  10109   1232    906    633  A    C  
ATOM   1508  CG  GLU A 204     125.535  98.013  16.167  1.00 98.22      A    C  
ANISOU 1508  CG  GLU A 204    13764  12177  11378   1002    928    617  A    C  
ATOM   1509  CD  GLU A 204     126.440  98.167  14.952  1.00111.27      A    C  
ANISOU 1509  CD  GLU A 204    15499  13720  13059    894   1024    675  A    C  
ATOM   1510  OE1 GLU A 204     127.639  98.532  15.122  1.00127.27      A    O  
ANISOU 1510  OE1 GLU A 204    17593  15576  15185    674   1051    670  A    O  
ATOM   1511  OE2 GLU A 204     125.958  97.917  13.826  1.00113.94      A    O1-
ANISOU 1511  OE2 GLU A 204    15829  14149  13314   1022   1071    729  A    O1-
ATOM   1512  N   LYS A 205     122.050  98.415  18.188  1.00 77.43      A    N  
ANISOU 1512  N   LYS A 205    11072   9888   8460   1574    830    551  A    N  
ATOM   1513  CA  LYS A 205     121.747  99.343  19.278  1.00 81.01      A    C  
ANISOU 1513  CA  LYS A 205    11714  10233   8834   1663    831    507  A    C  
ATOM   1514  C   LYS A 205     121.665  98.520  20.527  1.00 80.49      A    C  
ANISOU 1514  C   LYS A 205    11462  10293   8827   1545    766    449  A    C  
ATOM   1515  O   LYS A 205     122.195  98.918  21.564  1.00 82.55      A    O  
ANISOU 1515  O   LYS A 205    11854  10415   9096   1436    732    394  A    O  
ATOM   1516  CB  LYS A 205     120.422 100.129  19.085  1.00 86.87      A    C  
ANISOU 1516  CB  LYS A 205    12554  11042   9411   2005    883    533  A    C  
ATOM   1517  CG  LYS A 205     120.491 101.257  18.054  1.00 95.98      A    C  
ANISOU 1517  CG  LYS A 205    13991  12004  10473   2164    945    591  A    C  
ATOM   1518  CD  LYS A 205     119.118 101.743  17.551  1.00 98.62      A    C  
ANISOU 1518  CD  LYS A 205    14336  12472  10661   2533    979    640  A    C  
ATOM   1519  CE  LYS A 205     119.224 102.769  16.401  1.00 94.79      A    C  
ANISOU 1519  CE  LYS A 205    14141  11791  10082   2695   1028    716  A    C  
ATOM   1520  NZ  LYS A 205     119.587 102.171  15.085  1.00 89.40      A    N1+
ANISOU 1520  NZ  LYS A 205    13367  11166   9433   2609   1017    787  A    N1+
ATOM   1521  N   LEU A 206     120.988  97.377  20.430  1.00 79.81      A    N  
ANISOU 1521  N   LEU A 206    11093  10462   8766   1560    740    462  A    N  
ATOM   1522  CA  LEU A 206     120.734  96.530  21.596  1.00 80.59      A    C  
ANISOU 1522  CA  LEU A 206    11021  10697   8900   1466    684    421  A    C  
ATOM   1523  C   LEU A 206     122.029  96.001  22.222  1.00 77.68      A    C  
ANISOU 1523  C   LEU A 206    10629  10214   8671   1190    609    385  A    C  
ATOM   1524  O   LEU A 206     122.236  96.075  23.436  1.00 73.52      A    O  
ANISOU 1524  O   LEU A 206    10157   9638   8140   1111    559    340  A    O  
ATOM   1525  CB  LEU A 206     119.850  95.365  21.185  1.00 83.35      A    C  
ANISOU 1525  CB  LEU A 206    11085  11320   9262   1501    669    450  A    C  
ATOM   1526  CG  LEU A 206     118.403  95.425  21.662  1.00 85.48      A    C  
ANISOU 1526  CG  LEU A 206    11262  11799   9416   1694    701    457  A    C  
ATOM   1527  CD1 LEU A 206     117.533  94.536  20.792  1.00 84.26      A    C  
ANISOU 1527  CD1 LEU A 206    10857  11895   9260   1744    686    499  A    C  
ATOM   1528  CD2 LEU A 206     118.327  94.992  23.125  1.00 88.19      A    C  
ANISOU 1528  CD2 LEU A 206    11561  12183   9764   1586    673    414  A    C  
ATOM   1529  N   LEU A 207     122.905  95.496  21.366  1.00 75.77      A    N  
ANISOU 1529  N   LEU A 207    10308   9933   8547   1055    602    407  A    N  
ATOM   1530  CA  LEU A 207     124.200  94.997  21.800  1.00 73.40      A    C  
ANISOU 1530  CA  LEU A 207     9953   9539   8397    811    536    381  A    C  
ATOM   1531  C   LEU A 207     125.118  96.056  22.434  1.00 74.87      A    C  
ANISOU 1531  C   LEU A 207    10364   9491   8592    702    509    347  A    C  
ATOM   1532  O   LEU A 207     125.679  95.844  23.496  1.00 73.05      A    O  
ANISOU 1532  O   LEU A 207    10117   9221   8417    559    418    308  A    O  
ATOM   1533  CB  LEU A 207     124.901  94.365  20.614  1.00 71.85      A    C  
ANISOU 1533  CB  LEU A 207     9638   9352   8307    724    568    414  A    C  
ATOM   1534  CG  LEU A 207     124.239  93.071  20.174  1.00 71.44      A    C  
ANISOU 1534  CG  LEU A 207     9357   9513   8271    761    559    428  A    C  
ATOM   1535  CD1 LEU A 207     124.765  92.653  18.827  1.00 71.92      A    C  
ANISOU 1535  CD1 LEU A 207     9364   9575   8386    726    617    457  A    C  
ATOM   1536  CD2 LEU A 207     124.519  91.975  21.175  1.00 73.12      A    C  
ANISOU 1536  CD2 LEU A 207     9407   9791   8583    627    468    396  A    C  
ATOM   1537  N   THR A 208     125.290  97.193  21.772  1.00 78.50      A    N  
ANISOU 1537  N   THR A 208    11046   9787   8992    759    579    366  A    N  
ATOM   1538  CA  THR A 208     126.147  98.239  22.300  1.00 80.28      A    C  
ANISOU 1538  CA  THR A 208    11512   9773   9219    634    553    333  A    C  
ATOM   1539  C   THR A 208     125.592  98.755  23.626  1.00 90.65      A    C  
ANISOU 1539  C   THR A 208    12974  11052  10415    703    502    273  A    C  
ATOM   1540  O   THR A 208     126.356  99.118  24.529  1.00103.59      A    O  
ANISOU 1540  O   THR A 208    14728  12553  12079    537    418    223  A    O  
ATOM   1541  CB  THR A 208     126.243  99.404  21.336  1.00 76.36      A    C  
ANISOU 1541  CB  THR A 208    11271   9091   8650    710    648    370  A    C  
ATOM   1542  CG2 THR A 208     127.000  98.998  20.134  1.00 78.57      A    C  
ANISOU 1542  CG2 THR A 208    11443   9372   9038    598    703    425  A    C  
ATOM   1543  OG1 THR A 208     124.930  99.780  20.935  1.00 72.97      A    O  
ANISOU 1543  OG1 THR A 208    10918   8740   8067   1005    717    396  A    O  
ATOM   1544  N   GLU A 209     124.270  98.811  23.750  1.00 87.68      A    N  
ANISOU 1544  N   GLU A 209    12600  10807   9904    947    554    277  A    N  
ATOM   1545  CA  GLU A 209     123.684  99.302  24.974  1.00 86.67      A    C  
ANISOU 1545  CA  GLU A 209    12619  10660   9647   1035    538    221  A    C  
ATOM   1546  C   GLU A 209     123.793  98.274  26.076  1.00 76.63      A    C  
ANISOU 1546  C   GLU A 209    11166   9519   8428    897    439    193  A    C  
ATOM   1547  O   GLU A 209     123.988  98.630  27.206  1.00 77.39      A    O  
ANISOU 1547  O   GLU A 209    11411   9530   8464    836    378    138  A    O  
ATOM   1548  CB  GLU A 209     122.236  99.725  24.752  1.00 97.50      A    C  
ANISOU 1548  CB  GLU A 209    14032  12149  10863   1351    643    239  A    C  
ATOM   1549  CG  GLU A 209     122.080 101.019  23.948  1.00108.16      A    C  
ANISOU 1549  CG  GLU A 209    15660  13316  12118   1531    729    257  A    C  
ATOM   1550  CD  GLU A 209     120.648 101.248  23.452  1.00119.36      A    C  
ANISOU 1550  CD  GLU A 209    17037  14901  13413   1869    825    298  A    C  
ATOM   1551  OE1 GLU A 209     119.764 100.407  23.772  1.00118.62      A    O  
ANISOU 1551  OE1 GLU A 209    16684  15076  13309   1940    828    306  A    O  
ATOM   1552  OE2 GLU A 209     120.407 102.268  22.750  1.00123.61      A    O1-
ANISOU 1552  OE2 GLU A 209    17798  15303  13863   2061    893    324  A    O1-
ATOM   1553  N   TYR A 210     123.683  97.001  25.748  1.00 72.55      A    N  
ANISOU 1553  N   TYR A 210    10355   9195   8013    848    418    231  A    N  
ATOM   1554  CA  TYR A 210     123.852  95.933  26.752  1.00 71.68      A    C  
ANISOU 1554  CA  TYR A 210    10082   9190   7960    711    318    217  A    C  
ATOM   1555  C   TYR A 210     125.261  95.848  27.340  1.00 75.37      A    C  
ANISOU 1555  C   TYR A 210    10576   9515   8546    466    189    187  A    C  
ATOM   1556  O   TYR A 210     125.419  95.659  28.537  1.00 79.57      A    O  
ANISOU 1556  O   TYR A 210    11144  10039   9047    384     92    154  A    O  
ATOM   1557  CB  TYR A 210     123.539  94.574  26.155  1.00 66.54      A    C  
ANISOU 1557  CB  TYR A 210     9137   8740   7404    697    321    263  A    C  
ATOM   1558  CG  TYR A 210     123.703  93.430  27.115  1.00 62.92      A    C  
ANISOU 1558  CG  TYR A 210     8532   8370   7003    567    221    259  A    C  
ATOM   1559  CD1 TYR A 210     122.788  93.221  28.112  1.00 62.80      A    C  
ANISOU 1559  CD1 TYR A 210     8526   8463   6871    628    222    252  A    C  
ATOM   1560  CD2 TYR A 210     124.757  92.548  27.008  1.00 62.56      A    C  
ANISOU 1560  CD2 TYR A 210     8342   8302   7126    396    134    266  A    C  
ATOM   1561  CE1 TYR A 210     122.902  92.157  28.972  1.00 62.44      A    C  
ANISOU 1561  CE1 TYR A 210     8371   8487   6863    510    132    261  A    C  
ATOM   1562  CE2 TYR A 210     124.887  91.474  27.875  1.00 61.24      A    C  
ANISOU 1562  CE2 TYR A 210     8059   8202   7006    299     35    271  A    C  
ATOM   1563  CZ  TYR A 210     123.951  91.284  28.854  1.00 61.04      A    C  
ANISOU 1563  CZ  TYR A 210     8068   8270   6852    351     31    271  A    C  
ATOM   1564  OH  TYR A 210     124.072  90.260  29.755  1.00 60.63      A    O  
ANISOU 1564  OH  TYR A 210     7939   8266   6830    253    -67    284  A    O  
ATOM   1565  N   PHE A 211     126.282  95.978  26.501  1.00 75.65      A    N  
ANISOU 1565  N   PHE A 211    10584   9446   8711    346    186    203  A    N  
ATOM   1566  CA  PHE A 211     127.647  95.951  26.978  1.00 76.76      A    C  
ANISOU 1566  CA  PHE A 211    10714   9470   8979    111     65    180  A    C  
ATOM   1567  C   PHE A 211     128.212  97.364  27.253  1.00 82.90      A    C  
ANISOU 1567  C   PHE A 211    11789  10012   9694     34     46    136  A    C  
ATOM   1568  O   PHE A 211     129.338  97.495  27.747  1.00 83.12      A    O  
ANISOU 1568  O   PHE A 211    11827   9938   9816   -181    -73    111  A    O  
ATOM   1569  CB  PHE A 211     128.528  95.231  25.967  1.00 76.03      A    C  
ANISOU 1569  CB  PHE A 211    10398   9412   9075      1     82    221  A    C  
ATOM   1570  CG  PHE A 211     128.121  93.811  25.703  1.00 73.00      A    C  
ANISOU 1570  CG  PHE A 211     9753   9226   8758     52     88    252  A    C  
ATOM   1571  CD1 PHE A 211     128.325  92.843  26.647  1.00 73.22      A    C  
ANISOU 1571  CD1 PHE A 211     9644   9329   8844    -23    -31    244  A    C  
ATOM   1572  CD2 PHE A 211     127.574  93.444  24.486  1.00 75.09      A    C  
ANISOU 1572  CD2 PHE A 211     9927   9583   9019    167    205    290  A    C  
ATOM   1573  CE1 PHE A 211     127.977  91.522  26.408  1.00 71.65      A    C  
ANISOU 1573  CE1 PHE A 211     9237   9281   8705     13    -27    271  A    C  
ATOM   1574  CE2 PHE A 211     127.218  92.130  24.228  1.00 72.64      A    C  
ANISOU 1574  CE2 PHE A 211     9401   9435   8763    193    202    310  A    C  
ATOM   1575  CZ  PHE A 211     127.419  91.165  25.200  1.00 71.65      A    C  
ANISOU 1575  CZ  PHE A 211     9154   9368   8701    114     91    299  A    C  
ATOM   1576  N   GLY A 212     127.451  98.413  26.918  1.00 85.96      A    N  
ANISOU 1576  N   GLY A 212    12419  10310   9930    208    154    129  A    N  
ATOM   1577  CA  GLY A 212     127.877  99.790  27.175  1.00 89.36      A    C  
ANISOU 1577  CA  GLY A 212    13184  10488  10277    152    143     82  A    C  
ATOM   1578  C   GLY A 212     129.234 100.095  26.566  1.00 94.76      A    C  
ANISOU 1578  C   GLY A 212    13866  11023  11114    -90    114     98  A    C  
ATOM   1579  O   GLY A 212     130.164 100.519  27.253  1.00 98.35      A    O  
ANISOU 1579  O   GLY A 212    14421  11339  11606   -308     -5     53  A    O  
ATOM   1580  N   CYS A 213     129.333  99.867  25.263  1.00 98.19      A    N  
ANISOU 1580  N   CYS A 213    14181  11497  11628    -59    224    164  A    N  
ATOM   1581  CA  CYS A 213     130.526 100.156  24.493  1.00100.32      A    C  
ANISOU 1581  CA  CYS A 213    14439  11644  12033   -270    244    194  A    C  
ATOM   1582  C   CYS A 213     130.110 100.955  23.260  1.00102.85      A    C  
ANISOU 1582  C   CYS A 213    14955  11855  12267   -129    403    246  A    C  
ATOM   1583  O   CYS A 213     128.931 101.021  22.909  1.00 98.85      A    O  
ANISOU 1583  O   CYS A 213    14504  11423  11630    140    484    266  A    O  
ATOM   1584  CB  CYS A 213     131.235  98.857  24.084  1.00 99.87      A    C  
ANISOU 1584  CB  CYS A 213    14003  11764  12176   -390    226    233  A    C  
ATOM   1585  SG  CYS A 213     130.248  97.681  23.081  1.00 97.12      A    S  
ANISOU 1585  SG  CYS A 213    13415  11659  11824   -159    340    290  A    S  
ATOM   1586  N   GLN A 214     131.086 101.564  22.602  1.00106.47      A    N  
ANISOU 1586  N   GLN A 214    15511  12144  12797   -316    446    275  A    N  
ATOM   1587  CA  GLN A 214     130.810 102.437  21.476  1.00104.55      A    C  
ANISOU 1587  CA  GLN A 214    15510  11753  12458   -205    589    332  A    C  
ATOM   1588  C   GLN A 214     130.194 101.694  20.266  1.00 98.79      A    C  
ANISOU 1588  C   GLN A 214    14600  11208  11725    -16    705    407  A    C  
ATOM   1589  O   GLN A 214     129.085 101.978  19.848  1.00 92.71      A    O  
ANISOU 1589  O   GLN A 214    13948  10467  10808    257    769    432  A    O  
ATOM   1590  CB  GLN A 214     132.108 103.163  21.096  1.00106.78      A    C  
ANISOU 1590  CB  GLN A 214    15923  11816  12830   -501    608    353  A    C  
ATOM   1591  CG  GLN A 214     132.016 103.999  19.836  1.00110.52      A    C  
ANISOU 1591  CG  GLN A 214    16649  12121  13221   -433    763    430  A    C  
ATOM   1592  CD  GLN A 214     133.350 104.547  19.419  1.00109.99      A    C  
ANISOU 1592  CD  GLN A 214    16659  11867  13262   -764    797    463  A    C  
ATOM   1593  NE2 GLN A 214     134.026 105.178  20.352  1.00112.33      A    N  
ANISOU 1593  NE2 GLN A 214    17094  11998  13588   -996    684    397  A    N  
ATOM   1594  OE1 GLN A 214     133.750 104.440  18.266  1.00106.70      A    O  
ANISOU 1594  OE1 GLN A 214    16195  11454  12890   -817    927    545  A    O  
ATOM   1595  N   ASP A 215     130.925 100.750  19.704  1.00100.22      A    N  
ANISOU 1595  N   ASP A 215    14497  11518  12063   -158    728    442  A    N  
ATOM   1596  CA  ASP A 215     130.470 100.009  18.529  1.00 99.95      A    C  
ANISOU 1596  CA  ASP A 215    14308  11646  12021    -13    831    505  A    C  
ATOM   1597  C   ASP A 215     130.730  98.549  18.819  1.00 97.34      A    C  
ANISOU 1597  C   ASP A 215    13606  11542  11836    -79    772    483  A    C  
ATOM   1598  O   ASP A 215     130.860  98.167  19.986  1.00 98.89      A    O  
ANISOU 1598  O   ASP A 215    13694  11788  12090   -151    647    426  A    O  
ATOM   1599  CB  ASP A 215     131.242 100.475  17.287  1.00108.69      A    C  
ANISOU 1599  CB  ASP A 215    15519  12624  13152   -125    964    578  A    C  
ATOM   1600  CG  ASP A 215     132.774 100.623  17.536  1.00110.72      A    C  
ANISOU 1600  CG  ASP A 215    15711  12774  13583   -471    950    571  A    C  
ATOM   1601  OD1 ASP A 215     133.367  99.828  18.312  1.00104.58      A    O  
ANISOU 1601  OD1 ASP A 215    14664  12112  12957   -613    850    524  A    O  
ATOM   1602  OD2 ASP A 215     133.381 101.550  16.945  1.00109.00      A    O1-
ANISOU 1602  OD2 ASP A 215    15711  12354  13350   -603   1036    616  A    O1-
ATOM   1603  N   LEU A 216     130.840  97.720  17.792  1.00 94.69      A    N  
ANISOU 1603  N   LEU A 216    13093  11334  11551    -57    857    527  A    N  
ATOM   1604  CA  LEU A 216     131.128  96.315  18.047  1.00 93.83      A    C  
ANISOU 1604  CA  LEU A 216    12657  11415  11579   -112    806    503  A    C  
ATOM   1605  C   LEU A 216     132.473  95.835  17.519  1.00 92.02      A    C  
ANISOU 1605  C   LEU A 216    12247  11189  11525   -316    869    524  A    C  
ATOM   1606  O   LEU A 216     132.681  94.638  17.388  1.00 88.47      A    O  
ANISOU 1606  O   LEU A 216    11548  10892  11175   -316    867    514  A    O  
ATOM   1607  CB  LEU A 216     130.015  95.465  17.448  1.00 94.54      A    C  
ANISOU 1607  CB  LEU A 216    12649  11688  11582    101    835    517  A    C  
ATOM   1608  CG  LEU A 216     128.639  95.717  18.042  1.00 91.74      A    C  
ANISOU 1608  CG  LEU A 216    12385  11393  11078    304    775    497  A    C  
ATOM   1609  CD1 LEU A 216     127.598  95.026  17.179  1.00 89.94      A    C  
ANISOU 1609  CD1 LEU A 216    12070  11341  10762    489    815    524  A    C  
ATOM   1610  CD2 LEU A 216     128.590  95.258  19.498  1.00 89.11      A    C  
ANISOU 1610  CD2 LEU A 216    11944  11114  10799    246    643    438  A    C  
ATOM   1611  N   ARG A 217     133.384  96.752  17.215  1.00 95.78      A    N  
ANISOU 1611  N   ARG A 217    12852  11499  12041   -489    932    552  A    N  
ATOM   1612  CA  ARG A 217     134.649  96.369  16.561  1.00 96.73      A    C  
ANISOU 1612  CA  ARG A 217    12792  11637  12321   -678   1030    584  A    C  
ATOM   1613  C   ARG A 217     135.478  95.479  17.474  1.00 94.14      A    C  
ANISOU 1613  C   ARG A 217    12157  11419  12192   -814    916    539  A    C  
ATOM   1614  O   ARG A 217     136.065  94.504  17.016  1.00 95.01      A    O  
ANISOU 1614  O   ARG A 217    12018  11654  12428   -840    980    549  A    O  
ATOM   1615  CB  ARG A 217     135.485  97.596  16.154  1.00 97.80      A    C  
ANISOU 1615  CB  ARG A 217    13129  11566  12463   -877   1116    628  A    C  
ATOM   1616  CG  ARG A 217     134.754  98.642  15.337  1.00 94.13      A    C  
ANISOU 1616  CG  ARG A 217    13022  10947  11796   -747   1216    681  A    C  
ATOM   1617  CD  ARG A 217     135.663  99.788  14.957  1.00 93.31      A    C  
ANISOU 1617  CD  ARG A 217    13127  10619  11707   -974   1303    729  A    C  
ATOM   1618  NE  ARG A 217     136.856  99.935  15.803  1.00 92.57      A    N  
ANISOU 1618  NE  ARG A 217    12896  10481  11795  -1276   1220    694  A    N  
ATOM   1619  CZ  ARG A 217     136.925 100.644  16.937  1.00 89.82      A    C  
ANISOU 1619  CZ  ARG A 217    12680  10002  11444  -1377   1066    637  A    C  
ATOM   1620  NH1 ARG A 217     135.863 101.262  17.444  1.00 87.20      A    N1+
ANISOU 1620  NH1 ARG A 217    12623   9571  10938  -1187    991    601  A    N1+
ATOM   1621  NH2 ARG A 217     138.079 100.727  17.578  1.00 89.52      A    N  
ANISOU 1621  NH2 ARG A 217    12493   9943  11576  -1670    985    612  A    N  
ATOM   1622  N   GLY A 218     135.529  95.822  18.760  1.00 92.35      A    N  
ANISOU 1622  N   GLY A 218    11962  11140  11985   -888    745    489  A    N  
ATOM   1623  CA  GLY A 218     136.260  95.017  19.743  1.00 93.46      A    C  
ANISOU 1623  CA  GLY A 218    11829  11380  12299   -999    602    452  A    C  
ATOM   1624  C   GLY A 218     135.895  93.529  19.729  1.00 88.58      A    C  
ANISOU 1624  C   GLY A 218    10969  10956  11731   -847    587    440  A    C  
ATOM   1625  O   GLY A 218     136.728  92.654  19.974  1.00 83.50      A    O  
ANISOU 1625  O   GLY A 218    10054  10410  11261   -919    545    434  A    O  
ATOM   1626  N   PHE A 219     134.634  93.246  19.435  1.00 87.79      A    N  
ANISOU 1626  N   PHE A 219    10969  10909  11477   -635    618    439  A    N  
ATOM   1627  CA  PHE A 219     134.164  91.867  19.323  1.00 83.52      A    C  
ANISOU 1627  CA  PHE A 219    10243  10530  10958   -500    612    427  A    C  
ATOM   1628  C   PHE A 219     134.436  91.297  17.927  1.00 80.07      A    C  
ANISOU 1628  C   PHE A 219     9718  10153  10550   -460    787    459  A    C  
ATOM   1629  O   PHE A 219     134.331  90.099  17.699  1.00 74.50      A    O  
ANISOU 1629  O   PHE A 219     8852   9563   9889   -381    799    445  A    O  
ATOM   1630  CB  PHE A 219     132.666  91.800  19.616  1.00 81.79      A    C  
ANISOU 1630  CB  PHE A 219    10155  10359  10562   -313    565    413  A    C  
ATOM   1631  CG  PHE A 219     132.287  92.285  20.975  1.00 81.50      A    C  
ANISOU 1631  CG  PHE A 219    10220  10276  10468   -325    416    380  A    C  
ATOM   1632  CD1 PHE A 219     133.018  91.914  22.093  1.00 84.92      A    C  
ANISOU 1632  CD1 PHE A 219    10528  10716  11022   -448    270    353  A    C  
ATOM   1633  CD2 PHE A 219     131.184  93.096  21.137  1.00 83.85      A    C  
ANISOU 1633  CD2 PHE A 219    10740  10534  10583   -201    423    376  A    C  
ATOM   1634  CE1 PHE A 219     132.664  92.369  23.355  1.00 90.84      A    C  
ANISOU 1634  CE1 PHE A 219    11400  11419  11693   -461    132    321  A    C  
ATOM   1635  CE2 PHE A 219     130.821  93.560  22.393  1.00 90.52      A    C  
ANISOU 1635  CE2 PHE A 219    11699  11336  11358   -202    305    339  A    C  
ATOM   1636  CZ  PHE A 219     131.560  93.195  23.510  1.00 91.29      A    C  
ANISOU 1636  CZ  PHE A 219    11696  11430  11559   -340    160    310  A    C  
ATOM   1637  N   GLY A 220     134.769  92.179  16.997  1.00 81.48      A    N  
ANISOU 1637  N   GLY A 220    10033  10237  10685   -516    927    501  A    N  
ATOM   1638  CA  GLY A 220     135.237  91.786  15.685  1.00 81.73      A    C  
ANISOU 1638  CA  GLY A 220    10002  10308  10740   -514   1109    536  A    C  
ATOM   1639  C   GLY A 220     134.107  91.696  14.706  1.00 79.47      A    C  
ANISOU 1639  C   GLY A 220     9873  10059  10262   -326   1188    555  A    C  
ATOM   1640  O   GLY A 220     134.066  90.776  13.920  1.00 79.20      A    O  
ANISOU 1640  O   GLY A 220     9746  10120  10223   -254   1272    552  A    O  
ATOM   1641  N   LEU A 221     133.217  92.678  14.725  1.00 81.53      A    N  
ANISOU 1641  N   LEU A 221    10378  10239  10360   -243   1160    573  A    N  
ATOM   1642  CA  LEU A 221     132.056  92.650  13.863  1.00 82.50      A    C  
ANISOU 1642  CA  LEU A 221    10637  10413  10296    -47   1205    596  A    C  
ATOM   1643  C   LEU A 221     131.969  93.865  12.947  1.00 90.47      A    C  
ANISOU 1643  C   LEU A 221    11918  11286  11168    -23   1316    664  A    C  
ATOM   1644  O   LEU A 221     132.534  93.861  11.854  1.00 93.94      A    O  
ANISOU 1644  O   LEU A 221    12392  11703  11596    -68   1464    709  A    O  
ATOM   1645  CB  LEU A 221     130.812  92.503  14.716  1.00 80.98      A    C  
ANISOU 1645  CB  LEU A 221    10456  10294  10017     94   1061    560  A    C  
ATOM   1646  CG  LEU A 221     130.679  91.162  15.463  1.00 81.71      A    C  
ANISOU 1646  CG  LEU A 221    10314  10525  10206     95    960    507  A    C  
ATOM   1647  CD1 LEU A 221     130.145  91.351  16.868  1.00 83.08      A    C  
ANISOU 1647  CD1 LEU A 221    10492  10700  10372    107    811    472  A    C  
ATOM   1648  CD2 LEU A 221     129.749  90.210  14.740  1.00 81.78      A    C  
ANISOU 1648  CD2 LEU A 221    10273  10677  10121    234    973    500  A    C  
ATOM   1649  N   ASP A 222     131.281  94.912  13.385  1.00104.37      A    N  
ANISOU 1649  N   ASP A 222    13890  12946  12816     56   1254    673  A    N  
ATOM   1650  CA  ASP A 222     130.878  96.023  12.479  1.00121.02      A    C  
ANISOU 1650  CA  ASP A 222    16297  14929  14756    153   1341    743  A    C  
ATOM   1651  C   ASP A 222     130.000  95.569  11.293  1.00109.79      A    C  
ANISOU 1651  C   ASP A 222    14907  13627  13179    349   1392    781  A    C  
ATOM   1652  O   ASP A 222     130.306  94.574  10.627  1.00 97.77      A    O  
ANISOU 1652  O   ASP A 222    13234  12218  11694    321   1453    775  A    O  
ATOM   1653  CB  ASP A 222     132.092  96.814  11.965  1.00134.60      A    C  
ANISOU 1653  CB  ASP A 222    18145  16468  16528    -50   1469    796  A    C  
ATOM   1654  CG  ASP A 222     132.324  98.107  12.738  1.00137.32      A    C  
ANISOU 1654  CG  ASP A 222    18709  16597  16868   -142   1420    793  A    C  
ATOM   1655  OD1 ASP A 222     131.585  98.381  13.732  1.00137.28      A    O  
ANISOU 1655  OD1 ASP A 222    18754  16586  16818    -40   1290    743  A    O  
ATOM   1656  OD2 ASP A 222     133.258  98.843  12.331  1.00129.95      A    O1-
ANISOU 1656  OD2 ASP A 222    17907  15497  15968   -328   1519    840  A    O1-
ATOM   1657  N   SER A 223     128.941  96.339  11.026  1.00104.01      A    N  
ANISOU 1657  N   SER A 223    14385  12863  12270    551   1365    817  A    N  
ATOM   1658  CA  SER A 223     127.818  95.878  10.199  1.00108.26      A    C  
ANISOU 1658  CA  SER A 223    14917  13559  12655    767   1346    840  A    C  
ATOM   1659  C   SER A 223     128.155  95.657   8.734  1.00116.39      A    C  
ANISOU 1659  C   SER A 223    16025  14593  13603    766   1468    901  A    C  
ATOM   1660  O   SER A 223     127.257  95.697   7.897  1.00118.14      A    O  
ANISOU 1660  O   SER A 223    16343  14891  13655    953   1452    943  A    O  
ATOM   1661  CB  SER A 223     126.649  96.864  10.269  1.00106.76      A    C  
ANISOU 1661  CB  SER A 223    14924  13336  12302   1003   1287    874  A    C  
ATOM   1662  OG  SER A 223     126.410  97.256  11.605  1.00113.56      A    O  
ANISOU 1662  OG  SER A 223    15770  14161  13216   1004   1203    821  A    O  
ATOM   1663  N   LYS A 224     129.433  95.426   8.422  1.00121.58      A    N  
ANISOU 1663  N   LYS A 224    16637  15183  14374    559   1590    908  A    N  
ATOM   1664  CA  LYS A 224     129.847  95.139   7.056  1.00116.08      A    C  
ANISOU 1664  CA  LYS A 224    16012  14497  13595    542   1732    960  A    C  
ATOM   1665  C   LYS A 224     129.254  93.789   6.663  1.00107.04      A    C  
ANISOU 1665  C   LYS A 224    14686  13569  12413    636   1684    909  A    C  
ATOM   1666  O   LYS A 224     128.103  93.724   6.243  1.00101.86      A    O  
ANISOU 1666  O   LYS A 224    14092  13011  11598    824   1599    922  A    O  
ATOM   1667  CB  LYS A 224     131.381  95.176   6.930  1.00119.24      A    C  
ANISOU 1667  CB  LYS A 224    16365  14794  14145    291   1890    974  A    C  
ATOM   1668  CG  LYS A 224     131.996  96.547   7.189  1.00126.70      A    C  
ANISOU 1668  CG  LYS A 224    17521  15507  15111    162   1940   1030  A    C  
ATOM   1669  CD  LYS A 224     131.716  97.517   6.039  1.00128.31      A    C  
ANISOU 1669  CD  LYS A 224    18076  15572  15102    255   2038   1140  A    C  
ATOM   1670  CE  LYS A 224     131.901  98.976   6.447  1.00128.14      A    C  
ANISOU 1670  CE  LYS A 224    18329  15297  15061    194   2037   1186  A    C  
ATOM   1671  NZ  LYS A 224     131.328  99.907   5.435  1.00126.52      A    N1+
ANISOU 1671  NZ  LYS A 224    18492  14955  14623    359   2090   1293  A    N1+
ATOM   1672  N   GLU A 225     130.003  92.706   6.822  1.00105.70      A    N  
ANISOU 1672  N   GLU A 225    14293  13475  12392    509   1728    849  A    N  
ATOM   1673  CA  GLU A 225     129.497  91.393   6.392  1.00109.17      A    C  
ANISOU 1673  CA  GLU A 225    14600  14091  12788    584   1690    794  A    C  
ATOM   1674  C   GLU A 225     128.713  90.729   7.496  1.00 97.75      A    C  
ANISOU 1674  C   GLU A 225    12966  12761  11413    630   1513    721  A    C  
ATOM   1675  O   GLU A 225     127.760  89.993   7.228  1.00 93.78      A    O  
ANISOU 1675  O   GLU A 225    12417  12399  10814    733   1425    690  A    O  
ATOM   1676  CB  GLU A 225     130.620  90.461   5.906  1.00115.79      A    C  
ANISOU 1676  CB  GLU A 225    15316  14951  13726    461   1839    762  A    C  
ATOM   1677  CG  GLU A 225     131.518  89.880   6.999  1.00118.44      A    C  
ANISOU 1677  CG  GLU A 225    15398  15289  14313    320   1825    699  A    C  
ATOM   1678  CD  GLU A 225     132.793  90.690   7.226  1.00122.17      A    C  
ANISOU 1678  CD  GLU A 225    15865  15629  14923    144   1943    742  A    C  
ATOM   1679  OE1 GLU A 225     132.701  91.936   7.321  1.00127.32      A    O  
ANISOU 1679  OE1 GLU A 225    16699  16155  15520    120   1938    803  A    O  
ATOM   1680  OE2 GLU A 225     133.887  90.077   7.311  1.00109.38      A    O1-
ANISOU 1680  OE2 GLU A 225    14058  14032  13469     26   2040    716  A    O1-
ATOM   1681  N   HIS A 226     129.110  91.039   8.728  1.00 90.37      A    N  
ANISOU 1681  N   HIS A 226    11937  11763  10633    538   1459    697  A    N  
ATOM   1682  CA  HIS A 226     128.528  90.461   9.943  1.00 83.45      A    C  
ANISOU 1682  CA  HIS A 226    10891  10978   9838    552   1305    634  A    C  
ATOM   1683  C   HIS A 226     127.155  91.003  10.324  1.00 78.92      A    C  
ANISOU 1683  C   HIS A 226    10387  10461   9136    709   1184    647  A    C  
ATOM   1684  O   HIS A 226     126.665  90.724  11.397  1.00 70.93      A    O  
ANISOU 1684  O   HIS A 226     9261   9511   8177    714   1074    606  A    O  
ATOM   1685  CB  HIS A 226     129.465  90.745  11.111  1.00 84.53      A    C  
ANISOU 1685  CB  HIS A 226    10937  11017  10161    402   1285    612  A    C  
ATOM   1686  CG  HIS A 226     130.787  90.069  10.991  1.00 87.95      A    C  
ANISOU 1686  CG  HIS A 226    11221  11433  10760    256   1379    591  A    C  
ATOM   1687  CD2 HIS A 226     131.108  88.758  10.902  1.00 87.44      A    C  
ANISOU 1687  CD2 HIS A 226    10979  11460  10781    240   1391    542  A    C  
ATOM   1688  ND1 HIS A 226     131.978  90.762  10.960  1.00 90.65      A    N  
ANISOU 1688  ND1 HIS A 226    11584  11654  11203    107   1479    625  A    N  
ATOM   1689  CE1 HIS A 226     132.976  89.905  10.861  1.00 92.47      A    C  
ANISOU 1689  CE1 HIS A 226    11625  11925  11581     14   1552    598  A    C  
ATOM   1690  NE2 HIS A 226     132.473  88.682  10.813  1.00 91.93      A    N  
ANISOU 1690  NE2 HIS A 226    11446  11977  11503    107   1504    546  A    N  
ATOM   1691  N   ALA A 227     126.546  91.818   9.474  1.00 82.88      A    N  
ANISOU 1691  N   ALA A 227    11080  10943   9464    845   1211    710  A    N  
ATOM   1692  CA  ALA A 227     125.300  92.458   9.843  1.00 83.56      A    C  
ANISOU 1692  CA  ALA A 227    11225  11084   9437   1017   1110    728  A    C  
ATOM   1693  C   ALA A 227     124.272  91.395  10.170  1.00 82.79      A    C  
ANISOU 1693  C   ALA A 227    10930  11198   9326   1071    993    679  A    C  
ATOM   1694  O   ALA A 227     123.552  91.492  11.152  1.00 82.62      A    O  
ANISOU 1694  O   ALA A 227    10831  11242   9318   1120    905    657  A    O  
ATOM   1695  CB  ALA A 227     124.812  93.363   8.721  1.00 88.09      A    C  
ANISOU 1695  CB  ALA A 227    12028  11617   9823   1180   1151    809  A    C  
ATOM   1696  N   VAL A 228     124.214  90.363   9.345  1.00 85.24      A    N  
ANISOU 1696  N   VAL A 228    11171  11612   9603   1049    996    659  A    N  
ATOM   1697  CA  VAL A 228     123.195  89.329   9.502  1.00 82.19      A    C  
ANISOU 1697  CA  VAL A 228    10620  11420   9186   1078    880    615  A    C  
ATOM   1698  C   VAL A 228     123.340  88.577  10.814  1.00 77.99      A    C  
ANISOU 1698  C   VAL A 228     9908  10910   8811    962    822    552  A    C  
ATOM   1699  O   VAL A 228     122.374  88.084  11.353  1.00 86.60      A    O  
ANISOU 1699  O   VAL A 228    10879  12141   9885    985    721    530  A    O  
ATOM   1700  CB  VAL A 228     123.243  88.331   8.332  1.00 79.80      A    C  
ANISOU 1700  CB  VAL A 228    10318  11191   8812   1054    899    594  A    C  
ATOM   1701  CG1 VAL A 228     124.482  87.485   8.426  1.00 80.11      A    C  
ANISOU 1701  CG1 VAL A 228    10295  11143   8998    896    986    542  A    C  
ATOM   1702  CG2 VAL A 228     122.011  87.448   8.296  1.00 78.21      A    C  
ANISOU 1702  CG2 VAL A 228     9988  11191   8536   1088    763    559  A    C  
ATOM   1703  N   SER A 229     124.547  88.500  11.337  1.00 78.27      A    N  
ANISOU 1703  N   SER A 229     9923  10815   8999    832    881    531  A    N  
ATOM   1704  CA  SER A 229     124.781  87.800  12.593  1.00 77.41      A    C  
ANISOU 1704  CA  SER A 229     9662  10713   9035    728    815    481  A    C  
ATOM   1705  C   SER A 229     124.608  88.771  13.775  1.00 73.14      A    C  
ANISOU 1705  C   SER A 229     9154  10117   8516    745    771    494  A    C  
ATOM   1706  O   SER A 229     124.293  88.357  14.875  1.00 68.87      A    O  
ANISOU 1706  O   SER A 229     8513   9624   8030    707    690    465  A    O  
ATOM   1707  CB  SER A 229     126.165  87.130  12.586  1.00 78.97      A    C  
ANISOU 1707  CB  SER A 229     9796  10818   9391    594    884    449  A    C  
ATOM   1708  OG  SER A 229     127.178  88.042  12.192  1.00 87.77      A    O  
ANISOU 1708  OG  SER A 229    11010  11797  10538    553    994    487  A    O  
ATOM   1709  N   ILE A 230     124.785  90.068  13.538  1.00 72.54      A    N  
ANISOU 1709  N   ILE A 230     9245   9932   8384    803    827    538  A    N  
ATOM   1710  CA  ILE A 230     124.510  91.070  14.568  1.00 70.52      A    C  
ANISOU 1710  CA  ILE A 230     9066   9612   8114    845    790    543  A    C  
ATOM   1711  C   ILE A 230     123.017  91.056  14.892  1.00 68.28      A    C  
ANISOU 1711  C   ILE A 230     8733   9494   7715    995    720    545  A    C  
ATOM   1712  O   ILE A 230     122.604  91.095  16.050  1.00 66.59      A    O  
ANISOU 1712  O   ILE A 230     8469   9313   7516    995    664    522  A    O  
ATOM   1713  CB  ILE A 230     124.990  92.475  14.146  1.00 71.48      A    C  
ANISOU 1713  CB  ILE A 230     9417   9556   8185    880    870    589  A    C  
ATOM   1714  CG1 ILE A 230     126.499  92.582  14.299  1.00 73.60      A    C  
ANISOU 1714  CG1 ILE A 230     9699   9666   8600    684    924    580  A    C  
ATOM   1715  CG2 ILE A 230     124.391  93.551  15.020  1.00 73.83      A    C  
ANISOU 1715  CG2 ILE A 230     9839   9797   8413    982    835    590  A    C  
ATOM   1716  CD1 ILE A 230     127.105  93.783  13.597  1.00 75.86      A    C  
ANISOU 1716  CD1 ILE A 230    10211   9771   8840    671   1026    633  A    C  
ATOM   1717  N   GLY A 231     122.203  90.988  13.859  1.00 70.06      A    N  
ANISOU 1717  N   GLY A 231     8963   9834   7820   1121    722    577  A    N  
ATOM   1718  CA  GLY A 231     120.760  90.902  14.059  1.00 73.91      A    C  
ANISOU 1718  CA  GLY A 231     9357  10517   8207   1258    653    584  A    C  
ATOM   1719  C   GLY A 231     120.330  89.638  14.790  1.00 72.20      A    C  
ANISOU 1719  C   GLY A 231     8931  10445   8055   1149    578    540  A    C  
ATOM   1720  O   GLY A 231     119.402  89.640  15.602  1.00 71.46      A    O  
ANISOU 1720  O   GLY A 231     8747  10472   7929   1199    534    536  A    O  
ATOM   1721  N   ALA A 232     121.026  88.554  14.518  1.00 71.79      A    N  
ANISOU 1721  N   ALA A 232     8812  10370   8091   1002    574    506  A    N  
ATOM   1722  CA  ALA A 232     120.706  87.295  15.161  1.00 72.22      A    C  
ANISOU 1722  CA  ALA A 232     8706  10526   8208    889    503    467  A    C  
ATOM   1723  C   ALA A 232     121.050  87.363  16.657  1.00 69.49      A    C  
ANISOU 1723  C   ALA A 232     8336  10110   7955    812    480    448  A    C  
ATOM   1724  O   ALA A 232     120.348  86.784  17.479  1.00 68.65      A    O  
ANISOU 1724  O   ALA A 232     8127  10108   7847    774    423    438  A    O  
ATOM   1725  CB  ALA A 232     121.452  86.153  14.485  1.00 72.46      A    C  
ANISOU 1725  CB  ALA A 232     8707  10516   8305    775    514    432  A    C  
ATOM   1726  N   ALA A 233     122.126  88.067  17.004  1.00 66.37      A    N  
ANISOU 1726  N   ALA A 233     8044   9540   7631    777    520    447  A    N  
ATOM   1727  CA  ALA A 233     122.459  88.271  18.408  1.00 65.48      A    C  
ANISOU 1727  CA  ALA A 233     7937   9356   7583    711    481    430  A    C  
ATOM   1728  C   ALA A 233     121.385  89.127  19.012  1.00 65.01      A    C  
ANISOU 1728  C   ALA A 233     7925   9370   7406    838    478    447  A    C  
ATOM   1729  O   ALA A 233     120.986  88.925  20.141  1.00 66.63      A    O  
ANISOU 1729  O   ALA A 233     8087   9622   7607    809    438    435  A    O  
ATOM   1730  CB  ALA A 233     123.822  88.932  18.576  1.00 65.64      A    C  
ANISOU 1730  CB  ALA A 233     8057   9183   7698    635    511    425  A    C  
ATOM   1731  N   GLY A 234     120.917  90.100  18.252  1.00 64.77      A    N  
ANISOU 1731  N   GLY A 234     7991   9346   7270    993    531    477  A    N  
ATOM   1732  CA  GLY A 234     119.922  91.006  18.763  1.00 66.28      A    C  
ANISOU 1732  CA  GLY A 234     8235   9600   7346   1154    546    492  A    C  
ATOM   1733  C   GLY A 234     118.683  90.249  19.116  1.00 64.25      A    C  
ANISOU 1733  C   GLY A 234     7794   9576   7042   1178    508    495  A    C  
ATOM   1734  O   GLY A 234     118.083  90.501  20.149  1.00 63.24      A    O  
ANISOU 1734  O   GLY A 234     7650   9506   6870   1218    512    489  A    O  
ATOM   1735  N   ALA A 235     118.292  89.343  18.234  1.00 65.99      A    N  
ANISOU 1735  N   ALA A 235     7883   9927   7260   1149    477    504  A    N  
ATOM   1736  CA  ALA A 235     117.030  88.631  18.401  1.00 70.53      A    C  
ANISOU 1736  CA  ALA A 235     8271  10740   7785   1154    436    513  A    C  
ATOM   1737  C   ALA A 235     117.127  87.771  19.641  1.00 72.40      A    C  
ANISOU 1737  C   ALA A 235     8434  10981   8093    988    402    488  A    C  
ATOM   1738  O   ALA A 235     116.178  87.648  20.410  1.00 82.37      A    O  
ANISOU 1738  O   ALA A 235     9598  12392   9307    998    403    499  A    O  
ATOM   1739  CB  ALA A 235     116.702  87.786  17.178  1.00 68.34      A    C  
ANISOU 1739  CB  ALA A 235     7897  10579   7489   1121    390    517  A    C  
ATOM   1740  N   LEU A 236     118.302  87.221  19.865  1.00 68.57      A    N  
ANISOU 1740  N   LEU A 236     8000  10331   7719    842    380    460  A    N  
ATOM   1741  CA  LEU A 236     118.524  86.380  21.028  1.00 67.10      A    C  
ANISOU 1741  CA  LEU A 236     7770  10120   7601    692    334    444  A    C  
ATOM   1742  C   LEU A 236     118.365  87.185  22.301  1.00 67.02      A    C  
ANISOU 1742  C   LEU A 236     7837  10083   7545    735    353    448  A    C  
ATOM   1743  O   LEU A 236     117.686  86.788  23.217  1.00 65.83      A    O  
ANISOU 1743  O   LEU A 236     7623  10030   7356    691    343    457  A    O  
ATOM   1744  CB  LEU A 236     119.946  85.829  20.960  1.00 67.63      A    C  
ANISOU 1744  CB  LEU A 236     7885  10006   7803    572    306    417  A    C  
ATOM   1745  CG  LEU A 236     120.336  84.576  21.729  1.00 64.29      A    C  
ANISOU 1745  CG  LEU A 236     7410   9546   7472    418    238    405  A    C  
ATOM   1746  CD1 LEU A 236     119.301  83.495  21.517  1.00 65.09      A    C  
ANISOU 1746  CD1 LEU A 236     7399   9800   7532    359    209    410  A    C  
ATOM   1747  CD2 LEU A 236     121.704  84.124  21.242  1.00 61.54      A    C  
ANISOU 1747  CD2 LEU A 236     7080   9045   7254    356    231    380  A    C  
ATOM   1748  N   LEU A 237     119.011  88.341  22.320  1.00 68.91      A    N  
ANISOU 1748  N   LEU A 237     8228  10176   7775    815    388    439  A    N  
ATOM   1749  CA  LEU A 237     119.045  89.225  23.464  1.00 65.05      A    C  
ANISOU 1749  CA  LEU A 237     7865   9616   7233    855    404    427  A    C  
ATOM   1750  C   LEU A 237     117.635  89.712  23.745  1.00 63.54      A    C  
ANISOU 1750  C   LEU A 237     7633   9604   6905   1010    466    446  A    C  
ATOM   1751  O   LEU A 237     117.308  89.975  24.864  1.00 64.94      A    O  
ANISOU 1751  O   LEU A 237     7858   9797   7020   1021    484    439  A    O  
ATOM   1752  CB  LEU A 237     119.963  90.414  23.147  1.00 67.36      A    C  
ANISOU 1752  CB  LEU A 237     8347   9709   7535    907    431    413  A    C  
ATOM   1753  CG  LEU A 237     120.739  91.082  24.269  1.00 67.99      A    C  
ANISOU 1753  CG  LEU A 237     8592   9617   7623    848    402    381  A    C  
ATOM   1754  CD1 LEU A 237     121.515  90.061  25.047  1.00 65.70      A    C  
ANISOU 1754  CD1 LEU A 237     8233   9288   7443    658    307    368  A    C  
ATOM   1755  CD2 LEU A 237     121.664  92.166  23.732  1.00 70.57      A    C  
ANISOU 1755  CD2 LEU A 237     9096   9745   7973    863    426    370  A    C  
ATOM   1756  N   ASN A 238     116.798  89.851  22.734  1.00 63.31      A    N  
ANISOU 1756  N   ASN A 238     7511   9720   6822   1139    499    473  A    N  
ATOM   1757  CA  ASN A 238     115.436  90.273  22.979  1.00 66.47      A    C  
ANISOU 1757  CA  ASN A 238     7828  10322   7104   1299    559    496  A    C  
ATOM   1758  C   ASN A 238     114.619  89.173  23.550  1.00 66.22      A    C  
ANISOU 1758  C   ASN A 238     7599  10488   7073   1178    541    512  A    C  
ATOM   1759  O   ASN A 238     113.884  89.378  24.512  1.00 70.18      A    O  
ANISOU 1759  O   ASN A 238     8071  11095   7498   1220    597    520  A    O  
ATOM   1760  CB  ASN A 238     114.764  90.763  21.720  1.00 71.25      A    C  
ANISOU 1760  CB  ASN A 238     8377  11041   7652   1485    580    528  A    C  
ATOM   1761  CG  ASN A 238     114.836  92.251  21.600  1.00 78.74      A    C  
ANISOU 1761  CG  ASN A 238     9525  11870   8522   1708    648    529  A    C  
ATOM   1762  ND2 ASN A 238     114.872  92.747  20.355  1.00 84.83      A    N  
ANISOU 1762  ND2 ASN A 238    10349  12614   9268   1838    647    557  A    N  
ATOM   1763  OD1 ASN A 238     114.872  92.963  22.615  1.00 80.65      A    O  
ANISOU 1763  OD1 ASN A 238     9900  12027   8713   1765    699    506  A    O  
ATOM   1764  N   TYR A 239     114.750  87.992  22.981  1.00 63.72      A    N  
ANISOU 1764  N   TYR A 239     7164  10214   6833   1020    471    515  A    N  
ATOM   1765  CA  TYR A 239     114.001  86.844  23.479  1.00 63.81      A    C  
ANISOU 1765  CA  TYR A 239     7007  10390   6848    870    446    533  A    C  
ATOM   1766  C   TYR A 239     114.341  86.527  24.949  1.00 64.97      A    C  
ANISOU 1766  C   TYR A 239     7232  10449   7003    745    447    528  A    C  
ATOM   1767  O   TYR A 239     113.479  86.142  25.733  1.00 65.57      A    O  
ANISOU 1767  O   TYR A 239     7214  10674   7023    688    480    554  A    O  
ATOM   1768  CB  TYR A 239     114.313  85.647  22.623  1.00 62.25      A    C  
ANISOU 1768  CB  TYR A 239     6738  10182   6733    715    364    524  A    C  
ATOM   1769  CG  TYR A 239     113.435  84.468  22.855  1.00 62.32      A    C  
ANISOU 1769  CG  TYR A 239     6579  10361   6737    553    330    542  A    C  
ATOM   1770  CD1 TYR A 239     112.104  84.500  22.522  1.00 64.38      A    C  
ANISOU 1770  CD1 TYR A 239     6653  10886   6924    600    348    574  A    C  
ATOM   1771  CD2 TYR A 239     113.950  83.304  23.363  1.00 65.01      A    C  
ANISOU 1771  CD2 TYR A 239     6953  10596   7151    348    274    533  A    C  
ATOM   1772  CE1 TYR A 239     111.281  83.403  22.723  1.00 66.00      A    C  
ANISOU 1772  CE1 TYR A 239     6699  11250   7126    415    315    593  A    C  
ATOM   1773  CE2 TYR A 239     113.151  82.192  23.567  1.00 67.78      A    C  
ANISOU 1773  CE2 TYR A 239     7182  11077   7494    176    242    553  A    C  
ATOM   1774  CZ  TYR A 239     111.809  82.252  23.238  1.00 67.36      A    C  
ANISOU 1774  CZ  TYR A 239     6938  11290   7366    195    264    581  A    C  
ATOM   1775  OH  TYR A 239     111.003  81.163  23.440  1.00 68.71      A    O  
ANISOU 1775  OH  TYR A 239     6982  11591   7529     -7    233    604  A    O  
ATOM   1776  N   ILE A 240     115.604  86.686  25.327  1.00 63.60      A    N  
ANISOU 1776  N   ILE A 240     7227  10042   6894    694    408    499  A    N  
ATOM   1777  CA  ILE A 240     115.995  86.542  26.713  1.00 62.29      A    C  
ANISOU 1777  CA  ILE A 240     7163   9784   6719    601    389    496  A    C  
ATOM   1778  C   ILE A 240     115.208  87.554  27.523  1.00 64.96      A    C  
ANISOU 1778  C   ILE A 240     7556  10206   6917    740    486    500  A    C  
ATOM   1779  O   ILE A 240     114.711  87.222  28.594  1.00 65.87      A    O  
ANISOU 1779  O   ILE A 240     7666  10394   6966    674    512    519  A    O  
ATOM   1780  CB  ILE A 240     117.500  86.795  26.893  1.00 63.10      A    C  
ANISOU 1780  CB  ILE A 240     7426   9636   6911    553    322    462  A    C  
ATOM   1781  CG1 ILE A 240     118.304  85.627  26.315  1.00 61.96      A    C  
ANISOU 1781  CG1 ILE A 240     7219   9415   6908    414    238    459  A    C  
ATOM   1782  CG2 ILE A 240     117.877  87.067  28.354  1.00 63.02      A    C  
ANISOU 1782  CG2 ILE A 240     7560   9529   6853    505    295    454  A    C  
ATOM   1783  CD1 ILE A 240     119.781  85.956  26.062  1.00 62.15      A    C  
ANISOU 1783  CD1 ILE A 240     7340   9231   7042    394    191    428  A    C  
ATOM   1784  N   ARG A 241     115.103  88.786  27.019  1.00 66.86      A    N  
ANISOU 1784  N   ARG A 241     7870  10428   7105    938    547    483  A    N  
ATOM   1785  CA  ARG A 241     114.443  89.873  27.745  1.00 71.01      A    C  
ANISOU 1785  CA  ARG A 241     8485  11002   7491   1110    651    476  A    C  
ATOM   1786  C   ARG A 241     112.971  89.607  27.927  1.00 70.69      A    C  
ANISOU 1786  C   ARG A 241     8242  11249   7367   1169    741    516  A    C  
ATOM   1787  O   ARG A 241     112.428  89.826  29.003  1.00 70.81      A    O  
ANISOU 1787  O   ARG A 241     8290  11335   7278   1196    822    519  A    O  
ATOM   1788  CB  ARG A 241     114.664  91.206  27.036  1.00 74.62      A    C  
ANISOU 1788  CB  ARG A 241     9083  11353   7914   1321    693    453  A    C  
ATOM   1789  CG  ARG A 241     113.710  92.320  27.402  1.00 80.33      A    C  
ANISOU 1789  CG  ARG A 241     9862  12169   8491   1567    819    448  A    C  
ATOM   1790  CD  ARG A 241     114.229  93.643  26.883  1.00 85.74      A    C  
ANISOU 1790  CD  ARG A 241    10775  12656   9145   1744    842    420  A    C  
ATOM   1791  NE  ARG A 241     115.146  94.285  27.832  1.00 93.26      A    N  
ANISOU 1791  NE  ARG A 241    12008  13361  10063   1689    823    365  A    N  
ATOM   1792  CZ  ARG A 241     116.470  94.401  27.675  1.00102.96      A    C  
ANISOU 1792  CZ  ARG A 241    13388  14347  11381   1548    731    337  A    C  
ATOM   1793  NH1 ARG A 241     117.101  93.903  26.600  1.00102.38      A    N1+
ANISOU 1793  NH1 ARG A 241    13224  14235  11439   1454    666    360  A    N1+
ATOM   1794  NH2 ARG A 241     117.180  95.028  28.614  1.00107.16      A    N  
ANISOU 1794  NH2 ARG A 241    14168  14680  11867   1497    705    286  A    N  
ATOM   1795  N   LEU A 242     112.337  89.107  26.885  1.00 71.47      A    N  
ANISOU 1795  N   LEU A 242     8127  11520   7506   1176    725    546  A    N  
ATOM   1796  CA  LEU A 242     110.914  88.796  26.947  1.00 76.30      A    C  
ANISOU 1796  CA  LEU A 242     8497  12435   8056   1208    798    589  A    C  
ATOM   1797  C   LEU A 242     110.594  87.626  27.882  1.00 73.31      A    C  
ANISOU 1797  C   LEU A 242     8031  12140   7680    967    792    619  A    C  
ATOM   1798  O   LEU A 242     109.524  87.585  28.485  1.00 78.97      A    O  
ANISOU 1798  O   LEU A 242     8613  13075   8316    981    893    652  A    O  
ATOM   1799  CB  LEU A 242     110.351  88.507  25.553  1.00 81.33      A    C  
ANISOU 1799  CB  LEU A 242     8929  13238   8735   1250    750    614  A    C  
ATOM   1800  CG  LEU A 242     109.943  89.734  24.716  1.00 93.75      A    C  
ANISOU 1800  CG  LEU A 242    10504  14866  10247   1552    797    617  A    C  
ATOM   1801  CD1 LEU A 242     111.088  90.558  24.105  1.00 96.85      A    C  
ANISOU 1801  CD1 LEU A 242    11150  14979  10666   1652    763    585  A    C  
ATOM   1802  CD2 LEU A 242     109.015  89.274  23.607  1.00103.03      A    C  
ANISOU 1802  CD2 LEU A 242    11413  16299  11434   1574    748    656  A    C  
ATOM   1803  N   THR A 243     111.515  86.693  28.045  1.00 68.32      A    N  
ANISOU 1803  N   THR A 243     7482  11337   7140    753    686    609  A    N  
ATOM   1804  CA  THR A 243     111.200  85.500  28.813  1.00 67.33      A    C  
ANISOU 1804  CA  THR A 243     7291  11272   7018    522    670    645  A    C  
ATOM   1805  C   THR A 243     111.645  85.547  30.244  1.00 66.59      A    C  
ANISOU 1805  C   THR A 243     7387  11049   6862    457    688    646  A    C  
ATOM   1806  O   THR A 243     110.984  84.983  31.080  1.00 69.10      A    O  
ANISOU 1806  O   THR A 243     7657  11480   7117    339    741    691  A    O  
ATOM   1807  CB  THR A 243     111.850  84.257  28.218  1.00 66.89      A    C  
ANISOU 1807  CB  THR A 243     7218  11108   7088    322    538    642  A    C  
ATOM   1808  CG2 THR A 243     111.365  84.043  26.821  1.00 67.41      A    C  
ANISOU 1808  CG2 THR A 243     7109  11307   7195    352    506    639  A    C  
ATOM   1809  OG1 THR A 243     113.270  84.410  28.210  1.00 65.89      A    O  
ANISOU 1809  OG1 THR A 243     7285  10709   7038    325    457    602  A    O  
ATOM   1810  N   GLN A 244     112.771  86.194  30.527  1.00 65.38      A    N  
ANISOU 1810  N   GLN A 244     7456  10661   6722    518    640    603  A    N  
ATOM   1811  CA  GLN A 244     113.342  86.169  31.864  1.00 64.82      A    C  
ANISOU 1811  CA  GLN A 244     7583  10447   6594    440    617    601  A    C  
ATOM   1812  C   GLN A 244     112.727  87.232  32.739  1.00 67.89      A    C  
ANISOU 1812  C   GLN A 244     8071  10907   6814    592    752    591  A    C  
ATOM   1813  O   GLN A 244     112.324  88.292  32.297  1.00 68.23      A    O  
ANISOU 1813  O   GLN A 244     8107  11010   6805    801    839    563  A    O  
ATOM   1814  CB  GLN A 244     114.863  86.363  31.817  1.00 62.07      A    C  
ANISOU 1814  CB  GLN A 244     7416   9827   6340    415    486    556  A    C  
ATOM   1815  CG  GLN A 244     115.632  85.201  31.226  1.00 59.91      A    C  
ANISOU 1815  CG  GLN A 244     7079   9457   6227    260    358    564  A    C  
ATOM   1816  CD  GLN A 244     115.178  83.803  31.710  1.00 60.10      A    C  
ANISOU 1816  CD  GLN A 244     7030   9548   6257     70    329    620  A    C  
ATOM   1817  NE2 GLN A 244     114.428  83.113  30.845  1.00 58.77      A    N  
ANISOU 1817  NE2 GLN A 244     6676   9524   6128     18    351    640  A    N  
ATOM   1818  OE1 GLN A 244     115.551  83.323  32.810  1.00 58.21      A    O  
ANISOU 1818  OE1 GLN A 244     6916   9213   5986    -36    273    645  A    O  
ATOM   1819  N   ASN A 245     112.723  86.945  34.017  1.00 74.09      A    N  
ANISOU 1819  N   ASN A 245     8980  11665   7503    492    764    611  A    N  
ATOM   1820  CA  ASN A 245     112.202  87.867  34.999  1.00 79.12      A    C  
ANISOU 1820  CA  ASN A 245     9750  12353   7958    621    898    596  A    C  
ATOM   1821  C   ASN A 245     112.998  89.178  35.043  1.00 77.31      A    C  
ANISOU 1821  C   ASN A 245     9760  11925   7688    786    876    518  A    C  
ATOM   1822  O   ASN A 245     112.465  90.232  34.735  1.00 81.52      A    O  
ANISOU 1822  O   ASN A 245    10302  12521   8150   1005    994    486  A    O  
ATOM   1823  CB  ASN A 245     112.204  87.190  36.372  1.00 79.73      A    C  
ANISOU 1823  CB  ASN A 245     9954  12407   7932    452    893    640  A    C  
ATOM   1824  CG  ASN A 245     111.540  88.028  37.401  1.00 81.41      A    C  
ANISOU 1824  CG  ASN A 245    10299  12700   7931    575   1056    628  A    C  
ATOM   1825  ND2 ASN A 245     112.173  88.135  38.563  1.00 84.72      A    N  
ANISOU 1825  ND2 ASN A 245    10992  12958   8238    514   1000    614  A    N  
ATOM   1826  OD1 ASN A 245     110.486  88.623  37.146  1.00 79.63      A    O  
ANISOU 1826  OD1 ASN A 245     9939  12681   7636    742   1231    628  A    O  
ATOM   1827  N   LEU A 246     114.261  89.102  35.445  1.00 73.34      A    N  
ANISOU 1827  N   LEU A 246     9451  11182   7232    678    721    489  A    N  
ATOM   1828  CA  LEU A 246     115.149  90.234  35.414  1.00 72.30      A    C  
ANISOU 1828  CA  LEU A 246     9540  10842   7089    778    669    415  A    C  
ATOM   1829  C   LEU A 246     116.030  90.044  34.152  1.00 71.77      A    C  
ANISOU 1829  C   LEU A 246     9377  10666   7223    738    554    405  A    C  
ATOM   1830  O   LEU A 246     116.359  88.914  33.797  1.00 70.00      A    O  
ANISOU 1830  O   LEU A 246     9011  10452   7133    588    462    443  A    O  
ATOM   1831  CB  LEU A 246     115.977  90.227  36.695  1.00 73.59      A    C  
ANISOU 1831  CB  LEU A 246     9954  10833   7170    659    559    394  A    C  
ATOM   1832  CG  LEU A 246     116.548  91.557  37.187  1.00 78.92      A    C  
ANISOU 1832  CG  LEU A 246    10926  11324   7734    757    544    312  A    C  
ATOM   1833  CD1 LEU A 246     117.590  92.167  36.222  1.00 81.61      A    C  
ANISOU 1833  CD1 LEU A 246    11303  11481   8222    772    444    264  A    C  
ATOM   1834  CD2 LEU A 246     115.421  92.541  37.470  1.00 80.93      A    C  
ANISOU 1834  CD2 LEU A 246    11261  11691   7796    979    756    283  A    C  
ATOM   1835  N   MET A 247     116.406  91.118  33.454  1.00 72.76      A    N  
ANISOU 1835  N   MET A 247     9593  10684   7369    874    567    355  A    N  
ATOM   1836  CA  MET A 247     117.310  90.994  32.279  1.00 69.48      A    C  
ANISOU 1836  CA  MET A 247     9109  10157   7132    829    474    349  A    C  
ATOM   1837  C   MET A 247     118.730  90.703  32.701  1.00 67.12      A    C  
ANISOU 1837  C   MET A 247     8918   9654   6930    653    308    329  A    C  
ATOM   1838  O   MET A 247     119.395  91.548  33.267  1.00 72.09      A    O  
ANISOU 1838  O   MET A 247     9763  10120   7507    653    262    280  A    O  
ATOM   1839  CB  MET A 247     117.320  92.269  31.448  1.00 72.25      A    C  
ANISOU 1839  CB  MET A 247     9557  10433   7461   1014    543    314  A    C  
ATOM   1840  CG  MET A 247     118.285  92.249  30.279  1.00 72.82      A    C  
ANISOU 1840  CG  MET A 247     9593  10381   7694    962    467    311  A    C  
ATOM   1841  SD  MET A 247     117.899  90.983  29.047  1.00 75.62      A    S  
ANISOU 1841  SD  MET A 247     9639  10911   8180    910    459    366  A    S  
ATOM   1842  CE  MET A 247     119.349  91.188  28.018  1.00 75.45      A    C  
ANISOU 1842  CE  MET A 247     9670  10679   8315    839    381    348  A    C  
ATOM   1843  N   PRO A 248     119.214  89.512  32.409  1.00 65.54      A    N  
ANISOU 1843  N   PRO A 248     8566   9462   6873    508    213    364  A    N  
ATOM   1844  CA  PRO A 248     120.480  89.097  32.955  1.00 67.83      A    C  
ANISOU 1844  CA  PRO A 248     8922   9593   7255    354     52    355  A    C  
ATOM   1845  C   PRO A 248     121.661  89.906  32.476  1.00 68.95      A    C  
ANISOU 1845  C   PRO A 248     9152   9555   7489    342    -13    308  A    C  
ATOM   1846  O   PRO A 248     121.748  90.245  31.315  1.00 67.94      A    O  
ANISOU 1846  O   PRO A 248     8960   9418   7433    404     44    303  A    O  
ATOM   1847  CB  PRO A 248     120.626  87.670  32.438  1.00 66.93      A    C  
ANISOU 1847  CB  PRO A 248     8606   9536   7286    249     -2    401  A    C  
ATOM   1848  CG  PRO A 248     119.802  87.630  31.211  1.00 65.33      A    C  
ANISOU 1848  CG  PRO A 248     8250   9469   7105    342    113    412  A    C  
ATOM   1849  CD  PRO A 248     118.643  88.501  31.520  1.00 66.16      A    C  
ANISOU 1849  CD  PRO A 248     8409   9689   7036    484    244    408  A    C  
ATOM   1850  N   GLN A 249     122.583  90.172  33.384  1.00 71.83      A    N  
ANISOU 1850  N   GLN A 249     9664   9780   7848    245   -140    281  A    N  
ATOM   1851  CA  GLN A 249     123.737  90.961  33.073  1.00 73.23      A    C  
ANISOU 1851  CA  GLN A 249     9927   9788   8109    194   -213    239  A    C  
ATOM   1852  C   GLN A 249     125.019  90.111  33.094  1.00 72.56      A    C  
ANISOU 1852  C   GLN A 249     9717   9637   8212     36   -376    254  A    C  
ATOM   1853  O   GLN A 249     126.122  90.644  33.186  1.00 74.78      A    O  
ANISOU 1853  O   GLN A 249    10060   9785   8566    -55   -476    224  A    O  
ATOM   1854  CB  GLN A 249     123.807  92.080  34.102  1.00 77.19      A    C  
ANISOU 1854  CB  GLN A 249    10707  10175   8444    205   -243    183  A    C  
ATOM   1855  CG  GLN A 249     122.605  92.998  34.047  1.00 78.56      A    C  
ANISOU 1855  CG  GLN A 249    11011  10402   8436    396    -67    160  A    C  
ATOM   1856  CD  GLN A 249     122.557  93.789  32.763  1.00 80.25      A    C  
ANISOU 1856  CD  GLN A 249    11220  10571   8701    505     35    149  A    C  
ATOM   1857  NE2 GLN A 249     123.620  94.530  32.480  1.00 85.53      A    N  
ANISOU 1857  NE2 GLN A 249    12009  11049   9437    425    -34    112  A    N  
ATOM   1858  OE1 GLN A 249     121.571  93.759  32.046  1.00 82.96      A    O  
ANISOU 1858  OE1 GLN A 249    11458  11047   9014    655    169    177  A    O  
ATOM   1859  N   HIS A 250     124.875  88.793  33.004  1.00 68.22      A    N  
ANISOU 1859  N   HIS A 250     8993   9181   7744      3   -400    305  A    N  
ATOM   1860  CA  HIS A 250     126.019  87.898  33.120  1.00 66.39      A    C  
ANISOU 1860  CA  HIS A 250     8643   8897   7683   -111   -550    325  A    C  
ATOM   1861  C   HIS A 250     126.485  87.317  31.804  1.00 67.54      A    C  
ANISOU 1861  C   HIS A 250     8587   9058   8013   -109   -504    336  A    C  
ATOM   1862  O   HIS A 250     127.358  86.462  31.796  1.00 73.05      A    O  
ANISOU 1862  O   HIS A 250     9163   9730   8862   -174   -602    355  A    O  
ATOM   1863  CB  HIS A 250     125.733  86.751  34.067  1.00 63.68      A    C  
ANISOU 1863  CB  HIS A 250     8285   8604   7304   -152   -633    373  A    C  
ATOM   1864  CG  HIS A 250     124.809  85.717  33.508  1.00 64.52      A    C  
ANISOU 1864  CG  HIS A 250     8261   8830   7422   -115   -534    415  A    C  
ATOM   1865  CD2 HIS A 250     124.858  84.362  33.539  1.00 65.21      A    C  
ANISOU 1865  CD2 HIS A 250     8246   8939   7591   -161   -587    461  A    C  
ATOM   1866  ND1 HIS A 250     123.631  86.043  32.864  1.00 65.05      A    N  
ANISOU 1866  ND1 HIS A 250     8305   9010   7398    -27   -368    413  A    N  
ATOM   1867  CE1 HIS A 250     123.003  84.937  32.508  1.00 63.55      A    C  
ANISOU 1867  CE1 HIS A 250     7994   8915   7237    -41   -330    452  A    C  
ATOM   1868  NE2 HIS A 250     123.724  83.902  32.904  1.00 65.21      A    N  
ANISOU 1868  NE2 HIS A 250     8170   9058   7547   -124   -455    479  A    N  
ATOM   1869  N   LEU A 251     125.940  87.775  30.694  1.00 67.85      A    N  
ANISOU 1869  N   LEU A 251     8600   9139   8038    -25   -357    327  A    N  
ATOM   1870  CA  LEU A 251     126.332  87.216  29.408  1.00 69.81      A    C  
ANISOU 1870  CA  LEU A 251     8683   9406   8434    -19   -302    336  A    C  
ATOM   1871  C   LEU A 251     127.739  87.649  29.083  1.00 74.32      A    C  
ANISOU 1871  C   LEU A 251     9223   9861   9151    -98   -355    317  A    C  
ATOM   1872  O   LEU A 251     127.989  88.820  28.817  1.00 82.66      A    O  
ANISOU 1872  O   LEU A 251    10388  10841  10176   -100   -315    293  A    O  
ATOM   1873  CB  LEU A 251     125.420  87.700  28.291  1.00 69.43      A    C  
ANISOU 1873  CB  LEU A 251     8634   9429   8314     95   -146    336  A    C  
ATOM   1874  CG  LEU A 251     123.981  87.218  28.347  1.00 65.87      A    C  
ANISOU 1874  CG  LEU A 251     8151   9131   7744    169    -79    358  A    C  
ATOM   1875  CD1 LEU A 251     123.313  87.576  27.045  1.00 65.64      A    C  
ANISOU 1875  CD1 LEU A 251     8079   9178   7681    277     45    361  A    C  
ATOM   1876  CD2 LEU A 251     123.938  85.738  28.592  1.00 63.27      A    C  
ANISOU 1876  CD2 LEU A 251     7706   8853   7481     95   -142    386  A    C  
ATOM   1877  N   ASP A 252     128.661  86.699  29.095  1.00 77.15      A    N  
ANISOU 1877  N   ASP A 252     9435  10207   9669   -163   -440    332  A    N  
ATOM   1878  CA  ASP A 252     130.067  87.032  28.917  1.00 74.79      A    C  
ANISOU 1878  CA  ASP A 252     9066   9824   9526   -254   -499    319  A    C  
ATOM   1879  C   ASP A 252     130.238  87.554  27.528  1.00 67.25      A    C  
ANISOU 1879  C   ASP A 252     8077   8857   8617   -231   -348    312  A    C  
ATOM   1880  O   ASP A 252     129.451  87.226  26.655  1.00 56.69      A    O  
ANISOU 1880  O   ASP A 252     6717   7588   7232   -140   -228    321  A    O  
ATOM   1881  CB  ASP A 252     131.026  85.863  29.254  1.00 80.10      A    C  
ANISOU 1881  CB  ASP A 252     9562  10503  10368   -300   -620    340  A    C  
ATOM   1882  CG  ASP A 252     130.677  84.554  28.544  1.00 80.90      A    C  
ANISOU 1882  CG  ASP A 252     9539  10670  10528   -224   -549    359  A    C  
ATOM   1883  OD1 ASP A 252     130.049  84.596  27.472  1.00 84.45      A    O  
ANISOU 1883  OD1 ASP A 252     9988  11161  10936   -164   -400    353  A    O  
ATOM   1884  OD2 ASP A 252     131.052  83.477  29.060  1.00 81.09      A    O1-
ANISOU 1884  OD2 ASP A 252     9482  10695  10634   -222   -651    382  A    O1-
ATOM   1885  N   GLY A 253     131.206  88.461  27.394  1.00 72.00      A    N  
ANISOU 1885  N   GLY A 253     8701   9367   9286   -325   -362    298  A    N  
ATOM   1886  CA  GLY A 253     131.594  89.089  26.130  1.00 74.54      A    C  
ANISOU 1886  CA  GLY A 253     9015   9649   9657   -336   -221    299  A    C  
ATOM   1887  C   GLY A 253     130.622  88.826  24.996  1.00 74.50      A    C  
ANISOU 1887  C   GLY A 253     9017   9714   9572   -201    -65    314  A    C  
ATOM   1888  O   GLY A 253     129.393  88.830  25.196  1.00 77.90      A    O  
ANISOU 1888  O   GLY A 253     9537  10205   9856    -97    -43    314  A    O  
ATOM   1889  N   LEU A 254     131.178  88.639  23.805  1.00 71.15      A    N  
ANISOU 1889  N   LEU A 254     8497   9294   9242   -208     45    326  A    N  
ATOM   1890  CA  LEU A 254     130.415  88.281  22.623  1.00 72.42      A    C  
ANISOU 1890  CA  LEU A 254     8655   9526   9336    -94    178    339  A    C  
ATOM   1891  C   LEU A 254     131.422  88.047  21.532  1.00 75.99      A    C  
ANISOU 1891  C   LEU A 254     8996   9961   9915   -140    282    350  A    C  
ATOM   1892  O   LEU A 254     131.859  88.965  20.864  1.00 81.49      A    O  
ANISOU 1892  O   LEU A 254     9768  10586  10608   -181    372    364  A    O  
ATOM   1893  CB  LEU A 254     129.451  89.389  22.188  1.00 74.80      A    C  
ANISOU 1893  CB  LEU A 254     9149   9807   9464     -1    259    348  A    C  
ATOM   1894  CG  LEU A 254     128.738  89.122  20.841  1.00 77.02      A    C  
ANISOU 1894  CG  LEU A 254     9426  10166   9671    115    382    367  A    C  
ATOM   1895  CD1 LEU A 254     127.910  87.870  20.918  1.00 76.00      A    C  
ANISOU 1895  CD1 LEU A 254     9187  10171   9517    173    348    360  A    C  
ATOM   1896  CD2 LEU A 254     127.862  90.269  20.366  1.00 80.54      A    C  
ANISOU 1896  CD2 LEU A 254    10057  10590   9951    229    452    385  A    C  
ATOM   1897  N   SER A 255     131.845  86.814  21.378  1.00 80.21      A    N  
ANISOU 1897  N   SER A 255     9359  10553  10564   -135    276    345  A    N  
ATOM   1898  CA  SER A 255     132.935  86.520  20.477  1.00 82.82      A    C  
ANISOU 1898  CA  SER A 255     9561  10875  11028   -177    381    350  A    C  
ATOM   1899  C   SER A 255     132.414  86.025  19.142  1.00 81.63      A    C  
ANISOU 1899  C   SER A 255     9432  10778  10803    -78    526    351  A    C  
ATOM   1900  O   SER A 255     131.397  85.342  19.054  1.00 73.43      A    O  
ANISOU 1900  O   SER A 255     8426   9805   9669     12    505    339  A    O  
ATOM   1901  CB  SER A 255     133.868  85.477  21.110  1.00 89.25      A    C  
ANISOU 1901  CB  SER A 255    10170  11715  12023   -210    292    340  A    C  
ATOM   1902  OG  SER A 255     133.138  84.541  21.909  1.00 93.08      A    O  
ANISOU 1902  OG  SER A 255    10656  12239  12469   -144    174    329  A    O  
ATOM   1903  N   LEU A 256     133.136  86.397  18.097  1.00 87.25      A    N  
ANISOU 1903  N   LEU A 256    10135  11462  11552   -111    672    367  A    N  
ATOM   1904  CA  LEU A 256     132.878  85.902  16.755  1.00 86.29      A    C  
ANISOU 1904  CA  LEU A 256    10038  11385  11363    -29    817    366  A    C  
ATOM   1905  C   LEU A 256     133.576  84.571  16.599  1.00 83.85      A    C  
ANISOU 1905  C   LEU A 256     9552  11118  11189     -9    846    337  A    C  
ATOM   1906  O   LEU A 256     134.782  84.481  16.785  1.00 83.89      A    O  
ANISOU 1906  O   LEU A 256     9403  11108  11361    -79    870    341  A    O  
ATOM   1907  CB  LEU A 256     133.422  86.887  15.721  1.00 86.36      A    C  
ANISOU 1907  CB  LEU A 256    10133  11336  11344    -79    975    404  A    C  
ATOM   1908  CG  LEU A 256     133.455  86.409  14.281  1.00 87.90      A    C  
ANISOU 1908  CG  LEU A 256    10352  11567  11475    -15   1145    407  A    C  
ATOM   1909  CD1 LEU A 256     132.027  86.229  13.786  1.00 89.36      A    C  
ANISOU 1909  CD1 LEU A 256    10682  11809  11461    115   1118    401  A    C  
ATOM   1910  CD2 LEU A 256     134.190  87.426  13.418  1.00 96.36      A    C  
ANISOU 1910  CD2 LEU A 256    11507  12567  12537    -95   1305    458  A    C  
ATOM   1911  N   GLU A 257     132.834  83.528  16.263  1.00 81.51      A    N  
ANISOU 1911  N   GLU A 257     9274  10875  10822     87    841    307  A    N  
ATOM   1912  CA  GLU A 257     133.481  82.259  15.988  1.00 80.12      A    C  
ANISOU 1912  CA  GLU A 257     8970  10715  10755    128    889    272  A    C  
ATOM   1913  C   GLU A 257     133.844  82.146  14.523  1.00 79.00      A    C  
ANISOU 1913  C   GLU A 257     8862  10585  10569    165   1090    265  A    C  
ATOM   1914  O   GLU A 257     133.013  82.305  13.641  1.00 76.36      A    O  
ANISOU 1914  O   GLU A 257     8678  10272  10062    210   1145    264  A    O  
ATOM   1915  CB  GLU A 257     132.641  81.075  16.430  1.00 79.60      A    C  
ANISOU 1915  CB  GLU A 257     8922  10674  10649    194    780    237  A    C  
ATOM   1916  CG  GLU A 257     133.075  80.530  17.785  1.00 82.51      A    C  
ANISOU 1916  CG  GLU A 257     9175  11017  11158    174    629    237  A    C  
ATOM   1917  CD  GLU A 257     132.474  79.171  18.087  1.00 83.74      A    C  
ANISOU 1917  CD  GLU A 257     9354  11169  11292    234    552    205  A    C  
ATOM   1918  OE1 GLU A 257     132.559  78.763  19.276  1.00 89.05      A    O  
ANISOU 1918  OE1 GLU A 257     9982  11815  12036    222    405    216  A    O  
ATOM   1919  OE2 GLU A 257     131.917  78.531  17.150  1.00 74.45      A    O1-
ANISOU 1919  OE2 GLU A 257     8262  10007  10018    286    628    170  A    O1-
ATOM   1920  N   THR A 258     135.124  81.907  14.298  1.00 80.00      A    N  
ANISOU 1920  N   THR A 258     8837  10705  10853    143   1197    264  A    N  
ATOM   1921  CA  THR A 258     135.647  81.672  12.994  1.00 82.04      A    C  
ANISOU 1921  CA  THR A 258     9107  10978  11087    178   1409    255  A    C  
ATOM   1922  C   THR A 258     135.830  80.173  12.889  1.00 87.53      A    C  
ANISOU 1922  C   THR A 258     9729  11688  11837    287   1428    193  A    C  
ATOM   1923  O   THR A 258     135.933  79.465  13.892  1.00 85.26      A    O  
ANISOU 1923  O   THR A 258     9337  11391  11664    313   1290    174  A    O  
ATOM   1924  CB  THR A 258     137.002  82.397  12.778  1.00 87.11      A    C  
ANISOU 1924  CB  THR A 258     9610  11615  11871     77   1547    297  A    C  
ATOM   1925  CG2 THR A 258     136.962  83.833  13.343  1.00 89.51      A    C  
ANISOU 1925  CG2 THR A 258     9969  11870  12167    -57   1468    353  A    C  
ATOM   1926  OG1 THR A 258     138.080  81.681  13.399  1.00 90.17      A    O  
ANISOU 1926  OG1 THR A 258     9747  12030  12482     83   1531    280  A    O  
ATOM   1927  N   ASP A 259     135.913  79.689  11.661  1.00 95.85      A    N  
ANISOU 1927  N   ASP A 259    10859  12753  12803    355   1603    162  A    N  
ATOM   1928  CA  ASP A 259     136.044  78.267  11.425  1.00 97.10      A    C  
ANISOU 1928  CA  ASP A 259    11001  12903  12987    472   1641     92  A    C  
ATOM   1929  C   ASP A 259     137.452  77.785  11.762  1.00 92.96      A    C  
ANISOU 1929  C   ASP A 259    10233  12388  12698    509   1720     87  A    C  
ATOM   1930  O   ASP A 259     137.667  76.608  11.988  1.00104.55      A    O  
ANISOU 1930  O   ASP A 259    11652  13832  14240    621   1702     35  A    O  
ATOM   1931  CB  ASP A 259     135.712  77.962   9.973  1.00105.43      A    C  
ANISOU 1931  CB  ASP A 259    12237  13967  13854    533   1808     55  A    C  
ATOM   1932  CG  ASP A 259     134.362  78.527   9.548  1.00114.86      A    C  
ANISOU 1932  CG  ASP A 259    13648  15176  14816    504   1725     70  A    C  
ATOM   1933  OD1 ASP A 259     134.086  79.721   9.809  1.00125.09      A    O  
ANISOU 1933  OD1 ASP A 259    14963  16481  16083    427   1673    136  A    O  
ATOM   1934  OD2 ASP A 259     133.574  77.785   8.932  1.00125.88      A    O1-
ANISOU 1934  OD2 ASP A 259    15196  16575  16056    559   1709     15  A    O1-
ATOM   1935  N   SER A 260     138.404  78.697  11.832  1.00 86.17      A    N  
ANISOU 1935  N   SER A 260     9218  11560  11960    415   1799    142  A    N  
ATOM   1936  CA  SER A 260     139.787  78.332  12.048  1.00 86.55      A    C  
ANISOU 1936  CA  SER A 260     8996  11649  12237    443   1888    145  A    C  
ATOM   1937  C   SER A 260     140.127  77.943  13.474  1.00 85.34      A    C  
ANISOU 1937  C   SER A 260     8658  11494  12273    457   1673    152  A    C  
ATOM   1938  O   SER A 260     141.251  77.514  13.731  1.00 90.79      A    O  
ANISOU 1938  O   SER A 260     9099  12230  13165    508   1718    154  A    O  
ATOM   1939  CB  SER A 260     140.682  79.512  11.664  1.00 88.94      A    C  
ANISOU 1939  CB  SER A 260     9187  11997  12609    297   2034    211  A    C  
ATOM   1940  OG  SER A 260     140.409  80.639  12.496  1.00 85.97      A    O  
ANISOU 1940  OG  SER A 260     8828  11593  12240    144   1862    264  A    O  
ATOM   1941  N   GLN A 261     139.199  78.135  14.405  1.00 83.38      A    N  
ANISOU 1941  N   GLN A 261     8517  11203  11959    413   1442    162  A    N  
ATOM   1942  CA  GLN A 261     139.532  78.021  15.830  1.00 84.34      A    C  
ANISOU 1942  CA  GLN A 261     8487  11322  12237    394   1223    184  A    C  
ATOM   1943  C   GLN A 261     139.548  76.585  16.328  1.00 86.31      A    C  
ANISOU 1943  C   GLN A 261     8701  11535  12555    556   1137    144  A    C  
ATOM   1944  O   GLN A 261     140.347  76.197  17.181  1.00 80.03      A    O  
ANISOU 1944  O   GLN A 261     7706  10755  11945    600   1034    161  A    O  
ATOM   1945  CB  GLN A 261     138.531  78.792  16.677  1.00 82.65      A    C  
ANISOU 1945  CB  GLN A 261     8420  11074  11909    288   1024    212  A    C  
ATOM   1946  CG  GLN A 261     138.238  80.222  16.267  1.00 83.19      A    C  
ANISOU 1946  CG  GLN A 261     8597  11142  11868    152   1080    248  A    C  
ATOM   1947  CD  GLN A 261     137.357  80.908  17.298  1.00 88.22      A    C  
ANISOU 1947  CD  GLN A 261     9355  11745  12417     77    877    269  A    C  
ATOM   1948  NE2 GLN A 261     137.947  81.210  18.443  1.00 93.80      A    N  
ANISOU 1948  NE2 GLN A 261     9935  12450  13253      4    722    291  A    N  
ATOM   1949  OE1 GLN A 261     136.158  81.128  17.095  1.00 89.51      A    O  
ANISOU 1949  OE1 GLN A 261     9718  11893  12395     93    855    263  A    O  
ATOM   1950  N   TYR A 262     138.618  75.807  15.799  1.00 57.42      A    N  
ATOM   1951  CA  TYR A 262     138.420  74.437  16.235  1.00 55.73      A    C  
ATOM   1952  C   TYR A 262     138.479  73.465  15.078  1.00 50.06      A    C  
ATOM   1953  O   TYR A 262     138.120  73.779  13.920  1.00 52.35      A    O  
ATOM   1954  CB  TYR A 262     137.043  74.311  16.919  1.00 68.09      A    C  
ATOM   1955  CG  TYR A 262     136.754  75.402  17.969  1.00 69.01      A    C  
ATOM   1956  CD1 TYR A 262     137.452  75.441  19.197  1.00 63.09      A    C  
ATOM   1957  CD2 TYR A 262     135.801  76.387  17.723  1.00 55.72      A    C  
ATOM   1958  CE1 TYR A 262     137.211  76.442  20.105  1.00 58.69      A    C  
ATOM   1959  CE2 TYR A 262     135.542  77.377  18.646  1.00 54.20      A    C  
ATOM   1960  CZ  TYR A 262     136.248  77.406  19.811  1.00 60.18      A    C  
ATOM   1961  OH  TYR A 262     135.962  78.419  20.665  1.00 78.15      A    O  
ATOM   1962  N   ILE A 263     138.917  72.262  15.401  1.00 76.60      A    N  
ANISOU 1962  N   ILE A 263     9955   9439   9707    331   1649   -186  A    N  
ATOM   1963  CA  ILE A 263     138.877  71.160  14.451  1.00 69.97      A    C  
ANISOU 1963  CA  ILE A 263     9243   8516   8824    273   1753   -160  A    C  
ATOM   1964  C   ILE A 263     137.438  70.828  14.098  1.00 69.03      A    C  
ANISOU 1964  C   ILE A 263     9179   8423   8625    339   1605   -180  A    C  
ATOM   1965  O   ILE A 263     136.686  70.291  14.891  1.00 72.63      A    O  
ANISOU 1965  O   ILE A 263     9455   9018   9121    399   1551   -188  A    O  
ATOM   1966  CB  ILE A 263     139.547  69.940  15.040  1.00 65.64      A    C  
ANISOU 1966  CB  ILE A 263     8515   8033   8391    243   1912   -124  A    C  
ATOM   1967  CG1 ILE A 263     141.018  70.274  15.250  1.00 68.76      A    C  
ANISOU 1967  CG1 ILE A 263     8858   8382   8885    176   2056   -128  A    C  
ATOM   1968  CG2 ILE A 263     139.344  68.761  14.123  1.00 65.14      A    C  
ANISOU 1968  CG2 ILE A 263     8569   7898   8280    197   2003   -104  A    C  
ATOM   1969  CD1 ILE A 263     141.893  69.094  15.602  1.00 72.22      A    C  
ANISOU 1969  CD1 ILE A 263     9146   8837   9457    140   2219   -113  A    C  
ATOM   1970  N   GLY A 264     137.042  71.196  12.904  1.00 68.06      A    N  
ANISOU 1970  N   GLY A 264     9318   8155   8384    320   1530   -197  A    N  
ATOM   1971  CA  GLY A 264     135.670  71.024  12.511  1.00 68.47      A    C  
ANISOU 1971  CA  GLY A 264     9427   8212   8372    391   1359   -234  A    C  
ATOM   1972  C   GLY A 264     135.335  69.571  12.372  1.00 65.63      A    C  
ANISOU 1972  C   GLY A 264     9022   7891   8023    372   1448   -201  A    C  
ATOM   1973  O   GLY A 264     136.179  68.787  12.039  1.00 64.97      A    O  
ANISOU 1973  O   GLY A 264     8981   7752   7949    289   1630   -153  A    O  
ATOM   1974  N   MET A 265     134.083  69.237  12.642  1.00 66.99      A    N  
ANISOU 1974  N   MET A 265     9097   8158   8197    447   1316   -243  A    N  
ATOM   1975  CA  MET A 265     133.561  67.891  12.488  1.00 67.92      A    C  
ANISOU 1975  CA  MET A 265     9180   8312   8314    433   1369   -219  A    C  
ATOM   1976  C   MET A 265     132.119  68.043  12.077  1.00 68.79      A    C  
ANISOU 1976  C   MET A 265     9335   8422   8379    507   1165   -295  A    C  
ATOM   1977  O   MET A 265     131.394  68.828  12.659  1.00 71.09      A    O  
ANISOU 1977  O   MET A 265     9504   8800   8705    586   1015   -376  A    O  
ATOM   1978  CB  MET A 265     133.637  67.125  13.809  1.00 69.16      A    C  
ANISOU 1978  CB  MET A 265     9059   8650   8569    439   1457   -195  A    C  
ATOM   1979  CG  MET A 265     135.048  67.086  14.380  1.00 72.11      A    C  
ANISOU 1979  CG  MET A 265     9352   9027   9017    388   1618   -141  A    C  
ATOM   1980  SD  MET A 265     135.148  66.593  16.109  1.00 75.07      A    S  
ANISOU 1980  SD  MET A 265     9425   9596   9500    408   1652   -124  A    S  
ATOM   1981  CE  MET A 265     134.731  64.880  15.879  1.00 76.53      A    C  
ANISOU 1981  CE  MET A 265     9611   9792   9675    374   1725    -81  A    C  
ATOM   1982  N   ASP A 266     131.702  67.314  11.055  1.00 70.62      A    N  
ANISOU 1982  N   ASP A 266     9740   8551   8542    483   1151   -282  A    N  
ATOM   1983  CA  ASP A 266     130.325  67.390  10.610  1.00 71.53      A    C  
ANISOU 1983  CA  ASP A 266     9896   8652   8630    556    943   -365  A    C  
ATOM   1984  C   ASP A 266     129.458  66.655  11.616  1.00 70.33      A    C  
ANISOU 1984  C   ASP A 266     9463   8701   8559    588    946   -405  A    C  
ATOM   1985  O   ASP A 266     129.956  65.945  12.501  1.00 67.27      A    O  
ANISOU 1985  O   ASP A 266     8908   8431   8220    545   1107   -348  A    O  
ATOM   1986  CB  ASP A 266     130.153  66.804   9.211  1.00 74.67      A    C  
ANISOU 1986  CB  ASP A 266    10579   8867   8924    514    922   -337  A    C  
ATOM   1987  CG  ASP A 266     130.795  65.434   9.068  1.00 83.39      A    C  
ANISOU 1987  CG  ASP A 266    11692   9972  10019    423   1149   -246  A    C  
ATOM   1988  OD1 ASP A 266     132.055  65.347   8.956  1.00 98.10      A    O  
ANISOU 1988  OD1 ASP A 266    13622  11776  11873    341   1336   -179  A    O  
ATOM   1989  OD2 ASP A 266     130.043  64.433   9.063  1.00 89.35      A    O1-
ANISOU 1989  OD2 ASP A 266    12382  10783  10784    433   1139   -249  A    O1-
ATOM   1990  N   ALA A 267     128.149  66.836  11.478  1.00 70.74      A    N  
ANISOU 1990  N   ALA A 267     9471   8782   8624    661    759   -515  A    N  
ATOM   1991  CA  ALA A 267     127.190  66.246  12.412  1.00 68.04      A    C  
ANISOU 1991  CA  ALA A 267     8866   8629   8353    677    756   -581  A    C  
ATOM   1992  C   ALA A 267     127.394  64.761  12.498  1.00 63.82      A    C  
ANISOU 1992  C   ALA A 267     8310   8135   7804    599    926   -489  A    C  
ATOM   1993  O   ALA A 267     127.507  64.228  13.596  1.00 62.57      A    O  
ANISOU 1993  O   ALA A 267     7957   8127   7688    561   1040   -464  A    O  
ATOM   1994  CB  ALA A 267     125.756  66.557  12.000  1.00 70.04      A    C  
ANISOU 1994  CB  ALA A 267     9098   8879   8634    758    533   -730  A    C  
ATOM   1995  N   ALA A 268     127.440  64.107  11.337  1.00 63.26      A    N  
ANISOU 1995  N   ALA A 268     8456   7916   7665    570    933   -440  A    N  
ATOM   1996  CA  ALA A 268     127.566  62.659  11.287  1.00 62.77      A    C  
ANISOU 1996  CA  ALA A 268     8392   7871   7586    502   1077   -360  A    C  
ATOM   1997  C   ALA A 268     128.861  62.185  11.954  1.00 61.25      A    C  
ANISOU 1997  C   ALA A 268     8136   7716   7419    439   1288   -253  A    C  
ATOM   1998  O   ALA A 268     128.886  61.179  12.648  1.00 62.23      A    O  
ANISOU 1998  O   ALA A 268     8131   7937   7574    398   1390   -212  A    O  
ATOM   1999  CB  ALA A 268     127.483  62.174   9.869  1.00 63.14      A    C  
ANISOU 1999  CB  ALA A 268     8706   7734   7547    483   1046   -330  A    C  
ATOM   2000  N   THR A 269     129.927  62.945  11.806  1.00 60.02      A    N  
ANISOU 2000  N   THR A 269     8063   7480   7260    429   1341   -218  A    N  
ATOM   2001  CA  THR A 269     131.143  62.585  12.481  1.00 59.61      A    C  
ANISOU 2001  CA  THR A 269     7925   7463   7261    379   1519   -142  A    C  
ATOM   2002  C   THR A 269     131.032  62.678  13.992  1.00 59.98      A    C  
ANISOU 2002  C   THR A 269     7713   7692   7383    396   1521   -157  A    C  
ATOM   2003  O   THR A 269     131.611  61.848  14.699  1.00 60.56      A    O  
ANISOU 2003  O   THR A 269     7685   7820   7502    357   1636    -96  A    O  
ATOM   2004  CB  THR A 269     132.298  63.432  12.003  1.00 59.57      A    C  
ANISOU 2004  CB  THR A 269     8052   7335   7243    354   1580   -119  A    C  
ATOM   2005  CG2 THR A 269     133.559  63.124  12.823  1.00 57.71      A    C  
ANISOU 2005  CG2 THR A 269     7683   7145   7097    314   1748    -64  A    C  
ATOM   2006  OG1 THR A 269     132.488  63.152  10.604  1.00 60.14      A    O  
ANISOU 2006  OG1 THR A 269     8395   7228   7228    307   1614    -98  A    O  
ATOM   2007  N   ARG A 270     130.306  63.668  14.509  1.00 59.99      A    N  
ANISOU 2007  N   ARG A 270     7614   7781   7396    451   1388   -241  A    N  
ATOM   2008  CA  ARG A 270     130.153  63.756  15.970  1.00 59.20      A    C  
ANISOU 2008  CA  ARG A 270     7286   7854   7351    450   1398   -261  A    C  
ATOM   2009  C   ARG A 270     129.400  62.520  16.451  1.00 62.45      A    C  
ANISOU 2009  C   ARG A 270     7606   8366   7756    408   1432   -257  A    C  
ATOM   2010  O   ARG A 270     129.721  61.978  17.513  1.00 63.21      A    O  
ANISOU 2010  O   ARG A 270     7586   8553   7877    364   1508   -214  A    O  
ATOM   2011  CB  ARG A 270     129.441  65.032  16.395  1.00 56.90      A    C  
ANISOU 2011  CB  ARG A 270     6903   7638   7074    513   1258   -374  A    C  
ATOM   2012  CG  ARG A 270     130.291  66.256  16.235  1.00 56.45      A    C  
ANISOU 2012  CG  ARG A 270     6915   7504   7027    545   1232   -368  A    C  
ATOM   2013  CD  ARG A 270     129.498  67.495  16.567  1.00 57.40      A    C  
ANISOU 2013  CD  ARG A 270     6954   7688   7166    618   1074   -492  A    C  
ATOM   2014  NE  ARG A 270     130.178  68.700  16.125  1.00 58.92      A    N  
ANISOU 2014  NE  ARG A 270     7266   7771   7351    653   1016   -492  A    N  
ATOM   2015  CZ  ARG A 270     131.307  69.162  16.660  1.00 60.89      A    C  
ANISOU 2015  CZ  ARG A 270     7489   8019   7626    630   1100   -433  A    C  
ATOM   2016  NH1 ARG A 270     131.859  70.268  16.212  1.00 63.43      A    N1+
ANISOU 2016  NH1 ARG A 270     7930   8236   7932    653   1044   -440  A    N1+
ATOM   2017  NH2 ARG A 270     131.911  68.528  17.636  1.00 62.55      A    N  
ANISOU 2017  NH2 ARG A 270     7565   8321   7878    582   1228   -368  A    N  
ATOM   2018  N   ARG A 271     128.411  62.081  15.663  1.00 63.09      A    N  
ANISOU 2018  N   ARG A 271     7753   8417   7799    416   1365   -302  A    N  
ATOM   2019  CA  ARG A 271     127.529  60.999  16.058  1.00 63.18      A    C  
ANISOU 2019  CA  ARG A 271     7680   8524   7800    369   1384   -318  A    C  
ATOM   2020  C   ARG A 271     128.254  59.708  16.044  1.00 63.22      A    C  
ANISOU 2020  C   ARG A 271     7739   8485   7794    309   1515   -201  A    C  
ATOM   2021  O   ARG A 271     128.138  58.924  16.981  1.00 62.22      A    O  
ANISOU 2021  O   ARG A 271     7513   8453   7672    253   1570   -173  A    O  
ATOM   2022  CB  ARG A 271     126.341  60.905  15.110  1.00 65.99      A    C  
ANISOU 2022  CB  ARG A 271     8099   8841   8133    400   1267   -404  A    C  
ATOM   2023  CG  ARG A 271     125.296  61.979  15.322  1.00 71.75      A    C  
ANISOU 2023  CG  ARG A 271     8714   9648   8899    461   1115   -562  A    C  
ATOM   2024  CD  ARG A 271     124.835  61.968  16.768  1.00 79.92      A    C  
ANISOU 2024  CD  ARG A 271     9524  10878   9964    414   1163   -621  A    C  
ATOM   2025  NE  ARG A 271     124.511  60.618  17.228  1.00 79.66      A    N  
ANISOU 2025  NE  ARG A 271     9446  10919   9903    319   1264   -578  A    N  
ATOM   2026  CZ  ARG A 271     123.280  60.169  17.286  1.00 84.13      A    C  
ANISOU 2026  CZ  ARG A 271     9924  11567  10473    287   1229   -683  A    C  
ATOM   2027  NH1 ARG A 271     122.267  60.969  16.921  1.00 85.63      A    N1+
ANISOU 2027  NH1 ARG A 271    10043  11776  10713    352   1090   -850  A    N1+
ATOM   2028  NH2 ARG A 271     123.063  58.935  17.706  1.00 88.57      A    N  
ANISOU 2028  NH2 ARG A 271    10470  12184  10996    189   1325   -632  A    N  
ATOM   2029  N   ASN A 272     128.995  59.506  14.963  1.00 65.32      A    N  
ANISOU 2029  N   ASN A 272     8179   8595   8045    314   1562   -141  A    N  
ATOM   2030  CA  ASN A 272     129.666  58.267  14.691  1.00 69.25      A    C  
ANISOU 2030  CA  ASN A 272     8748   9023   8542    267   1684    -49  A    C  
ATOM   2031  C   ASN A 272     130.772  57.987  15.677  1.00 71.10      A    C  
ANISOU 2031  C   ASN A 272     8885   9290   8841    241   1783     16  A    C  
ATOM   2032  O   ASN A 272     131.009  56.839  16.041  1.00 76.70      A    O  
ANISOU 2032  O   ASN A 272     9572  10004   9566    203   1847     72  A    O  
ATOM   2033  CB  ASN A 272     130.259  58.294  13.286  1.00 75.82      A    C  
ANISOU 2033  CB  ASN A 272     9794   9676   9339    268   1725    -22  A    C  
ATOM   2034  CG  ASN A 272     129.247  57.925  12.204  1.00 82.17      A    C  
ANISOU 2034  CG  ASN A 272    10738  10411  10071    274   1642    -55  A    C  
ATOM   2035  ND2 ASN A 272     129.252  56.653  11.829  1.00 88.90      A    N  
ANISOU 2035  ND2 ASN A 272    11653  11221  10903    231   1718     -4  A    N  
ATOM   2036  OD1 ASN A 272     128.484  58.766  11.702  1.00 79.41      A    O  
ANISOU 2036  OD1 ASN A 272    10445  10036   9690    320   1501   -129  A    O  
ATOM   2037  N   LEU A 273     131.466  59.023  16.119  1.00 73.62      A    N  
ANISOU 2037  N   LEU A 273     9151   9619   9203    268   1780      7  A    N  
ATOM   2038  CA  LEU A 273     132.559  58.829  17.079  1.00 73.33      A    C  
ANISOU 2038  CA  LEU A 273     9016   9601   9243    252   1852     59  A    C  
ATOM   2039  C   LEU A 273     132.030  58.642  18.489  1.00 70.02      A    C  
ANISOU 2039  C   LEU A 273     8451   9329   8823    230   1803     54  A    C  
ATOM   2040  O   LEU A 273     132.784  58.274  19.384  1.00 75.63      A    O  
ANISOU 2040  O   LEU A 273     9094  10052   9586    211   1834    101  A    O  
ATOM   2041  CB  LEU A 273     133.541  60.006  17.043  1.00 76.23      A    C  
ANISOU 2041  CB  LEU A 273     9381   9920   9659    280   1869     49  A    C  
ATOM   2042  CG  LEU A 273     134.344  60.204  15.745  1.00 76.48      A    C  
ANISOU 2042  CG  LEU A 273     9575   9792   9690    271   1951     56  A    C  
ATOM   2043  CD1 LEU A 273     135.236  61.415  15.911  1.00 74.32      A    C  
ANISOU 2043  CD1 LEU A 273     9282   9492   9463    285   1963     38  A    C  
ATOM   2044  CD2 LEU A 273     135.165  58.969  15.406  1.00 77.66      A    C  
ANISOU 2044  CD2 LEU A 273     9758   9856   9891    232   2083    103  A    C  
ATOM   2045  N   GLU A 274     130.741  58.906  18.679  1.00 65.73      A    N  
ANISOU 2045  N   GLU A 274     7865   8888   8219    225   1725    -15  A    N  
ATOM   2046  CA  GLU A 274     130.081  58.731  19.956  1.00 60.88      A    C  
ANISOU 2046  CA  GLU A 274     7131   8417   7580    175   1696    -38  A    C  
ATOM   2047  C   GLU A 274     130.717  59.629  21.023  1.00 57.39      A    C  
ANISOU 2047  C   GLU A 274     6597   8030   7176    186   1681    -40  A    C  
ATOM   2048  O   GLU A 274     131.134  59.181  22.065  1.00 54.15      A    O  
ANISOU 2048  O   GLU A 274     6145   7655   6775    142   1695      8  A    O  
ATOM   2049  CB  GLU A 274     130.114  57.263  20.327  1.00 62.46      A    C  
ANISOU 2049  CB  GLU A 274     7355   8613   7763    109   1745     33  A    C  
ATOM   2050  CG  GLU A 274     129.237  56.385  19.440  1.00 67.43      A    C  
ANISOU 2050  CG  GLU A 274     8060   9215   8343     88   1749     21  A    C  
ATOM   2051  CD  GLU A 274     129.026  54.939  19.990  1.00 78.34      A    C  
ANISOU 2051  CD  GLU A 274     9459  10614   9689      6   1781     80  A    C  
ATOM   2052  OE1 GLU A 274     129.852  54.396  20.791  1.00 78.63      A    O  
ANISOU 2052  OE1 GLU A 274     9493  10629   9753    -20   1802    153  A    O  
ATOM   2053  OE2 GLU A 274     127.997  54.314  19.634  1.00 86.62      A    O1-
ANISOU 2053  OE2 GLU A 274    10533  11694  10682    -34   1772     48  A    O1-
ATOM   2054  N   ILE A 275     130.790  60.921  20.743  1.00 58.06      A    N  
ANISOU 2054  N   ILE A 275     6668   8111   7280    244   1635    -97  A    N  
ATOM   2055  CA  ILE A 275     131.521  61.831  21.591  1.00 60.87      A    C  
ANISOU 2055  CA  ILE A 275     6952   8496   7677    263   1621    -95  A    C  
ATOM   2056  C   ILE A 275     130.749  62.065  22.863  1.00 63.69      A    C  
ANISOU 2056  C   ILE A 275     7199   9005   7993    218   1585   -150  A    C  
ATOM   2057  O   ILE A 275     131.272  61.800  23.966  1.00 69.78      A    O  
ANISOU 2057  O   ILE A 275     7933   9808   8769    173   1598   -101  A    O  
ATOM   2058  CB  ILE A 275     131.747  63.166  20.910  1.00 63.98      A    C  
ANISOU 2058  CB  ILE A 275     7377   8839   8091    333   1576   -144  A    C  
ATOM   2059  CG1 ILE A 275     132.682  62.971  19.725  1.00 66.91      A    C  
ANISOU 2059  CG1 ILE A 275     7881   9050   8492    350   1638    -88  A    C  
ATOM   2060  CG2 ILE A 275     132.404  64.155  21.858  1.00 66.79      A    C  
ANISOU 2060  CG2 ILE A 275     7650   9238   8489    350   1555   -150  A    C  
ATOM   2061  CD1 ILE A 275     132.794  64.180  18.818  1.00 68.81      A    C  
ANISOU 2061  CD1 ILE A 275     8211   9210   8722    400   1589   -133  A    C  
ATOM   2062  N   THR A 276     129.515  62.561  22.717  1.00 61.55      A    N  
ANISOU 2062  N   THR A 276     6880   8819   7685    224   1533   -265  A    N  
ATOM   2063  CA  THR A 276     128.607  62.688  23.854  1.00 59.16      A    C  
ANISOU 2063  CA  THR A 276     6470   8672   7337    156   1524   -348  A    C  
ATOM   2064  C   THR A 276     127.295  61.912  23.713  1.00 61.05      A    C  
ANISOU 2064  C   THR A 276     6687   8984   7525     92   1536   -420  A    C  
ATOM   2065  O   THR A 276     126.331  62.192  24.369  1.00 64.70      A    O  
ANISOU 2065  O   THR A 276     7049   9573   7958     39   1533   -536  A    O  
ATOM   2066  CB  THR A 276     128.301  64.160  24.148  1.00 57.75      A    C  
ANISOU 2066  CB  THR A 276     6202   8560   7180    208   1459   -462  A    C  
ATOM   2067  CG2 THR A 276     129.571  64.882  24.441  1.00 58.14      A    C  
ANISOU 2067  CG2 THR A 276     6269   8549   7272    254   1453   -391  A    C  
ATOM   2068  OG1 THR A 276     127.602  64.772  23.054  1.00 56.35      A    O  
ANISOU 2068  OG1 THR A 276     6031   8350   7028    288   1384   -560  A    O  
ATOM   2069  N   GLN A 277     127.249  60.891  22.891  1.00 63.30      A    N  
ANISOU 2069  N   GLN A 277     7057   9191   7801     84   1560   -361  A    N  
ATOM   2070  CA  GLN A 277     125.993  60.243  22.650  1.00 65.37      A    C  
ANISOU 2070  CA  GLN A 277     7294   9515   8026     31   1562   -440  A    C  
ATOM   2071  C   GLN A 277     126.246  59.078  21.729  1.00 68.56      A    C  
ANISOU 2071  C   GLN A 277     7821   9806   8421     31   1591   -342  A    C  
ATOM   2072  O   GLN A 277     127.022  59.177  20.770  1.00 73.06      A    O  
ANISOU 2072  O   GLN A 277     8487  10244   9027    106   1583   -277  A    O  
ATOM   2073  CB  GLN A 277     125.068  61.259  22.010  1.00 69.79      A    C  
ANISOU 2073  CB  GLN A 277     7783  10106   8627    106   1473   -596  A    C  
ATOM   2074  CG  GLN A 277     123.782  60.714  21.440  1.00 73.81      A    C  
ANISOU 2074  CG  GLN A 277     8263  10650   9131     81   1448   -699  A    C  
ATOM   2075  CD  GLN A 277     123.127  61.701  20.499  1.00 74.85      A    C  
ANISOU 2075  CD  GLN A 277     8365  10746   9326    192   1318   -836  A    C  
ATOM   2076  NE2 GLN A 277     121.813  61.542  20.291  1.00 79.42      A    N  
ANISOU 2076  NE2 GLN A 277     8851  11393   9930    175   1272   -989  A    N  
ATOM   2077  OE1 GLN A 277     123.783  62.611  19.982  1.00 71.00      A    O  
ANISOU 2077  OE1 GLN A 277     7941  10165   8869    291   1249   -813  A    O  
ATOM   2078  N   THR A 278     125.589  57.968  22.001  1.00 72.20      A    N  
ANISOU 2078  N   THR A 278     8288  10313   8830    -65   1631   -336  A    N  
ATOM   2079  CA  THR A 278     125.827  56.755  21.226  1.00 78.19      A    C  
ANISOU 2079  CA  THR A 278     9164  10966   9575    -74   1662   -241  A    C  
ATOM   2080  C   THR A 278     125.086  56.773  19.889  1.00 83.29      A    C  
ANISOU 2080  C   THR A 278     9852  11559  10236    -16   1610   -307  A    C  
ATOM   2081  O   THR A 278     124.410  57.753  19.551  1.00 87.10      A    O  
ANISOU 2081  O   THR A 278    10269  12076  10747     39   1533   -430  A    O  
ATOM   2082  CB  THR A 278     125.353  55.524  21.987  1.00 80.26      A    C  
ANISOU 2082  CB  THR A 278     9440  11287   9767   -202   1713   -210  A    C  
ATOM   2083  CG2 THR A 278     125.702  55.649  23.457  1.00 82.52      A    C  
ANISOU 2083  CG2 THR A 278     9688  11649  10016   -282   1736   -185  A    C  
ATOM   2084  OG1 THR A 278     123.934  55.409  21.826  1.00 89.69      A    O  
ANISOU 2084  OG1 THR A 278    10568  12576  10934   -256   1702   -337  A    O  
ATOM   2085  N   LEU A 279     125.202  55.682  19.131  1.00 84.76      A    N  
ANISOU 2085  N   LEU A 279    10151  11649  10402    -27   1638   -231  A    N  
ATOM   2086  CA  LEU A 279     124.473  55.560  17.874  1.00 85.72      A    C  
ANISOU 2086  CA  LEU A 279    10337  11708  10525     15   1579   -286  A    C  
ATOM   2087  C   LEU A 279     123.023  55.168  18.102  1.00 93.21      A    C  
ANISOU 2087  C   LEU A 279    11193  12769  11452    -54   1554   -401  A    C  
ATOM   2088  O   LEU A 279     122.167  55.410  17.250  1.00102.43      A    O  
ANISOU 2088  O   LEU A 279    12358  13917  12643    -10   1468   -499  A    O  
ATOM   2089  CB  LEU A 279     125.180  54.606  16.938  1.00 80.54      A    C  
ANISOU 2089  CB  LEU A 279     9843  10901   9854     27   1626   -170  A    C  
ATOM   2090  CG  LEU A 279     126.483  55.236  16.421  1.00 84.20      A    C  
ANISOU 2090  CG  LEU A 279    10394  11244  10353     97   1650   -104  A    C  
ATOM   2091  CD1 LEU A 279     127.476  54.208  15.901  1.00 83.55      A    C  
ANISOU 2091  CD1 LEU A 279    10436  11034  10274     85   1742     10  A    C  
ATOM   2092  CD2 LEU A 279     126.210  56.305  15.359  1.00 87.52      A    C  
ANISOU 2092  CD2 LEU A 279    10882  11590  10778    179   1556   -176  A    C  
ATOM   2093  N   SER A 280     122.744  54.594  19.267  1.00 95.95      A    N  
ANISOU 2093  N   SER A 280    11467  13230  11758   -169   1622   -398  A    N  
ATOM   2094  CA  SER A 280     121.369  54.401  19.730  1.00101.25      A    C  
ANISOU 2094  CA  SER A 280    12021  14037  12410   -263   1624   -536  A    C  
ATOM   2095  C   SER A 280     120.924  55.533  20.687  1.00111.23      A    C  
ANISOU 2095  C   SER A 280    13120  15444  13697   -283   1619   -674  A    C  
ATOM   2096  O   SER A 280     119.873  55.449  21.327  1.00110.50      A    O  
ANISOU 2096  O   SER A 280    12909  15486  13590   -387   1653   -805  A    O  
ATOM   2097  CB  SER A 280     121.246  53.028  20.386  1.00 94.49      A    C  
ANISOU 2097  CB  SER A 280    11216  13211  11473   -406   1710   -459  A    C  
ATOM   2098  OG  SER A 280     122.437  52.701  21.066  1.00 88.83      A    O  
ANISOU 2098  OG  SER A 280    10580  12445  10724   -424   1757   -311  A    O  
ATOM   2099  N   GLY A 281     121.738  56.582  20.787  1.00120.70      A    N  
ANISOU 2099  N   GLY A 281    14313  16613  14934   -192   1586   -650  A    N  
ATOM   2100  CA  GLY A 281     121.375  57.805  21.523  1.00128.13      A    C  
ANISOU 2100  CA  GLY A 281    15105  17670  15909   -183   1564   -787  A    C  
ATOM   2101  C   GLY A 281     121.313  57.731  23.044  1.00126.29      A    C  
ANISOU 2101  C   GLY A 281    14802  17569  15610   -320   1659   -801  A    C  
ATOM   2102  O   GLY A 281     120.278  58.035  23.618  1.00128.38      A    O  
ANISOU 2102  O   GLY A 281    14930  17970  15875   -398   1684   -968  A    O  
ATOM   2103  N   LYS A 282     122.422  57.370  23.695  1.00120.22      A    N  
ANISOU 2103  N   LYS A 282    14131  16754  14791   -352   1703   -642  A    N  
ATOM   2104  CA  LYS A 282     122.480  57.226  25.154  1.00117.70      A    C  
ANISOU 2104  CA  LYS A 282    13799  16531  14391   -491   1774   -632  A    C  
ATOM   2105  C   LYS A 282     123.802  57.714  25.776  1.00115.14      A    C  
ANISOU 2105  C   LYS A 282    13527  16151  14070   -445   1759   -513  A    C  
ATOM   2106  O   LYS A 282     124.532  58.457  25.159  1.00122.43      A    O  
ANISOU 2106  O   LYS A 282    14451  16996  15070   -309   1706   -482  A    O  
ATOM   2107  CB  LYS A 282     122.253  55.759  25.509  1.00115.74      A    C  
ANISOU 2107  CB  LYS A 282    13651  16275  14048   -633   1838   -553  A    C  
ATOM   2108  CG  LYS A 282     120.857  55.284  25.182  1.00121.97      A    C  
ANISOU 2108  CG  LYS A 282    14372  17146  14822   -718   1871   -689  A    C  
ATOM   2109  CD  LYS A 282     120.798  53.788  25.188  1.00121.50      A    C  
ANISOU 2109  CD  LYS A 282    14444  17036  14681   -826   1912   -583  A    C  
ATOM   2110  CE  LYS A 282     121.673  53.255  24.086  1.00116.61      A    C  
ANISOU 2110  CE  LYS A 282    13940  16253  14114   -695   1858   -436  A    C  
ATOM   2111  NZ  LYS A 282     121.212  51.889  23.740  1.00127.54      A    N1+
ANISOU 2111  NZ  LYS A 282    15414  17600  15444   -779   1885   -391  A    N1+
ATOM   2112  N   LYS A 283     124.068  57.311  27.015  1.00115.71      A    N  
ANISOU 2112  N   LYS A 283    13649  16258  14054   -569   1801   -457  A    N  
ATOM   2113  CA  LYS A 283     125.363  57.492  27.679  1.00111.14      A    C  
ANISOU 2113  CA  LYS A 283    13141  15607  13478   -539   1772   -330  A    C  
ATOM   2114  C   LYS A 283     126.049  56.124  27.956  1.00109.41      A    C  
ANISOU 2114  C   LYS A 283    13075  15282  13214   -599   1770   -171  A    C  
ATOM   2115  O   LYS A 283     126.894  55.970  28.861  1.00 88.99      A    O  
ANISOU 2115  O   LYS A 283    10563  12646  10601   -630   1738    -80  A    O  
ATOM   2116  CB  LYS A 283     125.137  58.248  28.989  1.00129.06      A    C  
ANISOU 2116  CB  LYS A 283    15361  17990  15684   -632   1793   -405  A    C  
ATOM   2117  CG  LYS A 283     125.474  59.721  28.898  1.00139.23      A    C  
ANISOU 2117  CG  LYS A 283    16545  19300  17053   -511   1749   -472  A    C  
ATOM   2118  CD  LYS A 283     126.984  59.880  28.709  1.00136.36      A    C  
ANISOU 2118  CD  LYS A 283    16247  18800  16763   -396   1690   -324  A    C  
ATOM   2119  CE  LYS A 283     127.336  61.075  27.847  1.00119.57      A    C  
ANISOU 2119  CE  LYS A 283    14047  16640  14744   -239   1643   -369  A    C  
ATOM   2120  NZ  LYS A 283     126.893  60.874  26.452  1.00110.51      A    N1+
ANISOU 2120  NZ  LYS A 283    12898  15443  13645   -164   1633   -400  A    N1+
ATOM   2121  N   THR A 284     125.611  55.120  27.191  1.00112.51      A    N  
ANISOU 2121  N   THR A 284    13515  15635  13597   -616   1790   -150  A    N  
ATOM   2122  CA  THR A 284     126.206  53.779  27.150  1.00 99.54      A    C  
ANISOU 2122  CA  THR A 284    12013  13874  11934   -643   1778    -11  A    C  
ATOM   2123  C   THR A 284     127.548  53.881  26.445  1.00 84.64      A    C  
ANISOU 2123  C   THR A 284    10147  11843  10168   -488   1737     83  A    C  
ATOM   2124  O   THR A 284     127.603  54.178  25.285  1.00 87.44      A    O  
ANISOU 2124  O   THR A 284    10469  12158  10596   -384   1745     62  A    O  
ATOM   2125  CB  THR A 284     125.313  52.814  26.327  1.00108.52      A    C  
ANISOU 2125  CB  THR A 284    13180  15010  13042   -685   1812    -33  A    C  
ATOM   2126  CG2 THR A 284     125.810  51.365  26.451  1.00109.35      A    C  
ANISOU 2126  CG2 THR A 284    13437  15000  13109   -735   1797     99  A    C  
ATOM   2127  OG1 THR A 284     123.933  52.919  26.744  1.00112.13      A    O  
ANISOU 2127  OG1 THR A 284    13571  15615  13417   -817   1867   -168  A    O  
ATOM   2128  N   PRO A 285     128.638  53.612  27.140  1.00 80.32      A    N  
ANISOU 2128  N   PRO A 285     9661  11211   9642   -481   1691    180  A    N  
ATOM   2129  CA  PRO A 285     129.977  54.060  26.846  1.00 74.92      A    C  
ANISOU 2129  CA  PRO A 285     8956  10421   9086   -351   1658    234  A    C  
ATOM   2130  C   PRO A 285     130.172  55.058  25.689  1.00 71.40      A    C  
ANISOU 2130  C   PRO A 285     8429   9965   8732   -226   1686    182  A    C  
ATOM   2131  O   PRO A 285     130.160  54.714  24.519  1.00 71.42      A    O  
ANISOU 2131  O   PRO A 285     8457   9902   8774   -172   1719    187  A    O  
ATOM   2132  CB  PRO A 285     130.693  52.745  26.621  1.00 76.87      A    C  
ANISOU 2132  CB  PRO A 285     9301  10529   9375   -340   1637    333  A    C  
ATOM   2133  CG  PRO A 285     130.081  51.855  27.650  1.00 84.31      A    C  
ANISOU 2133  CG  PRO A 285    10345  11503  10187   -486   1605    362  A    C  
ATOM   2134  CD  PRO A 285     128.724  52.446  28.021  1.00 90.66      A    C  
ANISOU 2134  CD  PRO A 285    11099  12475  10869   -593   1658    260  A    C  
ATOM   2135  N   THR A 286     130.354  56.311  26.039  1.00 68.79      A    N  
ANISOU 2135  N   THR A 286     8020   9689   8428   -187   1669    132  A    N  
ATOM   2136  CA  THR A 286     130.764  57.290  25.069  1.00 69.91      A    C  
ANISOU 2136  CA  THR A 286     8116   9792   8653    -74   1677     98  A    C  
ATOM   2137  C   THR A 286     132.141  57.819  25.451  1.00 69.05      A    C  
ANISOU 2137  C   THR A 286     7985   9609   8639    -14   1654    147  A    C  
ATOM   2138  O   THR A 286     132.684  57.485  26.501  1.00 67.50      A    O  
ANISOU 2138  O   THR A 286     7801   9398   8445    -51   1613    198  A    O  
ATOM   2139  CB  THR A 286     129.774  58.453  25.004  1.00 71.95      A    C  
ANISOU 2139  CB  THR A 286     8293  10169   8876    -66   1664    -22  A    C  
ATOM   2140  CG2 THR A 286     128.372  57.921  24.784  1.00 74.09      A    C  
ANISOU 2140  CG2 THR A 286     8557  10522   9070   -136   1682    -94  A    C  
ATOM   2141  OG1 THR A 286     129.813  59.187  26.232  1.00 80.27      A    O  
ANISOU 2141  OG1 THR A 286     9286  11308   9902   -105   1638    -52  A    O  
ATOM   2142  N   LEU A 287     132.704  58.659  24.596  1.00 66.49      A    N  
ANISOU 2142  N   LEU A 287     7640   9231   8391     75   1671    126  A    N  
ATOM   2143  CA  LEU A 287     133.990  59.239  24.881  1.00 64.25      A    C  
ANISOU 2143  CA  LEU A 287     7321   8881   8207    126   1659    154  A    C  
ATOM   2144  C   LEU A 287     133.896  60.108  26.127  1.00 64.83      A    C  
ANISOU 2144  C   LEU A 287     7332   9048   8250    104   1598    128  A    C  
ATOM   2145  O   LEU A 287     134.864  60.217  26.895  1.00 62.24      A    O  
ANISOU 2145  O   LEU A 287     6985   8678   7985    114   1559    168  A    O  
ATOM   2146  CB  LEU A 287     134.439  60.087  23.712  1.00 63.45      A    C  
ANISOU 2146  CB  LEU A 287     7228   8714   8165    200   1698    125  A    C  
ATOM   2147  CG  LEU A 287     135.785  60.769  23.946  1.00 65.42      A    C  
ANISOU 2147  CG  LEU A 287     7433   8896   8526    244   1701    139  A    C  
ATOM   2148  CD1 LEU A 287     136.929  59.758  23.914  1.00 64.97      A    C  
ANISOU 2148  CD1 LEU A 287     7380   8722   8580    250   1738    194  A    C  
ATOM   2149  CD2 LEU A 287     136.009  61.871  22.913  1.00 68.09      A    C  
ANISOU 2149  CD2 LEU A 287     7796   9191   8883    292   1732     95  A    C  
ATOM   2150  N   PHE A 288     132.730  60.737  26.307  1.00 62.96      A    N  
ANISOU 2150  N   PHE A 288     7061   8934   7925     74   1588     48  A    N  
ATOM   2151  CA  PHE A 288     132.526  61.659  27.408  1.00 60.96      A    C  
ANISOU 2151  CA  PHE A 288     6749   8780   7633     47   1545     -0  A    C  
ATOM   2152  C   PHE A 288     132.346  60.913  28.716  1.00 60.98      A    C  
ANISOU 2152  C   PHE A 288     6790   8824   7555    -62   1523     38  A    C  
ATOM   2153  O   PHE A 288     132.869  61.327  29.740  1.00 60.81      A    O  
ANISOU 2153  O   PHE A 288     6763   8809   7532    -81   1474     56  A    O  
ATOM   2154  CB  PHE A 288     131.327  62.538  27.125  1.00 60.16      A    C  
ANISOU 2154  CB  PHE A 288     6588   8790   7481     52   1545   -124  A    C  
ATOM   2155  CG  PHE A 288     130.926  63.400  28.278  1.00 61.79      A    C  
ANISOU 2155  CG  PHE A 288     6727   9112   7635      8   1518   -195  A    C  
ATOM   2156  CD1 PHE A 288     131.585  64.572  28.528  1.00 63.21      A    C  
ANISOU 2156  CD1 PHE A 288     6864   9284   7867     72   1478   -210  A    C  
ATOM   2157  CD2 PHE A 288     129.876  63.057  29.086  1.00 63.03      A    C  
ANISOU 2157  CD2 PHE A 288     6871   9388   7690   -107   1543   -257  A    C  
ATOM   2158  CE1 PHE A 288     131.203  65.379  29.569  1.00 63.58      A    C  
ANISOU 2158  CE1 PHE A 288     6855   9437   7865     30   1457   -283  A    C  
ATOM   2159  CE2 PHE A 288     129.500  63.857  30.127  1.00 63.59      A    C  
ANISOU 2159  CE2 PHE A 288     6887   9566   7707   -161   1536   -338  A    C  
ATOM   2160  CZ  PHE A 288     130.161  65.025  30.365  1.00 62.56      A    C  
ANISOU 2160  CZ  PHE A 288     6715   9425   7631    -86   1490   -350  A    C  
ATOM   2161  N   SER A 289     131.620  59.799  28.674  1.00 62.06      A    N  
ANISOU 2161  N   SER A 289     6984   8977   7616   -142   1551     50  A    N  
ATOM   2162  CA  SER A 289     131.323  59.033  29.892  1.00 62.74      A    C  
ANISOU 2162  CA  SER A 289     7144   9096   7595   -272   1530     84  A    C  
ATOM   2163  C   SER A 289     132.542  58.296  30.359  1.00 60.99      A    C  
ANISOU 2163  C   SER A 289     7001   8739   7433   -257   1461    198  A    C  
ATOM   2164  O   SER A 289     132.723  58.068  31.519  1.00 64.40      A    O  
ANISOU 2164  O   SER A 289     7502   9164   7801   -335   1399    234  A    O  
ATOM   2165  CB  SER A 289     130.187  58.028  29.670  1.00 63.07      A    C  
ANISOU 2165  CB  SER A 289     7234   9187   7539   -372   1582     62  A    C  
ATOM   2166  OG  SER A 289     130.677  56.799  29.166  1.00 61.29      A    O  
ANISOU 2166  OG  SER A 289     7093   8842   7351   -355   1574    157  A    O  
ATOM   2167  N   ILE A 290     133.381  57.918  29.432  1.00 60.59      A    N  
ANISOU 2167  N   ILE A 290     6942   8572   7507   -159   1468    245  A    N  
ATOM   2168  CA  ILE A 290     134.606  57.255  29.784  1.00 62.57      A    C  
ANISOU 2168  CA  ILE A 290     7234   8684   7854   -124   1396    327  A    C  
ATOM   2169  C   ILE A 290     135.613  58.209  30.367  1.00 63.70      A    C  
ANISOU 2169  C   ILE A 290     7317   8797   8087    -65   1333    325  A    C  
ATOM   2170  O   ILE A 290     136.524  57.781  31.022  1.00 70.18      A    O  
ANISOU 2170  O   ILE A 290     8170   9518   8977    -52   1241    376  A    O  
ATOM   2171  CB  ILE A 290     135.210  56.607  28.540  1.00 64.23      A    C  
ANISOU 2171  CB  ILE A 290     7434   8783   8184    -41   1447    349  A    C  
ATOM   2172  CG1 ILE A 290     134.497  55.285  28.298  1.00 69.77      A    C  
ANISOU 2172  CG1 ILE A 290     8229   9473   8808   -108   1465    381  A    C  
ATOM   2173  CG2 ILE A 290     136.694  56.402  28.665  1.00 62.46      A    C  
ANISOU 2173  CG2 ILE A 290     7183   8421   8128     36   1391    385  A    C  
ATOM   2174  CD1 ILE A 290     134.417  54.372  29.511  1.00 72.60      A    C  
ANISOU 2174  CD1 ILE A 290     8697   9802   9082   -204   1368    439  A    C  
ATOM   2175  N   LEU A 291     135.477  59.499  30.125  1.00 62.95      A    N  
ANISOU 2175  N   LEU A 291     7138   8777   8002    -24   1370    263  A    N  
ATOM   2176  CA  LEU A 291     136.426  60.443  30.643  1.00 62.34      A    C  
ANISOU 2176  CA  LEU A 291     7004   8671   8012     31   1313    260  A    C  
ATOM   2177  C   LEU A 291     135.854  61.278  31.726  1.00 62.84      A    C  
ANISOU 2177  C   LEU A 291     7068   8845   7962    -35   1274    222  A    C  
ATOM   2178  O   LEU A 291     136.558  62.145  32.211  1.00 67.22      A    O  
ANISOU 2178  O   LEU A 291     7579   9386   8574      6   1222    216  A    O  
ATOM   2179  CB  LEU A 291     136.856  61.407  29.551  1.00 63.48      A    C  
ANISOU 2179  CB  LEU A 291     7062   8800   8255    127   1378    216  A    C  
ATOM   2180  CG  LEU A 291     137.511  60.832  28.302  1.00 64.97      A    C  
ANISOU 2180  CG  LEU A 291     7247   8877   8559    187   1448    232  A    C  
ATOM   2181  CD1 LEU A 291     137.959  61.998  27.429  1.00 66.76      A    C  
ANISOU 2181  CD1 LEU A 291     7421   9087   8856    253   1504    185  A    C  
ATOM   2182  CD2 LEU A 291     138.721  59.989  28.645  1.00 67.12      A    C  
ANISOU 2182  CD2 LEU A 291     7516   9018   8967    212   1398    280  A    C  
ATOM   2183  N   ASP A 292     134.587  61.083  32.089  1.00 62.59      A    N  
ANISOU 2183  N   ASP A 292     7078   8927   7775   -139   1309    184  A    N  
ATOM   2184  CA  ASP A 292     133.916  62.067  32.953  1.00 63.82      A    C  
ANISOU 2184  CA  ASP A 292     7213   9208   7827   -202   1308    111  A    C  
ATOM   2185  C   ASP A 292     134.134  61.783  34.392  1.00 62.94      A    C  
ANISOU 2185  C   ASP A 292     7207   9080   7626   -303   1225    156  A    C  
ATOM   2186  O   ASP A 292     133.266  61.259  35.044  1.00 62.50      A    O  
ANISOU 2186  O   ASP A 292     7240   9086   7419   -440   1247    142  A    O  
ATOM   2187  CB  ASP A 292     132.406  62.129  32.689  1.00 66.99      A    C  
ANISOU 2187  CB  ASP A 292     7587   9749   8114   -276   1397     11  A    C  
ATOM   2188  CG  ASP A 292     131.712  63.336  33.372  1.00 67.96      A    C  
ANISOU 2188  CG  ASP A 292     7646  10010   8165   -319   1414   -103  A    C  
ATOM   2189  OD1 ASP A 292     132.387  64.284  33.877  1.00 67.15      A    O  
ANISOU 2189  OD1 ASP A 292     7514   9897   8102   -273   1361   -104  A    O  
ATOM   2190  OD2 ASP A 292     130.458  63.317  33.372  1.00 67.63      A    O1-
ANISOU 2190  OD2 ASP A 292     7573  10086   8034   -401   1485   -207  A    O1-
ATOM   2191  N   GLY A 293     135.280  62.183  34.904  1.00 65.74      A    N  
ANISOU 2191  N   GLY A 293     7560   9346   8069   -243   1129    202  A    N  
ATOM   2192  CA  GLY A 293     135.577  61.991  36.298  1.00 70.37      A    C  
ANISOU 2192  CA  GLY A 293     8269   9895   8573   -333   1020    247  A    C  
ATOM   2193  C   GLY A 293     135.579  63.317  36.980  1.00 73.19      A    C  
ANISOU 2193  C   GLY A 293     8581  10327   8898   -336   1005    189  A    C  
ATOM   2194  O   GLY A 293     136.351  63.520  37.900  1.00 86.44      A    O  
ANISOU 2194  O   GLY A 293    10320  11933  10588   -341    888    232  A    O  
ATOM   2195  N   CYS A 294     134.715  64.224  36.550  1.00 72.78      A    N  
ANISOU 2195  N   CYS A 294     8428  10413   8810   -331   1109     85  A    N  
ATOM   2196  CA  CYS A 294     134.723  65.563  37.098  1.00 73.10      A    C  
ANISOU 2196  CA  CYS A 294     8412  10526   8835   -319   1097     18  A    C  
ATOM   2197  C   CYS A 294     134.041  65.582  38.435  1.00 71.31      A    C  
ANISOU 2197  C   CYS A 294     8299  10373   8418   -486   1095    -16  A    C  
ATOM   2198  O   CYS A 294     133.094  64.871  38.643  1.00 73.16      A    O  
ANISOU 2198  O   CYS A 294     8605  10669   8521   -615   1163    -43  A    O  
ATOM   2199  CB  CYS A 294     134.064  66.530  36.146  1.00 76.68      A    C  
ANISOU 2199  CB  CYS A 294     8721  11082   9330   -244   1186    -92  A    C  
ATOM   2200  SG  CYS A 294     135.052  66.730  34.646  1.00 90.91      A    S  
ANISOU 2200  SG  CYS A 294    10431  12774  11336    -66   1183    -50  A    S  
ATOM   2201  N   ALA A 295     134.556  66.396  39.346  1.00 71.29      A    N  
ANISOU 2201  N   ALA A 295     8323  10361   8401   -492   1020    -17  A    N  
ATOM   2202  CA  ALA A 295     134.059  66.478  40.686  1.00 71.85      A    C  
ANISOU 2202  CA  ALA A 295     8530  10483   8284   -658   1011    -45  A    C  
ATOM   2203  C   ALA A 295     132.833  67.357  40.735  1.00 74.89      A    C  
ANISOU 2203  C   ALA A 295     8823  11051   8578   -723   1148   -206  A    C  
ATOM   2204  O   ALA A 295     132.025  67.224  41.648  1.00 84.11      A    O  
ANISOU 2204  O   ALA A 295    10094  12298   9565   -903   1209   -267  A    O  
ATOM   2205  CB  ALA A 295     135.130  67.047  41.593  1.00 72.10      A    C  
ANISOU 2205  CB  ALA A 295     8627  10423   8345   -629    866     12  A    C  
ATOM   2206  N   THR A 296     132.706  68.284  39.789  1.00 74.34      A    N  
ANISOU 2206  N   THR A 296     8568  11043   8633   -586   1193   -287  A    N  
ATOM   2207  CA  THR A 296     131.585  69.221  39.795  1.00 76.15      A    C  
ANISOU 2207  CA  THR A 296     8686  11434   8811   -619   1297   -463  A    C  
ATOM   2208  C   THR A 296     130.688  68.999  38.595  1.00 78.98      A    C  
ANISOU 2208  C   THR A 296     8920  11861   9228   -571   1387   -548  A    C  
ATOM   2209  O   THR A 296     131.077  68.361  37.616  1.00 77.28      A    O  
ANISOU 2209  O   THR A 296     8694  11561   9107   -481   1365   -463  A    O  
ATOM   2210  CB  THR A 296     132.065  70.670  39.745  1.00 74.87      A    C  
ANISOU 2210  CB  THR A 296     8417  11285   8743   -495   1247   -515  A    C  
ATOM   2211  CG2 THR A 296     133.075  70.954  40.854  1.00 77.97      A    C  
ANISOU 2211  CG2 THR A 296     8924  11596   9105   -520   1137   -427  A    C  
ATOM   2212  OG1 THR A 296     132.685  70.896  38.486  1.00 71.04      A    O  
ANISOU 2212  OG1 THR A 296     7833  10726   8431   -316   1208   -471  A    O  
ATOM   2213  N   HIS A 297     129.476  69.537  38.676  1.00 82.01      A    N  
ANISOU 2213  N   HIS A 297     9207  12392   9558   -632   1485   -727  A    N  
ATOM   2214  CA  HIS A 297     128.565  69.473  37.554  1.00 77.54      A    C  
ANISOU 2214  CA  HIS A 297     8509  11888   9061   -576   1547   -834  A    C  
ATOM   2215  C   HIS A 297     129.034  70.393  36.452  1.00 74.29      A    C  
ANISOU 2215  C   HIS A 297     7985  11427   8814   -368   1472   -842  A    C  
ATOM   2216  O   HIS A 297     129.008  69.998  35.293  1.00 72.32      A    O  
ANISOU 2216  O   HIS A 297     7704  11124   8647   -279   1462   -812  A    O  
ATOM   2217  CB  HIS A 297     127.187  69.908  37.993  1.00 80.68      A    C  
ANISOU 2217  CB  HIS A 297     8812  12455   9387   -690   1658  -1052  A    C  
ATOM   2218  CG  HIS A 297     126.505  68.923  38.865  1.00 82.20      A    C  
ANISOU 2218  CG  HIS A 297     9117  12706   9408   -919   1764  -1070  A    C  
ATOM   2219  CD2 HIS A 297     125.569  69.077  39.829  1.00 85.79      A    C  
ANISOU 2219  CD2 HIS A 297     9574  13291   9730  -1109   1883  -1227  A    C  
ATOM   2220  ND1 HIS A 297     126.735  67.570  38.756  1.00 81.83      A    N  
ANISOU 2220  ND1 HIS A 297     9208  12576   9307   -985   1759   -926  A    N  
ATOM   2221  CE1 HIS A 297     125.991  66.933  39.640  1.00 85.41      A    C  
ANISOU 2221  CE1 HIS A 297     9763  13098   9591  -1211   1862   -980  A    C  
ATOM   2222  NE2 HIS A 297     125.273  67.824  40.302  1.00 88.33      A    N  
ANISOU 2222  NE2 HIS A 297    10054  13600   9906  -1297   1949  -1164  A    N  
ATOM   2223  N   MET A 298     129.438  71.619  36.822  1.00 71.54      A    N  
ANISOU 2223  N   MET A 298     7590  11089   8500   -302   1420   -885  A    N  
ATOM   2224  CA  MET A 298     129.998  72.597  35.871  1.00 70.27      A    C  
ANISOU 2224  CA  MET A 298     7354  10864   8480   -118   1338   -884  A    C  
ATOM   2225  C   MET A 298     131.314  72.086  35.178  1.00 68.74      A    C  
ANISOU 2225  C   MET A 298     7235  10506   8374    -28   1276   -694  A    C  
ATOM   2226  O   MET A 298     131.635  72.442  34.018  1.00 64.41      A    O  
ANISOU 2226  O   MET A 298     6653   9887   7932    100   1241   -682  A    O  
ATOM   2227  CB  MET A 298     130.196  73.940  36.556  1.00 69.13      A    C  
ANISOU 2227  CB  MET A 298     7165  10761   8340    -87   1296   -962  A    C  
ATOM   2228  CG  MET A 298     131.096  73.835  37.757  1.00 73.35      A    C  
ANISOU 2228  CG  MET A 298     7812  11252   8804   -165   1265   -850  A    C  
ATOM   2229  SD  MET A 298     130.580  74.884  39.126  1.00 79.40      A    S  
ANISOU 2229  SD  MET A 298     8560  12142   9465   -262   1291   -997  A    S  
ATOM   2230  CE  MET A 298     131.091  76.485  38.535  1.00 82.54      A    C  
ANISOU 2230  CE  MET A 298     8850  12510  10002    -71   1193  -1050  A    C  
ATOM   2231  N   GLY A 299     132.050  71.221  35.869  1.00 66.16      A    N  
ANISOU 2231  N   GLY A 299     7018  10113   8006   -100   1263   -561  A    N  
ATOM   2232  CA  GLY A 299     133.232  70.600  35.286  1.00 61.67      A    C  
ANISOU 2232  CA  GLY A 299     6500   9396   7533    -29   1218   -409  A    C  
ATOM   2233  C   GLY A 299     132.830  69.583  34.246  1.00 58.51      A    C  
ANISOU 2233  C   GLY A 299     6109   8968   7153    -20   1270   -384  A    C  
ATOM   2234  O   GLY A 299     133.394  69.521  33.167  1.00 58.41      A    O  
ANISOU 2234  O   GLY A 299     6087   8864   7242     78   1261   -335  A    O  
ATOM   2235  N   SER A 300     131.831  68.789  34.554  1.00 57.65      A    N  
ANISOU 2235  N   SER A 300     6028   8937   6940   -134   1331   -425  A    N  
ATOM   2236  CA  SER A 300     131.356  67.818  33.595  1.00 57.76      A    C  
ANISOU 2236  CA  SER A 300     6051   8930   6965   -132   1378   -409  A    C  
ATOM   2237  C   SER A 300     130.843  68.478  32.343  1.00 55.65      A    C  
ANISOU 2237  C   SER A 300     5693   8678   6772    -22   1383   -502  A    C  
ATOM   2238  O   SER A 300     131.128  68.039  31.243  1.00 54.41      A    O  
ANISOU 2238  O   SER A 300     5559   8433   6681     48   1383   -447  A    O  
ATOM   2239  CB  SER A 300     130.255  66.999  34.208  1.00 60.22      A    C  
ANISOU 2239  CB  SER A 300     6398   9337   7143   -288   1448   -462  A    C  
ATOM   2240  OG  SER A 300     130.769  66.293  35.327  1.00 64.39      A    O  
ANISOU 2240  OG  SER A 300     7055   9822   7586   -397   1423   -362  A    O  
ATOM   2241  N   ARG A 301     130.118  69.568  32.496  1.00 55.59      A    N  
ANISOU 2241  N   ARG A 301     5593   8768   6758     -4   1377   -647  A    N  
ATOM   2242  CA  ARG A 301     129.600  70.258  31.318  1.00 56.59      A    C  
ANISOU 2242  CA  ARG A 301     5648   8890   6960    110   1346   -746  A    C  
ATOM   2243  C   ARG A 301     130.706  70.868  30.461  1.00 57.70      A    C  
ANISOU 2243  C   ARG A 301     5826   8897   7197    238   1282   -664  A    C  
ATOM   2244  O   ARG A 301     130.640  70.864  29.213  1.00 56.18      A    O  
ANISOU 2244  O   ARG A 301     5658   8631   7056    317   1260   -665  A    O  
ATOM   2245  CB  ARG A 301     128.596  71.327  31.724  1.00 56.19      A    C  
ANISOU 2245  CB  ARG A 301     5481   8967   6899    110   1336   -941  A    C  
ATOM   2246  CG  ARG A 301     127.391  70.757  32.446  1.00 55.96      A    C  
ANISOU 2246  CG  ARG A 301     5403   9078   6782    -34   1426  -1058  A    C  
ATOM   2247  CD  ARG A 301     126.292  71.774  32.484  1.00 56.27      A    C  
ANISOU 2247  CD  ARG A 301     5294   9231   6853     -7   1418  -1289  A    C  
ATOM   2248  NE  ARG A 301     126.660  72.911  33.302  1.00 56.10      A    N  
ANISOU 2248  NE  ARG A 301     5242   9245   6828      9   1389  -1335  A    N  
ATOM   2249  CZ  ARG A 301     126.313  73.086  34.570  1.00 57.83      A    C  
ANISOU 2249  CZ  ARG A 301     5439   9574   6956   -121   1461  -1414  A    C  
ATOM   2250  NH1 ARG A 301     125.568  72.225  35.223  1.00 58.58      A    N1+
ANISOU 2250  NH1 ARG A 301     5547   9760   6950   -292   1576  -1463  A    N1+
ATOM   2251  NH2 ARG A 301     126.702  74.166  35.193  1.00 61.25      A    N  
ANISOU 2251  NH2 ARG A 301     5852  10025   7396    -89   1422  -1452  A    N  
ATOM   2252  N   LEU A 302     131.723  71.400  31.138  1.00 58.31      A    N  
ANISOU 2252  N   LEU A 302     5921   8940   7294    250   1251   -598  A    N  
ATOM   2253  CA  LEU A 302     132.866  71.969  30.439  1.00 56.16      A    C  
ANISOU 2253  CA  LEU A 302     5684   8542   7113    348   1208   -524  A    C  
ATOM   2254  C   LEU A 302     133.557  70.903  29.629  1.00 56.04      A    C  
ANISOU 2254  C   LEU A 302     5743   8409   7140    353   1247   -405  A    C  
ATOM   2255  O   LEU A 302     133.915  71.169  28.488  1.00 56.84      A    O  
ANISOU 2255  O   LEU A 302     5882   8417   7296    422   1242   -391  A    O  
ATOM   2256  CB  LEU A 302     133.830  72.625  31.412  1.00 55.49      A    C  
ANISOU 2256  CB  LEU A 302     5593   8443   7048    345   1170   -480  A    C  
ATOM   2257  CG  LEU A 302     135.014  73.315  30.774  1.00 55.37      A    C  
ANISOU 2257  CG  LEU A 302     5601   8306   7129    430   1135   -423  A    C  
ATOM   2258  CD1 LEU A 302     134.583  74.440  29.848  1.00 55.36      A    C  
ANISOU 2258  CD1 LEU A 302     5592   8292   7147    516   1090   -517  A    C  
ATOM   2259  CD2 LEU A 302     135.911  73.838  31.883  1.00 57.16      A    C  
ANISOU 2259  CD2 LEU A 302     5812   8527   7378    416   1093   -383  A    C  
ATOM   2260  N   LEU A 303     133.734  69.706  30.192  1.00 56.13      A    N  
ANISOU 2260  N   LEU A 303     5787   8417   7122    275   1285   -326  A    N  
ATOM   2261  CA  LEU A 303     134.369  68.628  29.443  1.00 57.58      A    C  
ANISOU 2261  CA  LEU A 303     6032   8489   7356    282   1325   -226  A    C  
ATOM   2262  C   LEU A 303     133.590  68.270  28.184  1.00 59.71      A    C  
ANISOU 2262  C   LEU A 303     6328   8746   7613    307   1357   -264  A    C  
ATOM   2263  O   LEU A 303     134.173  67.944  27.145  1.00 61.09      A    O  
ANISOU 2263  O   LEU A 303     6559   8809   7843    347   1387   -212  A    O  
ATOM   2264  CB  LEU A 303     134.493  67.382  30.276  1.00 59.06      A    C  
ANISOU 2264  CB  LEU A 303     6259   8675   7504    195   1337   -151  A    C  
ATOM   2265  CG  LEU A 303     135.088  66.138  29.572  1.00 59.51      A    C  
ANISOU 2265  CG  LEU A 303     6372   8618   7620    202   1374    -60  A    C  
ATOM   2266  CD1 LEU A 303     136.516  66.392  29.088  1.00 57.30      A    C  
ANISOU 2266  CD1 LEU A 303     6084   8209   7475    274   1373     -7  A    C  
ATOM   2267  CD2 LEU A 303     135.048  64.931  30.527  1.00 61.27      A    C  
ANISOU 2267  CD2 LEU A 303     6649   8841   7787    111   1358      4  A    C  
ATOM   2268  N   ALA A 304     132.266  68.349  28.259  1.00 60.16      A    N  
ANISOU 2268  N   ALA A 304     6346   8912   7601    279   1355   -366  A    N  
ATOM   2269  CA  ALA A 304     131.465  68.067  27.095  1.00 59.04      A    C  
ANISOU 2269  CA  ALA A 304     6225   8752   7452    308   1361   -416  A    C  
ATOM   2270  C   ALA A 304     131.781  69.113  26.067  1.00 61.81      A    C  
ANISOU 2270  C   ALA A 304     6607   9019   7857    410   1308   -444  A    C  
ATOM   2271  O   ALA A 304     131.865  68.823  24.867  1.00 68.19      A    O  
ANISOU 2271  O   ALA A 304     7499   9727   8681    445   1314   -419  A    O  
ATOM   2272  CB  ALA A 304     130.012  68.110  27.437  1.00 58.88      A    C  
ANISOU 2272  CB  ALA A 304     6128   8868   7374    264   1358   -549  A    C  
ATOM   2273  N   LEU A 305     131.996  70.340  26.529  1.00 60.54      A    N  
ANISOU 2273  N   LEU A 305     6400   8885   7716    449   1254   -496  A    N  
ATOM   2274  CA  LEU A 305     132.314  71.422  25.610  1.00 57.94      A    C  
ANISOU 2274  CA  LEU A 305     6122   8464   7426    538   1189   -525  A    C  
ATOM   2275  C   LEU A 305     133.636  71.156  24.924  1.00 57.65      A    C  
ANISOU 2275  C   LEU A 305     6186   8281   7435    544   1240   -405  A    C  
ATOM   2276  O   LEU A 305     133.784  71.409  23.723  1.00 58.29      A    O  
ANISOU 2276  O   LEU A 305     6373   8253   7522    581   1225   -403  A    O  
ATOM   2277  CB  LEU A 305     132.369  72.755  26.344  1.00 55.85      A    C  
ANISOU 2277  CB  LEU A 305     5789   8255   7174    573   1122   -598  A    C  
ATOM   2278  CG  LEU A 305     132.556  73.967  25.462  1.00 54.51      A    C  
ANISOU 2278  CG  LEU A 305     5684   7994   7033    662   1033   -643  A    C  
ATOM   2279  CD1 LEU A 305     131.380  74.127  24.535  1.00 55.09      A    C  
ANISOU 2279  CD1 LEU A 305     5780   8058   7093    715    951   -755  A    C  
ATOM   2280  CD2 LEU A 305     132.706  75.220  26.291  1.00 54.95      A    C  
ANISOU 2280  CD2 LEU A 305     5670   8103   7103    693    970   -706  A    C  
ATOM   2281  N   TRP A 306     134.605  70.661  25.682  1.00 57.06      A    N  
ANISOU 2281  N   TRP A 306     6085   8198   7397    502   1295   -317  A    N  
ATOM   2282  CA  TRP A 306     135.945  70.590  25.151  1.00 58.95      A    C  
ANISOU 2282  CA  TRP A 306     6384   8307   7708    507   1347   -235  A    C  
ATOM   2283  C   TRP A 306     136.066  69.484  24.154  1.00 57.23      A    C  
ANISOU 2283  C   TRP A 306     6248   8002   7494    486   1423   -185  A    C  
ATOM   2284  O   TRP A 306     136.784  69.636  23.147  1.00 57.85      A    O  
ANISOU 2284  O   TRP A 306     6416   7957   7604    493   1470   -162  A    O  
ATOM   2285  CB  TRP A 306     136.993  70.451  26.258  1.00 58.96      A    C  
ANISOU 2285  CB  TRP A 306     6317   8310   7773    481   1359   -175  A    C  
ATOM   2286  CG  TRP A 306     137.259  71.726  26.973  1.00 59.11      A    C  
ANISOU 2286  CG  TRP A 306     6286   8367   7805    509   1293   -213  A    C  
ATOM   2287  CD1 TRP A 306     136.576  72.889  26.839  1.00 59.40      A    C  
ANISOU 2287  CD1 TRP A 306     6319   8449   7799    552   1225   -300  A    C  
ATOM   2288  CD2 TRP A 306     138.284  71.973  27.934  1.00 60.47      A    C  
ANISOU 2288  CD2 TRP A 306     6403   8527   8046    500   1275   -173  A    C  
ATOM   2289  CE2 TRP A 306     138.157  73.312  28.343  1.00 59.95      A    C  
ANISOU 2289  CE2 TRP A 306     6308   8507   7963    533   1205   -233  A    C  
ATOM   2290  CE3 TRP A 306     139.299  71.191  28.489  1.00 62.72      A    C  
ANISOU 2290  CE3 TRP A 306     6659   8758   8413    473   1294   -101  A    C  
ATOM   2291  NE1 TRP A 306     137.104  73.846  27.663  1.00 59.91      A    N  
ANISOU 2291  NE1 TRP A 306     6333   8536   7891    566   1176   -311  A    N  
ATOM   2292  CZ2 TRP A 306     138.978  73.883  29.289  1.00 61.86      A    C  
ANISOU 2292  CZ2 TRP A 306     6501   8748   8254    533   1164   -214  A    C  
ATOM   2293  CZ3 TRP A 306     140.139  71.760  29.418  1.00 63.42      A    C  
ANISOU 2293  CZ3 TRP A 306     6695   8837   8563    479   1240    -88  A    C  
ATOM   2294  CH2 TRP A 306     139.969  73.099  29.813  1.00 64.80      A    C  
ANISOU 2294  CH2 TRP A 306     6848   9064   8708    505   1179   -141  A    C  
ATOM   2295  N   LEU A 307     135.347  68.402  24.407  1.00 54.82      A    N  
ANISOU 2295  N   LEU A 307     5925   7755   7147    449   1441   -174  A    N  
ATOM   2296  CA  LEU A 307     135.438  67.252  23.534  1.00 56.44      A    C  
ANISOU 2296  CA  LEU A 307     6205   7882   7356    427   1513   -124  A    C  
ATOM   2297  C   LEU A 307     134.836  67.556  22.182  1.00 59.56      A    C  
ANISOU 2297  C   LEU A 307     6709   8215   7705    457   1497   -168  A    C  
ATOM   2298  O   LEU A 307     135.195  66.943  21.197  1.00 60.13      A    O  
ANISOU 2298  O   LEU A 307     6881   8182   7782    444   1563   -129  A    O  
ATOM   2299  CB  LEU A 307     134.729  66.071  24.142  1.00 56.98      A    C  
ANISOU 2299  CB  LEU A 307     6240   8027   7379    376   1523   -105  A    C  
ATOM   2300  CG  LEU A 307     135.402  65.516  25.398  1.00 57.53      A    C  
ANISOU 2300  CG  LEU A 307     6253   8120   7486    335   1525    -45  A    C  
ATOM   2301  CD1 LEU A 307     134.607  64.368  25.999  1.00 59.01      A    C  
ANISOU 2301  CD1 LEU A 307     6442   8375   7602    267   1527    -27  A    C  
ATOM   2302  CD2 LEU A 307     136.804  65.075  25.112  1.00 56.00      A    C  
ANISOU 2302  CD2 LEU A 307     6075   7799   7403    348   1576     21  A    C  
ATOM   2303  N   HIS A 308     133.926  68.517  22.122  1.00 63.04      A    N  
ANISOU 2303  N   HIS A 308     7137   8710   8102    498   1401   -258  A    N  
ATOM   2304  CA  HIS A 308     133.363  68.941  20.836  1.00 63.26      A    C  
ANISOU 2304  CA  HIS A 308     7288   8656   8092    538   1344   -307  A    C  
ATOM   2305  C   HIS A 308     134.055  70.129  20.189  1.00 61.71      A    C  
ANISOU 2305  C   HIS A 308     7195   8348   7902    572   1308   -315  A    C  
ATOM   2306  O   HIS A 308     133.745  70.471  19.051  1.00 63.56      A    O  
ANISOU 2306  O   HIS A 308     7577   8479   8092    595   1252   -344  A    O  
ATOM   2307  CB  HIS A 308     131.919  69.315  21.015  1.00 63.75      A    C  
ANISOU 2307  CB  HIS A 308     7281   8820   8118    575   1235   -424  A    C  
ATOM   2308  CG  HIS A 308     131.014  68.145  21.139  1.00 62.43      A    C  
ANISOU 2308  CG  HIS A 308     7069   8726   7922    533   1264   -435  A    C  
ATOM   2309  CD2 HIS A 308     130.451  67.575  22.222  1.00 63.76      A    C  
ANISOU 2309  CD2 HIS A 308     7113   9034   8078    480   1295   -457  A    C  
ATOM   2310  ND1 HIS A 308     130.536  67.462  20.048  1.00 60.94      A    N  
ANISOU 2310  ND1 HIS A 308     6985   8462   7706    534   1259   -432  A    N  
ATOM   2311  CE1 HIS A 308     129.730  66.506  20.455  1.00 62.87      A    C  
ANISOU 2311  CE1 HIS A 308     7157   8801   7930    488   1286   -451  A    C  
ATOM   2312  NE2 HIS A 308     129.650  66.562  21.771  1.00 64.84      A    N  
ANISOU 2312  NE2 HIS A 308     7271   9180   8183    449   1312   -467  A    N  
ATOM   2313  N   HIS A 309     134.954  70.771  20.914  1.00 60.54      A    N  
ANISOU 2313  N   HIS A 309     6984   8213   7804    569   1327   -293  A    N  
ATOM   2314  CA  HIS A 309     135.701  71.874  20.356  1.00 62.71      A    C  
ANISOU 2314  CA  HIS A 309     7361   8379   8085    584   1307   -297  A    C  
ATOM   2315  C   HIS A 309     137.206  71.704  20.561  1.00 63.96      A    C  
ANISOU 2315  C   HIS A 309     7506   8475   8318    534   1430   -224  A    C  
ATOM   2316  O   HIS A 309     137.807  72.380  21.391  1.00 65.89      A    O  
ANISOU 2316  O   HIS A 309     7663   8757   8615    542   1416   -225  A    O  
ATOM   2317  CB  HIS A 309     135.212  73.168  20.958  1.00 62.60      A    C  
ANISOU 2317  CB  HIS A 309     7281   8436   8065    644   1177   -379  A    C  
ATOM   2318  CG  HIS A 309     133.763  73.433  20.715  1.00 62.45      A    C  
ANISOU 2318  CG  HIS A 309     7255   8468   8002    702   1047   -484  A    C  
ATOM   2319  CD2 HIS A 309     133.139  74.338  19.924  1.00 65.48      A    C  
ANISOU 2319  CD2 HIS A 309     7743   8780   8355    765    906   -567  A    C  
ATOM   2320  ND1 HIS A 309     132.769  72.724  21.339  1.00 62.60      A    N  
ANISOU 2320  ND1 HIS A 309     7146   8621   8017    696   1046   -530  A    N  
ATOM   2321  CE1 HIS A 309     131.590  73.174  20.939  1.00 64.90      A    C  
ANISOU 2321  CE1 HIS A 309     7436   8929   8290    755    919   -647  A    C  
ATOM   2322  NE2 HIS A 309     131.785  74.156  20.082  1.00 65.80      A    N  
ANISOU 2322  NE2 HIS A 309     7692   8917   8392    806    818   -672  A    N  
ATOM   2323  N   PRO A 310     137.811  70.774  19.806  1.00 63.51      A    N  
ANISOU 2323  N   PRO A 310     7529   8323   8278    482   1552   -171  A    N  
ATOM   2324  CA  PRO A 310     139.236  70.596  19.883  1.00 62.82      A    C  
ANISOU 2324  CA  PRO A 310     7416   8166   8283    432   1675   -131  A    C  
ATOM   2325  C   PRO A 310     139.901  71.793  19.264  1.00 65.81      A    C  
ANISOU 2325  C   PRO A 310     7910   8442   8651    413   1681   -154  A    C  
ATOM   2326  O   PRO A 310     139.521  72.214  18.165  1.00 63.19      A    O  
ANISOU 2326  O   PRO A 310     7767   8016   8227    403   1652   -174  A    O  
ATOM   2327  CB  PRO A 310     139.489  69.343  19.039  1.00 64.05      A    C  
ANISOU 2327  CB  PRO A 310     7648   8241   8444    383   1800    -97  A    C  
ATOM   2328  CG  PRO A 310     138.158  68.696  18.809  1.00 63.97      A    C  
ANISOU 2328  CG  PRO A 310     7671   8286   8348    408   1733   -102  A    C  
ATOM   2329  CD  PRO A 310     137.173  69.817  18.881  1.00 64.37      A    C  
ANISOU 2329  CD  PRO A 310     7742   8387   8327    465   1580   -161  A    C  
ATOM   2330  N   LEU A 311     140.898  72.337  19.958  1.00 41.56      A    N  
ATOM   2331  CA  LEU A 311     141.491  73.601  19.529  1.00 47.59      A    C  
ATOM   2332  C   LEU A 311     142.424  73.387  18.350  1.00 51.67      A    C  
ATOM   2333  O   LEU A 311     143.054  72.341  18.247  1.00 48.51      A    O  
ATOM   2334  CB  LEU A 311     142.258  74.252  20.664  1.00 49.29      A    C  
ATOM   2335  CG  LEU A 311     141.608  74.220  22.048  1.00 53.19      A    C  
ATOM   2336  CD1 LEU A 311     142.458  74.900  23.111  1.00 52.82      A    C  
ATOM   2337  CD2 LEU A 311     140.257  74.881  21.962  1.00 57.37      A    C  
ATOM   2338  N   ARG A 312     142.477  74.365  17.445  1.00 58.61      A    N  
ATOM   2339  CA  ARG A 312     143.521  74.417  16.415  1.00 56.95      A    C  
ATOM   2340  C   ARG A 312     144.745  75.140  16.982  1.00 57.54      A    C  
ATOM   2341  O   ARG A 312     145.869  74.695  16.767  1.00 78.42      A    O  
ATOM   2342  CB  ARG A 312     143.055  75.097  15.112  1.00 53.54      A    C  
ATOM   2343  CG  ARG A 312     141.861  74.441  14.445  1.00 55.63      A    C  
ATOM   2344  CD  ARG A 312     142.243  73.685  13.204  1.00 61.88      A    C  
ATOM   2345  NE  ARG A 312     141.949  74.418  11.971  1.00 67.42      A    N  
ATOM   2346  CZ  ARG A 312     142.859  74.733  11.042  1.00 79.79      A    C  
ATOM   2347  NH1 ARG A 312     144.163  74.398  11.182  1.00 77.83      A    N1+
ATOM   2348  NH2 ARG A 312     142.463  75.395   9.953  1.00 77.64      A    N  
ATOM   2349  N   ASN A 313     144.549  76.240  17.699  1.00 97.04      A    N  
ANISOU 2349  N   ASN A 313    12085  13760  11026    553   1035    612  A    N  
ATOM   2350  CA  ASN A 313     145.692  76.982  18.229  1.00 96.09      A    C  
ANISOU 2350  CA  ASN A 313    12029  13329  11152    407   1230    584  A    C  
ATOM   2351  C   ASN A 313     146.577  76.127  19.155  1.00 86.75      A    C  
ANISOU 2351  C   ASN A 313    10742  12084  10132    146   1087    369  A    C  
ATOM   2352  O   ASN A 313     146.166  75.768  20.247  1.00 77.65      A    O  
ANISOU 2352  O   ASN A 313     9510  10970   9024     35    911    259  A    O  
ATOM   2353  CB  ASN A 313     145.204  78.236  18.946  1.00100.58      A    C  
ANISOU 2353  CB  ASN A 313    12657  13737  11818    422   1356    639  A    C  
ATOM   2354  CG  ASN A 313     146.348  79.090  19.457  1.00105.86      A    C  
ANISOU 2354  CG  ASN A 313    13366  14098  12755    265   1592    564  A    C  
ATOM   2355  ND2 ASN A 313     146.746  80.091  18.675  1.00111.18      A    N  
ANISOU 2355  ND2 ASN A 313    14167  14586  13489    387   1929    713  A    N  
ATOM   2356  OD1 ASN A 313     146.876  78.846  20.542  1.00105.39      A    O  
ANISOU 2356  OD1 ASN A 313    13215  13981  12848     46   1491    364  A    O  
ATOM   2357  N   ARG A 314     147.791  75.799  18.713  1.00 88.83      A    N  
ANISOU 2357  N   ARG A 314    11009  12264  10478     73   1176    323  A    N  
ATOM   2358  CA  ARG A 314     148.597  74.787  19.424  1.00 89.08      A    C  
ANISOU 2358  CA  ARG A 314    10928  12299  10617   -127   1023    136  A    C  
ATOM   2359  C   ARG A 314     149.182  75.361  20.699  1.00 86.17      A    C  
ANISOU 2359  C   ARG A 314    10514  11776  10449   -293   1055     -1  A    C  
ATOM   2360  O   ARG A 314     149.658  74.619  21.550  1.00 89.29      A    O  
ANISOU 2360  O   ARG A 314    10803  12213  10908   -424    908   -145  A    O  
ATOM   2361  CB  ARG A 314     149.674  74.147  18.518  1.00 92.33      A    C  
ANISOU 2361  CB  ARG A 314    11341  12702  11038   -145   1087    118  A    C  
ATOM   2362  CG  ARG A 314     149.089  73.502  17.244  1.00103.93      A    C  
ANISOU 2362  CG  ARG A 314    12825  14380  12282     25   1041    220  A    C  
ATOM   2363  CD  ARG A 314     149.881  72.312  16.710  1.00111.02      A    C  
ANISOU 2363  CD  ARG A 314    13661  15347  13172    -43    975    132  A    C  
ATOM   2364  NE  ARG A 314     151.319  72.606  16.705  1.00129.32      A    N  
ANISOU 2364  NE  ARG A 314    16008  17458  15670   -153   1141     87  A    N  
ATOM   2365  CZ  ARG A 314     152.053  72.877  15.624  1.00146.39      A    C  
ANISOU 2365  CZ  ARG A 314    18247  19551  17820    -80   1342    169  A    C  
ATOM   2366  NH1 ARG A 314     151.502  72.873  14.422  1.00162.40      A    N1+
ANISOU 2366  NH1 ARG A 314    20336  21734  19634    131   1393    316  A    N1+
ATOM   2367  NH2 ARG A 314     153.355  73.150  15.745  1.00146.79      A    N  
ANISOU 2367  NH2 ARG A 314    18305  19400  18067   -209   1500     92  A    N  
ATOM   2368  N   ALA A 315     149.119  76.682  20.840  1.00 84.59      A    N  
ANISOU 2368  N   ALA A 315    10384  11413  10339   -272   1260     41  A    N  
ATOM   2369  CA  ALA A 315     149.594  77.360  22.044  1.00 84.62      A    C  
ANISOU 2369  CA  ALA A 315    10323  11298  10528   -429   1308   -127  A    C  
ATOM   2370  C   ALA A 315     148.642  77.140  23.216  1.00 87.04      A    C  
ANISOU 2370  C   ALA A 315    10560  11734  10778   -452   1083   -175  A    C  
ATOM   2371  O   ALA A 315     149.064  76.810  24.332  1.00 84.24      A    O  
ANISOU 2371  O   ALA A 315    10088  11429  10487   -577    960   -341  A    O  
ATOM   2372  CB  ALA A 315     149.744  78.848  21.784  1.00 86.06      A    C  
ANISOU 2372  CB  ALA A 315    10600  11248  10849   -405   1636    -81  A    C  
ATOM   2373  N   HIS A 316     147.351  77.357  22.963  1.00 87.99      A    N  
ANISOU 2373  N   HIS A 316    10747  11920  10763   -312   1041    -25  A    N  
ATOM   2374  CA  HIS A 316     146.329  77.138  23.971  1.00 80.48      A    C  
ANISOU 2374  CA  HIS A 316     9741  11083   9752   -319    844    -51  A    C  
ATOM   2375  C   HIS A 316     146.357  75.683  24.388  1.00 76.82      A    C  
ANISOU 2375  C   HIS A 316     9179  10777   9229   -371    609   -124  A    C  
ATOM   2376  O   HIS A 316     146.251  75.374  25.571  1.00 76.68      A    O  
ANISOU 2376  O   HIS A 316     9082  10812   9239   -441    481   -216  A    O  
ATOM   2377  CB  HIS A 316     144.961  77.515  23.437  1.00 81.81      A    C  
ANISOU 2377  CB  HIS A 316     9986  11318   9777   -148    845    117  A    C  
ATOM   2378  CG  HIS A 316     144.811  78.982  23.161  1.00 90.95      A    C  
ANISOU 2378  CG  HIS A 316    11249  12307  10998    -68   1100    215  A    C  
ATOM   2379  CD2 HIS A 316     145.463  80.056  23.668  1.00 93.09      A    C  
ANISOU 2379  CD2 HIS A 316    11534  12370  11464   -167   1308    134  A    C  
ATOM   2380  ND1 HIS A 316     143.904  79.482  22.246  1.00 96.36      A    N  
ANISOU 2380  ND1 HIS A 316    12029  13035  11546    145   1190    415  A    N  
ATOM   2381  CE1 HIS A 316     144.002  80.798  22.205  1.00 95.45      A    C  
ANISOU 2381  CE1 HIS A 316    12004  12715  11546    187   1460    486  A    C  
ATOM   2382  NE2 HIS A 316     144.937  81.171  23.060  1.00 94.76      A    N  
ANISOU 2382  NE2 HIS A 316    11867  12461  11677    -17   1544    302  A    N  
ATOM   2383  N   ILE A 317     146.546  74.790  23.421  1.00 73.05      A    N  
ANISOU 2383  N   ILE A 317     8707  10372   8676   -328    575    -83  A    N  
ATOM   2384  CA  ILE A 317     146.560  73.371  23.716  1.00 69.21      A    C  
ANISOU 2384  CA  ILE A 317     8132  10003   8158   -375    398   -149  A    C  
ATOM   2385  C   ILE A 317     147.700  73.038  24.679  1.00 69.72      A    C  
ANISOU 2385  C   ILE A 317     8114  10033   8344   -499    367   -280  A    C  
ATOM   2386  O   ILE A 317     147.514  72.286  25.620  1.00 66.25      A    O  
ANISOU 2386  O   ILE A 317     7599   9668   7903   -524    236   -326  A    O  
ATOM   2387  CB  ILE A 317     146.660  72.536  22.441  1.00 67.11      A    C  
ANISOU 2387  CB  ILE A 317     7874   9818   7804   -319    396   -111  A    C  
ATOM   2388  CG1 ILE A 317     145.496  72.828  21.519  1.00 66.41      A    C  
ANISOU 2388  CG1 ILE A 317     7834   9843   7555   -164    407     -3  A    C  
ATOM   2389  CG2 ILE A 317     146.671  71.056  22.774  1.00 66.97      A    C  
ANISOU 2389  CG2 ILE A 317     7762   9890   7793   -380    253   -193  A    C  
ATOM   2390  CD1 ILE A 317     145.575  72.073  20.210  1.00 69.15      A    C  
ANISOU 2390  CD1 ILE A 317     8167  10321   7783    -89    407     12  A    C  
ATOM   2391  N   ARG A 318     148.871  73.622  24.438  1.00 76.97      A    N  
ANISOU 2391  N   ARG A 318     9036  10843   9364   -560    507   -340  A    N  
ATOM   2392  CA  ARG A 318     150.040  73.426  25.309  1.00 81.44      A    C  
ANISOU 2392  CA  ARG A 318     9493  11413  10034   -668    487   -499  A    C  
ATOM   2393  C   ARG A 318     149.811  74.119  26.688  1.00 79.14      A    C  
ANISOU 2393  C   ARG A 318     9134  11154   9777   -705    448   -594  A    C  
ATOM   2394  O   ARG A 318     150.192  73.622  27.750  1.00 68.93      A    O  
ANISOU 2394  O   ARG A 318     7729   9977   8483   -729    335   -691  A    O  
ATOM   2395  CB  ARG A 318     151.305  73.955  24.612  1.00 88.60      A    C  
ANISOU 2395  CB  ARG A 318    10411  12195  11058   -734    675   -570  A    C  
ATOM   2396  CG  ARG A 318     152.605  73.286  25.044  1.00 97.55      A    C  
ANISOU 2396  CG  ARG A 318    11418  13382  12265   -824    632   -724  A    C  
ATOM   2397  CD  ARG A 318     153.757  73.506  24.063  1.00105.97      A    C  
ANISOU 2397  CD  ARG A 318    12506  14324  13433   -880    815   -771  A    C  
ATOM   2398  NE  ARG A 318     153.455  72.960  22.738  1.00107.99      A    N  
ANISOU 2398  NE  ARG A 318    12871  14557  13601   -796    841   -609  A    N  
ATOM   2399  CZ  ARG A 318     153.237  73.690  21.649  1.00117.23      A    C  
ANISOU 2399  CZ  ARG A 318    14169  15612  14760   -728   1026   -488  A    C  
ATOM   2400  NH1 ARG A 318     153.302  75.027  21.698  1.00120.76      A    N1+
ANISOU 2400  NH1 ARG A 318    14667  15902  15311   -743   1237   -499  A    N1+
ATOM   2401  NH2 ARG A 318     152.959  73.082  20.498  1.00122.89      A    N  
ANISOU 2401  NH2 ARG A 318    14956  16378  15357   -629   1020   -357  A    N  
ATOM   2402  N   ALA A 319     149.160  75.272  26.666  1.00 80.76      A    N  
ANISOU 2402  N   ALA A 319     9408  11274  10001   -687    551   -558  A    N  
ATOM   2403  CA  ALA A 319     148.819  75.946  27.909  1.00 80.59      A    C  
ANISOU 2403  CA  ALA A 319     9325  11291  10004   -719    517   -650  A    C  
ATOM   2404  C   ALA A 319     148.082  74.990  28.813  1.00 77.16      A    C  
ANISOU 2404  C   ALA A 319     8841  11018   9457   -663    304   -611  A    C  
ATOM   2405  O   ALA A 319     148.346  74.941  30.010  1.00 75.64      A    O  
ANISOU 2405  O   ALA A 319     8541  10937   9259   -683    224   -721  A    O  
ATOM   2406  CB  ALA A 319     147.961  77.179  27.638  1.00 80.33      A    C  
ANISOU 2406  CB  ALA A 319     9394  11134   9993   -682    657   -573  A    C  
ATOM   2407  N   ARG A 320     147.144  74.254  28.219  1.00 76.74      A    N  
ANISOU 2407  N   ARG A 320     8857  10986   9312   -584    232   -461  A    N  
ATOM   2408  CA  ARG A 320     146.320  73.297  28.945  1.00 75.82      A    C  
ANISOU 2408  CA  ARG A 320     8710  10979   9119   -533     80   -413  A    C  
ATOM   2409  C   ARG A 320     147.166  72.102  29.378  1.00 73.61      A    C  
ANISOU 2409  C   ARG A 320     8341  10778   8847   -539      9   -457  A    C  
ATOM   2410  O   ARG A 320     147.026  71.606  30.499  1.00 69.20      A    O  
ANISOU 2410  O   ARG A 320     7720  10314   8257   -498    -72   -463  A    O  
ATOM   2411  CB  ARG A 320     145.135  72.829  28.079  1.00 76.27      A    C  
ANISOU 2411  CB  ARG A 320     8836  11040   9100   -465     54   -294  A    C  
ATOM   2412  CG  ARG A 320     144.000  73.850  27.873  1.00 75.17      A    C  
ANISOU 2412  CG  ARG A 320     8770  10873   8918   -410     92   -224  A    C  
ATOM   2413  CD  ARG A 320     142.775  73.160  27.256  1.00 75.23      A    C  
ANISOU 2413  CD  ARG A 320     8790  10960   8831   -337     28   -153  A    C  
ATOM   2414  NE  ARG A 320     141.751  74.068  26.756  1.00 73.96      A    N  
ANISOU 2414  NE  ARG A 320     8692  10808   8601   -252     69    -76  A    N  
ATOM   2415  CZ  ARG A 320     140.765  73.701  25.942  1.00 72.80      A    C  
ANISOU 2415  CZ  ARG A 320     8541  10769   8349   -168     33    -37  A    C  
ATOM   2416  NH1 ARG A 320     140.663  72.453  25.554  1.00 72.91      A    N1+
ANISOU 2416  NH1 ARG A 320     8490  10871   8340   -186    -31    -92  A    N1+
ATOM   2417  NH2 ARG A 320     139.870  74.584  25.510  1.00 74.53      A    N  
ANISOU 2417  NH2 ARG A 320     8807  11022   8485    -60     73     43  A    N  
ATOM   2418  N   GLN A 321     148.045  71.659  28.482  1.00 72.66      A    N  
ANISOU 2418  N   GLN A 321     8223  10621   8763   -571     56   -475  A    N  
ATOM   2419  CA  GLN A 321     148.910  70.517  28.748  1.00 72.49      A    C  
ANISOU 2419  CA  GLN A 321     8123  10663   8756   -569      8   -508  A    C  
ATOM   2420  C   GLN A 321     149.921  70.823  29.841  1.00 76.91      A    C  
ANISOU 2420  C   GLN A 321     8565  11320   9336   -582    -12   -636  A    C  
ATOM   2421  O   GLN A 321     150.274  69.941  30.618  1.00 76.91      A    O  
ANISOU 2421  O   GLN A 321     8485  11432   9303   -518    -80   -633  A    O  
ATOM   2422  CB  GLN A 321     149.643  70.084  27.486  1.00 72.63      A    C  
ANISOU 2422  CB  GLN A 321     8166  10617   8810   -607     73   -509  A    C  
ATOM   2423  CG  GLN A 321     148.801  69.236  26.574  1.00 73.09      A    C  
ANISOU 2423  CG  GLN A 321     8280  10665   8823   -573     58   -420  A    C  
ATOM   2424  CD  GLN A 321     149.488  68.937  25.278  1.00 73.70      A    C  
ANISOU 2424  CD  GLN A 321     8383  10702   8916   -601    125   -427  A    C  
ATOM   2425  NE2 GLN A 321     148.830  68.140  24.435  1.00 76.27      A    N  
ANISOU 2425  NE2 GLN A 321     8725  11059   9192   -575    112   -392  A    N  
ATOM   2426  OE1 GLN A 321     150.582  69.437  25.015  1.00 70.79      A    O  
ANISOU 2426  OE1 GLN A 321     8009  10284   8603   -648    201   -482  A    O  
ATOM   2427  N   GLU A 322     150.412  72.060  29.887  1.00 81.53      A    N  
ANISOU 2427  N   GLU A 322     9127  11874   9976   -655     66   -758  A    N  
ATOM   2428  CA  GLU A 322     151.372  72.434  30.915  1.00 85.10      A    C  
ANISOU 2428  CA  GLU A 322     9426  12461  10443   -679     50   -943  A    C  
ATOM   2429  C   GLU A 322     150.669  72.280  32.239  1.00 85.19      A    C  
ANISOU 2429  C   GLU A 322     9386  12630  10351   -583    -65   -914  A    C  
ATOM   2430  O   GLU A 322     151.267  71.874  33.217  1.00 90.56      A    O  
ANISOU 2430  O   GLU A 322     9935  13506  10967   -513   -139   -988  A    O  
ATOM   2431  CB  GLU A 322     151.867  73.875  30.729  1.00 89.50      A    C  
ANISOU 2431  CB  GLU A 322     9961  12931  11113   -797    196  -1114  A    C  
ATOM   2432  CG  GLU A 322     152.967  74.024  29.686  1.00 95.85      A    C  
ANISOU 2432  CG  GLU A 322    10769  13611  12037   -890    339  -1192  A    C  
ATOM   2433  CD  GLU A 322     153.217  75.472  29.250  1.00100.87      A    C  
ANISOU 2433  CD  GLU A 322    11431  14069  12822  -1000    563  -1310  A    C  
ATOM   2434  OE1 GLU A 322     152.700  76.390  29.951  1.00100.43      A    O  
ANISOU 2434  OE1 GLU A 322    11353  14020  12784  -1022    593  -1384  A    O  
ATOM   2435  OE2 GLU A 322     153.920  75.677  28.204  1.00 93.50      A    O1-
ANISOU 2435  OE2 GLU A 322    10548  12978  11996  -1061    730  -1323  A    O1-
ATOM   2436  N   ALA A 323     149.384  72.604  32.265  1.00 85.82      A    N  
ANISOU 2436  N   ALA A 323     9567  12639  10401   -557    -73   -802  A    N  
ATOM   2437  CA  ALA A 323     148.635  72.584  33.499  1.00 90.39      A    C  
ANISOU 2437  CA  ALA A 323    10110  13345  10888   -470   -159   -771  A    C  
ATOM   2438  C   ALA A 323     148.443  71.148  33.959  1.00 88.69      A    C  
ANISOU 2438  C   ALA A 323     9885  13212  10599   -341   -232   -634  A    C  
ATOM   2439  O   ALA A 323     148.615  70.819  35.136  1.00 91.37      A    O  
ANISOU 2439  O   ALA A 323    10135  13733  10849   -227   -291   -638  A    O  
ATOM   2440  CB  ALA A 323     147.289  73.282  33.318  1.00 93.58      A    C  
ANISOU 2440  CB  ALA A 323    10627  13636  11292   -481   -135   -684  A    C  
ATOM   2441  N   VAL A 324     148.078  70.279  33.037  1.00 84.57      A    N  
ANISOU 2441  N   VAL A 324     9452  12564  10116   -345   -207   -513  A    N  
ATOM   2442  CA  VAL A 324     147.721  68.935  33.451  1.00 85.51      A    C  
ANISOU 2442  CA  VAL A 324     9577  12707  10207   -235   -222   -383  A    C  
ATOM   2443  C   VAL A 324     148.945  68.212  33.984  1.00 88.40      A    C  
ANISOU 2443  C   VAL A 324     9834  13208  10546   -152   -236   -409  A    C  
ATOM   2444  O   VAL A 324     148.828  67.478  34.955  1.00 90.12      A    O  
ANISOU 2444  O   VAL A 324    10017  13526  10699     -2   -243   -316  A    O  
ATOM   2445  CB  VAL A 324     147.013  68.138  32.337  1.00 84.82      A    C  
ANISOU 2445  CB  VAL A 324     9580  12465  10183   -276   -175   -297  A    C  
ATOM   2446  CG1 VAL A 324     147.763  68.251  31.028  1.00 89.79      A    C  
ANISOU 2446  CG1 VAL A 324    10226  13022  10866   -374   -139   -359  A    C  
ATOM   2447  CG2 VAL A 324     146.846  66.686  32.741  1.00 83.19      A    C  
ANISOU 2447  CG2 VAL A 324     9361  12249   9997   -182   -136   -195  A    C  
ATOM   2448  N   THR A 325     150.114  68.436  33.371  1.00 92.98      A    N  
ANISOU 2448  N   THR A 325    10361  13796  11170   -231   -223   -529  A    N  
ATOM   2449  CA  THR A 325     151.373  67.825  33.856  1.00 90.33      A    C  
ANISOU 2449  CA  THR A 325     9899  13620  10799   -147   -243   -580  A    C  
ATOM   2450  C   THR A 325     151.680  68.358  35.231  1.00 86.08      A    C  
ANISOU 2450  C   THR A 325     9226  13341  10140    -41   -312   -671  A    C  
ATOM   2451  O   THR A 325     152.130  67.608  36.074  1.00 87.79      A    O  
ANISOU 2451  O   THR A 325     9353  13742  10259    135   -340   -618  A    O  
ATOM   2452  CB  THR A 325     152.604  68.134  32.981  1.00 91.28      A    C  
ANISOU 2452  CB  THR A 325     9969  13712  10998   -270   -211   -732  A    C  
ATOM   2453  CG2 THR A 325     152.552  67.403  31.666  1.00 89.31      A    C  
ANISOU 2453  CG2 THR A 325     9825  13269  10840   -339   -149   -648  A    C  
ATOM   2454  OG1 THR A 325     152.671  69.545  32.729  1.00108.30      A    O  
ANISOU 2454  OG1 THR A 325    12120  15827  13202   -404   -179   -887  A    O  
ATOM   2455  N   ALA A 326     151.426  69.648  35.453  1.00 84.25      A    N  
ANISOU 2455  N   ALA A 326     8972  13131   9906   -131   -325   -807  A    N  
ATOM   2456  CA  ALA A 326     151.672  70.273  36.759  1.00 88.98      A    C  
ANISOU 2456  CA  ALA A 326     9417  14005  10383    -46   -390   -943  A    C  
ATOM   2457  C   ALA A 326     150.754  69.738  37.857  1.00 90.43      A    C  
ANISOU 2457  C   ALA A 326     9626  14300  10431    153   -433   -763  A    C  
ATOM   2458  O   ALA A 326     151.127  69.718  39.036  1.00 87.06      A    O  
ANISOU 2458  O   ALA A 326     9058  14172   9848    318   -493   -812  A    O  
ATOM   2459  CB  ALA A 326     151.558  71.797  36.676  1.00 87.04      A    C  
ANISOU 2459  CB  ALA A 326     9148  13719  10204   -212   -357  -1149  A    C  
ATOM   2460  N   LEU A 327     149.558  69.301  37.468  1.00 90.05      A    N  
ANISOU 2460  N   LEU A 327     9746  14030  10436    147   -390   -565  A    N  
ATOM   2461  CA  LEU A 327     148.575  68.840  38.442  1.00 89.41      A    C  
ANISOU 2461  CA  LEU A 327     9708  14002  10261    314   -390   -392  A    C  
ATOM   2462  C   LEU A 327     148.769  67.382  38.814  1.00 90.35      A    C  
ANISOU 2462  C   LEU A 327     9831  14155  10341    515   -336   -198  A    C  
ATOM   2463  O   LEU A 327     148.044  66.857  39.667  1.00 88.60      A    O  
ANISOU 2463  O   LEU A 327     9646  13965  10050    686   -292    -29  A    O  
ATOM   2464  CB  LEU A 327     147.169  69.017  37.881  1.00 87.78      A    C  
ANISOU 2464  CB  LEU A 327     9659  13545  10146    214   -347   -294  A    C  
ATOM   2465  CG  LEU A 327     146.610  70.425  37.832  1.00 85.31      A    C  
ANISOU 2465  CG  LEU A 327     9364  13202   9847     87   -375   -414  A    C  
ATOM   2466  CD1 LEU A 327     145.190  70.374  37.291  1.00 84.00      A    C  
ANISOU 2466  CD1 LEU A 327     9342  12823   9749     33   -334   -291  A    C  
ATOM   2467  CD2 LEU A 327     146.637  71.046  39.209  1.00 86.99      A    C  
ANISOU 2467  CD2 LEU A 327     9468  13663   9921    192   -433   -491  A    C  
ATOM   2468  N   GLU A 328     149.732  66.732  38.168  1.00 91.53      A    N  
ANISOU 2468  N   GLU A 328     9949  14279  10547    497   -313   -215  A    N  
ATOM   2469  CA  GLU A 328     149.923  65.294  38.305  1.00 97.73      A    C  
ANISOU 2469  CA  GLU A 328    10756  15033  11342    666   -221    -25  A    C  
ATOM   2470  C   GLU A 328     150.212  64.918  39.744  1.00 93.12      A    C  
ANISOU 2470  C   GLU A 328    10076  14737  10567    967   -224     81  A    C  
ATOM   2471  O   GLU A 328     149.843  63.840  40.181  1.00 90.10      A    O  
ANISOU 2471  O   GLU A 328     9753  14295  10182   1158    -99    307  A    O  
ATOM   2472  CB  GLU A 328     151.062  64.816  37.391  1.00113.08      A    C  
ANISOU 2472  CB  GLU A 328    12660  16934  13368    590   -208    -95  A    C  
ATOM   2473  CG  GLU A 328     151.233  63.297  37.319  1.00127.17      A    C  
ANISOU 2473  CG  GLU A 328    14484  18625  15210    732    -80     94  A    C  
ATOM   2474  CD  GLU A 328     152.694  62.849  37.178  1.00136.09      A    C  
ANISOU 2474  CD  GLU A 328    15497  19898  16314    798    -97     37  A    C  
ATOM   2475  OE1 GLU A 328     152.954  61.622  37.245  1.00136.60      A    O  
ANISOU 2475  OE1 GLU A 328    15578  19910  16413    947     21    198  A    O  
ATOM   2476  OE2 GLU A 328     153.590  63.707  36.992  1.00140.13      A    O1-
ANISOU 2476  OE2 GLU A 328    15895  20561  16786    700   -204   -179  A    O1-
ATOM   2477  N   SER A 329     150.868  65.820  40.470  1.00 93.89      A    N  
ANISOU 2477  N   SER A 329    10014  15153  10507   1018   -346    -95  A    N  
ATOM   2478  CA  SER A 329     151.323  65.551  41.832  1.00 96.57      A    C  
ANISOU 2478  CA  SER A 329    10215  15864  10610   1337   -374    -34  A    C  
ATOM   2479  C   SER A 329     150.386  66.103  42.906  1.00 95.15      A    C  
ANISOU 2479  C   SER A 329    10041  15817  10292   1453   -397     15  A    C  
ATOM   2480  O   SER A 329     150.697  65.991  44.079  1.00 96.06      A    O  
ANISOU 2480  O   SER A 329    10035  16283  10177   1737   -427     60  A    O  
ATOM   2481  CB  SER A 329     152.717  66.154  42.043  1.00102.83      A    C  
ANISOU 2481  CB  SER A 329    10776  17007  11288   1342   -499   -310  A    C  
ATOM   2482  OG  SER A 329     152.665  67.578  42.162  1.00113.06      A    O  
ANISOU 2482  OG  SER A 329    11981  18406  12571   1159   -596   -593  A    O  
ATOM   2483  N   GLN A 330     149.246  66.683  42.517  1.00 92.98      A    N  
ANISOU 2483  N   GLN A 330     9901  15286  10138   1256   -382     12  A    N  
ATOM   2484  CA  GLN A 330     148.407  67.443  43.456  1.00 87.93      A    C  
ANISOU 2484  CA  GLN A 330     9255  14772   9379   1317   -422      2  A    C  
ATOM   2485  C   GLN A 330     146.910  67.425  43.117  1.00 83.97      A    C  
ANISOU 2485  C   GLN A 330     8948  13934   9020   1202   -337    142  A    C  
ATOM   2486  O   GLN A 330     146.192  68.348  43.491  1.00 81.53      A    O  
ANISOU 2486  O   GLN A 330     8648  13651   8678   1138   -385     68  A    O  
ATOM   2487  CB  GLN A 330     148.915  68.896  43.519  1.00 88.80      A    C  
ANISOU 2487  CB  GLN A 330     9214  15079   9447   1148   -555   -335  A    C  
ATOM   2488  CG  GLN A 330     149.253  69.512  42.164  1.00 91.39      A    C  
ANISOU 2488  CG  GLN A 330     9576  15160   9988    826   -560   -521  A    C  
ATOM   2489  CD  GLN A 330     149.956  70.872  42.250  1.00 98.96      A    C  
ANISOU 2489  CD  GLN A 330    10366  16297  10935    668   -633   -873  A    C  
ATOM   2490  NE2 GLN A 330     149.986  71.592  41.112  1.00104.60      A    N  
ANISOU 2490  NE2 GLN A 330    11148  16744  11850    393   -590  -1002  A    N  
ATOM   2491  OE1 GLN A 330     150.468  71.275  43.303  1.00100.05      A    O  
ANISOU 2491  OE1 GLN A 330    10308  16813  10893    797   -706  -1036  A    O  
ATOM   2492  N   TYR A 331     146.429  66.389  42.423  1.00 82.74      A    N  
ANISOU 2492  N   TYR A 331     8932  13477   9029   1173   -204    320  A    N  
ATOM   2493  CA  TYR A 331     145.002  66.314  42.037  1.00 81.03      A    C  
ANISOU 2493  CA  TYR A 331     8870  12960   8956   1055   -118    409  A    C  
ATOM   2494  C   TYR A 331     144.075  65.635  43.077  1.00 80.51      A    C  
ANISOU 2494  C   TYR A 331     8873  12875   8842   1280     23    645  A    C  
ATOM   2495  O   TYR A 331     142.873  65.821  43.046  1.00 77.90      A    O  
ANISOU 2495  O   TYR A 331     8636  12370   8592   1199     75    681  A    O  
ATOM   2496  CB  TYR A 331     144.815  65.699  40.615  1.00 80.09      A    C  
ANISOU 2496  CB  TYR A 331     8845  12527   9058    856    -43    407  A    C  
ATOM   2497  CG  TYR A 331     145.113  64.218  40.485  1.00 81.55      A    C  
ANISOU 2497  CG  TYR A 331     9060  12599   9327    976    119    570  A    C  
ATOM   2498  CD1 TYR A 331     144.242  63.264  40.991  1.00 84.73      A    C  
ANISOU 2498  CD1 TYR A 331     9545  12852   9796   1110    314    770  A    C  
ATOM   2499  CD2 TYR A 331     146.251  63.772  39.867  1.00 82.07      A    C  
ANISOU 2499  CD2 TYR A 331     9073  12685   9424    954    106    521  A    C  
ATOM   2500  CE1 TYR A 331     144.513  61.909  40.895  1.00 83.07      A    C  
ANISOU 2500  CE1 TYR A 331     9363  12508   9692   1223    511    918  A    C  
ATOM   2501  CE2 TYR A 331     146.523  62.424  39.773  1.00 84.23      A    C  
ANISOU 2501  CE2 TYR A 331     9372  12845   9784   1068    273    670  A    C  
ATOM   2502  CZ  TYR A 331     145.644  61.500  40.301  1.00 83.20      A    C  
ANISOU 2502  CZ  TYR A 331     9327  12555   9730   1205    485    871  A    C  
ATOM   2503  OH  TYR A 331     145.880  60.153  40.249  1.00 84.67      A    O  
ANISOU 2503  OH  TYR A 331     9543  12594  10033   1325    704   1024  A    O  
ATOM   2504  N   GLU A 332     144.629  64.860  43.995  1.00 88.36      A    N  
ANISOU 2504  N   GLU A 332     9820  14049   9701   1579    103    811  A    N  
ATOM   2505  CA  GLU A 332     143.806  64.201  45.016  1.00 99.47      A    C  
ANISOU 2505  CA  GLU A 332    11303  15429  11059   1830    280   1065  A    C  
ATOM   2506  C   GLU A 332     143.298  65.155  46.135  1.00103.87      A    C  
ANISOU 2506  C   GLU A 332    11818  16231  11415   1940    190   1043  A    C  
ATOM   2507  O   GLU A 332     142.189  64.974  46.622  1.00113.71      A    O  
ANISOU 2507  O   GLU A 332    13165  17341  12697   2003    320   1188  A    O  
ATOM   2508  CB  GLU A 332     144.474  62.920  45.591  1.00107.87      A    C  
ANISOU 2508  CB  GLU A 332    12359  16568  12059   2159    458   1310  A    C  
ATOM   2509  CG  GLU A 332     145.992  62.972  45.850  1.00116.69      A    C  
ANISOU 2509  CG  GLU A 332    13308  18051  12975   2322    324   1240  A    C  
ATOM   2510  CD  GLU A 332     146.867  62.621  44.629  1.00120.83      A    C  
ANISOU 2510  CD  GLU A 332    13810  18439  13658   2125    291   1117  A    C  
ATOM   2511  OE1 GLU A 332     147.203  61.428  44.454  1.00127.41      A    O  
ANISOU 2511  OE1 GLU A 332    14687  19142  14580   2255    471   1293  A    O  
ATOM   2512  OE2 GLU A 332     147.250  63.533  43.847  1.00112.97      A    O1-
ANISOU 2512  OE2 GLU A 332    12755  17461  12705   1849    108    850  A    O1-
ATOM   2513  N   PRO A 333     144.081  66.180  46.527  1.00100.65      A    N  
ANISOU 2513  N   PRO A 333    11254  16175  10813   1946    -17    838  A    N  
ATOM   2514  CA  PRO A 333     143.528  67.241  47.374  1.00100.12      A    C  
ANISOU 2514  CA  PRO A 333    11140  16304  10595   1968   -114    748  A    C  
ATOM   2515  C   PRO A 333     142.575  68.165  46.626  1.00100.16      A    C  
ANISOU 2515  C   PRO A 333    11228  16048  10777   1638   -167    599  A    C  
ATOM   2516  O   PRO A 333     141.608  68.646  47.200  1.00101.13      A    O  
ANISOU 2516  O   PRO A 333    11397  16162  10864   1652   -155    630  A    O  
ATOM   2517  CB  PRO A 333     144.759  68.050  47.795  1.00101.74      A    C  
ANISOU 2517  CB  PRO A 333    11123  16943  10591   2016   -304    499  A    C  
ATOM   2518  CG  PRO A 333     145.926  67.192  47.485  1.00105.40      A    C  
ANISOU 2518  CG  PRO A 333    11520  17490  11038   2127   -284    539  A    C  
ATOM   2519  CD  PRO A 333     145.518  66.376  46.304  1.00105.42      A    C  
ANISOU 2519  CD  PRO A 333    11697  17032  11325   1947   -152    662  A    C  
ATOM   2520  N   LEU A 334     142.868  68.436  45.360  1.00103.27      A    N  
ANISOU 2520  N   LEU A 334    11640  16248  11347   1363   -221    446  A    N  
ATOM   2521  CA  LEU A 334     142.028  69.320  44.550  1.00103.54      A    C  
ANISOU 2521  CA  LEU A 334    11750  16055  11536   1082   -260    322  A    C  
ATOM   2522  C   LEU A 334     140.656  68.739  44.388  1.00 98.37      A    C  
ANISOU 2522  C   LEU A 334    11245  15118  11012   1063   -126    492  A    C  
ATOM   2523  O   LEU A 334     139.669  69.419  44.593  1.00100.39      A    O  
ANISOU 2523  O   LEU A 334    11544  15316  11280    995   -139    467  A    O  
ATOM   2524  CB  LEU A 334     142.616  69.538  43.154  1.00106.19      A    C  
ANISOU 2524  CB  LEU A 334    12090  16234  12024    842   -304    175  A    C  
ATOM   2525  CG  LEU A 334     143.387  70.841  42.947  1.00114.85      A    C  
ANISOU 2525  CG  LEU A 334    13074  17470  13091    693   -424    -91  A    C  
ATOM   2526  CD1 LEU A 334     142.405  71.998  42.861  1.00108.62      A    C  
ANISOU 2526  CD1 LEU A 334    12338  16579  12352    545   -445   -173  A    C  
ATOM   2527  CD2 LEU A 334     144.437  71.082  44.039  1.00124.86      A    C  
ANISOU 2527  CD2 LEU A 334    14155  19129  14154    861   -502   -206  A    C  
ATOM   2528  N   GLN A 335     140.587  67.476  44.009  1.00 95.60      A    N  
ANISOU 2528  N   GLN A 335    10961  14584  10778   1113     21    644  A    N  
ATOM   2529  CA  GLN A 335     139.309  66.890  43.708  1.00 94.68      A    C  
ANISOU 2529  CA  GLN A 335    10960  14181  10829   1052    172    745  A    C  
ATOM   2530  C   GLN A 335     138.473  66.615  44.930  1.00 97.44      A    C  
ANISOU 2530  C   GLN A 335    11356  14553  11111   1255    301    921  A    C  
ATOM   2531  O   GLN A 335     137.313  66.234  44.806  1.00 98.07      A    O  
ANISOU 2531  O   GLN A 335    11521  14403  11338   1198    442    980  A    O  
ATOM   2532  CB  GLN A 335     139.484  65.638  42.881  1.00 98.54      A    C  
ANISOU 2532  CB  GLN A 335    11490  14455  11493   1015    318    808  A    C  
ATOM   2533  CG  GLN A 335     139.646  65.980  41.414  1.00105.29      A    C  
ANISOU 2533  CG  GLN A 335    12341  15197  12468    751    220    627  A    C  
ATOM   2534  CD  GLN A 335     139.662  64.750  40.539  1.00113.12      A    C  
ANISOU 2534  CD  GLN A 335    13361  15976  13642    689    369    653  A    C  
ATOM   2535  NE2 GLN A 335     139.040  64.869  39.372  1.00113.98      A    N  
ANISOU 2535  NE2 GLN A 335    13489  15937  13880    477    352    523  A    N  
ATOM   2536  OE1 GLN A 335     140.234  63.701  40.899  1.00109.01      A    O  
ANISOU 2536  OE1 GLN A 335    12836  15437  13142    843    507    783  A    O  
ATOM   2537  N   CYS A 336     139.026  66.837  46.116  1.00100.00      A    N  
ANISOU 2537  N   CYS A 336    11612  15174  11209   1497    260    988  A    N  
ATOM   2538  CA  CYS A 336     138.204  66.764  47.318  1.00 97.81      A    C  
ANISOU 2538  CA  CYS A 336    11378  14951  10834   1704    371   1153  A    C  
ATOM   2539  C   CYS A 336     137.525  68.077  47.624  1.00 92.90      A    C  
ANISOU 2539  C   CYS A 336    10739  14417  10141   1590    229   1010  A    C  
ATOM   2540  O   CYS A 336     136.375  68.092  48.012  1.00102.43      A    O  
ANISOU 2540  O   CYS A 336    12024  15495  11398   1599    329   1092  A    O  
ATOM   2541  CB  CYS A 336     138.990  66.246  48.506  1.00101.93      A    C  
ANISOU 2541  CB  CYS A 336    11839  15768  11120   2075    430   1332  A    C  
ATOM   2542  SG  CYS A 336     138.927  64.434  48.476  1.00117.33      A    S  
ANISOU 2542  SG  CYS A 336    13901  17448  13231   2272    773   1637  A    S  
ATOM   2543  N   HIS A 337     138.221  69.185  47.437  1.00 89.55      A    N  
ANISOU 2543  N   HIS A 337    10208  14195   9622   1472     19    787  A    N  
ATOM   2544  CA  HIS A 337     137.600  70.502  47.579  1.00 84.61      A    C  
ANISOU 2544  CA  HIS A 337     9566  13611   8969   1329    -97    626  A    C  
ATOM   2545  C   HIS A 337     136.497  70.696  46.575  1.00 81.87      A    C  
ANISOU 2545  C   HIS A 337     9327  12934   8843   1085    -63    592  A    C  
ATOM   2546  O   HIS A 337     135.396  71.057  46.935  1.00 81.71      A    O  
ANISOU 2546  O   HIS A 337     9361  12839   8844   1066    -27    620  A    O  
ATOM   2547  CB  HIS A 337     138.627  71.587  47.360  1.00 85.13      A    C  
ANISOU 2547  CB  HIS A 337     9496  13890   8958   1211   -274    367  A    C  
ATOM   2548  CG  HIS A 337     139.453  71.848  48.554  1.00 88.00      A    C  
ANISOU 2548  CG  HIS A 337     9705  14669   9062   1430   -348    310  A    C  
ATOM   2549  CD2 HIS A 337     139.649  71.113  49.666  1.00 91.02      A    C  
ANISOU 2549  CD2 HIS A 337    10052  15288   9243   1758   -287    489  A    C  
ATOM   2550  ND1 HIS A 337     140.163  73.013  48.723  1.00 94.16      A    N  
ANISOU 2550  ND1 HIS A 337    10328  15692   9754   1336   -486     25  A    N  
ATOM   2551  CE1 HIS A 337     140.771  72.980  49.890  1.00 99.46      A    C  
ANISOU 2551  CE1 HIS A 337    10852  16771  10167   1587   -533      0  A    C  
ATOM   2552  NE2 HIS A 337     140.475  71.837  50.481  1.00 98.68      A    N  
ANISOU 2552  NE2 HIS A 337    10829  16686   9977   1865   -418    300  A    N  
ATOM   2553  N   LEU A 338     136.803  70.462  45.307  1.00 81.41      A    N  
ANISOU 2553  N   LEU A 338     9289  12704   8936    911    -75    524  A    N  
ATOM   2554  CA  LEU A 338     135.847  70.701  44.246  1.00 79.91      A    C  
ANISOU 2554  CA  LEU A 338     9172  12266   8922    698    -64    466  A    C  
ATOM   2555  C   LEU A 338     134.609  69.823  44.405  1.00 81.22      A    C  
ANISOU 2555  C   LEU A 338     9420  12233   9203    737    106    601  A    C  
ATOM   2556  O   LEU A 338     133.517  70.195  43.977  1.00 79.47      A    O  
ANISOU 2556  O   LEU A 338     9239  11878   9076    610    113    550  A    O  
ATOM   2557  CB  LEU A 338     136.496  70.450  42.891  1.00 78.19      A    C  
ANISOU 2557  CB  LEU A 338     8950  11944   8815    551    -93    383  A    C  
ATOM   2558  CG  LEU A 338     137.738  71.274  42.565  1.00 80.89      A    C  
ANISOU 2558  CG  LEU A 338     9212  12431   9090    485   -222    232  A    C  
ATOM   2559  CD1 LEU A 338     138.259  70.902  41.185  1.00 85.10      A    C  
ANISOU 2559  CD1 LEU A 338     9760  12832   9739    353   -221    183  A    C  
ATOM   2560  CD2 LEU A 338     137.461  72.758  42.600  1.00 81.80      A    C  
ANISOU 2560  CD2 LEU A 338     9309  12592   9178    377   -306     93  A    C  
ATOM   2561  N   LYS A 339     134.776  68.658  45.024  1.00 84.27      A    N  
ANISOU 2561  N   LYS A 339     9826  12601   9591    918    265    771  A    N  
ATOM   2562  CA  LYS A 339     133.698  67.691  45.107  1.00 86.34      A    C  
ANISOU 2562  CA  LYS A 339    10162  12630  10012    940    487    884  A    C  
ATOM   2563  C   LYS A 339     132.638  68.192  46.076  1.00 88.11      A    C  
ANISOU 2563  C   LYS A 339    10422  12871  10182   1010    528    939  A    C  
ATOM   2564  O   LYS A 339     131.513  67.707  46.065  1.00 96.14      A    O  
ANISOU 2564  O   LYS A 339    11491  13684  11354    971    697    975  A    O  
ATOM   2565  CB  LYS A 339     134.242  66.336  45.540  1.00 92.72      A    C  
ANISOU 2565  CB  LYS A 339    10990  13388  10849   1138    693   1069  A    C  
ATOM   2566  CG  LYS A 339     133.283  65.184  45.338  1.00102.97      A    C  
ANISOU 2566  CG  LYS A 339    12352  14381  12390   1111    979   1141  A    C  
ATOM   2567  CD  LYS A 339     134.017  63.835  45.252  1.00118.64      A    C  
ANISOU 2567  CD  LYS A 339    14348  16258  14469   1231   1186   1271  A    C  
ATOM   2568  CE  LYS A 339     135.065  63.615  46.350  1.00123.01      A    C  
ANISOU 2568  CE  LYS A 339    14894  17041  14803   1555   1205   1482  A    C  
ATOM   2569  NZ  LYS A 339     134.513  63.809  47.727  1.00130.25      A    N1+
ANISOU 2569  NZ  LYS A 339    15853  18060  15576   1797   1302   1662  A    N1+
ATOM   2570  N   SER A 340     132.987  69.183  46.896  1.00 84.53      A    N  
ANISOU 2570  N   SER A 340     9928  12668   9522   1100    383    919  A    N  
ATOM   2571  CA  SER A 340     132.084  69.692  47.910  1.00 83.78      A    C  
ANISOU 2571  CA  SER A 340     9860  12624   9348   1187    416    974  A    C  
ATOM   2572  C   SER A 340     131.613  71.112  47.609  1.00 80.22      A    C  
ANISOU 2572  C   SER A 340     9383  12216   8877   1003    237    789  A    C  
ATOM   2573  O   SER A 340     131.028  71.766  48.456  1.00 87.46      A    O  
ANISOU 2573  O   SER A 340    10305  13223   9702   1062    222    798  A    O  
ATOM   2574  CB  SER A 340     132.772  69.650  49.281  1.00 90.61      A    C  
ANISOU 2574  CB  SER A 340    10684  13780   9965   1484    424   1106  A    C  
ATOM   2575  OG  SER A 340     133.727  70.697  49.408  1.00 96.19      A    O  
ANISOU 2575  OG  SER A 340    11277  14778  10490   1463    197    937  A    O  
ATOM   2576  N   ILE A 341     131.855  71.616  46.419  1.00 78.23      A    N  
ANISOU 2576  N   ILE A 341     9110  11902   8709    796    119    632  A    N  
ATOM   2577  CA  ILE A 341     131.267  72.898  46.057  1.00 79.96      A    C  
ANISOU 2577  CA  ILE A 341     9326  12112   8940    641      3    490  A    C  
ATOM   2578  C   ILE A 341     129.990  72.649  45.268  1.00 78.54      A    C  
ANISOU 2578  C   ILE A 341     9199  11707   8935    513     77    477  A    C  
ATOM   2579  O   ILE A 341     129.827  71.583  44.719  1.00 81.33      A    O  
ANISOU 2579  O   ILE A 341     9567  11919   9412    493    186    514  A    O  
ATOM   2580  CB  ILE A 341     132.233  73.762  45.242  1.00 83.45      A    C  
ANISOU 2580  CB  ILE A 341     9715  12624   9365    513   -140    333  A    C  
ATOM   2581  CG1 ILE A 341     132.277  73.287  43.803  1.00 89.17      A    C  
ANISOU 2581  CG1 ILE A 341    10463  13183  10233    380   -128    302  A    C  
ATOM   2582  CG2 ILE A 341     133.633  73.763  45.858  1.00 83.95      A    C  
ANISOU 2582  CG2 ILE A 341     9693  12921   9283    623   -198    305  A    C  
ATOM   2583  CD1 ILE A 341     132.738  74.375  42.856  1.00 98.79      A    C  
ANISOU 2583  CD1 ILE A 341    11664  14404  11465    240   -230    163  A    C  
ATOM   2584  N   ALA A 342     129.070  73.606  45.228  1.00 79.13      A    N  
ANISOU 2584  N   ALA A 342     9285  11758   9020    433     29    409  A    N  
ATOM   2585  CA  ALA A 342     127.765  73.391  44.557  1.00 79.00      A    C  
ANISOU 2585  CA  ALA A 342     9291  11575   9148    334     94    376  A    C  
ATOM   2586  C   ALA A 342     127.870  73.926  43.148  1.00 73.42      A    C  
ANISOU 2586  C   ALA A 342     8564  10848   8484    196     -8    257  A    C  
ATOM   2587  O   ALA A 342     128.947  74.275  42.720  1.00 74.32      A    O  
ANISOU 2587  O   ALA A 342     8662  11028   8546    175    -91    223  A    O  
ATOM   2588  CB  ALA A 342     126.614  74.078  45.319  1.00 82.05      A    C  
ANISOU 2588  CB  ALA A 342     9699  11959   9516    350    111    382  A    C  
ATOM   2589  N   ASP A 343     126.758  74.019  42.432  1.00 70.16      A    N  
ANISOU 2589  N   ASP A 343     8142  10362   8154    118      5    192  A    N  
ATOM   2590  CA  ASP A 343     126.801  74.484  41.052  1.00 66.25      A    C  
ANISOU 2590  CA  ASP A 343     7622   9880   7669     34    -78    101  A    C  
ATOM   2591  C   ASP A 343     126.793  75.995  40.991  1.00 65.83      A    C  
ANISOU 2591  C   ASP A 343     7591   9881   7539     24   -168     81  A    C  
ATOM   2592  O   ASP A 343     125.755  76.595  40.731  1.00 65.76      A    O  
ANISOU 2592  O   ASP A 343     7579   9865   7540     11   -177     51  A    O  
ATOM   2593  CB  ASP A 343     125.604  73.924  40.299  1.00 66.91      A    C  
ANISOU 2593  CB  ASP A 343     7657   9916   7847    -19    -25     20  A    C  
ATOM   2594  CG  ASP A 343     125.849  73.801  38.825  1.00 65.62      A    C  
ANISOU 2594  CG  ASP A 343     7446   9800   7684    -68    -79    -65  A    C  
ATOM   2595  OD1 ASP A 343     126.640  74.625  38.321  1.00 64.34      A    O  
ANISOU 2595  OD1 ASP A 343     7314   9689   7442    -60   -165    -44  A    O  
ATOM   2596  OD2 ASP A 343     125.231  72.888  38.197  1.00 64.42      A    O1-
ANISOU 2596  OD2 ASP A 343     7220   9636   7618   -114    -17   -166  A    O1-
ATOM   2597  N   ILE A 344     127.951  76.620  41.213  1.00 66.47      A    N  
ANISOU 2597  N   ILE A 344     7683  10015   7557     31   -215     83  A    N  
ATOM   2598  CA  ILE A 344     127.991  78.079  41.306  1.00 70.43      A    C  
ANISOU 2598  CA  ILE A 344     8200  10538   8021     11   -250     44  A    C  
ATOM   2599  C   ILE A 344     127.821  78.784  39.964  1.00 72.11      A    C  
ANISOU 2599  C   ILE A 344     8430  10711   8255    -22   -258     23  A    C  
ATOM   2600  O   ILE A 344     127.457  79.964  39.936  1.00 73.55      A    O  
ANISOU 2600  O   ILE A 344     8637  10872   8434    -22   -243     13  A    O  
ATOM   2601  CB  ILE A 344     129.248  78.598  42.016  1.00 73.38      A    C  
ANISOU 2601  CB  ILE A 344     8551  10990   8339     13   -272     -1  A    C  
ATOM   2602  CG1 ILE A 344     130.458  78.542  41.110  1.00 82.05      A    C  
ANISOU 2602  CG1 ILE A 344     9636  12083   9454    -31   -283    -37  A    C  
ATOM   2603  CG2 ILE A 344     129.519  77.774  43.258  1.00 74.45      A    C  
ANISOU 2603  CG2 ILE A 344     8660  11217   8410     98   -265     45  A    C  
ATOM   2604  CD1 ILE A 344     131.678  79.223  41.700  1.00 88.38      A    C  
ANISOU 2604  CD1 ILE A 344    10385  12972  10220    -52   -292   -137  A    C  
ATOM   2605  N   GLU A 345     128.073  78.066  38.866  1.00 71.22      A    N  
ANISOU 2605  N   GLU A 345     8304  10594   8159    -31   -263     24  A    N  
ATOM   2606  CA  GLU A 345     127.850  78.595  37.532  1.00 67.20      A    C  
ANISOU 2606  CA  GLU A 345     7806  10087   7638    -15   -263     25  A    C  
ATOM   2607  C   GLU A 345     126.373  78.822  37.319  1.00 66.24      A    C  
ANISOU 2607  C   GLU A 345     7667   9996   7505     25   -266     23  A    C  
ATOM   2608  O   GLU A 345     125.997  79.864  36.747  1.00 70.05      A    O  
ANISOU 2608  O   GLU A 345     8175  10485   7954     78   -250     53  A    O  
ATOM   2609  CB  GLU A 345     128.346  77.643  36.473  1.00 69.65      A    C  
ANISOU 2609  CB  GLU A 345     8087  10426   7950    -23   -275     10  A    C  
ATOM   2610  CG  GLU A 345     128.177  78.181  35.061  1.00 74.51      A    C  
ANISOU 2610  CG  GLU A 345     8710  11086   8513     33   -270     27  A    C  
ATOM   2611  CD  GLU A 345     128.606  77.202  33.979  1.00 76.51      A    C  
ANISOU 2611  CD  GLU A 345     8919  11399   8750     31   -286     -6  A    C  
ATOM   2612  OE1 GLU A 345     128.023  76.103  33.842  1.00 73.20      A    O  
ANISOU 2612  OE1 GLU A 345     8424  11033   8352      8   -302    -79  A    O  
ATOM   2613  OE2 GLU A 345     129.545  77.561  33.251  1.00 82.69      A    O1-
ANISOU 2613  OE2 GLU A 345     9740  12169   9511     46   -262     28  A    O1-
ATOM   2614  N   ARG A 346     125.545  77.859  37.758  1.00 63.24      A    N  
ANISOU 2614  N   ARG A 346     7238   9627   7161     11   -263    -14  A    N  
ATOM   2615  CA  ARG A 346     124.075  78.000  37.672  1.00 64.34      A    C  
ANISOU 2615  CA  ARG A 346     7335   9808   7303     37   -260    -51  A    C  
ATOM   2616  C   ARG A 346     123.515  78.979  38.661  1.00 65.87      A    C  
ANISOU 2616  C   ARG A 346     7570   9962   7492     53   -248    -15  A    C  
ATOM   2617  O   ARG A 346     122.550  79.686  38.348  1.00 70.45      A    O  
ANISOU 2617  O   ARG A 346     8138  10580   8047     99   -253    -19  A    O  
ATOM   2618  CB  ARG A 346     123.345  76.700  37.896  1.00 62.77      A    C  
ANISOU 2618  CB  ARG A 346     7061   9604   7183     -4   -217   -130  A    C  
ATOM   2619  CG  ARG A 346     123.460  75.790  36.720  1.00 65.69      A    C  
ANISOU 2619  CG  ARG A 346     7351  10046   7562    -24   -222   -222  A    C  
ATOM   2620  CD  ARG A 346     122.696  74.513  36.918  1.00 66.70      A    C  
ANISOU 2620  CD  ARG A 346     7386  10147   7807    -87   -135   -342  A    C  
ATOM   2621  NE  ARG A 346     122.904  73.612  35.786  1.00 67.05      A    N  
ANISOU 2621  NE  ARG A 346     7335  10270   7870   -122   -130   -465  A    N  
ATOM   2622  CZ  ARG A 346     122.244  72.473  35.641  1.00 68.98      A    C  
ANISOU 2622  CZ  ARG A 346     7464  10509   8235   -195    -33   -631  A    C  
ATOM   2623  NH1 ARG A 346     121.358  72.102  36.587  1.00 73.69      A    N1+
ANISOU 2623  NH1 ARG A 346     8043  11000   8956   -235     83   -669  A    N1+
ATOM   2624  NH2 ARG A 346     122.467  71.709  34.576  1.00 64.87      A    N  
ANISOU 2624  NH2 ARG A 346     6839  10082   7725   -232    -30   -770  A    N  
ATOM   2625  N   ILE A 347     124.114  79.029  39.851  1.00 63.14      A    N  
ANISOU 2625  N   ILE A 347     7265   9566   7158     30   -232     17  A    N  
ATOM   2626  CA  ILE A 347     123.633  79.948  40.867  1.00 60.12      A    C  
ANISOU 2626  CA  ILE A 347     6914   9164   6764     41   -218     32  A    C  
ATOM   2627  C   ILE A 347     123.890  81.380  40.411  1.00 60.75      A    C  
ANISOU 2627  C   ILE A 347     7030   9228   6822     54   -212     41  A    C  
ATOM   2628  O   ILE A 347     123.066  82.271  40.618  1.00 59.64      A    O  
ANISOU 2628  O   ILE A 347     6904   9071   6682     79   -191     48  A    O  
ATOM   2629  CB  ILE A 347     124.300  79.700  42.211  1.00 58.41      A    C  
ANISOU 2629  CB  ILE A 347     6710   8954   6528     41   -205     50  A    C  
ATOM   2630  CG1 ILE A 347     123.884  78.335  42.740  1.00 56.74      A    C  
ANISOU 2630  CG1 ILE A 347     6480   8723   6353     61   -155     77  A    C  
ATOM   2631  CG2 ILE A 347     123.907  80.798  43.192  1.00 59.11      A    C  
ANISOU 2631  CG2 ILE A 347     6818   9053   6589     50   -197     39  A    C  
ATOM   2632  CD1 ILE A 347     124.821  77.802  43.789  1.00 56.37      A    C  
ANISOU 2632  CD1 ILE A 347     6443   8715   6259    110   -134    129  A    C  
ATOM   2633  N   ALA A 348     125.032  81.601  39.767  1.00 61.73      A    N  
ANISOU 2633  N   ALA A 348     7173   9339   6942     40   -205     44  A    N  
ATOM   2634  CA  ALA A 348     125.302  82.916  39.214  1.00 62.00      A    C  
ANISOU 2634  CA  ALA A 348     7250   9319   6987     58   -141     61  A    C  
ATOM   2635  C   ALA A 348     124.249  83.225  38.153  1.00 60.94      A    C  
ANISOU 2635  C   ALA A 348     7120   9213   6823    153   -129    118  A    C  
ATOM   2636  O   ALA A 348     123.885  84.403  37.982  1.00 63.71      A    O  
ANISOU 2636  O   ALA A 348     7511   9512   7183    206    -53    162  A    O  
ATOM   2637  CB  ALA A 348     126.718  83.027  38.654  1.00 61.01      A    C  
ANISOU 2637  CB  ALA A 348     7140   9159   6881     25   -105     47  A    C  
ATOM   2638  N   ALA A 349     123.766  82.192  37.458  1.00 57.22      A    N  
ANISOU 2638  N   ALA A 349     6594   8834   6312    184   -190    108  A    N  
ATOM   2639  CA  ALA A 349     122.796  82.395  36.401  1.00 57.60      A    C  
ANISOU 2639  CA  ALA A 349     6608   8983   6295    298   -196    134  A    C  
ATOM   2640  C   ALA A 349     121.472  82.800  36.980  1.00 58.61      A    C  
ANISOU 2640  C   ALA A 349     6710   9131   6424    326   -199    119  A    C  
ATOM   2641  O   ALA A 349     120.877  83.799  36.543  1.00 61.89      A    O  
ANISOU 2641  O   ALA A 349     7145   9569   6800    435   -157    182  A    O  
ATOM   2642  CB  ALA A 349     122.643  81.157  35.558  1.00 57.20      A    C  
ANISOU 2642  CB  ALA A 349     6468   9060   6203    305   -258     69  A    C  
ATOM   2643  N   ARG A 350     121.024  82.061  37.989  1.00 58.74      A    N  
ANISOU 2643  N   ARG A 350     6691   9132   6494    242   -227     51  A    N  
ATOM   2644  CA  ARG A 350     119.755  82.365  38.656  1.00 59.36      A    C  
ANISOU 2644  CA  ARG A 350     6744   9218   6590    255   -221     26  A    C  
ATOM   2645  C   ARG A 350     119.789  83.732  39.317  1.00 58.33      A    C  
ANISOU 2645  C   ARG A 350     6692   8995   6472    268   -168     86  A    C  
ATOM   2646  O   ARG A 350     118.804  84.446  39.319  1.00 62.59      A    O  
ANISOU 2646  O   ARG A 350     7226   9554   7002    331   -148    103  A    O  
ATOM   2647  CB  ARG A 350     119.410  81.306  39.690  1.00 62.09      A    C  
ANISOU 2647  CB  ARG A 350     7056   9529   7004    168   -217    -39  A    C  
ATOM   2648  CG  ARG A 350     118.962  79.979  39.093  1.00 66.89      A    C  
ANISOU 2648  CG  ARG A 350     7560  10210   7643    142   -224   -142  A    C  
ATOM   2649  CD  ARG A 350     118.238  79.090  40.114  1.00 70.49      A    C  
ANISOU 2649  CD  ARG A 350     7983  10598   8200     76   -156   -202  A    C  
ATOM   2650  NE  ARG A 350     119.160  78.402  41.006  1.00 72.38      A    N  
ANISOU 2650  NE  ARG A 350     8285  10734   8482     34   -107   -144  A    N  
ATOM   2651  CZ  ARG A 350     119.784  77.275  40.695  1.00 80.16      A    C  
ANISOU 2651  CZ  ARG A 350     9243  11699   9512     -1    -75   -169  A    C  
ATOM   2652  NH1 ARG A 350     119.583  76.715  39.516  1.00 89.06      A    N1+
ANISOU 2652  NH1 ARG A 350    10279  12906  10654    -19    -91   -277  A    N1+
ATOM   2653  NH2 ARG A 350     120.617  76.702  41.551  1.00 82.57      A    N  
ANISOU 2653  NH2 ARG A 350     9606  11926   9838     -2    -22    -92  A    N  
ATOM   2654  N   ILE A 351     120.920  84.128  39.863  1.00 56.29      A    N  
ANISOU 2654  N   ILE A 351     6494   8648   6243    209   -135    100  A    N  
ATOM   2655  CA  ILE A 351     121.039  85.476  40.354  1.00 56.90      A    C  
ANISOU 2655  CA  ILE A 351     6626   8638   6353    207    -56    117  A    C  
ATOM   2656  C   ILE A 351     120.806  86.498  39.231  1.00 57.34      A    C  
ANISOU 2656  C   ILE A 351     6719   8669   6398    321     28    203  A    C  
ATOM   2657  O   ILE A 351     120.081  87.474  39.421  1.00 57.86      A    O  
ANISOU 2657  O   ILE A 351     6807   8691   6483    372     96    234  A    O  
ATOM   2658  CB  ILE A 351     122.398  85.668  41.031  1.00 57.73      A    C  
ANISOU 2658  CB  ILE A 351     6752   8690   6493    116    -28     65  A    C  
ATOM   2659  CG1 ILE A 351     122.351  85.018  42.400  1.00 57.75      A    C  
ANISOU 2659  CG1 ILE A 351     6722   8741   6477     62    -84     10  A    C  
ATOM   2660  CG2 ILE A 351     122.752  87.142  41.180  1.00 59.20      A    C  
ANISOU 2660  CG2 ILE A 351     6978   8770   6743     99     99     45  A    C  
ATOM   2661  CD1 ILE A 351     123.725  84.926  43.021  1.00 59.24      A    C  
ANISOU 2661  CD1 ILE A 351     6893   8957   6657      1    -86    -56  A    C  
ATOM   2662  N   ALA A 352     121.408  86.258  38.072  1.00 58.15      A    N  
ANISOU 2662  N   ALA A 352     6829   8801   6463    378     38    252  A    N  
ATOM   2663  CA  ALA A 352     121.375  87.199  36.960  1.00 60.84      A    C  
ANISOU 2663  CA  ALA A 352     7219   9118   6777    525    152    368  A    C  
ATOM   2664  C   ALA A 352     119.992  87.426  36.403  1.00 62.80      A    C  
ANISOU 2664  C   ALA A 352     7427   9495   6938    686    133    427  A    C  
ATOM   2665  O   ALA A 352     119.667  88.582  36.012  1.00 63.57      A    O  
ANISOU 2665  O   ALA A 352     7580   9537   7035    820    266    540  A    O  
ATOM   2666  CB  ALA A 352     122.269  86.725  35.837  1.00 62.31      A    C  
ANISOU 2666  CB  ALA A 352     7413   9344   6917    568    157    411  A    C  
ATOM   2667  N   VAL A 353     119.202  86.343  36.346  1.00 61.67      A    N  
ANISOU 2667  N   VAL A 353     7181   9518   6731    681     -7    344  A    N  
ATOM   2668  CA  VAL A 353     117.806  86.424  35.859  1.00 64.19      A    C  
ANISOU 2668  CA  VAL A 353     7416  10012   6959    826    -46    346  A    C  
ATOM   2669  C   VAL A 353     116.726  86.661  36.947  1.00 65.98      A    C  
ANISOU 2669  C   VAL A 353     7616  10209   7243    771    -62    285  A    C  
ATOM   2670  O   VAL A 353     115.514  86.503  36.714  1.00 61.75      A    O  
ANISOU 2670  O   VAL A 353     6981   9831   6648    853   -112    236  A    O  
ATOM   2671  CB  VAL A 353     117.440  85.185  35.072  1.00 63.18      A    C  
ANISOU 2671  CB  VAL A 353     7154  10111   6740    853   -163    241  A    C  
ATOM   2672  CG1 VAL A 353     118.272  85.115  33.819  1.00 64.68      A    C  
ANISOU 2672  CG1 VAL A 353     7360  10379   6835    964   -144    319  A    C  
ATOM   2673  CG2 VAL A 353     117.663  83.965  35.924  1.00 62.77      A    C  
ANISOU 2673  CG2 VAL A 353     7062  10002   6784    649   -228    102  A    C  
ATOM   2674  N   GLY A 354     117.187  87.073  38.123  1.00 70.44      A    N  
ANISOU 2674  N   GLY A 354     8259  10588   7915    638    -13    276  A    N  
ATOM   2675  CA  GLY A 354     116.296  87.402  39.227  1.00 78.65      A    C  
ANISOU 2675  CA  GLY A 354     9291  11582   9008    587     -9    231  A    C  
ATOM   2676  C   GLY A 354     115.444  86.236  39.681  1.00 77.98      A    C  
ANISOU 2676  C   GLY A 354     9107  11592   8928    519   -102    114  A    C  
ATOM   2677  O   GLY A 354     114.225  86.341  39.842  1.00 80.25      A    O  
ANISOU 2677  O   GLY A 354     9334  11947   9211    560   -113     74  A    O  
ATOM   2678  N   ASN A 355     116.107  85.123  39.901  1.00 76.40      A    N  
ANISOU 2678  N   ASN A 355     8891  11382   8753    417   -143     57  A    N  
ATOM   2679  CA  ASN A 355     115.427  83.875  40.088  1.00 77.66      A    C  
ANISOU 2679  CA  ASN A 355     8954  11609   8943    358   -182    -57  A    C  
ATOM   2680  C   ASN A 355     116.029  83.109  41.226  1.00 72.73      A    C  
ANISOU 2680  C   ASN A 355     8371  10873   8389    239   -160    -71  A    C  
ATOM   2681  O   ASN A 355     115.750  81.937  41.381  1.00 67.27      A    O  
ANISOU 2681  O   ASN A 355     7619  10190   7749    185   -148   -148  A    O  
ATOM   2682  CB  ASN A 355     115.605  83.065  38.815  1.00 85.66      A    C  
ANISOU 2682  CB  ASN A 355     9880  12764   9901    397   -231   -112  A    C  
ATOM   2683  CG  ASN A 355     114.524  82.062  38.626  1.00 97.08      A    C  
ANISOU 2683  CG  ASN A 355    11177  14330  11378    369   -247   -278  A    C  
ATOM   2684  ND2 ASN A 355     114.886  80.788  38.690  1.00103.12      A    N  
ANISOU 2684  ND2 ASN A 355    11898  15068  12214    267   -231   -369  A    N  
ATOM   2685  OD1 ASN A 355     113.364  82.425  38.419  1.00112.10      A    O  
ANISOU 2685  OD1 ASN A 355    12993  16347  13250    439   -259   -338  A    O  
ATOM   2686  N   ALA A 356     116.901  83.765  41.986  1.00 74.07      A    N  
ANISOU 2686  N   ALA A 356     8633  10950   8559    211   -138     -6  A    N  
ATOM   2687  CA  ALA A 356     117.667  83.093  43.036  1.00 76.38      A    C  
ANISOU 2687  CA  ALA A 356     8959  11189   8872    143   -125     -3  A    C  
ATOM   2688  C   ALA A 356     116.891  83.159  44.314  1.00 76.20      A    C  
ANISOU 2688  C   ALA A 356     8945  11132   8874    131    -83    -10  A    C  
ATOM   2689  O   ALA A 356     116.238  84.158  44.617  1.00 70.83      A    O  
ANISOU 2689  O   ALA A 356     8279  10440   8192    149    -68     -8  A    O  
ATOM   2690  CB  ALA A 356     119.048  83.720  43.246  1.00 78.31      A    C  
ANISOU 2690  CB  ALA A 356     9261  11405   9087    124   -126     26  A    C  
ATOM   2691  N   ARG A 357     116.994  82.073  45.063  1.00 77.11      A    N  
ANISOU 2691  N   ARG A 357     9057  11225   9013    111    -43     -5  A    N  
ATOM   2692  CA  ARG A 357     116.265  81.920  46.283  1.00 79.54      A    C  
ANISOU 2692  CA  ARG A 357     9379  11498   9342    120     26      9  A    C  
ATOM   2693  C   ARG A 357     117.259  81.837  47.445  1.00 78.09      A    C  
ANISOU 2693  C   ARG A 357     9245  11340   9085    151     40     71  A    C  
ATOM   2694  O   ARG A 357     118.431  81.526  47.242  1.00 79.58      A    O  
ANISOU 2694  O   ARG A 357     9439  11563   9233    155      6     88  A    O  
ATOM   2695  CB  ARG A 357     115.379  80.674  46.156  1.00 86.66      A    C  
ANISOU 2695  CB  ARG A 357    10226  12353  10345     99    112    -35  A    C  
ATOM   2696  CG  ARG A 357     114.530  80.686  44.900  1.00 96.50      A    C  
ANISOU 2696  CG  ARG A 357    11379  13649  11636     77     77   -142  A    C  
ATOM   2697  CD  ARG A 357     113.232  79.917  45.049  1.00110.38      A    C  
ANISOU 2697  CD  ARG A 357    13054  15371  13512     40    181   -247  A    C  
ATOM   2698  NE  ARG A 357     113.504  78.498  45.220  1.00122.54      A    N  
ANISOU 2698  NE  ARG A 357    14578  16827  15154     -1    303   -267  A    N  
ATOM   2699  CZ  ARG A 357     113.109  77.775  46.268  1.00130.79      A    C  
ANISOU 2699  CZ  ARG A 357    15652  17746  16296     -6    473   -236  A    C  
ATOM   2700  NH1 ARG A 357     112.404  78.333  47.247  1.00118.02      A    N1+
ANISOU 2700  NH1 ARG A 357    14077  16091  14672     24    520   -191  A    N1+
ATOM   2701  NH2 ARG A 357     113.415  76.479  46.330  1.00139.07      A    N  
ANISOU 2701  NH2 ARG A 357    16690  18695  17452    -29    619   -241  A    N  
ATOM   2702  N   PRO A 358     116.795  82.109  48.672  1.00 75.91      A    N  
ANISOU 2702  N   PRO A 358     8992  11070   8777    187     90     97  A    N  
ATOM   2703  CA  PRO A 358     117.674  82.167  49.828  1.00 74.25      A    C  
ANISOU 2703  CA  PRO A 358     8806  10953   8452    251     93    139  A    C  
ATOM   2704  C   PRO A 358     118.749  81.103  49.931  1.00 70.83      A    C  
ANISOU 2704  C   PRO A 358     8374  10563   7975    306    107    201  A    C  
ATOM   2705  O   PRO A 358     119.880  81.457  50.151  1.00 71.94      A    O  
ANISOU 2705  O   PRO A 358     8498  10817   8019    326     42    179  A    O  
ATOM   2706  CB  PRO A 358     116.706  82.035  50.989  1.00 79.27      A    C  
ANISOU 2706  CB  PRO A 358     9463  11574   9079    310    188    186  A    C  
ATOM   2707  CG  PRO A 358     115.467  82.736  50.509  1.00 77.38      A    C  
ANISOU 2707  CG  PRO A 358     9212  11257   8931    243    185    123  A    C  
ATOM   2708  CD  PRO A 358     115.400  82.440  49.032  1.00 78.70      A    C  
ANISOU 2708  CD  PRO A 358     9343  11376   9184    182    143     77  A    C  
ATOM   2709  N   ARG A 359     118.443  79.825  49.774  1.00 70.54      A    N  
ANISOU 2709  N   ARG A 359     8344  10438   8018    328    205    263  A    N  
ATOM   2710  CA  ARG A 359     119.496  78.803  49.991  1.00 72.78      A    C  
ANISOU 2710  CA  ARG A 359     8636  10758   8257    407    243    345  A    C  
ATOM   2711  C   ARG A 359     120.547  78.723  48.918  1.00 70.26      A    C  
ANISOU 2711  C   ARG A 359     8291  10463   7942    348    148    297  A    C  
ATOM   2712  O   ARG A 359     121.596  78.138  49.153  1.00 70.54      A    O  
ANISOU 2712  O   ARG A 359     8324  10564   7911    416    150    351  A    O  
ATOM   2713  CB  ARG A 359     118.911  77.421  50.177  1.00 76.30      A    C  
ANISOU 2713  CB  ARG A 359     9105  11067   8817    452    429    428  A    C  
ATOM   2714  CG  ARG A 359     117.945  77.420  51.321  1.00 80.87      A    C  
ANISOU 2714  CG  ARG A 359     9721  11610   9393    529    561    498  A    C  
ATOM   2715  CD  ARG A 359     117.753  76.049  51.893  1.00 83.94      A    C  
ANISOU 2715  CD  ARG A 359    10151  11879   9861    635    800    632  A    C  
ATOM   2716  NE  ARG A 359     117.159  76.182  53.205  1.00 86.76      A    N  
ANISOU 2716  NE  ARG A 359    10558  12254  10151    765    922    740  A    N  
ATOM   2717  CZ  ARG A 359     116.599  75.179  53.847  1.00 95.49      A    C  
ANISOU 2717  CZ  ARG A 359    11716  13212  11353    865   1189    866  A    C  
ATOM   2718  NH1 ARG A 359     116.553  73.984  53.267  1.00108.19      A    N1+
ANISOU 2718  NH1 ARG A 359    13321  14633  13151    825   1365    873  A    N1+
ATOM   2719  NH2 ARG A 359     116.086  75.360  55.055  1.00 99.03      A    N  
ANISOU 2719  NH2 ARG A 359    12218  13690  11718   1004   1304    981  A    N  
ATOM   2720  N   ASP A 360     120.267  79.276  47.744  1.00 68.00      A    N  
ANISOU 2720  N   ASP A 360     7982  10131   7722    242     73    206  A    N  
ATOM   2721  CA  ASP A 360     121.282  79.400  46.702  1.00 68.85      A    C  
ANISOU 2721  CA  ASP A 360     8072  10266   7822    193    -13    164  A    C  
ATOM   2722  C   ASP A 360     122.452  80.259  47.194  1.00 65.59      A    C  
ANISOU 2722  C   ASP A 360     7654   9970   7298    210    -83    137  A    C  
ATOM   2723  O   ASP A 360     123.598  79.929  46.974  1.00 62.61      A    O  
ANISOU 2723  O   ASP A 360     7259   9646   6885    217   -115    133  A    O  
ATOM   2724  CB  ASP A 360     120.682  80.052  45.441  1.00 72.41      A    C  
ANISOU 2724  CB  ASP A 360     8503  10677   8330    122    -62     94  A    C  
ATOM   2725  CG  ASP A 360     119.750  79.129  44.691  1.00 72.74      A    C  
ANISOU 2725  CG  ASP A 360     8504  10663   8471     95    -13     59  A    C  
ATOM   2726  OD1 ASP A 360     120.054  77.913  44.637  1.00 74.29      A    O  
ANISOU 2726  OD1 ASP A 360     8686  10822   8717     94     50     72  A    O  
ATOM   2727  OD2 ASP A 360     118.736  79.626  44.154  1.00 71.73      A    O1-
ANISOU 2727  OD2 ASP A 360     8343  10539   8370     78    -28      4  A    O1-
ATOM   2728  N   LEU A 361     122.152  81.368  47.859  1.00 64.25      A    N  
ANISOU 2728  N   LEU A 361     7481   9845   7083    207    -98     90  A    N  
ATOM   2729  CA  LEU A 361     123.194  82.239  48.388  1.00 63.70      A    C  
ANISOU 2729  CA  LEU A 361     7374   9902   6926    200   -143      6  A    C  
ATOM   2730  C   LEU A 361     123.988  81.554  49.494  1.00 64.77      A    C  
ANISOU 2730  C   LEU A 361     7474  10206   6928    315   -144     39  A    C  
ATOM   2731  O   LEU A 361     125.193  81.749  49.627  1.00 62.90      A    O  
ANISOU 2731  O   LEU A 361     7176  10103   6617    320   -192    -41  A    O  
ATOM   2732  CB  LEU A 361     122.581  83.515  48.920  1.00 63.37      A    C  
ANISOU 2732  CB  LEU A 361     7327   9869   6881    168   -132    -71  A    C  
ATOM   2733  CG  LEU A 361     121.704  84.270  47.944  1.00 62.63      A    C  
ANISOU 2733  CG  LEU A 361     7270   9627   6900    101   -112    -79  A    C  
ATOM   2734  CD1 LEU A 361     121.289  85.602  48.536  1.00 65.06      A    C  
ANISOU 2734  CD1 LEU A 361     7567   9937   7211     70    -80   -161  A    C  
ATOM   2735  CD2 LEU A 361     122.495  84.490  46.678  1.00 63.96      A    C  
ANISOU 2735  CD2 LEU A 361     7439   9738   7123     48   -123   -102  A    C  
ATOM   2736  N   ALA A 362     123.308  80.745  50.290  1.00 66.58      A    N  
ANISOU 2736  N   ALA A 362     7734  10437   7123    423    -74    157  A    N  
ATOM   2737  CA  ALA A 362     123.997  79.923  51.267  1.00 70.52      A    C  
ANISOU 2737  CA  ALA A 362     8213  11096   7485    586    -44    244  A    C  
ATOM   2738  C   ALA A 362     125.016  79.012  50.613  1.00 69.58      A    C  
ANISOU 2738  C   ALA A 362     8083  10973   7380    602    -55    281  A    C  
ATOM   2739  O   ALA A 362     126.145  78.982  51.056  1.00 68.49      A    O  
ANISOU 2739  O   ALA A 362     7881  11030   7111    682   -105    251  A    O  
ATOM   2740  CB  ALA A 362     123.011  79.096  52.052  1.00 74.54      A    C  
ANISOU 2740  CB  ALA A 362     8782  11543   7997    709     91    400  A    C  
ATOM   2741  N   SER A 363     124.611  78.286  49.566  1.00 70.93      A    N  
ANISOU 2741  N   SER A 363     8298  10944   7705    527     -8    327  A    N  
ATOM   2742  CA  SER A 363     125.518  77.378  48.835  1.00 73.08      A    C  
ANISOU 2742  CA  SER A 363     8561  11190   8013    526     -8    355  A    C  
ATOM   2743  C   SER A 363     126.638  78.107  48.159  1.00 72.45      A    C  
ANISOU 2743  C   SER A 363     8431  11188   7907    438   -127    229  A    C  
ATOM   2744  O   SER A 363     127.772  77.617  48.154  1.00 76.89      A    O  
ANISOU 2744  O   SER A 363     8956  11846   8412    489   -150    235  A    O  
ATOM   2745  CB  SER A 363     124.802  76.572  47.775  1.00 73.38      A    C  
ANISOU 2745  CB  SER A 363     8632  11020   8225    440     62    376  A    C  
ATOM   2746  OG  SER A 363     123.536  76.219  48.270  1.00 84.61      A    O  
ANISOU 2746  OG  SER A 363    10090  12341   9717    467    183    432  A    O  
ATOM   2747  N   LEU A 364     126.321  79.270  47.587  1.00 71.03      A    N  
ANISOU 2747  N   LEU A 364     8249  10957   7779    314   -179    119  A    N  
ATOM   2748  CA  LEU A 364     127.317  80.077  46.873  1.00 68.47      A    C  
ANISOU 2748  CA  LEU A 364     7887  10660   7467    220   -241     -3  A    C  
ATOM   2749  C   LEU A 364     128.351  80.615  47.845  1.00 71.42      A    C  
ANISOU 2749  C   LEU A 364     8172  11248   7715    261   -281   -113  A    C  
ATOM   2750  O   LEU A 364     129.566  80.614  47.590  1.00 67.88      A    O  
ANISOU 2750  O   LEU A 364     7662  10884   7243    240   -315   -196  A    O  
ATOM   2751  CB  LEU A 364     126.650  81.227  46.182  1.00 65.08      A    C  
ANISOU 2751  CB  LEU A 364     7486  10115   7125    117   -236    -66  A    C  
ATOM   2752  CG  LEU A 364     127.603  82.231  45.607  1.00 66.54      A    C  
ANISOU 2752  CG  LEU A 364     7640  10297   7344     29   -239   -190  A    C  
ATOM   2753  CD1 LEU A 364     128.435  81.583  44.520  1.00 70.47      A    C  
ANISOU 2753  CD1 LEU A 364     8145  10749   7882      3   -252   -167  A    C  
ATOM   2754  CD2 LEU A 364     126.808  83.381  45.027  1.00 69.03      A    C  
ANISOU 2754  CD2 LEU A 364     7999  10483   7746    -31   -190   -211  A    C  
ATOM   2755  N   ARG A 365     127.846  81.041  48.993  1.00 75.59      A    N  
ANISOU 2755  N   ARG A 365     8678  11888   8154    327   -273   -129  A    N  
ATOM   2756  CA  ARG A 365     128.693  81.565  50.044  1.00 74.34      A    C  
ANISOU 2756  CA  ARG A 365     8403  11996   7845    384   -315   -267  A    C  
ATOM   2757  C   ARG A 365     129.670  80.509  50.466  1.00 72.18      A    C  
ANISOU 2757  C   ARG A 365     8076  11906   7440    533   -339   -204  A    C  
ATOM   2758  O   ARG A 365     130.859  80.760  50.513  1.00 72.74      A    O  
ANISOU 2758  O   ARG A 365     8038  12152   7449    522   -391   -352  A    O  
ATOM   2759  CB  ARG A 365     127.839  82.005  51.224  1.00 73.79      A    C  
ANISOU 2759  CB  ARG A 365     8325  12029   7680    461   -296   -264  A    C  
ATOM   2760  CG  ARG A 365     128.648  82.366  52.443  1.00 77.41      A    C  
ANISOU 2760  CG  ARG A 365     8641  12834   7934    565   -343   -407  A    C  
ATOM   2761  CD  ARG A 365     127.786  82.442  53.680  1.00 77.51      A    C  
ANISOU 2761  CD  ARG A 365     8659  12976   7814    701   -317   -343  A    C  
ATOM   2762  NE  ARG A 365     127.146  81.169  53.937  1.00 77.10      A    N  
ANISOU 2762  NE  ARG A 365     8714  12844   7733    867   -244    -69  A    N  
ATOM   2763  CZ  ARG A 365     125.966  81.041  54.531  1.00 78.74      A    C  
ANISOU 2763  CZ  ARG A 365     9001  12978   7937    939   -166     59  A    C  
ATOM   2764  NH1 ARG A 365     125.300  82.121  54.930  1.00 78.43      A    N1+
ANISOU 2764  NH1 ARG A 365     8945  12953   7902    863   -177    -57  A    N1+
ATOM   2765  NH2 ARG A 365     125.438  79.831  54.707  1.00 80.84      A    N  
ANISOU 2765  NH2 ARG A 365     9363  13135   8216   1078    -54    298  A    N  
ATOM   2766  N   ASP A 366     129.157  79.322  50.747  1.00 71.48      A    N  
ANISOU 2766  N   ASP A 366     8062  11769   7326    674   -278     12  A    N  
ATOM   2767  CA  ASP A 366     129.960  78.272  51.316  1.00 75.05      A    C  
ANISOU 2767  CA  ASP A 366     8476  12398   7640    869   -264    119  A    C  
ATOM   2768  C   ASP A 366     130.914  77.685  50.313  1.00 74.23      A    C  
ANISOU 2768  C   ASP A 366     8364  12226   7612    809   -287    111  A    C  
ATOM   2769  O   ASP A 366     132.006  77.266  50.685  1.00 83.10      A    O  
ANISOU 2769  O   ASP A 366     9402  13564   8608    931   -319     99  A    O  
ATOM   2770  CB  ASP A 366     129.083  77.165  51.881  1.00 77.85      A    C  
ANISOU 2770  CB  ASP A 366     8929  12663   7984   1039   -130    367  A    C  
ATOM   2771  CG  ASP A 366     128.089  77.684  52.895  1.00 80.05      A    C  
ANISOU 2771  CG  ASP A 366     9226  13000   8186   1109    -92    393  A    C  
ATOM   2772  OD1 ASP A 366     128.384  78.732  53.504  1.00 82.52      A    O  
ANISOU 2772  OD1 ASP A 366     9443  13538   8372   1103   -183    227  A    O  
ATOM   2773  OD2 ASP A 366     127.009  77.071  53.055  1.00 80.70      A    O1-
ANISOU 2773  OD2 ASP A 366     9410  12899   8352   1157     40    555  A    O1-
ATOM   2774  N   SER A 367     130.536  77.624  49.052  1.00 66.73      A    N  
ANISOU 2774  N   SER A 367     7490  11008   6856    643   -270    115  A    N  
ATOM   2775  CA  SER A 367     131.466  77.072  48.102  1.00 64.36      A    C  
ANISOU 2775  CA  SER A 367     7178  10655   6619    590   -289    104  A    C  
ATOM   2776  C   SER A 367     132.527  78.093  47.711  1.00 64.88      A    C  
ANISOU 2776  C   SER A 367     7151  10819   6680    469   -372   -112  A    C  
ATOM   2777  O   SER A 367     133.653  77.714  47.411  1.00 69.72      A    O  
ANISOU 2777  O   SER A 367     7706  11512   7272    480   -400   -154  A    O  
ATOM   2778  CB  SER A 367     130.755  76.501  46.882  1.00 61.64      A    C  
ANISOU 2778  CB  SER A 367     6930  10032   6455    483   -236    179  A    C  
ATOM   2779  OG  SER A 367     129.611  77.218  46.590  1.00 60.17      A    O  
ANISOU 2779  OG  SER A 367     6792   9719   6350    386   -227    151  A    O  
ATOM   2780  N   LEU A 368     132.199  79.381  47.703  1.00 64.06      A    N  
ANISOU 2780  N   LEU A 368     7029  10694   6614    352   -385   -256  A    N  
ATOM   2781  CA  LEU A 368     133.215  80.407  47.396  1.00 62.71      A    C  
ANISOU 2781  CA  LEU A 368     6761  10591   6474    227   -409   -488  A    C  
ATOM   2782  C   LEU A 368     134.289  80.461  48.454  1.00 63.99      A    C  
ANISOU 2782  C   LEU A 368     6757  11090   6464    324   -463   -637  A    C  
ATOM   2783  O   LEU A 368     135.420  80.824  48.160  1.00 63.38      A    O  
ANISOU 2783  O   LEU A 368     6575  11099   6408    246   -477   -824  A    O  
ATOM   2784  CB  LEU A 368     132.596  81.784  47.300  1.00 61.75      A    C  
ANISOU 2784  CB  LEU A 368     6650  10367   6442     97   -366   -610  A    C  
ATOM   2785  CG  LEU A 368     131.927  82.076  45.985  1.00 60.55      A    C  
ANISOU 2785  CG  LEU A 368     6622   9923   6460    -12   -310   -531  A    C  
ATOM   2786  CD1 LEU A 368     131.348  83.466  46.073  1.00 63.46      A    C  
ANISOU 2786  CD1 LEU A 368     6996  10211   6904   -101   -245   -638  A    C  
ATOM   2787  CD2 LEU A 368     132.903  82.032  44.851  1.00 60.25      A    C  
ANISOU 2787  CD2 LEU A 368     6583   9794   6513    -95   -286   -575  A    C  
ATOM   2788  N   PHE A 369     133.898  80.152  49.689  1.00 65.86      A    N  
ANISOU 2788  N   PHE A 369     6962  11534   6527    502   -483   -567  A    N  
ATOM   2789  CA  PHE A 369     134.834  79.982  50.794  1.00 70.31      A    C  
ANISOU 2789  CA  PHE A 369     7357  12492   6863    671   -543   -668  A    C  
ATOM   2790  C   PHE A 369     135.684  78.711  50.569  1.00 74.71      A    C  
ANISOU 2790  C   PHE A 369     7909  13116   7361    809   -555   -531  A    C  
ATOM   2791  O   PHE A 369     136.899  78.697  50.818  1.00 77.51      A    O  
ANISOU 2791  O   PHE A 369     8104  13740   7605    862   -613   -686  A    O  
ATOM   2792  CB  PHE A 369     134.105  79.889  52.165  1.00 69.29      A    C  
ANISOU 2792  CB  PHE A 369     7215  12575   6536    877   -541   -576  A    C  
ATOM   2793  CG  PHE A 369     133.804  81.214  52.799  1.00 67.76      A    C  
ANISOU 2793  CG  PHE A 369     6926  12510   6310    790   -558   -813  A    C  
ATOM   2794  CD1 PHE A 369     134.760  82.194  52.869  1.00 68.25      A    C  
ANISOU 2794  CD1 PHE A 369     6801  12764   6367    665   -596  -1157  A    C  
ATOM   2795  CD2 PHE A 369     132.559  81.461  53.353  1.00 67.59      A    C  
ANISOU 2795  CD2 PHE A 369     6991  12414   6273    827   -518   -708  A    C  
ATOM   2796  CE1 PHE A 369     134.471  83.410  53.455  1.00 69.91      A    C  
ANISOU 2796  CE1 PHE A 369     6912  13077   6569    571   -584  -1400  A    C  
ATOM   2797  CE2 PHE A 369     132.256  82.669  53.952  1.00 67.46      A    C  
ANISOU 2797  CE2 PHE A 369     6887  12511   6233    747   -524   -927  A    C  
ATOM   2798  CZ  PHE A 369     133.212  83.648  53.994  1.00 69.49      A    C  
ANISOU 2798  CZ  PHE A 369     6956  12949   6494    614   -554  -1277  A    C  
ATOM   2799  N   GLU A 370     135.045  77.641  50.107  1.00 75.99      A    N  
ANISOU 2799  N   GLU A 370     8230  13038   7606    863   -488   -261  A    N  
ATOM   2800  CA  GLU A 370     135.747  76.404  49.855  1.00 78.10      A    C  
ANISOU 2800  CA  GLU A 370     8506  13319   7848    988   -465   -116  A    C  
ATOM   2801  C   GLU A 370     136.649  76.571  48.645  1.00 78.63      A    C  
ANISOU 2801  C   GLU A 370     8546  13271   8056    798   -501   -254  A    C  
ATOM   2802  O   GLU A 370     137.691  75.945  48.574  1.00 92.00      A    O  
ANISOU 2802  O   GLU A 370    10169  15095   9691    879   -522   -256  A    O  
ATOM   2803  CB  GLU A 370     134.764  75.253  49.661  1.00 80.43      A    C  
ANISOU 2803  CB  GLU A 370     8967  13358   8235   1066   -344    169  A    C  
ATOM   2804  CG  GLU A 370     135.415  73.903  49.424  1.00 85.77      A    C  
ANISOU 2804  CG  GLU A 370     9663  14012   8913   1199   -278    333  A    C  
ATOM   2805  CD  GLU A 370     136.190  73.359  50.622  1.00 94.13      A    C  
ANISOU 2805  CD  GLU A 370    10622  15422   9718   1510   -272    420  A    C  
ATOM   2806  OE1 GLU A 370     136.814  74.148  51.381  1.00 98.91      A    O  
ANISOU 2806  OE1 GLU A 370    11074  16378  10129   1578   -383    245  A    O  
ATOM   2807  OE2 GLU A 370     136.185  72.116  50.797  1.00102.57      A    O1-
ANISOU 2807  OE2 GLU A 370    11760  16428  10784   1699   -139    660  A    O1-
ATOM   2808  N   LEU A 371     136.298  77.436  47.713  1.00 75.53      A    N  
ANISOU 2808  N   LEU A 371     8206  12652   7839    567   -495   -363  A    N  
ATOM   2809  CA  LEU A 371     137.218  77.725  46.644  1.00 78.58      A    C  
ANISOU 2809  CA  LEU A 371     8562  12951   8345    406   -505   -501  A    C  
ATOM   2810  C   LEU A 371     138.414  78.560  47.118  1.00 82.88      A    C  
ANISOU 2810  C   LEU A 371     8912  13764   8814    369   -552   -790  A    C  
ATOM   2811  O   LEU A 371     139.531  78.418  46.587  1.00 87.95      A    O  
ANISOU 2811  O   LEU A 371     9480  14443   9491    317   -562   -897  A    O  
ATOM   2812  CB  LEU A 371     136.502  78.430  45.504  1.00 82.74      A    C  
ANISOU 2812  CB  LEU A 371     9202  13170   9063    211   -456   -510  A    C  
ATOM   2813  CG  LEU A 371     135.684  77.544  44.554  1.00 83.87      A    C  
ANISOU 2813  CG  LEU A 371     9494  13061   9313    201   -416   -302  A    C  
ATOM   2814  CD1 LEU A 371     135.259  78.386  43.354  1.00 87.47      A    C  
ANISOU 2814  CD1 LEU A 371    10022  13294   9916     38   -377   -345  A    C  
ATOM   2815  CD2 LEU A 371     136.444  76.332  44.076  1.00 79.75      A    C  
ANISOU 2815  CD2 LEU A 371     8972  12531   8796    253   -414   -218  A    C  
ATOM   2816  N   ALA A 372     138.200  79.426  48.106  1.00 83.29      A    N  
ANISOU 2816  N   ALA A 372     8865  14012   8768    388   -572   -944  A    N  
ATOM   2817  CA  ALA A 372     139.283  80.271  48.612  1.00 86.48      A    C  
ANISOU 2817  CA  ALA A 372     9047  14701   9109    335   -603  -1283  A    C  
ATOM   2818  C   ALA A 372     140.365  79.463  49.317  1.00 89.84      A    C  
ANISOU 2818  C   ALA A 372     9309  15505   9318    540   -684  -1317  A    C  
ATOM   2819  O   ALA A 372     141.501  79.922  49.440  1.00 98.42      A    O  
ANISOU 2819  O   ALA A 372    10194  16824  10377    484   -712  -1613  A    O  
ATOM   2820  CB  ALA A 372     138.752  81.351  49.536  1.00 87.00      A    C  
ANISOU 2820  CB  ALA A 372     9027  14911   9114    311   -599  -1462  A    C  
ATOM   2821  N   GLN A 373     140.023  78.260  49.753  1.00 88.73      A    N  
ANISOU 2821  N   GLN A 373     9249  15425   9039    781   -700  -1021  A    N  
ATOM   2822  CA  GLN A 373     140.989  77.386  50.389  1.00 94.94      A    C  
ANISOU 2822  CA  GLN A 373     9903  16560   9610   1027   -756   -989  A    C  
ATOM   2823  C   GLN A 373     141.880  76.593  49.418  1.00101.10      A    C  
ANISOU 2823  C   GLN A 373    10706  17214  10492    989   -746   -934  A    C  
ATOM   2824  O   GLN A 373     142.756  75.835  49.828  1.00102.57      A    O  
ANISOU 2824  O   GLN A 373    10783  17672  10515   1192   -784   -901  A    O  
ATOM   2825  CB  GLN A 373     140.258  76.431  51.305  1.00 96.09      A    C  
ANISOU 2825  CB  GLN A 373    10136  16802   9572   1331   -727   -670  A    C  
ATOM   2826  CG  GLN A 373     139.722  77.099  52.557  1.00 98.25      A    C  
ANISOU 2826  CG  GLN A 373    10321  17359   9649   1454   -756   -748  A    C  
ATOM   2827  CD  GLN A 373     138.727  76.209  53.244  1.00102.82      A    C  
ANISOU 2827  CD  GLN A 373    11051  17893  10123   1711   -672   -387  A    C  
ATOM   2828  NE2 GLN A 373     137.605  76.788  53.686  1.00106.04      A    N  
ANISOU 2828  NE2 GLN A 373    11532  18217  10541   1675   -641   -362  A    N  
ATOM   2829  OE1 GLN A 373     138.940  74.999  53.341  1.00104.51      A    O  
ANISOU 2829  OE1 GLN A 373    11325  18113  10269   1935   -607   -125  A    O  
ATOM   2830  N   ILE A 374     141.687  76.781  48.128  1.00106.41      A    N  
ANISOU 2830  N   ILE A 374    11511  17498  11419    746   -692   -924  A    N  
ATOM   2831  CA  ILE A 374     142.520  76.091  47.174  1.00110.57      A    C  
ANISOU 2831  CA  ILE A 374    12059  17907  12046    698   -680   -889  A    C  
ATOM   2832  C   ILE A 374     143.773  76.901  46.908  1.00127.15      A    C  
ANISOU 2832  C   ILE A 374    13971  20153  14188    545   -706  -1237  A    C  
ATOM   2833  O   ILE A 374     144.690  76.408  46.266  1.00133.81      A    O  
ANISOU 2833  O   ILE A 374    14783  20973  15084    518   -705  -1260  A    O  
ATOM   2834  CB  ILE A 374     141.769  75.864  45.858  1.00109.70      A    C  
ANISOU 2834  CB  ILE A 374    12165  17348  12167    528   -605   -723  A    C  
ATOM   2835  CG1 ILE A 374     140.411  75.244  46.140  1.00105.22      A    C  
ANISOU 2835  CG1 ILE A 374    11755  16629  11591    635   -559   -451  A    C  
ATOM   2836  CG2 ILE A 374     142.562  74.959  44.924  1.00108.73      A    C  
ANISOU 2836  CG2 ILE A 374    12070  17115  12125    511   -588   -653  A    C  
ATOM   2837  CD1 ILE A 374     139.661  74.880  44.887  1.00105.28      A    C  
ANISOU 2837  CD1 ILE A 374    11939  16264  11799    496   -494   -313  A    C  
ATOM   2838  N   ASP A 375     143.826  78.146  47.392  1.00158.13      A    N  
ANISOU 2838  N   ASP A 375    17760  24214  18106    436   -710  -1527  A    N  
ATOM   2839  CA  ASP A 375     145.013  79.011  47.195  1.00170.31      A    C  
ANISOU 2839  CA  ASP A 375    19095  25888  19723    264   -693  -1918  A    C  
ATOM   2840  C   ASP A 375     146.324  78.281  47.565  1.00172.99      A    C  
ANISOU 2840  C   ASP A 375    19235  26592  19899    420   -775  -2020  A    C  
ATOM   2841  O   ASP A 375     147.339  78.455  46.884  1.00169.69      A    O  
ANISOU 2841  O   ASP A 375    18728  26138  19607    275   -739  -2219  A    O  
ATOM   2842  CB  ASP A 375     144.879  80.338  47.969  1.00162.62      A    C  
ANISOU 2842  CB  ASP A 375    17960  25094  18735    165   -674  -2249  A    C  
ATOM   2843  CG  ASP A 375     145.187  80.197  49.450  1.00151.38      A    C  
ANISOU 2843  CG  ASP A 375    16304  24216  16994    406   -793  -2379  A    C  
ATOM   2844  OD1 ASP A 375     144.561  79.356  50.143  1.00134.51      A    O  
ANISOU 2844  OD1 ASP A 375    14249  22206  14650    671   -858  -2082  A    O  
ATOM   2845  OD2 ASP A 375     146.069  80.940  49.916  1.00148.56      A    O1-
ANISOU 2845  OD2 ASP A 375    15672  24176  16597    334   -804  -2794  A    O1-
ATOM   2846  N   LEU A 376     146.297  77.484  48.641  1.00168.71      A    N  
ANISOU 2846  N   LEU A 376    18624  26402  19075    731   -866  -1875  A    N  
ATOM   2847  CA  LEU A 376     147.352  76.502  48.908  1.00156.05      A    C  
ANISOU 2847  CA  LEU A 376    16889  25104  17299    952   -931  -1841  A    C  
ATOM   2848  C   LEU A 376     147.050  75.350  47.957  1.00143.14      A    C  
ANISOU 2848  C   LEU A 376    15504  23085  15797    972   -871  -1468  A    C  
ATOM   2849  O   LEU A 376     147.203  75.515  46.749  1.00122.59      A    O  
ANISOU 2849  O   LEU A 376    13004  20137  13438    730   -811  -1499  A    O  
ATOM   2850  CB  LEU A 376     147.386  76.055  50.389  1.00159.83      A    C  
ANISOU 2850  CB  LEU A 376    17215  26100  17412   1325  -1019  -1781  A    C  
ATOM   2851  CG  LEU A 376     148.426  74.999  50.832  1.00158.18      A    C  
ANISOU 2851  CG  LEU A 376    16859  26273  16967   1637  -1080  -1704  A    C  
ATOM   2852  CD1 LEU A 376     149.832  75.389  50.384  1.00157.79      A    C  
ANISOU 2852  CD1 LEU A 376    16571  26401  16980   1480  -1123  -2092  A    C  
ATOM   2853  CD2 LEU A 376     148.372  74.792  52.345  1.00157.65      A    C  
ANISOU 2853  CD2 LEU A 376    16630  26757  16510   2028  -1152  -1662  A    C  
ATOM   2854  N   SER A 377     146.589  74.214  48.481  1.00149.94      A    N  
ANISOU 2854  N   SER A 377    16466  23995  16508   1257   -862  -1123  A    N  
ATOM   2855  CA  SER A 377     146.193  73.057  47.668  1.00158.34      A    C  
ANISOU 2855  CA  SER A 377    17757  24693  17710   1279   -776   -784  A    C  
ATOM   2856  C   SER A 377     147.179  72.712  46.531  1.00169.60      A    C  
ANISOU 2856  C   SER A 377    19175  25969  19296   1131   -764   -857  A    C  
ATOM   2857  O   SER A 377     147.637  71.565  46.426  1.00181.00      A    O  
ANISOU 2857  O   SER A 377    20641  27429  20701   1296   -735   -671  A    O  
ATOM   2858  CB  SER A 377     144.788  73.274  47.098  1.00151.06      A    C  
ANISOU 2858  CB  SER A 377    17068  23347  16977   1111   -701   -629  A    C  
ATOM   2859  OG  SER A 377     143.780  73.183  48.092  1.00132.97      A    O  
ANISOU 2859  OG  SER A 377    14834  21133  14555   1291   -679   -463  A    O  
ATOM   2860  N   ALA A 378     147.502  73.706  45.698  1.00158.99      A    N  
ANISOU 2860  N   ALA A 378    17800  24471  18135    831   -761  -1119  A    N  
ATOM   2861  CA  ALA A 378     148.433  73.533  44.589  1.00147.27      A    C  
ANISOU 2861  CA  ALA A 378    16309  22835  16809    673   -735  -1210  A    C  
ATOM   2862  C   ALA A 378     148.964  74.880  44.087  1.00134.81      A    C  
ANISOU 2862  C   ALA A 378    14626  21210  15385    392   -709  -1571  A    C  
ATOM   2863  O   ALA A 378     148.319  75.910  44.305  1.00123.77      A    O  
ANISOU 2863  O   ALA A 378    13238  19757  14031    277   -683  -1687  A    O  
ATOM   2864  CB  ALA A 378     147.716  72.796  43.469  1.00149.49      A    C  
ANISOU 2864  CB  ALA A 378    16841  22685  17271    592   -655   -934  A    C  
ATOM   2865  N   THR A 379     150.118  74.872  43.411  1.00122.74      A    N  
ANISOU 2865  N   THR A 379    13005  19678  13952    282   -686  -1744  A    N  
ATOM   2866  CA  THR A 379     150.568  76.066  42.675  1.00125.93      A    C  
ANISOU 2866  CA  THR A 379    13360  19914  14570     -8   -589  -2041  A    C  
ATOM   2867  C   THR A 379     150.933  75.673  41.240  1.00121.43      A    C  
ANISOU 2867  C   THR A 379    12934  19004  14198   -145   -503  -1938  A    C  
ATOM   2868  O   THR A 379     150.068  75.243  40.503  1.00129.96      A    O  
ANISOU 2868  O   THR A 379    14242  19783  15351   -158   -470  -1661  A    O  
ATOM   2869  CB  THR A 379     151.729  76.804  43.376  1.00126.36      A    C  
ANISOU 2869  CB  THR A 379    13094  20346  14568    -50   -609  -2481  A    C  
ATOM   2870  CG2 THR A 379     151.274  77.384  44.714  1.00124.43      A    C  
ANISOU 2870  CG2 THR A 379    12702  20438  14136     58   -681  -2622  A    C  
ATOM   2871  OG1 THR A 379     152.806  75.898  43.600  1.00125.54      A    O  
ANISOU 2871  OG1 THR A 379    12837  20532  14329    110   -691  -2510  A    O  
ATOM   2872  N   GLY A 380     152.187  75.815  40.835  1.00122.58      A    N  
ANISOU 2872  N   GLY A 380    12936  19211  14425   -247   -463  -2174  A    N  
ATOM   2873  CA  GLY A 380     152.618  75.289  39.548  1.00116.16      A    C  
ANISOU 2873  CA  GLY A 380    12249  18121  13764   -337   -391  -2060  A    C  
ATOM   2874  C   GLY A 380     153.426  76.260  38.708  1.00117.29      A    C  
ANISOU 2874  C   GLY A 380    12338  18093  14133   -586   -233  -2335  A    C  
ATOM   2875  O   GLY A 380     154.279  76.986  39.197  1.00114.29      A    O  
ANISOU 2875  O   GLY A 380    11726  17917  13782   -670   -196  -2696  A    O  
ATOM   2876  N   SER A 381     153.146  76.251  37.414  1.00125.12      A    N  
ANISOU 2876  N   SER A 381    13540  18709  15288   -694   -118  -2166  A    N  
ATOM   2877  CA  SER A 381     153.884  77.050  36.436  1.00113.22      A    C  
ANISOU 2877  CA  SER A 381    12031  16977  14010   -904     79  -2352  A    C  
ATOM   2878  C   SER A 381     153.194  76.981  35.048  1.00111.69      A    C  
ANISOU 2878  C   SER A 381    12112  16392  13931   -949    189  -2069  A    C  
ATOM   2879  O   SER A 381     153.725  76.356  34.112  1.00 97.89      A    O  
ANISOU 2879  O   SER A 381    10430  14528  12236   -963    223  -1979  A    O  
ATOM   2880  CB  SER A 381     155.277  76.497  36.323  1.00101.06      A    C  
ANISOU 2880  CB  SER A 381    10324  15594  12479   -912     63  -2521  A    C  
ATOM   2881  OG  SER A 381     155.179  75.154  35.870  1.00 91.15      A    O  
ANISOU 2881  OG  SER A 381     9192  14306  11135   -778    -38  -2224  A    O  
ATOM   2882  N   SER A 382     152.023  77.623  34.935  1.00104.43      A    N  
ANISOU 2882  N   SER A 382    11339  15303  13033   -958    241  -1938  A    N  
ATOM   2883  CA  SER A 382     151.300  77.659  33.698  1.00 99.70      A    C  
ANISOU 2883  CA  SER A 382    10973  14403  12505   -966    339  -1689  A    C  
ATOM   2884  C   SER A 382     150.161  78.677  33.730  1.00 94.30      A    C  
ANISOU 2884  C   SER A 382    10397  13570  11860   -982    426  -1623  A    C  
ATOM   2885  O   SER A 382     150.173  79.629  34.461  1.00 83.82      A    O  
ANISOU 2885  O   SER A 382     8972  12288  10584  -1051    491  -1824  A    O  
ATOM   2886  CB  SER A 382     150.761  76.243  33.426  1.00101.41      A    C  
ANISOU 2886  CB  SER A 382    11293  14654  12582   -827    176  -1411  A    C  
ATOM   2887  OG  SER A 382     150.133  76.149  32.156  1.00107.43      A    O  
ANISOU 2887  OG  SER A 382    12246  15186  13385   -822    251  -1200  A    O  
ATOM   2888  N   LEU A 383     149.211  78.470  32.835  1.00100.51      A    N  
ANISOU 2888  N   LEU A 383    11381  14181  12624   -918    441  -1352  A    N  
ATOM   2889  CA  LEU A 383     147.821  78.915  32.957  1.00 91.10      A    C  
ANISOU 2889  CA  LEU A 383    10303  12923  11385   -858    430  -1200  A    C  
ATOM   2890  C   LEU A 383     147.216  78.741  34.358  1.00 86.86      A    C  
ANISOU 2890  C   LEU A 383     9679  12599  10723   -797    262  -1237  A    C  
ATOM   2891  O   LEU A 383     146.385  79.528  34.751  1.00 86.62      A    O  
ANISOU 2891  O   LEU A 383     9682  12529  10701   -799    297  -1233  A    O  
ATOM   2892  CB  LEU A 383     146.991  78.079  31.958  1.00 89.18      A    C  
ANISOU 2892  CB  LEU A 383    10221  12604  11059   -755    369   -921  A    C  
ATOM   2893  CG  LEU A 383     145.499  77.851  32.198  1.00 82.98      A    C  
ANISOU 2893  CG  LEU A 383     9517  11845  10163   -656    261   -745  A    C  
ATOM   2894  CD1 LEU A 383     144.754  79.099  31.777  1.00 86.51      A    C  
ANISOU 2894  CD1 LEU A 383    10064  12133  10671   -655    413   -693  A    C  
ATOM   2895  CD2 LEU A 383     145.006  76.680  31.396  1.00 78.35      A    C  
ANISOU 2895  CD2 LEU A 383     9007  11267   9494   -575    173   -567  A    C  
ATOM   2896  N   LEU A 384     147.601  77.688  35.081  1.00 87.70      A    N  
ANISOU 2896  N   LEU A 384     9684  12926  10709   -723     95  -1248  A    N  
ATOM   2897  CA  LEU A 384     147.198  77.473  36.492  1.00 84.73      A    C  
ANISOU 2897  CA  LEU A 384     9210  12787  10194   -630    -44  -1281  A    C  
ATOM   2898  C   LEU A 384     147.359  78.710  37.376  1.00 84.58      A    C  
ANISOU 2898  C   LEU A 384     9061  12866  10209   -707     13  -1538  A    C  
ATOM   2899  O   LEU A 384     146.519  78.992  38.194  1.00 79.73      A    O  
ANISOU 2899  O   LEU A 384     8444  12332   9516   -654    -42  -1515  A    O  
ATOM   2900  CB  LEU A 384     148.049  76.374  37.136  1.00 85.16      A    C  
ANISOU 2900  CB  LEU A 384     9133  13091  10132   -530   -169  -1312  A    C  
ATOM   2901  CG  LEU A 384     147.717  74.929  36.809  1.00 83.18      A    C  
ANISOU 2901  CG  LEU A 384     8978  12815   9812   -410   -248  -1062  A    C  
ATOM   2902  CD1 LEU A 384     148.791  73.952  37.244  1.00 86.71      A    C  
ANISOU 2902  CD1 LEU A 384     9297  13469  10180   -315   -317  -1098  A    C  
ATOM   2903  CD2 LEU A 384     146.457  74.602  37.511  1.00 81.00      A    C  
ANISOU 2903  CD2 LEU A 384     8768  12569   9438   -297   -313   -895  A    C  
ATOM   2904  N   GLU A 385     148.457  79.437  37.222  1.00 89.39      A    N  
ANISOU 2904  N   GLU A 385     9546  13470  10946   -840    138  -1806  A    N  
ATOM   2905  CA  GLU A 385     148.716  80.552  38.111  1.00 93.97      A    C  
ANISOU 2905  CA  GLU A 385     9958  14172  11571   -931    206  -2114  A    C  
ATOM   2906  C   GLU A 385     147.715  81.682  37.914  1.00 95.68      A    C  
ANISOU 2906  C   GLU A 385    10295  14154  11901   -999    352  -2075  A    C  
ATOM   2907  O   GLU A 385     147.471  82.443  38.839  1.00102.70      A    O  
ANISOU 2907  O   GLU A 385    11077  15161  12783  -1034    365  -2261  A    O  
ATOM   2908  CB  GLU A 385     150.173  81.034  38.011  1.00 99.67      A    C  
ANISOU 2908  CB  GLU A 385    10487  14951  12430  -1077    332  -2465  A    C  
ATOM   2909  CG  GLU A 385     151.094  80.275  38.969  1.00105.57      A    C  
ANISOU 2909  CG  GLU A 385    10996  16111  13003   -984    152  -2640  A    C  
ATOM   2910  CD  GLU A 385     152.544  80.697  38.867  1.00113.98      A    C  
ANISOU 2910  CD  GLU A 385    11840  17265  14200  -1130    268  -3019  A    C  
ATOM   2911  OE1 GLU A 385     152.818  81.900  39.065  1.00126.07      A    O  
ANISOU 2911  OE1 GLU A 385    13246  18757  15896  -1301    446  -3345  A    O  
ATOM   2912  OE2 GLU A 385     153.415  79.834  38.607  1.00116.53      A    O1-
ANISOU 2912  OE2 GLU A 385    12103  17695  14477  -1081    197  -3011  A    O1-
ATOM   2913  N   THR A 386     147.124  81.796  36.727  1.00 99.99      A    N  
ANISOU 2913  N   THR A 386    11057  14394  12539  -1002    464  -1837  A    N  
ATOM   2914  CA  THR A 386     146.026  82.757  36.524  1.00 99.07      A    C  
ANISOU 2914  CA  THR A 386    11073  14073  12496  -1014    589  -1738  A    C  
ATOM   2915  C   THR A 386     144.755  82.210  37.138  1.00 94.35      A    C  
ANISOU 2915  C   THR A 386    10544  13587  11718   -877    394  -1532  A    C  
ATOM   2916  O   THR A 386     143.973  82.976  37.691  1.00101.77      A    O  
ANISOU 2916  O   THR A 386    11492  14510  12666   -885    427  -1560  A    O  
ATOM   2917  CB  THR A 386     145.785  83.133  35.042  1.00 98.62      A    C  
ANISOU 2917  CB  THR A 386    11214  13689  12569  -1018    791  -1540  A    C  
ATOM   2918  CG2 THR A 386     146.845  84.163  34.553  1.00100.82      A    C  
ANISOU 2918  CG2 THR A 386    11440  13774  13092  -1173   1096  -1766  A    C  
ATOM   2919  OG1 THR A 386     145.828  81.949  34.233  1.00 98.00      A    O  
ANISOU 2919  OG1 THR A 386    11223  13620  12391   -927    672  -1324  A    O  
ATOM   2920  N   LEU A 387     144.567  80.891  37.069  1.00 91.39      A    N  
ANISOU 2920  N   LEU A 387    10208  13316  11197   -760    213  -1344  A    N  
ATOM   2921  CA  LEU A 387     143.426  80.218  37.754  1.00 87.98      A    C  
ANISOU 2921  CA  LEU A 387     9824  12995  10609   -630     48  -1166  A    C  
ATOM   2922  C   LEU A 387     143.445  80.416  39.266  1.00 87.73      A    C  
ANISOU 2922  C   LEU A 387     9640  13220  10471   -594    -41  -1325  A    C  
ATOM   2923  O   LEU A 387     142.435  80.731  39.865  1.00 81.58      A    O  
ANISOU 2923  O   LEU A 387     8897  12458   9640   -551    -72  -1268  A    O  
ATOM   2924  CB  LEU A 387     143.403  78.708  37.481  1.00 81.91      A    C  
ANISOU 2924  CB  LEU A 387     9099  12283   9739   -524    -81   -977  A    C  
ATOM   2925  CG  LEU A 387     142.873  78.266  36.125  1.00 80.94      A    C  
ANISOU 2925  CG  LEU A 387     9132  11964   9658   -511    -45   -776  A    C  
ATOM   2926  CD1 LEU A 387     142.764  76.763  36.070  1.00 80.90      A    C  
ANISOU 2926  CD1 LEU A 387     9141  12027   9568   -421   -157   -636  A    C  
ATOM   2927  CD2 LEU A 387     141.521  78.874  35.870  1.00 80.79      A    C  
ANISOU 2927  CD2 LEU A 387     9225  11825   9643   -488     -8   -657  A    C  
ATOM   2928  N   LYS A 388     144.607  80.222  39.872  1.00 92.55      A    N  
ANISOU 2928  N   LYS A 388    10070  14057  11034   -599    -85  -1530  A    N  
ATOM   2929  CA  LYS A 388     144.749  80.337  41.310  1.00 97.42      A    C  
ANISOU 2929  CA  LYS A 388    10511  14996  11506   -528   -181  -1697  A    C  
ATOM   2930  C   LYS A 388     144.454  81.748  41.749  1.00 94.41      A    C  
ANISOU 2930  C   LYS A 388    10068  14590  11212   -646    -74  -1916  A    C  
ATOM   2931  O   LYS A 388     143.972  81.934  42.870  1.00 95.39      A    O  
ANISOU 2931  O   LYS A 388    10113  14922  11206   -572   -152  -1973  A    O  
ATOM   2932  CB  LYS A 388     146.183  79.974  41.747  1.00116.77      A    C  
ANISOU 2932  CB  LYS A 388    12746  17732  13890   -510   -235  -1923  A    C  
ATOM   2933  CG  LYS A 388     146.589  78.525  41.486  1.00129.58      A    C  
ANISOU 2933  CG  LYS A 388    14402  19416  15414   -371   -335  -1721  A    C  
ATOM   2934  CD  LYS A 388     145.642  77.543  42.183  1.00135.25      A    C  
ANISOU 2934  CD  LYS A 388    15203  20228  15955   -160   -449  -1442  A    C  
ATOM   2935  CE  LYS A 388     145.632  76.153  41.547  1.00132.36      A    C  
ANISOU 2935  CE  LYS A 388    14958  19753  15580    -64   -475  -1176  A    C  
ATOM   2936  NZ  LYS A 388     146.792  75.322  41.945  1.00128.81      A    N1+
ANISOU 2936  NZ  LYS A 388    14364  19557  15019     60   -536  -1223  A    N1+
ATOM   2937  N   ALA A 389     144.776  82.729  40.886  1.00 90.44      A    N  
ANISOU 2937  N   ALA A 389     9596  13832  10933   -821    128  -2042  A    N  
ATOM   2938  CA  ALA A 389     144.668  84.162  41.224  1.00 91.88      A    C  
ANISOU 2938  CA  ALA A 389     9705  13947  11258   -962    297  -2296  A    C  
ATOM   2939  C   ALA A 389     143.228  84.583  41.396  1.00 94.08      A    C  
ANISOU 2939  C   ALA A 389    10130  14097  11518   -914    301  -2108  A    C  
ATOM   2940  O   ALA A 389     142.917  85.575  42.060  1.00 94.21      A    O  
ANISOU 2940  O   ALA A 389    10071  14140  11584   -983    381  -2295  A    O  
ATOM   2941  CB  ALA A 389     145.331  85.028  40.167  1.00 90.99      A    C  
ANISOU 2941  CB  ALA A 389     9621  13536  11414  -1137    568  -2425  A    C  
ATOM   2942  N   VAL A 390     142.344  83.794  40.805  1.00 95.95      A    N  
ANISOU 2942  N   VAL A 390    10561  14208  11685   -798    215  -1760  A    N  
ATOM   2943  CA  VAL A 390     140.930  84.119  40.742  1.00 91.27      A    C  
ANISOU 2943  CA  VAL A 390    10120  13471  11087   -748    225  -1560  A    C  
ATOM   2944  C   VAL A 390     140.222  83.818  42.070  1.00 87.48      A    C  
ANISOU 2944  C   VAL A 390     9580  13234  10425   -643     65  -1548  A    C  
ATOM   2945  O   VAL A 390     139.342  84.557  42.484  1.00 98.39      A    O  
ANISOU 2945  O   VAL A 390    10992  14566  11825   -654    106  -1553  A    O  
ATOM   2946  CB  VAL A 390     140.264  83.374  39.544  1.00 84.78      A    C  
ANISOU 2946  CB  VAL A 390     9496  12457  10258   -668    202  -1237  A    C  
ATOM   2947  CG1 VAL A 390     138.812  83.771  39.384  1.00 82.94      A    C  
ANISOU 2947  CG1 VAL A 390     9399  12091  10024   -615    223  -1055  A    C  
ATOM   2948  CG2 VAL A 390     141.013  83.674  38.254  1.00 85.33      A    C  
ANISOU 2948  CG2 VAL A 390     9624  12315  10480   -744    369  -1238  A    C  
ATOM   2949  N   PHE A 391     140.605  82.749  42.747  1.00 82.99      A    N  
ANISOU 2949  N   PHE A 391     8928  12922   9681   -525    -99  -1522  A    N  
ATOM   2950  CA  PHE A 391     139.796  82.251  43.851  1.00 83.43      A    C  
ANISOU 2950  CA  PHE A 391     8976  13169   9554   -377   -229  -1414  A    C  
ATOM   2951  C   PHE A 391     139.816  83.149  45.077  1.00 87.14      A    C  
ANISOU 2951  C   PHE A 391     9287  13866   9958   -393   -230  -1665  A    C  
ATOM   2952  O   PHE A 391     138.778  83.339  45.730  1.00 88.61      A    O  
ANISOU 2952  O   PHE A 391     9518  14073  10074   -330   -258  -1582  A    O  
ATOM   2953  CB  PHE A 391     140.232  80.847  44.244  1.00 82.43      A    C  
ANISOU 2953  CB  PHE A 391     8812  13246   9260   -212   -360  -1289  A    C  
ATOM   2954  CG  PHE A 391     140.073  79.846  43.155  1.00 76.48      A    C  
ANISOU 2954  CG  PHE A 391     8207  12287   8563   -189   -361  -1049  A    C  
ATOM   2955  CD1 PHE A 391     138.827  79.544  42.653  1.00 74.45      A    C  
ANISOU 2955  CD1 PHE A 391     8115  11825   8345   -167   -348   -823  A    C  
ATOM   2956  CD2 PHE A 391     141.174  79.203  42.651  1.00 75.65      A    C  
ANISOU 2956  CD2 PHE A 391     8054  12217   8470   -192   -373  -1076  A    C  
ATOM   2957  CE1 PHE A 391     138.686  78.613  41.643  1.00 75.87      A    C  
ANISOU 2957  CE1 PHE A 391     8401  11851   8573   -154   -346   -649  A    C  
ATOM   2958  CE2 PHE A 391     141.048  78.267  41.661  1.00 74.83      A    C  
ANISOU 2958  CE2 PHE A 391     8073  11942   8417   -176   -369   -879  A    C  
ATOM   2959  CZ  PHE A 391     139.803  77.969  41.144  1.00 75.12      A    C  
ANISOU 2959  CZ  PHE A 391     8263  11786   8491   -160   -354   -675  A    C  
ATOM   2960  N   PRO A 392     140.996  83.688  45.413  1.00 86.71      A    N  
ANISOU 2960  N   PRO A 392     9027  13996   9922   -478   -194  -1995  A    N  
ATOM   2961  CA  PRO A 392     140.977  84.633  46.495  1.00 89.41      A    C  
ANISOU 2961  CA  PRO A 392     9197  14554  10217   -516   -177  -2279  A    C  
ATOM   2962  C   PRO A 392     140.319  85.965  46.117  1.00 95.52      A    C  
ANISOU 2962  C   PRO A 392    10044  15036  11211   -689     10  -2366  A    C  
ATOM   2963  O   PRO A 392     139.921  86.713  47.005  1.00 98.73      A    O  
ANISOU 2963  O   PRO A 392    10358  15571  11584   -710     27  -2537  A    O  
ATOM   2964  CB  PRO A 392     142.458  84.817  46.806  1.00 93.08      A    C  
ANISOU 2964  CB  PRO A 392     9400  15294  10669   -579   -170  -2647  A    C  
ATOM   2965  CG  PRO A 392     143.105  83.572  46.332  1.00 91.37      A    C  
ANISOU 2965  CG  PRO A 392     9219  15123  10373   -468   -268  -2467  A    C  
ATOM   2966  CD  PRO A 392     142.366  83.264  45.084  1.00 87.90      A    C  
ANISOU 2966  CD  PRO A 392     9054  14258  10083   -504   -203  -2135  A    C  
ATOM   2967  N   GLU A 393     140.220  86.264  44.817  1.00105.94      A    N  
ANISOU 2967  N   GLU A 393    11527  15979  12745   -793    160  -2245  A    N  
ATOM   2968  CA  GLU A 393     139.627  87.533  44.320  1.00113.44      A    C  
ANISOU 2968  CA  GLU A 393    12568  16615  13916   -926    382  -2282  A    C  
ATOM   2969  C   GLU A 393     138.162  87.649  44.728  1.00110.66      A    C  
ANISOU 2969  C   GLU A 393    12338  16215  13489   -835    326  -2078  A    C  
ATOM   2970  O   GLU A 393     137.599  88.735  44.819  1.00106.51      A    O  
ANISOU 2970  O   GLU A 393    11835  15542  13090   -915    475  -2158  A    O  
ATOM   2971  CB  GLU A 393     139.759  87.624  42.780  1.00119.98      A    C  
ANISOU 2971  CB  GLU A 393    13570  17081  14935   -977    546  -2109  A    C  
ATOM   2972  CG  GLU A 393     139.200  88.895  42.140  1.00132.61      A    C  
ANISOU 2972  CG  GLU A 393    15283  18339  16764  -1067    816  -2094  A    C  
ATOM   2973  CD  GLU A 393     138.881  88.751  40.652  1.00139.42      A    C  
ANISOU 2973  CD  GLU A 393    16364  18896  17712  -1010    921  -1785  A    C  
ATOM   2974  OE1 GLU A 393     139.280  89.646  39.877  1.00145.67      A    O  
ANISOU 2974  OE1 GLU A 393    17198  19423  18724  -1098   1204  -1842  A    O  
ATOM   2975  OE2 GLU A 393     138.213  87.769  40.253  1.00138.22      A    O1-
ANISOU 2975  OE2 GLU A 393    16334  18771  17410   -871    745  -1495  A    O1-
ATOM   2976  N   THR A 394     137.570  86.500  44.997  1.00 74.78      A    N  
ATOM   2977  CA  THR A 394     136.140  86.369  45.189  1.00 87.21      A    C  
ATOM   2978  C   THR A 394     135.732  86.301  46.683  1.00 85.27      A    C  
ATOM   2979  O   THR A 394     134.546  86.225  47.003  1.00 85.83      A    O  
ATOM   2980  CB  THR A 394     135.670  85.088  44.454  1.00 90.46      A    C  
ATOM   2981  CG2 THR A 394     135.916  83.824  45.333  1.00 82.56      A    C  
ATOM   2982  OG1 THR A 394     134.289  85.216  44.092  1.00 91.18      A    O  
ATOM   2983  N   LEU A 395     136.710  86.322  47.589  1.00112.40      A    N  
ANISOU 2983  N   LEU A 395    12607  18056  12043   -246   1038  -1079  A    N  
ATOM   2984  CA  LEU A 395     136.432  86.303  49.032  1.00101.22      A    C  
ANISOU 2984  CA  LEU A 395    11056  16858  10544   -181    923  -1012  A    C  
ATOM   2985  C   LEU A 395     135.579  87.477  49.512  1.00 97.55      A    C  
ANISOU 2985  C   LEU A 395    10759  16285  10017   -367    891  -1119  A    C  
ATOM   2986  O   LEU A 395     134.709  87.275  50.347  1.00 96.42      A    O  
ANISOU 2986  O   LEU A 395    10654  16117   9863   -260    811  -1039  A    O  
ATOM   2987  CB  LEU A 395     137.727  86.285  49.844  1.00103.46      A    C  
ANISOU 2987  CB  LEU A 395    10977  17633  10699   -223    886  -1003  A    C  
ATOM   2988  CG  LEU A 395     138.190  84.909  50.290  1.00102.72      A    C  
ANISOU 2988  CG  LEU A 395    10637  17740  10650    105    880   -766  A    C  
ATOM   2989  CD1 LEU A 395     139.658  84.923  50.675  1.00106.30      A    C  
ANISOU 2989  CD1 LEU A 395    10699  18707  10982     59    874   -737  A    C  
ATOM   2990  CD2 LEU A 395     137.341  84.440  51.448  1.00102.48      A    C  
ANISOU 2990  CD2 LEU A 395    10589  17751  10597    295    785   -605  A    C  
ATOM   2991  N   PRO A 396     135.842  88.709  49.023  1.00 92.22      A    N  
ANISOU 2991  N   PRO A 396    10192  15535   9311   -644    987  -1293  A    N  
ATOM   2992  CA  PRO A 396     134.978  89.843  49.344  1.00 89.38      A    C  
ANISOU 2992  CA  PRO A 396    10038  14986   8937   -801   1036  -1382  A    C  
ATOM   2993  C   PRO A 396     133.481  89.596  49.139  1.00 91.94      A    C  
ANISOU 2993  C   PRO A 396    10587  14979   9367   -614   1004  -1248  A    C  
ATOM   2994  O   PRO A 396     132.653  90.078  49.917  1.00 99.10      A    O  
ANISOU 2994  O   PRO A 396    11578  15821  10254   -635    989  -1254  A    O  
ATOM   2995  CB  PRO A 396     135.451  90.907  48.375  1.00 89.48      A    C  
ANISOU 2995  CB  PRO A 396    10186  14840   8971  -1040   1213  -1527  A    C  
ATOM   2996  CG  PRO A 396     136.911  90.647  48.282  1.00 95.05      A    C  
ANISOU 2996  CG  PRO A 396    10641  15877   9597  -1142   1216  -1607  A    C  
ATOM   2997  CD  PRO A 396     137.076  89.158  48.350  1.00 94.23      A    C  
ANISOU 2997  CD  PRO A 396    10356  15917   9530   -841   1086  -1425  A    C  
ATOM   2998  N   VAL A 397     133.131  88.846  48.104  1.00 91.41      A    N  
ANISOU 2998  N   VAL A 397    10608  14732   9390   -457   1004  -1137  A    N  
ATOM   2999  CA  VAL A 397     131.741  88.440  47.894  1.00 84.44      A    C  
ANISOU 2999  CA  VAL A 397     9892  13621   8571   -297    962  -1005  A    C  
ATOM   3000  C   VAL A 397     131.306  87.422  48.962  1.00 77.90      A    C  
ANISOU 3000  C   VAL A 397     8968  12898   7731   -107    845   -915  A    C  
ATOM   3001  O   VAL A 397     130.218  87.504  49.490  1.00 75.51      A    O  
ANISOU 3001  O   VAL A 397     8761  12493   7435    -48    798   -861  A    O  
ATOM   3002  CB  VAL A 397     131.543  87.869  46.465  1.00 86.06      A    C  
ANISOU 3002  CB  VAL A 397    10195  13675   8827   -245   1007   -937  A    C  
ATOM   3003  CG1 VAL A 397     130.124  87.393  46.266  1.00 84.74      A    C  
ANISOU 3003  CG1 VAL A 397    10160  13357   8681   -125    961   -815  A    C  
ATOM   3004  CG2 VAL A 397     131.893  88.903  45.399  1.00 86.89      A    C  
ANISOU 3004  CG2 VAL A 397    10401  13677   8937   -412   1130   -985  A    C  
ATOM   3005  N   ALA A 398     132.168  86.478  49.304  1.00 77.17      A    N  
ANISOU 3005  N   ALA A 398     8681  13011   7627     -0    819   -877  A    N  
ATOM   3006  CA  ALA A 398     131.828  85.484  50.313  1.00 76.95      A    C  
ANISOU 3006  CA  ALA A 398     8562  13076   7599    209    747   -750  A    C  
ATOM   3007  C   ALA A 398     131.595  86.100  51.679  1.00 78.05      A    C  
ANISOU 3007  C   ALA A 398     8624  13395   7636    153    656   -765  A    C  
ATOM   3008  O   ALA A 398     130.706  85.670  52.405  1.00 77.31      A    O  
ANISOU 3008  O   ALA A 398     8575  13251   7546    283    599   -673  A    O  
ATOM   3009  CB  ALA A 398     132.904  84.418  50.397  1.00 78.88      A    C  
ANISOU 3009  CB  ALA A 398     8590  13513   7866    368    786   -660  A    C  
ATOM   3010  N   GLU A 399     132.393  87.104  52.033  1.00 81.63      A    N  
ANISOU 3010  N   GLU A 399     8967  14067   7982    -72    663   -900  A    N  
ATOM   3011  CA  GLU A 399     132.315  87.714  53.372  1.00 84.51      A    C  
ANISOU 3011  CA  GLU A 399     9236  14669   8204   -195    599   -952  A    C  
ATOM   3012  C   GLU A 399     130.984  88.401  53.558  1.00 82.34      A    C  
ANISOU 3012  C   GLU A 399     9209  14105   7968   -245    621   -995  A    C  
ATOM   3013  O   GLU A 399     130.322  88.256  54.579  1.00 79.73      A    O  
ANISOU 3013  O   GLU A 399     8870  13835   7588   -186    550   -944  A    O  
ATOM   3014  CB  GLU A 399     133.415  88.750  53.577  1.00 89.59      A    C  
ANISOU 3014  CB  GLU A 399     9741  15595   8704   -513    652  -1147  A    C  
ATOM   3015  CG  GLU A 399     134.828  88.218  53.436  1.00 94.48      A    C  
ANISOU 3015  CG  GLU A 399    10067  16574   9257   -496    632  -1110  A    C  
ATOM   3016  CD  GLU A 399     135.200  87.232  54.529  1.00 97.01      A    C  
ANISOU 3016  CD  GLU A 399    10077  17304   9476   -288    508   -905  A    C  
ATOM   3017  OE1 GLU A 399     134.291  86.812  55.302  1.00 87.69      A    O  
ANISOU 3017  OE1 GLU A 399     8948  16069   8298   -127    436   -782  A    O  
ATOM   3018  OE2 GLU A 399     136.418  86.892  54.596  1.00102.52      A    O1-
ANISOU 3018  OE2 GLU A 399    10472  18390  10090   -276    496   -847  A    O1-
ATOM   3019  N   THR A 400     130.601  89.159  52.550  1.00 82.64      A    N  
ANISOU 3019  N   THR A 400     9461  13837   8100   -341    736  -1065  A    N  
ATOM   3020  CA  THR A 400     129.362  89.893  52.605  1.00 84.94      A    C  
ANISOU 3020  CA  THR A 400     9975  13848   8451   -364    796  -1071  A    C  
ATOM   3021  C   THR A 400     128.182  88.941  52.672  1.00 80.17      A    C  
ANISOU 3021  C   THR A 400     9440  13108   7912   -114    699   -900  A    C  
ATOM   3022  O   THR A 400     127.181  89.229  53.312  1.00 78.91      A    O  
ANISOU 3022  O   THR A 400     9372  12852   7756    -92    689   -880  A    O  
ATOM   3023  CB  THR A 400     129.228  90.827  51.399  1.00 88.48      A    C  
ANISOU 3023  CB  THR A 400    10610  14015   8993   -462    962  -1107  A    C  
ATOM   3024  CG2 THR A 400     130.437  91.811  51.328  1.00 93.71      A    C  
ANISOU 3024  CG2 THR A 400    11228  14784   9592   -748   1105  -1308  A    C  
ATOM   3025  OG1 THR A 400     129.179  90.044  50.210  1.00 90.96      A    O  
ANISOU 3025  OG1 THR A 400    10947  14235   9376   -315    930   -988  A    O  
ATOM   3026  N   LEU A 401     128.309  87.790  52.028  1.00 79.91      A    N  
ANISOU 3026  N   LEU A 401     9368  13065   7926     52    654   -796  A    N  
ATOM   3027  CA  LEU A 401     127.272  86.762  52.121  1.00 79.89      A    C  
ANISOU 3027  CA  LEU A 401     9431  12952   7969    248    595   -665  A    C  
ATOM   3028  C   LEU A 401     127.250  86.082  53.477  1.00 80.51      A    C  
ANISOU 3028  C   LEU A 401     9386  13208   7992    367    511   -600  A    C  
ATOM   3029  O   LEU A 401     126.188  85.628  53.930  1.00 77.33      A    O  
ANISOU 3029  O   LEU A 401     9066  12704   7610    478    477   -524  A    O  
ATOM   3030  CB  LEU A 401     127.461  85.692  51.056  1.00 79.98      A    C  
ANISOU 3030  CB  LEU A 401     9455  12892   8040    345    633   -608  A    C  
ATOM   3031  CG  LEU A 401     126.457  85.804  49.927  1.00 79.87      A    C  
ANISOU 3031  CG  LEU A 401     9614  12672   8060    317    670   -575  A    C  
ATOM   3032  CD1 LEU A 401     126.498  87.197  49.319  1.00 81.33      A    C  
ANISOU 3032  CD1 LEU A 401     9868  12786   8246    171    728   -615  A    C  
ATOM   3033  CD2 LEU A 401     126.797  84.759  48.894  1.00 82.38      A    C  
ANISOU 3033  CD2 LEU A 401     9938  12962   8401    343    733   -566  A    C  
ATOM   3034  N   LYS A 402     128.418  85.985  54.113  1.00 78.39      A    N  
ANISOU 3034  N   LYS A 402     8904  13238   7642    349    482   -610  A    N  
ATOM   3035  CA  LYS A 402     128.492  85.383  55.432  1.00 76.38      A    C  
ANISOU 3035  CA  LYS A 402     8491  13224   7306    471    402   -501  A    C  
ATOM   3036  C   LYS A 402     127.815  86.285  56.412  1.00 74.54      A    C  
ANISOU 3036  C   LYS A 402     8308  13034   6981    332    359   -580  A    C  
ATOM   3037  O   LYS A 402     127.150  85.804  57.321  1.00 74.05      A    O  
ANISOU 3037  O   LYS A 402     8240  13005   6889    452    301   -480  A    O  
ATOM   3038  CB  LYS A 402     129.923  85.151  55.871  1.00 80.22      A    C  
ANISOU 3038  CB  LYS A 402     8682  14105   7689    477    378   -458  A    C  
ATOM   3039  CG  LYS A 402     130.066  84.288  57.117  1.00 82.97      A    C  
ANISOU 3039  CG  LYS A 402     8823  14743   7958    680    310   -253  A    C  
ATOM   3040  CD  LYS A 402     131.482  84.413  57.665  1.00 87.21      A    C  
ANISOU 3040  CD  LYS A 402     9012  15794   8329    620    264   -212  A    C  
ATOM   3041  CE  LYS A 402     131.840  83.319  58.651  1.00 90.27      A    C  
ANISOU 3041  CE  LYS A 402     9139  16500   8661    913    230     90  A    C  
ATOM   3042  NZ  LYS A 402     133.314  83.116  58.604  1.00 98.79      A    N1+
ANISOU 3042  NZ  LYS A 402     9874  18003   9656    946    236    188  A    N1+
ATOM   3043  N   ALA A 403     127.972  87.591  56.219  1.00 74.31      A    N  
ANISOU 3043  N   ALA A 403     8344  12976   6915     73    421   -761  A    N  
ATOM   3044  CA  ALA A 403     127.400  88.561  57.145  1.00 77.38      A    C  
ANISOU 3044  CA  ALA A 403     8799  13381   7219   -103    442   -874  A    C  
ATOM   3045  C   ALA A 403     125.918  88.819  56.929  1.00 77.55      A    C  
ANISOU 3045  C   ALA A 403     9065  13037   7363    -31    487   -844  A    C  
ATOM   3046  O   ALA A 403     125.216  89.190  57.864  1.00 84.73      A    O  
ANISOU 3046  O   ALA A 403    10022  13946   8222    -81    486   -875  A    O  
ATOM   3047  CB  ALA A 403     128.153  89.867  57.075  1.00 78.48      A    C  
ANISOU 3047  CB  ALA A 403     8935  13602   7280   -430    564  -1098  A    C  
ATOM   3048  N   ALA A 404     125.427  88.617  55.715  1.00 75.53      A    N  
ANISOU 3048  N   ALA A 404     8944  12506   7246     76    529   -776  A    N  
ATOM   3049  CA  ALA A 404     124.049  88.990  55.404  1.00 72.37      A    C  
ANISOU 3049  CA  ALA A 404     8735  11818   6941    130    581   -725  A    C  
ATOM   3050  C   ALA A 404     123.072  87.826  55.439  1.00 70.30      A    C  
ANISOU 3050  C   ALA A 404     8503  11491   6715    338    489   -578  A    C  
ATOM   3051  O   ALA A 404     121.884  88.029  55.649  1.00 66.05      A    O  
ANISOU 3051  O   ALA A 404     8071  10814   6212    379    499   -534  A    O  
ATOM   3052  CB  ALA A 404     123.993  89.661  54.049  1.00 72.48      A    C  
ANISOU 3052  CB  ALA A 404     8864  11624   7050     87    699   -718  A    C  
ATOM   3053  N   VAL A 405     123.565  86.609  55.228  1.00 72.71      A    N  
ANISOU 3053  N   VAL A 405     8722  11884   7019    461    433   -508  A    N  
ATOM   3054  CA  VAL A 405     122.692  85.437  55.154  1.00 73.42      A    C  
ANISOU 3054  CA  VAL A 405     8869  11877   7147    623    407   -399  A    C  
ATOM   3055  C   VAL A 405     122.953  84.459  56.302  1.00 75.33      A    C  
ANISOU 3055  C   VAL A 405     9006  12268   7347    760    361   -319  A    C  
ATOM   3056  O   VAL A 405     124.088  84.234  56.699  1.00 80.43      A    O  
ANISOU 3056  O   VAL A 405     9489  13126   7944    787    345   -298  A    O  
ATOM   3057  CB  VAL A 405     122.857  84.722  53.796  1.00 72.29      A    C  
ANISOU 3057  CB  VAL A 405     8765  11641   7058    648    462   -376  A    C  
ATOM   3058  CG1 VAL A 405     121.917  83.544  53.700  1.00 73.65      A    C  
ANISOU 3058  CG1 VAL A 405     9019  11710   7253    745    485   -310  A    C  
ATOM   3059  CG2 VAL A 405     122.563  85.677  52.653  1.00 71.54      A    C  
ANISOU 3059  CG2 VAL A 405     8751  11443   6985    532    504   -401  A    C  
ATOM   3060  N   MET A 406     121.891  83.884  56.841  1.00 74.09      A    N  
ANISOU 3060  N   MET A 406     8928  12020   7198    854    349   -252  A    N  
ATOM   3061  CA  MET A 406     122.020  82.886  57.887  1.00 77.77      A    C  
ANISOU 3061  CA  MET A 406     9318  12591   7637   1017    339   -134  A    C  
ATOM   3062  C   MET A 406     122.889  81.751  57.434  1.00 77.04      A    C  
ANISOU 3062  C   MET A 406     9156  12509   7604   1159    427    -47  A    C  
ATOM   3063  O   MET A 406     122.932  81.445  56.254  1.00 78.75      A    O  
ANISOU 3063  O   MET A 406     9452  12576   7892   1126    508    -95  A    O  
ATOM   3064  CB  MET A 406     120.662  82.244  58.142  1.00 83.43      A    C  
ANISOU 3064  CB  MET A 406    10181  13129   8389   1089    365    -86  A    C  
ATOM   3065  CG  MET A 406     119.620  83.156  58.726  1.00 81.08      A    C  
ANISOU 3065  CG  MET A 406     9955  12800   8050    998    305   -137  A    C  
ATOM   3066  SD  MET A 406     120.000  83.371  60.441  1.00 76.53      A    S  
ANISOU 3066  SD  MET A 406     9246  12480   7349   1021    228    -91  A    S  
ATOM   3067  CE  MET A 406     118.542  84.279  60.945  1.00 77.71      A    C  
ANISOU 3067  CE  MET A 406     9536  12501   7490    914    215   -170  A    C  
ATOM   3068  N   PRO A 407     123.529  81.065  58.372  1.00 78.73      A    N  
ANISOU 3068  N   PRO A 407     9220  12904   7787   1328    436    104  A    N  
ATOM   3069  CA  PRO A 407     124.162  79.803  58.041  1.00 82.72      A    C  
ANISOU 3069  CA  PRO A 407     9687  13353   8389   1525    589    234  A    C  
ATOM   3070  C   PRO A 407     123.187  78.829  57.410  1.00 82.38      A    C  
ANISOU 3070  C   PRO A 407     9873  12967   8459   1563    751    214  A    C  
ATOM   3071  O   PRO A 407     123.562  78.107  56.474  1.00 89.72      A    O  
ANISOU 3071  O   PRO A 407    10859  13749   9482   1587    916    192  A    O  
ATOM   3072  CB  PRO A 407     124.624  79.283  59.389  1.00 86.53      A    C  
ANISOU 3072  CB  PRO A 407     9981  14083   8810   1737    577    460  A    C  
ATOM   3073  CG  PRO A 407     124.906  80.517  60.150  1.00 87.86      A    C  
ANISOU 3073  CG  PRO A 407    10000  14580   8802   1566    384    392  A    C  
ATOM   3074  CD  PRO A 407     123.837  81.488  59.736  1.00 82.93      A    C  
ANISOU 3074  CD  PRO A 407     9586  13744   8181   1336    326    175  A    C  
ATOM   3075  N   GLU A 408     121.957  78.783  57.907  1.00 77.59      A    N  
ANISOU 3075  N   GLU A 408     9399  12248   7831   1540    727    203  A    N  
ATOM   3076  CA  GLU A 408     120.927  78.035  57.202  1.00 76.56      A    C  
ANISOU 3076  CA  GLU A 408     9483  11839   7767   1483    871    129  A    C  
ATOM   3077  C   GLU A 408     119.688  78.870  57.088  1.00 72.79      A    C  
ANISOU 3077  C   GLU A 408     9103  11331   7223   1306    743     18  A    C  
ATOM   3078  O   GLU A 408     118.914  78.928  58.019  1.00 78.76      A    O  
ANISOU 3078  O   GLU A 408     9889  12091   7945   1341    695     60  A    O  
ATOM   3079  CB  GLU A 408     120.623  76.695  57.882  1.00 79.02      A    C  
ANISOU 3079  CB  GLU A 408     9874  11998   8150   1674   1074    264  A    C  
ATOM   3080  CG  GLU A 408     119.460  75.950  57.239  1.00 82.84      A    C  
ANISOU 3080  CG  GLU A 408    10591  12213   8668   1544   1245    143  A    C  
ATOM   3081  CD  GLU A 408     119.693  74.447  57.134  1.00 95.86      A    C  
ANISOU 3081  CD  GLU A 408    12358  13620  10445   1675   1594    203  A    C  
ATOM   3082  OE1 GLU A 408     120.354  73.874  58.037  1.00110.62      A    O  
ANISOU 3082  OE1 GLU A 408    14141  15501  12385   1954   1700    425  A    O  
ATOM   3083  OE2 GLU A 408     119.225  73.833  56.140  1.00 96.54      A    O1-
ANISOU 3083  OE2 GLU A 408    12615  13511  10555   1494   1791     40  A    O1-
ATOM   3084  N   PRO A 409     119.497  79.541  55.949  1.00 71.20      A    N  
ANISOU 3084  N   PRO A 409     8934  11115   7002   1129    699    -99  A    N  
ATOM   3085  CA  PRO A 409     118.262  80.335  55.777  1.00 71.13      A    C  
ANISOU 3085  CA  PRO A 409     8994  11093   6940    997    605   -151  A    C  
ATOM   3086  C   PRO A 409     117.020  79.484  55.475  1.00 70.15      A    C  
ANISOU 3086  C   PRO A 409     9002  10851   6799    930    701   -183  A    C  
ATOM   3087  O   PRO A 409     117.153  78.348  55.017  1.00 71.90      A    O  
ANISOU 3087  O   PRO A 409     9299  10968   7049    918    874   -216  A    O  
ATOM   3088  CB  PRO A 409     118.587  81.224  54.577  1.00 68.80      A    C  
ANISOU 3088  CB  PRO A 409     8668  10842   6628    866    563   -211  A    C  
ATOM   3089  CG  PRO A 409     119.537  80.393  53.779  1.00 70.03      A    C  
ANISOU 3089  CG  PRO A 409     8817  10969   6821    869    681   -240  A    C  
ATOM   3090  CD  PRO A 409     120.339  79.551  54.743  1.00 68.96      A    C  
ANISOU 3090  CD  PRO A 409     8626  10832   6741   1056    754   -161  A    C  
ATOM   3091  N   SER A 410     115.831  80.033  55.728  1.00 68.12      A    N  
ANISOU 3091  N   SER A 410     8773  10615   6492    869    621   -182  A    N  
ATOM   3092  CA  SER A 410     114.574  79.364  55.382  1.00 67.95      A    C  
ANISOU 3092  CA  SER A 410     8847  10551   6420    755    695   -224  A    C  
ATOM   3093  C   SER A 410     114.429  79.308  53.884  1.00 65.78      A    C  
ANISOU 3093  C   SER A 410     8570  10346   6076    572    734   -288  A    C  
ATOM   3094  O   SER A 410     115.088  80.045  53.152  1.00 61.58      A    O  
ANISOU 3094  O   SER A 410     7965   9887   5544    550    672   -275  A    O  
ATOM   3095  CB  SER A 410     113.380  80.108  55.937  1.00 68.83      A    C  
ANISOU 3095  CB  SER A 410     8947  10715   6490    740    591   -186  A    C  
ATOM   3096  OG  SER A 410     113.617  80.452  57.283  1.00 71.80      A    O  
ANISOU 3096  OG  SER A 410     9305  11071   6905    880    532   -134  A    O  
ATOM   3097  N   VAL A 411     113.554  78.423  53.432  1.00 66.10      A    N  
ANISOU 3097  N   VAL A 411     8689  10386   6040    412    850   -365  A    N  
ATOM   3098  CA  VAL A 411     113.487  78.113  52.011  1.00 64.75      A    C  
ANISOU 3098  CA  VAL A 411     8515  10324   5760    186    921   -450  A    C  
ATOM   3099  C   VAL A 411     112.933  79.299  51.250  1.00 65.20      A    C  
ANISOU 3099  C   VAL A 411     8438  10616   5716    115    752   -358  A    C  
ATOM   3100  O   VAL A 411     113.485  79.689  50.235  1.00 67.86      A    O  
ANISOU 3100  O   VAL A 411     8717  11053   6013     50    730   -345  A    O  
ATOM   3101  CB  VAL A 411     112.670  76.834  51.784  1.00 63.16      A    C  
ANISOU 3101  CB  VAL A 411     8434  10090   5472    -26   1124   -589  A    C  
ATOM   3102  CG1 VAL A 411     112.092  76.757  50.392  1.00 63.70      A    C  
ANISOU 3102  CG1 VAL A 411     8453  10410   5338   -339   1144   -672  A    C  
ATOM   3103  CG2 VAL A 411     113.550  75.626  52.067  1.00 64.24      A    C  
ANISOU 3103  CG2 VAL A 411     8716   9959   5732     41   1383   -668  A    C  
ATOM   3104  N   TRP A 412     111.853  79.874  51.763  1.00 66.79      A    N  
ANISOU 3104  N   TRP A 412     8589  10899   5886    148    654   -271  A    N  
ATOM   3105  CA  TRP A 412     111.185  80.975  51.107  1.00 67.97      A    C  
ANISOU 3105  CA  TRP A 412     8599  11270   5956    126    536   -128  A    C  
ATOM   3106  C   TRP A 412     111.488  82.250  51.849  1.00 70.42      A    C  
ANISOU 3106  C   TRP A 412     8877  11473   6403    344    449    -10  A    C  
ATOM   3107  O   TRP A 412     111.341  82.314  53.072  1.00 65.46      A    O  
ANISOU 3107  O   TRP A 412     8302  10710   5859    459    437    -24  A    O  
ATOM   3108  CB  TRP A 412     109.682  80.751  51.080  1.00 67.47      A    C  
ANISOU 3108  CB  TRP A 412     8479  11403   5754      1    525    -97  A    C  
ATOM   3109  CG  TRP A 412     109.293  79.509  50.373  1.00 71.16      A    C  
ANISOU 3109  CG  TRP A 412     8984  12002   6050   -287    645   -254  A    C  
ATOM   3110  CD1 TRP A 412     109.096  78.281  50.928  1.00 72.67      A    C  
ANISOU 3110  CD1 TRP A 412     9328  12037   6244   -390    802   -429  A    C  
ATOM   3111  CD2 TRP A 412     109.038  79.360  48.971  1.00 74.20      A    C  
ANISOU 3111  CD2 TRP A 412     9262  12711   6219   -543    654   -261  A    C  
ATOM   3112  CE2 TRP A 412     108.707  78.009  48.749  1.00 76.65      A    C  
ANISOU 3112  CE2 TRP A 412     9677  13044   6400   -836    832   -487  A    C  
ATOM   3113  CE3 TRP A 412     109.080  80.230  47.884  1.00 76.67      A    C  
ANISOU 3113  CE3 TRP A 412     9402  13303   6427   -562    552    -91  A    C  
ATOM   3114  NE1 TRP A 412     108.749  77.370  49.957  1.00 75.96      A    N  
ANISOU 3114  NE1 TRP A 412     9761  12630   6469   -723    939   -584  A    N  
ATOM   3115  CZ2 TRP A 412     108.422  77.511  47.493  1.00 81.25      A    C  
ANISOU 3115  CZ2 TRP A 412    10192  13949   6728  -1187    901   -582  A    C  
ATOM   3116  CZ3 TRP A 412     108.811  79.733  46.639  1.00 80.55      A    C  
ANISOU 3116  CZ3 TRP A 412     9805  14135   6663   -873    591   -142  A    C  
ATOM   3117  CH2 TRP A 412     108.478  78.385  46.448  1.00 83.27      A    C  
ANISOU 3117  CH2 TRP A 412    10250  14531   6855  -1205    758   -404  A    C  
ATOM   3118  N   LEU A 413     111.905  83.275  51.103  1.00 79.06      A    N  
ANISOU 3118  N   LEU A 413     9893  12630   7513    380    415     97  A    N  
ATOM   3119  CA  LEU A 413     112.220  84.583  51.703  1.00 75.00      A    C  
ANISOU 3119  CA  LEU A 413     9372  11991   7133    544    398    183  A    C  
ATOM   3120  C   LEU A 413     111.021  85.155  52.419  1.00 74.99      A    C  
ANISOU 3120  C   LEU A 413     9344  11994   7153    625    387    284  A    C  
ATOM   3121  O   LEU A 413     111.181  85.901  53.361  1.00 75.40      A    O  
ANISOU 3121  O   LEU A 413     9439  11892   7316    729    408    279  A    O  
ATOM   3122  CB  LEU A 413     112.657  85.579  50.635  1.00 74.64      A    C  
ANISOU 3122  CB  LEU A 413     9261  12004   7095    557    418    308  A    C  
ATOM   3123  CG  LEU A 413     112.971  87.017  51.058  1.00 70.32      A    C  
ANISOU 3123  CG  LEU A 413     8730  11298   6690    687    478    386  A    C  
ATOM   3124  CD1 LEU A 413     114.180  87.018  51.969  1.00 72.68      A    C  
ANISOU 3124  CD1 LEU A 413     9113  11428   7074    691    488    207  A    C  
ATOM   3125  CD2 LEU A 413     113.235  87.904  49.849  1.00 69.28      A    C  
ANISOU 3125  CD2 LEU A 413     8540  11222   6560    704    541    551  A    C  
ATOM   3126  N   LYS A 414     109.820  84.818  51.950  1.00 79.37      A    N  
ANISOU 3126  N   LYS A 414     9814  12754   7587    555    368    370  A    N  
ATOM   3127  CA  LYS A 414     108.586  85.392  52.487  1.00 77.26      A    C  
ANISOU 3127  CA  LYS A 414     9486  12532   7336    642    369    501  A    C  
ATOM   3128  C   LYS A 414     108.401  85.003  53.936  1.00 74.83      A    C  
ANISOU 3128  C   LYS A 414     9291  12046   7095    681    369    369  A    C  
ATOM   3129  O   LYS A 414     107.658  85.672  54.639  1.00 76.36      A    O  
ANISOU 3129  O   LYS A 414     9469  12191   7351    776    392    446  A    O  
ATOM   3130  CB  LYS A 414     107.349  84.990  51.629  1.00 80.21      A    C  
ANISOU 3130  CB  LYS A 414     9700  13252   7520    523    337    623  A    C  
ATOM   3131  CG  LYS A 414     106.842  83.547  51.766  1.00 78.96      A    C  
ANISOU 3131  CG  LYS A 414     9585  13197   7217    312    331    441  A    C  
ATOM   3132  CD  LYS A 414     106.148  83.069  50.507  1.00 77.88      A    C  
ANISOU 3132  CD  LYS A 414     9287  13468   6833     87    314    496  A    C  
ATOM   3133  CE  LYS A 414     104.913  83.874  50.186  1.00 78.11      A    C  
ANISOU 3133  CE  LYS A 414     9086  13813   6778    156    270    773  A    C  
ATOM   3134  NZ  LYS A 414     104.253  83.334  48.958  1.00 84.37      A    N1+
ANISOU 3134  NZ  LYS A 414     9681  15106   7269   -110    237    829  A    N1+
ATOM   3135  N   ASP A 415     109.070  83.929  54.374  1.00 75.03      A    N  
ANISOU 3135  N   ASP A 415     9422  11972   7111    618    368    194  A    N  
ATOM   3136  CA  ASP A 415     108.891  83.412  55.732  1.00 79.62      A    C  
ANISOU 3136  CA  ASP A 415    10100  12418   7731    661    376    103  A    C  
ATOM   3137  C   ASP A 415     109.815  84.093  56.743  1.00 83.45      A    C  
ANISOU 3137  C   ASP A 415    10635  12744   8326    774    369     68  A    C  
ATOM   3138  O   ASP A 415     109.766  83.769  57.922  1.00100.96      A    O  
ANISOU 3138  O   ASP A 415    12913  14887  10559    816    367     17  A    O  
ATOM   3139  CB  ASP A 415     109.127  81.893  55.781  1.00 79.54      A    C  
ANISOU 3139  CB  ASP A 415    10180  12372   7668    568    431    -27  A    C  
ATOM   3140  CG  ASP A 415     108.081  81.111  55.036  1.00 83.49      A    C  
ANISOU 3140  CG  ASP A 415    10656  13039   8028    381    474    -55  A    C  
ATOM   3141  OD1 ASP A 415     107.108  81.698  54.530  1.00 83.93      A    O  
ANISOU 3141  OD1 ASP A 415    10586  13296   8004    337    427     53  A    O  
ATOM   3142  OD2 ASP A 415     108.257  79.882  54.920  1.00 96.90      A    O1-
ANISOU 3142  OD2 ASP A 415    12452  14681   9685    267    582   -183  A    O1-
ATOM   3143  N   GLY A 416     110.678  84.994  56.294  1.00 79.13      A    N  
ANISOU 3143  N   GLY A 416    10059  12171   7834    799    377     90  A    N  
ATOM   3144  CA  GLY A 416     111.710  85.526  57.165  1.00 77.26      A    C  
ANISOU 3144  CA  GLY A 416     9855  11841   7656    836    382     15  A    C  
ATOM   3145  C   GLY A 416     112.774  84.490  57.548  1.00 84.06      A    C  
ANISOU 3145  C   GLY A 416    10733  12713   8492    842    353    -66  A    C  
ATOM   3146  O   GLY A 416     112.881  83.400  56.954  1.00 88.90      A    O  
ANISOU 3146  O   GLY A 416    11358  13342   9074    820    370    -78  A    O  
ATOM   3147  N   ASN A 417     113.568  84.828  58.555  1.00 84.54      A    N  
ANISOU 3147  N   ASN A 417    10783  12780   8558    864    338   -116  A    N  
ATOM   3148  CA  ASN A 417     114.731  84.033  58.939  1.00 86.82      A    C  
ANISOU 3148  CA  ASN A 417    11033  13131   8820    906    317   -137  A    C  
ATOM   3149  C   ASN A 417     115.658  83.686  57.806  1.00 78.96      A    C  
ANISOU 3149  C   ASN A 417    10006  12150   7846    890    339   -147  A    C  
ATOM   3150  O   ASN A 417     116.071  82.540  57.654  1.00 78.69      A    O  
ANISOU 3150  O   ASN A 417     9974  12108   7815    944    378   -131  A    O  
ATOM   3151  CB  ASN A 417     114.328  82.781  59.696  1.00 92.67      A    C  
ANISOU 3151  CB  ASN A 417    11813  13858   9538    991    330    -94  A    C  
ATOM   3152  CG  ASN A 417     114.683  82.882  61.156  1.00105.12      A    C  
ANISOU 3152  CG  ASN A 417    13345  15534  11060   1044    289    -72  A    C  
ATOM   3153  ND2 ASN A 417     115.255  81.812  61.696  1.00120.97      A    N  
ANISOU 3153  ND2 ASN A 417    15320  17591  13050   1164    313     12  A    N  
ATOM   3154  OD1 ASN A 417     114.478  83.924  61.790  1.00 99.11      A    O  
ANISOU 3154  OD1 ASN A 417    12573  14815  10266    973    259   -120  A    O  
ATOM   3155  N   VAL A 418     115.993  84.704  57.028  1.00 74.31      A    N  
ANISOU 3155  N   VAL A 418     9395  11557   7280    819    350   -170  A    N  
ATOM   3156  CA  VAL A 418     116.954  84.572  55.954  1.00 73.46      A    C  
ANISOU 3156  CA  VAL A 418     9252  11473   7186    785    373   -188  A    C  
ATOM   3157  C   VAL A 418     118.148  85.462  56.259  1.00 68.93      A    C  
ANISOU 3157  C   VAL A 418     8613  10964   6613    736    372   -252  A    C  
ATOM   3158  O   VAL A 418     119.298  85.012  56.273  1.00 65.25      A    O  
ANISOU 3158  O   VAL A 418     8070  10591   6131    751    363   -275  A    O  
ATOM   3159  CB  VAL A 418     116.322  84.944  54.588  1.00 73.87      A    C  
ANISOU 3159  CB  VAL A 418     9326  11499   7241    724    401   -140  A    C  
ATOM   3160  CG1 VAL A 418     117.372  84.915  53.496  1.00 79.83      A    C  
ANISOU 3160  CG1 VAL A 418    10048  12284   7999    672    430   -166  A    C  
ATOM   3161  CG2 VAL A 418     115.224  83.954  54.227  1.00 73.13      A    C  
ANISOU 3161  CG2 VAL A 418     9268  11420   7098    708    406   -107  A    C  
ATOM   3162  N   ILE A 419     117.871  86.727  56.507  1.00 67.86      A    N  
ANISOU 3162  N   ILE A 419     8506  10782   6493    669    410   -283  A    N  
ATOM   3163  CA  ILE A 419     118.931  87.656  56.857  1.00 70.32      A    C  
ANISOU 3163  CA  ILE A 419     8776  11157   6785    557    452   -388  A    C  
ATOM   3164  C   ILE A 419     119.553  87.263  58.215  1.00 74.41      A    C  
ANISOU 3164  C   ILE A 419     9196  11871   7201    546    381   -435  A    C  
ATOM   3165  O   ILE A 419     118.854  86.893  59.181  1.00 72.40      A    O  
ANISOU 3165  O   ILE A 419     8955  11641   6910    602    338   -398  A    O  
ATOM   3166  CB  ILE A 419     118.426  89.110  56.940  1.00 69.30      A    C  
ANISOU 3166  CB  ILE A 419     8733  10888   6708    466    583   -429  A    C  
ATOM   3167  CG1 ILE A 419     117.666  89.507  55.678  1.00 69.65      A    C  
ANISOU 3167  CG1 ILE A 419     8840  10779   6843    528    660   -302  A    C  
ATOM   3168  CG2 ILE A 419     119.588  90.065  57.170  1.00 68.71      A    C  
ANISOU 3168  CG2 ILE A 419     8638  10865   6603    287    678   -582  A    C  
ATOM   3169  CD1 ILE A 419     118.531  89.655  54.451  1.00 71.06      A    C  
ANISOU 3169  CD1 ILE A 419     8998  10961   7041    490    697   -293  A    C  
ATOM   3170  N   ASN A 420     120.875  87.367  58.281  1.00 75.93      A    N  
ANISOU 3170  N   ASN A 420     9272  12240   7335    470    371   -498  A    N  
ATOM   3171  CA  ASN A 420     121.626  86.937  59.445  1.00 74.86      A    C  
ANISOU 3171  CA  ASN A 420     8981  12392   7070    470    293   -492  A    C  
ATOM   3172  C   ASN A 420     121.403  87.801  60.671  1.00 78.73      A    C  
ANISOU 3172  C   ASN A 420     9466  13000   7448    309    305   -595  A    C  
ATOM   3173  O   ASN A 420     120.861  88.911  60.595  1.00 81.53      A    O  
ANISOU 3173  O   ASN A 420     9950  13182   7845    170    419   -709  A    O  
ATOM   3174  CB  ASN A 420     123.109  86.923  59.108  1.00 73.27      A    C  
ANISOU 3174  CB  ASN A 420     8620  12401   6816    408    286   -528  A    C  
ATOM   3175  CG  ASN A 420     123.860  85.926  59.915  1.00 72.08      A    C  
ANISOU 3175  CG  ASN A 420     8265  12555   6566    536    200   -400  A    C  
ATOM   3176  ND2 ASN A 420     125.152  85.916  59.758  1.00 73.47      A    N  
ANISOU 3176  ND2 ASN A 420     8259  12977   6678    490    190   -410  A    N  
ATOM   3177  OD1 ASN A 420     123.278  85.137  60.644  1.00 72.96      A    O  
ANISOU 3177  OD1 ASN A 420     8375  12682   6666    695    159   -269  A    O  
ATOM   3178  N   HIS A 421     121.806  87.278  61.821  1.00 83.65      A    N  
ANISOU 3178  N   HIS A 421     9935  13924   7923    331    214   -539  A    N  
ATOM   3179  CA  HIS A 421     121.698  88.034  63.059  1.00 89.59      A    C  
ANISOU 3179  CA  HIS A 421    10655  14868   8516    133    221   -651  A    C  
ATOM   3180  C   HIS A 421     122.827  89.018  63.095  1.00 93.63      A    C  
ANISOU 3180  C   HIS A 421    11067  15603   8903   -157    283   -840  A    C  
ATOM   3181  O   HIS A 421     123.956  88.654  62.819  1.00102.67      A    O  
ANISOU 3181  O   HIS A 421    12033  16988   9987   -148    227   -801  A    O  
ATOM   3182  CB  HIS A 421     121.736  87.112  64.275  1.00 91.30      A    C  
ANISOU 3182  CB  HIS A 421    10718  15386   8583    256     99   -493  A    C  
ATOM   3183  CG  HIS A 421     120.520  86.244  64.387  1.00 93.31      A    C  
ANISOU 3183  CG  HIS A 421    11104  15398   8950    490     82   -345  A    C  
ATOM   3184  CD2 HIS A 421     119.230  86.555  64.657  1.00 91.94      A    C  
ANISOU 3184  CD2 HIS A 421    11105  14990   8834    477    125   -389  A    C  
ATOM   3185  ND1 HIS A 421     120.546  84.884  64.151  1.00 92.46      A    N  
ANISOU 3185  ND1 HIS A 421    10963  15249   8917    765     50   -136  A    N  
ATOM   3186  CE1 HIS A 421     119.332  84.388  64.297  1.00 89.27      A    C  
ANISOU 3186  CE1 HIS A 421    10712  14611   8593    879     72    -78  A    C  
ATOM   3187  NE2 HIS A 421     118.513  85.383  64.594  1.00 91.88      A    N  
ANISOU 3187  NE2 HIS A 421    11156  14839   8912    715     98   -220  A    N  
ATOM   3188  N   GLY A 422     122.512  90.277  63.364  1.00 94.32      A    N  
ANISOU 3188  N   GLY A 422    11282  15585   8968   -423    436  -1054  A    N  
ATOM   3189  CA  GLY A 422     123.532  91.300  63.485  1.00 94.64      A    C  
ANISOU 3189  CA  GLY A 422    11258  15826   8871   -773    551  -1287  A    C  
ATOM   3190  C   GLY A 422     123.815  92.075  62.221  1.00 94.37      A    C  
ANISOU 3190  C   GLY A 422    11365  15485   9003   -850    728  -1392  A    C  
ATOM   3191  O   GLY A 422     124.501  93.086  62.262  1.00100.52      A    O  
ANISOU 3191  O   GLY A 422    12158  16333   9702  -1174    895  -1621  A    O  
ATOM   3192  N   PHE A 423     123.308  91.616  61.089  1.00 93.60      A    N  
ANISOU 3192  N   PHE A 423    11372  15068   9121   -581    708  -1229  A    N  
ATOM   3193  CA  PHE A 423     123.560  92.324  59.831  1.00 95.45      A    C  
ANISOU 3193  CA  PHE A 423    11731  15030   9504   -629    872  -1283  A    C  
ATOM   3194  C   PHE A 423     122.895  93.678  59.878  1.00100.06      A    C  
ANISOU 3194  C   PHE A 423    12537  15300  10180   -796   1155  -1423  A    C  
ATOM   3195  O   PHE A 423     123.467  94.680  59.421  1.00105.90      A    O  
ANISOU 3195  O   PHE A 423    13363  15922  10952  -1009   1382  -1578  A    O  
ATOM   3196  CB  PHE A 423     123.022  91.540  58.636  1.00 91.60      A    C  
ANISOU 3196  CB  PHE A 423    11298  14314   9190   -325    794  -1067  A    C  
ATOM   3197  CG  PHE A 423     123.200  92.233  57.313  1.00 87.09      A    C  
ANISOU 3197  CG  PHE A 423    10842  13491   8756   -350    954  -1074  A    C  
ATOM   3198  CD1 PHE A 423     124.436  92.308  56.722  1.00 90.33      A    C  
ANISOU 3198  CD1 PHE A 423    11167  14024   9128   -462    971  -1150  A    C  
ATOM   3199  CD2 PHE A 423     122.119  92.774  56.644  1.00 89.16      A    C  
ANISOU 3199  CD2 PHE A 423    11278  13419   9178   -243   1090   -971  A    C  
ATOM   3200  CE1 PHE A 423     124.607  92.931  55.492  1.00 95.32      A    C  
ANISOU 3200  CE1 PHE A 423    11910  14426   9879   -481   1126  -1139  A    C  
ATOM   3201  CE2 PHE A 423     122.277  93.393  55.410  1.00 92.02      A    C  
ANISOU 3201  CE2 PHE A 423    11729  13578   9655   -238   1244   -924  A    C  
ATOM   3202  CZ  PHE A 423     123.525  93.475  54.830  1.00 91.41      A    C  
ANISOU 3202  CZ  PHE A 423    11591  13601   9540   -363   1264  -1014  A    C  
ATOM   3203  N   HIS A 424     121.677  93.690  60.416  1.00100.42      A    N  
ANISOU 3203  N   HIS A 424    12685  15187  10281   -691   1173  -1358  A    N  
ATOM   3204  CA  HIS A 424     120.934  94.929  60.596  1.00 99.95      A    C  
ANISOU 3204  CA  HIS A 424    12836  14812  10328   -814   1476  -1466  A    C  
ATOM   3205  C   HIS A 424     120.437  94.972  62.029  1.00103.00      A    C  
ANISOU 3205  C   HIS A 424    13216  15339  10579   -938   1466  -1571  A    C  
ATOM   3206  O   HIS A 424     119.787  94.024  62.485  1.00107.66      A    O  
ANISOU 3206  O   HIS A 424    13735  16032  11137   -735   1247  -1417  A    O  
ATOM   3207  CB  HIS A 424     119.774  95.000  59.603  1.00 94.93      A    C  
ANISOU 3207  CB  HIS A 424    12335  13804   9930   -522   1551  -1235  A    C  
ATOM   3208  CG  HIS A 424     119.346  96.394  59.273  1.00 90.39      A    C  
ANISOU 3208  CG  HIS A 424    11967  12849   9525   -597   1941  -1282  A    C  
ATOM   3209  CD2 HIS A 424     119.913  97.342  58.490  1.00 93.06      A    C  
ANISOU 3209  CD2 HIS A 424    12415  12978   9965   -706   2218  -1341  A    C  
ATOM   3210  ND1 HIS A 424     118.187  96.947  59.765  1.00 88.08      A    N  
ANISOU 3210  ND1 HIS A 424    11804  12323   9339   -539   2128  -1248  A    N  
ATOM   3211  CE1 HIS A 424     118.057  98.177  59.304  1.00 90.89      A    C  
ANISOU 3211  CE1 HIS A 424    12340  12326   9867   -590   2524  -1269  A    C  
ATOM   3212  NE2 HIS A 424     119.089  98.443  58.526  1.00 92.02      A    N  
ANISOU 3212  NE2 HIS A 424    12483  12470  10012   -694   2591  -1324  A    N  
ATOM   3213  N   PRO A 425     120.763  96.059  62.754  1.00103.42      A    N  
ANISOU 3213  N   PRO A 425    13350  15406  10539  -1299   1722  -1847  A    N  
ATOM   3214  CA  PRO A 425     120.413  96.177  64.168  1.00101.76      A    C  
ANISOU 3214  CA  PRO A 425    13125  15385  10153  -1492   1732  -1989  A    C  
ATOM   3215  C   PRO A 425     118.912  96.283  64.370  1.00101.68      A    C  
ANISOU 3215  C   PRO A 425    13276  15041  10314  -1287   1822  -1871  A    C  
ATOM   3216  O   PRO A 425     118.373  95.702  65.302  1.00101.89      A    O  
ANISOU 3216  O   PRO A 425    13240  15242  10229  -1239   1661  -1829  A    O  
ATOM   3217  CB  PRO A 425     121.083  97.479  64.581  1.00104.63      A    C  
ANISOU 3217  CB  PRO A 425    13589  15751  10414  -1968   2080  -2345  A    C  
ATOM   3218  CG  PRO A 425     121.157  98.279  63.322  1.00106.39      A    C  
ANISOU 3218  CG  PRO A 425    13998  15531  10893  -1917   2369  -2334  A    C  
ATOM   3219  CD  PRO A 425     121.400  97.284  62.235  1.00103.65      A    C  
ANISOU 3219  CD  PRO A 425    13517  15233  10632  -1568   2070  -2053  A    C  
ATOM   3220  N   GLU A 426     118.245  97.005  63.477  1.00105.77      A    N  
ANISOU 3220  N   GLU A 426    13985  15101  11101  -1149   2085  -1791  A    N  
ATOM   3221  CA  GLU A 426     116.798  97.173  63.547  1.00108.52      A    C  
ANISOU 3221  CA  GLU A 426    14460  15141  11631   -928   2197  -1643  A    C  
ATOM   3222  C   GLU A 426     116.117  95.820  63.427  1.00100.30      A    C  
ANISOU 3222  C   GLU A 426    13285  14241  10583   -594   1825  -1375  A    C  
ATOM   3223  O   GLU A 426     115.221  95.519  64.193  1.00 97.27      A    O  
ANISOU 3223  O   GLU A 426    12910  13871  10176   -527   1769  -1337  A    O  
ATOM   3224  CB  GLU A 426     116.314  98.116  62.434  1.00119.35      A    C  
ANISOU 3224  CB  GLU A 426    16004  16052  13291   -779   2534  -1519  A    C  
ATOM   3225  CG  GLU A 426     114.902  98.663  62.618  1.00130.33      A    C  
ANISOU 3225  CG  GLU A 426    17533  17110  14876   -608   2779  -1398  A    C  
ATOM   3226  CD  GLU A 426     114.551  99.775  61.617  1.00142.94      A    C  
ANISOU 3226  CD  GLU A 426    19292  18262  16757   -473   3199  -1256  A    C  
ATOM   3227  OE1 GLU A 426     115.436 100.212  60.842  1.00134.46      A    O  
ANISOU 3227  OE1 GLU A 426    18258  17109  15721   -555   3329  -1293  A    O  
ATOM   3228  OE2 GLU A 426     113.374 100.216  61.600  1.00155.74      A    O1-
ANISOU 3228  OE2 GLU A 426    20993  19612  18567   -264   3414  -1081  A    O1-
ATOM   3229  N   LEU A 427     116.551  95.001  62.471  1.00 97.48      A    N  
ANISOU 3229  N   LEU A 427    12816  13981  10241   -412   1601  -1210  A    N  
ATOM   3230  CA  LEU A 427     115.952  93.682  62.258  1.00 92.67      A    C  
ANISOU 3230  CA  LEU A 427    12102  13479   9627   -134   1304   -987  A    C  
ATOM   3231  C   LEU A 427     116.100  92.813  63.497  1.00 89.00      A    C  
ANISOU 3231  C   LEU A 427    11527  13326   8961   -184   1089  -1033  A    C  
ATOM   3232  O   LEU A 427     115.209  92.056  63.831  1.00 82.86      A    O  
ANISOU 3232  O   LEU A 427    10739  12556   8188    -17    964   -907  A    O  
ATOM   3233  CB  LEU A 427     116.580  92.969  61.052  1.00 92.05      A    C  
ANISOU 3233  CB  LEU A 427    11933  13464   9575      2   1147   -856  A    C  
ATOM   3234  CG  LEU A 427     116.038  91.573  60.719  1.00 91.87      A    C  
ANISOU 3234  CG  LEU A 427    11828  13532   9546    239    899   -662  A    C  
ATOM   3235  CD1 LEU A 427     114.614  91.621  60.192  1.00 89.17      A    C  
ANISOU 3235  CD1 LEU A 427    11551  12995   9334    417    950   -490  A    C  
ATOM   3236  CD2 LEU A 427     116.939  90.864  59.714  1.00 94.04      A    C  
ANISOU 3236  CD2 LEU A 427    12013  13906   9810    296    779   -603  A    C  
ATOM   3237  N   ASP A 428     117.240  92.905  64.166  1.00 93.38      A    N  
ANISOU 3237  N   ASP A 428    11982  14172   9324   -416   1052  -1196  A    N  
ATOM   3238  CA  ASP A 428     117.465  92.098  65.353  1.00 93.67      A    C  
ANISOU 3238  CA  ASP A 428    11876  14568   9144   -447    854  -1188  A    C  
ATOM   3239  C   ASP A 428     116.491  92.514  66.414  1.00 93.80      A    C  
ANISOU 3239  C   ASP A 428    11991  14524   9125   -536    953  -1264  A    C  
ATOM   3240  O   ASP A 428     115.893  91.657  67.057  1.00 91.25      A    O  
ANISOU 3240  O   ASP A 428    11625  14303   8744   -392    798  -1140  A    O  
ATOM   3241  CB  ASP A 428     118.881  92.252  65.870  1.00 99.70      A    C  
ANISOU 3241  CB  ASP A 428    12471  15734   9675   -707    810  -1332  A    C  
ATOM   3242  CG  ASP A 428     119.909  91.793  64.875  1.00107.54      A    C  
ANISOU 3242  CG  ASP A 428    13347  16812  10699   -617    713  -1254  A    C  
ATOM   3243  OD1 ASP A 428     119.674  90.765  64.175  1.00116.74      A    O  
ANISOU 3243  OD1 ASP A 428    14487  17887  11980   -315    572  -1040  A    O  
ATOM   3244  OD2 ASP A 428     120.949  92.479  64.791  1.00110.01      A    O1-
ANISOU 3244  OD2 ASP A 428    13601  17281  10914   -878    804  -1430  A    O1-
ATOM   3245  N   GLU A 429     116.317  93.828  66.566  1.00 98.18      A    N  
ANISOU 3245  N   GLU A 429    12695  14882   9727   -771   1248  -1470  A    N  
ATOM   3246  CA  GLU A 429     115.371  94.393  67.532  1.00101.21      A    C  
ANISOU 3246  CA  GLU A 429    13202  15154  10099   -884   1416  -1578  A    C  
ATOM   3247  C   GLU A 429     113.920  93.978  67.235  1.00 90.88      A    C  
ANISOU 3247  C   GLU A 429    11977  13565   8989   -563   1390  -1364  A    C  
ATOM   3248  O   GLU A 429     113.195  93.556  68.139  1.00 83.19      A    O  
ANISOU 3248  O   GLU A 429    10998  12668   7939   -532   1314  -1336  A    O  
ATOM   3249  CB  GLU A 429     115.497  95.917  67.547  1.00112.54      A    C  
ANISOU 3249  CB  GLU A 429    14814  16345  11598  -1186   1823  -1840  A    C  
ATOM   3250  CG  GLU A 429     114.544  96.613  68.511  1.00130.87      A    C  
ANISOU 3250  CG  GLU A 429    17289  18504  13929  -1330   2071  -1981  A    C  
ATOM   3251  CD  GLU A 429     114.787  96.237  69.975  1.00148.11      A    C  
ANISOU 3251  CD  GLU A 429    19357  21131  15783  -1580   1920  -2118  A    C  
ATOM   3252  OE1 GLU A 429     115.947  95.935  70.335  1.00164.01      A    O  
ANISOU 3252  OE1 GLU A 429    21191  23593  17532  -1784   1751  -2200  A    O  
ATOM   3253  OE2 GLU A 429     113.821  96.244  70.775  1.00147.81      A    O1-
ANISOU 3253  OE2 GLU A 429    19392  21031  15737  -1572   1972  -2127  A    O1-
ATOM   3254  N   LEU A 430     113.518  94.107  65.967  1.00 87.46      A    N  
ANISOU 3254  N   LEU A 430    11600  12845   8787   -344   1456  -1207  A    N  
ATOM   3255  CA  LEU A 430     112.192  93.704  65.503  1.00 82.70      A    C  
ANISOU 3255  CA  LEU A 430    11027  12046   8347    -54   1422   -985  A    C  
ATOM   3256  C   LEU A 430     112.008  92.244  65.779  1.00 81.74      A    C  
ANISOU 3256  C   LEU A 430    10790  12153   8115     97   1105   -852  A    C  
ATOM   3257  O   LEU A 430     110.953  91.801  66.185  1.00 82.35      A    O  
ANISOU 3257  O   LEU A 430    10885  12194   8209    211   1059   -767  A    O  
ATOM   3258  CB  LEU A 430     112.026  93.958  63.996  1.00 82.18      A    C  
ANISOU 3258  CB  LEU A 430    10976  11767   8479    135   1497   -810  A    C  
ATOM   3259  CG  LEU A 430     111.367  95.275  63.557  1.00 88.18      A    C  
ANISOU 3259  CG  LEU A 430    11872  12177   9455    172   1865   -772  A    C  
ATOM   3260  CD1 LEU A 430     109.955  95.369  64.112  1.00 90.54      A    C  
ANISOU 3260  CD1 LEU A 430    12210  12356   9832    291   1952   -685  A    C  
ATOM   3261  CD2 LEU A 430     112.157  96.525  63.954  1.00 92.02      A    C  
ANISOU 3261  CD2 LEU A 430    12490  12524   9948   -117   2195  -1031  A    C  
ATOM   3262  N   ARG A 431     113.057  91.488  65.523  1.00 88.46      A    N  
ANISOU 3262  N   ARG A 431    11523  13223   8863    104    916   -830  A    N  
ATOM   3263  CA  ARG A 431     113.020  90.039  65.634  1.00 90.66      A    C  
ANISOU 3263  CA  ARG A 431    11707  13669   9068    272    673   -683  A    C  
ATOM   3264  C   ARG A 431     113.016  89.693  67.110  1.00 89.62      A    C  
ANISOU 3264  C   ARG A 431    11533  13765   8753    186    601   -729  A    C  
ATOM   3265  O   ARG A 431     112.570  88.639  67.503  1.00 91.37      A    O  
ANISOU 3265  O   ARG A 431    11727  14053   8935    331    475   -602  A    O  
ATOM   3266  CB  ARG A 431     114.251  89.461  64.909  1.00 94.67      A    C  
ANISOU 3266  CB  ARG A 431    12105  14324   9542    305    558   -642  A    C  
ATOM   3267  CG  ARG A 431     114.252  87.992  64.546  1.00 92.77      A    C  
ANISOU 3267  CG  ARG A 431    11801  14145   9303    510    395   -474  A    C  
ATOM   3268  CD  ARG A 431     115.549  87.678  63.780  1.00 92.44      A    C  
ANISOU 3268  CD  ARG A 431    11659  14213   9248    519    342   -461  A    C  
ATOM   3269  NE  ARG A 431     115.384  87.664  62.319  1.00 90.86      A    N  
ANISOU 3269  NE  ARG A 431    11506  13828   9188    593    378   -410  A    N  
ATOM   3270  CZ  ARG A 431     116.382  87.564  61.442  1.00 85.88      A    C  
ANISOU 3270  CZ  ARG A 431    10817  13238   8573    586    367   -413  A    C  
ATOM   3271  NH1 ARG A 431     117.633  87.532  61.853  1.00 90.79      A    N1+
ANISOU 3271  NH1 ARG A 431    11321  14079   9094    512    325   -466  A    N1+
ATOM   3272  NH2 ARG A 431     116.128  87.523  60.151  1.00 81.27      A    N  
ANISOU 3272  NH2 ARG A 431    10274  12513   8090    640    398   -357  A    N  
ATOM   3273  N   ARG A 432     113.504  90.602  67.939  1.00 97.91      A    N  
ANISOU 3273  N   ARG A 432    12584  14941   9675    -72    706   -917  A    N  
ATOM   3274  CA  ARG A 432     113.596  90.344  69.383  1.00101.94      A    C  
ANISOU 3274  CA  ARG A 432    13025  15750   9956   -197    632   -961  A    C  
ATOM   3275  C   ARG A 432     112.247  90.236  70.041  1.00 99.21      A    C  
ANISOU 3275  C   ARG A 432    12785  15261   9649   -132    673   -929  A    C  
ATOM   3276  O   ARG A 432     112.081  89.474  70.979  1.00116.39      A    O  
ANISOU 3276  O   ARG A 432    14901  17642  11678    -91    549   -847  A    O  
ATOM   3277  CB  ARG A 432     114.405  91.419  70.086  1.00 97.53      A    C  
ANISOU 3277  CB  ARG A 432    12440  15401   9215   -566    761  -1212  A    C  
ATOM   3278  CG  ARG A 432     115.338  90.839  71.108  1.00 96.21      A    C  
ANISOU 3278  CG  ARG A 432    12058  15759   8738   -678    579  -1184  A    C  
ATOM   3279  CD  ARG A 432     116.205  91.929  71.677  1.00108.57      A    C  
ANISOU 3279  CD  ARG A 432    13576  17592  10085  -1110    716  -1465  A    C  
ATOM   3280  NE  ARG A 432     115.384  92.904  72.393  1.00123.52      A    N  
ANISOU 3280  NE  ARG A 432    15646  19321  11965  -1356    954  -1689  A    N  
ATOM   3281  CZ  ARG A 432     115.754  93.571  73.488  1.00128.50      A    C  
ANISOU 3281  CZ  ARG A 432    16237  20276  12312  -1766   1057  -1930  A    C  
ATOM   3282  NH1 ARG A 432     116.959  93.393  74.030  1.00132.06      A    N1+
ANISOU 3282  NH1 ARG A 432    16439  21304  12433  -1991    914  -1964  A    N1+
ATOM   3283  NH2 ARG A 432     114.902  94.426  74.040  1.00123.72      A    N  
ANISOU 3283  NH2 ARG A 432    15828  19437  11740  -1968   1320  -2136  A    N  
ATOM   3284  N   ILE A 433     111.278  90.981  69.537  1.00 93.39      A    N  
ANISOU 3284  N   ILE A 433    12193  14176   9113   -101    860   -966  A    N  
ATOM   3285  CA  ILE A 433     109.897  90.799  69.953  1.00 88.97      A    C  
ANISOU 3285  CA  ILE A 433    11718  13461   8624      5    897   -903  A    C  
ATOM   3286  C   ILE A 433     109.398  89.395  69.471  1.00 95.85      A    C  
ANISOU 3286  C   ILE A 433    12541  14332   9544    278    700   -678  A    C  
ATOM   3287  O   ILE A 433     108.887  89.181  68.358  1.00 79.83      A    O  
ANISOU 3287  O   ILE A 433    10528  12128   7677    439    702   -567  A    O  
ATOM   3288  CB  ILE A 433     109.037  91.955  69.444  1.00 83.56      A    C  
ANISOU 3288  CB  ILE A 433    11165  12430   8153      4   1171   -953  A    C  
ATOM   3289  CG1 ILE A 433     109.728  93.305  69.755  1.00 78.01      A    C  
ANISOU 3289  CG1 ILE A 433    10539  11678   7421   -289   1432  -1198  A    C  
ATOM   3290  CG2 ILE A 433     107.656  91.852  70.058  1.00 85.02      A    C  
ANISOU 3290  CG2 ILE A 433    11413  12504   8383     81   1224   -908  A    C  
ATOM   3291  CD1 ILE A 433     109.195  94.497  68.995  1.00 73.68      A    C  
ANISOU 3291  CD1 ILE A 433    10124  10742   7127   -253   1766  -1210  A    C  
ATOM   3292  N   GLN A 434     109.638  88.422  70.338  1.00113.57      A    N  
ANISOU 3292  N   GLN A 434    14720  16807  11625    307    549   -611  A    N  
ATOM   3293  CA  GLN A 434     109.382  87.016  70.059  1.00117.87      A    C  
ANISOU 3293  CA  GLN A 434    15237  17355  12191    525    415   -424  A    C  
ATOM   3294  C   GLN A 434     109.448  86.240  71.375  1.00133.13      A    C  
ANISOU 3294  C   GLN A 434    17127  19514  13941    539    331   -349  A    C  
ATOM   3295  O   GLN A 434     108.606  85.377  71.640  1.00156.59      A    O  
ANISOU 3295  O   GLN A 434    20155  22407  16935    664    317   -243  A    O  
ATOM   3296  CB  GLN A 434     110.440  86.459  69.124  1.00110.46      A    C  
ANISOU 3296  CB  GLN A 434    14213  16475  11279    615    333   -348  A    C  
ATOM   3297  CG  GLN A 434     111.854  86.570  69.682  1.00101.98      A    C  
ANISOU 3297  CG  GLN A 434    13003  15711  10031    514    265   -374  A    C  
ATOM   3298  CD  GLN A 434     112.819  85.759  68.901  1.00103.11      A    C  
ANISOU 3298  CD  GLN A 434    13051  15921  10202    650    188   -257  A    C  
ATOM   3299  NE2 GLN A 434     114.094  86.081  69.021  1.00105.36      A    N  
ANISOU 3299  NE2 GLN A 434    13197  16463  10370    549    147   -294  A    N  
ATOM   3300  OE1 GLN A 434     112.423  84.845  68.177  1.00107.88      A    O  
ANISOU 3300  OE1 GLN A 434    13705  16357  10927    823    183   -146  A    O  
ATOM   3301  N   ASN A 435     110.455  86.533  72.193  1.00125.78      A    N  
ANISOU 3301  N   ASN A 435    16085  18893  12811    399    286   -391  A    N  
ATOM   3302  CA  ASN A 435     110.449  86.064  73.557  1.00150.05      A    C  
ANISOU 3302  CA  ASN A 435    19099  22237  15673    376    224   -314  A    C  
ATOM   3303  C   ASN A 435     109.340  86.808  74.293  1.00155.91      A    C  
ANISOU 3303  C   ASN A 435    19968  22868  16402    222    337   -462  A    C  
ATOM   3304  O   ASN A 435     108.605  86.209  75.086  1.00164.13      A    O  
ANISOU 3304  O   ASN A 435    21048  23929  17385    288    320   -372  A    O  
ATOM   3305  CB  ASN A 435     111.818  86.258  74.234  1.00161.43      A    C  
ANISOU 3305  CB  ASN A 435    20342  24137  16857    230    140   -312  A    C  
ATOM   3306  CG  ASN A 435     112.158  87.723  74.507  1.00151.52      A    C  
ANISOU 3306  CG  ASN A 435    19091  22985  15494   -131    245   -601  A    C  
ATOM   3307  ND2 ASN A 435     113.048  87.946  75.457  1.00133.95      A    N  
ANISOU 3307  ND2 ASN A 435    16693  21236  12964   -347    187   -636  A    N  
ATOM   3308  OD1 ASN A 435     111.639  88.634  73.864  1.00153.05      A    O  
ANISOU 3308  OD1 ASN A 435    19435  22847  15867   -220    402   -778  A    O  
ATOM   3309  N   HIS A 436     109.204  88.103  74.000  1.00146.82      A    N  
ANISOU 3309  N   HIS A 436    18890  21569  15323     27    488   -680  A    N  
ATOM   3310  CA  HIS A 436     108.075  88.883  74.492  1.00157.08      A    C  
ANISOU 3310  CA  HIS A 436    20328  22676  16677    -88    658   -818  A    C  
ATOM   3311  C   HIS A 436     106.784  88.242  73.971  1.00164.61      A    C  
ANISOU 3311  C   HIS A 436    21367  23346  17830    152    659   -683  A    C  
ATOM   3312  O   HIS A 436     105.691  88.544  74.454  1.00194.99      A    O  
ANISOU 3312  O   HIS A 436    25307  27059  21721    123    768   -732  A    O  
ATOM   3313  CB  HIS A 436     108.185  90.364  74.057  1.00157.94      A    C  
ANISOU 3313  CB  HIS A 436    20522  22597  16892   -289    891  -1043  A    C  
ATOM   3314  CG  HIS A 436     107.142  91.266  74.661  1.00144.85      A    C  
ANISOU 3314  CG  HIS A 436    19006  20739  15292   -424   1130  -1196  A    C  
ATOM   3315  CD2 HIS A 436     106.662  91.355  75.926  1.00140.18      A    C  
ANISOU 3315  CD2 HIS A 436    18453  20272  14538   -582   1178  -1286  A    C  
ATOM   3316  ND1 HIS A 436     106.453  92.211  73.927  1.00130.56      A    N  
ANISOU 3316  ND1 HIS A 436    17313  18554  13738   -384   1381  -1249  A    N  
ATOM   3317  CE1 HIS A 436     105.598  92.841  74.712  1.00131.50      A    C  
ANISOU 3317  CE1 HIS A 436    17542  18551  13869   -503   1589  -1369  A    C  
ATOM   3318  NE2 HIS A 436     105.706  92.342  75.930  1.00135.35      A    N  
ANISOU 3318  NE2 HIS A 436    17991  19336  14099   -643   1465  -1414  A    N  
ATOM   3319  N   GLY A 437     106.905  87.353  72.987  1.00153.68      A    N  
ANISOU 3319  N   GLY A 437    19947  21890  16552    362    554   -527  A    N  
ATOM   3320  CA  GLY A 437     105.754  86.630  72.476  1.00143.45      A    C  
ANISOU 3320  CA  GLY A 437    18711  20398  15394    534    553   -416  A    C  
ATOM   3321  C   GLY A 437     105.295  85.663  73.537  1.00130.12      A    C  
ANISOU 3321  C   GLY A 437    17047  18808  13585    582    499   -330  A    C  
ATOM   3322  O   GLY A 437     104.257  85.855  74.177  1.00120.79      A    O  
ANISOU 3322  O   GLY A 437    15936  17556  12401    538    573   -372  A    O  
ATOM   3323  N   ASP A 438     106.099  84.633  73.745  1.00118.55      A    N  
ANISOU 3323  N   ASP A 438    15518  17503  12021    681    394   -191  A    N  
ATOM   3324  CA  ASP A 438     105.676  83.534  74.576  1.00116.24      A    C  
ANISOU 3324  CA  ASP A 438    15261  17258  11647    783    377    -52  A    C  
ATOM   3325  C   ASP A 438     105.705  83.893  76.050  1.00111.46      A    C  
ANISOU 3325  C   ASP A 438    14630  16887  10831    656    367    -74  A    C  
ATOM   3326  O   ASP A 438     104.841  83.447  76.793  1.00110.36      A    O  
ANISOU 3326  O   ASP A 438    14566  16713  10653    678    404    -28  A    O  
ATOM   3327  CB  ASP A 438     106.522  82.293  74.283  1.00122.03      A    C  
ANISOU 3327  CB  ASP A 438    15940  18050  12375    970    330    144  A    C  
ATOM   3328  CG  ASP A 438     106.100  81.591  73.000  1.00115.23      A    C  
ANISOU 3328  CG  ASP A 438    15154  16927  11700   1073    385    160  A    C  
ATOM   3329  OD1 ASP A 438     105.106  82.016  72.384  1.00102.87      A    O  
ANISOU 3329  OD1 ASP A 438    13651  15192  10241   1004    430     50  A    O  
ATOM   3330  OD2 ASP A 438     106.757  80.607  72.607  1.00115.63      A    O1-
ANISOU 3330  OD2 ASP A 438    15189  16963  11782   1213    401    290  A    O1-
ATOM   3331  N   GLU A 439     106.674  84.700  76.474  1.00111.29      A    N  
ANISOU 3331  N   GLU A 439    14503  17127  10655    491    329   -158  A    N  
ATOM   3332  CA  GLU A 439     106.810  85.022  77.908  1.00116.89      A    C  
ANISOU 3332  CA  GLU A 439    15159  18151  11100    317    315   -187  A    C  
ATOM   3333  C   GLU A 439     105.751  86.013  78.426  1.00112.26      A    C  
ANISOU 3333  C   GLU A 439    14700  17424  10527    111    456   -408  A    C  
ATOM   3334  O   GLU A 439     105.346  85.935  79.575  1.00122.89      A    O  
ANISOU 3334  O   GLU A 439    16062  18926  11702     20    467   -403  A    O  
ATOM   3335  CB  GLU A 439     108.217  85.537  78.240  1.00124.54      A    C  
ANISOU 3335  CB  GLU A 439    15947  19527  11846    146    240   -224  A    C  
ATOM   3336  CG  GLU A 439     108.378  87.050  78.162  1.00134.33      A    C  
ANISOU 3336  CG  GLU A 439    17220  20753  13064   -179    359   -540  A    C  
ATOM   3337  CD  GLU A 439     109.783  87.515  78.503  1.00145.01      A    C  
ANISOU 3337  CD  GLU A 439    18382  22554  14158   -405    296   -605  A    C  
ATOM   3338  OE1 GLU A 439     110.774  86.968  77.944  1.00135.89      A    O  
ANISOU 3338  OE1 GLU A 439    17081  21547  13000   -260    177   -450  A    O  
ATOM   3339  OE2 GLU A 439     109.890  88.433  79.346  1.00152.26      A    O1-
ANISOU 3339  OE2 GLU A 439    19292  23694  14863   -752    383   -824  A    O1-
ATOM   3340  N   PHE A 440     105.311  86.936  77.583  1.00105.09      A    N  
ANISOU 3340  N   PHE A 440    13877  16224   9824     51    583   -578  A    N  
ATOM   3341  CA  PHE A 440     104.246  87.852  77.945  1.00 98.64      A    C  
ANISOU 3341  CA  PHE A 440    13184  15216   9078    -90    767   -756  A    C  
ATOM   3342  C   PHE A 440     102.936  87.086  78.040  1.00102.98      A    C  
ANISOU 3342  C   PHE A 440    13815  15582   9729     79    774   -644  A    C  
ATOM   3343  O   PHE A 440     102.050  87.481  78.800  1.00110.65      A    O  
ANISOU 3343  O   PHE A 440    14866  16499  10677    -24    888   -736  A    O  
ATOM   3344  CB  PHE A 440     104.115  88.953  76.898  1.00 99.14      A    C  
ANISOU 3344  CB  PHE A 440    13303  14995   9370   -123    934   -890  A    C  
ATOM   3345  CG  PHE A 440     103.046  89.969  77.195  1.00100.46      A    C  
ANISOU 3345  CG  PHE A 440    13592  14926   9651   -228   1185  -1044  A    C  
ATOM   3346  CD1 PHE A 440     101.734  89.763  76.780  1.00 98.74      A    C  
ANISOU 3346  CD1 PHE A 440    13423  14462   9629    -46   1245   -950  A    C  
ATOM   3347  CD2 PHE A 440     103.356  91.144  77.859  1.00106.60      A    C  
ANISOU 3347  CD2 PHE A 440    14429  15733  10338   -527   1392  -1286  A    C  
ATOM   3348  CE1 PHE A 440     100.752  90.692  77.045  1.00 95.72      A    C  
ANISOU 3348  CE1 PHE A 440    13131  13869   9369   -109   1498  -1057  A    C  
ATOM   3349  CE2 PHE A 440     102.378  92.086  78.125  1.00106.87      A    C  
ANISOU 3349  CE2 PHE A 440    14592  15506  10507   -610   1682  -1424  A    C  
ATOM   3350  CZ  PHE A 440     101.076  91.855  77.715  1.00103.47      A    C  
ANISOU 3350  CZ  PHE A 440    14193  14828  10291   -375   1731  -1289  A    C  
ATOM   3351  N   LEU A 441     102.796  86.006  77.266  1.00100.00      A    N  
ANISOU 3351  N   LEU A 441    13425  15109   9461    309    677   -467  A    N  
ATOM   3352  CA  LEU A 441     101.569  85.199  77.302  1.00 92.89      A    C  
ANISOU 3352  CA  LEU A 441    12600  14053   8639    428    703   -382  A    C  
ATOM   3353  C   LEU A 441     101.534  84.242  78.495  1.00 97.19      A    C  
ANISOU 3353  C   LEU A 441    13164  14764   8997    455    651   -261  A    C  
ATOM   3354  O   LEU A 441     100.478  84.041  79.105  1.00108.46      A    O  
ANISOU 3354  O   LEU A 441    14675  16118  10416    437    719   -271  A    O  
ATOM   3355  CB  LEU A 441     101.361  84.448  75.989  1.00 85.64      A    C  
ANISOU 3355  CB  LEU A 441    11675  12972   7890    597    670   -283  A    C  
ATOM   3356  CG  LEU A 441     101.176  85.362  74.784  1.00 84.31      A    C  
ANISOU 3356  CG  LEU A 441    11475  12657   7901    595    729   -354  A    C  
ATOM   3357  CD1 LEU A 441     100.855  84.537  73.555  1.00 83.15      A    C  
ANISOU 3357  CD1 LEU A 441    11307  12420   7865    718    691   -258  A    C  
ATOM   3358  CD2 LEU A 441     100.066  86.370  74.999  1.00 87.85      A    C  
ANISOU 3358  CD2 LEU A 441    11960  12977   8438    527    884   -449  A    C  
ATOM   3359  N   LEU A 442     102.676  83.668  78.846  1.00 99.34      A    N  
ANISOU 3359  N   LEU A 442    13350  15277   9117    510    544   -122  A    N  
ATOM   3360  CA  LEU A 442     102.760  82.892  80.080  1.00108.25      A    C  
ANISOU 3360  CA  LEU A 442    14466  16621  10042    548    511     41  A    C  
ATOM   3361  C   LEU A 442     102.478  83.800  81.291  1.00110.68      A    C  
ANISOU 3361  C   LEU A 442    14777  17121  10153    303    548   -104  A    C  
ATOM   3362  O   LEU A 442     101.750  83.409  82.205  1.00111.03      A    O  
ANISOU 3362  O   LEU A 442    14888  17191  10105    294    587    -51  A    O  
ATOM   3363  CB  LEU A 442     104.125  82.210  80.194  1.00116.15      A    C  
ANISOU 3363  CB  LEU A 442    15322  17897  10912    679    403    263  A    C  
ATOM   3364  CG  LEU A 442     104.534  81.259  79.057  1.00115.56      A    C  
ANISOU 3364  CG  LEU A 442    15251  17634  11021    913    404    405  A    C  
ATOM   3365  CD1 LEU A 442     105.785  80.488  79.461  1.00121.10      A    C  
ANISOU 3365  CD1 LEU A 442    15800  18629  11580   1081    339    682  A    C  
ATOM   3366  CD2 LEU A 442     103.419  80.295  78.682  1.00116.97      A    C  
ANISOU 3366  CD2 LEU A 442    15598  17476  11370   1036    524    449  A    C  
ATOM   3367  N   ASP A 443     103.029  85.018  81.262  1.00112.16      A    N  
ANISOU 3367  N   ASP A 443    14911  17422  10282     80    568   -307  A    N  
ATOM   3368  CA  ASP A 443     102.761  86.059  82.274  1.00110.30      A    C  
ANISOU 3368  CA  ASP A 443    14705  17326   9878   -221    667   -522  A    C  
ATOM   3369  C   ASP A 443     101.313  86.566  82.220  1.00104.26      A    C  
ANISOU 3369  C   ASP A 443    14100  16209   9302   -258    846   -674  A    C  
ATOM   3370  O   ASP A 443     100.939  87.427  82.991  1.00104.88      A    O  
ANISOU 3370  O   ASP A 443    14235  16325   9289   -497    982   -868  A    O  
ATOM   3371  CB  ASP A 443     103.709  87.258  82.060  1.00109.65      A    C  
ANISOU 3371  CB  ASP A 443    14556  17378   9725   -476    715   -740  A    C  
ATOM   3372  CG  ASP A 443     104.523  87.595  83.287  1.00113.02      A    C  
ANISOU 3372  CG  ASP A 443    14863  18312   9767   -767    672   -801  A    C  
ATOM   3373  OD1 ASP A 443     103.959  87.638  84.396  1.00112.51      A    O  
ANISOU 3373  OD1 ASP A 443    14837  18388   9521   -912    719   -839  A    O  
ATOM   3374  OD2 ASP A 443     105.742  87.829  83.129  1.00119.08      A    O1-
ANISOU 3374  OD2 ASP A 443    15480  19373  10390   -874    592   -814  A    O1-
ATOM   3375  N   LEU A 444     100.522  86.072  81.275  1.00103.79      A    N  
ANISOU 3375  N   LEU A 444    14100  15834   9501    -39    863   -595  A    N  
ATOM   3376  CA  LEU A 444      99.155  86.538  81.105  1.00109.24      A    C  
ANISOU 3376  CA  LEU A 444    14892  16238  10376    -46   1025   -700  A    C  
ATOM   3377  C   LEU A 444      98.162  85.416  81.400  1.00119.32      A    C  
ANISOU 3377  C   LEU A 444    16227  17441  11664     89   1003   -563  A    C  
ATOM   3378  O   LEU A 444      97.155  85.659  82.071  1.00132.90      A    O  
ANISOU 3378  O   LEU A 444    18022  19095  13378      8   1117   -641  A    O  
ATOM   3379  CB  LEU A 444      98.934  87.109  79.699  1.00105.41      A    C  
ANISOU 3379  CB  LEU A 444    14394  15491  10163     51   1097   -736  A    C  
ATOM   3380  CG  LEU A 444      97.715  88.019  79.563  1.00104.27      A    C  
ANISOU 3380  CG  LEU A 444    14309  15107  10202     23   1315   -844  A    C  
ATOM   3381  CD1 LEU A 444      97.995  89.211  78.667  1.00107.94      A    C  
ANISOU 3381  CD1 LEU A 444    14757  15404  10847     12   1466   -927  A    C  
ATOM   3382  CD2 LEU A 444      96.534  87.234  79.032  1.00101.90      A    C  
ANISOU 3382  CD2 LEU A 444    14000  14682  10033    198   1295   -715  A    C  
ATOM   3383  N   GLU A 445      98.436  84.202  80.913  1.00118.65      A    N  
ANISOU 3383  N   GLU A 445    16126  17353  11603    278    893   -375  A    N  
ATOM   3384  CA  GLU A 445      97.622  83.032  81.270  1.00118.02      A    C  
ANISOU 3384  CA  GLU A 445    16124  17201  11514    377    913   -251  A    C  
ATOM   3385  C   GLU A 445      97.543  82.878  82.790  1.00120.08      A    C  
ANISOU 3385  C   GLU A 445    16424  17657  11543    286    924   -213  A    C  
ATOM   3386  O   GLU A 445      96.450  82.835  83.354  1.00124.48      A    O  
ANISOU 3386  O   GLU A 445    17068  18128  12100    230   1021   -264  A    O  
ATOM   3387  CB  GLU A 445      98.197  81.763  80.665  1.00117.87      A    C  
ANISOU 3387  CB  GLU A 445    16101  17154  11529    565    849    -61  A    C  
ATOM   3388  CG  GLU A 445      98.083  81.729  79.164  1.00126.93      A    C  
ANISOU 3388  CG  GLU A 445    17224  18120  12881    629    851    -99  A    C  
ATOM   3389  CD  GLU A 445      99.339  81.198  78.511  1.00140.34      A    C  
ANISOU 3389  CD  GLU A 445    18861  19873  14588    749    769     17  A    C  
ATOM   3390  OE1 GLU A 445     100.280  80.824  79.251  1.00136.89      A    O  
ANISOU 3390  OE1 GLU A 445    18384  19623  14002    807    713    155  A    O  
ATOM   3391  OE2 GLU A 445      99.388  81.171  77.256  1.00151.15      A    O1-
ANISOU 3391  OE2 GLU A 445    20203  21126  16100    786    763    -14  A    O1-
ATOM   3392  N   ALA A 446      98.705  82.811  83.446  1.00117.39      A    N  
ANISOU 3392  N   ALA A 446    15997  17619  10986    264    825   -112  A    N  
ATOM   3393  CA  ALA A 446      98.777  82.668  84.910  1.00108.87      A    C  
ANISOU 3393  CA  ALA A 446    14909  16825   9628    168    815    -36  A    C  
ATOM   3394  C   ALA A 446      98.093  83.827  85.608  1.00108.41      A    C  
ANISOU 3394  C   ALA A 446    14903  16784   9501   -104    922   -293  A    C  
ATOM   3395  O   ALA A 446      97.505  83.651  86.667  1.00109.16      A    O  
ANISOU 3395  O   ALA A 446    15056  16972   9446   -186    971   -278  A    O  
ATOM   3396  CB  ALA A 446     100.218  82.560  85.377  1.00110.29      A    C  
ANISOU 3396  CB  ALA A 446    14923  17420   9562    167    678    122  A    C  
ATOM   3397  N   LYS A 447      98.152  85.009  85.001  1.00109.48      A    N  
ANISOU 3397  N   LYS A 447    15030  16807   9759   -240    993   -525  A    N  
ATOM   3398  CA  LYS A 447      97.430  86.164  85.525  1.00111.59      A    C  
ANISOU 3398  CA  LYS A 447    15373  16998  10027   -482   1175   -785  A    C  
ATOM   3399  C   LYS A 447      95.953  86.167  85.150  1.00113.30      A    C  
ANISOU 3399  C   LYS A 447    15692  16864  10491   -391   1315   -833  A    C  
ATOM   3400  O   LYS A 447      95.262  87.151  85.375  1.00136.03      A    O  
ANISOU 3400  O   LYS A 447    18631  19608  13444   -537   1508  -1028  A    O  
ATOM   3401  CB  LYS A 447      98.082  87.460  85.066  1.00112.41      A    C  
ANISOU 3401  CB  LYS A 447    15447  17084  10178   -662   1268  -1004  A    C  
ATOM   3402  CG  LYS A 447      98.930  88.086  86.158  1.00120.32      A    C  
ANISOU 3402  CG  LYS A 447    16400  18474  10843   -993   1280  -1145  A    C  
ATOM   3403  CD  LYS A 447      99.931  89.097  85.630  1.00129.40      A    C  
ANISOU 3403  CD  LYS A 447    17499  19669  11995  -1172   1341  -1329  A    C  
ATOM   3404  CE  LYS A 447      99.242  90.180  84.814  1.00142.89      A    C  
ANISOU 3404  CE  LYS A 447    19331  20925  14036  -1183   1612  -1530  A    C  
ATOM   3405  NZ  LYS A 447     100.219  91.076  84.133  1.00149.11      A    N1+
ANISOU 3405  NZ  LYS A 447    20091  21689  14872  -1314   1698  -1678  A    N1+
ATOM   3406  N   GLU A 448      95.469  85.077  84.575  1.00106.37      A    N  
ANISOU 3406  N   GLU A 448    14827  15850   9738   -166   1248   -659  A    N  
ATOM   3407  CA  GLU A 448      94.056  84.940  84.289  1.00102.59      A    C  
ANISOU 3407  CA  GLU A 448    14410  15128   9439   -108   1363   -688  A    C  
ATOM   3408  C   GLU A 448      93.487  83.648  84.879  1.00 98.87      A    C  
ANISOU 3408  C   GLU A 448    14013  14673   8879    -33   1338   -541  A    C  
ATOM   3409  O   GLU A 448      92.277  83.555  85.077  1.00 88.20      A    O  
ANISOU 3409  O   GLU A 448    12720  13194   7594    -58   1449   -592  A    O  
ATOM   3410  CB  GLU A 448      93.823  85.006  82.763  1.00108.25      A    C  
ANISOU 3410  CB  GLU A 448    15065  15649  10417     42   1361   -665  A    C  
ATOM   3411  CG  GLU A 448      94.201  86.335  82.084  1.00102.69      A    C  
ANISOU 3411  CG  GLU A 448    14303  14864   9848     -0   1444   -786  A    C  
ATOM   3412  CD  GLU A 448      93.225  87.477  82.360  1.00 98.27      A    C  
ANISOU 3412  CD  GLU A 448    13777  14153   9406    -91   1684   -934  A    C  
ATOM   3413  OE1 GLU A 448      92.007  87.239  82.494  1.00 88.70      A    O  
ANISOU 3413  OE1 GLU A 448    12577  12857   8264    -52   1764   -915  A    O  
ATOM   3414  OE2 GLU A 448      93.682  88.631  82.431  1.00 97.56      A    O1-
ANISOU 3414  OE2 GLU A 448    13701  14019   9345   -208   1824  -1074  A    O1-
ATOM   3415  N   ARG A 449      94.347  82.652  85.127  1.00107.47      A    N  
ANISOU 3415  N   ARG A 449    15095  15907   9831     69   1221   -346  A    N  
ATOM   3416  CA  ARG A 449      93.932  81.391  85.769  1.00116.30      A    C  
ANISOU 3416  CA  ARG A 449    16306  17017  10862    156   1247   -173  A    C  
ATOM   3417  C   ARG A 449      93.438  81.719  87.171  1.00122.36      A    C  
ANISOU 3417  C   ARG A 449    17128  17927  11433     -6   1313   -225  A    C  
ATOM   3418  O   ARG A 449      92.311  81.385  87.533  1.00122.88      A    O  
ANISOU 3418  O   ARG A 449    17294  17862  11533    -34   1425   -256  A    O  
ATOM   3419  CB  ARG A 449      95.073  80.374  85.909  1.00116.31      A    C  
ANISOU 3419  CB  ARG A 449    16277  17165  10750    326   1157     93  A    C  
ATOM   3420  CG  ARG A 449      95.931  80.161  84.691  1.00118.60      A    C  
ANISOU 3420  CG  ARG A 449    16494  17391  11178    462   1081    147  A    C  
ATOM   3421  CD  ARG A 449      95.507  78.976  83.859  1.00128.28      A    C  
ANISOU 3421  CD  ARG A 449    17813  18351  12574    609   1170    233  A    C  
ATOM   3422  NE  ARG A 449      96.555  78.666  82.882  1.00140.14      A    N  
ANISOU 3422  NE  ARG A 449    19244  19841  14161    742   1103    320  A    N  
ATOM   3423  CZ  ARG A 449      96.424  77.802  81.884  1.00141.38      A    C  
ANISOU 3423  CZ  ARG A 449    19462  19780  14474    832   1184    347  A    C  
ATOM   3424  NH1 ARG A 449      95.284  77.133  81.731  1.00146.80      A    N1+
ANISOU 3424  NH1 ARG A 449    20279  20259  15237    784   1335    288  A    N1+
ATOM   3425  NH2 ARG A 449      97.435  77.605  81.038  1.00134.64      A    N  
ANISOU 3425  NH2 ARG A 449    18541  18928  13687    940   1128    414  A    N  
ATOM   3426  N   GLU A 450      94.288  82.385  87.952  1.00128.56      A    N  
ANISOU 3426  N   GLU A 450    17840  19010  11994   -144   1249   -250  A    N  
ATOM   3427  CA  GLU A 450      93.939  82.779  89.321  1.00134.74      A    C  
ANISOU 3427  CA  GLU A 450    18663  19993  12540   -351   1311   -319  A    C  
ATOM   3428  C   GLU A 450      92.835  83.842  89.371  1.00127.24      A    C  
ANISOU 3428  C   GLU A 450    17782  18847  11714   -537   1485   -611  A    C  
ATOM   3429  O   GLU A 450      92.109  83.952  90.354  1.00123.18      A    O  
ANISOU 3429  O   GLU A 450    17344  18375  11082   -676   1586   -679  A    O  
ATOM   3430  CB  GLU A 450      95.167  83.311  90.057  1.00140.18      A    C  
ANISOU 3430  CB  GLU A 450    19226  21115  12919   -517   1208   -307  A    C  
ATOM   3431  CG  GLU A 450      96.364  82.378  90.041  1.00145.91      A    C  
ANISOU 3431  CG  GLU A 450    19830  22099  13508   -316   1043     17  A    C  
ATOM   3432  CD  GLU A 450      97.351  82.708  91.145  1.00153.11      A    C  
ANISOU 3432  CD  GLU A 450    20589  23570  14015   -503    943     88  A    C  
ATOM   3433  OE1 GLU A 450      97.207  82.130  92.246  1.00158.58      A    O  
ANISOU 3433  OE1 GLU A 450    21277  24511  14463   -500    937    287  A    O  
ATOM   3434  OE2 GLU A 450      98.254  83.550  90.923  1.00151.73      A    O1-
ANISOU 3434  OE2 GLU A 450    20289  23611  13748   -675    880    -53  A    O1-
ATOM   3435  N   ARG A 451      92.720  84.621  88.302  1.00122.08      A    N  
ANISOU 3435  N   ARG A 451    17096  17978  11308   -521   1538   -760  A    N  
ATOM   3436  CA  ARG A 451      91.712  85.668  88.195  1.00110.22      A    C  
ANISOU 3436  CA  ARG A 451    15639  16262   9978   -633   1744   -988  A    C  
ATOM   3437  C   ARG A 451      90.307  85.100  87.820  1.00105.86      A    C  
ANISOU 3437  C   ARG A 451    15129  15472   9618   -504   1825   -946  A    C  
ATOM   3438  O   ARG A 451      89.281  85.767  87.977  1.00 95.44      A    O  
ANISOU 3438  O   ARG A 451    13837  14014   8411   -577   2008  -1085  A    O  
ATOM   3439  CB  ARG A 451      92.196  86.691  87.158  1.00105.46      A    C  
ANISOU 3439  CB  ARG A 451    14970  15534   9566   -625   1794  -1102  A    C  
ATOM   3440  CG  ARG A 451      91.660  88.085  87.367  1.00105.82      A    C  
ANISOU 3440  CG  ARG A 451    15063  15429   9714   -801   2064  -1347  A    C  
ATOM   3441  CD  ARG A 451      92.136  89.046  86.300  1.00103.13      A    C  
ANISOU 3441  CD  ARG A 451    14673  14925   9586   -760   2154  -1420  A    C  
ATOM   3442  NE  ARG A 451      91.050  89.924  85.882  1.00106.94      A    N  
ANISOU 3442  NE  ARG A 451    15175  15111  10346   -707   2430  -1500  A    N  
ATOM   3443  CZ  ARG A 451      91.000  90.560  84.716  1.00111.28      A    C  
ANISOU 3443  CZ  ARG A 451    15661  15453  11165   -552   2533  -1463  A    C  
ATOM   3444  NH1 ARG A 451      91.992  90.445  83.834  1.00111.04      A    N1+
ANISOU 3444  NH1 ARG A 451    15563  15467  11159   -465   2378  -1384  A    N1+
ATOM   3445  NH2 ARG A 451      89.951  91.325  84.434  1.00114.89      A    N  
ANISOU 3445  NH2 ARG A 451    16110  15672  11867   -470   2808  -1481  A    N  
ATOM   3446  N   THR A 452      90.270  83.868  87.321  1.00102.32      A    N  
ANISOU 3446  N   THR A 452    14681  14987   9205   -329   1714   -763  A    N  
ATOM   3447  CA  THR A 452      89.020  83.237  86.955  1.00 99.12      A    C  
ANISOU 3447  CA  THR A 452    14307  14415   8939   -261   1792   -741  A    C  
ATOM   3448  C   THR A 452      88.815  81.906  87.663  1.00100.46      A    C  
ANISOU 3448  C   THR A 452    14587  14618   8965   -231   1780   -597  A    C  
ATOM   3449  O   THR A 452      87.714  81.379  87.652  1.00103.70      A    O  
ANISOU 3449  O   THR A 452    15049  14913   9435   -243   1879   -613  A    O  
ATOM   3450  CB  THR A 452      88.931  83.011  85.419  1.00104.89      A    C  
ANISOU 3450  CB  THR A 452    14941  15024   9885   -117   1744   -696  A    C  
ATOM   3451  CG2 THR A 452      89.092  84.324  84.657  1.00108.61      A    C  
ANISOU 3451  CG2 THR A 452    15302  15442  10519   -109   1786   -792  A    C  
ATOM   3452  OG1 THR A 452      89.931  82.082  84.976  1.00 94.24      A    O  
ANISOU 3452  OG1 THR A 452    13600  13716   8491     -4   1608   -548  A    O  
ATOM   3453  N   GLY A 453      89.857  81.358  88.277  1.00107.18      A    N  
ANISOU 3453  N   GLY A 453    15465  15637   9622   -190   1681   -439  A    N  
ATOM   3454  CA  GLY A 453      89.769  80.039  88.920  1.00115.51      A    C  
ANISOU 3454  CA  GLY A 453    16632  16698  10558   -109   1710   -239  A    C  
ATOM   3455  C   GLY A 453      89.619  78.904  87.914  1.00121.95      A    C  
ANISOU 3455  C   GLY A 453    17493  17305  11536     40   1747   -141  A    C  
ATOM   3456  O   GLY A 453      89.042  77.865  88.235  1.00139.41      A    O  
ANISOU 3456  O   GLY A 453    19836  19401  13733     66   1871    -55  A    O  
ATOM   3457  N   LEU A 454      90.129  79.103  86.698  1.00119.57      A    N  
ANISOU 3457  N   LEU A 454    17098  16950  11381    112   1666   -170  A    N  
ATOM   3458  CA  LEU A 454      89.996  78.129  85.623  1.00117.96      A    C  
ANISOU 3458  CA  LEU A 454    16928  16567  11321    199   1715   -127  A    C  
ATOM   3459  C   LEU A 454      91.367  77.770  85.048  1.00128.93      A    C  
ANISOU 3459  C   LEU A 454    18272  17994  12723    356   1616     23  A    C  
ATOM   3460  O   LEU A 454      92.045  78.624  84.458  1.00131.34      A    O  
ANISOU 3460  O   LEU A 454    18446  18385  13071    364   1487    -34  A    O  
ATOM   3461  CB  LEU A 454      89.115  78.697  84.506  1.00112.99      A    C  
ANISOU 3461  CB  LEU A 454    16202  15863  10865    117   1731   -311  A    C  
ATOM   3462  CG  LEU A 454      87.785  79.346  84.907  1.00115.60      A    C  
ANISOU 3462  CG  LEU A 454    16511  16193  11217    -19   1822   -460  A    C  
ATOM   3463  CD1 LEU A 454      87.046  79.908  83.698  1.00114.35      A    C  
ANISOU 3463  CD1 LEU A 454    16196  16026  11223    -47   1828   -564  A    C  
ATOM   3464  CD2 LEU A 454      86.889  78.362  85.652  1.00124.18      A    C  
ANISOU 3464  CD2 LEU A 454    17750  17203  12229    -92   1973   -445  A    C  
ATOM   3465  N   SER A 455      91.774  76.511  85.224  1.00132.82      A    N  
ANISOU 3465  N   SER A 455    18875  18402  13187    488   1709    222  A    N  
ATOM   3466  CA  SER A 455      92.958  75.978  84.533  1.00131.62      A    C  
ANISOU 3466  CA  SER A 455    18690  18232  13087    658   1669    372  A    C  
ATOM   3467  C   SER A 455      92.569  75.452  83.152  1.00145.93      A    C  
ANISOU 3467  C   SER A 455    20538  19828  15081    622   1760    254  A    C  
ATOM   3468  O   SER A 455      93.366  74.791  82.472  1.00126.14      A    O  
ANISOU 3468  O   SER A 455    18047  17236  12644    742   1796    352  A    O  
ATOM   3469  CB  SER A 455      93.596  74.859  85.334  1.00124.21      A    C  
ANISOU 3469  CB  SER A 455    17848  17288  12056    848   1783    678  A    C  
ATOM   3470  OG  SER A 455      94.127  75.377  86.521  1.00120.00      A    O  
ANISOU 3470  OG  SER A 455    17226  17057  11309    871   1663    815  A    O  
ATOM   3471  N   THR A 456      91.327  75.742  82.761  1.00166.66      A    N  
ANISOU 3471  N   THR A 456    23161  22395  17766    446   1807     46  A    N  
ATOM   3472  CA  THR A 456      90.824  75.444  81.418  1.00177.76      A    C  
ANISOU 3472  CA  THR A 456    24544  23706  19291    346   1863    -95  A    C  
ATOM   3473  C   THR A 456      90.651  76.746  80.608  1.00177.18      A    C  
ANISOU 3473  C   THR A 456    24261  23777  19282    288   1692   -226  A    C  
ATOM   3474  O   THR A 456      89.578  77.012  80.040  1.00165.37      A    O  
ANISOU 3474  O   THR A 456    22687  22317  17829    154   1724   -357  A    O  
ATOM   3475  CB  THR A 456      89.504  74.642  81.475  1.00180.97      A    C  
ANISOU 3475  CB  THR A 456    25075  23990  19693    173   2078   -206  A    C  
ATOM   3476  CG2 THR A 456      88.565  75.208  82.538  1.00173.84      A    C  
ANISOU 3476  CG2 THR A 456    24173  23159  18718     93   2082   -257  A    C  
ATOM   3477  OG1 THR A 456      88.863  74.657  80.188  1.00178.60      A    O  
ANISOU 3477  OG1 THR A 456    24676  23727  19456     11   2090   -373  A    O  
ATOM   3478  N   LEU A 457      91.719  77.553  80.594  1.00169.51      A    N  
ANISOU 3478  N   LEU A 457    23191  22904  18310    395   1534   -169  A    N  
ATOM   3479  CA  LEU A 457      91.858  78.684  79.673  1.00146.95      A    C  
ANISOU 3479  CA  LEU A 457    20161  20132  15541    384   1412   -250  A    C  
ATOM   3480  C   LEU A 457      93.320  78.886  79.261  1.00135.95      A    C  
ANISOU 3480  C   LEU A 457    18712  18783  14157    502   1290   -168  A    C  
ATOM   3481  O   LEU A 457      94.235  78.896  80.095  1.00116.72      A    O  
ANISOU 3481  O   LEU A 457    16300  16421  11625    577   1239    -68  A    O  
ATOM   3482  CB  LEU A 457      91.283  79.979  80.262  1.00138.73      A    C  
ANISOU 3482  CB  LEU A 457    19046  19164  14499    326   1396   -337  A    C  
ATOM   3483  CG  LEU A 457      91.915  80.631  81.495  1.00134.00      A    C  
ANISOU 3483  CG  LEU A 457    18479  18649  13786    324   1357   -323  A    C  
ATOM   3484  CD1 LEU A 457      93.200  81.387  81.208  1.00129.33      A    C  
ANISOU 3484  CD1 LEU A 457    17801  18145  13192    371   1242   -310  A    C  
ATOM   3485  CD2 LEU A 457      90.889  81.590  82.058  1.00143.07      A    C  
ANISOU 3485  CD2 LEU A 457    19607  19799  14953    219   1444   -446  A    C  
ATOM   3486  N   LYS A 458      93.524  79.031  77.955  1.00130.62      A    N  
ANISOU 3486  N   LYS A 458    17944  18105  13581    508   1244   -202  A    N  
ATOM   3487  CA  LYS A 458      94.847  79.273  77.389  1.00127.76      A    C  
ANISOU 3487  CA  LYS A 458    17517  17782  13243    605   1135   -144  A    C  
ATOM   3488  C   LYS A 458      94.681  80.322  76.311  1.00119.19      A    C  
ANISOU 3488  C   LYS A 458    16283  16741  12260    576   1074   -219  A    C  
ATOM   3489  O   LYS A 458      93.625  80.407  75.678  1.00132.93      A    O  
ANISOU 3489  O   LYS A 458    17962  18493  14050    506   1120   -270  A    O  
ATOM   3490  CB  LYS A 458      95.419  77.970  76.796  1.00128.23      A    C  
ANISOU 3490  CB  LYS A 458    17655  17745  13321    667   1198    -67  A    C  
ATOM   3491  CG  LYS A 458      96.907  77.994  76.458  1.00127.24      A    C  
ANISOU 3491  CG  LYS A 458    17477  17662  13206    794   1107     30  A    C  
ATOM   3492  CD  LYS A 458      97.754  78.311  77.681  1.00133.78      A    C  
ANISOU 3492  CD  LYS A 458    18284  18626  13916    879   1033    145  A    C  
ATOM   3493  CE  LYS A 458      99.235  77.974  77.509  1.00129.26      A    C  
ANISOU 3493  CE  LYS A 458    17657  18131  13326   1026    975    292  A    C  
ATOM   3494  NZ  LYS A 458      99.519  76.556  77.857  1.00132.46      A    N1+
ANISOU 3494  NZ  LYS A 458    18173  18431  13726   1176   1125    485  A    N1+
ATOM   3495  N   VAL A 459      95.712  81.124  76.095  1.00103.43      A    N  
ANISOU 3495  N   VAL A 459    14216  14795  10285    630    983   -207  A    N  
ATOM   3496  CA  VAL A 459      95.649  82.132  75.034  1.00 96.47      A    C  
ANISOU 3496  CA  VAL A 459    13206  13932   9515    631    956   -243  A    C  
ATOM   3497  C   VAL A 459      95.850  81.449  73.681  1.00 89.32      A    C  
ANISOU 3497  C   VAL A 459    12253  13031   8653    648    926   -209  A    C  
ATOM   3498  O   VAL A 459      96.881  80.821  73.444  1.00 84.11      A    O  
ANISOU 3498  O   VAL A 459    11630  12354   7972    698    884   -167  A    O  
ATOM   3499  CB  VAL A 459      96.713  83.225  75.244  1.00 94.20      A    C  
ANISOU 3499  CB  VAL A 459    12881  13675   9233    648    909   -268  A    C  
ATOM   3500  CG1 VAL A 459      96.564  84.322  74.212  1.00 90.86      A    C  
ANISOU 3500  CG1 VAL A 459    12350  13224   8948    669    940   -282  A    C  
ATOM   3501  CG2 VAL A 459      96.598  83.813  76.634  1.00 97.14      A    C  
ANISOU 3501  CG2 VAL A 459    13312  14078   9517    571    960   -333  A    C  
ATOM   3502  N   GLU A 460      94.862  81.546  72.799  1.00 87.32      A    N  
ANISOU 3502  N   GLU A 460    11900  12832   8443    596    956   -218  A    N  
ATOM   3503  CA  GLU A 460      94.967  80.882  71.501  1.00 89.19      A    C  
ANISOU 3503  CA  GLU A 460    12082  13129   8678    554    937   -207  A    C  
ATOM   3504  C   GLU A 460      95.107  81.876  70.325  1.00 86.10      A    C  
ANISOU 3504  C   GLU A 460    11514  12839   8360    599    879   -151  A    C  
ATOM   3505  O   GLU A 460      95.081  83.098  70.504  1.00 85.58      A    O  
ANISOU 3505  O   GLU A 460    11381  12758   8375    678    889   -115  A    O  
ATOM   3506  CB  GLU A 460      93.794  79.921  71.321  1.00 88.17      A    C  
ANISOU 3506  CB  GLU A 460    11968  13055   8477    406   1028   -259  A    C  
ATOM   3507  CG  GLU A 460      93.818  78.753  72.302  1.00 89.73      A    C  
ANISOU 3507  CG  GLU A 460    12372  13105   8615    369   1132   -298  A    C  
ATOM   3508  CD  GLU A 460      92.839  77.632  71.953  1.00 97.45      A    C  
ANISOU 3508  CD  GLU A 460    13401  14105   9519    172   1274   -387  A    C  
ATOM   3509  OE1 GLU A 460      92.535  76.821  72.848  1.00104.74      A    O  
ANISOU 3509  OE1 GLU A 460    14495  14894  10406    135   1404   -415  A    O  
ATOM   3510  OE2 GLU A 460      92.383  77.526  70.794  1.00 99.05      A    O1-
ANISOU 3510  OE2 GLU A 460    13477  14474   9681     33   1273   -433  A    O1-
ATOM   3511  N   PHE A 461      95.298  81.350  69.128  1.00 79.74      A    N  
ANISOU 3511  N   PHE A 461    10645  12125   7528    545    851   -139  A    N  
ATOM   3512  CA  PHE A 461      95.438  82.213  67.974  1.00 81.84      A    C  
ANISOU 3512  CA  PHE A 461    10737  12512   7845    596    800    -51  A    C  
ATOM   3513  C   PHE A 461      94.877  81.557  66.742  1.00 83.60      A    C  
ANISOU 3513  C   PHE A 461    10836  12956   7971    456    794    -41  A    C  
ATOM   3514  O   PHE A 461      95.043  80.366  66.555  1.00101.32      A    O  
ANISOU 3514  O   PHE A 461    13182  15184  10130    319    830   -140  A    O  
ATOM   3515  CB  PHE A 461      96.907  82.510  67.727  1.00 79.09      A    C  
ANISOU 3515  CB  PHE A 461    10436  12064   7551    682    738    -44  A    C  
ATOM   3516  CG  PHE A 461      97.145  83.470  66.596  1.00 80.11      A    C  
ANISOU 3516  CG  PHE A 461    10410  12282   7746    748    708     57  A    C  
ATOM   3517  CD1 PHE A 461      97.307  83.009  65.301  1.00 81.15      A    C  
ANISOU 3517  CD1 PHE A 461    10451  12561   7821    684    665     91  A    C  
ATOM   3518  CD2 PHE A 461      97.203  84.842  66.827  1.00 82.23      A    C  
ANISOU 3518  CD2 PHE A 461    10635  12476   8130    863    759    119  A    C  
ATOM   3519  CE1 PHE A 461      97.539  83.893  64.257  1.00 80.78      A    C  
ANISOU 3519  CE1 PHE A 461    10255  12611   7823    758    642    216  A    C  
ATOM   3520  CE2 PHE A 461      97.418  85.733  65.789  1.00 78.95      A    C  
ANISOU 3520  CE2 PHE A 461    10093  12111   7792    948    776    243  A    C  
ATOM   3521  CZ  PHE A 461      97.591  85.253  64.504  1.00 79.81      A    C  
ANISOU 3521  CZ  PHE A 461    10096  12392   7836    907    702    307  A    C  
ATOM   3522  N   ASN A 462      94.212  82.321  65.897  1.00 79.97      A    N  
ANISOU 3522  N   ASN A 462    10152  12719   7514    479    775     86  A    N  
ATOM   3523  CA  ASN A 462      93.978  81.848  64.557  1.00 83.36      A    C  
ANISOU 3523  CA  ASN A 462    10426  13428   7817    338    740    117  A    C  
ATOM   3524  C   ASN A 462      94.079  83.003  63.569  1.00 76.33      A    C  
ANISOU 3524  C   ASN A 462     9316  12703   6983    482    693    326  A    C  
ATOM   3525  O   ASN A 462      94.045  84.156  63.947  1.00 66.82      A    O  
ANISOU 3525  O   ASN A 462     8073  11388   5925    682    732    446  A    O  
ATOM   3526  CB  ASN A 462      92.673  81.042  64.448  1.00 88.04      A    C  
ANISOU 3526  CB  ASN A 462    10929  14276   8243    110    790     56  A    C  
ATOM   3527  CG  ASN A 462      91.459  81.908  64.450  1.00 88.77      A    C  
ANISOU 3527  CG  ASN A 462    10777  14610   8340    184    797    221  A    C  
ATOM   3528  ND2 ASN A 462      90.660  81.758  65.488  1.00 95.77      A    N  
ANISOU 3528  ND2 ASN A 462    11729  15424   9236    158    868    156  A    N  
ATOM   3529  OD1 ASN A 462      91.223  82.683  63.525  1.00 83.80      A    O  
ANISOU 3529  OD1 ASN A 462     9893  14240   7704    274    757    427  A    O  
ATOM   3530  N   ARG A 463      94.258  82.655  62.304  1.00 75.25      A    N  
ANISOU 3530  N   ARG A 463     9052  12811   6727    370    640    364  A    N  
ATOM   3531  CA  ARG A 463      94.613  83.631  61.307  1.00 74.66      A    C  
ANISOU 3531  CA  ARG A 463     8801  12865   6701    516    600    574  A    C  
ATOM   3532  C   ARG A 463      93.511  84.677  61.135  1.00 76.19      A    C  
ANISOU 3532  C   ARG A 463     8731  13282   6934    673    645    840  A    C  
ATOM   3533  O   ARG A 463      93.771  85.824  60.789  1.00 69.36      A    O  
ANISOU 3533  O   ARG A 463     7777  12368   6210    901    690   1049  A    O  
ATOM   3534  CB  ARG A 463      94.841  82.900  59.983  1.00 77.33      A    C  
ANISOU 3534  CB  ARG A 463     9034  13496   6850    310    539    555  A    C  
ATOM   3535  CG  ARG A 463      96.128  82.097  59.889  1.00 73.76      A    C  
ANISOU 3535  CG  ARG A 463     8815  12806   6405    220    531    356  A    C  
ATOM   3536  CD  ARG A 463      96.457  81.866  58.429  1.00 72.22      A    C  
ANISOU 3536  CD  ARG A 463     8479  12897   6061     80    483    399  A    C  
ATOM   3537  NE  ARG A 463      97.639  81.062  58.222  1.00 72.03      A    N  
ANISOU 3537  NE  ARG A 463     8660  12664   6044    -14    505    214  A    N  
ATOM   3538  CZ  ARG A 463      98.881  81.529  58.164  1.00 71.02      A    C  
ANISOU 3538  CZ  ARG A 463     8624  12301   6058    152    477    237  A    C  
ATOM   3539  NH1 ARG A 463      99.136  82.819  58.310  1.00 65.39      A    N1+
ANISOU 3539  NH1 ARG A 463     7848  11501   5495    398    443    410  A    N1+
ATOM   3540  NH2 ARG A 463      99.871  80.663  57.951  1.00 75.31      A    N  
ANISOU 3540  NH2 ARG A 463     9331  12690   6593     57    516     75  A    N  
ATOM   3541  N   VAL A 464      92.273  84.234  61.360  1.00 80.80      A    N  
ANISOU 3541  N   VAL A 464     9189  14115   7395    548    661    836  A    N  
ATOM   3542  CA  VAL A 464      91.069  85.011  61.069  1.00 83.30      A    C  
ANISOU 3542  CA  VAL A 464     9189  14758   7701    672    705   1116  A    C  
ATOM   3543  C   VAL A 464      90.767  85.997  62.188  1.00 82.50      A    C  
ANISOU 3543  C   VAL A 464     9166  14341   7837    921    839   1181  A    C  
ATOM   3544  O   VAL A 464      90.514  87.155  61.943  1.00 80.81      A    O  
ANISOU 3544  O   VAL A 464     8795  14140   7767   1179    941   1454  A    O  
ATOM   3545  CB  VAL A 464      89.851  84.066  60.896  1.00 89.38      A    C  
ANISOU 3545  CB  VAL A 464     9780  15966   8214    388    674   1055  A    C  
ATOM   3546  CG1 VAL A 464      88.563  84.843  60.698  1.00 90.09      A    C  
ANISOU 3546  CG1 VAL A 464     9506  16438   8286    533    719   1368  A    C  
ATOM   3547  CG2 VAL A 464      90.067  83.060  59.754  1.00 91.99      A    C  
ANISOU 3547  CG2 VAL A 464    10032  16647   8272     67    585    951  A    C  
ATOM   3548  N   HIS A 465      90.795  85.509  63.424  1.00 88.71      A    N  
ANISOU 3548  N   HIS A 465    10207  14837   8661    836    868    932  A    N  
ATOM   3549  CA  HIS A 465      90.377  86.280  64.617  1.00 90.26      A    C  
ANISOU 3549  CA  HIS A 465    10493  14766   9034    994   1006    937  A    C  
ATOM   3550  C   HIS A 465      91.522  86.987  65.349  1.00 85.85      A    C  
ANISOU 3550  C   HIS A 465    10197  13754   8667   1121   1077    837  A    C  
ATOM   3551  O   HIS A 465      91.314  87.971  66.021  1.00 85.29      A    O  
ANISOU 3551  O   HIS A 465    10166  13476   8763   1273   1238    886  A    O  
ATOM   3552  CB  HIS A 465      89.667  85.337  65.604  1.00 90.72      A    C  
ANISOU 3552  CB  HIS A 465    10663  14813   8989    802   1006    728  A    C  
ATOM   3553  CG  HIS A 465      88.415  84.725  65.055  1.00 99.67      A    C  
ANISOU 3553  CG  HIS A 465    11538  16405   9926    635    977    792  A    C  
ATOM   3554  CD2 HIS A 465      88.205  83.582  64.355  1.00103.36      A    C  
ANISOU 3554  CD2 HIS A 465    11937  17180  10154    348    892    686  A    C  
ATOM   3555  ND1 HIS A 465      87.180  85.319  65.196  1.00107.33      A    N  
ANISOU 3555  ND1 HIS A 465    12267  17592  10920    735   1064    977  A    N  
ATOM   3556  CE1 HIS A 465      86.260  84.561  64.623  1.00114.11      A    C  
ANISOU 3556  CE1 HIS A 465    12897  18916  11544    510   1007    987  A    C  
ATOM   3557  NE2 HIS A 465      86.857  83.506  64.096  1.00112.89      A    N  
ANISOU 3557  NE2 HIS A 465    12852  18821  11219    251    910    796  A    N  
ATOM   3558  N   GLY A 466      92.733  86.455  65.222  1.00 90.10      A    N  
ANISOU 3558  N   GLY A 466    10909  14158   9167   1034    975    684  A    N  
ATOM   3559  CA  GLY A 466      93.906  86.961  65.927  1.00 83.38      A    C  
ANISOU 3559  CA  GLY A 466    10284  12958   8435   1093   1014    562  A    C  
ATOM   3560  C   GLY A 466      93.978  86.302  67.277  1.00 78.86      A    C  
ANISOU 3560  C   GLY A 466     9924  12225   7814    981   1002    348  A    C  
ATOM   3561  O   GLY A 466      93.525  85.170  67.455  1.00 77.26      A    O  
ANISOU 3561  O   GLY A 466     9747  12127   7479    842    938    263  A    O  
ATOM   3562  N   PHE A 467      94.565  86.999  68.239  1.00 78.40      A    N  
ANISOU 3562  N   PHE A 467    10020  11921   7844   1020   1083    257  A    N  
ATOM   3563  CA  PHE A 467      94.681  86.439  69.580  1.00 74.50      A    C  
ANISOU 3563  CA  PHE A 467     9708  11319   7279    921   1069     86  A    C  
ATOM   3564  C   PHE A 467      93.328  86.508  70.267  1.00 75.15      A    C  
ANISOU 3564  C   PHE A 467     9757  11430   7364    909   1167     94  A    C  
ATOM   3565  O   PHE A 467      92.513  87.406  69.989  1.00 76.31      A    O  
ANISOU 3565  O   PHE A 467     9769  11603   7622   1013   1298    219  A    O  
ATOM   3566  CB  PHE A 467      95.729  87.185  70.397  1.00 72.14      A    C  
ANISOU 3566  CB  PHE A 467     9553  10835   7023    916   1122    -22  A    C  
ATOM   3567  CG  PHE A 467      97.157  86.954  69.941  1.00 70.04      A    C  
ANISOU 3567  CG  PHE A 467     9327  10563   6722    902   1012    -56  A    C  
ATOM   3568  CD1 PHE A 467      97.856  85.819  70.321  1.00 66.48      A    C  
ANISOU 3568  CD1 PHE A 467     8960  10151   6146    841    882   -120  A    C  
ATOM   3569  CD2 PHE A 467      97.815  87.894  69.161  1.00 69.20      A    C  
ANISOU 3569  CD2 PHE A 467     9174  10399   6719    963   1068     -8  A    C  
ATOM   3570  CE1 PHE A 467      99.168  85.627  69.928  1.00 64.57      A    C  
ANISOU 3570  CE1 PHE A 467     8734   9919   5879    845    797   -134  A    C  
ATOM   3571  CE2 PHE A 467      99.133  87.694  68.765  1.00 65.70      A    C  
ANISOU 3571  CE2 PHE A 467     8760   9962   6240    939    970    -48  A    C  
ATOM   3572  CZ  PHE A 467      99.801  86.561  69.146  1.00 63.74      A    C  
ANISOU 3572  CZ  PHE A 467     8573   9778   5863    882    828   -110  A    C  
ATOM   3573  N   TYR A 468      93.089  85.533  71.138  1.00 76.19      A    N  
ANISOU 3573  N   TYR A 468    10005  11559   7382    797   1125    -18  A    N  
ATOM   3574  CA  TYR A 468      91.841  85.449  71.882  1.00 76.72      A    C  
ANISOU 3574  CA  TYR A 468    10064  11655   7431    757   1211    -36  A    C  
ATOM   3575  C   TYR A 468      91.984  84.575  73.103  1.00 78.94      A    C  
ANISOU 3575  C   TYR A 468    10538  11854   7598    651   1189   -169  A    C  
ATOM   3576  O   TYR A 468      93.012  83.886  73.274  1.00 72.55      A    O  
ANISOU 3576  O   TYR A 468     9847  10999   6717    626   1101   -212  A    O  
ATOM   3577  CB  TYR A 468      90.719  84.903  70.993  1.00 77.08      A    C  
ANISOU 3577  CB  TYR A 468     9918  11946   7420    714   1192     55  A    C  
ATOM   3578  CG  TYR A 468      90.890  83.500  70.464  1.00 76.78      A    C  
ANISOU 3578  CG  TYR A 468     9915  12022   7236    564   1092     -9  A    C  
ATOM   3579  CD1 TYR A 468      90.641  82.405  71.257  1.00 78.31      A    C  
ANISOU 3579  CD1 TYR A 468    10269  12157   7328    431   1112   -135  A    C  
ATOM   3580  CD2 TYR A 468      91.247  83.275  69.145  1.00 81.08      A    C  
ANISOU 3580  CD2 TYR A 468    10336  12727   7743    543   1014     57  A    C  
ATOM   3581  CE1 TYR A 468      90.775  81.120  70.769  1.00 83.07      A    C  
ANISOU 3581  CE1 TYR A 468    10934  12809   7817    281   1097   -207  A    C  
ATOM   3582  CE2 TYR A 468      91.373  81.993  68.645  1.00 85.33      A    C  
ANISOU 3582  CE2 TYR A 468    10923  13350   8146    369    977    -34  A    C  
ATOM   3583  CZ  TYR A 468      91.130  80.921  69.463  1.00 85.92      A    C  
ANISOU 3583  CZ  TYR A 468    11180  13320   8143    237   1037   -172  A    C  
ATOM   3584  OH  TYR A 468      91.248  79.640  68.976  1.00 94.40      A    O  
ANISOU 3584  OH  TYR A 468    12338  14423   9104     52   1073   -276  A    O  
ATOM   3585  N   ILE A 469      90.947  84.605  73.945  1.00 86.48      A    N  
ANISOU 3585  N   ILE A 469    11513  12803   8540    608   1283   -205  A    N  
ATOM   3586  CA  ILE A 469      90.803  83.649  75.061  1.00 98.40      A    C  
ANISOU 3586  CA  ILE A 469    13192  14267   9927    505   1281   -297  A    C  
ATOM   3587  C   ILE A 469      89.398  83.069  75.049  1.00 99.98      A    C  
ANISOU 3587  C   ILE A 469    13329  14572  10083    418   1345   -302  A    C  
ATOM   3588  O   ILE A 469      88.445  83.827  74.979  1.00 90.22      A    O  
ANISOU 3588  O   ILE A 469    11957  13402   8919    450   1431   -260  A    O  
ATOM   3589  CB  ILE A 469      91.033  84.297  76.439  1.00103.44      A    C  
ANISOU 3589  CB  ILE A 469    13956  14795  10550    490   1350   -374  A    C  
ATOM   3590  CG1 ILE A 469      92.184  85.301  76.379  1.00109.04      A    C  
ANISOU 3590  CG1 ILE A 469    14673  15441  11313    535   1343   -392  A    C  
ATOM   3591  CG2 ILE A 469      91.345  83.227  77.471  1.00107.57      A    C  
ANISOU 3591  CG2 ILE A 469    14649  15298  10923    422   1312   -411  A    C  
ATOM   3592  CD1 ILE A 469      92.302  86.189  77.599  1.00106.80      A    C  
ANISOU 3592  CD1 ILE A 469    14486  15087  11006    461   1459   -502  A    C  
ATOM   3593  N   GLU A 470      89.274  81.738  75.105  1.00110.68      A    N  
ANISOU 3593  N   GLU A 470    14784  15941  11328    305   1334   -350  A    N  
ATOM   3594  CA  GLU A 470      87.963  81.077  75.024  1.00116.71      A    C  
ANISOU 3594  CA  GLU A 470    15493  16828  12022    163   1412   -390  A    C  
ATOM   3595  C   GLU A 470      87.562  80.355  76.319  1.00118.46      A    C  
ANISOU 3595  C   GLU A 470    15914  16927  12165     76   1504   -471  A    C  
ATOM   3596  O   GLU A 470      88.395  79.783  77.033  1.00110.82      A    O  
ANISOU 3596  O   GLU A 470    15143  15808  11155    104   1502   -476  A    O  
ATOM   3597  CB  GLU A 470      87.900  80.118  73.812  1.00121.65      A    C  
ANISOU 3597  CB  GLU A 470    16052  17599  12569     31   1389   -407  A    C  
ATOM   3598  CG  GLU A 470      88.364  78.683  74.056  1.00130.69      A    C  
ANISOU 3598  CG  GLU A 470    17430  18595  13630    -82   1455   -497  A    C  
ATOM   3599  CD  GLU A 470      88.229  77.805  72.814  1.00134.69      A    C  
ANISOU 3599  CD  GLU A 470    17879  19244  14053   -269   1488   -559  A    C  
ATOM   3600  OE1 GLU A 470      89.076  76.900  72.622  1.00138.69      A    O  
ANISOU 3600  OE1 GLU A 470    18554  19594  14546   -295   1540   -598  A    O  
ATOM   3601  OE2 GLU A 470      87.282  78.019  72.025  1.00122.35      A    O1-
ANISOU 3601  OE2 GLU A 470    16089  17972  12425   -398   1477   -562  A    O1-
ATOM   3602  N   LEU A 471      86.265  80.386  76.605  1.00123.46      A    N  
ANISOU 3602  N   LEU A 471    16476  17656  12775    -18   1596   -508  A    N  
ATOM   3603  CA  LEU A 471      85.724  79.767  77.799  1.00133.73      A    C  
ANISOU 3603  CA  LEU A 471    17954  18856  14001   -112   1703   -582  A    C  
ATOM   3604  C   LEU A 471      84.427  79.063  77.458  1.00151.22      A    C  
ANISOU 3604  C   LEU A 471    20090  21227  16137   -312   1802   -654  A    C  
ATOM   3605  O   LEU A 471      83.668  79.540  76.613  1.00157.78      A    O  
ANISOU 3605  O   LEU A 471    20664  22304  16980   -344   1784   -619  A    O  
ATOM   3606  CB  LEU A 471      85.456  80.829  78.842  1.00126.00      A    C  
ANISOU 3606  CB  LEU A 471    16980  17817  13074    -34   1742   -581  A    C  
ATOM   3607  CG  LEU A 471      86.636  81.761  79.094  1.00123.51      A    C  
ANISOU 3607  CG  LEU A 471    16699  17409  12821    105   1670   -544  A    C  
ATOM   3608  CD1 LEU A 471      86.132  83.030  79.749  1.00119.13      A    C  
ANISOU 3608  CD1 LEU A 471    16096  16825  12344    140   1769   -570  A    C  
ATOM   3609  CD2 LEU A 471      87.706  81.070  79.938  1.00129.28      A    C  
ANISOU 3609  CD2 LEU A 471    17642  18030  13446    113   1624   -539  A    C  
ATOM   3610  N   SER A 472      84.179  77.922  78.104  1.00167.66      A    N  
ANISOU 3610  N   SER A 472    22383  23191  18128   -452   1924   -739  A    N  
ATOM   3611  CA  SER A 472      82.972  77.135  77.841  1.00165.75      A    C  
ANISOU 3611  CA  SER A 472    22101  23091  17786   -704   2056   -850  A    C  
ATOM   3612  C   SER A 472      81.714  77.989  78.049  1.00154.48      A    C  
ANISOU 3612  C   SER A 472    20451  21872  16370   -726   2071   -843  A    C  
ATOM   3613  O   SER A 472      81.746  78.976  78.779  1.00130.41      A    O  
ANISOU 3613  O   SER A 472    17388  18748  13412   -561   2049   -782  A    O  
ATOM   3614  CB  SER A 472      82.940  75.874  78.711  1.00167.25      A    C  
ANISOU 3614  CB  SER A 472    22599  23045  17900   -827   2240   -932  A    C  
ATOM   3615  OG  SER A 472      81.891  75.007  78.314  1.00168.48      A    O  
ANISOU 3615  OG  SER A 472    22742  23326  17947  -1126   2402  -1079  A    O  
ATOM   3616  N   LYS A 473      80.620  77.614  77.393  1.00154.03      A    N  
ANISOU 3616  N   LYS A 473    20208  22100  16215   -946   2132   -908  A    N  
ATOM   3617  CA  LYS A 473      79.360  78.348  77.525  1.00156.87      A    C  
ANISOU 3617  CA  LYS A 473    20312  22709  16580   -959   2165   -872  A    C  
ATOM   3618  C   LYS A 473      78.921  78.430  78.990  1.00159.85      A    C  
ANISOU 3618  C   LYS A 473    20878  22874  16983   -943   2280   -928  A    C  
ATOM   3619  O   LYS A 473      78.319  79.425  79.425  1.00133.17      A    O  
ANISOU 3619  O   LYS A 473    17357  19552  13689   -825   2304   -864  A    O  
ATOM   3620  CB  LYS A 473      78.280  77.688  76.670  1.00158.92      A    C  
ANISOU 3620  CB  LYS A 473    20350  23362  16669  -1262   2221   -952  A    C  
ATOM   3621  CG  LYS A 473      78.353  78.110  75.217  1.00158.67      A    C  
ANISOU 3621  CG  LYS A 473    19982  23702  16604  -1242   2088   -829  A    C  
ATOM   3622  CD  LYS A 473      77.370  77.340  74.367  1.00161.98      A    C  
ANISOU 3622  CD  LYS A 473    20176  24578  16789  -1612   2142   -932  A    C  
ATOM   3623  CE  LYS A 473      77.299  77.939  72.973  1.00160.82      A    C  
ANISOU 3623  CE  LYS A 473    19618  24903  16582  -1568   1994   -748  A    C  
ATOM   3624  NZ  LYS A 473      76.549  77.074  72.018  1.00159.56      A    N1+
ANISOU 3624  NZ  LYS A 473    19241  25251  16133  -1997   2032   -874  A    N1+
ATOM   3625  N   THR A 474      79.242  77.371  79.739  1.00175.83      A    N  
ANISOU 3625  N   THR A 474    23226  24644  18936  -1054   2379  -1032  A    N  
ATOM   3626  CA  THR A 474      79.041  77.334  81.187  1.00166.03      A    C  
ANISOU 3626  CA  THR A 474    22206  23185  17694  -1033   2480  -1066  A    C  
ATOM   3627  C   THR A 474      79.891  78.438  81.822  1.00161.70      A    C  
ANISOU 3627  C   THR A 474    21694  22488  17254   -773   2379   -962  A    C  
ATOM   3628  O   THR A 474      79.400  79.191  82.654  1.00148.83      A    O  
ANISOU 3628  O   THR A 474    20047  20839  15661   -729   2430   -967  A    O  
ATOM   3629  CB  THR A 474      79.405  75.947  81.811  1.00164.42      A    C  
ANISOU 3629  CB  THR A 474    22350  22722  17399  -1152   2625  -1134  A    C  
ATOM   3630  CG2 THR A 474      78.574  74.805  81.181  1.00164.45      A    C  
ANISOU 3630  CG2 THR A 474    22359  22834  17287  -1476   2794  -1289  A    C  
ATOM   3631  OG1 THR A 474      80.808  75.669  81.649  1.00155.67      A    O  
ANISOU 3631  OG1 THR A 474    21392  21426  16328   -995   2548  -1044  A    O  
ATOM   3632  N   GLN A 475      81.159  78.527  81.411  1.00163.45      A    N  
ANISOU 3632  N   GLN A 475    21967  22618  17518   -632   2256   -888  A    N  
ATOM   3633  CA  GLN A 475      82.107  79.498  81.972  1.00151.25      A    C  
ANISOU 3633  CA  GLN A 475    20468  20958  16041   -441   2169   -819  A    C  
ATOM   3634  C   GLN A 475      82.087  80.837  81.250  1.00137.63      A    C  
ANISOU 3634  C   GLN A 475    18495  19343  14453   -308   2109   -760  A    C  
ATOM   3635  O   GLN A 475      82.709  81.796  81.700  1.00115.44      A    O  
ANISOU 3635  O   GLN A 475    15713  16437  11709   -191   2093   -739  A    O  
ATOM   3636  CB  GLN A 475      83.534  78.955  81.947  1.00145.52      A    C  
ANISOU 3636  CB  GLN A 475    19905  20099  15286   -353   2079   -757  A    C  
ATOM   3637  CG  GLN A 475      83.687  77.531  82.435  1.00147.71      A    C  
ANISOU 3637  CG  GLN A 475    20422  20239  15461   -432   2181   -758  A    C  
ATOM   3638  CD  GLN A 475      85.046  76.974  82.073  1.00141.92      A    C  
ANISOU 3638  CD  GLN A 475    19787  19406  14729   -316   2114   -662  A    C  
ATOM   3639  NE2 GLN A 475      85.759  76.466  83.070  1.00136.52      A    N  
ANISOU 3639  NE2 GLN A 475    19293  18602  13976   -229   2147   -558  A    N  
ATOM   3640  OE1 GLN A 475      85.445  76.989  80.909  1.00143.64      A    O  
ANISOU 3640  OE1 GLN A 475    19894  19678  15003   -298   2039   -661  A    O  
ATOM   3641  N   ALA A 476      81.386  80.902  80.123  1.00140.64      A    N  
ANISOU 3641  N   ALA A 476    18629  19939  14866   -336   2101   -722  A    N  
ATOM   3642  CA  ALA A 476      81.253  82.154  79.397  1.00140.47      A    C  
ANISOU 3642  CA  ALA A 476    18351  20033  14987   -173   2085   -607  A    C  
ATOM   3643  C   ALA A 476      80.581  83.181  80.297  1.00138.73      A    C  
ANISOU 3643  C   ALA A 476    18106  19741  14863   -104   2235   -613  A    C  
ATOM   3644  O   ALA A 476      80.874  84.370  80.212  1.00123.79      A    O  
ANISOU 3644  O   ALA A 476    16144  17771  13119     60   2289   -544  A    O  
ATOM   3645  CB  ALA A 476      80.472  81.950  78.103  1.00141.04      A    C  
ANISOU 3645  CB  ALA A 476    18122  20437  15027   -230   2056   -528  A    C  
ATOM   3646  N   GLU A 477      79.703  82.693  81.174  1.00155.46      A    N  
ANISOU 3646  N   GLU A 477    20305  21860  16900   -244   2336   -707  A    N  
ATOM   3647  CA  GLU A 477      79.008  83.531  82.163  1.00163.07      A    C  
ANISOU 3647  CA  GLU A 477    21279  22741  17936   -217   2505   -744  A    C  
ATOM   3648  C   GLU A 477      79.938  83.956  83.295  1.00159.65      A    C  
ANISOU 3648  C   GLU A 477    21111  22057  17492   -205   2528   -829  A    C  
ATOM   3649  O   GLU A 477      79.632  84.887  84.033  1.00150.27      A    O  
ANISOU 3649  O   GLU A 477    19945  20770  16379   -182   2688   -876  A    O  
ATOM   3650  CB  GLU A 477      77.803  82.780  82.751  1.00160.70      A    C  
ANISOU 3650  CB  GLU A 477    20992  22536  17528   -400   2602   -830  A    C  
ATOM   3651  CG  GLU A 477      76.880  82.177  81.701  1.00167.15      A    C  
ANISOU 3651  CG  GLU A 477    21549  23675  18285   -502   2578   -786  A    C  
ATOM   3652  CD  GLU A 477      76.393  83.203  80.691  1.00169.61      A    C  
ANISOU 3652  CD  GLU A 477    21486  24224  18733   -321   2595   -600  A    C  
ATOM   3653  OE1 GLU A 477      75.647  84.108  81.109  1.00162.47      A    O  
ANISOU 3653  OE1 GLU A 477    20457  23322  17950   -212   2756   -543  A    O  
ATOM   3654  OE2 GLU A 477      76.747  83.103  79.489  1.00163.39      A    O1-
ANISOU 3654  OE2 GLU A 477    20525  23623  17932   -280   2470   -492  A    O1-
ATOM   3655  N   GLN A 478      81.071  83.273  83.422  1.00164.45      A    N  
ANISOU 3655  N   GLN A 478    21902  22588  17993   -233   2387   -845  A    N  
ATOM   3656  CA  GLN A 478      82.038  83.579  84.470  1.00172.13      A    C  
ANISOU 3656  CA  GLN A 478    23083  23422  18894   -247   2379   -903  A    C  
ATOM   3657  C   GLN A 478      83.015  84.681  84.039  1.00165.25      A    C  
ANISOU 3657  C   GLN A 478    22162  22492  18131   -134   2354   -882  A    C  
ATOM   3658  O   GLN A 478      83.858  85.115  84.820  1.00151.83      A    O  
ANISOU 3658  O   GLN A 478    20597  20729  16361   -180   2357   -948  A    O  
ATOM   3659  CB  GLN A 478      82.810  82.308  84.862  1.00178.66      A    C  
ANISOU 3659  CB  GLN A 478    24102  24229  19548   -303   2260   -881  A    C  
ATOM   3660  CG  GLN A 478      81.934  81.216  85.453  1.00180.25      A    C  
ANISOU 3660  CG  GLN A 478    24415  24430  19641   -429   2341   -912  A    C  
ATOM   3661  CD  GLN A 478      81.103  81.723  86.599  1.00178.05      A    C  
ANISOU 3661  CD  GLN A 478    24188  24132  19330   -518   2489   -998  A    C  
ATOM   3662  NE2 GLN A 478      79.851  81.297  86.657  1.00178.38      A    N  
ANISOU 3662  NE2 GLN A 478    24190  24216  19369   -616   2601  -1045  A    N  
ATOM   3663  OE1 GLN A 478      81.588  82.480  87.441  1.00163.76      A    O  
ANISOU 3663  OE1 GLN A 478    22452  22288  17480   -527   2513  -1039  A    O  
ATOM   3664  N   ALA A 479      82.900  85.135  82.796  1.00162.49      A    N  
ANISOU 3664  N   ALA A 479    21610  22192  17934     -6   2341   -787  A    N  
ATOM   3665  CA  ALA A 479      83.869  86.077  82.236  1.00150.65      A    C  
ANISOU 3665  CA  ALA A 479    20072  20619  16546    104   2331   -753  A    C  
ATOM   3666  C   ALA A 479      83.578  87.527  82.618  1.00134.76      A    C  
ANISOU 3666  C   ALA A 479    18042  18470  14689    145   2581   -801  A    C  
ATOM   3667  O   ALA A 479      82.421  87.915  82.660  1.00142.61      A    O  
ANISOU 3667  O   ALA A 479    18925  19470  15790    188   2754   -769  A    O  
ATOM   3668  CB  ALA A 479      83.901  85.926  80.722  1.00161.26      A    C  
ANISOU 3668  CB  ALA A 479    21212  22081  17977    228   2227   -606  A    C  
ATOM   3669  N   PRO A 480      84.626  88.333  82.885  1.00127.09      A    N  
ANISOU 3669  N   PRO A 480    17180  17373  13735    120   2634   -883  A    N  
ATOM   3670  CA  PRO A 480      84.425  89.769  83.159  1.00131.91      A    C  
ANISOU 3670  CA  PRO A 480    17805  17796  14517    138   2946   -953  A    C  
ATOM   3671  C   PRO A 480      83.975  90.567  81.928  1.00133.17      A    C  
ANISOU 3671  C   PRO A 480    17752  17901  14944    381   3094   -765  A    C  
ATOM   3672  O   PRO A 480      84.090  90.073  80.815  1.00130.27      A    O  
ANISOU 3672  O   PRO A 480    17228  17674  14592    506   2906   -599  A    O  
ATOM   3673  CB  PRO A 480      85.811  90.255  83.624  1.00124.28      A    C  
ANISOU 3673  CB  PRO A 480    17006  16760  13454     -3   2942  -1104  A    C  
ATOM   3674  CG  PRO A 480      86.579  89.023  83.961  1.00125.77      A    C  
ANISOU 3674  CG  PRO A 480    17270  17130  13386    -95   2628  -1103  A    C  
ATOM   3675  CD  PRO A 480      86.025  87.928  83.100  1.00125.65      A    C  
ANISOU 3675  CD  PRO A 480    17126  17223  13390     39   2444   -934  A    C  
ATOM   3676  N   ALA A 481      83.456  91.781  82.143  1.00141.13      A    N  
ANISOU 3676  N   ALA A 481    18754  18711  16156    448   3454   -779  A    N  
ATOM   3677  CA  ALA A 481      83.160  92.740  81.047  1.00135.88      A    C  
ANISOU 3677  CA  ALA A 481    17900  17954  15773    718   3670   -558  A    C  
ATOM   3678  C   ALA A 481      84.440  93.461  80.599  1.00134.44      A    C  
ANISOU 3678  C   ALA A 481    17819  17599  15662    728   3727   -598  A    C  
ATOM   3679  O   ALA A 481      84.427  94.278  79.648  1.00113.77      A    O  
ANISOU 3679  O   ALA A 481    15078  14873  13275    957   3915   -405  A    O  
ATOM   3680  CB  ALA A 481      82.108  93.758  81.469  1.00136.15      A    C  
ANISOU 3680  CB  ALA A 481    17901  17800  16030    818   4101   -533  A    C  
ATOM   3681  N   ASP A 482      85.533  93.152  81.309  1.00136.18      A    N  
ANISOU 3681  N   ASP A 482    18253  17818  15672    477   3577   -832  A    N  
ATOM   3682  CA  ASP A 482      86.906  93.406  80.833  1.00130.15      A    C  
ANISOU 3682  CA  ASP A 482    17559  17009  14881    437   3491   -878  A    C  
ATOM   3683  C   ASP A 482      87.205  92.631  79.520  1.00120.00      A    C  
ANISOU 3683  C   ASP A 482    16090  15915  13587    616   3172   -651  A    C  
ATOM   3684  O   ASP A 482      87.978  93.090  78.674  1.00112.30      A    O  
ANISOU 3684  O   ASP A 482    15087  14875  12706    704   3183   -580  A    O  
ATOM   3685  CB  ASP A 482      87.922  93.006  81.916  1.00120.25      A    C  
ANISOU 3685  CB  ASP A 482    16507  15840  13342    130   3338  -1134  A    C  
ATOM   3686  CG  ASP A 482      89.351  93.327  81.523  1.00113.85      A    C  
ANISOU 3686  CG  ASP A 482    15755  15017  12486     55   3271  -1202  A    C  
ATOM   3687  OD1 ASP A 482      89.602  94.502  81.212  1.00123.03      A    O  
ANISOU 3687  OD1 ASP A 482    16964  15946  13834     67   3585  -1251  A    O  
ATOM   3688  OD2 ASP A 482      90.218  92.429  81.527  1.00103.81      A    O1-
ANISOU 3688  OD2 ASP A 482    14484  13954  11005    -13   2940  -1202  A    O1-
ATOM   3689  N   TYR A 483      86.587  91.456  79.375  1.00107.02      A    N  
ANISOU 3689  N   TYR A 483    14337  14502  11821    637   2917   -557  A    N  
ATOM   3690  CA  TYR A 483      86.658  90.693  78.152  1.00 99.66      A    C  
ANISOU 3690  CA  TYR A 483    13227  13771  10868    762   2664   -367  A    C  
ATOM   3691  C   TYR A 483      85.709  91.302  77.114  1.00105.24      A    C  
ANISOU 3691  C   TYR A 483    13672  14531  11781   1009   2819   -104  A    C  
ATOM   3692  O   TYR A 483      84.699  91.913  77.466  1.00108.58      A    O  
ANISOU 3692  O   TYR A 483    14030  14890  12335   1088   3074    -51  A    O  
ATOM   3693  CB  TYR A 483      86.322  89.229  78.433  1.00 94.66      A    C  
ANISOU 3693  CB  TYR A 483    12599  13346  10022    646   2405   -399  A    C  
ATOM   3694  CG  TYR A 483      87.410  88.442  79.171  1.00 92.47      A    C  
ANISOU 3694  CG  TYR A 483    12527  13071   9535    476   2214   -553  A    C  
ATOM   3695  CD1 TYR A 483      88.350  89.067  79.998  1.00 86.96      A    C  
ANISOU 3695  CD1 TYR A 483    11998  12254   8787    361   2285   -709  A    C  
ATOM   3696  CD2 TYR A 483      87.481  87.042  79.039  1.00 94.81      A    C  
ANISOU 3696  CD2 TYR A 483    12837  13513   9672    422   1988   -530  A    C  
ATOM   3697  CE1 TYR A 483      89.327  88.325  80.656  1.00 85.59      A    C  
ANISOU 3697  CE1 TYR A 483    11953  12167   8400    231   2101   -791  A    C  
ATOM   3698  CE2 TYR A 483      88.441  86.284  79.702  1.00 87.86      A    C  
ANISOU 3698  CE2 TYR A 483    12120  12643   8620    323   1845   -606  A    C  
ATOM   3699  CZ  TYR A 483      89.362  86.920  80.500  1.00 88.26      A    C  
ANISOU 3699  CZ  TYR A 483    12289  12633   8610    245   1882   -712  A    C  
ATOM   3700  OH  TYR A 483      90.291  86.114  81.131  1.00 89.09      A    O  
ANISOU 3700  OH  TYR A 483    12504  12823   8523    173   1730   -727  A    O  
ATOM   3701  N   GLN A 484      86.039  91.140  75.834  1.00111.90      A    N  
ANISOU 3701  N   GLN A 484    14350  15517  12648   1137   2676     83  A    N  
ATOM   3702  CA  GLN A 484      85.338  91.847  74.762  1.00122.76      A    C  
ANISOU 3702  CA  GLN A 484    15451  16982  14209   1399   2829    390  A    C  
ATOM   3703  C   GLN A 484      84.467  90.949  73.870  1.00125.74      A    C  
ANISOU 3703  C   GLN A 484    15532  17778  14465   1435   2618    587  A    C  
ATOM   3704  O   GLN A 484      83.444  91.393  73.354  1.00140.17      A    O  
ANISOU 3704  O   GLN A 484    17083  19780  16392   1620   2755    846  A    O  
ATOM   3705  CB  GLN A 484      86.355  92.607  73.909  1.00122.52      A    C  
ANISOU 3705  CB  GLN A 484    15432  16811  14308   1528   2893    488  A    C  
ATOM   3706  CG  GLN A 484      85.797  93.832  73.196  1.00122.58      A    C  
ANISOU 3706  CG  GLN A 484    15251  16736  14586   1834   3226    795  A    C  
ATOM   3707  CD  GLN A 484      86.898  94.738  72.688  1.00120.31      A    C  
ANISOU 3707  CD  GLN A 484    15077  16182  14448   1919   3386    818  A    C  
ATOM   3708  NE2 GLN A 484      86.764  95.189  71.440  1.00118.65      A    N  
ANISOU 3708  NE2 GLN A 484    14634  16082  14365   2186   3452   1168  A    N  
ATOM   3709  OE1 GLN A 484      87.876  95.019  73.404  1.00111.40      A    O  
ANISOU 3709  OE1 GLN A 484    14235  14787  13304   1730   3452    531  A    O  
ATOM   3710  N   ARG A 485      84.880  89.704  73.672  1.00123.57      A    N  
ANISOU 3710  N   ARG A 485    15300  17679  13968   1249   2314    474  A    N  
ATOM   3711  CA  ARG A 485      84.084  88.737  72.933  1.00134.85      A    C  
ANISOU 3711  CA  ARG A 485    16490  19510  15234   1182   2138    579  A    C  
ATOM   3712  C   ARG A 485      84.064  89.030  71.426  1.00153.19      A    C  
ANISOU 3712  C   ARG A 485    18512  22112  17581   1342   2086    871  A    C  
ATOM   3713  O   ARG A 485      84.346  90.144  71.008  1.00150.88      A    O  
ANISOU 3713  O   ARG A 485    18157  21684  17483   1574   2252   1055  A    O  
ATOM   3714  CB  ARG A 485      82.661  88.702  73.508  1.00130.47      A    C  
ANISOU 3714  CB  ARG A 485    15804  19093  14673   1165   2263    609  A    C  
ATOM   3715  CG  ARG A 485      81.766  87.620  72.935  1.00139.09      A    C  
ANISOU 3715  CG  ARG A 485    16666  20629  15551   1008   2102    651  A    C  
ATOM   3716  CD  ARG A 485      80.323  87.808  73.375  1.00151.41      A    C  
ANISOU 3716  CD  ARG A 485    18031  22367  17128   1029   2254    731  A    C  
ATOM   3717  NE  ARG A 485      79.378  87.218  72.433  1.00153.36      A    N  
ANISOU 3717  NE  ARG A 485    17911  23159  17197    944   2149    889  A    N  
ATOM   3718  CZ  ARG A 485      78.061  87.331  72.531  1.00159.39      A    C  
ANISOU 3718  CZ  ARG A 485    18400  24221  17939    961   2253   1014  A    C  
ATOM   3719  NH1 ARG A 485      77.508  88.013  73.532  1.00160.18      A    N1+
ANISOU 3719  NH1 ARG A 485    18568  24083  18210   1081   2480   1004  A    N1+
ATOM   3720  NH2 ARG A 485      77.292  86.753  71.625  1.00165.44      A    N  
ANISOU 3720  NH2 ARG A 485    18811  25556  18492    832   2138   1143  A    N  
ATOM   3721  N   ARG A 486      83.782  87.998  70.624  1.00176.63      A    N  
ANISOU 3721  N   ARG A 486    21311  25463  20336   1191   1875    898  A    N  
ATOM   3722  CA  ARG A 486      83.267  88.180  69.256  1.00183.04      A    C  
ANISOU 3722  CA  ARG A 486    21733  26715  21097   1300   1832   1212  A    C  
ATOM   3723  C   ARG A 486      82.411  86.957  68.770  1.00186.72      A    C  
ANISOU 3723  C   ARG A 486    21989  27684  21272   1026   1665   1172  A    C  
ATOM   3724  O   ARG A 486      81.228  86.871  69.108  1.00191.56      A    O  
ANISOU 3724  O   ARG A 486    22426  28523  21834    985   1736   1217  A    O  
ATOM   3725  CB  ARG A 486      84.365  88.659  68.273  1.00177.02      A    C  
ANISOU 3725  CB  ARG A 486    20965  25890  20405   1438   1782   1345  A    C  
ATOM   3726  CG  ARG A 486      85.312  87.633  67.698  1.00186.83      A    C  
ANISOU 3726  CG  ARG A 486    22326  27199  21463   1219   1543   1175  A    C  
ATOM   3727  CD  ARG A 486      86.062  86.818  68.736  1.00214.87      A    C  
ANISOU 3727  CD  ARG A 486    26260  30416  24964   1017   1475    818  A    C  
ATOM   3728  NE  ARG A 486      86.534  85.580  68.115  1.00250.84      A    N  
ANISOU 3728  NE  ARG A 486    30858  35135  29312    784   1289    686  A    N  
ATOM   3729  CZ  ARG A 486      85.955  84.385  68.237  1.00255.71      A    C  
ANISOU 3729  CZ  ARG A 486    31489  35935  29734    519   1234    529  A    C  
ATOM   3730  NH1 ARG A 486      84.883  84.215  69.010  1.00250.24      A    N1+
ANISOU 3730  NH1 ARG A 486    30770  35300  29010    448   1317    479  A    N1+
ATOM   3731  NH2 ARG A 486      86.465  83.340  67.595  1.00257.81      A    N  
ANISOU 3731  NH2 ARG A 486    31813  36304  29838    309   1129    405  A    N  
ATOM   3732  N   GLN A 487      82.976  86.019  68.012  1.00184.94      A    N  
ANISOU 3732  N   GLN A 487    21784  27632  20849    812   1476   1068  A    N  
ATOM   3733  CA  GLN A 487      82.201  84.877  67.475  1.00189.48      A    C  
ANISOU 3733  CA  GLN A 487    22173  28692  21130    490   1368    994  A    C  
ATOM   3734  C   GLN A 487      81.732  83.871  68.549  1.00185.59      A    C  
ANISOU 3734  C   GLN A 487    21912  28068  20536    217   1402    681  A    C  
ATOM   3735  O   GLN A 487      82.450  83.588  69.504  1.00171.42      A    O  
ANISOU 3735  O   GLN A 487    20493  25813  18826    198   1426    462  A    O  
ATOM   3736  CB  GLN A 487      83.005  84.155  66.364  1.00182.86      A    C  
ANISOU 3736  CB  GLN A 487    21333  28030  20115    307   1209    935  A    C  
ATOM   3737  CG  GLN A 487      82.565  82.723  66.073  1.00171.86      A    C  
ANISOU 3737  CG  GLN A 487    19933  26946  18418   -130   1149    695  A    C  
ATOM   3738  CD  GLN A 487      83.076  82.182  64.747  1.00154.87      A    C  
ANISOU 3738  CD  GLN A 487    17665  25112  16063   -323   1033    696  A    C  
ATOM   3739  NE2 GLN A 487      82.792  80.909  64.487  1.00145.86      A    N  
ANISOU 3739  NE2 GLN A 487    16568  24190  14660   -749   1034    437  A    N  
ATOM   3740  OE1 GLN A 487      83.693  82.899  63.961  1.00155.95      A    O  
ANISOU 3740  OE1 GLN A 487    17681  25297  16273   -112    969    915  A    O  
ATOM   3741  N   THR A 488      80.530  83.325  68.362  1.00183.43      A    N  
ANISOU 3741  N   THR A 488    21394  28239  20060     -3   1411    677  A    N  
ATOM   3742  CA  THR A 488      79.965  82.310  69.259  1.00182.00      A    C  
ANISOU 3742  CA  THR A 488    21407  27983  19759   -297   1473    387  A    C  
ATOM   3743  C   THR A 488      80.206  80.888  68.745  1.00168.51      A    C  
ANISOU 3743  C   THR A 488    19819  26408  17797   -703   1422    131  A    C  
ATOM   3744  O   THR A 488      80.108  80.632  67.544  1.00157.43      A    O  
ANISOU 3744  O   THR A 488    18160  25454  16203   -863   1342    198  A    O  
ATOM   3745  CB  THR A 488      78.450  82.502  69.399  1.00194.51      A    C  
ANISOU 3745  CB  THR A 488    22661  29983  21261   -347   1552    500  A    C  
ATOM   3746  CG2 THR A 488      78.134  83.789  70.137  1.00189.91      A    C  
ANISOU 3746  CG2 THR A 488    22030  29173  20953     30   1682    702  A    C  
ATOM   3747  OG1 THR A 488      77.860  82.554  68.093  1.00203.79      A    O  
ANISOU 3747  OG1 THR A 488    23370  31825  22235   -427   1470    721  A    O  
ATOM   3748  N   LEU A 489      80.499  79.963  69.656  1.00162.15      A    N  
ANISOU 3748  N   LEU A 489    19402  25222  16986   -876   1501   -154  A    N  
ATOM   3749  CA  LEU A 489      80.837  78.588  69.280  1.00163.25      A    C  
ANISOU 3749  CA  LEU A 489    19734  25357  16937  -1239   1537   -413  A    C  
ATOM   3750  C   LEU A 489      79.761  77.594  69.762  1.00163.59      A    C  
ANISOU 3750  C   LEU A 489    19827  25533  16798  -1609   1691   -639  A    C  
ATOM   3751  O   LEU A 489      78.587  77.941  69.822  1.00159.09      A    O  
ANISOU 3751  O   LEU A 489    18969  25327  16149  -1661   1708   -559  A    O  
ATOM   3752  CB  LEU A 489      82.239  78.212  69.808  1.00161.39      A    C  
ANISOU 3752  CB  LEU A 489    19923  24548  16848  -1121   1548   -527  A    C  
ATOM   3753  CG  LEU A 489      83.503  78.714  69.077  1.00150.22      A    C  
ANISOU 3753  CG  LEU A 489    18514  23027  15537   -908   1418   -404  A    C  
ATOM   3754  CD1 LEU A 489      83.502  78.287  67.612  1.00150.71      A    C  
ANISOU 3754  CD1 LEU A 489    18358  23505  15397  -1142   1364   -408  A    C  
ATOM   3755  CD2 LEU A 489      83.678  80.220  69.202  1.00141.41      A    C  
ANISOU 3755  CD2 LEU A 489    17242  21861  14624   -525   1338   -148  A    C  
ATOM   3756  N   LYS A 490      80.170  76.369  70.091  1.00169.96      A    N  
ANISOU 3756  N   LYS A 490    20994  26037  17544  -1857   1830   -907  A    N  
ATOM   3757  CA  LYS A 490      79.255  75.279  70.437  1.00180.69      A    C  
ANISOU 3757  CA  LYS A 490    22453  27479  18720  -2265   2032  -1161  A    C  
ATOM   3758  C   LYS A 490      79.493  74.816  71.879  1.00180.92      A    C  
ANISOU 3758  C   LYS A 490    22910  26935  18893  -2178   2186  -1274  A    C  
ATOM   3759  O   LYS A 490      78.567  74.765  72.691  1.00165.82      A    O  
ANISOU 3759  O   LYS A 490    21005  25038  16960  -2253   2285  -1327  A    O  
ATOM   3760  CB  LYS A 490      79.447  74.113  69.452  1.00189.70      A    C  
ANISOU 3760  CB  LYS A 490    23660  28780  19637  -2698   2148  -1393  A    C  
ATOM   3761  CG  LYS A 490      78.732  72.813  69.813  1.00198.02      A    C  
ANISOU 3761  CG  LYS A 490    24928  29792  20517  -3168   2441  -1717  A    C  
ATOM   3762  CD  LYS A 490      77.231  72.992  70.000  1.00201.24      A    C  
ANISOU 3762  CD  LYS A 490    25034  30671  20755  -3384   2462  -1736  A    C  
ATOM   3763  CE  LYS A 490      76.522  73.293  68.687  1.00194.18      A    C  
ANISOU 3763  CE  LYS A 490    23616  30580  19581  -3635   2330  -1666  A    C  
ATOM   3764  NZ  LYS A 490      75.050  73.403  68.881  1.00187.32      A    N1+
ANISOU 3764  NZ  LYS A 490    22424  30221  18526  -3859   2363  -1676  A    N1+
ATOM   3765  N   ASN A 491      80.738  74.477  72.193  1.00189.90      A    N  
ANISOU 3765  N   ASN A 491    24381  27602  20169  -2013   2211  -1287  A    N  
ATOM   3766  CA  ASN A 491      81.114  74.164  73.560  1.00189.66      A    C  
ANISOU 3766  CA  ASN A 491    24714  27073  20273  -1860   2327  -1311  A    C  
ATOM   3767  C   ASN A 491      81.587  75.413  74.304  1.00179.06      A    C  
ANISOU 3767  C   ASN A 491    23339  25572  19122  -1441   2151  -1100  A    C  
ATOM   3768  O   ASN A 491      81.355  75.544  75.499  1.00183.07      A    O  
ANISOU 3768  O   ASN A 491    23995  25870  19692  -1344   2210  -1093  A    O  
ATOM   3769  CB  ASN A 491      82.205  73.089  73.580  1.00190.28      A    C  
ANISOU 3769  CB  ASN A 491    25155  26754  20388  -1889   2479  -1402  A    C  
ATOM   3770  CG  ASN A 491      81.844  71.867  72.749  1.00192.57      A    C  
ANISOU 3770  CG  ASN A 491    25511  27158  20497  -2336   2713  -1646  A    C  
ATOM   3771  ND2 ASN A 491      82.820  70.992  72.530  1.00185.33      A    N  
ANISOU 3771  ND2 ASN A 491    24876  25914  19628  -2357   2877  -1714  A    N  
ATOM   3772  OD1 ASN A 491      80.699  71.703  72.322  1.00199.15      A    O  
ANISOU 3772  OD1 ASN A 491    26142  28381  21144  -2675   2770  -1778  A    O  
ATOM   3773  N   ALA A 492      82.230  76.331  73.591  1.00164.83      A    N  
ANISOU 3773  N   ALA A 492    21347  23876  17402  -1225   1962   -943  A    N  
ATOM   3774  CA  ALA A 492      82.895  77.465  74.220  1.00152.43      A    C  
ANISOU 3774  CA  ALA A 492    19794  22108  16014   -870   1842   -783  A    C  
ATOM   3775  C   ALA A 492      82.413  78.843  73.714  1.00147.17      A    C  
ANISOU 3775  C   ALA A 492    18777  21719  15420   -697   1731   -604  A    C  
ATOM   3776  O   ALA A 492      81.302  78.974  73.205  1.00142.12      A    O  
ANISOU 3776  O   ALA A 492    17858  21449  14690   -819   1748   -571  A    O  
ATOM   3777  CB  ALA A 492      84.411  77.305  74.063  1.00148.13      A    C  
ANISOU 3777  CB  ALA A 492    19435  21300  15545   -718   1774   -749  A    C  
ATOM   3778  N   GLU A 493      83.258  79.861  73.902  1.00148.18      A    N  
ANISOU 3778  N   GLU A 493    18924  21666  15710   -414   1647   -480  A    N  
ATOM   3779  CA  GLU A 493      83.011  81.252  73.478  1.00143.69      A    C  
ANISOU 3779  CA  GLU A 493    18082  21246  15266   -192   1607   -287  A    C  
ATOM   3780  C   GLU A 493      84.304  82.112  73.676  1.00137.07      A    C  
ANISOU 3780  C   GLU A 493    17370  20118  14588     52   1552   -223  A    C  
ATOM   3781  O   GLU A 493      84.818  82.209  74.799  1.00121.02      A    O  
ANISOU 3781  O   GLU A 493    15578  17798  12605    101   1587   -301  A    O  
ATOM   3782  CB  GLU A 493      81.839  81.837  74.273  1.00149.87      A    C  
ANISOU 3782  CB  GLU A 493    18766  22081  16096   -155   1722   -257  A    C  
ATOM   3783  CG  GLU A 493      81.710  83.343  74.157  1.00155.33      A    C  
ANISOU 3783  CG  GLU A 493    19264  22777  16978    125   1769    -55  A    C  
ATOM   3784  CD  GLU A 493      81.545  83.783  72.722  1.00163.84      A    C  
ANISOU 3784  CD  GLU A 493    19995  24204  18050    215   1704    166  A    C  
ATOM   3785  OE1 GLU A 493      80.501  83.431  72.141  1.00163.84      A    O  
ANISOU 3785  OE1 GLU A 493    19717  24619  17912     85   1700    231  A    O  
ATOM   3786  OE2 GLU A 493      82.455  84.452  72.176  1.00182.44      A    O1-
ANISOU 3786  OE2 GLU A 493    22345  26453  20519    398   1660    278  A    O1-
ATOM   3787  N   ARG A 494      84.823  82.715  72.593  1.00134.63      A    N  
ANISOU 3787  N   ARG A 494    16895  19918  14338    177   1474    -82  A    N  
ATOM   3788  CA  ARG A 494      86.165  83.371  72.593  1.00119.54      A    C  
ANISOU 3788  CA  ARG A 494    15109  17758  12551    350   1425    -51  A    C  
ATOM   3789  C   ARG A 494      86.123  84.896  72.758  1.00104.70      A    C  
ANISOU 3789  C   ARG A 494    13138  15780  10863    577   1526     80  A    C  
ATOM   3790  O   ARG A 494      85.278  85.551  72.197  1.00 96.43      A    O  
ANISOU 3790  O   ARG A 494    11833  14927   9876    679   1597    253  A    O  
ATOM   3791  CB  ARG A 494      86.967  83.048  71.311  1.00120.16      A    C  
ANISOU 3791  CB  ARG A 494    15115  17954  12585    336   1304     -1  A    C  
ATOM   3792  CG  ARG A 494      86.789  81.648  70.723  1.00123.39      A    C  
ANISOU 3792  CG  ARG A 494    15537  18537  12807     85   1265   -110  A    C  
ATOM   3793  CD  ARG A 494      87.786  81.393  69.591  1.00122.65      A    C  
ANISOU 3793  CD  ARG A 494    15423  18495  12685     74   1167    -87  A    C  
ATOM   3794  NE  ARG A 494      87.305  80.399  68.638  1.00116.54      A    N  
ANISOU 3794  NE  ARG A 494    14541  18019  11719   -190   1164   -153  A    N  
ATOM   3795  CZ  ARG A 494      87.744  79.150  68.562  1.00113.16      A    C  
ANISOU 3795  CZ  ARG A 494    14316  17486  11195   -392   1212   -329  A    C  
ATOM   3796  NH1 ARG A 494      88.707  78.716  69.358  1.00109.63      A    N1+
ANISOU 3796  NH1 ARG A 494    14163  16663  10828   -313   1246   -407  A    N1+
ATOM   3797  NH2 ARG A 494      87.219  78.324  67.673  1.00120.70      A    N  
ANISOU 3797  NH2 ARG A 494    15166  18733  11959   -685   1251   -421  A    N  
ATOM   3798  N   PHE A 495      87.076  85.438  73.503  1.00103.47      A    N  
ANISOU 3798  N   PHE A 495    13187  15333  10791    645   1556      4  A    N  
ATOM   3799  CA  PHE A 495      87.057  86.836  73.928  1.00108.33      A    C  
ANISOU 3799  CA  PHE A 495    13799  15775  11585    797   1730     53  A    C  
ATOM   3800  C   PHE A 495      88.353  87.557  73.599  1.00111.29      A    C  
ANISOU 3800  C   PHE A 495    14251  15981  12050    885   1725     60  A    C  
ATOM   3801  O   PHE A 495      89.449  87.053  73.864  1.00112.88      A    O  
ANISOU 3801  O   PHE A 495    14621  16100  12167    802   1603    -58  A    O  
ATOM   3802  CB  PHE A 495      86.862  86.942  75.456  1.00113.25      A    C  
ANISOU 3802  CB  PHE A 495    14626  16209  12191    712   1839   -112  A    C  
ATOM   3803  CG  PHE A 495      85.533  86.443  75.949  1.00112.62      A    C  
ANISOU 3803  CG  PHE A 495    14488  16250  12050    631   1895   -131  A    C  
ATOM   3804  CD1 PHE A 495      85.324  85.091  76.159  1.00115.11      A    C  
ANISOU 3804  CD1 PHE A 495    14881  16663  12190    461   1781   -221  A    C  
ATOM   3805  CD2 PHE A 495      84.502  87.323  76.201  1.00113.08      A    C  
ANISOU 3805  CD2 PHE A 495    14421  16307  12235    724   2098    -56  A    C  
ATOM   3806  CE1 PHE A 495      84.112  84.622  76.605  1.00120.07      A    C  
ANISOU 3806  CE1 PHE A 495    15466  17402  12753    359   1849   -256  A    C  
ATOM   3807  CE2 PHE A 495      83.283  86.865  76.637  1.00122.41      A    C  
ANISOU 3807  CE2 PHE A 495    15531  17624  13352    641   2149    -75  A    C  
ATOM   3808  CZ  PHE A 495      83.085  85.511  76.846  1.00129.08      A    C  
ANISOU 3808  CZ  PHE A 495    16458  18580  14004    444   2016   -185  A    C  
ATOM   3809  N   ILE A 496      88.219  88.754  73.051  1.00117.11      A    N  
ANISOU 3809  N   ILE A 496    14862  16665  12967   1061   1888    212  A    N  
ATOM   3810  CA  ILE A 496      89.354  89.632  72.828  1.00125.39      A    C  
ANISOU 3810  CA  ILE A 496    16002  17511  14128   1130   1959    202  A    C  
ATOM   3811  C   ILE A 496      89.515  90.470  74.084  1.00132.48      A    C  
ANISOU 3811  C   ILE A 496    17099  18138  15098   1071   2179     30  A    C  
ATOM   3812  O   ILE A 496      88.538  90.698  74.793  1.00156.14      A    O  
ANISOU 3812  O   ILE A 496    20092  21100  18132   1067   2333     11  A    O  
ATOM   3813  CB  ILE A 496      89.103  90.582  71.626  1.00132.00      A    C  
ANISOU 3813  CB  ILE A 496    16623  18389  15142   1360   2096    472  A    C  
ATOM   3814  CG1 ILE A 496      88.537  89.835  70.398  1.00129.67      A    C  
ANISOU 3814  CG1 ILE A 496    16055  18471  14740   1397   1911    677  A    C  
ATOM   3815  CG2 ILE A 496      90.390  91.300  71.254  1.00139.77      A    C  
ANISOU 3815  CG2 ILE A 496    17717  19169  16217   1399   2151    446  A    C  
ATOM   3816  CD1 ILE A 496      89.581  89.084  69.579  1.00120.41      A    C  
ANISOU 3816  CD1 ILE A 496    14908  17397  13443   1311   1674    637  A    C  
ATOM   3817  N   THR A 497      90.721  90.936  74.380  1.00139.45      A    N  
ANISOU 3817  N   THR A 497    18148  18855  15982    994   2209   -109  A    N  
ATOM   3818  CA  THR A 497      90.887  91.938  75.454  1.00151.38      A    C  
ANISOU 3818  CA  THR A 497    19834  20127  17554    895   2479   -289  A    C  
ATOM   3819  C   THR A 497      91.899  93.025  75.042  1.00171.22      A    C  
ANISOU 3819  C   THR A 497    22421  22442  20193    906   2660   -325  A    C  
ATOM   3820  O   THR A 497      92.930  92.710  74.440  1.00192.12      A    O  
ANISOU 3820  O   THR A 497    25064  25158  22773    888   2474   -322  A    O  
ATOM   3821  CB  THR A 497      91.345  91.311  76.784  1.00132.92      A    C  
ANISOU 3821  CB  THR A 497    17675  17834  14991    654   2357   -525  A    C  
ATOM   3822  CG2 THR A 497      90.490  90.109  77.153  1.00127.43      A    C  
ANISOU 3822  CG2 THR A 497    16940  17313  14165    633   2181   -491  A    C  
ATOM   3823  OG1 THR A 497      92.705  90.899  76.664  1.00141.82      A    O  
ANISOU 3823  OG1 THR A 497    18863  19037  15984    564   2155   -594  A    O  
ATOM   3824  N   PRO A 498      91.611  94.304  75.360  1.00170.06      A    N  
ANISOU 3824  N   PRO A 498    22349  22027  20236    928   3059   -368  A    N  
ATOM   3825  CA  PRO A 498      92.499  95.401  74.950  1.00159.66      A    C  
ANISOU 3825  CA  PRO A 498    21126  20476  19060    923   3309   -413  A    C  
ATOM   3826  C   PRO A 498      93.952  95.344  75.480  1.00143.95      A    C  
ANISOU 3826  C   PRO A 498    19304  18510  16878    633   3200   -691  A    C  
ATOM   3827  O   PRO A 498      94.815  96.022  74.929  1.00144.27      A    O  
ANISOU 3827  O   PRO A 498    19395  18420  17001    619   3329   -717  A    O  
ATOM   3828  CB  PRO A 498      91.766  96.649  75.454  1.00157.85      A    C  
ANISOU 3828  CB  PRO A 498    20988  19928  19057    957   3816   -447  A    C  
ATOM   3829  CG  PRO A 498      90.336  96.247  75.502  1.00157.37      A    C  
ANISOU 3829  CG  PRO A 498    20762  19983  19047   1137   3795   -256  A    C  
ATOM   3830  CD  PRO A 498      90.351  94.811  75.930  1.00163.72      A    C  
ANISOU 3830  CD  PRO A 498    21534  21107  19563    994   3344   -337  A    C  
ATOM   3831  N   GLU A 499      94.235  94.548  76.507  1.00126.13      A    N  
ANISOU 3831  N   GLU A 499    17116  16447  14362    415   2973   -871  A    N  
ATOM   3832  CA  GLU A 499      95.626  94.416  76.968  1.00122.93      A    C  
ANISOU 3832  CA  GLU A 499    16803  16164  13738    161   2835  -1079  A    C  
ATOM   3833  C   GLU A 499      96.420  93.350  76.191  1.00113.50      A    C  
ANISOU 3833  C   GLU A 499    15495  15196  12433    251   2443   -947  A    C  
ATOM   3834  O   GLU A 499      97.644  93.297  76.292  1.00 93.60      A    O  
ANISOU 3834  O   GLU A 499    13004  12787   9770    100   2335  -1060  A    O  
ATOM   3835  CB  GLU A 499      95.708  94.157  78.479  1.00128.87      A    C  
ANISOU 3835  CB  GLU A 499    17661  17063  14237   -122   2802  -1304  A    C  
ATOM   3836  CG  GLU A 499      95.479  92.715  78.911  1.00132.26      A    C  
ANISOU 3836  CG  GLU A 499    18024  17764  14462    -83   2438  -1209  A    C  
ATOM   3837  CD  GLU A 499      93.998  92.332  78.981  1.00137.43      A    C  
ANISOU 3837  CD  GLU A 499    18633  18365  15218     73   2470  -1084  A    C  
ATOM   3838  OE1 GLU A 499      93.699  91.208  79.447  1.00129.90      A    O  
ANISOU 3838  OE1 GLU A 499    17660  17588  14106     74   2243  -1033  A    O  
ATOM   3839  OE2 GLU A 499      93.129  93.139  78.570  1.00137.71      A    O1-
ANISOU 3839  OE2 GLU A 499    18644  18185  15492    203   2743  -1021  A    O1-
ATOM   3840  N   LEU A 500      95.724  92.491  75.440  1.00114.25      A    N  
ANISOU 3840  N   LEU A 500    15455  15379  12576    471   2250   -723  A    N  
ATOM   3841  CA  LEU A 500      96.389  91.633  74.447  1.00113.42      A    C  
ANISOU 3841  CA  LEU A 500    15249  15423  12421    570   1965   -592  A    C  
ATOM   3842  C   LEU A 500      96.207  92.218  73.045  1.00117.49      A    C  
ANISOU 3842  C   LEU A 500    15654  15837  13149    773   2067   -401  A    C  
ATOM   3843  O   LEU A 500      96.994  91.909  72.146  1.00129.58      A    O  
ANISOU 3843  O   LEU A 500    17128  17441  14665    820   1914   -332  A    O  
ATOM   3844  CB  LEU A 500      95.950  90.149  74.496  1.00105.58      A    C  
ANISOU 3844  CB  LEU A 500    14195  14627  11293    616   1688   -503  A    C  
ATOM   3845  CG  LEU A 500      94.516  89.683  74.240  1.00109.84      A    C  
ANISOU 3845  CG  LEU A 500    14639  15205  11890    731   1691   -368  A    C  
ATOM   3846  CD1 LEU A 500      93.992  89.895  72.814  1.00111.26      A    C  
ANISOU 3846  CD1 LEU A 500    14642  15413  12217    915   1713   -157  A    C  
ATOM   3847  CD2 LEU A 500      94.451  88.206  74.612  1.00108.69      A    C  
ANISOU 3847  CD2 LEU A 500    14514  15216  11564    679   1466   -372  A    C  
ATOM   3848  N   LYS A 501      95.176  93.042  72.844  1.00116.34      A    N  
ANISOU 3848  N   LYS A 501    15464  15541  13199    910   2335   -289  A    N  
ATOM   3849  CA  LYS A 501      95.040  93.767  71.578  1.00119.50      A    C  
ANISOU 3849  CA  LYS A 501    15749  15851  13805   1126   2487    -62  A    C  
ATOM   3850  C   LYS A 501      96.259  94.641  71.398  1.00119.06      A    C  
ANISOU 3850  C   LYS A 501    15818  15608  13810   1039   2648   -181  A    C  
ATOM   3851  O   LYS A 501      96.771  94.768  70.287  1.00126.00      A    O  
ANISOU 3851  O   LYS A 501    16623  16497  14754   1153   2608    -38  A    O  
ATOM   3852  CB  LYS A 501      93.771  94.625  71.522  1.00120.95      A    C  
ANISOU 3852  CB  LYS A 501    15858  15891  14206   1315   2813    111  A    C  
ATOM   3853  CG  LYS A 501      92.685  94.081  70.608  1.00123.19      A    C  
ANISOU 3853  CG  LYS A 501    15876  16423  14508   1536   2679    422  A    C  
ATOM   3854  CD  LYS A 501      93.065  94.139  69.134  1.00121.11      A    C  
ANISOU 3854  CD  LYS A 501    15448  16275  14290   1702   2598    671  A    C  
ATOM   3855  CE  LYS A 501      92.088  93.332  68.288  1.00121.30      A    C  
ANISOU 3855  CE  LYS A 501    15188  16674  14223   1820   2387    927  A    C  
ATOM   3856  NZ  LYS A 501      92.247  91.850  68.443  1.00114.79      A    N1+
ANISOU 3856  NZ  LYS A 501    14375  16095  13145   1616   2022    768  A    N1+
ATOM   3857  N   ALA A 502      96.718  95.237  72.495  1.00113.72      A    N  
ANISOU 3857  N   ALA A 502    15330  14786  13090    807   2838   -455  A    N  
ATOM   3858  CA  ALA A 502      97.927  96.042  72.476  1.00110.60      A    C  
ANISOU 3858  CA  ALA A 502    15067  14249  12707    637   3008   -635  A    C  
ATOM   3859  C   ALA A 502      99.120  95.180  72.191  1.00100.79      A    C  
ANISOU 3859  C   ALA A 502    13780  13250  11262    541   2643   -686  A    C  
ATOM   3860  O   ALA A 502     100.041  95.611  71.516  1.00109.91      A    O  
ANISOU 3860  O   ALA A 502    14953  14345  12461    519   2693   -699  A    O  
ATOM   3861  CB  ALA A 502      98.112  96.751  73.793  1.00117.06      A    C  
ANISOU 3861  CB  ALA A 502    16077  14941  13456    337   3277   -952  A    C  
ATOM   3862  N   PHE A 503      99.091  93.955  72.692  1.00 94.76      A    N  
ANISOU 3862  N   PHE A 503    12963  12749  10292    498   2306   -699  A    N  
ATOM   3863  CA  PHE A 503     100.148  92.977  72.402  1.00 89.02      A    C  
ANISOU 3863  CA  PHE A 503    12178  12254   9390    459   1971   -697  A    C  
ATOM   3864  C   PHE A 503     100.022  92.461  70.973  1.00 85.96      A    C  
ANISOU 3864  C   PHE A 503    11654  11908   9097    687   1819   -458  A    C  
ATOM   3865  O   PHE A 503     101.012  92.425  70.260  1.00 90.63      A    O  
ANISOU 3865  O   PHE A 503    12220  12536   9676    683   1735   -449  A    O  
ATOM   3866  CB  PHE A 503     100.089  91.827  73.407  1.00 85.73      A    C  
ANISOU 3866  CB  PHE A 503    11758  12066   8748    375   1725   -746  A    C  
ATOM   3867  CG  PHE A 503     100.947  90.655  73.059  1.00 81.75      A    C  
ANISOU 3867  CG  PHE A 503    11181  11773   8107    412   1417   -676  A    C  
ATOM   3868  CD1 PHE A 503     102.284  90.644  73.334  1.00 82.08      A    C  
ANISOU 3868  CD1 PHE A 503    11222  11959   8003    271   1332   -778  A    C  
ATOM   3869  CD2 PHE A 503     100.386  89.535  72.488  1.00 86.94      A    C  
ANISOU 3869  CD2 PHE A 503    11766  12496   8770    570   1241   -512  A    C  
ATOM   3870  CE1 PHE A 503     103.059  89.546  73.026  1.00 81.53      A    C  
ANISOU 3870  CE1 PHE A 503    11077  12071   7829    339   1084   -685  A    C  
ATOM   3871  CE2 PHE A 503     101.155  88.432  72.158  1.00 87.11      A    C  
ANISOU 3871  CE2 PHE A 503    11742  12663   8691    607   1022   -452  A    C  
ATOM   3872  CZ  PHE A 503     102.495  88.438  72.436  1.00 84.31      A    C  
ANISOU 3872  CZ  PHE A 503    11386  12427   8222    516    947   -523  A    C  
ATOM   3873  N   GLU A 504      98.810  92.079  70.559  1.00 80.92      A    N  
ANISOU 3873  N   GLU A 504    10917  11297   8531    857   1793   -275  A    N  
ATOM   3874  CA  GLU A 504      98.554  91.613  69.210  1.00 78.02      A    C  
ANISOU 3874  CA  GLU A 504    10396  11035   8213   1030   1665    -52  A    C  
ATOM   3875  C   GLU A 504      98.998  92.658  68.216  1.00 80.17      A    C  
ANISOU 3875  C   GLU A 504    10643  11167   8648   1129   1846     54  A    C  
ATOM   3876  O   GLU A 504      99.596  92.324  67.221  1.00 82.66      A    O  
ANISOU 3876  O   GLU A 504    10886  11578   8942   1175   1708    140  A    O  
ATOM   3877  CB  GLU A 504      97.077  91.316  69.029  1.00 83.63      A    C  
ANISOU 3877  CB  GLU A 504    10982  11831   8961   1155   1675    117  A    C  
ATOM   3878  CG  GLU A 504      96.659  90.822  67.656  1.00 89.50      A    C  
ANISOU 3878  CG  GLU A 504    11528  12773   9701   1286   1547    347  A    C  
ATOM   3879  CD  GLU A 504      95.165  90.561  67.596  1.00 97.98      A    C  
ANISOU 3879  CD  GLU A 504    12449  14002  10775   1365   1565    497  A    C  
ATOM   3880  OE1 GLU A 504      94.489  91.274  66.804  1.00103.00      A    O  
ANISOU 3880  OE1 GLU A 504    12914  14688  11532   1544   1706    745  A    O  
ATOM   3881  OE2 GLU A 504      94.675  89.673  68.347  1.00 92.77      A    O1-
ANISOU 3881  OE2 GLU A 504    11830  13424   9991   1254   1457    385  A    O1-
ATOM   3882  N   ASP A 505      98.724  93.931  68.469  1.00 89.02      A    N  
ANISOU 3882  N   ASP A 505    11839  12042   9943   1162   2191     46  A    N  
ATOM   3883  CA  ASP A 505      99.115  94.979  67.510  1.00 97.81      A    C  
ANISOU 3883  CA  ASP A 505    12946  12975  11240   1279   2430    175  A    C  
ATOM   3884  C   ASP A 505     100.587  95.310  67.586  1.00 98.64      A    C  
ANISOU 3884  C   ASP A 505    13186  12997  11295   1086   2451    -41  A    C  
ATOM   3885  O   ASP A 505     101.104  96.034  66.754  1.00107.34      A    O  
ANISOU 3885  O   ASP A 505    14300  13959  12521   1152   2619     40  A    O  
ATOM   3886  CB  ASP A 505      98.259  96.234  67.662  1.00104.03      A    C  
ANISOU 3886  CB  ASP A 505    13772  13482  12269   1418   2869    283  A    C  
ATOM   3887  CG  ASP A 505      96.828  96.019  67.150  1.00119.38      A    C  
ANISOU 3887  CG  ASP A 505    15499  15571  14288   1682   2857    611  A    C  
ATOM   3888  OD1 ASP A 505      96.677  95.429  66.061  1.00127.87      A    O  
ANISOU 3888  OD1 ASP A 505    16374  16903  15304   1814   2632    844  A    O  
ATOM   3889  OD2 ASP A 505      95.847  96.421  67.821  1.00132.04      A    O1-
ANISOU 3889  OD2 ASP A 505    17112  17068  15989   1740   3074    633  A    O1-
ATOM   3890  N   LYS A 506     101.279  94.748  68.561  1.00 96.34      A    N  
ANISOU 3890  N   LYS A 506    12975  12826  10803    850   2277   -296  A    N  
ATOM   3891  CA  LYS A 506     102.700  94.980  68.685  1.00 92.99      A    C  
ANISOU 3891  CA  LYS A 506    12632  12412  10286    641   2266   -500  A    C  
ATOM   3892  C   LYS A 506     103.501  93.881  67.998  1.00 92.34      A    C  
ANISOU 3892  C   LYS A 506    12440  12573  10070    673   1906   -435  A    C  
ATOM   3893  O   LYS A 506     104.478  94.176  67.314  1.00 97.26      A    O  
ANISOU 3893  O   LYS A 506    13064  13177  10713    639   1921   -453  A    O  
ATOM   3894  CB  LYS A 506     103.070  95.042  70.146  1.00 91.63      A    C  
ANISOU 3894  CB  LYS A 506    12570  12306   9939    356   2292   -788  A    C  
ATOM   3895  CG  LYS A 506     104.542  95.206  70.409  1.00 94.54      A    C  
ANISOU 3895  CG  LYS A 506    12977  12794  10148     97   2253  -1006  A    C  
ATOM   3896  CD  LYS A 506     104.798  94.930  71.874  1.00104.28      A    C  
ANISOU 3896  CD  LYS A 506    14244  14247  11130   -168   2176  -1225  A    C  
ATOM   3897  CE  LYS A 506     106.259  95.081  72.241  1.00111.38      A    C  
ANISOU 3897  CE  LYS A 506    15131  15369  11817   -459   2124  -1435  A    C  
ATOM   3898  NZ  LYS A 506     106.682  96.503  72.126  1.00118.57      A    N1+
ANISOU 3898  NZ  LYS A 506    16185  16039  12827   -681   2531  -1647  A    N1+
ATOM   3899  N   VAL A 507     103.106  92.619  68.178  1.00 86.06      A    N  
ANISOU 3899  N   VAL A 507    11564  11985   9150    729   1621   -369  A    N  
ATOM   3900  CA  VAL A 507     103.875  91.493  67.630  1.00 80.73      A    C  
ANISOU 3900  CA  VAL A 507    10809  11509   8354    747   1331   -327  A    C  
ATOM   3901  C   VAL A 507     103.570  91.272  66.159  1.00 80.92      A    C  
ANISOU 3901  C   VAL A 507    10724  11549   8471    920   1277   -113  A    C  
ATOM   3902  O   VAL A 507     104.456  90.908  65.377  1.00 84.86      A    O  
ANISOU 3902  O   VAL A 507    11182  12123   8936    920   1158    -94  A    O  
ATOM   3903  CB  VAL A 507     103.655  90.166  68.399  1.00 77.48      A    C  
ANISOU 3903  CB  VAL A 507    10382  11278   7778    728   1105   -342  A    C  
ATOM   3904  CG1 VAL A 507     104.214  90.279  69.803  1.00 78.94      A    C  
ANISOU 3904  CG1 VAL A 507    10635  11541   7816    547   1112   -524  A    C  
ATOM   3905  CG2 VAL A 507     102.188  89.755  68.436  1.00 74.77      A    C  
ANISOU 3905  CG2 VAL A 507    10006  10926   7475    832   1108   -230  A    C  
ATOM   3906  N   LEU A 508     102.320  91.483  65.773  1.00 79.88      A    N  
ANISOU 3906  N   LEU A 508    10525  11388   8438   1060   1366     57  A    N  
ATOM   3907  CA  LEU A 508     101.950  91.325  64.379  1.00 79.50      A    C  
ANISOU 3907  CA  LEU A 508    10333  11436   8434   1206   1316    285  A    C  
ATOM   3908  C   LEU A 508     102.520  92.462  63.555  1.00 81.95      A    C  
ANISOU 3908  C   LEU A 508    10649  11597   8888   1275   1511    373  A    C  
ATOM   3909  O   LEU A 508     102.850  92.259  62.396  1.00 93.49      A    O  
ANISOU 3909  O   LEU A 508    12018  13164  10338   1335   1425    506  A    O  
ATOM   3910  CB  LEU A 508     100.436  91.234  64.194  1.00 78.77      A    C  
ANISOU 3910  CB  LEU A 508    10115  11439   8374   1330   1351    475  A    C  
ATOM   3911  CG  LEU A 508      99.760  90.061  64.918  1.00 77.79      A    C  
ANISOU 3911  CG  LEU A 508     9988  11459   8109   1248   1183    392  A    C  
ATOM   3912  CD1 LEU A 508      98.286  90.002  64.518  1.00 82.44      A    C  
ANISOU 3912  CD1 LEU A 508    10408  12204   8711   1352   1216    593  A    C  
ATOM   3913  CD2 LEU A 508     100.459  88.731  64.653  1.00 73.02      A    C  
ANISOU 3913  CD2 LEU A 508     9396  10997   7348   1146    948    304  A    C  
ATOM   3914  N   THR A 509     102.641  93.649  64.137  1.00 80.56      A    N  
ANISOU 3914  N   THR A 509    10596  11169   8842   1249   1800    290  A    N  
ATOM   3915  CA  THR A 509     103.287  94.756  63.440  1.00 80.56      A    C  
ANISOU 3915  CA  THR A 509    10646  10973   8989   1288   2046    343  A    C  
ATOM   3916  C   THR A 509     104.768  94.506  63.315  1.00 80.55      A    C  
ANISOU 3916  C   THR A 509    10706  11016   8884   1115   1917    154  A    C  
ATOM   3917  O   THR A 509     105.360  94.809  62.284  1.00 88.81      A    O  
ANISOU 3917  O   THR A 509    11723  12035   9984   1167   1954    253  A    O  
ATOM   3918  CB  THR A 509     103.134  96.070  64.197  1.00 82.66      A    C  
ANISOU 3918  CB  THR A 509    11073  10914   9417   1243   2455    239  A    C  
ATOM   3919  CG2 THR A 509     103.463  97.227  63.291  1.00 85.07      A    C  
ANISOU 3919  CG2 THR A 509    11423  10975   9924   1356   2786    384  A    C  
ATOM   3920  OG1 THR A 509     101.799  96.187  64.677  1.00 82.43      A    O  
ANISOU 3920  OG1 THR A 509    11005  10851   9463   1367   2567    352  A    O  
ATOM   3921  N   ALA A 510     105.363  93.964  64.372  1.00 77.44      A    N  
ANISOU 3921  N   ALA A 510    10375  10716   8332    914   1773    -94  A    N  
ATOM   3922  CA  ALA A 510     106.773  93.631  64.373  1.00 75.59      A    C  
ANISOU 3922  CA  ALA A 510    10155  10590   7974    754   1632   -257  A    C  
ATOM   3923  C   ALA A 510     107.051  92.531  63.362  1.00 74.01      A    C  
ANISOU 3923  C   ALA A 510     9832  10582   7705    855   1357   -122  A    C  
ATOM   3924  O   ALA A 510     108.092  92.507  62.715  1.00 75.42      A    O  
ANISOU 3924  O   ALA A 510     9995  10797   7863    812   1309   -149  A    O  
ATOM   3925  CB  ALA A 510     107.198  93.188  65.754  1.00 76.70      A    C  
ANISOU 3925  CB  ALA A 510    10337  10869   7935    558   1523   -480  A    C  
ATOM   3926  N   GLN A 511     106.114  91.615  63.212  1.00 72.87      A    N  
ANISOU 3926  N   GLN A 511     9606  10560   7519    963   1200      7  A    N  
ATOM   3927  CA  GLN A 511     106.256  90.573  62.226  1.00 71.25      A    C  
ANISOU 3927  CA  GLN A 511     9302  10525   7244   1018    994    111  A    C  
ATOM   3928  C   GLN A 511     106.264  91.174  60.836  1.00 70.23      A    C  
ANISOU 3928  C   GLN A 511     9100  10374   7207   1118   1081    293  A    C  
ATOM   3929  O   GLN A 511     107.046  90.771  60.011  1.00 71.27      A    O  
ANISOU 3929  O   GLN A 511     9196  10590   7293   1095    979    301  A    O  
ATOM   3930  CB  GLN A 511     105.113  89.583  62.371  1.00 70.90      A    C  
ANISOU 3930  CB  GLN A 511     9197  10610   7131   1064    875    186  A    C  
ATOM   3931  CG  GLN A 511     105.139  88.419  61.419  1.00 71.07      A    C  
ANISOU 3931  CG  GLN A 511     9136  10807   7057   1062    708    249  A    C  
ATOM   3932  CD  GLN A 511     104.118  87.399  61.835  1.00 72.07      A    C  
ANISOU 3932  CD  GLN A 511     9247  11038   7098   1040    631    249  A    C  
ATOM   3933  NE2 GLN A 511     104.270  86.182  61.370  1.00 79.16      A    N  
ANISOU 3933  NE2 GLN A 511    10133  12049   7895    978    524    222  A    N  
ATOM   3934  OE1 GLN A 511     103.206  87.703  62.571  1.00 70.80      A    O  
ANISOU 3934  OE1 GLN A 511     9097  10840   6963   1065    696    262  A    O  
ATOM   3935  N   ASP A 512     105.384  92.119  60.568  1.00 75.96      A    N  
ANISOU 3935  N   ASP A 512     9797  10998   8063   1245   1281    463  A    N  
ATOM   3936  CA  ASP A 512     105.255  92.658  59.228  1.00 84.84      A    C  
ANISOU 3936  CA  ASP A 512    10822  12146   9264   1382   1369    713  A    C  
ATOM   3937  C   ASP A 512     106.432  93.533  58.889  1.00 85.77      A    C  
ANISOU 3937  C   ASP A 512    11040  12077   9472   1338   1531    648  A    C  
ATOM   3938  O   ASP A 512     106.964  93.451  57.782  1.00100.44      A    O  
ANISOU 3938  O   ASP A 512    12836  14017  11309   1365   1479    751  A    O  
ATOM   3939  CB  ASP A 512     103.936  93.414  59.044  1.00 94.28      A    C  
ANISOU 3939  CB  ASP A 512    11927  13311  10582   1579   1566    982  A    C  
ATOM   3940  CG  ASP A 512     102.727  92.475  58.977  1.00107.08      A    C  
ANISOU 3940  CG  ASP A 512    13383  15219  12079   1613   1382   1098  A    C  
ATOM   3941  OD1 ASP A 512     102.859  91.277  59.353  1.00112.48      A    O  
ANISOU 3941  OD1 ASP A 512    14085  16042  12607   1465   1150    919  A    O  
ATOM   3942  OD2 ASP A 512     101.637  92.930  58.545  1.00125.57      A    O1-
ANISOU 3942  OD2 ASP A 512    15571  17659  14479   1787   1492   1381  A    O1-
ATOM   3943  N   GLN A 513     106.865  94.351  59.828  1.00 82.08      A    N  
ANISOU 3943  N   GLN A 513    10729  11374   9083   1236   1737    454  A    N  
ATOM   3944  CA  GLN A 513     108.001  95.235  59.573  1.00 85.31      A    C  
ANISOU 3944  CA  GLN A 513    11248  11598   9566   1141   1935    348  A    C  
ATOM   3945  C   GLN A 513     109.314  94.468  59.410  1.00 82.63      A    C  
ANISOU 3945  C   GLN A 513    10895  11424   9076    980   1695    171  A    C  
ATOM   3946  O   GLN A 513     110.185  94.879  58.652  1.00 79.00      A    O  
ANISOU 3946  O   GLN A 513    10454  10909   8650    947   1770    173  A    O  
ATOM   3947  CB  GLN A 513     108.146  96.223  60.711  1.00 90.47      A    C  
ANISOU 3947  CB  GLN A 513    12076  11999  10296    992   2231    126  A    C  
ATOM   3948  CG  GLN A 513     106.995  97.209  60.837  1.00 93.35      A    C  
ANISOU 3948  CG  GLN A 513    12489  12115  10864   1158   2579    295  A    C  
ATOM   3949  CD  GLN A 513     107.105  98.081  62.075  1.00 90.99      A    C  
ANISOU 3949  CD  GLN A 513    12385  11567  10618    955   2893     18  A    C  
ATOM   3950  NE2 GLN A 513     106.116  98.938  62.264  1.00 92.73      A    N  
ANISOU 3950  NE2 GLN A 513    12666  11532  11035   1099   3244    148  A    N  
ATOM   3951  OE1 GLN A 513     108.064  97.989  62.846  1.00 83.71      A    O  
ANISOU 3951  OE1 GLN A 513    11544  10707   9552    663   2837   -303  A    O  
ATOM   3952  N   ALA A 514     109.438  93.351  60.125  1.00 80.98      A    N  
ANISOU 3952  N   ALA A 514    10648  11408   8709    897   1432     42  A    N  
ATOM   3953  CA  ALA A 514     110.600  92.469  60.008  1.00 78.24      A    C  
ANISOU 3953  CA  ALA A 514    10260  11238   8229    794   1211    -78  A    C  
ATOM   3954  C   ALA A 514     110.578  91.740  58.680  1.00 74.16      A    C  
ANISOU 3954  C   ALA A 514     9640  10846   7689    899   1065     93  A    C  
ATOM   3955  O   ALA A 514     111.597  91.639  58.021  1.00 78.12      A    O  
ANISOU 3955  O   ALA A 514    10124  11387   8166    848   1026     57  A    O  
ATOM   3956  CB  ALA A 514     110.627  91.445  61.138  1.00 76.43      A    C  
ANISOU 3956  CB  ALA A 514    10013  11168   7856    730   1015   -199  A    C  
ATOM   3957  N   LEU A 515     109.429  91.192  58.308  1.00 68.94      A    N  
ANISOU 3957  N   LEU A 515     8902  10278   7013   1014    986    261  A    N  
ATOM   3958  CA  LEU A 515     109.311  90.516  57.053  1.00 66.83      A    C  
ANISOU 3958  CA  LEU A 515     8528  10176   6685   1059    868    403  A    C  
ATOM   3959  C   LEU A 515     109.596  91.495  55.923  1.00 69.46      A    C  
ANISOU 3959  C   LEU A 515     8837  10448   7105   1124   1016    564  A    C  
ATOM   3960  O   LEU A 515     110.227  91.130  54.904  1.00 70.43      A    O  
ANISOU 3960  O   LEU A 515     8911  10679   7171   1094    938    599  A    O  
ATOM   3961  CB  LEU A 515     107.937  89.889  56.898  1.00 66.93      A    C  
ANISOU 3961  CB  LEU A 515     8444  10347   6636   1121    791    544  A    C  
ATOM   3962  CG  LEU A 515     107.853  88.398  57.189  1.00 69.04      A    C  
ANISOU 3962  CG  LEU A 515     8708  10754   6766   1031    610    427  A    C  
ATOM   3963  CD1 LEU A 515     108.574  88.033  58.456  1.00 75.36      A    C  
ANISOU 3963  CD1 LEU A 515     9617  11457   7559    973    574    226  A    C  
ATOM   3964  CD2 LEU A 515     106.403  87.957  57.280  1.00 72.28      A    C  
ANISOU 3964  CD2 LEU A 515     9044  11299   7119   1052    581    525  A    C  
ATOM   3965  N   ALA A 516     109.144  92.733  56.082  1.00 70.33      A    N  
ANISOU 3965  N   ALA A 516     8990  10368   7361   1219   1260    670  A    N  
ATOM   3966  CA  ALA A 516     109.331  93.719  55.024  1.00 74.93      A    C  
ANISOU 3966  CA  ALA A 516     9558  10859   8052   1320   1457    874  A    C  
ATOM   3967  C   ALA A 516     110.765  94.142  54.965  1.00 76.33      A    C  
ANISOU 3967  C   ALA A 516     9850  10891   8257   1184   1538    683  A    C  
ATOM   3968  O   ALA A 516     111.316  94.392  53.879  1.00 79.48      A    O  
ANISOU 3968  O   ALA A 516    10223  11305   8669   1207   1581    793  A    O  
ATOM   3969  CB  ALA A 516     108.452  94.920  55.243  1.00 78.39      A    C  
ANISOU 3969  CB  ALA A 516    10027  11088   8670   1485   1764   1061  A    C  
ATOM   3970  N   LEU A 517     111.384  94.196  56.135  1.00 74.85      A    N  
ANISOU 3970  N   LEU A 517     9774  10609   8057   1021   1554    395  A    N  
ATOM   3971  CA  LEU A 517     112.776  94.589  56.203  1.00 74.05      A    C  
ANISOU 3971  CA  LEU A 517     9755  10430   7949    845   1628    183  A    C  
ATOM   3972  C   LEU A 517     113.707  93.520  55.604  1.00 75.23      A    C  
ANISOU 3972  C   LEU A 517     9817  10803   7965    782   1366    127  A    C  
ATOM   3973  O   LEU A 517     114.636  93.853  54.875  1.00 81.08      A    O  
ANISOU 3973  O   LEU A 517    10571  11514   8721    724   1429    104  A    O  
ATOM   3974  CB  LEU A 517     113.154  94.863  57.638  1.00 71.57      A    C  
ANISOU 3974  CB  LEU A 517     9535  10058   7599    655   1694    -97  A    C  
ATOM   3975  CG  LEU A 517     114.448  95.630  57.797  1.00 70.49      A    C  
ANISOU 3975  CG  LEU A 517     9488   9835   7459    428   1867   -326  A    C  
ATOM   3976  CD1 LEU A 517     114.283  96.967  57.098  1.00 71.05      A    C  
ANISOU 3976  CD1 LEU A 517     9681   9589   7725    485   2253   -214  A    C  
ATOM   3977  CD2 LEU A 517     114.782  95.762  59.286  1.00 70.61      A    C  
ANISOU 3977  CD2 LEU A 517     9551   9910   7365    194   1890   -612  A    C  
ATOM   3978  N   GLU A 518     113.456  92.246  55.895  1.00 72.36      A    N  
ANISOU 3978  N   GLU A 518     9373  10636   7483    795   1110    105  A    N  
ATOM   3979  CA  GLU A 518     114.246  91.174  55.321  1.00 72.42      A    C  
ANISOU 3979  CA  GLU A 518     9310  10816   7387    754    917     63  A    C  
ATOM   3980  C   GLU A 518     114.147  91.171  53.795  1.00 72.69      A    C  
ANISOU 3980  C   GLU A 518     9286  10905   7427    819    923    249  A    C  
ATOM   3981  O   GLU A 518     115.135  90.920  53.084  1.00 70.26      A    O  
ANISOU 3981  O   GLU A 518     8959  10651   7085    756    886    202  A    O  
ATOM   3982  CB  GLU A 518     113.778  89.820  55.844  1.00 75.98      A    C  
ANISOU 3982  CB  GLU A 518     9714  11413   7740    779    723     39  A    C  
ATOM   3983  CG  GLU A 518     114.252  89.473  57.238  1.00 79.35      A    C  
ANISOU 3983  CG  GLU A 518    10161  11874   8112    713    664   -129  A    C  
ATOM   3984  CD  GLU A 518     114.214  87.974  57.517  1.00 85.42      A    C  
ANISOU 3984  CD  GLU A 518    10889  12769   8794    751    505   -134  A    C  
ATOM   3985  OE1 GLU A 518     114.644  87.163  56.663  1.00 84.39      A    O  
ANISOU 3985  OE1 GLU A 518    10723  12702   8637    760    450   -111  A    O  
ATOM   3986  OE2 GLU A 518     113.774  87.598  58.623  1.00102.05      A    O1-
ANISOU 3986  OE2 GLU A 518    13012  14897  10863    768    465   -165  A    O1-
ATOM   3987  N   LYS A 519     112.953  91.429  53.284  1.00 73.60      A    N  
ANISOU 3987  N   LYS A 519     9351  11044   7567    941    968    475  A    N  
ATOM   3988  CA  LYS A 519     112.778  91.470  51.847  1.00 77.40      A    C  
ANISOU 3988  CA  LYS A 519     9743  11650   8013    997    970    691  A    C  
ATOM   3989  C   LYS A 519     113.648  92.584  51.256  1.00 77.60      A    C  
ANISOU 3989  C   LYS A 519     9832  11509   8141    998   1166    730  A    C  
ATOM   3990  O   LYS A 519     114.362  92.377  50.260  1.00 76.37      A    O  
ANISOU 3990  O   LYS A 519     9642  11441   7931    949   1128    753  A    O  
ATOM   3991  CB  LYS A 519     111.307  91.632  51.492  1.00 78.96      A    C  
ANISOU 3991  CB  LYS A 519     9830  11973   8198   1134    990    966  A    C  
ATOM   3992  CG  LYS A 519     111.033  92.106  50.075  1.00 85.14      A    C  
ANISOU 3992  CG  LYS A 519    10492  12902   8954   1229   1055   1275  A    C  
ATOM   3993  CD  LYS A 519     111.109  90.999  49.049  1.00 91.45      A    C  
ANISOU 3993  CD  LYS A 519    11173  14029   9545   1108    859   1287  A    C  
ATOM   3994  CE  LYS A 519     110.557  91.497  47.721  1.00103.03      A    C  
ANISOU 3994  CE  LYS A 519    12469  15738  10938   1207    910   1652  A    C  
ATOM   3995  NZ  LYS A 519     110.449  90.435  46.678  1.00109.59      A    N1+
ANISOU 3995  NZ  LYS A 519    13162  16960  11515   1039    733   1667  A    N1+
ATOM   3996  N   GLN A 520     113.622  93.757  51.873  1.00 76.89      A    N  
ANISOU 3996  N   GLN A 520     9850  11164   8201   1032   1408    716  A    N  
ATOM   3997  CA  GLN A 520     114.356  94.858  51.286  1.00 82.77      A    C  
ANISOU 3997  CA  GLN A 520    10678  11711   9056   1026   1659    759  A    C  
ATOM   3998  C   GLN A 520     115.870  94.716  51.438  1.00 78.86      A    C  
ANISOU 3998  C   GLN A 520    10247  11196   8519    816   1624    469  A    C  
ATOM   3999  O   GLN A 520     116.626  95.237  50.625  1.00 83.45      A    O  
ANISOU 3999  O   GLN A 520    10864  11706   9138    782   1751    499  A    O  
ATOM   4000  CB  GLN A 520     113.871  96.205  51.809  1.00 87.16      A    C  
ANISOU 4000  CB  GLN A 520    11356  11955   9803   1108   2012    828  A    C  
ATOM   4001  CG  GLN A 520     114.396  96.561  53.169  1.00 92.93      A    C  
ANISOU 4001  CG  GLN A 520    12230  12513  10564    914   2119    487  A    C  
ATOM   4002  CD  GLN A 520     114.705  98.053  53.308  1.00 99.46      A    C  
ANISOU 4002  CD  GLN A 520    13243  12973  11574    864   2570    443  A    C  
ATOM   4003  NE2 GLN A 520     113.782  98.800  53.938  1.00 98.07      A    N  
ANISOU 4003  NE2 GLN A 520    13151  12572  11537    956   2834    512  A    N  
ATOM   4004  OE1 GLN A 520     115.776  98.520  52.890  1.00 98.51      A    O  
ANISOU 4004  OE1 GLN A 520    13201  12755  11470    726   2708    329  A    O  
ATOM   4005  N   LEU A 521     116.312  94.019  52.464  1.00 74.16      A    N  
ANISOU 4005  N   LEU A 521     9649  10686   7839    687   1461    215  A    N  
ATOM   4006  CA  LEU A 521     117.729  93.826  52.663  1.00 74.37      A    C  
ANISOU 4006  CA  LEU A 521     9683  10769   7803    502   1414    -27  A    C  
ATOM   4007  C   LEU A 521     118.260  92.693  51.804  1.00 76.31      A    C  
ANISOU 4007  C   LEU A 521     9823  11222   7946    508   1195     -3  A    C  
ATOM   4008  O   LEU A 521     119.429  92.718  51.377  1.00 77.84      A    O  
ANISOU 4008  O   LEU A 521    10009  11448   8118    400   1209   -107  A    O  
ATOM   4009  CB  LEU A 521     118.008  93.523  54.115  1.00 74.95      A    C  
ANISOU 4009  CB  LEU A 521     9757  10914   7805    380   1333   -257  A    C  
ATOM   4010  CG  LEU A 521     117.692  94.667  55.074  1.00 77.34      A    C  
ANISOU 4010  CG  LEU A 521    10182  11021   8182    291   1582   -364  A    C  
ATOM   4011  CD1 LEU A 521     118.022  94.276  56.512  1.00 77.23      A    C  
ANISOU 4011  CD1 LEU A 521    10134  11167   8040    140   1469   -587  A    C  
ATOM   4012  CD2 LEU A 521     118.485  95.885  54.651  1.00 81.39      A    C  
ANISOU 4012  CD2 LEU A 521    10805  11337   8778    150   1884   -451  A    C  
ATOM   4013  N   PHE A 522     117.401  91.704  51.546  1.00 75.26      A    N  
ANISOU 4013  N   PHE A 522     9615  11231   7748    609   1023    121  A    N  
ATOM   4014  CA  PHE A 522     117.737  90.610  50.631  1.00 71.40      A    C  
ANISOU 4014  CA  PHE A 522     9048  10917   7162    593    872    141  A    C  
ATOM   4015  C   PHE A 522     117.845  91.114  49.209  1.00 69.43      A    C  
ANISOU 4015  C   PHE A 522     8782  10681   6917    608    958    308  A    C  
ATOM   4016  O   PHE A 522     118.793  90.790  48.519  1.00 65.62      A    O  
ANISOU 4016  O   PHE A 522     8281  10257   6392    528    933    242  A    O  
ATOM   4017  CB  PHE A 522     116.684  89.507  50.701  1.00 70.64      A    C  
ANISOU 4017  CB  PHE A 522     8897  10958   6983    646    727    207  A    C  
ATOM   4018  CG  PHE A 522     117.094  88.238  50.022  1.00 67.75      A    C  
ANISOU 4018  CG  PHE A 522     8487  10739   6515    581    620    152  A    C  
ATOM   4019  CD1 PHE A 522     117.973  87.371  50.628  1.00 66.87      A    C  
ANISOU 4019  CD1 PHE A 522     8378  10633   6393    545    565    -17  A    C  
ATOM   4020  CD2 PHE A 522     116.597  87.920  48.791  1.00 69.19      A    C  
ANISOU 4020  CD2 PHE A 522     8613  11070   6606    551    601    281  A    C  
ATOM   4021  CE1 PHE A 522     118.355  86.207  50.017  1.00 66.68      A    C  
ANISOU 4021  CE1 PHE A 522     8334  10692   6306    495    532    -68  A    C  
ATOM   4022  CE2 PHE A 522     116.961  86.753  48.172  1.00 70.34      A    C  
ANISOU 4022  CE2 PHE A 522     8741  11331   6654    448    551    193  A    C  
ATOM   4023  CZ  PHE A 522     117.843  85.892  48.790  1.00 68.60      A    C  
ANISOU 4023  CZ  PHE A 522     8556  11045   6462    427    537     12  A    C  
ATOM   4024  N   ASP A 523     116.872  91.914  48.783  1.00 72.66      A    N  
ANISOU 4024  N   ASP A 523     9186  11044   7375    726   1073    549  A    N  
ATOM   4025  CA  ASP A 523     116.923  92.549  47.459  1.00 78.85      A    C  
ANISOU 4025  CA  ASP A 523     9941  11852   8164    775   1187    775  A    C  
ATOM   4026  C   ASP A 523     118.123  93.497  47.346  1.00 73.46      A    C  
ANISOU 4026  C   ASP A 523     9368  10956   7586    702   1383    671  A    C  
ATOM   4027  O   ASP A 523     118.615  93.781  46.272  1.00 72.28      A    O  
ANISOU 4027  O   ASP A 523     9210  10828   7423    689   1453    775  A    O  
ATOM   4028  CB  ASP A 523     115.628  93.340  47.178  1.00 91.59      A    C  
ANISOU 4028  CB  ASP A 523    11507  13459   9832    966   1315   1110  A    C  
ATOM   4029  CG  ASP A 523     114.356  92.434  47.040  1.00100.40      A    C  
ANISOU 4029  CG  ASP A 523    12470  14872  10804   1012   1125   1250  A    C  
ATOM   4030  OD1 ASP A 523     114.425  91.203  47.298  1.00 98.77      A    O  
ANISOU 4030  OD1 ASP A 523    12240  14812  10476    885    925   1054  A    O  
ATOM   4031  OD2 ASP A 523     113.279  92.977  46.665  1.00105.25      A    O1-
ANISOU 4031  OD2 ASP A 523    12985  15579  11426   1175   1202   1569  A    O1-
ATOM   4032  N   GLY A 524     118.579  93.998  48.478  1.00 72.23      A    N  
ANISOU 4032  N   GLY A 524     9313  10613   7516    624   1486    454  A    N  
ATOM   4033  CA  GLY A 524     119.724  94.867  48.523  1.00 70.32      A    C  
ANISOU 4033  CA  GLY A 524     9177  10194   7348    489   1688    295  A    C  
ATOM   4034  C   GLY A 524     120.975  94.093  48.251  1.00 69.21      A    C  
ANISOU 4034  C   GLY A 524     8977  10213   7105    341   1533    101  A    C  
ATOM   4035  O   GLY A 524     121.844  94.591  47.570  1.00 70.96      A    O  
ANISOU 4035  O   GLY A 524     9236  10373   7350    257   1661     73  A    O  
ATOM   4036  N   VAL A 525     121.107  92.887  48.799  1.00 68.78      A    N  
ANISOU 4036  N   VAL A 525     8833  10345   6952    316   1291    -25  A    N  
ATOM   4037  CA  VAL A 525     122.365  92.159  48.612  1.00 71.84      A    C  
ANISOU 4037  CA  VAL A 525     9154  10874   7266    201   1184   -191  A    C  
ATOM   4038  C   VAL A 525     122.360  91.503  47.252  1.00 73.67      A    C  
ANISOU 4038  C   VAL A 525     9336  11216   7438    236   1112    -62  A    C  
ATOM   4039  O   VAL A 525     123.417  91.246  46.693  1.00 81.89      A    O  
ANISOU 4039  O   VAL A 525    10347  12316   8449    146   1108   -153  A    O  
ATOM   4040  CB  VAL A 525     122.684  91.124  49.723  1.00 73.38      A    C  
ANISOU 4040  CB  VAL A 525     9266  11221   7393    182   1006   -348  A    C  
ATOM   4041  CG1 VAL A 525     122.576  91.753  51.106  1.00 76.48      A    C  
ANISOU 4041  CG1 VAL A 525     9691  11567   7801    122   1063   -468  A    C  
ATOM   4042  CG2 VAL A 525     121.762  89.939  49.654  1.00 76.80      A    C  
ANISOU 4042  CG2 VAL A 525     9658  11743   7778    302    849   -245  A    C  
ATOM   4043  N   LEU A 526     121.174  91.234  46.711  1.00 74.27      A    N  
ANISOU 4043  N   LEU A 526     9389  11352   7478    343   1061    146  A    N  
ATOM   4044  CA  LEU A 526     121.053  90.788  45.319  1.00 72.88      A    C  
ANISOU 4044  CA  LEU A 526     9157  11327   7207    333   1022    287  A    C  
ATOM   4045  C   LEU A 526     121.463  91.890  44.342  1.00 75.02      A    C  
ANISOU 4045  C   LEU A 526     9468  11514   7519    330   1199    427  A    C  
ATOM   4046  O   LEU A 526     122.084  91.610  43.337  1.00 76.79      A    O  
ANISOU 4046  O   LEU A 526     9664  11837   7674    253   1191    432  A    O  
ATOM   4047  CB  LEU A 526     119.645  90.317  45.001  1.00 70.66      A    C  
ANISOU 4047  CB  LEU A 526     8808  11206   6832    408    932    481  A    C  
ATOM   4048  CG  LEU A 526     119.272  88.959  45.596  1.00 70.59      A    C  
ANISOU 4048  CG  LEU A 526     8768  11304   6746    371    777    343  A    C  
ATOM   4049  CD1 LEU A 526     117.829  88.611  45.232  1.00 70.63      A    C  
ANISOU 4049  CD1 LEU A 526     8696  11500   6637    399    712    526  A    C  
ATOM   4050  CD2 LEU A 526     120.234  87.865  45.142  1.00 70.97      A    C  
ANISOU 4050  CD2 LEU A 526     8807  11428   6728    247    733    168  A    C  
ATOM   4051  N   LYS A 527     121.131  93.135  44.658  1.00 77.60      A    N  
ANISOU 4051  N   LYS A 527     9873  11638   7973    412   1394    536  A    N  
ATOM   4052  CA  LYS A 527     121.626  94.289  43.919  1.00 83.00      A    C  
ANISOU 4052  CA  LYS A 527    10635  12160   8740    415   1639    652  A    C  
ATOM   4053  C   LYS A 527     123.151  94.278  43.861  1.00 82.83      A    C  
ANISOU 4053  C   LYS A 527    10656  12095   8720    226   1675    384  A    C  
ATOM   4054  O   LYS A 527     123.754  94.633  42.851  1.00 81.43      A    O  
ANISOU 4054  O   LYS A 527    10499  11905   8533    182   1780    455  A    O  
ATOM   4055  CB  LYS A 527     121.194  95.563  44.639  1.00 92.25      A    C  
ANISOU 4055  CB  LYS A 527    11928  13037  10082    497   1907    710  A    C  
ATOM   4056  CG  LYS A 527     120.854  96.740  43.755  1.00100.81      A    C  
ANISOU 4056  CG  LYS A 527    13075  13955  11272    641   2204   1037  A    C  
ATOM   4057  CD  LYS A 527     119.379  96.683  43.407  1.00112.32      A    C  
ANISOU 4057  CD  LYS A 527    14414  15559  12701    880   2157   1415  A    C  
ATOM   4058  CE  LYS A 527     119.008  97.732  42.363  1.00124.16      A    C  
ANISOU 4058  CE  LYS A 527    15919  16974  14281   1080   2439   1840  A    C  
ATOM   4059  NZ  LYS A 527     117.650  97.477  41.794  1.00127.02      A    N1+
ANISOU 4059  NZ  LYS A 527    16080  17641  14540   1299   2327   2255  A    N1+
ATOM   4060  N   ASN A 528     123.766  93.904  44.982  1.00 84.46      A    N  
ANISOU 4060  N   ASN A 528    10858  12303   8927    116   1595     97  A    N  
ATOM   4061  CA  ASN A 528     125.218  93.849  45.105  1.00 86.27      A    C  
ANISOU 4061  CA  ASN A 528    11080  12559   9139    -68   1613   -158  A    C  
ATOM   4062  C   ASN A 528     125.830  92.658  44.422  1.00 80.66      A    C  
ANISOU 4062  C   ASN A 528    10260  12059   8325   -102   1433   -207  A    C  
ATOM   4063  O   ASN A 528     126.861  92.766  43.771  1.00 80.86      A    O  
ANISOU 4063  O   ASN A 528    10280  12104   8336   -212   1496   -284  A    O  
ATOM   4064  CB  ASN A 528     125.633  93.814  46.565  1.00 93.06      A    C  
ANISOU 4064  CB  ASN A 528    11919  13441   9999   -171   1577   -407  A    C  
ATOM   4065  CG  ASN A 528     125.964  95.183  47.082  1.00106.84      A    C  
ANISOU 4065  CG  ASN A 528    13791  14979  11824   -313   1856   -528  A    C  
ATOM   4066  ND2 ASN A 528     126.945  95.256  47.991  1.00120.68      A    N  
ANISOU 4066  ND2 ASN A 528    15496  16840  13517   -523   1859   -805  A    N  
ATOM   4067  OD1 ASN A 528     125.357  96.176  46.665  1.00109.70      A    O  
ANISOU 4067  OD1 ASN A 528    14285  15098  12294   -244   2096   -368  A    O  
ATOM   4068  N   LEU A 529     125.215  91.508  44.596  1.00 73.43      A    N  
ANISOU 4068  N   LEU A 529     9270  11286   7342    -23   1239   -177  A    N  
ATOM   4069  CA  LEU A 529     125.702  90.333  43.936  1.00 71.19      A    C  
ANISOU 4069  CA  LEU A 529     8911  11161   6975    -62   1129   -228  A    C  
ATOM   4070  C   LEU A 529     125.665  90.483  42.426  1.00 74.10      A    C  
ANISOU 4070  C   LEU A 529     9293  11580   7280    -96   1186    -79  A    C  
ATOM   4071  O   LEU A 529     126.616  90.093  41.720  1.00 74.74      A    O  
ANISOU 4071  O   LEU A 529     9348  11726   7322   -196   1202   -170  A    O  
ATOM   4072  CB  LEU A 529     124.848  89.166  44.321  1.00 68.08      A    C  
ANISOU 4072  CB  LEU A 529     8475  10864   6527     14    983   -209  A    C  
ATOM   4073  CG  LEU A 529     125.200  88.577  45.657  1.00 66.15      A    C  
ANISOU 4073  CG  LEU A 529     8185  10632   6313     47    909   -359  A    C  
ATOM   4074  CD1 LEU A 529     124.090  87.616  46.041  1.00 66.07      A    C  
ANISOU 4074  CD1 LEU A 529     8174  10662   6267    133    811   -304  A    C  
ATOM   4075  CD2 LEU A 529     126.539  87.868  45.584  1.00 66.09      A    C  
ANISOU 4075  CD2 LEU A 529     8099  10709   6302     -6    908   -503  A    C  
ATOM   4076  N   ARG A 530     124.571  91.051  41.927  1.00 73.51      A    N  
ANISOU 4076  N   ARG A 530     9239  11501   7186     -9   1226    169  A    N  
ATOM   4077  CA  ARG A 530     124.409  91.190  40.493  1.00 75.49      A    C  
ANISOU 4077  CA  ARG A 530     9468  11875   7338    -32   1268    368  A    C  
ATOM   4078  C   ARG A 530     125.434  92.140  39.900  1.00 77.79      A    C  
ANISOU 4078  C   ARG A 530     9827  12036   7693    -94   1449    366  A    C  
ATOM   4079  O   ARG A 530     125.829  91.993  38.747  1.00 83.04      A    O  
ANISOU 4079  O   ARG A 530    10470  12816   8264   -169   1470    430  A    O  
ATOM   4080  CB  ARG A 530     122.985  91.618  40.133  1.00 75.08      A    C  
ANISOU 4080  CB  ARG A 530     9377  11914   7237    104   1272    693  A    C  
ATOM   4081  CG  ARG A 530     121.961  90.506  40.339  1.00 73.74      A    C  
ANISOU 4081  CG  ARG A 530     9119  11959   6939    100   1090    699  A    C  
ATOM   4082  CD  ARG A 530     120.641  90.807  39.639  1.00 75.67      A    C  
ANISOU 4082  CD  ARG A 530     9258  12428   7062    189   1075   1048  A    C  
ATOM   4083  NE  ARG A 530     120.121  92.095  40.062  1.00 76.53      A    N  
ANISOU 4083  NE  ARG A 530     9403  12346   7327    392   1226   1273  A    N  
ATOM   4084  CZ  ARG A 530     119.308  92.277  41.094  1.00 74.88      A    C  
ANISOU 4084  CZ  ARG A 530     9205  12034   7210    511   1219   1290  A    C  
ATOM   4085  NH1 ARG A 530     118.897  91.224  41.793  1.00 74.77      A    N1+
ANISOU 4085  NH1 ARG A 530     9162  12112   7132    449   1047   1109  A    N1+
ATOM   4086  NH2 ARG A 530     118.919  93.517  41.421  1.00 73.49      A    N  
ANISOU 4086  NH2 ARG A 530     9084  11638   7199    691   1421   1488  A    N  
ATOM   4087  N   THR A 531     125.896  93.108  40.672  1.00 77.76      A    N  
ANISOU 4087  N   THR A 531     9911  11798   7832    -96   1601    272  A    N  
ATOM   4088  CA  THR A 531     126.956  93.972  40.171  1.00 80.89      A    C  
ANISOU 4088  CA  THR A 531    10386  12057   8287   -199   1806    219  A    C  
ATOM   4089  C   THR A 531     128.298  93.246  40.276  1.00 78.12      A    C  
ANISOU 4089  C   THR A 531     9979  11804   7898   -368   1725    -80  A    C  
ATOM   4090  O   THR A 531     129.194  93.499  39.490  1.00 80.99      A    O  
ANISOU 4090  O   THR A 531    10362  12160   8248   -476   1827   -120  A    O  
ATOM   4091  CB  THR A 531     126.981  95.319  40.915  1.00 84.73      A    C  
ANISOU 4091  CB  THR A 531    11008  12253   8932   -196   2063    194  A    C  
ATOM   4092  CG2 THR A 531     125.628  96.138  40.679  1.00 83.86      A    C  
ANISOU 4092  CG2 THR A 531    10952  12015   8893     24   2212    558  A    C  
ATOM   4093  OG1 THR A 531     127.204  95.073  42.310  1.00 86.66      A    O  
ANISOU 4093  OG1 THR A 531    11235  12490   9203   -267   1983    -71  A    O  
ATOM   4094  N   ALA A 532     128.420  92.328  41.234  1.00 75.79      A    N  
ANISOU 4094  N   ALA A 532     9042  10227   9528   -377   1051   -586  A    N  
ATOM   4095  CA  ALA A 532     129.638  91.534  41.407  1.00 74.26      A    C  
ANISOU 4095  CA  ALA A 532     8760  10159   9294   -461    946   -719  A    C  
ATOM   4096  C   ALA A 532     129.602  90.273  40.583  1.00 69.05      A    C  
ANISOU 4096  C   ALA A 532     8154   9580   8500   -357    775   -525  A    C  
ATOM   4097  O   ALA A 532     130.356  89.339  40.822  1.00 67.12      A    O  
ANISOU 4097  O   ALA A 532     7844   9477   8180   -394    634   -590  A    O  
ATOM   4098  CB  ALA A 532     129.838  91.185  42.875  1.00 76.55      A    C  
ANISOU 4098  CB  ALA A 532     8913  10683   9490   -541    783   -925  A    C  
ATOM   4099  N   LEU A 533     128.739  90.261  39.591  1.00 68.39      A    N  
ANISOU 4099  N   LEU A 533     8177   9421   8385   -218    800   -301  A    N  
ATOM   4100  CA  LEU A 533     128.579  89.104  38.713  1.00 68.87      A    C  
ANISOU 4100  CA  LEU A 533     8272   9574   8320   -116    651   -141  A    C  
ATOM   4101  C   LEU A 533     129.806  88.767  37.803  1.00 70.62      A    C  
ANISOU 4101  C   LEU A 533     8505   9751   8576   -136    710   -138  A    C  
ATOM   4102  O   LEU A 533     130.060  87.605  37.525  1.00 70.45      A    O  
ANISOU 4102  O   LEU A 533     8461   9847   8457   -120    552   -104  A    O  
ATOM   4103  CB  LEU A 533     127.370  89.340  37.841  1.00 68.28      A    C  
ANISOU 4103  CB  LEU A 533     8279   9471   8193     51    681     63  A    C  
ATOM   4104  CG  LEU A 533     126.377  88.238  37.589  1.00 66.97      A    C  
ANISOU 4104  CG  LEU A 533     8096   9473   7874    146    475    161  A    C  
ATOM   4105  CD1 LEU A 533     126.115  87.497  38.855  1.00 67.59      A    C  
ANISOU 4105  CD1 LEU A 533     8104   9666   7909     57    308     55  A    C  
ATOM   4106  CD2 LEU A 533     125.094  88.874  37.074  1.00 69.73      A    C  
ANISOU 4106  CD2 LEU A 533     8490   9816   8186    300    532    298  A    C  
ATOM   4107  N   PRO A 534     130.565  89.778  37.340  1.00 70.85      A    N  
ANISOU 4107  N   PRO A 534     8568   9592   8759   -174    964   -179  A    N  
ATOM   4108  CA  PRO A 534     131.817  89.459  36.696  1.00 71.38      A    C  
ANISOU 4108  CA  PRO A 534     8628   9618   8874   -221   1025   -218  A    C  
ATOM   4109  C   PRO A 534     132.740  88.563  37.518  1.00 73.37      A    C  
ANISOU 4109  C   PRO A 534     8758  10034   9083   -349    847   -405  A    C  
ATOM   4110  O   PRO A 534     133.226  87.574  36.989  1.00 72.48      A    O  
ANISOU 4110  O   PRO A 534     8644   9997   8896   -325    738   -353  A    O  
ATOM   4111  CB  PRO A 534     132.440  90.831  36.479  1.00 73.57      A    C  
ANISOU 4111  CB  PRO A 534     8932   9646   9371   -284   1366   -300  A    C  
ATOM   4112  CG  PRO A 534     131.260  91.691  36.226  1.00 74.33      A    C  
ANISOU 4112  CG  PRO A 534     9123   9633   9483   -151   1496   -135  A    C  
ATOM   4113  CD  PRO A 534     130.262  91.213  37.229  1.00 73.11      A    C  
ANISOU 4113  CD  PRO A 534     8912   9668   9196   -156   1240   -164  A    C  
ATOM   4114  N   GLN A 535     132.998  88.901  38.781  1.00 80.57      A    N  
ANISOU 4114  N   GLN A 535     9563  11021  10030   -465    826   -622  A    N  
ATOM   4115  CA  GLN A 535     133.968  88.124  39.579  1.00 85.92      A    C  
ANISOU 4115  CA  GLN A 535    10108  11892  10645   -549    676   -802  A    C  
ATOM   4116  C   GLN A 535     133.407  86.766  39.838  1.00 78.36      A    C  
ANISOU 4116  C   GLN A 535     9156  11114   9502   -456    422   -667  A    C  
ATOM   4117  O   GLN A 535     134.159  85.825  39.968  1.00 81.23      A    O  
ANISOU 4117  O   GLN A 535     9459  11603   9798   -463    308   -701  A    O  
ATOM   4118  CB  GLN A 535     134.304  88.770  40.921  1.00 98.13      A    C  
ANISOU 4118  CB  GLN A 535    11511  13548  12225   -661    696  -1079  A    C  
ATOM   4119  CG  GLN A 535     134.989  90.134  40.842  1.00109.48      A    C  
ANISOU 4119  CG  GLN A 535    12899  14809  13887   -799    984  -1301  A    C  
ATOM   4120  CD  GLN A 535     133.996  91.307  40.744  1.00119.79      A    C  
ANISOU 4120  CD  GLN A 535    14294  15909  15311   -784   1179  -1237  A    C  
ATOM   4121  NE2 GLN A 535     134.365  92.426  41.364  1.00131.74      A    N  
ANISOU 4121  NE2 GLN A 535    15707  17357  16992   -924   1381  -1511  A    N  
ATOM   4122  OE1 GLN A 535     132.910  91.208  40.137  1.00115.61      A    O  
ANISOU 4122  OE1 GLN A 535    13905  15296  14723   -646   1154   -963  A    O  
ATOM   4123  N   LEU A 536     132.085  86.674  39.916  1.00 73.11      A    N  
ANISOU 4123  N   LEU A 536     8555  10450   8771   -368    357   -520  A    N  
ATOM   4124  CA  LEU A 536     131.415  85.397  40.151  1.00 71.53      A    C  
ANISOU 4124  CA  LEU A 536     8360  10385   8432   -289    164   -402  A    C  
ATOM   4125  C   LEU A 536     131.521  84.420  38.994  1.00 68.48      A    C  
ANISOU 4125  C   LEU A 536     8022   9985   8010   -232    113   -268  A    C  
ATOM   4126  O   LEU A 536     131.792  83.241  39.197  1.00 62.71      A    O  
ANISOU 4126  O   LEU A 536     7255   9360   7211   -218     -5   -255  A    O  
ATOM   4127  CB  LEU A 536     129.930  85.619  40.468  1.00 74.45      A    C  
ANISOU 4127  CB  LEU A 536     8775  10745   8766   -223    135   -309  A    C  
ATOM   4128  CG  LEU A 536     129.572  86.073  41.901  1.00 78.43      A    C  
ANISOU 4128  CG  LEU A 536     9221  11333   9246   -255    112   -420  A    C  
ATOM   4129  CD1 LEU A 536     128.104  86.476  41.989  1.00 78.87      A    C  
ANISOU 4129  CD1 LEU A 536     9331  11336   9295   -196    120   -323  A    C  
ATOM   4130  CD2 LEU A 536     129.899  85.036  42.979  1.00 74.84      A    C  
ANISOU 4130  CD2 LEU A 536     8689  11073   8674   -234    -27   -460  A    C  
ATOM   4131  N   GLN A 537     131.258  84.918  37.788  1.00 71.58      A    N  
ANISOU 4131  N   GLN A 537     8494  10259   8443   -180    218   -166  A    N  
ATOM   4132  CA  GLN A 537     131.391  84.138  36.555  1.00 71.49      A    C  
ANISOU 4132  CA  GLN A 537     8518  10256   8386   -115    188    -56  A    C  
ATOM   4133  C   GLN A 537     132.847  83.679  36.324  1.00 73.40      A    C  
ANISOU 4133  C   GLN A 537     8724  10500   8662   -187    199   -133  A    C  
ATOM   4134  O   GLN A 537     133.059  82.578  35.826  1.00 70.64      A    O  
ANISOU 4134  O   GLN A 537     8366  10218   8255   -163    107    -89  A    O  
ATOM   4135  CB  GLN A 537     130.938  84.978  35.368  1.00 74.95      A    C  
ANISOU 4135  CB  GLN A 537     9042  10595   8840    -11    331     72  A    C  
ATOM   4136  CG  GLN A 537     129.431  85.040  35.192  1.00 77.52      A    C  
ANISOU 4136  CG  GLN A 537     9388  10981   9086    107    280    177  A    C  
ATOM   4137  CD  GLN A 537     128.827  83.808  34.515  1.00 80.79      A    C  
ANISOU 4137  CD  GLN A 537     9767  11548   9382    180    135    228  A    C  
ATOM   4138  NE2 GLN A 537     128.602  83.921  33.208  1.00 86.99      A    N  
ANISOU 4138  NE2 GLN A 537    10582  12373  10097    316    184    335  A    N  
ATOM   4139  OE1 GLN A 537     128.537  82.790  35.151  1.00 76.67      A    O  
ANISOU 4139  OE1 GLN A 537     9185  11112   8834    127      1    168  A    O  
ATOM   4140  N   LYS A 538     133.835  84.518  36.684  1.00 74.69      A    N  
ANISOU 4140  N   LYS A 538     8856  10591   8930   -281    322   -270  A    N  
ATOM   4141  CA  LYS A 538     135.261  84.147  36.610  1.00 72.10      A    C  
ANISOU 4141  CA  LYS A 538     8469  10283   8643   -361    333   -383  A    C  
ATOM   4142  C   LYS A 538     135.537  83.042  37.577  1.00 67.04      A    C  
ANISOU 4142  C   LYS A 538     7736   9828   7907   -373    150   -445  A    C  
ATOM   4143  O   LYS A 538     136.324  82.146  37.306  1.00 63.96      A    O  
ANISOU 4143  O   LYS A 538     7315   9495   7490   -378     90   -450  A    O  
ATOM   4144  CB  LYS A 538     136.190  85.320  36.936  1.00 77.78      A    C  
ANISOU 4144  CB  LYS A 538     9136  10906   9510   -477    520   -576  A    C  
ATOM   4145  CG  LYS A 538     136.253  86.397  35.870  1.00 85.85      A    C  
ANISOU 4145  CG  LYS A 538    10256  11694  10668   -463    780   -509  A    C  
ATOM   4146  CD  LYS A 538     137.128  87.570  36.295  1.00 92.94      A    C  
ANISOU 4146  CD  LYS A 538    11085  12467  11758   -605   1009   -744  A    C  
ATOM   4147  CE  LYS A 538     138.577  87.143  36.446  1.00 99.00      A    C  
ANISOU 4147  CE  LYS A 538    11735  13308  12571   -721    997   -946  A    C  
ATOM   4148  NZ  LYS A 538     139.486  88.313  36.613  1.00106.45      A    N1+
ANISOU 4148  NZ  LYS A 538    12600  14105  13738   -874   1274  -1204  A    N1+
ATOM   4149  N   ALA A 539     134.891  83.118  38.726  1.00 66.38      A    N  
ANISOU 4149  N   ALA A 539     7613   9839   7768   -360     77   -481  A    N  
ATOM   4150  CA  ALA A 539     135.031  82.072  39.720  1.00 68.89      A    C  
ANISOU 4150  CA  ALA A 539     7857  10339   7978   -323    -69   -498  A    C  
ATOM   4151  C   ALA A 539     134.450  80.749  39.197  1.00 68.89      A    C  
ANISOU 4151  C   ALA A 539     7910  10343   7922   -245   -155   -331  A    C  
ATOM   4152  O   ALA A 539     135.028  79.674  39.334  1.00 73.49      A    O  
ANISOU 4152  O   ALA A 539     8455  11005   8461   -220   -218   -315  A    O  
ATOM   4153  CB  ALA A 539     134.370  82.486  41.021  1.00 67.31      A    C  
ANISOU 4153  CB  ALA A 539     7613  10238   7723   -303   -104   -553  A    C  
ATOM   4154  N   ALA A 540     133.306  80.822  38.573  1.00 67.56      A    N  
ANISOU 4154  N   ALA A 540     7815  10094   7758   -207   -144   -220  A    N  
ATOM   4155  CA  ALA A 540     132.721  79.631  38.061  1.00 66.97      A    C  
ANISOU 4155  CA  ALA A 540     7761  10032   7649   -157   -204   -119  A    C  
ATOM   4156  C   ALA A 540     133.602  79.035  36.966  1.00 67.62      A    C  
ANISOU 4156  C   ALA A 540     7847  10093   7749   -173   -195   -108  A    C  
ATOM   4157  O   ALA A 540     133.855  77.838  36.963  1.00 67.65      A    O  
ANISOU 4157  O   ALA A 540     7825  10141   7738   -160   -242    -89  A    O  
ATOM   4158  CB  ALA A 540     131.321  79.926  37.550  1.00 67.78      A    C  
ANISOU 4158  CB  ALA A 540     7910  10094   7745   -111   -194    -48  A    C  
ATOM   4159  N   LYS A 541     134.078  79.858  36.041  1.00 69.73      A    N  
ANISOU 4159  N   LYS A 541     8151  10282   8058   -191   -110   -115  A    N  
ATOM   4160  CA  LYS A 541     134.845  79.336  34.897  1.00 71.97      A    C  
ANISOU 4160  CA  LYS A 541     8448  10545   8349   -192    -90    -93  A    C  
ATOM   4161  C   LYS A 541     136.191  78.780  35.373  1.00 72.02      A    C  
ANISOU 4161  C   LYS A 541     8392  10595   8378   -252   -115   -179  A    C  
ATOM   4162  O   LYS A 541     136.677  77.790  34.852  1.00 67.55      A    O  
ANISOU 4162  O   LYS A 541     7813  10051   7801   -249   -149   -159  A    O  
ATOM   4163  CB  LYS A 541     135.068  80.420  33.829  1.00 75.56      A    C  
ANISOU 4163  CB  LYS A 541     8969  10894   8844   -172     47    -55  A    C  
ATOM   4164  CG  LYS A 541     133.837  80.882  33.024  1.00 77.23      A    C  
ANISOU 4164  CG  LYS A 541     9240  11100   9001    -61     81     62  A    C  
ATOM   4165  CD  LYS A 541     134.173  82.185  32.286  1.00 81.02      A    C  
ANISOU 4165  CD  LYS A 541     9797  11447   9536    -18    274    119  A    C  
ATOM   4166  CE  LYS A 541     133.148  82.607  31.263  1.00 83.64      A    C  
ANISOU 4166  CE  LYS A 541    10190  11806   9782    149    327    268  A    C  
ATOM   4167  NZ  LYS A 541     131.932  83.100  31.932  1.00 86.98      A    N1+
ANISOU 4167  NZ  LYS A 541    10610  12251  10187    185    297    283  A    N1+
ATOM   4168  N   ALA A 542     136.784  79.420  36.376  1.00 75.95      A    N  
ANISOU 4168  N   ALA A 542     8833  11124   8898   -299    -97   -291  A    N  
ATOM   4169  CA  ALA A 542     138.069  78.986  36.913  1.00 74.83      A    C  
ANISOU 4169  CA  ALA A 542     8602  11076   8754   -334   -127   -400  A    C  
ATOM   4170  C   ALA A 542     137.920  77.686  37.668  1.00 71.74      A    C  
ANISOU 4170  C   ALA A 542     8171  10806   8278   -261   -235   -342  A    C  
ATOM   4171  O   ALA A 542     138.735  76.788  37.532  1.00 75.22      A    O  
ANISOU 4171  O   ALA A 542     8575  11294   8709   -247   -262   -340  A    O  
ATOM   4172  CB  ALA A 542     138.645  80.062  37.823  1.00 78.55      A    C  
ANISOU 4172  CB  ALA A 542     8989  11599   9255   -397    -79   -579  A    C  
ATOM   4173  N   ALA A 543     136.875  77.584  38.470  1.00 68.32      A    N  
ANISOU 4173  N   ALA A 543     7750  10412   7796   -204   -272   -285  A    N  
ATOM   4174  CA  ALA A 543     136.603  76.337  39.156  1.00 69.33      A    C  
ANISOU 4174  CA  ALA A 543     7860  10614   7866   -115   -320   -199  A    C  
ATOM   4175  C   ALA A 543     136.339  75.173  38.177  1.00 67.67      A    C  
ANISOU 4175  C   ALA A 543     7694  10318   7699   -110   -308   -108  A    C  
ATOM   4176  O   ALA A 543     136.782  74.038  38.366  1.00 67.02      A    O  
ANISOU 4176  O   ALA A 543     7586  10265   7611    -62   -306    -65  A    O  
ATOM   4177  CB  ALA A 543     135.430  76.504  40.093  1.00 69.25      A    C  
ANISOU 4177  CB  ALA A 543     7868  10627   7814    -59   -328   -149  A    C  
ATOM   4178  N   ALA A 544     135.620  75.436  37.117  1.00 66.64      A    N  
ANISOU 4178  N   ALA A 544     7616  10095   7606   -148   -289    -87  A    N  
ATOM   4179  CA  ALA A 544     135.289  74.337  36.238  1.00 70.36      A    C  
ANISOU 4179  CA  ALA A 544     8096  10526   8109   -147   -278    -47  A    C  
ATOM   4180  C   ALA A 544     136.481  73.947  35.379  1.00 67.71      A    C  
ANISOU 4180  C   ALA A 544     7748  10183   7794   -180   -272    -74  A    C  
ATOM   4181  O   ALA A 544     136.663  72.789  35.053  1.00 67.16      A    O  
ANISOU 4181  O   ALA A 544     7658  10104   7753   -177   -259    -59  A    O  
ATOM   4182  CB  ALA A 544     134.085  74.692  35.380  1.00 74.39      A    C  
ANISOU 4182  CB  ALA A 544     8636  11007   8621   -150   -272    -38  A    C  
ATOM   4183  N   ALA A 545     137.297  74.924  35.016  1.00 68.00      A    N  
ANISOU 4183  N   ALA A 545     7792  10208   7833   -219   -254   -122  A    N  
ATOM   4184  CA  ALA A 545     138.469  74.649  34.189  1.00 68.08      A    C  
ANISOU 4184  CA  ALA A 545     7793  10202   7871   -255   -232   -152  A    C  
ATOM   4185  C   ALA A 545     139.357  73.745  34.964  1.00 66.96      A    C  
ANISOU 4185  C   ALA A 545     7588  10128   7726   -237   -260   -172  A    C  
ATOM   4186  O   ALA A 545     139.761  72.703  34.476  1.00 68.74      A    O  
ANISOU 4186  O   ALA A 545     7801  10344   7972   -234   -256   -150  A    O  
ATOM   4187  CB  ALA A 545     139.219  75.930  33.876  1.00 70.89      A    C  
ANISOU 4187  CB  ALA A 545     8164  10511   8260   -304   -166   -217  A    C  
ATOM   4188  N   LEU A 546     139.667  74.170  36.182  1.00 63.76      A    N  
ANISOU 4188  N   LEU A 546     7131   9811   7281   -211   -285   -217  A    N  
ATOM   4189  CA  LEU A 546     140.535  73.435  37.043  1.00 61.58      A    C  
ANISOU 4189  CA  LEU A 546     6778   9655   6963   -147   -313   -228  A    C  
ATOM   4190  C   LEU A 546     139.991  72.036  37.290  1.00 60.77      A    C  
ANISOU 4190  C   LEU A 546     6695   9534   6860    -60   -296   -102  A    C  
ATOM   4191  O   LEU A 546     140.738  71.090  37.427  1.00 61.65      A    O  
ANISOU 4191  O   LEU A 546     6770   9684   6970     -5   -282    -71  A    O  
ATOM   4192  CB  LEU A 546     140.687  74.197  38.342  1.00 62.40      A    C  
ANISOU 4192  CB  LEU A 546     6810   9906   6992   -104   -346   -306  A    C  
ATOM   4193  CG  LEU A 546     141.559  73.553  39.414  1.00 64.63      A    C  
ANISOU 4193  CG  LEU A 546     6988  10391   7177     15   -384   -319  A    C  
ATOM   4194  CD1 LEU A 546     142.963  73.267  38.925  1.00 64.24      A    C  
ANISOU 4194  CD1 LEU A 546     6867  10391   7150    -17   -387   -407  A    C  
ATOM   4195  CD2 LEU A 546     141.608  74.505  40.576  1.00 68.24      A    C  
ANISOU 4195  CD2 LEU A 546     7355  11029   7542     48   -421   -438  A    C  
ATOM   4196  N   ASP A 547     138.689  71.882  37.327  1.00 61.28      A    N  
ANISOU 4196  N   ASP A 547     6811   9526   6944    -49   -273    -37  A    N  
ATOM   4197  CA  ASP A 547     138.143  70.560  37.556  1.00 65.52      A    C  
ANISOU 4197  CA  ASP A 547     7360  10010   7523     13   -206     58  A    C  
ATOM   4198  C   ASP A 547     138.417  69.598  36.392  1.00 67.08      A    C  
ANISOU 4198  C   ASP A 547     7561  10120   7806    -44   -161     46  A    C  
ATOM   4199  O   ASP A 547     138.736  68.429  36.610  1.00 70.47      A    O  
ANISOU 4199  O   ASP A 547     7974  10520   8280     11    -86    102  A    O  
ATOM   4200  CB  ASP A 547     136.641  70.650  37.772  1.00 66.71      A    C  
ANISOU 4200  CB  ASP A 547     7550  10096   7700     12   -173     90  A    C  
ATOM   4201  CG  ASP A 547     136.046  69.344  38.275  1.00 68.52      A    C  
ANISOU 4201  CG  ASP A 547     7786  10251   7997     81    -52    177  A    C  
ATOM   4202  OD1 ASP A 547     136.826  68.454  38.734  1.00 73.23      A    O  
ANISOU 4202  OD1 ASP A 547     8365  10861   8596    172      9    249  A    O  
ATOM   4203  OD2 ASP A 547     134.801  69.235  38.235  1.00 66.52      A    O1-
ANISOU 4203  OD2 ASP A 547     7551   9920   7802     54     -0    172  A    O1-
ATOM   4204  N   VAL A 548     138.281  70.088  35.163  1.00 64.41      A    N  
ANISOU 4204  N   VAL A 548     7241   9746   7486   -138   -190    -21  A    N  
ATOM   4205  CA  VAL A 548     138.520  69.281  33.977  1.00 62.54      A    C  
ANISOU 4205  CA  VAL A 548     6993   9462   7307   -191   -158    -56  A    C  
ATOM   4206  C   VAL A 548     140.017  68.966  33.881  1.00 61.10      A    C  
ANISOU 4206  C   VAL A 548     6784   9304   7125   -188   -163    -63  A    C  
ATOM   4207  O   VAL A 548     140.414  67.826  33.628  1.00 61.72      A    O  
ANISOU 4207  O   VAL A 548     6842   9345   7263   -183   -107    -52  A    O  
ATOM   4208  CB  VAL A 548     138.045  70.027  32.715  1.00 64.00      A    C  
ANISOU 4208  CB  VAL A 548     7199   9653   7465   -247   -190   -110  A    C  
ATOM   4209  CG1 VAL A 548     138.468  69.327  31.428  1.00 65.42      A    C  
ANISOU 4209  CG1 VAL A 548     7357   9830   7668   -290   -169   -160  A    C  
ATOM   4210  CG2 VAL A 548     136.542  70.193  32.737  1.00 64.97      A    C  
ANISOU 4210  CG2 VAL A 548     7323   9779   7582   -240   -187   -119  A    C  
ATOM   4211  N   LEU A 549     140.859  69.970  34.092  1.00 58.29      A    N  
ANISOU 4211  N   LEU A 549     6421   9008   6718   -196   -214   -100  A    N  
ATOM   4212  CA  LEU A 549     142.291  69.751  34.030  1.00 57.20      A    C  
ANISOU 4212  CA  LEU A 549     6237   8913   6582   -198   -218   -136  A    C  
ATOM   4213  C   LEU A 549     142.713  68.717  35.095  1.00 60.62      A    C  
ANISOU 4213  C   LEU A 549     6621   9410   7000    -84   -197    -70  A    C  
ATOM   4214  O   LEU A 549     143.563  67.867  34.840  1.00 60.22      A    O  
ANISOU 4214  O   LEU A 549     6541   9359   6980    -65   -167    -60  A    O  
ATOM   4215  CB  LEU A 549     143.033  71.076  34.167  1.00 54.57      A    C  
ANISOU 4215  CB  LEU A 549     5880   8633   6220   -242   -247   -230  A    C  
ATOM   4216  CG  LEU A 549     142.695  72.070  33.059  1.00 53.44      A    C  
ANISOU 4216  CG  LEU A 549     5801   8398   6102   -320   -215   -257  A    C  
ATOM   4217  CD1 LEU A 549     143.288  73.440  33.284  1.00 53.31      A    C  
ANISOU 4217  CD1 LEU A 549     5766   8387   6099   -371   -185   -357  A    C  
ATOM   4218  CD2 LEU A 549     143.191  71.553  31.727  1.00 55.03      A    C  
ANISOU 4218  CD2 LEU A 549     6027   8541   6340   -360   -179   -255  A    C  
ATOM   4219  N   SER A 550     142.092  68.775  36.271  1.00 64.12      A    N  
ANISOU 4219  N   SER A 550     7061   9910   7389     12   -196     -7  A    N  
ATOM   4220  CA  SER A 550     142.357  67.813  37.337  1.00 68.43      A    C  
ANISOU 4220  CA  SER A 550     7575  10525   7900    173   -143    100  A    C  
ATOM   4221  C   SER A 550     141.962  66.409  36.936  1.00 69.37      A    C  
ANISOU 4221  C   SER A 550     7729  10492   8134    188    -15    188  A    C  
ATOM   4222  O   SER A 550     142.588  65.423  37.315  1.00 70.73      A    O  
ANISOU 4222  O   SER A 550     7878  10676   8318    302     63    273  A    O  
ATOM   4223  CB  SER A 550     141.574  68.185  38.585  1.00 71.98      A    C  
ANISOU 4223  CB  SER A 550     8029  11051   8267    281   -145    163  A    C  
ATOM   4224  OG  SER A 550     142.008  69.432  39.069  1.00 80.56      A    O  
ANISOU 4224  OG  SER A 550     9057  12296   9252    267   -248     54  A    O  
ATOM   4225  N   THR A 551     140.883  66.324  36.185  1.00 69.71      A    N  
ANISOU 4225  N   THR A 551     7818  10401   8266     82     23    156  A    N  
ATOM   4226  CA  THR A 551     140.395  65.049  35.726  1.00 70.00      A    C  
ANISOU 4226  CA  THR A 551     7864  10291   8440     60    166    177  A    C  
ATOM   4227  C   THR A 551     141.344  64.529  34.652  1.00 70.50      A    C  
ANISOU 4227  C   THR A 551     7901  10330   8554    -13    167    112  A    C  
ATOM   4228  O   THR A 551     141.706  63.356  34.646  1.00 70.64      A    O  
ANISOU 4228  O   THR A 551     7904  10270   8664     27    292    156  A    O  
ATOM   4229  CB  THR A 551     138.983  65.222  35.166  1.00 71.09      A    C  
ANISOU 4229  CB  THR A 551     8018  10350   8642    -43    186    102  A    C  
ATOM   4230  CG2 THR A 551     138.422  63.934  34.679  1.00 73.60      A    C  
ANISOU 4230  CG2 THR A 551     8313  10528   9122    -94    353     60  A    C  
ATOM   4231  OG1 THR A 551     138.131  65.734  36.192  1.00 71.25      A    O  
ANISOU 4231  OG1 THR A 551     8066  10389   8617     23    188    164  A    O  
ATOM   4232  N   PHE A 552     141.777  65.408  33.760  1.00 69.09      A    N  
ANISOU 4232  N   PHE A 552     7720  10207   8324   -110     50     17  A    N  
ATOM   4233  CA  PHE A 552     142.742  65.008  32.762  1.00 70.03      A    C  
ANISOU 4233  CA  PHE A 552     7817  10314   8477   -171     50    -40  A    C  
ATOM   4234  C   PHE A 552     144.021  64.453  33.377  1.00 71.90      A    C  
ANISOU 4234  C   PHE A 552     8017  10598   8704    -76     72     19  A    C  
ATOM   4235  O   PHE A 552     144.657  63.551  32.818  1.00 73.80      A    O  
ANISOU 4235  O   PHE A 552     8237  10785   9016    -93    135      9  A    O  
ATOM   4236  CB  PHE A 552     143.069  66.188  31.879  1.00 69.38      A    C  
ANISOU 4236  CB  PHE A 552     7750  10281   8330   -255    -51   -120  A    C  
ATOM   4237  CG  PHE A 552     141.991  66.523  30.913  1.00 68.48      A    C  
ANISOU 4237  CG  PHE A 552     7661  10147   8211   -322    -60   -174  A    C  
ATOM   4238  CD1 PHE A 552     140.945  65.658  30.699  1.00 66.03      A    C  
ANISOU 4238  CD1 PHE A 552     7329   9790   7968   -341      9   -204  A    C  
ATOM   4239  CD2 PHE A 552     142.067  67.689  30.168  1.00 70.70      A    C  
ANISOU 4239  CD2 PHE A 552     7975  10463   8423   -355   -116   -206  A    C  
ATOM   4240  CE1 PHE A 552     139.967  65.964  29.793  1.00 66.83      A    C  
ANISOU 4240  CE1 PHE A 552     7419   9932   8040   -385    -13   -282  A    C  
ATOM   4241  CE2 PHE A 552     141.096  67.997  29.257  1.00 69.21      A    C  
ANISOU 4241  CE2 PHE A 552     7799  10300   8197   -372   -125   -238  A    C  
ATOM   4242  CZ  PHE A 552     140.041  67.129  29.074  1.00 68.67      A    C  
ANISOU 4242  CZ  PHE A 552     7687  10235   8168   -384    -89   -285  A    C  
ATOM   4243  N   SER A 553     144.392  65.022  34.516  1.00 71.73      A    N  
ANISOU 4243  N   SER A 553     7972  10701   8581     33     16     64  A    N  
ATOM   4244  CA  SER A 553     145.594  64.637  35.215  1.00 74.01      A    C  
ANISOU 4244  CA  SER A 553     8197  11107   8816    158     16    107  A    C  
ATOM   4245  C   SER A 553     145.449  63.248  35.753  1.00 76.28      A    C  
ANISOU 4245  C   SER A 553     8493  11322   9165    299    171    254  A    C  
ATOM   4246  O   SER A 553     146.294  62.408  35.528  1.00 74.34      A    O  
ANISOU 4246  O   SER A 553     8219  11061   8964    343    233    282  A    O  
ATOM   4247  CB  SER A 553     145.856  65.618  36.359  1.00 75.40      A    C  
ANISOU 4247  CB  SER A 553     8319  11483   8845    254    -81     90  A    C  
ATOM   4248  OG  SER A 553     147.141  65.441  36.902  1.00 82.76      A    O  
ANISOU 4248  OG  SER A 553     9151  12596   9695    369   -113     75  A    O  
ATOM   4249  N   ALA A 554     144.355  63.015  36.459  1.00 84.51      A    N  
ANISOU 4249  N   ALA A 554     9580  12304  10226    372    258    351  A    N  
ATOM   4250  CA  ALA A 554     144.075  61.719  37.058  1.00 90.53      A    C  
ANISOU 4250  CA  ALA A 554    10366  12954  11073    520    468    511  A    C  
ATOM   4251  C   ALA A 554     143.927  60.616  36.014  1.00 92.21      A    C  
ANISOU 4251  C   ALA A 554    10594  12953  11487    401    620    466  A    C  
ATOM   4252  O   ALA A 554     144.392  59.516  36.236  1.00 99.38      A    O  
ANISOU 4252  O   ALA A 554    11497  13784  12475    512    788    570  A    O  
ATOM   4253  CB  ALA A 554     142.817  61.796  37.894  1.00 96.51      A    C  
ANISOU 4253  CB  ALA A 554    11173  13657  11836    587    553    598  A    C  
ATOM   4254  N   LEU A 555     143.286  60.895  34.881  1.00 89.72      A    N  
ANISOU 4254  N   LEU A 555    10284  12557  11247    191    574    307  A    N  
ATOM   4255  CA  LEU A 555     143.157  59.881  33.823  1.00 89.75      A    C  
ANISOU 4255  CA  LEU A 555    10270  12402  11425     67    707    213  A    C  
ATOM   4256  C   LEU A 555     144.524  59.428  33.332  1.00 88.76      A    C  
ANISOU 4256  C   LEU A 555    10113  12306  11304     76    694    208  A    C  
ATOM   4257  O   LEU A 555     144.754  58.246  33.116  1.00 86.51      A    O  
ANISOU 4257  O   LEU A 555     9815  11888  11165     87    875    227  A    O  
ATOM   4258  CB  LEU A 555     142.387  60.430  32.626  1.00 89.00      A    C  
ANISOU 4258  CB  LEU A 555    10160  12312  11343   -129    612     24  A    C  
ATOM   4259  CG  LEU A 555     140.931  60.707  32.919  1.00 91.91      A    C  
ANISOU 4259  CG  LEU A 555    10540  12641  11739   -161    647     -7  A    C  
ATOM   4260  CD1 LEU A 555     140.397  61.755  31.952  1.00 93.68      A    C  
ANISOU 4260  CD1 LEU A 555    10751  12972  11868   -282    473   -147  A    C  
ATOM   4261  CD2 LEU A 555     140.131  59.419  32.859  1.00 93.05      A    C  
ANISOU 4261  CD2 LEU A 555    10654  12600  12100   -204    902    -60  A    C  
ATOM   4262  N   ALA A 556     145.422  60.386  33.125  1.00 86.45      A    N  
ANISOU 4262  N   ALA A 556     9803  12173  10869     60    498    167  A    N  
ATOM   4263  CA  ALA A 556     146.698  60.078  32.528  1.00 86.32      A    C  
ANISOU 4263  CA  ALA A 556     9751  12188  10859     42    474    130  A    C  
ATOM   4264  C   ALA A 556     147.466  59.250  33.520  1.00 89.73      A    C  
ANISOU 4264  C   ALA A 556    10158  12645  11288    247    582    286  A    C  
ATOM   4265  O   ALA A 556     148.075  58.252  33.162  1.00 94.96      A    O  
ANISOU 4265  O   ALA A 556    10803  13224  12052    264    700    306  A    O  
ATOM   4266  CB  ALA A 556     147.457  61.353  32.165  1.00 87.39      A    C  
ANISOU 4266  CB  ALA A 556     9866  12473  10865    -22    277     38  A    C  
ATOM   4267  N   LYS A 557     147.426  59.661  34.779  1.00 91.64      A    N  
ANISOU 4267  N   LYS A 557    10395  13019  11404    424    548    401  A    N  
ATOM   4268  CA  LYS A 557     148.193  58.981  35.810  1.00 96.23      A    C  
ANISOU 4268  CA  LYS A 557    10942  13695  11926    679    637    569  A    C  
ATOM   4269  C   LYS A 557     147.624  57.594  36.107  1.00 95.06      A    C  
ANISOU 4269  C   LYS A 557    10847  13327  11944    788    929    731  A    C  
ATOM   4270  O   LYS A 557     148.379  56.714  36.496  1.00 97.98      A    O  
ANISOU 4270  O   LYS A 557    11198  13701  12329    973   1063    867  A    O  
ATOM   4271  CB  LYS A 557     148.253  59.832  37.092  1.00 98.09      A    C  
ANISOU 4271  CB  LYS A 557    11141  14181  11949    860    521    634  A    C  
ATOM   4272  CG  LYS A 557     149.284  59.361  38.104  1.00102.57      A    C  
ANISOU 4272  CG  LYS A 557    11632  14962  12376   1156    553    776  A    C  
ATOM   4273  CD  LYS A 557     149.414  60.329  39.267  1.00106.50      A    C  
ANISOU 4273  CD  LYS A 557    12054  15776  12634   1317    404    773  A    C  
ATOM   4274  CE  LYS A 557     150.299  59.772  40.384  1.00111.80      A    C  
ANISOU 4274  CE  LYS A 557    12635  16719  13125   1675    449    935  A    C  
ATOM   4275  NZ  LYS A 557     150.012  60.425  41.699  1.00114.31      A    N1+
ANISOU 4275  NZ  LYS A 557    12899  17322  13210   1891    377    990  A    N1+
ATOM   4276  N   GLU A 558     146.318  57.399  35.902  1.00 93.44      A    N  
ANISOU 4276  N   GLU A 558    10700  12926  11876    676   1048    703  A    N  
ATOM   4277  CA  GLU A 558     145.626  56.161  36.300  1.00 95.98      A    C  
ANISOU 4277  CA  GLU A 558    11070  13008  12391    768   1376    835  A    C  
ATOM   4278  C   GLU A 558     145.308  55.209  35.150  1.00 98.49      A    C  
ANISOU 4278  C   GLU A 558    11379  13074  12967    563   1555    690  A    C  
ATOM   4279  O   GLU A 558     144.842  54.102  35.383  1.00 96.91      A    O  
ANISOU 4279  O   GLU A 558    11203  12642  12973    613   1872    766  A    O  
ATOM   4280  CB  GLU A 558     144.318  56.483  37.024  1.00101.19      A    C  
ANISOU 4280  CB  GLU A 558    11781  13611  13055    798   1444    889  A    C  
ATOM   4281  CG  GLU A 558     144.475  57.244  38.339  1.00109.64      A    C  
ANISOU 4281  CG  GLU A 558    12858  14917  13883   1037   1329   1049  A    C  
ATOM   4282  CD  GLU A 558     143.142  57.653  38.973  1.00111.18      A    C  
ANISOU 4282  CD  GLU A 558    13107  15056  14081   1041   1380   1083  A    C  
ATOM   4283  OE1 GLU A 558     142.081  57.116  38.580  1.00110.87      A    O  
ANISOU 4283  OE1 GLU A 558    13100  14766  14258    904   1571   1021  A    O  
ATOM   4284  OE2 GLU A 558     143.166  58.521  39.874  1.00109.91      A    O1-
ANISOU 4284  OE2 GLU A 558    12938  15115  13706   1176   1232   1151  A    O1-
ATOM   4285  N   ARG A 559     145.528  55.648  33.916  1.00 66.85      A    N  
ATOM   4286  CA  ARG A 559     145.370  54.785  32.717  1.00 73.24      A    C  
ATOM   4287  C   ARG A 559     146.523  54.980  31.724  1.00 67.18      A    C  
ATOM   4288  O   ARG A 559     146.403  54.625  30.545  1.00 64.22      A    O  
ATOM   4289  CB  ARG A 559     144.069  55.100  31.969  1.00 77.86      A    C  
ATOM   4290  CG  ARG A 559     142.836  54.939  32.808  1.00 79.04      A    C  
ATOM   4291  CD  ARG A 559     141.658  55.679  32.220  1.00 81.16      A    C  
ATOM   4292  NE  ARG A 559     140.515  55.550  33.105  1.00 82.73      A    N  
ATOM   4293  CZ  ARG A 559     139.278  55.906  32.799  1.00 81.34      A    C  
ATOM   4294  NH1 ARG A 559     138.999  56.433  31.621  1.00 69.75      A    N1+
ATOM   4295  NH2 ARG A 559     138.312  55.735  33.696  1.00113.94      A    N  
ATOM   4296  N   ASN A 560     147.615  55.583  32.176  1.00 96.73      A    N  
ANISOU 4296  N   ASN A 560    10878  11689  14186    640    516    174  A    N  
ATOM   4297  CA  ASN A 560     148.823  55.619  31.381  1.00 93.30      A    C  
ANISOU 4297  CA  ASN A 560    10241  11169  14037    718    612     48  A    C  
ATOM   4298  C   ASN A 560     148.680  56.417  30.081  1.00 85.67      A    C  
ANISOU 4298  C   ASN A 560     9201  10305  13041    687    898      6  A    C  
ATOM   4299  O   ASN A 560     149.030  55.935  29.012  1.00 81.52      A    O  
ANISOU 4299  O   ASN A 560     8609   9737  12627    700   1057    -64  A    O  
ATOM   4300  CB  ASN A 560     149.260  54.175  31.101  1.00 93.96      A    C  
ANISOU 4300  CB  ASN A 560    10308  11110  14282    772    557      1  A    C  
ATOM   4301  CG  ASN A 560     150.687  54.082  30.689  1.00 98.43      A    C  
ANISOU 4301  CG  ASN A 560    10651  11553  15194    861    583   -155  A    C  
ATOM   4302  ND2 ASN A 560     151.054  52.938  30.169  1.00100.99      A    N  
ANISOU 4302  ND2 ASN A 560    10930  11771  15669    905    598   -223  A    N  
ATOM   4303  OD1 ASN A 560     151.460  55.039  30.816  1.00111.55      A    O  
ANISOU 4303  OD1 ASN A 560    12171  13216  16995    885    599   -226  A    O  
ATOM   4304  N   PHE A 561     148.171  57.640  30.179  1.00 84.25      A    N  
ANISOU 4304  N   PHE A 561     9051  10250  12707    642    954     44  A    N  
ATOM   4305  CA  PHE A 561     148.114  58.534  29.021  1.00 85.23      A    C  
ANISOU 4305  CA  PHE A 561     9128  10450  12805    614   1187      2  A    C  
ATOM   4306  C   PHE A 561     149.389  59.351  28.967  1.00 88.89      A    C  
ANISOU 4306  C   PHE A 561     9421  10857  13494    651   1219    -99  A    C  
ATOM   4307  O   PHE A 561     150.049  59.556  29.987  1.00 97.04      A    O  
ANISOU 4307  O   PHE A 561    10387  11835  14648    694   1043   -116  A    O  
ATOM   4308  CB  PHE A 561     146.919  59.494  29.057  1.00 83.52      A    C  
ANISOU 4308  CB  PHE A 561     9021  10388  12323    554   1229     77  A    C  
ATOM   4309  CG  PHE A 561     145.552  58.828  28.946  1.00 81.57      A    C  
ANISOU 4309  CG  PHE A 561     8926  10218  11848    502   1239    157  A    C  
ATOM   4310  CD1 PHE A 561     145.419  57.473  28.710  1.00 80.34      A    C  
ANISOU 4310  CD1 PHE A 561     8819   9995  11711    504   1228    172  A    C  
ATOM   4311  CD2 PHE A 561     144.402  59.589  29.041  1.00 77.16      A    C  
ANISOU 4311  CD2 PHE A 561     8451   9796  11067    450   1264    201  A    C  
ATOM   4312  CE1 PHE A 561     144.183  56.897  28.609  1.00 74.57      A    C  
ANISOU 4312  CE1 PHE A 561     8223   9334  10775    447   1242    240  A    C  
ATOM   4313  CE2 PHE A 561     143.172  59.016  28.934  1.00 74.19      A    C  
ANISOU 4313  CE2 PHE A 561     8191   9493  10503    396   1280    253  A    C  
ATOM   4314  CZ  PHE A 561     143.067  57.666  28.714  1.00 74.80      A    C  
ANISOU 4314  CZ  PHE A 561     8321   9503  10596    391   1272    276  A    C  
ATOM   4315  N   VAL A 562     149.730  59.807  27.767  1.00 87.04      A    N  
ANISOU 4315  N   VAL A 562     9132  10627  13310    624   1441   -170  A    N  
ATOM   4316  CA  VAL A 562     150.985  60.493  27.529  1.00 85.13      A    C  
ANISOU 4316  CA  VAL A 562     8726  10325  13291    637   1516   -286  A    C  
ATOM   4317  C   VAL A 562     150.694  61.789  26.820  1.00 84.01      A    C  
ANISOU 4317  C   VAL A 562     8634  10268  13016    575   1675   -281  A    C  
ATOM   4318  O   VAL A 562     149.816  61.854  25.955  1.00 84.21      A    O  
ANISOU 4318  O   VAL A 562     8789  10354  12851    525   1801   -236  A    O  
ATOM   4319  CB  VAL A 562     151.923  59.635  26.659  1.00 90.63      A    C  
ANISOU 4319  CB  VAL A 562     9304  10907  14221    647   1656   -415  A    C  
ATOM   4320  CG1 VAL A 562     152.341  58.380  27.410  1.00 96.96      A    C  
ANISOU 4320  CG1 VAL A 562    10042  11600  15195    726   1465   -441  A    C  
ATOM   4321  CG2 VAL A 562     151.263  59.227  25.346  1.00 89.83      A    C  
ANISOU 4321  CG2 VAL A 562     9321  10833  13976    584   1869   -401  A    C  
ATOM   4322  N   ARG A 563     151.433  62.826  27.186  1.00 82.87      A    N  
ANISOU 4322  N   ARG A 563     8392  10119  12974    580   1654   -330  A    N  
ATOM   4323  CA  ARG A 563     151.277  64.148  26.567  1.00 79.92      A    C  
ANISOU 4323  CA  ARG A 563     8068   9809  12488    521   1785   -332  A    C  
ATOM   4324  C   ARG A 563     151.706  64.095  25.095  1.00 76.59      A    C  
ANISOU 4324  C   ARG A 563     7656   9333  12111    452   2043   -417  A    C  
ATOM   4325  O   ARG A 563     152.882  63.953  24.794  1.00 82.25      A    O  
ANISOU 4325  O   ARG A 563     8230   9960  13060    438   2141   -541  A    O  
ATOM   4326  CB  ARG A 563     152.137  65.147  27.338  1.00 82.30      A    C  
ANISOU 4326  CB  ARG A 563     8250  10096  12922    541   1697   -378  A    C  
ATOM   4327  CG  ARG A 563     152.299  66.505  26.706  1.00 86.14      A    C  
ANISOU 4327  CG  ARG A 563     8763  10614  13350    480   1831   -405  A    C  
ATOM   4328  CD  ARG A 563     153.302  67.328  27.504  1.00 93.56      A    C  
ANISOU 4328  CD  ARG A 563     9561  11523  14464    502   1740   -465  A    C  
ATOM   4329  NE  ARG A 563     153.247  68.738  27.102  1.00105.20      A    N  
ANISOU 4329  NE  ARG A 563    11094  13041  15833    446   1823   -465  A    N  
ATOM   4330  CZ  ARG A 563     153.431  69.794  27.909  1.00105.22      A    C  
ANISOU 4330  CZ  ARG A 563    11066  13076  15834    465   1705   -451  A    C  
ATOM   4331  NH1 ARG A 563     153.682  69.638  29.204  1.00103.61      A    N1+
ANISOU 4331  NH1 ARG A 563    10777  12866  15723    535   1494   -433  A    N1+
ATOM   4332  NH2 ARG A 563     153.360  71.025  27.407  1.00 98.30      A    N  
ANISOU 4332  NH2 ARG A 563    10263  12229  14857    410   1791   -455  A    N  
ATOM   4333  N   PRO A 564     150.766  64.193  24.169  1.00 72.21      A    N  
ANISOU 4333  N   PRO A 564     7270   8826  11339    401   2154   -363  A    N  
ATOM   4334  CA  PRO A 564     151.143  64.181  22.785  1.00 75.61      A    C  
ANISOU 4334  CA  PRO A 564     7750   9195  11782    318   2392   -437  A    C  
ATOM   4335  C   PRO A 564     151.940  65.418  22.364  1.00 79.09      A    C  
ANISOU 4335  C   PRO A 564     8168   9607  12275    249   2512   -513  A    C  
ATOM   4336  O   PRO A 564     151.802  66.497  22.945  1.00 76.62      A    O  
ANISOU 4336  O   PRO A 564     7861   9347  11901    263   2412   -474  A    O  
ATOM   4337  CB  PRO A 564     149.804  64.141  22.058  1.00 74.10      A    C  
ANISOU 4337  CB  PRO A 564     7772   9060  11320    290   2423   -345  A    C  
ATOM   4338  CG  PRO A 564     148.885  64.840  22.954  1.00 74.23      A    C  
ANISOU 4338  CG  PRO A 564     7833   9185  11184    336   2240   -250  A    C  
ATOM   4339  CD  PRO A 564     149.354  64.511  24.341  1.00 74.83      A    C  
ANISOU 4339  CD  PRO A 564     7757   9264  11406    406   2067   -247  A    C  
ATOM   4340  N   GLU A 565     152.773  65.228  21.347  1.00 83.76      A    N  
ANISOU 4340  N   GLU A 565     8740  10109  12975    164   2734   -626  A    N  
ATOM   4341  CA  GLU A 565     153.591  66.275  20.787  1.00 88.05      A    C  
ANISOU 4341  CA  GLU A 565     9282  10608  13564     66   2891   -713  A    C  
ATOM   4342  C   GLU A 565     152.915  66.809  19.532  1.00 85.99      A    C  
ANISOU 4342  C   GLU A 565     9284  10337  13050    -36   3031   -672  A    C  
ATOM   4343  O   GLU A 565     152.164  66.085  18.851  1.00 83.39      A    O  
ANISOU 4343  O   GLU A 565     9095  10002  12586    -47   3076   -627  A    O  
ATOM   4344  CB  GLU A 565     154.942  65.689  20.372  1.00 97.73      A    C  
ANISOU 4344  CB  GLU A 565    10333  11731  15065      9   3077   -889  A    C  
ATOM   4345  CG  GLU A 565     155.568  64.716  21.360  1.00101.79      A    C  
ANISOU 4345  CG  GLU A 565    10602  12218  15852    121   2941   -951  A    C  
ATOM   4346  CD  GLU A 565     156.332  65.401  22.473  1.00105.78      A    C  
ANISOU 4346  CD  GLU A 565    10920  12727  16543    177   2791   -994  A    C  
ATOM   4347  OE1 GLU A 565     156.508  66.638  22.434  1.00108.40      A    O  
ANISOU 4347  OE1 GLU A 565    11290  13082  16813    119   2824   -991  A    O  
ATOM   4348  OE2 GLU A 565     156.772  64.677  23.386  1.00109.50      A    O1-
ANISOU 4348  OE2 GLU A 565    11214  13165  17224    279   2627  -1034  A    O1-
ATOM   4349  N   PHE A 566     153.235  68.051  19.182  1.00 84.52      A    N  
ANISOU 4349  N   PHE A 566     9176  10132  12805   -118   3100   -696  A    N  
ATOM   4350  CA  PHE A 566     152.727  68.620  17.941  1.00 88.41      A    C  
ANISOU 4350  CA  PHE A 566     9945  10583  13064   -227   3223   -671  A    C  
ATOM   4351  C   PHE A 566     153.830  68.941  16.940  1.00 89.11      A    C  
ANISOU 4351  C   PHE A 566    10076  10558  13221   -396   3493   -802  A    C  
ATOM   4352  O   PHE A 566     154.925  69.285  17.332  1.00 97.27      A    O  
ANISOU 4352  O   PHE A 566    10930  11569  14458   -428   3554   -906  A    O  
ATOM   4353  CB  PHE A 566     151.913  69.852  18.250  1.00 91.64      A    C  
ANISOU 4353  CB  PHE A 566    10483  11052  13282   -192   3057   -574  A    C  
ATOM   4354  CG  PHE A 566     150.734  69.578  19.151  1.00 93.11      A    C  
ANISOU 4354  CG  PHE A 566    10645  11352  13378    -51   2821   -460  A    C  
ATOM   4355  CD1 PHE A 566     149.636  68.886  18.660  1.00 92.76      A    C  
ANISOU 4355  CD1 PHE A 566    10739  11328  13174    -27   2793   -394  A    C  
ATOM   4356  CD2 PHE A 566     150.726  70.004  20.480  1.00 88.61      A    C  
ANISOU 4356  CD2 PHE A 566     9922  10865  12879     44   2636   -429  A    C  
ATOM   4357  CE1 PHE A 566     148.565  68.613  19.479  1.00 92.05      A    C  
ANISOU 4357  CE1 PHE A 566    10621  11345  13006     80   2600   -307  A    C  
ATOM   4358  CE2 PHE A 566     149.660  69.738  21.299  1.00 84.46      A    C  
ANISOU 4358  CE2 PHE A 566     9387  10442  12260    145   2446   -339  A    C  
ATOM   4359  CZ  PHE A 566     148.576  69.040  20.799  1.00 87.88      A    C  
ANISOU 4359  CZ  PHE A 566     9947  10900  12541    159   2435   -282  A    C  
ATOM   4360  N   ALA A 567     153.547  68.781  15.654  1.00 87.97      A    N  
ANISOU 4360  N   ALA A 567    10174  10340  12910   -512   3657   -808  A    N  
ATOM   4361  CA  ALA A 567     154.547  68.975  14.612  1.00 90.73      A    C  
ANISOU 4361  CA  ALA A 567    10602  10574  13294   -703   3944   -940  A    C  
ATOM   4362  C   ALA A 567     154.018  69.998  13.665  1.00 93.49      A    C  
ANISOU 4362  C   ALA A 567    11301  10861  13360   -816   3973   -882  A    C  
ATOM   4363  O   ALA A 567     152.827  70.290  13.702  1.00 93.83      A    O  
ANISOU 4363  O   ALA A 567    11504  10947  13199   -732   3778   -751  A    O  
ATOM   4364  CB  ALA A 567     154.831  67.676  13.867  1.00 89.55      A    C  
ANISOU 4364  CB  ALA A 567    10444  10363  13217   -762   4143  -1025  A    C  
ATOM   4365  N   ASP A 568     154.898  70.537  12.821  1.00 98.28      A    N  
ANISOU 4365  N   ASP A 568    12025  11361  13955  -1013   4210   -988  A    N  
ATOM   4366  CA  ASP A 568     154.509  71.527  11.823  1.00104.55      A    C  
ANISOU 4366  CA  ASP A 568    13195  12061  14467  -1150   4244   -942  A    C  
ATOM   4367  C   ASP A 568     154.293  70.930  10.426  1.00 97.93      A    C  
ANISOU 4367  C   ASP A 568    12651  11105  13451  -1297   4435   -962  A    C  
ATOM   4368  O   ASP A 568     153.684  71.541   9.544  1.00 96.99      A    O  
ANISOU 4368  O   ASP A 568    12895  10896  13059  -1384   4408   -897  A    O  
ATOM   4369  CB  ASP A 568     155.545  72.642  11.755  1.00116.57      A    C  
ANISOU 4369  CB  ASP A 568    14726  13526  16040  -1298   4373  -1034  A    C  
ATOM   4370  CG  ASP A 568     154.931  73.988  11.357  1.00130.27      A    C  
ANISOU 4370  CG  ASP A 568    16788  15205  17503  -1346   4243   -938  A    C  
ATOM   4371  OD1 ASP A 568     153.696  74.061  11.136  1.00134.70      A    O  
ANISOU 4371  OD1 ASP A 568    17554  15773  17851  -1254   4045   -813  A    O  
ATOM   4372  OD2 ASP A 568     155.682  74.985  11.268  1.00139.62      A    O1-
ANISOU 4372  OD2 ASP A 568    18023  16332  18693  -1475   4329   -999  A    O1-
ATOM   4373  N   TYR A 569     154.767  69.714  10.242  1.00 92.25      A    N  
ANISOU 4373  N   TYR A 569    11783  10380  12888  -1319   4610  -1054  A    N  
ATOM   4374  CA  TYR A 569     154.559  68.990   8.996  1.00 90.41      A    C  
ANISOU 4374  CA  TYR A 569    11803  10044  12503  -1447   4793  -1077  A    C  
ATOM   4375  C   TYR A 569     153.386  68.016   9.115  1.00 88.41      A    C  
ANISOU 4375  C   TYR A 569    11563   9851  12177  -1282   4611   -961  A    C  
ATOM   4376  O   TYR A 569     153.091  67.537  10.194  1.00 88.10      A    O  
ANISOU 4376  O   TYR A 569    11252   9933  12288  -1092   4430   -914  A    O  
ATOM   4377  CB  TYR A 569     155.819  68.214   8.625  1.00 89.21      A    C  
ANISOU 4377  CB  TYR A 569    11485   9839  12569  -1588   5123  -1274  A    C  
ATOM   4378  CG  TYR A 569     156.371  67.395   9.753  1.00 86.97      A    C  
ANISOU 4378  CG  TYR A 569    10753   9659  12633  -1430   5075  -1349  A    C  
ATOM   4379  CD1 TYR A 569     157.093  68.000  10.772  1.00 88.66      A    C  
ANISOU 4379  CD1 TYR A 569    10686   9932  13065  -1371   5006  -1402  A    C  
ATOM   4380  CD2 TYR A 569     156.190  66.027   9.806  1.00 87.26      A    C  
ANISOU 4380  CD2 TYR A 569    10657   9718  12778  -1339   5085  -1368  A    C  
ATOM   4381  CE1 TYR A 569     157.612  67.276  11.829  1.00 90.07      A    C  
ANISOU 4381  CE1 TYR A 569    10473  10184  13563  -1223   4928  -1472  A    C  
ATOM   4382  CE2 TYR A 569     156.713  65.277  10.858  1.00 89.61      A    C  
ANISOU 4382  CE2 TYR A 569    10562  10088  13395  -1191   5012  -1439  A    C  
ATOM   4383  CZ  TYR A 569     157.426  65.915  11.881  1.00 90.99      A    C  
ANISOU 4383  CZ  TYR A 569    10471  10314  13786  -1131   4925  -1491  A    C  
ATOM   4384  OH  TYR A 569     157.969  65.251  12.975  1.00 88.62      A    O  
ANISOU 4384  OH  TYR A 569     9799  10068  13804   -978   4814  -1563  A    O  
ATOM   4385  N   PRO A 570     152.712  67.732   7.998  1.00 88.72      A    N  
ANISOU 4385  N   PRO A 570    11933   9798  11976  -1363   4655   -914  A    N  
ATOM   4386  CA  PRO A 570     151.714  66.693   7.960  1.00 88.64      A    C  
ANISOU 4386  CA  PRO A 570    11940   9828  11908  -1237   4532   -828  A    C  
ATOM   4387  C   PRO A 570     152.233  65.385   8.523  1.00 89.49      A    C  
ANISOU 4387  C   PRO A 570    11716  10001  12284  -1160   4616   -906  A    C  
ATOM   4388  O   PRO A 570     153.044  64.751   7.869  1.00 99.46      A    O  
ANISOU 4388  O   PRO A 570    12973  11187  13630  -1292   4884  -1037  A    O  
ATOM   4389  CB  PRO A 570     151.445  66.494   6.454  1.00 90.54      A    C  
ANISOU 4389  CB  PRO A 570    12583   9916  11902  -1411   4685   -833  A    C  
ATOM   4390  CG  PRO A 570     151.910  67.720   5.777  1.00 95.69      A    C  
ANISOU 4390  CG  PRO A 570    13506  10449  12400  -1600   4785   -867  A    C  
ATOM   4391  CD  PRO A 570     152.876  68.409   6.699  1.00 97.31      A    C  
ANISOU 4391  CD  PRO A 570    13425  10725  12825  -1592   4820   -941  A    C  
ATOM   4392  N   VAL A 571     151.740  64.958   9.688  1.00 86.34      A    N  
ANISOU 4392  N   VAL A 571    11065   9732  12007   -954   4389   -833  A    N  
ATOM   4393  CA  VAL A 571     152.172  63.710  10.301  1.00 83.03      A    C  
ANISOU 4393  CA  VAL A 571    10348   9361  11837   -863   4419   -897  A    C  
ATOM   4394  C   VAL A 571     151.160  63.205  11.319  1.00 83.00      A    C  
ANISOU 4394  C   VAL A 571    10218   9479  11840   -657   4133   -768  A    C  
ATOM   4395  O   VAL A 571     150.466  64.007  11.935  1.00 91.32      A    O  
ANISOU 4395  O   VAL A 571    11291  10606  12797   -572   3920   -664  A    O  
ATOM   4396  CB  VAL A 571     153.524  63.915  11.014  1.00 84.27      A    C  
ANISOU 4396  CB  VAL A 571    10195   9531  12291   -875   4515  -1038  A    C  
ATOM   4397  CG1 VAL A 571     153.426  64.912  12.153  1.00 82.07      A    C  
ANISOU 4397  CG1 VAL A 571     9782   9343  12054   -767   4291   -970  A    C  
ATOM   4398  CG2 VAL A 571     154.075  62.598  11.529  1.00 86.83      A    C  
ANISOU 4398  CG2 VAL A 571    10226   9873  12891   -789   4547  -1132  A    C  
ATOM   4399  N   VAL A 572     151.074  61.887  11.489  1.00 80.94      A    N  
ANISOU 4399  N   VAL A 572     9836   9231  11685   -587   4133   -780  A    N  
ATOM   4400  CA  VAL A 572     150.298  61.268  12.574  1.00 78.46      A    C  
ANISOU 4400  CA  VAL A 572     9374   9024  11411   -410   3884   -678  A    C  
ATOM   4401  C   VAL A 572     151.016  60.023  13.096  1.00 82.38      A    C  
ANISOU 4401  C   VAL A 572     9616   9513  12171   -348   3920   -767  A    C  
ATOM   4402  O   VAL A 572     150.783  58.911  12.622  1.00 88.22      A    O  
ANISOU 4402  O   VAL A 572    10398  10217  12904   -347   3979   -776  A    O  
ATOM   4403  CB  VAL A 572     148.915  60.833  12.086  1.00 76.88      A    C  
ANISOU 4403  CB  VAL A 572     9393   8842  10974   -378   3779   -557  A    C  
ATOM   4404  CG1 VAL A 572     148.104  60.260  13.223  1.00 74.07      A    C  
ANISOU 4404  CG1 VAL A 572     8897   8600  10646   -222   3539   -460  A    C  
ATOM   4405  CG2 VAL A 572     148.184  61.991  11.425  1.00 79.27      A    C  
ANISOU 4405  CG2 VAL A 572     9969   9125  11024   -437   3731   -488  A    C  
ATOM   4406  N   HIS A 573     151.899  60.201  14.063  1.00 85.33      A    N  
ANISOU 4406  N   HIS A 573     9727   9909  12784   -292   3871   -838  A    N  
ATOM   4407  CA  HIS A 573     152.667  59.093  14.610  1.00 87.95      A    C  
ANISOU 4407  CA  HIS A 573     9805  10214  13396   -221   3872   -941  A    C  
ATOM   4408  C   HIS A 573     152.163  58.754  15.985  1.00 85.91      A    C  
ANISOU 4408  C   HIS A 573     9414  10038  13189    -59   3578   -839  A    C  
ATOM   4409  O   HIS A 573     152.174  59.602  16.871  1.00 86.29      A    O  
ANISOU 4409  O   HIS A 573     9389  10147  13252     -9   3429   -793  A    O  
ATOM   4410  CB  HIS A 573     154.140  59.466  14.696  1.00 98.29      A    C  
ANISOU 4410  CB  HIS A 573    10904  11468  14973   -281   4025  -1125  A    C  
ATOM   4411  CG  HIS A 573     154.956  58.533  15.536  1.00107.18      A    C  
ANISOU 4411  CG  HIS A 573    11728  12568  16426   -173   3949  -1238  A    C  
ATOM   4412  CD2 HIS A 573     155.216  58.523  16.865  1.00110.20      A    C  
ANISOU 4412  CD2 HIS A 573    11900  12985  16986    -38   3712  -1226  A    C  
ATOM   4413  ND1 HIS A 573     155.618  57.444  15.007  1.00114.01      A    N  
ANISOU 4413  ND1 HIS A 573    12493  13349  17477   -197   4114  -1393  A    N  
ATOM   4414  CE1 HIS A 573     156.241  56.798  15.975  1.00117.79      A    C  
ANISOU 4414  CE1 HIS A 573    12703  13807  18243    -71   3965  -1474  A    C  
ATOM   4415  NE2 HIS A 573     156.018  57.435  17.113  1.00115.22      A    N  
ANISOU 4415  NE2 HIS A 573    12317  13548  17912     24   3715  -1370  A    N  
ATOM   4416  N   ILE A 574     151.720  57.508  16.157  1.00 87.19      A    N  
ANISOU 4416  N   ILE A 574     9562  10194  13369     14   3497   -803  A    N  
ATOM   4417  CA  ILE A 574     151.143  57.051  17.423  1.00 86.32      A    C  
ANISOU 4417  CA  ILE A 574     9373  10150  13274    148   3220   -699  A    C  
ATOM   4418  C   ILE A 574     151.805  55.759  17.858  1.00 87.62      A    C  
ANISOU 4418  C   ILE A 574     9359  10242  13688    224   3173   -789  A    C  
ATOM   4419  O   ILE A 574     151.570  54.714  17.266  1.00 92.67      A    O  
ANISOU 4419  O   ILE A 574    10062  10838  14312    217   3242   -802  A    O  
ATOM   4420  CB  ILE A 574     149.624  56.827  17.303  1.00 82.72      A    C  
ANISOU 4420  CB  ILE A 574     9127   9767  12536    163   3113   -536  A    C  
ATOM   4421  CG1 ILE A 574     148.935  58.127  16.901  1.00 83.11      A    C  
ANISOU 4421  CG1 ILE A 574     9344   9877  12354    106   3125   -462  A    C  
ATOM   4422  CG2 ILE A 574     149.046  56.347  18.621  1.00 81.40      A    C  
ANISOU 4422  CG2 ILE A 574     8894   9664  12370    271   2850   -438  A    C  
ATOM   4423  CD1 ILE A 574     147.552  57.921  16.317  1.00 85.16      A    C  
ANISOU 4423  CD1 ILE A 574     9825  10178  12353     92   3089   -351  A    C  
ATOM   4424  N   GLU A 575     152.636  55.838  18.885  1.00 89.42      A    N  
ANISOU 4424  N   GLU A 575     9374  10451  14152    300   3042   -854  A    N  
ATOM   4425  CA  GLU A 575     153.336  54.669  19.377  1.00 93.93      A    C  
ANISOU 4425  CA  GLU A 575     9764  10934  14989    387   2957   -955  A    C  
ATOM   4426  C   GLU A 575     152.362  53.853  20.227  1.00 90.59      A    C  
ANISOU 4426  C   GLU A 575     9426  10543  14451    478   2698   -804  A    C  
ATOM   4427  O   GLU A 575     151.854  54.321  21.239  1.00 85.20      A    O  
ANISOU 4427  O   GLU A 575     8772   9928  13672    522   2490   -688  A    O  
ATOM   4428  CB  GLU A 575     154.576  55.095  20.155  1.00100.00      A    C  
ANISOU 4428  CB  GLU A 575    10281  11655  16057    436   2888  -1089  A    C  
ATOM   4429  CG  GLU A 575     155.678  54.050  20.248  1.00106.15      A    C  
ANISOU 4429  CG  GLU A 575    10833  12310  17186    499   2889  -1281  A    C  
ATOM   4430  CD  GLU A 575     157.026  54.640  20.733  1.00112.99      A    C  
ANISOU 4430  CD  GLU A 575    11433  13124  18372    521   2884  -1459  A    C  
ATOM   4431  OE1 GLU A 575     157.389  55.782  20.340  1.00107.50      A    O  
ANISOU 4431  OE1 GLU A 575    10729  12467  17649    423   3050  -1501  A    O  
ATOM   4432  OE2 GLU A 575     157.730  53.966  21.531  1.00113.72      A    O1-
ANISOU 4432  OE2 GLU A 575    11328  13128  18750    637   2696  -1562  A    O1-
ATOM   4433  N   ASN A 576     152.119  52.625  19.777  1.00 93.60      A    N  
ANISOU 4433  N   ASN A 576     9856  10870  14837    492   2728   -816  A    N  
ATOM   4434  CA  ASN A 576     151.034  51.742  20.249  1.00 92.54      A    C  
ANISOU 4434  CA  ASN A 576     9857  10763  14540    540   2543   -671  A    C  
ATOM   4435  C   ASN A 576     149.933  52.414  21.080  1.00 85.08      A    C  
ANISOU 4435  C   ASN A 576     9039   9936  13348    543   2363   -491  A    C  
ATOM   4436  O   ASN A 576     149.908  52.390  22.313  1.00 76.35      A    O  
ANISOU 4436  O   ASN A 576     7893   8838  12279    606   2130   -439  A    O  
ATOM   4437  CB  ASN A 576     151.589  50.476  20.927  1.00 95.97      A    C  
ANISOU 4437  CB  ASN A 576    10171  11086  15207    643   2372   -738  A    C  
ATOM   4438  CG  ASN A 576     152.486  50.784  22.103  1.00 96.90      A    C  
ANISOU 4438  CG  ASN A 576    10103  11153  15557    727   2172   -801  A    C  
ATOM   4439  ND2 ASN A 576     152.903  49.743  22.804  1.00 96.67      A    N  
ANISOU 4439  ND2 ASN A 576     9994  11015  15720    826   1967   -849  A    N  
ATOM   4440  OD1 ASN A 576     152.812  51.940  22.373  1.00102.44      A    O  
ANISOU 4440  OD1 ASN A 576    10742  11906  16272    705   2187   -810  A    O  
ATOM   4441  N   GLY A 577     149.019  53.014  20.333  1.00 86.44      A    N  
ANISOU 4441  N   GLY A 577     9377  10195  13270    467   2481   -410  A    N  
ATOM   4442  CA  GLY A 577     147.880  53.725  20.888  1.00 86.53      A    C  
ANISOU 4442  CA  GLY A 577     9508  10329  13040    455   2357   -267  A    C  
ATOM   4443  C   GLY A 577     146.703  52.800  21.072  1.00 82.73      A    C  
ANISOU 4443  C   GLY A 577     9164   9884  12384    459   2253   -156  A    C  
ATOM   4444  O   GLY A 577     146.670  51.703  20.523  1.00 81.61      A    O  
ANISOU 4444  O   GLY A 577     9060   9677  12271    460   2305   -177  A    O  
ATOM   4445  N   ARG A 578     145.728  53.252  21.844  1.00 79.06      A    N  
ANISOU 4445  N   ARG A 578     8774   9525  11738    452   2113    -46  A    N  
ATOM   4446  CA  ARG A 578     144.601  52.409  22.190  1.00 77.49      A    C  
ANISOU 4446  CA  ARG A 578     8698   9367  11376    441   2006     52  A    C  
ATOM   4447  C   ARG A 578     143.328  53.236  22.074  1.00 76.24      A    C  
ANISOU 4447  C   ARG A 578     8651   9344  10969    388   2013    129  A    C  
ATOM   4448  O   ARG A 578     143.368  54.463  22.113  1.00 77.04      A    O  
ANISOU 4448  O   ARG A 578     8726   9504  11040    380   2035    118  A    O  
ATOM   4449  CB  ARG A 578     144.775  51.873  23.604  1.00 76.04      A    C  
ANISOU 4449  CB  ARG A 578     8480   9156  11255    483   1780     88  A    C  
ATOM   4450  CG  ARG A 578     146.223  51.618  23.962  1.00 77.64      A    C  
ANISOU 4450  CG  ARG A 578     8521   9231  11745    555   1729    -13  A    C  
ATOM   4451  CD  ARG A 578     146.382  51.285  25.429  1.00 79.96      A    C  
ANISOU 4451  CD  ARG A 578     8808   9486  12085    596   1469     29  A    C  
ATOM   4452  NE  ARG A 578     146.005  52.382  26.316  1.00 77.47      A    N  
ANISOU 4452  NE  ARG A 578     8514   9269  11649    571   1377     91  A    N  
ATOM   4453  CZ  ARG A 578     146.836  53.314  26.747  1.00 76.96      A    C  
ANISOU 4453  CZ  ARG A 578     8329   9196  11714    604   1345     37  A    C  
ATOM   4454  NH1 ARG A 578     148.103  53.315  26.357  1.00 81.14      A    N1+
ANISOU 4454  NH1 ARG A 578     8695   9625  12507    657   1406    -86  A    N1+
ATOM   4455  NH2 ARG A 578     146.395  54.256  27.566  1.00 76.68      A    N  
ANISOU 4455  NH2 ARG A 578     8330   9253  11549    577   1258     98  A    N  
ATOM   4456  N   HIS A 579     142.210  52.544  21.904  1.00 72.76      A    N  
ANISOU 4456  N   HIS A 579     8331   8946  10368    355   1991    193  A    N  
ATOM   4457  CA  HIS A 579     140.898  53.147  21.849  1.00 69.18      A    C  
ANISOU 4457  CA  HIS A 579     7969   8617   9698    310   1978    246  A    C  
ATOM   4458  C   HIS A 579     140.415  53.420  23.271  1.00 65.85      A    C  
ANISOU 4458  C   HIS A 579     7533   8283   9203    297   1815    297  A    C  
ATOM   4459  O   HIS A 579     140.226  52.495  24.023  1.00 66.45      A    O  
ANISOU 4459  O   HIS A 579     7645   8339   9264    284   1709    340  A    O  
ATOM   4460  CB  HIS A 579     139.944  52.160  21.183  1.00 70.62      A    C  
ANISOU 4460  CB  HIS A 579     8269   8803   9760    274   2013    281  A    C  
ATOM   4461  CG  HIS A 579     138.631  52.755  20.814  1.00 71.97      A    C  
ANISOU 4461  CG  HIS A 579     8521   9083   9738    232   2023    304  A    C  
ATOM   4462  CD2 HIS A 579     138.075  53.007  19.605  1.00 74.06      A    C  
ANISOU 4462  CD2 HIS A 579     8872   9349   9917    216   2115    287  A    C  
ATOM   4463  ND1 HIS A 579     137.731  53.196  21.753  1.00 71.84      A    N  
ANISOU 4463  ND1 HIS A 579     8501   9187   9605    203   1919    334  A    N  
ATOM   4464  CE1 HIS A 579     136.675  53.700  21.135  1.00 75.69      A    C  
ANISOU 4464  CE1 HIS A 579     9044   9750   9963    179   1948    322  A    C  
ATOM   4465  NE2 HIS A 579     136.854  53.586  19.831  1.00 73.42      A    N  
ANISOU 4465  NE2 HIS A 579     8820   9386   9689    190   2052    298  A    N  
ATOM   4466  N   PRO A 580     140.178  54.688  23.636  1.00 62.71      A    N  
ANISOU 4466  N   PRO A 580     7103   7975   8746    291   1796    291  A    N  
ATOM   4467  CA  PRO A 580     139.942  55.050  25.023  1.00 61.85      A    C  
ANISOU 4467  CA  PRO A 580     6976   7934   8586    275   1656    323  A    C  
ATOM   4468  C   PRO A 580     138.656  54.518  25.625  1.00 63.96      A    C  
ANISOU 4468  C   PRO A 580     7339   8290   8673    203   1588    375  A    C  
ATOM   4469  O   PRO A 580     138.585  54.374  26.845  1.00 67.44      A    O  
ANISOU 4469  O   PRO A 580     7800   8748   9075    170   1468    408  A    O  
ATOM   4470  CB  PRO A 580     139.881  56.552  24.970  1.00 60.90      A    C  
ANISOU 4470  CB  PRO A 580     6808   7892   8437    284   1685    290  A    C  
ATOM   4471  CG  PRO A 580     139.387  56.850  23.606  1.00 60.81      A    C  
ANISOU 4471  CG  PRO A 580     6848   7892   8365    279   1811    263  A    C  
ATOM   4472  CD  PRO A 580     140.063  55.851  22.748  1.00 62.14      A    C  
ANISOU 4472  CD  PRO A 580     7032   7939   8636    293   1898    251  A    C  
ATOM   4473  N   VAL A 581     137.657  54.220  24.804  1.00 63.52      A    N  
ANISOU 4473  N   VAL A 581     7348   8282   8505    169   1663    375  A    N  
ATOM   4474  CA  VAL A 581     136.400  53.683  25.317  1.00 65.79      A    C  
ANISOU 4474  CA  VAL A 581     7714   8655   8626     86   1618    406  A    C  
ATOM   4475  C   VAL A 581     136.435  52.169  25.355  1.00 68.47      A    C  
ANISOU 4475  C   VAL A 581     8133   8909   8971     61   1586    453  A    C  
ATOM   4476  O   VAL A 581     136.145  51.590  26.396  1.00 70.31      A    O  
ANISOU 4476  O   VAL A 581     8430   9149   9133     -1   1486    496  A    O  
ATOM   4477  CB  VAL A 581     135.183  54.180  24.500  1.00 68.16      A    C  
ANISOU 4477  CB  VAL A 581     8033   9058   8807     59   1692    367  A    C  
ATOM   4478  CG1 VAL A 581     133.865  53.695  25.058  1.00 65.55      A    C  
ANISOU 4478  CG1 VAL A 581     7757   8828   8320    -38   1660    373  A    C  
ATOM   4479  CG2 VAL A 581     135.149  55.704  24.458  1.00 72.03      A    C  
ANISOU 4479  CG2 VAL A 581     8451   9620   9296     92   1702    312  A    C  
ATOM   4480  N   VAL A 582     136.807  51.529  24.239  1.00 72.95      A    N  
ANISOU 4480  N   VAL A 582     8713   9386   9617    104   1667    444  A    N  
ATOM   4481  CA  VAL A 582     136.856  50.033  24.137  1.00 72.58      A    C  
ANISOU 4481  CA  VAL A 582     8744   9246   9587     91   1641    480  A    C  
ATOM   4482  C   VAL A 582     137.880  49.438  25.109  1.00 75.12      A    C  
ANISOU 4482  C   VAL A 582     9051   9456  10031    123   1512    501  A    C  
ATOM   4483  O   VAL A 582     137.825  48.274  25.432  1.00 77.83      A    O  
ANISOU 4483  O   VAL A 582     9478   9728  10365    102   1435    539  A    O  
ATOM   4484  CB  VAL A 582     137.246  49.537  22.716  1.00 68.02      A    C  
ANISOU 4484  CB  VAL A 582     8174   8579   9091    137   1764    450  A    C  
ATOM   4485  CG1 VAL A 582     137.086  48.034  22.619  1.00 65.91      A    C  
ANISOU 4485  CG1 VAL A 582     7993   8231   8816    118   1734    485  A    C  
ATOM   4486  CG2 VAL A 582     136.427  50.217  21.639  1.00 66.73      A    C  
ANISOU 4486  CG2 VAL A 582     8037   8488   8826    121   1871    423  A    C  
ATOM   4487  N   GLU A 583     138.823  50.255  25.553  1.00 75.37      A    N  
ANISOU 4487  N   GLU A 583     8986   9466  10185    177   1476    470  A    N  
ATOM   4488  CA  GLU A 583     139.856  49.821  26.446  1.00 76.28      A    C  
ANISOU 4488  CA  GLU A 583     9074   9465  10443    223   1334    473  A    C  
ATOM   4489  C   GLU A 583     139.310  49.462  27.813  1.00 78.82      A    C  
ANISOU 4489  C   GLU A 583     9512   9805  10629    147   1165    541  A    C  
ATOM   4490  O   GLU A 583     139.875  48.597  28.477  1.00 80.88      A    O  
ANISOU 4490  O   GLU A 583     9824   9940  10965    166   1014    563  A    O  
ATOM   4491  CB  GLU A 583     140.888  50.920  26.603  1.00 78.07      A    C  
ANISOU 4491  CB  GLU A 583     9163   9679  10820    289   1339    418  A    C  
ATOM   4492  CG  GLU A 583     142.252  50.402  26.981  1.00 80.17      A    C  
ANISOU 4492  CG  GLU A 583     9349   9788  11323    371   1235    375  A    C  
ATOM   4493  CD  GLU A 583     143.224  51.519  27.239  1.00 81.46      A    C  
ANISOU 4493  CD  GLU A 583     9372   9944  11632    425   1231    316  A    C  
ATOM   4494  OE1 GLU A 583     142.866  52.697  27.019  1.00 77.22      A    O  
ANISOU 4494  OE1 GLU A 583     8809   9519  11009    400   1321    312  A    O  
ATOM   4495  OE2 GLU A 583     144.350  51.213  27.674  1.00 88.11      A    O1-
ANISOU 4495  OE2 GLU A 583    10129  10661  12686    496   1125    266  A    O1-
ATOM   4496  N   GLN A 584     138.232  50.115  28.249  1.00 79.19      A    N  
ANISOU 4496  N   GLN A 584     9609   9995  10482     56   1184    565  A    N  
ATOM   4497  CA  GLN A 584     137.588  49.711  29.500  1.00 81.58      A    C  
ANISOU 4497  CA  GLN A 584    10055  10320  10622    -52   1054    623  A    C  
ATOM   4498  C   GLN A 584     136.387  48.855  29.224  1.00 82.64      A    C  
ANISOU 4498  C   GLN A 584    10308  10506  10587   -154   1104    653  A    C  
ATOM   4499  O   GLN A 584     135.339  49.077  29.807  1.00 98.61      A    O  
ANISOU 4499  O   GLN A 584    12403  12641  12422   -275   1114    663  A    O  
ATOM   4500  CB  GLN A 584     137.131  50.904  30.330  1.00 81.44      A    C  
ANISOU 4500  CB  GLN A 584    10026  10428  10488   -113   1044    613  A    C  
ATOM   4501  CG  GLN A 584     138.204  51.465  31.218  1.00 86.06      A    C  
ANISOU 4501  CG  GLN A 584    10569  10942  11186    -58    913    611  A    C  
ATOM   4502  CD  GLN A 584     138.818  52.697  30.611  1.00 92.94      A    C  
ANISOU 4502  CD  GLN A 584    11269  11854  12189     37   1005    550  A    C  
ATOM   4503  NE2 GLN A 584     139.916  53.158  31.185  1.00 94.07      A    N  
ANISOU 4503  NE2 GLN A 584    11346  11920  12477    104    902    535  A    N  
ATOM   4504  OE1 GLN A 584     138.311  53.228  29.628  1.00106.39      A    O  
ANISOU 4504  OE1 GLN A 584    12907  13648  13865     46   1157    513  A    O  
ATOM   4505  N   GLN A 585     136.505  47.894  28.327  1.00 81.15      A    N  
ANISOU 4505  N   GLN A 585    10132  10237  10463   -114   1148    657  A    N  
ATOM   4506  CA  GLN A 585     135.384  47.023  28.038  1.00 81.89      A    C  
ANISOU 4506  CA  GLN A 585    10341  10370  10402   -210   1189    686  A    C  
ATOM   4507  C   GLN A 585     135.778  45.570  27.793  1.00 79.34      A    C  
ANISOU 4507  C   GLN A 585    10104   9895  10144   -184   1122    720  A    C  
ATOM   4508  O   GLN A 585     134.910  44.748  27.523  1.00 75.79      A    O  
ANISOU 4508  O   GLN A 585     9758   9462   9575   -263   1151    749  A    O  
ATOM   4509  CB  GLN A 585     134.624  47.554  26.818  1.00 89.23      A    C  
ANISOU 4509  CB  GLN A 585    11195  11411  11294   -202   1363    638  A    C  
ATOM   4510  CG  GLN A 585     133.819  48.822  27.062  1.00 92.82      A    C  
ANISOU 4510  CG  GLN A 585    11590  12033  11643   -253   1419    595  A    C  
ATOM   4511  CD  GLN A 585     133.194  49.352  25.789  1.00104.67      A    C  
ANISOU 4511  CD  GLN A 585    13023  13610  13136   -221   1551    540  A    C  
ATOM   4512  NE2 GLN A 585     133.718  50.465  25.308  1.00114.79      A    N  
ANISOU 4512  NE2 GLN A 585    14200  14905  14507   -136   1598    495  A    N  
ATOM   4513  OE1 GLN A 585     132.241  48.783  25.250  1.00111.72      A    O  
ANISOU 4513  OE1 GLN A 585    13967  14540  13938   -276   1599    535  A    O  
ATOM   4514  N   VAL A 586     137.067  45.252  27.917  1.00 81.15      A    N  
ANISOU 4514  N   VAL A 586    10289   9972  10569    -76   1026    709  A    N  
ATOM   4515  CA  VAL A 586     137.611  44.024  27.328  1.00 84.98      A    C  
ANISOU 4515  CA  VAL A 586    10800  10309  11180    -10   1000    705  A    C  
ATOM   4516  C   VAL A 586     138.581  43.205  28.204  1.00 91.88      A    C  
ANISOU 4516  C   VAL A 586    11730  10998  12180     43    779    718  A    C  
ATOM   4517  O   VAL A 586     139.102  42.170  27.785  1.00 93.57      A    O  
ANISOU 4517  O   VAL A 586    11956  11075  12521    109    735    698  A    O  
ATOM   4518  CB  VAL A 586     138.335  44.368  26.012  1.00 82.49      A    C  
ANISOU 4518  CB  VAL A 586    10323   9972  11045    102   1160    625  A    C  
ATOM   4519  CG1 VAL A 586     137.347  44.793  24.918  1.00 76.41      A    C  
ANISOU 4519  CG1 VAL A 586     9548   9332  10151     57   1349    617  A    C  
ATOM   4520  CG2 VAL A 586     139.371  45.451  26.271  1.00 82.71      A    C  
ANISOU 4520  CG2 VAL A 586    10200   9991  11232    182   1152    570  A    C  
ATOM   4521  N   ARG A 587     138.831  43.672  29.413  1.00100.02      A    N  
ANISOU 4521  N   ARG A 587    12802  12015  13184     18    626    742  A    N  
ATOM   4522  CA  ARG A 587     139.829  43.062  30.277  1.00107.12      A    C  
ANISOU 4522  CA  ARG A 587    13750  12726  14223     82    385    743  A    C  
ATOM   4523  C   ARG A 587     141.229  43.062  29.680  1.00110.17      A    C  
ANISOU 4523  C   ARG A 587    13936  12993  14929    254    385    641  A    C  
ATOM   4524  O   ARG A 587     142.151  43.528  30.347  1.00129.97      A    O  
ANISOU 4524  O   ARG A 587    16368  15426  17584    324    253    605  A    O  
ATOM   4525  CB  ARG A 587     139.437  41.658  30.670  1.00112.37      A    C  
ANISOU 4525  CB  ARG A 587    14631  13272  14791     20    236    806  A    C  
ATOM   4526  CG  ARG A 587     140.046  41.240  32.000  1.00122.05      A    C  
ANISOU 4526  CG  ARG A 587    16002  14326  16045     24    -66    839  A    C  
ATOM   4527  CD  ARG A 587     139.720  39.792  32.306  1.00133.46      A    C  
ANISOU 4527  CD  ARG A 587    17679  15627  17400    -32   -228    899  A    C  
ATOM   4528  NE  ARG A 587     140.388  38.855  31.386  1.00140.83      A    N  
ANISOU 4528  NE  ARG A 587    18518  16432  18559    105   -226    835  A    N  
ATOM   4529  CZ  ARG A 587     139.821  38.256  30.331  1.00135.89      A    C  
ANISOU 4529  CZ  ARG A 587    17883  15856  17892     87    -55    833  A    C  
ATOM   4530  NH1 ARG A 587     138.544  38.475  30.009  1.00132.50      A    N1+
ANISOU 4530  NH1 ARG A 587    17522  15601  17219    -53    125    889  A    N1+
ATOM   4531  NH2 ARG A 587     140.541  37.426  29.587  1.00132.41      A    N  
ANISOU 4531  NH2 ARG A 587    17358  15283  17669    215    -67    762  A    N  
ATOM   4532  N   HIS A 588     141.415  42.553  28.459  1.00106.91      A    N  
ANISOU 4532  N   HIS A 588    13437  12555  14629    315    534    585  A    N  
ATOM   4533  CA  HIS A 588     142.705  42.736  27.745  1.00107.57      A    C  
ANISOU 4533  CA  HIS A 588    13303  12556  15011    454    604    462  A    C  
ATOM   4534  C   HIS A 588     142.482  43.346  26.349  1.00 95.98      A    C  
ANISOU 4534  C   HIS A 588    11723  11206  13536    449    898    414  A    C  
ATOM   4535  O   HIS A 588     141.683  42.823  25.577  1.00 92.16      A    O  
ANISOU 4535  O   HIS A 588    11323  10767  12927    398   1013    445  A    O  
ATOM   4536  CB  HIS A 588     143.496  41.412  27.641  1.00116.57      A    C  
ANISOU 4536  CB  HIS A 588    14438  13493  16357    548    473    401  A    C  
ATOM   4537  CG  HIS A 588     143.912  40.814  28.970  1.00128.49      A    C  
ANISOU 4537  CG  HIS A 588    16059  14844  17915    576    146    430  A    C  
ATOM   4538  CD2 HIS A 588     143.505  39.684  29.606  1.00127.94      A    C  
ANISOU 4538  CD2 HIS A 588    16207  14661  17742    535    -61    503  A    C  
ATOM   4539  ND1 HIS A 588     144.888  41.369  29.779  1.00128.84      A    N  
ANISOU 4539  ND1 HIS A 588    16007  14810  18136    653    -20    376  A    N  
ATOM   4540  CE1 HIS A 588     145.043  40.625  30.862  1.00124.99      A    C  
ANISOU 4540  CE1 HIS A 588    15682  14164  17644    660   -326    418  A    C  
ATOM   4541  NE2 HIS A 588     144.220  39.594  30.780  1.00124.42      A    N  
ANISOU 4541  NE2 HIS A 588    15809  14065  17399    586   -355    497  A    N  
ATOM   4542  N   PHE A 589     143.167  44.459  26.054  1.00 88.34      A    N  
ANISOU 4542  N   PHE A 589    10590  10282  12693    496   1005    341  A    N  
ATOM   4543  CA  PHE A 589     143.050  45.187  24.766  1.00 86.60      A    C  
ANISOU 4543  CA  PHE A 589    10288  10156  12458    483   1269    294  A    C  
ATOM   4544  C   PHE A 589     144.418  45.405  24.158  1.00 87.30      A    C  
ANISOU 4544  C   PHE A 589    10188  10153  12826    572   1367    156  A    C  
ATOM   4545  O   PHE A 589     145.288  46.005  24.792  1.00 86.15      A    O  
ANISOU 4545  O   PHE A 589     9922   9974  12837    623   1285    103  A    O  
ATOM   4546  CB  PHE A 589     142.430  46.581  24.978  1.00 88.07      A    C  
ANISOU 4546  CB  PHE A 589    10471  10503  12485    424   1328    336  A    C  
ATOM   4547  CG  PHE A 589     142.355  47.443  23.726  1.00 84.01      A    C  
ANISOU 4547  CG  PHE A 589     9898  10065  11953    414   1563    289  A    C  
ATOM   4548  CD1 PHE A 589     143.446  48.189  23.298  1.00 85.10      A    C  
ANISOU 4548  CD1 PHE A 589     9889  10167  12275    465   1662    192  A    C  
ATOM   4549  CD2 PHE A 589     141.175  47.537  23.009  1.00 81.51      A    C  
ANISOU 4549  CD2 PHE A 589     9687   9849  11432    345   1670    336  A    C  
ATOM   4550  CE1 PHE A 589     143.366  48.978  22.162  1.00 84.85      A    C  
ANISOU 4550  CE1 PHE A 589     9846  10189  12204    436   1867    154  A    C  
ATOM   4551  CE2 PHE A 589     141.087  48.308  21.866  1.00 80.70      A    C  
ANISOU 4551  CE2 PHE A 589     9567   9793  11301    334   1853    296  A    C  
ATOM   4552  CZ  PHE A 589     142.181  49.036  21.443  1.00 83.71      A    C  
ANISOU 4552  CZ  PHE A 589     9829  10130  11845    375   1952    210  A    C  
ATOM   4553  N   THR A 590     144.611  44.971  22.921  1.00 88.45      A    N  
ANISOU 4553  N   THR A 590    10309  10263  13035    578   1553     87  A    N  
ATOM   4554  CA  THR A 590     145.960  44.963  22.346  1.00 94.57      A    C  
ANISOU 4554  CA  THR A 590    10905  10934  14093    647   1659    -69  A    C  
ATOM   4555  C   THR A 590     146.236  46.291  21.632  1.00 91.25      A    C  
ANISOU 4555  C   THR A 590    10406  10595  13669    610   1869   -121  A    C  
ATOM   4556  O   THR A 590     145.496  46.661  20.715  1.00 86.40      A    O  
ANISOU 4556  O   THR A 590     9889  10062  12874    540   2035    -81  A    O  
ATOM   4557  CB  THR A 590     146.187  43.737  21.406  1.00 98.84      A    C  
ANISOU 4557  CB  THR A 590    11456  11369  14728    668   1759   -143  A    C  
ATOM   4558  CG2 THR A 590     145.441  42.489  21.929  1.00100.83      A    C  
ANISOU 4558  CG2 THR A 590    11864  11574  14872    668   1573    -46  A    C  
ATOM   4559  OG1 THR A 590     145.751  44.026  20.070  1.00101.83      A    O  
ANISOU 4559  OG1 THR A 590    11896  11809  14982    597   2015   -151  A    O  
ATOM   4560  N   ALA A 591     147.290  47.002  22.058  1.00 88.83      A    N  
ANISOU 4560  N   ALA A 591     9933  10257  13560    655   1847   -210  A    N  
ATOM   4561  CA  ALA A 591     147.642  48.312  21.462  1.00 86.54      A    C  
ANISOU 4561  CA  ALA A 591     9573  10034  13273    613   2034   -263  A    C  
ATOM   4562  C   ALA A 591     148.179  48.151  20.048  1.00 87.04      A    C  
ANISOU 4562  C   ALA A 591     9603  10044  13422    577   2303   -383  A    C  
ATOM   4563  O   ALA A 591     148.500  47.055  19.646  1.00 96.85      A    O  
ANISOU 4563  O   ALA A 591    10826  11190  14780    603   2337   -453  A    O  
ATOM   4564  CB  ALA A 591     148.635  49.074  22.325  1.00 84.65      A    C  
ANISOU 4564  CB  ALA A 591     9164   9769  13227    664   1934   -330  A    C  
ATOM   4565  N   ASN A 592     148.232  49.238  19.286  1.00 86.53      A    N  
ANISOU 4565  N   ASN A 592     9554  10036  13286    508   2493   -407  A    N  
ATOM   4566  CA  ASN A 592     148.670  49.197  17.893  1.00 85.69      A    C  
ANISOU 4566  CA  ASN A 592     9464   9878  13213    440   2768   -515  A    C  
ATOM   4567  C   ASN A 592     149.227  50.543  17.480  1.00 86.16      A    C  
ANISOU 4567  C   ASN A 592     9481   9966  13286    378   2923   -578  A    C  
ATOM   4568  O   ASN A 592     148.795  51.600  17.961  1.00 79.63      A    O  
ANISOU 4568  O   ASN A 592     8689   9230  12337    369   2843   -492  A    O  
ATOM   4569  CB  ASN A 592     147.530  48.817  16.932  1.00 85.73      A    C  
ANISOU 4569  CB  ASN A 592     9692   9917  12964    376   2859   -425  A    C  
ATOM   4570  CG  ASN A 592     147.240  47.324  16.901  1.00 89.48      A    C  
ANISOU 4570  CG  ASN A 592    10210  10328  13461    415   2795   -412  A    C  
ATOM   4571  ND2 ASN A 592     148.235  46.506  17.133  1.00 94.55      A    N  
ANISOU 4571  ND2 ASN A 592    10699  10861  14364    478   2776   -536  A    N  
ATOM   4572  OD1 ASN A 592     146.121  46.923  16.651  1.00100.28      A    O  
ANISOU 4572  OD1 ASN A 592    11743  11739  14618    389   2760   -302  A    O  
ATOM   4573  N   HIS A 593     150.178  50.480  16.558  1.00 92.69      A    N  
ANISOU 4573  N   HIS A 593    10242  10711  14262    324   3157   -735  A    N  
ATOM   4574  CA  HIS A 593     150.899  51.648  16.088  1.00 91.66      A    C  
ANISOU 4574  CA  HIS A 593    10068  10583  14174    244   3334   -825  A    C  
ATOM   4575  C   HIS A 593     150.129  52.322  14.994  1.00 87.50      A    C  
ANISOU 4575  C   HIS A 593     9785  10094  13366    131   3486   -752  A    C  
ATOM   4576  O   HIS A 593     149.165  51.788  14.456  1.00 81.01      A    O  
ANISOU 4576  O   HIS A 593     9146   9282  12351    114   3484   -662  A    O  
ATOM   4577  CB  HIS A 593     152.277  51.245  15.562  1.00 97.99      A    C  
ANISOU 4577  CB  HIS A 593    10695  11274  15261    213   3538  -1049  A    C  
ATOM   4578  CG  HIS A 593     153.121  50.571  16.588  1.00103.42      A    C  
ANISOU 4578  CG  HIS A 593    11127  11901  16264    336   3372  -1150  A    C  
ATOM   4579  CD2 HIS A 593     153.409  49.265  16.786  1.00109.16      A    C  
ANISOU 4579  CD2 HIS A 593    11759  12543  17171    419   3296  -1223  A    C  
ATOM   4580  ND1 HIS A 593     153.737  51.260  17.608  1.00108.23      A    N  
ANISOU 4580  ND1 HIS A 593    11562  12524  17034    395   3226  -1179  A    N  
ATOM   4581  CE1 HIS A 593     154.391  50.410  18.381  1.00112.40      A    C  
ANISOU 4581  CE1 HIS A 593    11900  12972  17833    510   3062  -1271  A    C  
ATOM   4582  NE2 HIS A 593     154.211  49.193  17.901  1.00114.98      A    N  
ANISOU 4582  NE2 HIS A 593    12271  13236  18181    528   3098  -1303  A    N  
ATOM   4583  N   THR A 594     150.566  53.524  14.676  1.00 91.39      A    N  
ANISOU 4583  N   THR A 594    10289  10596  13839     54   3603   -795  A    N  
ATOM   4584  CA  THR A 594     150.005  54.258  13.568  1.00 95.10      A    C  
ANISOU 4584  CA  THR A 594    11005  11069  14057    -63   3747   -748  A    C  
ATOM   4585  C   THR A 594     151.067  55.221  13.071  1.00101.59      A    C  
ANISOU 4585  C   THR A 594    11789  11844  14964   -172   3953   -878  A    C  
ATOM   4586  O   THR A 594     151.420  56.167  13.777  1.00101.50      A    O  
ANISOU 4586  O   THR A 594    11672  11877  15017   -149   3874   -877  A    O  
ATOM   4587  CB  THR A 594     148.749  55.026  13.977  1.00 90.99      A    C  
ANISOU 4587  CB  THR A 594    10623  10656  13292    -28   3553   -574  A    C  
ATOM   4588  CG2 THR A 594     148.183  55.764  12.791  1.00 88.84      A    C  
ANISOU 4588  CG2 THR A 594    10616  10362  12774   -138   3671   -539  A    C  
ATOM   4589  OG1 THR A 594     147.769  54.109  14.488  1.00 93.56      A    O  
ANISOU 4589  OG1 THR A 594    10974  11029  13543     56   3375   -467  A    O  
ATOM   4590  N   ASP A 595     151.585  54.947  11.871  1.00107.43      A    N  
ANISOU 4590  N   ASP A 595    12622  12489  15705   -299   4223   -995  A    N  
ATOM   4591  CA  ASP A 595     152.588  55.797  11.228  1.00106.94      A    C  
ANISOU 4591  CA  ASP A 595    12564  12368  15700   -443   4466  -1134  A    C  
ATOM   4592  C   ASP A 595     152.116  56.317   9.881  1.00102.61      A    C  
ANISOU 4592  C   ASP A 595    12357  11766  14865   -604   4636  -1099  A    C  
ATOM   4593  O   ASP A 595     151.898  55.527   8.966  1.00103.24      A    O  
ANISOU 4593  O   ASP A 595    12589  11779  14859   -668   4769  -1122  A    O  
ATOM   4594  CB  ASP A 595     153.885  55.026  11.038  1.00107.54      A    C  
ANISOU 4594  CB  ASP A 595    12419  12361  16078   -480   4672  -1358  A    C  
ATOM   4595  CG  ASP A 595     154.773  55.088  12.244  1.00111.42      A    C  
ANISOU 4595  CG  ASP A 595    12572  12876  16887   -370   4548  -1449  A    C  
ATOM   4596  OD1 ASP A 595     154.656  56.026  13.050  1.00107.52      A    O  
ANISOU 4596  OD1 ASP A 595    12030  12450  16370   -320   4382  -1367  A    O  
ATOM   4597  OD2 ASP A 595     155.611  54.186  12.387  1.00129.61      A    O1-
ANISOU 4597  OD2 ASP A 595    14653  15121  19470   -331   4609  -1615  A    O1-
ATOM   4598  N   LEU A 596     151.938  57.635   9.780  1.00 95.43      A    N  
ANISOU 4598  N   LEU A 596    11583  10875  13802   -665   4612  -1040  A    N  
ATOM   4599  CA  LEU A 596     151.607  58.279   8.522  1.00 97.34      A    C  
ANISOU 4599  CA  LEU A 596    12171  11039  13775   -828   4755  -1017  A    C  
ATOM   4600  C   LEU A 596     152.336  59.621   8.403  1.00106.24      A    C  
ANISOU 4600  C   LEU A 596    13329  12138  14897   -947   4859  -1079  A    C  
ATOM   4601  O   LEU A 596     152.532  60.317   9.399  1.00106.37      A    O  
ANISOU 4601  O   LEU A 596    13164  12230  15019   -862   4714  -1055  A    O  
ATOM   4602  CB  LEU A 596     150.109  58.506   8.392  1.00 94.01      A    C  
ANISOU 4602  CB  LEU A 596    11989  10657  13072   -763   4532   -826  A    C  
ATOM   4603  CG  LEU A 596     149.228  57.280   8.174  1.00 97.66      A    C  
ANISOU 4603  CG  LEU A 596    12517  11125  13462   -693   4458   -757  A    C  
ATOM   4604  CD1 LEU A 596     148.814  56.677   9.509  1.00 99.43      A    C  
ANISOU 4604  CD1 LEU A 596    12487  11466  13824   -504   4219   -686  A    C  
ATOM   4605  CD2 LEU A 596     147.982  57.652   7.385  1.00103.50      A    C  
ANISOU 4605  CD2 LEU A 596    13595  11838  13890   -722   4358   -631  A    C  
ATOM   4606  N   ASP A 597     152.734  59.972   7.175  1.00114.00      A    N  
ANISOU 4606  N   ASP A 597    14562  13005  15745  -1154   5113  -1157  A    N  
ATOM   4607  CA  ASP A 597     153.404  61.244   6.873  1.00110.78      A    C  
ANISOU 4607  CA  ASP A 597    14252  12548  15291  -1306   5240  -1218  A    C  
ATOM   4608  C   ASP A 597     152.997  61.735   5.483  1.00109.24      A    C  
ANISOU 4608  C   ASP A 597    14510  12225  14770  -1498   5364  -1184  A    C  
ATOM   4609  O   ASP A 597     151.971  61.297   4.935  1.00105.89      A    O  
ANISOU 4609  O   ASP A 597    14321  11773  14139  -1468   5265  -1074  A    O  
ATOM   4610  CB  ASP A 597     154.922  61.079   6.962  1.00115.33      A    C  
ANISOU 4610  CB  ASP A 597    14566  13091  16161  -1406   5507  -1443  A    C  
ATOM   4611  CG  ASP A 597     155.420  59.880   6.196  1.00122.63      A    C  
ANISOU 4611  CG  ASP A 597    15477  13940  17177  -1498   5768  -1591  A    C  
ATOM   4612  OD1 ASP A 597     155.110  59.740   4.984  1.00126.20      A    O  
ANISOU 4612  OD1 ASP A 597    16266  14291  17391  -1653   5928  -1586  A    O  
ATOM   4613  OD2 ASP A 597     156.122  59.058   6.823  1.00130.23      A    O1-
ANISOU 4613  OD2 ASP A 597    16093  14934  18454  -1408   5799  -1719  A    O1-
ATOM   4614  N   HIS A 598     153.794  62.641   4.917  1.00110.52      A    N  
ANISOU 4614  N   HIS A 598    14809  12301  14882  -1697   5569  -1279  A    N  
ATOM   4615  CA  HIS A 598     153.513  63.150   3.589  1.00116.30      A    C  
ANISOU 4615  CA  HIS A 598    16005  12887  15294  -1905   5688  -1255  A    C  
ATOM   4616  C   HIS A 598     153.528  62.046   2.528  1.00119.48      A    C  
ANISOU 4616  C   HIS A 598    16584  13192  15621  -2023   5908  -1324  A    C  
ATOM   4617  O   HIS A 598     152.688  62.051   1.620  1.00114.66      A    O  
ANISOU 4617  O   HIS A 598    16358  12486  14720  -2085   5856  -1226  A    O  
ATOM   4618  CB  HIS A 598     154.494  64.255   3.206  1.00123.81      A    C  
ANISOU 4618  CB  HIS A 598    17066  13755  16220  -2124   5898  -1363  A    C  
ATOM   4619  CG  HIS A 598     153.925  65.212   2.213  1.00130.82      A    C  
ANISOU 4619  CG  HIS A 598    18454  14508  16742  -2276   5861  -1271  A    C  
ATOM   4620  CD2 HIS A 598     153.809  66.565   2.228  1.00134.85      A    C  
ANISOU 4620  CD2 HIS A 598    19154  14979  17101  -2325   5742  -1205  A    C  
ATOM   4621  ND1 HIS A 598     153.334  64.786   1.044  1.00129.50      A    N  
ANISOU 4621  ND1 HIS A 598    18679  14213  16311  -2387   5915  -1230  A    N  
ATOM   4622  CE1 HIS A 598     152.898  65.834   0.367  1.00132.61      A    C  
ANISOU 4622  CE1 HIS A 598    19491  14485  16408  -2500   5826  -1147  A    C  
ATOM   4623  NE2 HIS A 598     153.169  66.924   1.066  1.00138.82      A    N  
ANISOU 4623  NE2 HIS A 598    20162  15324  17259  -2464   5719  -1130  A    N  
ATOM   4624  N   LYS A 599     154.472  61.106   2.651  1.00121.41      A    N  
ANISOU 4624  N   LYS A 599    16545  13451  16134  -2050   6140  -1498  A    N  
ATOM   4625  CA  LYS A 599     154.664  60.053   1.651  1.00122.48      A    C  
ANISOU 4625  CA  LYS A 599    16817  13490  16229  -2180   6395  -1602  A    C  
ATOM   4626  C   LYS A 599     153.826  58.817   1.921  1.00122.27      A    C  
ANISOU 4626  C   LYS A 599    16695  13522  16238  -1983   6220  -1512  A    C  
ATOM   4627  O   LYS A 599     153.709  57.959   1.060  1.00135.71      A    O  
ANISOU 4627  O   LYS A 599    18565  15144  17854  -2069   6372  -1554  A    O  
ATOM   4628  CB  LYS A 599     156.135  59.639   1.588  1.00128.31      A    C  
ANISOU 4628  CB  LYS A 599    17290  14206  17255  -2317   6750  -1868  A    C  
ATOM   4629  CG  LYS A 599     157.081  60.752   1.182  1.00134.32      A    C  
ANISOU 4629  CG  LYS A 599    18155  14895  17984  -2561   6993  -1994  A    C  
ATOM   4630  CD  LYS A 599     156.973  61.079  -0.300  1.00137.49      A    C  
ANISOU 4630  CD  LYS A 599    19082  15125  18032  -2851   7219  -2004  A    C  
ATOM   4631  CE  LYS A 599     157.458  62.498  -0.572  1.00144.09      A    C  
ANISOU 4631  CE  LYS A 599    20125  15891  18730  -3055   7313  -2026  A    C  
ATOM   4632  NZ  LYS A 599     158.891  62.703  -0.197  1.00147.55      A    N1+
ANISOU 4632  NZ  LYS A 599    20224  16360  19479  -3171   7592  -2268  A    N1+
ATOM   4633  N   HIS A 600     153.279  58.699   3.125  1.00119.74      A    N  
ANISOU 4633  N   HIS A 600    16106  13340  16047  -1733   5913  -1397  A    N  
ATOM   4634  CA  HIS A 600     152.401  57.581   3.487  1.00110.38      A    C  
ANISOU 4634  CA  HIS A 600    14837  12217  14885  -1545   5718  -1298  A    C  
ATOM   4635  C   HIS A 600     151.097  58.147   4.028  1.00103.52      A    C  
ANISOU 4635  C   HIS A 600    14061  11428  13843  -1386   5360  -1079  A    C  
ATOM   4636  O   HIS A 600     150.970  58.378   5.223  1.00101.94      A    O  
ANISOU 4636  O   HIS A 600    13598  11349  13785  -1219   5150  -1024  A    O  
ATOM   4637  CB  HIS A 600     153.067  56.705   4.546  1.00109.63      A    C  
ANISOU 4637  CB  HIS A 600    14290  12209  15155  -1395   5699  -1398  A    C  
ATOM   4638  CG  HIS A 600     154.242  55.947   4.036  1.00115.21      A    C  
ANISOU 4638  CG  HIS A 600    14868  12840  16067  -1519   6031  -1632  A    C  
ATOM   4639  CD2 HIS A 600     154.527  54.626   4.062  1.00120.49      A    C  
ANISOU 4639  CD2 HIS A 600    15356  13497  16925  -1459   6106  -1736  A    C  
ATOM   4640  ND1 HIS A 600     155.301  56.556   3.399  1.00120.93      A    N  
ANISOU 4640  ND1 HIS A 600    15640  13483  16821  -1741   6342  -1806  A    N  
ATOM   4641  CE1 HIS A 600     156.188  55.643   3.049  1.00129.43      A    C  
ANISOU 4641  CE1 HIS A 600    16560  14509  18108  -1816   6607  -2021  A    C  
ATOM   4642  NE2 HIS A 600     155.744  54.463   3.442  1.00131.88      A    N  
ANISOU 4642  NE2 HIS A 600    16727  14857  18523  -1640   6462  -1982  A    N  
ATOM   4643  N   ARG A 601     150.130  58.360   3.144  1.00101.31      A    N  
ANISOU 4643  N   ARG A 601    14158  11076  13259  -1440   5287   -969  A    N  
ATOM   4644  CA  ARG A 601     148.915  59.109   3.485  1.00100.80      A    C  
ANISOU 4644  CA  ARG A 601    14216  11066  13015  -1320   4966   -793  A    C  
ATOM   4645  C   ARG A 601     147.630  58.297   3.566  1.00 96.77      A    C  
ANISOU 4645  C   ARG A 601    13751  10603  12413  -1176   4745   -668  A    C  
ATOM   4646  O   ARG A 601     146.689  58.685   4.257  1.00102.17      A    O  
ANISOU 4646  O   ARG A 601    14383  11383  13053  -1028   4468   -549  A    O  
ATOM   4647  CB  ARG A 601     148.677  60.221   2.473  1.00100.72      A    C  
ANISOU 4647  CB  ARG A 601    14620  10926  12722  -1479   4982   -760  A    C  
ATOM   4648  CG  ARG A 601     149.629  61.381   2.623  1.00102.69      A    C  
ANISOU 4648  CG  ARG A 601    14843  11154  13020  -1590   5095   -835  A    C  
ATOM   4649  CD  ARG A 601     148.983  62.643   2.086  1.00104.83      A    C  
ANISOU 4649  CD  ARG A 601    15477  11339  13014  -1650   4940   -740  A    C  
ATOM   4650  NE  ARG A 601     148.624  62.534   0.678  1.00105.26      A    N  
ANISOU 4650  NE  ARG A 601    15987  11216  12791  -1814   5023   -729  A    N  
ATOM   4651  CZ  ARG A 601     149.486  62.669  -0.320  1.00105.56      A    C  
ANISOU 4651  CZ  ARG A 601    16272  11104  12732  -2069   5323   -838  A    C  
ATOM   4652  NH1 ARG A 601     150.768  62.896  -0.063  1.00104.03      A    N1+
ANISOU 4652  NH1 ARG A 601    15880  10925  12719  -2185   5581   -981  A    N1+
ATOM   4653  NH2 ARG A 601     149.065  62.570  -1.579  1.00108.83      A    N  
ANISOU 4653  NH2 ARG A 601    17137  11346  12867  -2217   5367   -814  A    N  
ATOM   4654  N   LEU A 602     147.555  57.200   2.843  1.00 90.80      A    N  
ANISOU 4654  N   LEU A 602    13097   9780  11623  -1226   4871   -699  A    N  
ATOM   4655  CA  LEU A 602     146.346  56.460   2.851  1.00 90.91      A    C  
ANISOU 4655  CA  LEU A 602    13172   9829  11540  -1106   4671   -586  A    C  
ATOM   4656  C   LEU A 602     146.651  55.049   3.260  1.00 92.78      A    C  
ANISOU 4656  C   LEU A 602    13159  10113  11980  -1033   4743   -639  A    C  
ATOM   4657  O   LEU A 602     147.386  54.364   2.578  1.00 96.58      A    O  
ANISOU 4657  O   LEU A 602    13679  10503  12511  -1146   4994   -754  A    O  
ATOM   4658  CB  LEU A 602     145.689  56.523   1.487  1.00 93.18      A    C  
ANISOU 4658  CB  LEU A 602    13896   9968  11536  -1227   4688   -545  A    C  
ATOM   4659  CG  LEU A 602     144.246  56.018   1.492  1.00 99.17      A    C  
ANISOU 4659  CG  LEU A 602    14741  10765  12173  -1096   4427   -417  A    C  
ATOM   4660  CD1 LEU A 602     143.372  56.851   0.556  1.00100.78      A    C  
ANISOU 4660  CD1 LEU A 602    15348  10853  12089  -1156   4282   -344  A    C  
ATOM   4661  CD2 LEU A 602     144.166  54.527   1.139  1.00102.37      A    C  
ANISOU 4661  CD2 LEU A 602    15130  11146  12618  -1092   4526   -440  A    C  
ATOM   4662  N   MET A 603     146.100  54.625   4.400  1.00 94.88      A    N  
ANISOU 4662  N   MET A 603    13173  10512  12363   -849   4522   -562  A    N  
ATOM   4663  CA  MET A 603     146.263  53.260   4.890  1.00 94.56      A    C  
ANISOU 4663  CA  MET A 603    12911  10511  12506   -760   4534   -594  A    C  
ATOM   4664  C   MET A 603     145.051  52.488   4.475  1.00 96.32      A    C  
ANISOU 4664  C   MET A 603    13306  10727  12562   -716   4406   -491  A    C  
ATOM   4665  O   MET A 603     143.935  52.840   4.835  1.00 97.61      A    O  
ANISOU 4665  O   MET A 603    13517  10963  12606   -629   4168   -368  A    O  
ATOM   4666  CB  MET A 603     146.356  53.237   6.397  1.00 94.54      A    C  
ANISOU 4666  CB  MET A 603    12569  10644  12708   -602   4354   -565  A    C  
ATOM   4667  CG  MET A 603     146.446  51.854   7.001  1.00 99.06      A    C  
ANISOU 4667  CG  MET A 603    12933  11245  13457   -499   4315   -585  A    C  
ATOM   4668  SD  MET A 603     146.527  52.005   8.805  1.00108.20      A    S  
ANISOU 4668  SD  MET A 603    13752  12542  14816   -331   4073   -539  A    S  
ATOM   4669  CE  MET A 603     148.147  52.771   9.011  1.00109.07      A    C  
ANISOU 4669  CE  MET A 603    13667  12616  15158   -392   4253   -702  A    C  
ATOM   4670  N   LEU A 604     145.267  51.433   3.705  1.00103.20      A    N  
ANISOU 4670  N   LEU A 604    14266  11509  13433   -778   4568   -552  A    N  
ATOM   4671  CA  LEU A 604     144.178  50.623   3.212  1.00101.36      A    C  
ANISOU 4671  CA  LEU A 604    14210  11255  13044   -750   4466   -464  A    C  
ATOM   4672  C   LEU A 604     144.100  49.375   4.070  1.00 97.94      A    C  
ANISOU 4672  C   LEU A 604    13524  10896  12791   -620   4383   -456  A    C  
ATOM   4673  O   LEU A 604     144.964  48.510   3.981  1.00 96.55      A    O  
ANISOU 4673  O   LEU A 604    13230  10671  12781   -640   4552   -569  A    O  
ATOM   4674  CB  LEU A 604     144.409  50.287   1.744  1.00102.85      A    C  
ANISOU 4674  CB  LEU A 604    14707  11283  13085   -914   4690   -530  A    C  
ATOM   4675  CG  LEU A 604     143.123  49.983   1.000  1.00107.51      A    C  
ANISOU 4675  CG  LEU A 604    15589  11826  13434   -912   4548   -420  A    C  
ATOM   4676  CD1 LEU A 604     143.208  50.553  -0.402  1.00108.44      A    C  
ANISOU 4676  CD1 LEU A 604    16106  11778  13318  -1095   4688   -449  A    C  
ATOM   4677  CD2 LEU A 604     142.874  48.479   0.978  1.00117.27      A    C  
ANISOU 4677  CD2 LEU A 604    16762  13061  14733   -857   4559   -422  A    C  
ATOM   4678  N   LEU A 605     143.078  49.309   4.926  1.00 95.23      A    N  
ANISOU 4678  N   LEU A 605    13098  10667  12418   -493   4122   -333  A    N  
ATOM   4679  CA  LEU A 605     142.864  48.153   5.775  1.00 92.08      A    C  
ANISOU 4679  CA  LEU A 605    12504  10331  12152   -380   4012   -306  A    C  
ATOM   4680  C   LEU A 605     142.034  47.158   5.052  1.00 92.76      A    C  
ANISOU 4680  C   LEU A 605    12772  10366  12104   -393   3994   -259  A    C  
ATOM   4681  O   LEU A 605     140.999  47.501   4.467  1.00 93.65      A    O  
ANISOU 4681  O   LEU A 605    13106  10471  12005   -417   3900   -179  A    O  
ATOM   4682  CB  LEU A 605     142.134  48.524   7.052  1.00 95.15      A    C  
ANISOU 4682  CB  LEU A 605    12736  10863  12554   -264   3756   -203  A    C  
ATOM   4683  CG  LEU A 605     143.030  48.562   8.276  1.00101.31      A    C  
ANISOU 4683  CG  LEU A 605    13220  11701  13571   -191   3724   -250  A    C  
ATOM   4684  CD1 LEU A 605     144.143  49.569   8.065  1.00100.53      A    C  
ANISOU 4684  CD1 LEU A 605    13076  11563  13558   -258   3883   -349  A    C  
ATOM   4685  CD2 LEU A 605     142.208  48.919   9.503  1.00107.16      A    C  
ANISOU 4685  CD2 LEU A 605    13850  12578  14286    -96   3475   -143  A    C  
ATOM   4686  N   THR A 606     142.503  45.917   5.086  1.00 97.33      A    N  
ANISOU 4686  N   THR A 606    13258  10903  12819   -372   4075   -319  A    N  
ATOM   4687  CA  THR A 606     141.724  44.764   4.637  1.00100.13      A    C  
ANISOU 4687  CA  THR A 606    13738  11222  13081   -361   4031   -270  A    C  
ATOM   4688  C   THR A 606     141.749  43.785   5.798  1.00 96.32      A    C  
ANISOU 4688  C   THR A 606    13019  10803  12773   -244   3898   -251  A    C  
ATOM   4689  O   THR A 606     142.628  43.851   6.665  1.00 92.37      A    O  
ANISOU 4689  O   THR A 606    12283  10331  12482   -191   3897   -313  A    O  
ATOM   4690  CB  THR A 606     142.285  44.122   3.335  1.00103.09      A    C  
ANISOU 4690  CB  THR A 606    14292  11451  13427   -473   4281   -373  A    C  
ATOM   4691  CG2 THR A 606     141.963  44.985   2.126  1.00102.57      A    C  
ANISOU 4691  CG2 THR A 606    14544  11303  13122   -600   4364   -358  A    C  
ATOM   4692  OG1 THR A 606     143.711  43.970   3.420  1.00102.46      A    O  
ANISOU 4692  OG1 THR A 606    14034  11322  13572   -502   4489   -532  A    O  
ATOM   4693  N   GLY A 607     140.775  42.901   5.860  1.00 94.90      A    N  
ANISOU 4693  N   GLY A 607    12907  10643  12507   -206   3767   -165  A    N  
ATOM   4694  CA  GLY A 607     140.763  41.989   6.974  1.00102.43      A    C  
ANISOU 4694  CA  GLY A 607    13672  11643  13601   -108   3625   -139  A    C  
ATOM   4695  C   GLY A 607     139.449  41.284   7.152  1.00106.68      A    C  
ANISOU 4695  C   GLY A 607    14305  12230  13997    -82   3451    -21  A    C  
ATOM   4696  O   GLY A 607     138.434  41.670   6.566  1.00110.82      A    O  
ANISOU 4696  O   GLY A 607    15004  12777  14325   -123   3405     48  A    O  
ATOM   4697  N   PRO A 608     139.470  40.227   7.961  1.00104.10      A    N  
ANISOU 4697  N   PRO A 608    13864  11908  13778    -17   3346     -4  A    N  
ATOM   4698  CA  PRO A 608     138.260  39.572   8.380  1.00101.71      A    C  
ANISOU 4698  CA  PRO A 608    13622  11665  13358      1   3169    107  A    C  
ATOM   4699  C   PRO A 608     137.310  40.514   9.144  1.00 97.70      A    C  
ANISOU 4699  C   PRO A 608    13087  11299  12736      5   3006    199  A    C  
ATOM   4700  O   PRO A 608     137.639  41.674   9.411  1.00 92.73      A    O  
ANISOU 4700  O   PRO A 608    12384  10719  12128      9   3018    182  A    O  
ATOM   4701  CB  PRO A 608     138.762  38.443   9.303  1.00109.08      A    C  
ANISOU 4701  CB  PRO A 608    14418  12564  14461     68   3081     92  A    C  
ATOM   4702  CG  PRO A 608     140.237  38.638   9.484  1.00107.05      A    C  
ANISOU 4702  CG  PRO A 608    13993  12243  14435    105   3188    -34  A    C  
ATOM   4703  CD  PRO A 608     140.689  39.500   8.356  1.00106.69      A    C  
ANISOU 4703  CD  PRO A 608    14024  12160  14351     33   3404   -110  A    C  
ATOM   4704  N   ASN A 609     136.160  39.969   9.512  1.00 91.37      A    N  
ANISOU 4704  N   ASN A 609    12336  10558  11822      1   2862    285  A    N  
ATOM   4705  CA  ASN A 609     135.091  40.717  10.087  1.00 89.36      A    C  
ANISOU 4705  CA  ASN A 609    12071  10435  11448    -10   2727    353  A    C  
ATOM   4706  C   ASN A 609     135.214  40.975  11.584  1.00 92.66      A    C  
ANISOU 4706  C   ASN A 609    12321  10947  11939     23   2602    383  A    C  
ATOM   4707  O   ASN A 609     134.658  41.951  12.058  1.00109.15      A    O  
ANISOU 4707  O   ASN A 609    14367  13143  13959     14   2531    405  A    O  
ATOM   4708  CB  ASN A 609     133.800  39.962   9.863  1.00 97.61      A    C  
ANISOU 4708  CB  ASN A 609    13230  11505  12349    -45   2640    413  A    C  
ATOM   4709  CG  ASN A 609     132.706  40.824   9.301  1.00101.51      A    C  
ANISOU 4709  CG  ASN A 609    13814  12062  12690    -76   2598    427  A    C  
ATOM   4710  ND2 ASN A 609     131.507  40.715   9.892  1.00106.04      A    N  
ANISOU 4710  ND2 ASN A 609    14368  12744  13178    -98   2464    472  A    N  
ATOM   4711  OD1 ASN A 609     132.920  41.572   8.350  1.00 99.87      A    O  
ANISOU 4711  OD1 ASN A 609    13699  11801  12445    -87   2677    390  A    O  
ATOM   4712  N   MET A 610     135.870  40.127  12.367  1.00 90.37      A    N  
ANISOU 4712  N   MET A 610    11947  10612  11776     58   2554    380  A    N  
ATOM   4713  CA  MET A 610     136.085  40.497  13.787  1.00 91.08      A    C  
ANISOU 4713  CA  MET A 610    11904  10771  11929     85   2426    405  A    C  
ATOM   4714  C   MET A 610     137.518  40.946  14.088  1.00 82.54      A    C  
ANISOU 4714  C   MET A 610    10679   9633  11047    143   2476    329  A    C  
ATOM   4715  O   MET A 610     137.857  41.160  15.264  1.00 75.15      A    O  
ANISOU 4715  O   MET A 610     9636   8729  10186    173   2360    343  A    O  
ATOM   4716  CB  MET A 610     135.679  39.363  14.741  1.00103.59      A    C  
ANISOU 4716  CB  MET A 610    13507  12352  13499     76   2276    467  A    C  
ATOM   4717  CG  MET A 610     134.217  38.967  14.664  1.00109.44      A    C  
ANISOU 4717  CG  MET A 610    14365  13168  14048      3   2217    536  A    C  
ATOM   4718  SD  MET A 610     133.215  40.257  15.379  1.00113.91      A    S  
ANISOU 4718  SD  MET A 610    14882  13914  14484    -47   2148    565  A    S  
ATOM   4719  CE  MET A 610     133.449  39.989  17.149  1.00114.31      A    C  
ANISOU 4719  CE  MET A 610    14870  13993  14569    -60   1990    610  A    C  
ATOM   4720  N   GLY A 611     138.337  41.065  13.033  1.00 79.18      A    N  
ANISOU 4720  N   GLY A 611    10260   9121  10704    148   2650    243  A    N  
ATOM   4721  CA  GLY A 611     139.657  41.714  13.105  1.00 77.90      A    C  
ANISOU 4721  CA  GLY A 611     9958   8912  10724    183   2739    147  A    C  
ATOM   4722  C   GLY A 611     139.390  43.187  13.345  1.00 80.90      A    C  
ANISOU 4722  C   GLY A 611    10312   9398  11025    164   2725    172  A    C  
ATOM   4723  O   GLY A 611     138.459  43.778  12.761  1.00 79.51      A    O  
ANISOU 4723  O   GLY A 611    10254   9282  10673    118   2740    215  A    O  
ATOM   4724  N   GLY A 612     140.149  43.797  14.241  1.00 80.13      A    N  
ANISOU 4724  N   GLY A 612    10062   9324  11060    205   2674    144  A    N  
ATOM   4725  CA  GLY A 612     139.749  45.125  14.763  1.00 78.14      A    C  
ANISOU 4725  CA  GLY A 612     9778   9186  10724    195   2614    184  A    C  
ATOM   4726  C   GLY A 612     139.984  46.327  13.846  1.00 75.20      A    C  
ANISOU 4726  C   GLY A 612     9446   8816  10309    159   2756    138  A    C  
ATOM   4727  O   GLY A 612     140.730  47.248  14.198  1.00 72.67      A    O  
ANISOU 4727  O   GLY A 612     9021   8508  10082    173   2778     95  A    O  
ATOM   4728  N   LYS A 613     139.333  46.344  12.689  1.00 72.86      A    N  
ANISOU 4728  N   LYS A 613     9317   8498   9867    108   2839    147  A    N  
ATOM   4729  CA  LYS A 613     139.540  47.435  11.723  1.00 75.32      A    C  
ANISOU 4729  CA  LYS A 613     9719   8782  10115     61   2962    105  A    C  
ATOM   4730  C   LYS A 613     138.855  48.706  12.196  1.00 76.23      A    C  
ANISOU 4730  C   LYS A 613     9824   9009  10130     68   2850    149  A    C  
ATOM   4731  O   LYS A 613     139.501  49.743  12.345  1.00 76.73      A    O  
ANISOU 4731  O   LYS A 613     9825   9079  10246     68   2887    112  A    O  
ATOM   4732  CB  LYS A 613     138.987  47.083  10.336  1.00 77.11      A    C  
ANISOU 4732  CB  LYS A 613    10164   8934  10197      3   3054    106  A    C  
ATOM   4733  CG  LYS A 613     139.691  45.935   9.644  1.00 76.19      A    C  
ANISOU 4733  CG  LYS A 613    10085   8696  10166    -19   3201     44  A    C  
ATOM   4734  CD  LYS A 613     139.200  45.752   8.229  1.00 76.44      A    C  
ANISOU 4734  CD  LYS A 613    10361   8645  10037    -91   3299     42  A    C  
ATOM   4735  CE  LYS A 613     137.704  45.444   8.143  1.00 78.95      A    C  
ANISOU 4735  CE  LYS A 613    10796   9020  10182    -83   3144    136  A    C  
ATOM   4736  NZ  LYS A 613     137.248  44.217   8.858  1.00 79.16      A    N1+
ANISOU 4736  NZ  LYS A 613    10747   9083  10245    -40   3039    184  A    N1+
ATOM   4737  N   SER A 614     137.542  48.615  12.429  1.00 75.17      A    N  
ANISOU 4737  N   SER A 614     9744   8961   9856     71   2717    218  A    N  
ATOM   4738  CA  SER A 614     136.766  49.738  12.902  1.00 74.77      A    C  
ANISOU 4738  CA  SER A 614     9671   9020   9716     81   2603    242  A    C  
ATOM   4739  C   SER A 614     137.359  50.308  14.170  1.00 72.07      A    C  
ANISOU 4739  C   SER A 614     9152   8748   9483    118   2543    240  A    C  
ATOM   4740  O   SER A 614     137.640  51.512  14.247  1.00 78.90      A    O  
ANISOU 4740  O   SER A 614     9986   9639  10353    125   2545    215  A    O  
ATOM   4741  CB  SER A 614     135.315  49.344  13.141  1.00 78.19      A    C  
ANISOU 4741  CB  SER A 614    10144   9541  10022     76   2476    291  A    C  
ATOM   4742  OG  SER A 614     134.557  49.623  11.980  1.00 88.26      A    O  
ANISOU 4742  OG  SER A 614    11583  10780  11170     52   2483    281  A    O  
ATOM   4743  N   THR A 615     137.525  49.462  15.173  1.00 65.92      A    N  
ANISOU 4743  N   THR A 615     8274   7990   8781    139   2473    267  A    N  
ATOM   4744  CA  THR A 615     138.046  49.924  16.437  1.00 64.01      A    C  
ANISOU 4744  CA  THR A 615     7886   7801   8631    171   2390    270  A    C  
ATOM   4745  C   THR A 615     139.371  50.664  16.218  1.00 63.93      A    C  
ANISOU 4745  C   THR A 615     7799   7725   8763    189   2490    202  A    C  
ATOM   4746  O   THR A 615     139.641  51.691  16.823  1.00 61.34      A    O  
ANISOU 4746  O   THR A 615     7392   7451   8464    205   2448    194  A    O  
ATOM   4747  CB  THR A 615     138.196  48.757  17.432  1.00 63.93      A    C  
ANISOU 4747  CB  THR A 615     7820   7777   8690    187   2294    304  A    C  
ATOM   4748  CG2 THR A 615     139.025  49.162  18.624  1.00 66.44      A    C  
ANISOU 4748  CG2 THR A 615     8002   8104   9134    225   2210    295  A    C  
ATOM   4749  OG1 THR A 615     136.908  48.386  17.939  1.00 67.22      A    O  
ANISOU 4749  OG1 THR A 615     8294   8286   8958    150   2189    367  A    O  
ATOM   4750  N   TYR A 616     140.201  50.146  15.337  1.00 66.00      A    N  
ANISOU 4750  N   TYR A 616     8087   7871   9117    179   2633    144  A    N  
ATOM   4751  CA  TYR A 616     141.517  50.712  15.197  1.00 70.39      A    C  
ANISOU 4751  CA  TYR A 616     8552   8364   9830    181   2743     60  A    C  
ATOM   4752  C   TYR A 616     141.407  52.064  14.542  1.00 71.87      A    C  
ANISOU 4752  C   TYR A 616     8820   8568   9919    141   2809     46  A    C  
ATOM   4753  O   TYR A 616     142.099  53.006  14.959  1.00 75.20      A    O  
ANISOU 4753  O   TYR A 616     9145   9004  10421    148   2815     10  A    O  
ATOM   4754  CB  TYR A 616     142.459  49.782  14.395  1.00 74.03      A    C  
ANISOU 4754  CB  TYR A 616     9010   8692  10423    166   2904    -25  A    C  
ATOM   4755  CG  TYR A 616     143.735  50.487  13.898  1.00 71.77      A    C  
ANISOU 4755  CG  TYR A 616     8661   8336  10273    131   3077   -138  A    C  
ATOM   4756  CD1 TYR A 616     144.861  50.540  14.692  1.00 72.43      A    C  
ANISOU 4756  CD1 TYR A 616     8539   8395  10583    176   3061   -213  A    C  
ATOM   4757  CD2 TYR A 616     143.781  51.112  12.667  1.00 68.02      A    C  
ANISOU 4757  CD2 TYR A 616     8338   7811   9693     47   3243   -174  A    C  
ATOM   4758  CE1 TYR A 616     146.003  51.189  14.285  1.00 72.33      A    C  
ANISOU 4758  CE1 TYR A 616     8452   8325  10702    136   3223   -328  A    C  
ATOM   4759  CE2 TYR A 616     144.916  51.745  12.252  1.00 70.65      A    C  
ANISOU 4759  CE2 TYR A 616     8624   8082  10137     -7   3410   -281  A    C  
ATOM   4760  CZ  TYR A 616     146.034  51.792  13.070  1.00 71.81      A    C  
ANISOU 4760  CZ  TYR A 616     8541   8219  10523     37   3408   -363  A    C  
ATOM   4761  OH  TYR A 616     147.197  52.449  12.672  1.00 71.05      A    O  
ANISOU 4761  OH  TYR A 616     8380   8063  10553    -27   3587   -487  A    O  
ATOM   4762  N   MET A 617     140.547  52.152  13.524  1.00 72.31      A    N  
ANISOU 4762  N   MET A 617     9059   8611   9802     98   2842     70  A    N  
ATOM   4763  CA  MET A 617     140.298  53.423  12.840  1.00 74.55      A    C  
ANISOU 4763  CA  MET A 617     9463   8893   9969     61   2868     61  A    C  
ATOM   4764  C   MET A 617     139.748  54.457  13.841  1.00 76.77      A    C  
ANISOU 4764  C   MET A 617     9657   9299  10213    105   2709     98  A    C  
ATOM   4765  O   MET A 617     140.327  55.534  14.018  1.00 79.09      A    O  
ANISOU 4765  O   MET A 617     9906   9597  10546    102   2725     67  A    O  
ATOM   4766  CB  MET A 617     139.313  53.244  11.704  1.00 74.11      A    C  
ANISOU 4766  CB  MET A 617     9626   8797   9733     23   2873     86  A    C  
ATOM   4767  CG  MET A 617     139.952  52.861  10.393  1.00 77.25      A    C  
ANISOU 4767  CG  MET A 617    10181   9051  10119    -53   3064     33  A    C  
ATOM   4768  SD  MET A 617     138.778  52.843   9.012  1.00 79.00      A    S  
ANISOU 4768  SD  MET A 617    10702   9204  10107   -102   3038     65  A    S  
ATOM   4769  CE  MET A 617     137.684  51.514   9.537  1.00 80.21      A    C  
ANISOU 4769  CE  MET A 617    10798   9436  10242    -46   2909    129  A    C  
ATOM   4770  N   ARG A 618     138.659  54.126  14.531  1.00 71.85      A    N  
ANISOU 4770  N   ARG A 618     9004   8776   9516    137   2565    153  A    N  
ATOM   4771  CA  ARG A 618     138.090  55.054  15.475  1.00 69.63      A    C  
ANISOU 4771  CA  ARG A 618     8642   8617   9197    168   2430    171  A    C  
ATOM   4772  C   ARG A 618     139.114  55.438  16.526  1.00 68.39      A    C  
ANISOU 4772  C   ARG A 618     8322   8479   9184    195   2416    157  A    C  
ATOM   4773  O   ARG A 618     139.061  56.534  17.053  1.00 70.99      A    O  
ANISOU 4773  O   ARG A 618     8599   8873   9501    211   2353    151  A    O  
ATOM   4774  CB  ARG A 618     136.870  54.448  16.151  1.00 74.60      A    C  
ANISOU 4774  CB  ARG A 618     9251   9350   9743    175   2306    216  A    C  
ATOM   4775  CG  ARG A 618     135.721  54.084  15.224  1.00 77.43      A    C  
ANISOU 4775  CG  ARG A 618     9750   9701   9968    154   2291    223  A    C  
ATOM   4776  CD  ARG A 618     134.757  53.146  15.945  1.00 80.93      A    C  
ANISOU 4776  CD  ARG A 618    10155  10230  10363    143   2206    259  A    C  
ATOM   4777  NE  ARG A 618     133.590  52.866  15.130  1.00 84.12      A    N  
ANISOU 4777  NE  ARG A 618    10672  10637  10650    124   2176    253  A    N  
ATOM   4778  CZ  ARG A 618     132.613  53.736  14.935  1.00 90.22      A    C  
ANISOU 4778  CZ  ARG A 618    11464  11474  11342    134   2093    216  A    C  
ATOM   4779  NH1 ARG A 618     132.655  54.939  15.509  1.00 90.92      A    N1+
ANISOU 4779  NH1 ARG A 618    11469  11631  11445    161   2040    184  A    N1+
ATOM   4780  NH2 ARG A 618     131.589  53.398  14.164  1.00 96.86      A    N  
ANISOU 4780  NH2 ARG A 618    12403  12302  12097    123   2052    200  A    N  
ATOM   4781  N   GLN A 619     140.023  54.528  16.853  1.00 69.92      A    N  
ANISOU 4781  N   GLN A 619     8432   8611   9521    205   2461    146  A    N  
ATOM   4782  CA  GLN A 619     141.097  54.787  17.852  1.00 71.38      A    C  
ANISOU 4782  CA  GLN A 619     8454   8793   9872    239   2429    120  A    C  
ATOM   4783  C   GLN A 619     142.003  55.927  17.419  1.00 65.51      A    C  
ANISOU 4783  C   GLN A 619     7687   8007   9195    224   2527     58  A    C  
ATOM   4784  O   GLN A 619     142.381  56.777  18.216  1.00 62.88      A    O  
ANISOU 4784  O   GLN A 619     7255   7718   8916    247   2463     51  A    O  
ATOM   4785  CB  GLN A 619     141.932  53.511  18.111  1.00 73.18      A    C  
ANISOU 4785  CB  GLN A 619     8604   8936  10265    261   2448     96  A    C  
ATOM   4786  CG  GLN A 619     143.339  53.749  18.616  1.00 74.40      A    C  
ANISOU 4786  CG  GLN A 619     8600   9031  10638    292   2467     26  A    C  
ATOM   4787  CD  GLN A 619     144.184  52.472  18.660  1.00 78.79      A    C  
ANISOU 4787  CD  GLN A 619     9078   9479  11379    323   2490    -29  A    C  
ATOM   4788  NE2 GLN A 619     145.436  52.579  18.204  1.00 82.54      A    N  
ANISOU 4788  NE2 GLN A 619     9456   9863  12043    319   2625   -142  A    N  
ATOM   4789  OE1 GLN A 619     143.735  51.415  19.113  1.00 77.01      A    O  
ANISOU 4789  OE1 GLN A 619     8876   9248  11135    345   2386     19  A    O  
ATOM   4790  N   VAL A 620     142.331  55.943  16.144  1.00 63.14      A    N  
ANISOU 4790  N   VAL A 620     7496   7617   8877    173   2685     13  A    N  
ATOM   4791  CA  VAL A 620     143.203  56.986  15.609  1.00 65.23      A    C  
ANISOU 4791  CA  VAL A 620     7772   7827   9185    130   2802    -52  A    C  
ATOM   4792  C   VAL A 620     142.474  58.348  15.692  1.00 64.42      A    C  
ANISOU 4792  C   VAL A 620     7739   7796   8939    133   2707    -18  A    C  
ATOM   4793  O   VAL A 620     142.995  59.325  16.252  1.00 64.41      A    O  
ANISOU 4793  O   VAL A 620     7652   7822   8998    145   2678    -38  A    O  
ATOM   4794  CB  VAL A 620     143.705  56.645  14.155  1.00 63.20      A    C  
ANISOU 4794  CB  VAL A 620     7656   7441   8916     47   3012   -115  A    C  
ATOM   4795  CG1 VAL A 620     144.493  57.782  13.547  1.00 60.82      A    C  
ANISOU 4795  CG1 VAL A 620     7408   7079   8621    -26   3140   -180  A    C  
ATOM   4796  CG2 VAL A 620     144.546  55.372  14.161  1.00 63.29      A    C  
ANISOU 4796  CG2 VAL A 620     7560   7381   9105     52   3109   -176  A    C  
ATOM   4797  N   ALA A 621     141.262  58.404  15.153  1.00 62.06      A    N  
ANISOU 4797  N   ALA A 621     7590   7524   8463    129   2647     25  A    N  
ATOM   4798  CA  ALA A 621     140.495  59.634  15.131  1.00 59.77      A    C  
ANISOU 4798  CA  ALA A 621     7371   7290   8048    142   2543     37  A    C  
ATOM   4799  C   ALA A 621     140.314  60.153  16.527  1.00 59.01      A    C  
ANISOU 4799  C   ALA A 621     7109   7315   7994    199   2406     56  A    C  
ATOM   4800  O   ALA A 621     140.292  61.353  16.701  1.00 61.31      A    O  
ANISOU 4800  O   ALA A 621     7400   7636   8257    210   2354     41  A    O  
ATOM   4801  CB  ALA A 621     139.126  59.405  14.489  1.00 60.07      A    C  
ANISOU 4801  CB  ALA A 621     7558   7344   7921    145   2466     66  A    C  
ATOM   4802  N   LEU A 622     140.133  59.255  17.506  1.00 58.69      A    N  
ANISOU 4802  N   LEU A 622     6952   7341   8007    230   2339     89  A    N  
ATOM   4803  CA  LEU A 622     139.877  59.631  18.912  1.00 56.85      A    C  
ANISOU 4803  CA  LEU A 622     6588   7221   7791    267   2205    111  A    C  
ATOM   4804  C   LEU A 622     141.127  60.164  19.574  1.00 56.19      A    C  
ANISOU 4804  C   LEU A 622     6381   7112   7856    282   2217     85  A    C  
ATOM   4805  O   LEU A 622     141.059  61.073  20.421  1.00 55.95      A    O  
ANISOU 4805  O   LEU A 622     6282   7156   7821    305   2127     87  A    O  
ATOM   4806  CB  LEU A 622     139.348  58.448  19.735  1.00 56.43      A    C  
ANISOU 4806  CB  LEU A 622     6487   7221   7730    273   2130    157  A    C  
ATOM   4807  CG  LEU A 622     137.865  58.142  19.550  1.00 56.20      A    C  
ANISOU 4807  CG  LEU A 622     6539   7269   7546    258   2073    177  A    C  
ATOM   4808  CD1 LEU A 622     137.412  56.978  20.438  1.00 55.79      A    C  
ANISOU 4808  CD1 LEU A 622     6452   7263   7480    242   2008    222  A    C  
ATOM   4809  CD2 LEU A 622     137.022  59.395  19.804  1.00 55.78      A    C  
ANISOU 4809  CD2 LEU A 622     6477   7316   7399    270   1990    151  A    C  
ATOM   4810  N   ILE A 623     142.268  59.613  19.183  1.00 55.06      A    N  
ANISOU 4810  N   ILE A 623     6199   6863   7854    268   2332     48  A    N  
ATOM   4811  CA  ILE A 623     143.535  60.108  19.705  1.00 55.71      A    C  
ANISOU 4811  CA  ILE A 623     6151   6908   8105    280   2353      2  A    C  
ATOM   4812  C   ILE A 623     143.851  61.507  19.158  1.00 56.50      A    C  
ANISOU 4812  C   ILE A 623     6301   6993   8173    249   2413    -35  A    C  
ATOM   4813  O   ILE A 623     144.333  62.387  19.869  1.00 55.96      A    O  
ANISOU 4813  O   ILE A 623     6141   6953   8167    267   2358    -50  A    O  
ATOM   4814  CB  ILE A 623     144.676  59.128  19.410  1.00 55.63      A    C  
ANISOU 4814  CB  ILE A 623     6066   6787   8282    272   2464    -58  A    C  
ATOM   4815  CG1 ILE A 623     144.514  57.886  20.281  1.00 55.71      A    C  
ANISOU 4815  CG1 ILE A 623     6009   6807   8352    318   2350    -21  A    C  
ATOM   4816  CG2 ILE A 623     146.012  59.791  19.666  1.00 55.88      A    C  
ANISOU 4816  CG2 ILE A 623     5965   6768   8498    270   2516   -136  A    C  
ATOM   4817  CD1 ILE A 623     145.285  56.675  19.812  1.00 56.87      A    C  
ANISOU 4817  CD1 ILE A 623     6113   6843   8651    319   2445    -78  A    C  
ATOM   4818  N   VAL A 624     143.556  61.713  17.890  1.00 57.81      A    N  
ANISOU 4818  N   VAL A 624     6631   7103   8229    197   2514    -49  A    N  
ATOM   4819  CA  VAL A 624     143.738  63.013  17.303  1.00 59.27      A    C  
ANISOU 4819  CA  VAL A 624     6911   7256   8352    159   2553    -77  A    C  
ATOM   4820  C   VAL A 624     142.826  64.024  17.938  1.00 60.78      A    C  
ANISOU 4820  C   VAL A 624     7106   7551   8436    208   2387    -43  A    C  
ATOM   4821  O   VAL A 624     143.226  65.144  18.180  1.00 65.33      A    O  
ANISOU 4821  O   VAL A 624     7660   8132   9028    207   2364    -64  A    O  
ATOM   4822  CB  VAL A 624     143.459  62.979  15.810  1.00 59.65      A    C  
ANISOU 4822  CB  VAL A 624     7183   7207   8272     88   2664    -90  A    C  
ATOM   4823  CG1 VAL A 624     143.380  64.393  15.256  1.00 59.45      A    C  
ANISOU 4823  CG1 VAL A 624     7303   7146   8140     52   2650   -105  A    C  
ATOM   4824  CG2 VAL A 624     144.550  62.168  15.138  1.00 62.13      A    C  
ANISOU 4824  CG2 VAL A 624     7491   7410   8703     19   2866   -151  A    C  
ATOM   4825  N   LEU A 625     141.593  63.626  18.202  1.00 64.18      A    N  
ANISOU 4825  N   LEU A 625     7561   8064   8760    246   2277     -0  A    N  
ATOM   4826  CA  LEU A 625     140.605  64.512  18.796  1.00 66.57      A    C  
ANISOU 4826  CA  LEU A 625     7852   8473   8965    289   2126      9  A    C  
ATOM   4827  C   LEU A 625     141.047  64.858  20.199  1.00 65.99      A    C  
ANISOU 4827  C   LEU A 625     7610   8478   8983    323   2051     14  A    C  
ATOM   4828  O   LEU A 625     141.172  66.041  20.545  1.00 69.91      A    O  
ANISOU 4828  O   LEU A 625     8083   9004   9476    339   1996     -6  A    O  
ATOM   4829  CB  LEU A 625     139.233  63.840  18.825  1.00 68.30      A    C  
ANISOU 4829  CB  LEU A 625     8105   8767   9076    308   2047     32  A    C  
ATOM   4830  CG  LEU A 625     138.012  64.697  19.160  1.00 70.17      A    C  
ANISOU 4830  CG  LEU A 625     8345   9107   9208    345   1909      9  A    C  
ATOM   4831  CD1 LEU A 625     136.775  63.961  18.696  1.00 73.38      A    C  
ANISOU 4831  CD1 LEU A 625     8818   9544   9518    344   1872      9  A    C  
ATOM   4832  CD2 LEU A 625     137.876  64.993  20.648  1.00 68.94      A    C  
ANISOU 4832  CD2 LEU A 625     8033   9076   9082    369   1821     11  A    C  
ATOM   4833  N   LEU A 626     141.303  63.842  21.006  1.00 63.57      A    N  
ANISOU 4833  N   LEU A 626     7199   8193   8759    332   2036     42  A    N  
ATOM   4834  CA  LEU A 626     141.740  64.100  22.348  1.00 66.54      A    C  
ANISOU 4834  CA  LEU A 626     7442   8623   9214    358   1946     50  A    C  
ATOM   4835  C   LEU A 626     142.975  64.994  22.333  1.00 72.02      A    C  
ANISOU 4835  C   LEU A 626     8079   9256  10030    356   1992     10  A    C  
ATOM   4836  O   LEU A 626     143.108  65.874  23.188  1.00 80.52      A    O  
ANISOU 4836  O   LEU A 626     9088  10385  11120    379   1906      6  A    O  
ATOM   4837  CB  LEU A 626     142.055  62.793  23.058  1.00 66.80      A    C  
ANISOU 4837  CB  LEU A 626     7404   8641   9333    363   1919     81  A    C  
ATOM   4838  CG  LEU A 626     141.009  62.316  24.045  1.00 68.71      A    C  
ANISOU 4838  CG  LEU A 626     7647   8987   9472    361   1801    125  A    C  
ATOM   4839  CD1 LEU A 626     139.606  62.657  23.592  1.00 69.00      A    C  
ANISOU 4839  CD1 LEU A 626     7768   9111   9338    347   1789    120  A    C  
ATOM   4840  CD2 LEU A 626     141.135  60.812  24.264  1.00 69.13      A    C  
ANISOU 4840  CD2 LEU A 626     7701   8991   9572    352   1793    160  A    C  
ATOM   4841  N   ALA A 627     143.880  64.776  21.378  1.00 69.99      A    N  
ANISOU 4841  N   ALA A 627     7846   8885   9859    320   2135    -29  A    N  
ATOM   4842  CA  ALA A 627     145.166  65.450  21.397  1.00 69.37      A    C  
ANISOU 4842  CA  ALA A 627     7693   8742   9923    303   2201    -83  A    C  
ATOM   4843  C   ALA A 627     144.998  66.947  21.458  1.00 68.31      A    C  
ANISOU 4843  C   ALA A 627     7600   8643   9712    303   2150    -91  A    C  
ATOM   4844  O   ALA A 627     145.759  67.622  22.165  1.00 73.70      A    O  
ANISOU 4844  O   ALA A 627     8177   9329  10496    314   2113   -112  A    O  
ATOM   4845  CB  ALA A 627     146.004  65.049  20.190  1.00 71.70      A    C  
ANISOU 4845  CB  ALA A 627     8036   8915  10293    236   2395   -141  A    C  
ATOM   4846  N   HIS A 628     143.981  67.444  20.753  1.00 65.42      A    N  
ANISOU 4846  N   HIS A 628     7385   8297   9173    296   2130    -76  A    N  
ATOM   4847  CA  HIS A 628     143.755  68.876  20.593  1.00 64.31      A    C  
ANISOU 4847  CA  HIS A 628     7319   8167   8949    298   2075    -93  A    C  
ATOM   4848  C   HIS A 628     142.778  69.445  21.623  1.00 62.48      A    C  
ANISOU 4848  C   HIS A 628     7031   8066   8641    362   1905    -75  A    C  
ATOM   4849  O   HIS A 628     142.256  70.554  21.480  1.00 59.87      A    O  
ANISOU 4849  O   HIS A 628     6767   7756   8221    382   1831    -95  A    O  
ATOM   4850  CB  HIS A 628     143.212  69.147  19.209  1.00 64.87      A    C  
ANISOU 4850  CB  HIS A 628     7601   8163   8881    258   2122   -103  A    C  
ATOM   4851  CG  HIS A 628     144.166  68.847  18.090  1.00 65.19      A    C  
ANISOU 4851  CG  HIS A 628     7741   8066   8962    167   2309   -134  A    C  
ATOM   4852  CD2 HIS A 628     144.805  69.669  17.222  1.00 65.62      A    C  
ANISOU 4852  CD2 HIS A 628     7932   8012   8986     88   2403   -171  A    C  
ATOM   4853  ND1 HIS A 628     144.481  67.561  17.701  1.00 64.39      A    N  
ANISOU 4853  ND1 HIS A 628     7623   7919   8922    137   2428   -136  A    N  
ATOM   4854  CE1 HIS A 628     145.298  67.606  16.665  1.00 64.77      A    C  
ANISOU 4854  CE1 HIS A 628     7778   7843   8985     40   2600   -182  A    C  
ATOM   4855  NE2 HIS A 628     145.499  68.873  16.343  1.00 65.74      A    N  
ANISOU 4855  NE2 HIS A 628     8008   7925   9045      1   2592   -202  A    N  
ATOM   4856  N   THR A 629     142.544  68.685  22.675  1.00 63.20      A    N  
ANISOU 4856  N   THR A 629     7007   8236   8768    390   1842    -46  A    N  
ATOM   4857  CA  THR A 629     141.807  69.204  23.797  1.00 68.48      A    C  
ANISOU 4857  CA  THR A 629     7613   9027   9379    430   1707    -42  A    C  
ATOM   4858  C   THR A 629     142.686  69.538  24.997  1.00 71.71      A    C  
ANISOU 4858  C   THR A 629     7896   9451   9897    442   1651    -37  A    C  
ATOM   4859  O   THR A 629     142.221  70.139  25.954  1.00 75.28      A    O  
ANISOU 4859  O   THR A 629     8307   9994  10300    463   1546    -39  A    O  
ATOM   4860  CB  THR A 629     140.754  68.199  24.254  1.00 69.84      A    C  
ANISOU 4860  CB  THR A 629     7777   9283   9476    430   1660    -15  A    C  
ATOM   4861  CG2 THR A 629     139.847  67.860  23.104  1.00 71.00      A    C  
ANISOU 4861  CG2 THR A 629     8040   9412   9522    422   1699    -24  A    C  
ATOM   4862  OG1 THR A 629     141.399  67.016  24.720  1.00 69.79      A    O  
ANISOU 4862  OG1 THR A 629     7710   9240   9566    417   1685     23  A    O  
ATOM   4863  N   GLY A 630     143.953  69.158  24.956  1.00 77.55      A    N  
ANISOU 4863  N   GLY A 630     8572  10099  10792    428   1718    -42  A    N  
ATOM   4864  CA  GLY A 630     144.839  69.344  26.100  1.00 79.87      A    C  
ANISOU 4864  CA  GLY A 630     8742  10391  11213    447   1645    -43  A    C  
ATOM   4865  C   GLY A 630     144.908  68.098  26.966  1.00 82.40      A    C  
ANISOU 4865  C   GLY A 630     9002  10714  11591    458   1580     -7  A    C  
ATOM   4866  O   GLY A 630     145.871  67.908  27.700  1.00 92.88      A    O  
ANISOU 4866  O   GLY A 630    10231  11991  13067    474   1525    -15  A    O  
ATOM   4867  N   CYS A 631     143.906  67.234  26.887  1.00 75.91      A    N  
ANISOU 4867  N   CYS A 631     8245   9941  10658    447   1572     29  A    N  
ATOM   4868  CA  CYS A 631     144.024  65.928  27.497  1.00 79.12      A    C  
ANISOU 4868  CA  CYS A 631     8625  10321  11116    447   1522     63  A    C  
ATOM   4869  C   CYS A 631     145.175  65.119  26.888  1.00 78.14      A    C  
ANISOU 4869  C   CYS A 631     8444  10068  11177    454   1607     33  A    C  
ATOM   4870  O   CYS A 631     145.589  65.348  25.740  1.00 79.66      A    O  
ANISOU 4870  O   CYS A 631     8652  10203  11412    437   1748    -10  A    O  
ATOM   4871  CB  CYS A 631     142.717  65.153  27.346  1.00 83.01      A    C  
ANISOU 4871  CB  CYS A 631     9207  10882  11449    421   1522    100  A    C  
ATOM   4872  SG  CYS A 631     142.716  63.488  28.061  1.00 92.26      A    S  
ANISOU 4872  SG  CYS A 631    10391  12014  12649    407   1450    151  A    S  
ATOM   4873  N   PHE A 632     145.701  64.182  27.674  1.00 75.95      A    N  
ANISOU 4873  N   PHE A 632     8109   9736  11012    475   1518     46  A    N  
ATOM   4874  CA  PHE A 632     146.728  63.271  27.190  1.00 74.71      A    C  
ANISOU 4874  CA  PHE A 632     7878   9456  11050    491   1583     -2  A    C  
ATOM   4875  C   PHE A 632     146.092  62.076  26.516  1.00 72.57      A    C  
ANISOU 4875  C   PHE A 632     7689   9173  10712    474   1647     24  A    C  
ATOM   4876  O   PHE A 632     145.016  61.643  26.889  1.00 75.94      A    O  
ANISOU 4876  O   PHE A 632     8205   9670  10979    457   1579     88  A    O  
ATOM   4877  CB  PHE A 632     147.590  62.778  28.335  1.00 78.78      A    C  
ANISOU 4877  CB  PHE A 632     8297   9900  11736    536   1424    -12  A    C  
ATOM   4878  CG  PHE A 632     148.424  63.846  28.991  1.00 77.17      A    C  
ANISOU 4878  CG  PHE A 632     7996   9683  11642    558   1355    -50  A    C  
ATOM   4879  CD1 PHE A 632     148.427  65.133  28.528  1.00 74.13      A    C  
ANISOU 4879  CD1 PHE A 632     7610   9349  11207    535   1445    -73  A    C  
ATOM   4880  CD2 PHE A 632     149.229  63.524  30.071  1.00 79.37      A    C  
ANISOU 4880  CD2 PHE A 632     8191   9885  12080    604   1182    -65  A    C  
ATOM   4881  CE1 PHE A 632     149.208  66.085  29.126  1.00 76.77      A    C  
ANISOU 4881  CE1 PHE A 632     7856   9668  11644    553   1381   -109  A    C  
ATOM   4882  CE2 PHE A 632     150.012  64.470  30.674  1.00 80.50      A    C  
ANISOU 4882  CE2 PHE A 632     8243  10010  12334    626   1108   -104  A    C  
ATOM   4883  CZ  PHE A 632     150.005  65.754  30.196  1.00 79.64      A    C  
ANISOU 4883  CZ  PHE A 632     8126   9962  12171    598   1217   -126  A    C  
ATOM   4884  N   VAL A 633     146.767  61.530  25.526  1.00 71.49      A    N  
ANISOU 4884  N   VAL A 633     7520   8945  10699    468   1785    -35  A    N  
ATOM   4885  CA  VAL A 633     146.185  60.485  24.705  1.00 69.53      A    C  
ANISOU 4885  CA  VAL A 633     7358   8678  10379    449   1869    -17  A    C  
ATOM   4886  C   VAL A 633     146.601  59.105  25.195  1.00 69.73      A    C  
ANISOU 4886  C   VAL A 633     7336   8623  10535    483   1786    -19  A    C  
ATOM   4887  O   VAL A 633     147.643  58.932  25.808  1.00 68.65      A    O  
ANISOU 4887  O   VAL A 633     7076   8408  10600    527   1710    -71  A    O  
ATOM   4888  CB  VAL A 633     146.584  60.666  23.238  1.00 69.64      A    C  
ANISOU 4888  CB  VAL A 633     7402   8634  10423    407   2081    -82  A    C  
ATOM   4889  CG1 VAL A 633     145.985  61.954  22.699  1.00 68.01      A    C  
ANISOU 4889  CG1 VAL A 633     7292   8493  10053    371   2131    -67  A    C  
ATOM   4890  CG2 VAL A 633     148.110  60.684  23.095  1.00 73.11      A    C  
ANISOU 4890  CG2 VAL A 633     7694   8967  11117    413   2163   -191  A    C  
ATOM   4891  N   PRO A 634     145.760  58.111  24.943  1.00 71.42      A    N  
ANISOU 4891  N   PRO A 634     7650   8849  10637    468   1785     32  A    N  
ATOM   4892  CA  PRO A 634     146.068  56.762  25.351  1.00 73.93      A    C  
ANISOU 4892  CA  PRO A 634     7948   9080  11059    501   1697     33  A    C  
ATOM   4893  C   PRO A 634     147.067  56.106  24.409  1.00 77.96      A    C  
ANISOU 4893  C   PRO A 634     8377   9471  11772    518   1836    -68  A    C  
ATOM   4894  O   PRO A 634     146.677  55.433  23.436  1.00 82.16      A    O  
ANISOU 4894  O   PRO A 634     8985   9986  12244    490   1958    -70  A    O  
ATOM   4895  CB  PRO A 634     144.706  56.060  25.268  1.00 73.54      A    C  
ANISOU 4895  CB  PRO A 634     8050   9098  10793    460   1675    120  A    C  
ATOM   4896  CG  PRO A 634     143.958  56.798  24.218  1.00 72.07      A    C  
ANISOU 4896  CG  PRO A 634     7937   8990  10456    417   1823    123  A    C  
ATOM   4897  CD  PRO A 634     144.404  58.223  24.373  1.00 72.09      A    C  
ANISOU 4897  CD  PRO A 634     7873   9028  10486    423   1837     91  A    C  
ATOM   4898  N   ALA A 635     148.345  56.305  24.691  1.00 79.42      A    N  
ANISOU 4898  N   ALA A 635     8403   9574  12198    559   1821   -164  A    N  
ATOM   4899  CA  ALA A 635     149.387  55.665  23.916  1.00 80.52      A    C  
ANISOU 4899  CA  ALA A 635     8432   9596  12562    573   1954   -291  A    C  
ATOM   4900  C   ALA A 635     150.665  55.684  24.708  1.00 82.26      A    C  
ANISOU 4900  C   ALA A 635     8461   9726  13069    640   1839   -393  A    C  
ATOM   4901  O   ALA A 635     150.696  56.140  25.853  1.00 81.79      A    O  
ANISOU 4901  O   ALA A 635     8379   9685  13009    676   1645   -346  A    O  
ATOM   4902  CB  ALA A 635     149.563  56.415  22.614  1.00 80.87      A    C  
ANISOU 4902  CB  ALA A 635     8499   9657  12571    499   2210   -351  A    C  
ATOM   4903  N   ASP A 636     151.736  55.203  24.104  1.00 86.98      A    N  
ANISOU 4903  N   ASP A 636     8915  10218  13915    654   1960   -544  A    N  
ATOM   4904  CA  ASP A 636     153.049  55.361  24.723  1.00 92.53      A    C  
ANISOU 4904  CA  ASP A 636     9401  10831  14926    716   1874   -676  A    C  
ATOM   4905  C   ASP A 636     153.714  56.638  24.261  1.00 86.27      A    C  
ANISOU 4905  C   ASP A 636     8516  10066  14193    657   2046   -759  A    C  
ATOM   4906  O   ASP A 636     154.483  57.242  25.012  1.00 84.99      A    O  
ANISOU 4906  O   ASP A 636     8215   9879  14197    695   1939   -816  A    O  
ATOM   4907  CB  ASP A 636     153.931  54.145  24.477  1.00100.32      A    C  
ANISOU 4907  CB  ASP A 636    10244  11677  16194    773   1883   -824  A    C  
ATOM   4908  CG  ASP A 636     153.430  52.912  25.232  1.00106.80      A    C  
ANISOU 4908  CG  ASP A 636    11148  12442  16989    849   1636   -744  A    C  
ATOM   4909  OD1 ASP A 636     152.208  52.844  25.515  1.00110.66      A    O  
ANISOU 4909  OD1 ASP A 636    11840  13015  17188    819   1558   -573  A    O  
ATOM   4910  OD2 ASP A 636     154.246  52.021  25.549  1.00111.19      A    O1-
ANISOU 4910  OD2 ASP A 636    11569  12863  17813    935   1517   -862  A    O1-
ATOM   4911  N   ALA A 637     153.394  57.061  23.047  1.00 81.47      A    N  
ANISOU 4911  N   ALA A 637     8008   9504  13440    559   2302   -762  A    N  
ATOM   4912  CA  ALA A 637     153.761  58.404  22.597  1.00 83.42      A    C  
ANISOU 4912  CA  ALA A 637     8242   9790  13661    481   2456   -802  A    C  
ATOM   4913  C   ALA A 637     152.964  58.741  21.350  1.00 81.05      A    C  
ANISOU 4913  C   ALA A 637     8149   9540  13102    376   2665   -745  A    C  
ATOM   4914  O   ALA A 637     152.467  57.835  20.681  1.00 81.49      A    O  
ANISOU 4914  O   ALA A 637     8304   9578  13078    361   2740   -725  A    O  
ATOM   4915  CB  ALA A 637     155.258  58.497  22.321  1.00 85.82      A    C  
ANISOU 4915  CB  ALA A 637     8320   9999  14286    463   2591  -1011  A    C  
ATOM   4916  N   ALA A 638     152.843  60.027  21.035  1.00 78.33      A    N  
ANISOU 4916  N   ALA A 638     7882   9248  12629    308   2745   -720  A    N  
ATOM   4917  CA  ALA A 638     152.111  60.429  19.851  1.00 79.91      A    C  
ANISOU 4917  CA  ALA A 638     8300   9475  12586    212   2913   -671  A    C  
ATOM   4918  C   ALA A 638     152.532  61.808  19.397  1.00 85.05      A    C  
ANISOU 4918  C   ALA A 638     8989  10128  13196    123   3035   -712  A    C  
ATOM   4919  O   ALA A 638     152.912  62.661  20.209  1.00 85.18      A    O  
ANISOU 4919  O   ALA A 638     8906  10175  13282    153   2930   -714  A    O  
ATOM   4920  CB  ALA A 638     150.616  60.398  20.096  1.00 77.84      A    C  
ANISOU 4920  CB  ALA A 638     8213   9309  12054    247   2765   -504  A    C  
ATOM   4921  N   THR A 639     152.463  62.007  18.081  1.00 88.24      A    N  
ANISOU 4921  N   THR A 639     9558  10489  13477      6   3254   -743  A    N  
ATOM   4922  CA  THR A 639     152.908  63.238  17.437  1.00 85.00      A    C  
ANISOU 4922  CA  THR A 639     9232  10052  13009   -109   3401   -791  A    C  
ATOM   4923  C   THR A 639     151.986  63.524  16.277  1.00 84.24      A    C  
ANISOU 4923  C   THR A 639     9436   9944  12626   -194   3490   -718  A    C  
ATOM   4924  O   THR A 639     151.904  62.722  15.343  1.00 92.26      A    O  
ANISOU 4924  O   THR A 639    10554  10900  13600   -254   3638   -751  A    O  
ATOM   4925  CB  THR A 639     154.336  63.081  16.895  1.00 83.60      A    C  
ANISOU 4925  CB  THR A 639     8918   9775  13069   -208   3644   -984  A    C  
ATOM   4926  CG2 THR A 639     154.903  64.427  16.516  1.00 85.96      A    C  
ANISOU 4926  CG2 THR A 639     9273  10050  13333   -326   3766  -1037  A    C  
ATOM   4927  OG1 THR A 639     155.159  62.463  17.894  1.00 81.44      A    O  
ANISOU 4927  OG1 THR A 639     8352   9491  13098   -108   3545  -1072  A    O  
ATOM   4928  N   ILE A 640     151.286  64.652  16.321  1.00 80.41      A    N  
ANISOU 4928  N   ILE A 640     9097   9509  11945   -196   3388   -627  A    N  
ATOM   4929  CA  ILE A 640     150.293  64.938  15.294  1.00 79.84      A    C  
ANISOU 4929  CA  ILE A 640     9317   9416  11600   -254   3413   -554  A    C  
ATOM   4930  C   ILE A 640     150.610  66.237  14.616  1.00 72.48      A    C  
ANISOU 4930  C   ILE A 640     8552   8426  10563   -370   3505   -582  A    C  
ATOM   4931  O   ILE A 640     151.020  67.151  15.263  1.00 73.37      A    O  
ANISOU 4931  O   ILE A 640     8569   8569  10738   -354   3441   -594  A    O  
ATOM   4932  CB  ILE A 640     148.861  65.000  15.875  1.00 84.98      A    C  
ANISOU 4932  CB  ILE A 640    10030  10173  12084   -139   3169   -417  A    C  
ATOM   4933  CG1 ILE A 640     148.467  63.657  16.487  1.00 86.90      A    C  
ANISOU 4933  CG1 ILE A 640    10152  10466  12400    -45   3082   -381  A    C  
ATOM   4934  CG2 ILE A 640     147.841  65.349  14.794  1.00 86.53      A    C  
ANISOU 4934  CG2 ILE A 640    10519  10336  12021   -189   3169   -360  A    C  
ATOM   4935  CD1 ILE A 640     148.855  63.535  17.940  1.00 92.05      A    C  
ANISOU 4935  CD1 ILE A 640    10561  11185  13228     53   2932   -379  A    C  
ATOM   4936  N   GLY A 641     150.399  66.313  13.313  1.00 70.24      A    N  
ANISOU 4936  N   GLY A 641     8535   8047  10105   -491   3646   -591  A    N  
ATOM   4937  CA  GLY A 641     150.655  67.524  12.578  1.00 71.57      A    C  
ANISOU 4937  CA  GLY A 641     8916   8134  10140   -618   3726   -613  A    C  
ATOM   4938  C   GLY A 641     149.475  68.445  12.684  1.00 70.66      A    C  
ANISOU 4938  C   GLY A 641     8972   8061   9812   -548   3496   -497  A    C  
ATOM   4939  O   GLY A 641     148.553  68.182  13.410  1.00 68.31      A    O  
ANISOU 4939  O   GLY A 641     8591   7868   9495   -407   3297   -418  A    O  
ATOM   4940  N   PRO A 642     149.511  69.556  11.964  1.00 73.29      A    N  
ANISOU 4940  N   PRO A 642     9549   8307   9989   -652   3522   -501  A    N  
ATOM   4941  CA  PRO A 642     148.373  70.454  11.853  1.00 72.51      A    C  
ANISOU 4941  CA  PRO A 642     9650   8216   9682   -591   3301   -413  A    C  
ATOM   4942  C   PRO A 642     147.162  69.776  11.234  1.00 72.57      A    C  
ANISOU 4942  C   PRO A 642     9832   8210   9528   -545   3210   -349  A    C  
ATOM   4943  O   PRO A 642     147.239  69.287  10.118  1.00 76.68      A    O  
ANISOU 4943  O   PRO A 642    10566   8617   9952   -658   3353   -370  A    O  
ATOM   4944  CB  PRO A 642     148.884  71.557  10.917  1.00 74.57      A    C  
ANISOU 4944  CB  PRO A 642    10190   8334   9810   -756   3400   -450  A    C  
ATOM   4945  CG  PRO A 642     150.371  71.507  11.034  1.00 77.03      A    C  
ANISOU 4945  CG  PRO A 642    10340   8617  10311   -875   3644   -559  A    C  
ATOM   4946  CD  PRO A 642     150.678  70.048  11.216  1.00 77.37      A    C  
ANISOU 4946  CD  PRO A 642    10168   8702  10525   -843   3765   -602  A    C  
ATOM   4947  N   VAL A 643     146.053  69.750  11.961  1.00 74.86      A    N  
ANISOU 4947  N   VAL A 643    10034   8617   9791   -390   2978   -280  A    N  
ATOM   4948  CA  VAL A 643     144.810  69.143  11.466  1.00 75.84      A    C  
ANISOU 4948  CA  VAL A 643    10296   8742   9778   -335   2868   -228  A    C  
ATOM   4949  C   VAL A 643     143.649  70.125  11.518  1.00 73.32      A    C  
ANISOU 4949  C   VAL A 643    10097   8444   9316   -249   2616   -190  A    C  
ATOM   4950  O   VAL A 643     143.531  70.893  12.483  1.00 72.39      A    O  
ANISOU 4950  O   VAL A 643     9826   8424   9252   -164   2485   -186  A    O  
ATOM   4951  CB  VAL A 643     144.421  67.924  12.297  1.00 77.03      A    C  
ANISOU 4951  CB  VAL A 643    10202   9019  10044   -228   2830   -201  A    C  
ATOM   4952  CG1 VAL A 643     143.174  67.264  11.722  1.00 78.07      A    C  
ANISOU 4952  CG1 VAL A 643    10477   9146  10038   -188   2733   -156  A    C  
ATOM   4953  CG2 VAL A 643     145.578  66.937  12.345  1.00 79.25      A    C  
ANISOU 4953  CG2 VAL A 643    10334   9278  10498   -290   3048   -254  A    C  
ATOM   4954  N   ASP A 644     142.806  70.097  10.482  1.00 70.36      A    N  
ANISOU 4954  N   ASP A 644     9994   7972   8765   -267   2542   -172  A    N  
ATOM   4955  CA  ASP A 644     141.773  71.109  10.327  1.00 71.89      A    C  
ANISOU 4955  CA  ASP A 644    10338   8147   8829   -194   2297   -161  A    C  
ATOM   4956  C   ASP A 644     140.382  70.575  10.556  1.00 70.41      A    C  
ANISOU 4956  C   ASP A 644    10087   8050   8614    -66   2114   -142  A    C  
ATOM   4957  O   ASP A 644     139.531  71.276  11.089  1.00 70.60      A    O  
ANISOU 4957  O   ASP A 644    10048   8148   8626     43   1905   -153  A    O  
ATOM   4958  CB  ASP A 644     141.844  71.802   8.944  1.00 76.95      A    C  
ANISOU 4958  CB  ASP A 644    11383   8575   9280   -313   2296   -171  A    C  
ATOM   4959  CG  ASP A 644     141.511  70.865   7.759  1.00 77.33      A    C  
ANISOU 4959  CG  ASP A 644    11672   8501   9206   -387   2365   -158  A    C  
ATOM   4960  OD1 ASP A 644     141.813  69.637   7.858  1.00 73.12      A    O  
ANISOU 4960  OD1 ASP A 644    10998   8022   8762   -407   2531   -155  A    O  
ATOM   4961  OD2 ASP A 644     140.971  71.399   6.737  1.00 74.00      A    O1-
ANISOU 4961  OD2 ASP A 644    11594   7921   8602   -426   2241   -154  A    O1-
ATOM   4962  N   GLN A 645     140.139  69.343  10.119  1.00 70.83      A    N  
ANISOU 4962  N   GLN A 645    10162   8092   8655    -87   2196   -123  A    N  
ATOM   4963  CA  GLN A 645     138.833  68.713  10.285  1.00 67.04      A    C  
ANISOU 4963  CA  GLN A 645     9624   7695   8153     17   2043   -110  A    C  
ATOM   4964  C   GLN A 645     139.007  67.229  10.467  1.00 61.90      A    C  
ANISOU 4964  C   GLN A 645     8837   7101   7579      3   2188    -85  A    C  
ATOM   4965  O   GLN A 645     139.992  66.687  10.056  1.00 63.98      A    O  
ANISOU 4965  O   GLN A 645     9139   7291   7877    -95   2391    -87  A    O  
ATOM   4966  CB  GLN A 645     137.980  68.956   9.059  1.00 70.51      A    C  
ANISOU 4966  CB  GLN A 645    10378   7988   8424      6   1909   -118  A    C  
ATOM   4967  CG  GLN A 645     137.556  70.391   8.799  1.00 74.83      A    C  
ANISOU 4967  CG  GLN A 645    11089   8458   8883     43   1702   -149  A    C  
ATOM   4968  CD  GLN A 645     137.037  70.577   7.373  1.00 78.92      A    C  
ANISOU 4968  CD  GLN A 645    11994   8769   9220     -4   1594   -154  A    C  
ATOM   4969  NE2 GLN A 645     137.894  70.306   6.366  1.00 76.06      A    N  
ANISOU 4969  NE2 GLN A 645    11892   8243   8762   -162   1779   -133  A    N  
ATOM   4970  OE1 GLN A 645     135.861  70.913   7.181  1.00 82.84      A    O  
ANISOU 4970  OE1 GLN A 645    12553   9251   9670     97   1344   -187  A    O  
ATOM   4971  N   ILE A 646     138.040  66.581  11.080  1.00 58.83      A    N  
ANISOU 4971  N   ILE A 646     8292   6838   7221     93   2082    -73  A    N  
ATOM   4972  CA  ILE A 646     137.975  65.142  11.120  1.00 59.02      A    C  
ANISOU 4972  CA  ILE A 646     8238   6896   7288     82   2180    -46  A    C  
ATOM   4973  C   ILE A 646     136.670  64.660  10.497  1.00 62.79      A    C  
ANISOU 4973  C   ILE A 646     8837   7357   7660    118   2052    -43  A    C  
ATOM   4974  O   ILE A 646     135.553  65.082  10.893  1.00 62.02      A    O  
ANISOU 4974  O   ILE A 646     8678   7344   7541    204   1862    -68  A    O  
ATOM   4975  CB  ILE A 646     138.049  64.643  12.547  1.00 57.67      A    C  
ANISOU 4975  CB  ILE A 646     7763   6893   7253    143   2178    -31  A    C  
ATOM   4976  CG1 ILE A 646     139.370  65.103  13.168  1.00 58.78      A    C  
ANISOU 4976  CG1 ILE A 646     7777   7039   7515    114   2286    -41  A    C  
ATOM   4977  CG2 ILE A 646     137.890  63.127  12.602  1.00 55.44      A    C  
ANISOU 4977  CG2 ILE A 646     7418   6639   7008    136   2251     -2  A    C  
ATOM   4978  CD1 ILE A 646     139.541  64.594  14.586  1.00 59.30      A    C  
ANISOU 4978  CD1 ILE A 646     7571   7245   7713    169   2268    -24  A    C  
ATOM   4979  N   PHE A 647     136.820  63.805   9.479  1.00 67.76      A    N  
ANISOU 4979  N   PHE A 647     9646   7871   8229     47   2160    -27  A    N  
ATOM   4980  CA  PHE A 647     135.674  63.215   8.772  1.00 69.31      A    C  
ANISOU 4980  CA  PHE A 647     9976   8029   8327     70   2052    -23  A    C  
ATOM   4981  C   PHE A 647     135.612  61.724   9.083  1.00 70.41      A    C  
ANISOU 4981  C   PHE A 647     9983   8236   8529     68   2151      8  A    C  
ATOM   4982  O   PHE A 647     136.630  61.050   9.125  1.00 76.42      A    O  
ANISOU 4982  O   PHE A 647    10698   8974   9362      9   2340     23  A    O  
ATOM   4983  CB  PHE A 647     135.790  63.404   7.255  1.00 67.32      A    C  
ANISOU 4983  CB  PHE A 647    10086   7567   7926    -16   2074    -27  A    C  
ATOM   4984  CG  PHE A 647     135.884  64.833   6.815  1.00 68.75      A    C  
ANISOU 4984  CG  PHE A 647    10456   7643   8020    -30   1968    -53  A    C  
ATOM   4985  CD1 PHE A 647     136.795  65.675   7.298  1.00 69.78      A    C  
ANISOU 4985  CD1 PHE A 647    10515   7791   8207    -56   2038    -64  A    C  
ATOM   4986  CD2 PHE A 647     135.071  65.307   5.874  1.00 70.79      A    C  
ANISOU 4986  CD2 PHE A 647    10982   7770   8142    -18   1786    -71  A    C  
ATOM   4987  CE1 PHE A 647     136.878  66.979   6.861  1.00 71.05      A    C  
ANISOU 4987  CE1 PHE A 647    10873   7843   8279    -76   1934    -85  A    C  
ATOM   4988  CE2 PHE A 647     135.138  66.602   5.424  1.00 70.38      A    C  
ANISOU 4988  CE2 PHE A 647    11139   7600   8003    -32   1664    -94  A    C  
ATOM   4989  CZ  PHE A 647     136.048  67.440   5.915  1.00 70.80      A    C  
ANISOU 4989  CZ  PHE A 647    11125   7673   8103    -64   1744    -99  A    C  
ATOM   4990  N   THR A 648     134.416  61.201   9.290  1.00 73.01      A    N  
ANISOU 4990  N   THR A 648    10253   8646   8841    129   2020      8  A    N  
ATOM   4991  CA  THR A 648     134.247  59.769   9.419  1.00 76.09      A    C  
ANISOU 4991  CA  THR A 648    10570   9076   9263    117   2096     41  A    C  
ATOM   4992  C   THR A 648     133.147  59.245   8.492  1.00 81.52      A    C  
ANISOU 4992  C   THR A 648    11429   9698   9844    122   1997     35  A    C  
ATOM   4993  O   THR A 648     132.390  60.001   7.883  1.00 83.78      A    O  
ANISOU 4993  O   THR A 648    11861   9924  10046    151   1837     -1  A    O  
ATOM   4994  CB  THR A 648     133.918  59.420  10.861  1.00 74.99      A    C  
ANISOU 4994  CB  THR A 648    10146   9122   9223    171   2055     48  A    C  
ATOM   4995  CG2 THR A 648     135.065  59.819  11.772  1.00 75.38      A    C  
ANISOU 4995  CG2 THR A 648    10037   9219   9383    167   2144     56  A    C  
ATOM   4996  OG1 THR A 648     132.737  60.128  11.246  1.00 76.65      A    O  
ANISOU 4996  OG1 THR A 648    10294   9424   9403    237   1866      4  A    O  
ATOM   4997  N   ARG A 649     133.073  57.931   8.401  1.00 91.35      A    N  
ANISOU 4997  N   ARG A 649    12656  10949  11102     96   2080     67  A    N  
ATOM   4998  CA  ARG A 649     132.072  57.254   7.600  1.00 95.52      A    C  
ANISOU 4998  CA  ARG A 649    13326  11422  11542     98   1997     66  A    C  
ATOM   4999  C   ARG A 649     132.080  55.771   8.010  1.00 90.56      A    C  
ANISOU 4999  C   ARG A 649    12583  10856  10969     80   2094    106  A    C  
ATOM   5000  O   ARG A 649     132.790  54.981   7.418  1.00 85.57      A    O  
ANISOU 5000  O   ARG A 649    12054  10127  10330     23   2244    131  A    O  
ATOM   5001  CB  ARG A 649     132.413  57.460   6.115  1.00 98.86      A    C  
ANISOU 5001  CB  ARG A 649    14081  11637  11843     29   2037     65  A    C  
ATOM   5002  CG  ARG A 649     131.614  56.639   5.125  1.00102.69      A    C  
ANISOU 5002  CG  ARG A 649    14759  12026  12230     13   1980     72  A    C  
ATOM   5003  CD  ARG A 649     130.131  56.984   5.097  1.00104.47      A    C  
ANISOU 5003  CD  ARG A 649    14975  12292  12424     94   1724     27  A    C  
ATOM   5004  NE  ARG A 649     129.363  55.739   5.068  1.00106.11      A    N  
ANISOU 5004  NE  ARG A 649    15138  12543  12635     99   1708     41  A    N  
ATOM   5005  CZ  ARG A 649     128.552  55.330   6.040  1.00105.82      A    C  
ANISOU 5005  CZ  ARG A 649    14852  12677  12675    147   1641     22  A    C  
ATOM   5006  NH1 ARG A 649     128.360  56.072   7.121  1.00111.07      A    N1+
ANISOU 5006  NH1 ARG A 649    15292  13489  13420    198   1580    -15  A    N1+
ATOM   5007  NH2 ARG A 649     127.912  54.178   5.931  1.00106.44      A    N  
ANISOU 5007  NH2 ARG A 649    14918  12778  12746    135   1638     36  A    N  
ATOM   5008  N   ILE A 650     131.328  55.417   9.052  1.00 91.50      A    N  
ANISOU 5008  N   ILE A 650    12492  11132  11139    123   2013    104  A    N  
ATOM   5009  CA  ILE A 650     131.340  54.059   9.592  1.00 95.34      A    C  
ANISOU 5009  CA  ILE A 650    12871  11679  11674    104   2087    145  A    C  
ATOM   5010  C   ILE A 650     129.925  53.533   9.790  1.00 92.45      A    C  
ANISOU 5010  C   ILE A 650    12455  11398  11270    120   1959    129  A    C  
ATOM   5011  O   ILE A 650     129.202  54.015  10.662  1.00 87.96      A    O  
ANISOU 5011  O   ILE A 650    11730  10965  10723    149   1857     91  A    O  
ATOM   5012  CB  ILE A 650     132.081  53.983  10.953  1.00105.78      A    C  
ANISOU 5012  CB  ILE A 650    13971  13109  13110    113   2146    168  A    C  
ATOM   5013  CG1 ILE A 650     133.414  54.762  10.922  1.00106.71      A    C  
ANISOU 5013  CG1 ILE A 650    14090  13165  13289    104   2249    161  A    C  
ATOM   5014  CG2 ILE A 650     132.317  52.522  11.352  1.00111.73      A    C  
ANISOU 5014  CG2 ILE A 650    14665  13874  13912     88   2222    214  A    C  
ATOM   5015  CD1 ILE A 650     133.349  56.081  11.647  1.00106.75      A    C  
ANISOU 5015  CD1 ILE A 650    13989  13255  13315    143   2160    133  A    C  
ATOM   5016  N   SER A 661     120.906  54.724   7.063  1.00110.23      A    N  
ANISOU 5016  N   SER A 661    14744  13703  13434    363    752   -489  A    N  
ATOM   5017  CA  SER A 661     121.392  53.346   6.934  1.00113.29      A    C  
ANISOU 5017  CA  SER A 661    15212  14067  13764    282    921   -366  A    C  
ATOM   5018  C   SER A 661     122.145  53.169   5.603  1.00111.18      A    C  
ANISOU 5018  C   SER A 661    15275  13573  13393    273    940   -276  A    C  
ATOM   5019  O   SER A 661     123.301  52.774   5.586  1.00108.14      A    O  
ANISOU 5019  O   SER A 661    14974  13143  12969    223   1123   -167  A    O  
ATOM   5020  CB  SER A 661     120.248  52.327   7.082  1.00110.08      A    C  
ANISOU 5020  CB  SER A 661    14699  13742  13383    245    886   -420  A    C  
ATOM   5021  N   THR A 662     121.485  53.487   4.493  1.00117.37      A    N  
ANISOU 5021  N   THR A 662    16246  14210  14138    317    748   -337  A    N  
ATOM   5022  CA  THR A 662     122.075  53.380   3.145  1.00108.11      A    C  
ANISOU 5022  CA  THR A 662    15431  12803  12842    294    746   -266  A    C  
ATOM   5023  C   THR A 662     121.045  53.924   2.174  1.00102.19      A    C  
ANISOU 5023  C   THR A 662    14840  11914  12072    361    461   -367  A    C  
ATOM   5024  O   THR A 662     119.924  54.210   2.568  1.00 98.02      A    O  
ANISOU 5024  O   THR A 662    14115  11484  11644    425    291   -493  A    O  
ATOM   5025  CB  THR A 662     122.389  51.920   2.812  1.00104.31      A    C  
ANISOU 5025  CB  THR A 662    15043  12284  12304    215    909   -170  A    C  
ATOM   5026  N   PHE A 663     121.402  54.126   0.918  1.00105.26      A    N  
ANISOU 5026  N   PHE A 663    15586  12070  12337    346    395   -327  A    N  
ATOM   5027  CA  PHE A 663     122.773  54.126   0.446  1.00104.14      A    C  
ANISOU 5027  CA  PHE A 663    15678  11805  12083    266    593   -213  A    C  
ATOM   5028  C   PHE A 663     123.108  55.505  -0.075  1.00105.83      A    C  
ANISOU 5028  C   PHE A 663    16097  11875  12236    293    463   -241  A    C  
ATOM   5029  O   PHE A 663     124.269  55.823  -0.307  1.00 94.59      A    O  
ANISOU 5029  O   PHE A 663    14832  10370  10735    223    624   -169  A    O  
ATOM   5030  CB  PHE A 663     122.911  53.131  -0.681  1.00105.60      A    C  
ANISOU 5030  CB  PHE A 663    16160  11818  12142    192    645   -148  A    C  
ATOM   5031  CG  PHE A 663     124.207  53.241  -1.457  1.00101.07      A    C  
ANISOU 5031  CG  PHE A 663    15894  11071  11432     96    823    -62  A    C  
ATOM   5032  CD1 PHE A 663     125.403  52.841  -0.886  1.00104.23      A    C  
ANISOU 5032  CD1 PHE A 663    16185  11554  11859     27   1118      8  A    C  
ATOM   5033  CD2 PHE A 663     124.222  53.672  -2.771  1.00 94.94      A    C  
ANISOU 5033  CD2 PHE A 663    15527  10043  10501     62    697    -62  A    C  
ATOM   5034  CE1 PHE A 663     126.593  52.906  -1.602  1.00 97.89      A    C  
ANISOU 5034  CE1 PHE A 663    15645  10599  10948    -75   1305     62  A    C  
ATOM   5035  CE2 PHE A 663     125.407  53.721  -3.499  1.00 89.38      A    C  
ANISOU 5035  CE2 PHE A 663    15118   9179   9661    -56    890      5  A    C  
ATOM   5036  CZ  PHE A 663     126.593  53.343  -2.916  1.00 88.18      A    C  
ANISOU 5036  CZ  PHE A 663    14826   9126   9552   -127   1205     58  A    C  
ATOM   5037  N   MET A 664     122.078  56.334  -0.241  1.00113.46      A    N  
ANISOU 5037  N   MET A 664    17053  12806  13247    393    165   -356  A    N  
ATOM   5038  CA  MET A 664     122.289  57.716  -0.616  1.00113.51      A    C  
ANISOU 5038  CA  MET A 664    17234  12683  13212    434      3   -395  A    C  
ATOM   5039  C   MET A 664     122.857  58.499   0.542  1.00115.35      A    C  
ANISOU 5039  C   MET A 664    17201  13087  13537    456    113   -402  A    C  
ATOM   5040  O   MET A 664     123.530  59.500   0.320  1.00127.09      A    O  
ANISOU 5040  O   MET A 664    18847  14474  14965    447     96   -387  A    O  
ATOM   5041  CB  MET A 664     121.003  58.378  -1.070  1.00118.52      A    C  
ANISOU 5041  CB  MET A 664    17909  13228  13895    550   -374   -534  A    C  
ATOM   5042  CG  MET A 664     121.268  59.370  -2.188  1.00123.73      A    C  
ANISOU 5042  CG  MET A 664    18988  13608  14416    553   -573   -533  A    C  
ATOM   5043  SD  MET A 664     119.848  60.368  -2.656  1.00135.76      A    S  
ANISOU 5043  SD  MET A 664    20557  15002  16022    716  -1065   -719  A    S  
ATOM   5044  CE  MET A 664     120.171  61.886  -1.749  1.00130.43      A    C  
ANISOU 5044  CE  MET A 664    19690  14426  15441    793  -1113   -786  A    C  
ATOM   5045  N   VAL A 665     122.588  58.060   1.774  1.00114.87      A    N  
ANISOU 5045  N   VAL A 665    16757  13276  13611    476    223   -426  A    N  
ATOM   5046  CA  VAL A 665     123.225  58.674   2.948  1.00104.72      A    C  
ANISOU 5046  CA  VAL A 665    15224  12159  12404    482    356   -419  A    C  
ATOM   5047  C   VAL A 665     124.690  58.278   3.041  1.00 95.76      A    C  
ANISOU 5047  C   VAL A 665    14166  11008  11208    379    650   -285  A    C  
ATOM   5048  O   VAL A 665     125.472  59.026   3.567  1.00 94.83      A    O  
ANISOU 5048  O   VAL A 665    13984  10933  11113    374    731   -267  A    O  
ATOM   5049  CB  VAL A 665     122.502  58.371   4.275  1.00106.24      A    C  
ANISOU 5049  CB  VAL A 665    15011  12611  12744    518    381   -490  A    C  
ATOM   5050  CG1 VAL A 665     121.220  59.178   4.374  1.00105.45      A    C  
ANISOU 5050  CG1 VAL A 665    14782  12545  12739    627    103   -663  A    C  
ATOM   5051  CG2 VAL A 665     122.227  56.878   4.428  1.00117.41      A    C  
ANISOU 5051  CG2 VAL A 665    16345  14103  14162    457    513   -442  A    C  
ATOM   5052  N   GLU A 666     125.074  57.117   2.528  1.00101.09      A    N  
ANISOU 5052  N   GLU A 666    14968  11622  11817    299    805   -203  A    N  
ATOM   5053  CA  GLU A 666     126.510  56.811   2.366  1.00108.36      A    C  
ANISOU 5053  CA  GLU A 666    16007  12483  12682    199   1070   -102  A    C  
ATOM   5054  C   GLU A 666     127.153  57.775   1.390  1.00103.34      A    C  
ANISOU 5054  C   GLU A 666    15702  11638  11925    157   1036    -93  A    C  
ATOM   5055  O   GLU A 666     128.246  58.302   1.639  1.00 93.80      A    O  
ANISOU 5055  O   GLU A 666    14496  10427  10717    108   1190    -62  A    O  
ATOM   5056  CB  GLU A 666     126.744  55.376   1.866  1.00120.47      A    C  
ANISOU 5056  CB  GLU A 666    17638  13968  14167    123   1229    -36  A    C  
ATOM   5057  CG  GLU A 666     127.482  54.478   2.851  1.00127.90      A    C  
ANISOU 5057  CG  GLU A 666    18334  15061  15201     87   1471     21  A    C  
ATOM   5058  CD  GLU A 666     127.942  53.149   2.255  1.00139.60      A    C  
ANISOU 5058  CD  GLU A 666    19946  16462  16633      9   1644     80  A    C  
ATOM   5059  OE1 GLU A 666     129.170  52.914   2.189  1.00132.86      A    O  
ANISOU 5059  OE1 GLU A 666    19134  15564  15780    -61   1863    120  A    O  
ATOM   5060  OE2 GLU A 666     127.074  52.328   1.867  1.00151.15      A    O1-
ANISOU 5060  OE2 GLU A 666    21456  17906  18065     16   1561     77  A    O1-
ATOM   5061  N   MET A 667     126.457  57.983   0.273  1.00109.58      A    N  
ANISOU 5061  N   MET A 667    16781  12243  12608    169    828   -125  A    N  
ATOM   5062  CA  MET A 667     126.954  58.820  -0.823  1.00110.87      A    C  
ANISOU 5062  CA  MET A 667    17341  12165  12617    109    766   -114  A    C  
ATOM   5063  C   MET A 667     126.860  60.325  -0.458  1.00107.04      A    C  
ANISOU 5063  C   MET A 667    16819  11684  12167    184    587   -174  A    C  
ATOM   5064  O   MET A 667     127.714  61.110  -0.861  1.00101.90      A    O  
ANISOU 5064  O   MET A 667    16389  10905  11423    114    642   -148  A    O  
ATOM   5065  CB  MET A 667     126.227  58.487  -2.133  1.00105.99      A    C  
ANISOU 5065  CB  MET A 667    17075  11329  11865     95    579   -124  A    C  
ATOM   5066  N   SER A 668     125.857  60.710   0.336  1.00 99.74      A    N  
ANISOU 5066  N   SER A 668    15608  10909  11379    315    393   -263  A    N  
ATOM   5067  CA  SER A 668     125.744  62.080   0.819  1.00 97.35      A    C  
ANISOU 5067  CA  SER A 668    15218  10635  11133    397    234   -332  A    C  
ATOM   5068  C   SER A 668     126.942  62.423   1.699  1.00 99.57      A    C  
ANISOU 5068  C   SER A 668    15336  11037  11458    345    482   -276  A    C  
ATOM   5069  O   SER A 668     127.563  63.478   1.522  1.00110.85      A    O  
ANISOU 5069  O   SER A 668    16913  12371  12833    324    459   -273  A    O  
ATOM   5070  CB  SER A 668     124.469  62.292   1.657  1.00 99.77      A    C  
ANISOU 5070  CB  SER A 668    15185  11116  11604    537     30   -458  A    C  
ATOM   5071  OG  SER A 668     123.302  62.402   0.875  1.00104.92      A    O  
ANISOU 5071  OG  SER A 668    15975  11641  12247    614   -276   -551  A    O  
ATOM   5072  N   GLU A 669     127.249  61.558   2.669  1.00 94.16      A    N  
ANISOU 5072  N   GLU A 669    14347  10553  10873    326    702   -238  A    N  
ATOM   5073  CA  GLU A 669     128.297  61.855   3.645  1.00 88.29      A    C  
ANISOU 5073  CA  GLU A 669    13405   9939  10200    295    906   -199  A    C  
ATOM   5074  C   GLU A 669     129.657  61.873   2.956  1.00 84.29      A    C  
ANISOU 5074  C   GLU A 669    13154   9281   9591    167   1117   -124  A    C  
ATOM   5075  O   GLU A 669     130.511  62.687   3.296  1.00 80.81      A    O  
ANISOU 5075  O   GLU A 669    12695   8844   9164    140   1196   -115  A    O  
ATOM   5076  CB  GLU A 669     128.267  60.873   4.820  1.00 89.51      A    C  
ANISOU 5076  CB  GLU A 669    13210  10320  10479    304   1060   -178  A    C  
ATOM   5077  N   THR A 670     129.843  61.009   1.961  1.00 86.59      A    N  
ANISOU 5077  N   THR A 670    13688   9432   9777     79   1209    -80  A    N  
ATOM   5078  CA  THR A 670     131.113  60.988   1.183  1.00 89.20      A    C  
ANISOU 5078  CA  THR A 670    14287   9603   9999    -68   1430    -30  A    C  
ATOM   5079  C   THR A 670     131.223  62.158   0.199  1.00 85.45      A    C  
ANISOU 5079  C   THR A 670    14191   8905   9369   -115   1292    -47  A    C  
ATOM   5080  O   THR A 670     132.322  62.624  -0.079  1.00 85.96      A    O  
ANISOU 5080  O   THR A 670    14407   8881   9372   -228   1460    -28  A    O  
ATOM   5081  CB  THR A 670     131.314  59.678   0.382  1.00 89.73      A    C  
ANISOU 5081  CB  THR A 670    14518   9581   9992   -161   1591     10  A    C  
ATOM   5082  CG2 THR A 670     131.757  58.548   1.286  1.00 89.79      A    C  
ANISOU 5082  CG2 THR A 670    14206   9768  10141   -160   1809     37  A    C  
ATOM   5083  OG1 THR A 670     130.068  59.315  -0.212  1.00 96.48      A    O  
ANISOU 5083  OG1 THR A 670    15496  10372  10789   -102   1365     -9  A    O  
ATOM   5084  N   ALA A 671     130.101  62.626  -0.339  1.00 80.43      A    N  
ANISOU 5084  N   ALA A 671    13718   8168   8672    -34    981    -91  A    N  
ATOM   5085  CA  ALA A 671     130.132  63.821  -1.183  1.00 79.09      A    C  
ANISOU 5085  CA  ALA A 671    13913   7779   8359    -63    797   -112  A    C  
ATOM   5086  C   ALA A 671     130.732  64.947  -0.407  1.00 77.54      A    C  
ANISOU 5086  C   ALA A 671    13571   7661   8231    -43    820   -128  A    C  
ATOM   5087  O   ALA A 671     131.693  65.553  -0.853  1.00 78.32      A    O  
ANISOU 5087  O   ALA A 671    13907   7627   8223   -164    934   -102  A    O  
ATOM   5088  CB  ALA A 671     128.741  64.215  -1.651  1.00 81.22      A    C  
ANISOU 5088  CB  ALA A 671    14300   7952   8607     62    409   -180  A    C  
ATOM   5089  N   TYR A 672     130.145  65.228   0.756  1.00 77.92      A    N  
ANISOU 5089  N   TYR A 672    13235   7920   8449    101    714   -177  A    N  
ATOM   5090  CA  TYR A 672     130.658  66.245   1.670  1.00 76.76      A    C  
ANISOU 5090  CA  TYR A 672    12896   7880   8387    135    735   -196  A    C  
ATOM   5091  C   TYR A 672     132.156  66.059   1.927  1.00 75.01      A    C  
ANISOU 5091  C   TYR A 672    12640   7687   8170      0   1076   -132  A    C  
ATOM   5092  O   TYR A 672     132.901  67.010   1.898  1.00 74.58      A    O  
ANISOU 5092  O   TYR A 672    12693   7567   8078    -55   1112   -130  A    O  
ATOM   5093  CB  TYR A 672     129.930  66.154   2.982  1.00 76.34      A    C  
ANISOU 5093  CB  TYR A 672    12399   8083   8521    274    668   -248  A    C  
ATOM   5094  CG  TYR A 672     130.353  67.175   3.998  1.00 80.00      A    C  
ANISOU 5094  CG  TYR A 672    12649   8668   9078    319    673   -273  A    C  
ATOM   5095  CD1 TYR A 672     129.718  68.409   4.054  1.00 82.27      A    C  
ANISOU 5095  CD1 TYR A 672    12965   8916   9376    421    400   -355  A    C  
ATOM   5096  CD2 TYR A 672     131.353  66.895   4.944  1.00 83.75      A    C  
ANISOU 5096  CD2 TYR A 672    12882   9295   9642    271    934   -224  A    C  
ATOM   5097  CE1 TYR A 672     130.060  69.359   4.998  1.00 84.21      A    C  
ANISOU 5097  CE1 TYR A 672    13015   9275   9708    467    397   -384  A    C  
ATOM   5098  CE2 TYR A 672     131.724  67.845   5.898  1.00 86.67      A    C  
ANISOU 5098  CE2 TYR A 672    13061   9773  10096    314    927   -248  A    C  
ATOM   5099  CZ  TYR A 672     131.060  69.081   5.918  1.00 87.38      A    C  
ANISOU 5099  CZ  TYR A 672    13191   9826  10183    409    663   -325  A    C  
ATOM   5100  OH  TYR A 672     131.380  70.054   6.837  1.00 86.81      A    O  
ANISOU 5100  OH  TYR A 672    12941   9854  10189    456    644   -354  A    O  
ATOM   5101  N   ILE A 673     132.593  64.826   2.170  1.00 73.91      A    N  
ANISOU 5101  N   ILE A 673    12350   7643   8088    -53   1319    -89  A    N  
ATOM   5102  CA  ILE A 673     134.005  64.561   2.497  1.00 72.16      A    C  
ANISOU 5102  CA  ILE A 673    12042   7460   7913   -166   1636    -54  A    C  
ATOM   5103  C   ILE A 673     134.919  64.891   1.360  1.00 72.83      A    C  
ANISOU 5103  C   ILE A 673    12511   7320   7836   -336   1773    -41  A    C  
ATOM   5104  O   ILE A 673     135.993  65.428   1.572  1.00 68.44      A    O  
ANISOU 5104  O   ILE A 673    11942   6759   7303   -419   1939    -45  A    O  
ATOM   5105  CB  ILE A 673     134.266  63.088   2.934  1.00 70.35      A    C  
ANISOU 5105  CB  ILE A 673    11586   7358   7786   -180   1849    -25  A    C  
ATOM   5106  CG1 ILE A 673     133.620  62.863   4.291  1.00 70.12      A    C  
ANISOU 5106  CG1 ILE A 673    11157   7566   7920    -43   1761    -36  A    C  
ATOM   5107  CG2 ILE A 673     135.771  62.768   2.992  1.00 67.12      A    C  
ANISOU 5107  CG2 ILE A 673    11144   6936   7422   -309   2169    -12  A    C  
ATOM   5108  CD1 ILE A 673     133.513  61.438   4.721  1.00 71.75      A    C  
ANISOU 5108  CD1 ILE A 673    11167   7885   8208    -35   1881     -8  A    C  
ATOM   5109  N   LEU A 674     134.475  64.554   0.154  1.00 77.91      A    N  
ANISOU 5109  N   LEU A 674    13506   7778   8316   -396   1702    -32  A    N  
ATOM   5110  CA  LEU A 674     135.350  64.622  -1.004  1.00 82.72      A    C  
ANISOU 5110  CA  LEU A 674    14514   8165   8750   -593   1876    -20  A    C  
ATOM   5111  C   LEU A 674     135.686  66.062  -1.367  1.00 81.82      A    C  
ANISOU 5111  C   LEU A 674    14663   7902   8519   -652   1774    -35  A    C  
ATOM   5112  O   LEU A 674     136.831  66.350  -1.724  1.00 76.61      A    O  
ANISOU 5112  O   LEU A 674    14165   7151   7793   -823   2007    -39  A    O  
ATOM   5113  CB  LEU A 674     134.769  63.846  -2.190  1.00 85.36      A    C  
ANISOU 5113  CB  LEU A 674    15177   8329   8925   -648   1821     -4  A    C  
ATOM   5114  CG  LEU A 674     135.038  62.340  -2.086  1.00 86.81      A    C  
ANISOU 5114  CG  LEU A 674    15190   8606   9187   -679   2063     12  A    C  
ATOM   5115  CD1 LEU A 674     134.615  61.638  -3.374  1.00 90.85      A    C  
ANISOU 5115  CD1 LEU A 674    16080   8921   9516   -763   2037     27  A    C  
ATOM   5116  CD2 LEU A 674     136.491  62.029  -1.775  1.00 84.94      A    C  
ANISOU 5116  CD2 LEU A 674    14816   8424   9033   -806   2433     -2  A    C  
ATOM   5117  N   HIS A 675     134.711  66.964  -1.243  1.00 81.21      A    N  
ANISOU 5117  N   HIS A 675    14619   7805   8430   -515   1431    -55  A    N  
ATOM   5118  CA  HIS A 675     135.013  68.361  -1.500  1.00 85.17      A    C  
ANISOU 5118  CA  HIS A 675    15360   8168   8833   -558   1311    -70  A    C  
ATOM   5119  C   HIS A 675     134.923  69.215  -0.264  1.00 82.73      A    C  
ANISOU 5119  C   HIS A 675    14696   8043   8691   -417   1207   -100  A    C  
ATOM   5120  O   HIS A 675     134.301  70.259  -0.262  1.00 83.71      A    O  
ANISOU 5120  O   HIS A 675    14908   8105   8789   -324    918   -134  A    O  
ATOM   5121  CB  HIS A 675     134.193  68.957  -2.655  1.00 90.98      A    C  
ANISOU 5121  CB  HIS A 675    16563   8639   9367   -559    989    -80  A    C  
ATOM   5122  CG  HIS A 675     132.726  68.777  -2.521  1.00 92.45      A    C  
ANISOU 5122  CG  HIS A 675    16629   8871   9623   -359    655   -117  A    C  
ATOM   5123  CD2 HIS A 675     131.935  68.727  -1.429  1.00 96.11      A    C  
ANISOU 5123  CD2 HIS A 675    16656   9567  10294   -165    524   -161  A    C  
ATOM   5124  ND1 HIS A 675     131.899  68.609  -3.612  1.00 95.15      A    N  
ANISOU 5124  ND1 HIS A 675    17333   9001   9819   -355    416   -123  A    N  
ATOM   5125  CE1 HIS A 675     130.656  68.466  -3.196  1.00 99.30      A    C  
ANISOU 5125  CE1 HIS A 675    17623   9629  10474   -159    149   -179  A    C  
ATOM   5126  NE2 HIS A 675     130.652  68.529  -1.876  1.00104.33      A    N  
ANISOU 5126  NE2 HIS A 675    17777  10538  11322    -49    222   -205  A    N  
ATOM   5127  N   HIS A 676     135.568  68.758   0.798  1.00 80.21      A    N  
ANISOU 5127  N   HIS A 676    13981   7944   8550   -403   1440    -93  A    N  
ATOM   5128  CA  HIS A 676     135.840  69.609   1.946  1.00 74.99      A    C  
ANISOU 5128  CA  HIS A 676    13024   7438   8028   -320   1414   -114  A    C  
ATOM   5129  C   HIS A 676     137.142  69.210   2.631  1.00 74.88      A    C  
ANISOU 5129  C   HIS A 676    12765   7548   8136   -409   1751    -99  A    C  
ATOM   5130  O   HIS A 676     137.771  70.049   3.253  1.00 76.48      A    O  
ANISOU 5130  O   HIS A 676    12852   7803   8402   -414   1788   -112  A    O  
ATOM   5131  CB  HIS A 676     134.701  69.556   2.940  1.00 72.58      A    C  
ANISOU 5131  CB  HIS A 676    12371   7330   7872   -115   1198   -148  A    C  
ATOM   5132  CG  HIS A 676     133.504  70.335   2.528  1.00 73.95      A    C  
ANISOU 5132  CG  HIS A 676    12709   7404   7982      0    833   -199  A    C  
ATOM   5133  CD2 HIS A 676     132.231  69.951   2.273  1.00 76.73      A    C  
ANISOU 5133  CD2 HIS A 676    13060   7752   8341    112    604   -238  A    C  
ATOM   5134  ND1 HIS A 676     133.542  71.695   2.337  1.00 77.40      A    N  
ANISOU 5134  ND1 HIS A 676    13332   7720   8353     14    649   -229  A    N  
ATOM   5135  CE1 HIS A 676     132.345  72.121   1.974  1.00 80.89      A    C  
ANISOU 5135  CE1 HIS A 676    13882   8081   8770    138    310   -290  A    C  
ATOM   5136  NE2 HIS A 676     131.531  71.079   1.927  1.00 81.58      A    N  
ANISOU 5136  NE2 HIS A 676    13851   8240   8906    199    279   -302  A    N  
ATOM   5137  N   ALA A 677     137.554  67.945   2.514  1.00 73.92      A    N  
ANISOU 5137  N   ALA A 677    12564   7466   8055   -476   1985    -81  A    N  
ATOM   5138  CA  ALA A 677     138.778  67.478   3.164  1.00 73.00      A    C  
ANISOU 5138  CA  ALA A 677    12194   7457   8082   -547   2287    -86  A    C  
ATOM   5139  C   ALA A 677     139.969  68.132   2.507  1.00 74.07      A    C  
ANISOU 5139  C   ALA A 677    12577   7438   8127   -737   2480   -109  A    C  
ATOM   5140  O   ALA A 677     139.902  68.501   1.368  1.00 77.10      A    O  
ANISOU 5140  O   ALA A 677    13367   7614   8312   -850   2447   -107  A    O  
ATOM   5141  CB  ALA A 677     138.897  65.978   3.053  1.00 73.64      A    C  
ANISOU 5141  CB  ALA A 677    12174   7585   8220   -573   2470    -75  A    C  
ATOM   5142  N   THR A 678     141.062  68.272   3.232  1.00 77.62      A    N  
ANISOU 5142  N   THR A 678    12789   7979   8722   -780   2680   -136  A    N  
ATOM   5143  CA  THR A 678     142.249  68.949   2.723  1.00 85.04      A    C  
ANISOU 5143  CA  THR A 678    13920   8789   9600   -971   2882   -174  A    C  
ATOM   5144  C   THR A 678     143.507  68.183   3.079  1.00 89.42      A    C  
ANISOU 5144  C   THR A 678    14230   9417  10328  -1063   3218   -226  A    C  
ATOM   5145  O   THR A 678     143.417  67.050   3.557  1.00 93.93      A    O  
ANISOU 5145  O   THR A 678    14543  10107  11038   -986   3281   -225  A    O  
ATOM   5146  CB  THR A 678     142.375  70.355   3.331  1.00 86.63      A    C  
ANISOU 5146  CB  THR A 678    14075   9017   9821   -925   2738   -178  A    C  
ATOM   5147  CG2 THR A 678     141.022  71.076   3.292  1.00 88.26      A    C  
ANISOU 5147  CG2 THR A 678    14407   9199   9928   -774   2364   -146  A    C  
ATOM   5148  OG1 THR A 678     142.853  70.272   4.683  1.00 84.28      A    O  
ANISOU 5148  OG1 THR A 678    13334   8927   9760   -828   2798   -192  A    O  
ATOM   5149  N   GLU A 679     144.667  68.808   2.881  1.00 91.07      A    N  
ANISOU 5149  N   GLU A 679    14511   9551  10538  -1227   3420   -283  A    N  
ATOM   5150  CA  GLU A 679     145.939  68.221   3.283  1.00 95.80      A    C  
ANISOU 5150  CA  GLU A 679    14843  10217  11337  -1310   3729   -362  A    C  
ATOM   5151  C   GLU A 679     146.060  68.021   4.798  1.00 92.89      A    C  
ANISOU 5151  C   GLU A 679    13990  10068  11234  -1129   3662   -360  A    C  
ATOM   5152  O   GLU A 679     146.848  67.217   5.283  1.00 93.62      A    O  
ANISOU 5152  O   GLU A 679    13804  10239  11528  -1134   3849   -418  A    O  
ATOM   5153  CB  GLU A 679     147.086  69.105   2.850  1.00107.68      A    C  
ANISOU 5153  CB  GLU A 679    16509  11605  12797  -1519   3932   -435  A    C  
ATOM   5154  CG  GLU A 679     147.107  69.461   1.369  1.00122.22      A    C  
ANISOU 5154  CG  GLU A 679    18879  13206  14352  -1738   4012   -442  A    C  
ATOM   5155  CD  GLU A 679     146.229  70.651   0.992  1.00123.21      A    C  
ANISOU 5155  CD  GLU A 679    19342  13218  14254  -1704   3703   -367  A    C  
ATOM   5156  OE1 GLU A 679     145.564  71.243   1.874  1.00124.81      A    O  
ANISOU 5156  OE1 GLU A 679    19356  13536  14528  -1505   3430   -317  A    O  
ATOM   5157  OE2 GLU A 679     146.217  70.990  -0.211  1.00119.87      A    O1-
ANISOU 5157  OE2 GLU A 679    19389  12575  13578  -1884   3733   -365  A    O1-
ATOM   5158  N   GLN A 680     145.279  68.767   5.555  1.00 90.67      A    N  
ANISOU 5158  N   GLN A 680    13618   9880  10954   -971   3386   -301  A    N  
ATOM   5159  CA  GLN A 680     145.369  68.697   6.990  1.00 88.52      A    C  
ANISOU 5159  CA  GLN A 680    12932   9800  10899   -817   3312   -295  A    C  
ATOM   5160  C   GLN A 680     144.232  67.920   7.582  1.00 87.55      A    C  
ANISOU 5160  C   GLN A 680    12647   9807  10810   -640   3125   -235  A    C  
ATOM   5161  O   GLN A 680     144.196  67.748   8.780  1.00 92.03      A    O  
ANISOU 5161  O   GLN A 680    12899  10529  11537   -518   3053   -223  A    O  
ATOM   5162  CB  GLN A 680     145.328  70.097   7.567  1.00 91.88      A    C  
ANISOU 5162  CB  GLN A 680    13339  10255  11313   -769   3149   -283  A    C  
ATOM   5163  CG  GLN A 680     146.305  71.063   6.907  1.00 96.70      A    C  
ANISOU 5163  CG  GLN A 680    14171  10720  11847   -954   3297   -334  A    C  
ATOM   5164  CD  GLN A 680     146.110  72.481   7.377  1.00 96.96      A    C  
ANISOU 5164  CD  GLN A 680    14233  10765  11840   -899   3100   -313  A    C  
ATOM   5165  NE2 GLN A 680     146.559  72.768   8.591  1.00 94.76      A    N  
ANISOU 5165  NE2 GLN A 680    13622  10628  11751   -812   3081   -327  A    N  
ATOM   5166  OE1 GLN A 680     145.519  73.303   6.671  1.00105.05      A    O  
ANISOU 5166  OE1 GLN A 680    15583  11666  12666   -924   2945   -287  A    O  
ATOM   5167  N   SER A 681     143.281  67.468   6.767  1.00 84.06      A    N  
ANISOU 5167  N   SER A 681    12428   9296  10214   -633   3039   -199  A    N  
ATOM   5168  CA  SER A 681     142.150  66.723   7.294  1.00 77.86      A    C  
ANISOU 5168  CA  SER A 681    11493   8632   9457   -479   2867   -151  A    C  
ATOM   5169  C   SER A 681     142.546  65.299   7.585  1.00 73.56      A    C  
ANISOU 5169  C   SER A 681    10747   8150   9051   -477   3029   -161  A    C  
ATOM   5170  O   SER A 681     143.554  64.819   7.112  1.00 78.30      A    O  
ANISOU 5170  O   SER A 681    11374   8675   9699   -596   3269   -211  A    O  
ATOM   5171  CB  SER A 681     140.992  66.737   6.314  1.00 82.01      A    C  
ANISOU 5171  CB  SER A 681    12320   9054   9785   -468   2703   -121  A    C  
ATOM   5172  OG  SER A 681     140.483  68.050   6.177  1.00 84.02      A    O  
ANISOU 5172  OG  SER A 681    12734   9255   9933   -435   2495   -118  A    O  
ATOM   5173  N   ILE A 682     141.743  64.635   8.384  1.00 70.07      A    N  
ANISOU 5173  N   ILE A 682    10102   7846   8676   -343   2897   -122  A    N  
ATOM   5174  CA  ILE A 682     141.906  63.219   8.661  1.00 71.00      A    C  
ANISOU 5174  CA  ILE A 682    10054   8017   8905   -325   3001   -120  A    C  
ATOM   5175  C   ILE A 682     140.613  62.492   8.350  1.00 68.06      A    C  
ANISOU 5175  C   ILE A 682     9765   7661   8429   -263   2866    -72  A    C  
ATOM   5176  O   ILE A 682     139.606  62.688   9.035  1.00 66.41      A    O  
ANISOU 5176  O   ILE A 682     9454   7565   8213   -151   2664    -40  A    O  
ATOM   5177  CB  ILE A 682     142.231  62.995  10.139  1.00 72.55      A    C  
ANISOU 5177  CB  ILE A 682     9898   8369   9296   -228   2965   -117  A    C  
ATOM   5178  CG1 ILE A 682     143.630  63.552  10.417  1.00 76.73      A    C  
ANISOU 5178  CG1 ILE A 682    10322   8872   9960   -293   3115   -178  A    C  
ATOM   5179  CG2 ILE A 682     142.099  61.517  10.498  1.00 71.01      A    C  
ANISOU 5179  CG2 ILE A 682     9556   8228   9193   -185   3000   -101  A    C  
ATOM   5180  CD1 ILE A 682     144.089  63.387  11.853  1.00 77.01      A    C  
ANISOU 5180  CD1 ILE A 682    10030   9035  10195   -204   3069   -182  A    C  
ATOM   5181  N   VAL A 683     140.643  61.654   7.323  1.00 65.81      A    N  
ANISOU 5181  N   VAL A 683     9666   7266   8071   -341   2983    -78  A    N  
ATOM   5182  CA  VAL A 683     139.436  61.010   6.849  1.00 64.27      A    C  
ANISOU 5182  CA  VAL A 683     9592   7061   7764   -297   2857    -38  A    C  
ATOM   5183  C   VAL A 683     139.395  59.566   7.291  1.00 64.67      A    C  
ANISOU 5183  C   VAL A 683     9462   7187   7921   -260   2921    -23  A    C  
ATOM   5184  O   VAL A 683     140.418  58.901   7.303  1.00 66.26      A    O  
ANISOU 5184  O   VAL A 683     9579   7361   8233   -315   3118    -59  A    O  
ATOM   5185  CB  VAL A 683     139.336  61.108   5.323  1.00 64.06      A    C  
ANISOU 5185  CB  VAL A 683     9948   6841   7549   -410   2905    -47  A    C  
ATOM   5186  CG1 VAL A 683     138.035  60.490   4.822  1.00 62.76      A    C  
ANISOU 5186  CG1 VAL A 683     9912   6659   7275   -357   2744    -11  A    C  
ATOM   5187  CG2 VAL A 683     139.423  62.575   4.901  1.00 65.39      A    C  
ANISOU 5187  CG2 VAL A 683    10323   6915   7604   -455   2824    -60  A    C  
ATOM   5188  N   LEU A 684     138.214  59.097   7.682  1.00 65.06      A    N  
ANISOU 5188  N   LEU A 684     9444   7328   7944   -168   2751     18  A    N  
ATOM   5189  CA  LEU A 684     138.013  57.717   8.027  1.00 67.21      A    C  
ANISOU 5189  CA  LEU A 684     9591   7658   8287   -139   2785     40  A    C  
ATOM   5190  C   LEU A 684     136.866  57.171   7.244  1.00 70.77      A    C  
ANISOU 5190  C   LEU A 684    10221   8064   8603   -132   2688     65  A    C  
ATOM   5191  O   LEU A 684     135.775  57.739   7.258  1.00 70.65      A    O  
ANISOU 5191  O   LEU A 684    10249   8086   8507    -76   2493     73  A    O  
ATOM   5192  CB  LEU A 684     137.710  57.578   9.498  1.00 70.39      A    C  
ANISOU 5192  CB  LEU A 684     9706   8234   8805    -43   2676     64  A    C  
ATOM   5193  CG  LEU A 684     138.977  57.479  10.336  1.00 75.01      A    C  
ANISOU 5193  CG  LEU A 684    10082   8851   9565    -46   2793     40  A    C  
ATOM   5194  CD1 LEU A 684     139.523  58.869  10.623  1.00 76.31      A    C  
ANISOU 5194  CD1 LEU A 684    10218   9023   9752    -50   2780     14  A    C  
ATOM   5195  CD2 LEU A 684     138.682  56.762  11.639  1.00 79.06      A    C  
ANISOU 5195  CD2 LEU A 684    10362   9497  10178     28   2704     74  A    C  
ATOM   5196  N   MET A 685     137.109  56.044   6.580  1.00 77.57      A    N  
ANISOU 5196  N   MET A 685    11174   8845   9453   -187   2818     66  A    N  
ATOM   5197  CA  MET A 685     136.103  55.396   5.759  1.00 83.04      A    C  
ANISOU 5197  CA  MET A 685    12050   9480  10020   -191   2741     89  A    C  
ATOM   5198  C   MET A 685     136.072  53.888   6.000  1.00 85.73      A    C  
ANISOU 5198  C   MET A 685    12286   9857  10431   -181   2811    109  A    C  
ATOM   5199  O   MET A 685     137.077  53.217   5.818  1.00 94.59      A    O  
ANISOU 5199  O   MET A 685    13389  10922  11630   -234   3003     83  A    O  
ATOM   5200  CB  MET A 685     136.398  55.696   4.311  1.00 83.36      A    C  
ANISOU 5200  CB  MET A 685    12430   9326   9913   -298   2826     67  A    C  
ATOM   5201  CG  MET A 685     136.335  57.178   4.052  1.00 86.22      A    C  
ANISOU 5201  CG  MET A 685    12930   9637  10190   -307   2723     53  A    C  
ATOM   5202  SD  MET A 685     135.694  57.619   2.431  1.00100.79      A    S  
ANISOU 5202  SD  MET A 685    15232  11267  11796   -381   2623     52  A    S  
ATOM   5203  CE  MET A 685     134.272  56.518   2.292  1.00104.75      A    C  
ANISOU 5203  CE  MET A 685    15728  11808  12264   -300   2454     83  A    C  
ATOM   5204  N   ASP A 686     134.910  53.376   6.395  1.00 81.19      A    N  
ANISOU 5204  N   ASP A 686    11643   9372   9834   -116   2655    143  A    N  
ATOM   5205  CA  ASP A 686     134.748  51.997   6.796  1.00 81.71      A    C  
ANISOU 5205  CA  ASP A 686    11599   9486   9961   -100   2686    170  A    C  
ATOM   5206  C   ASP A 686     133.839  51.290   5.802  1.00 87.33      A    C  
ANISOU 5206  C   ASP A 686    12514  10118  10547   -122   2636    186  A    C  
ATOM   5207  O   ASP A 686     132.635  51.512   5.770  1.00 91.11      A    O  
ANISOU 5207  O   ASP A 686    13021  10641  10953    -83   2459    193  A    O  
ATOM   5208  CB  ASP A 686     134.123  51.958   8.188  1.00 87.55      A    C  
ANISOU 5208  CB  ASP A 686    12091  10401  10772    -27   2550    195  A    C  
ATOM   5209  CG  ASP A 686     134.085  50.566   8.799  1.00 90.24      A    C  
ANISOU 5209  CG  ASP A 686    12313  10790  11182    -18   2574    226  A    C  
ATOM   5210  OD1 ASP A 686     133.162  49.771   8.494  1.00 91.08      A    O  
ANISOU 5210  OD1 ASP A 686    12487  10899  11220    -21   2513    248  A    O  
ATOM   5211  OD2 ASP A 686     134.953  50.298   9.649  1.00 95.32      A    O1-
ANISOU 5211  OD2 ASP A 686    12794  11469  11954     -4   2635    227  A    O1-
ATOM   5212  N   GLU A 687     134.424  50.421   4.991  1.00 98.80      A    N  
ANISOU 5212  N   GLU A 687    14101  11452  11985   -185   2794    178  A    N  
ATOM   5213  CA  GLU A 687     133.676  49.540   4.101  1.00 98.99      A    C  
ANISOU 5213  CA  GLU A 687    14312  11397  11903   -209   2764    196  A    C  
ATOM   5214  C   GLU A 687     132.679  50.305   3.249  1.00 96.02      A    C  
ANISOU 5214  C   GLU A 687    14159  10952  11371   -211   2599    194  A    C  
ATOM   5215  O   GLU A 687     131.495  50.013   3.271  1.00102.50      A    O  
ANISOU 5215  O   GLU A 687    14978  11818  12148   -167   2434    208  A    O  
ATOM   5216  CB  GLU A 687     132.984  48.430   4.922  1.00102.73      A    C  
ANISOU 5216  CB  GLU A 687    14609  11986  12437   -157   2687    234  A    C  
ATOM   5217  CG  GLU A 687     133.965  47.577   5.731  1.00105.28      A    C  
ANISOU 5217  CG  GLU A 687    14739  12348  12914   -150   2816    234  A    C  
ATOM   5218  CD  GLU A 687     133.372  46.261   6.200  1.00118.26      A    C  
ANISOU 5218  CD  GLU A 687    16306  14046  14582   -127   2762    274  A    C  
ATOM   5219  OE1 GLU A 687     132.711  45.568   5.403  1.00138.10      A    O  
ANISOU 5219  OE1 GLU A 687    18979  16494  17000   -152   2742    288  A    O  
ATOM   5220  OE2 GLU A 687     133.552  45.907   7.375  1.00131.05      A    O1-
ANISOU 5220  OE2 GLU A 687    17720  15762  16307    -90   2731    291  A    O1-
ATOM   5221  N   VAL A 688     133.159  51.303   2.518  1.00100.88      A    N  
ANISOU 5221  N   VAL A 688    14969  11453  11907   -262   2634    169  A    N  
ATOM   5222  CA  VAL A 688     132.303  52.023   1.564  1.00106.50      A    C  
ANISOU 5222  CA  VAL A 688    15948  12053  12460   -268   2460    161  A    C  
ATOM   5223  C   VAL A 688     132.089  51.189   0.302  1.00109.70      A    C  
ANISOU 5223  C   VAL A 688    16648  12296  12736   -340   2501    170  A    C  
ATOM   5224  O   VAL A 688     133.049  50.720  -0.316  1.00110.61      A    O  
ANISOU 5224  O   VAL A 688    16899  12302  12823   -439   2721    159  A    O  
ATOM   5225  CB  VAL A 688     132.885  53.392   1.156  1.00105.00      A    C  
ANISOU 5225  CB  VAL A 688    15917  11770  12207   -313   2468    135  A    C  
ATOM   5226  CG1 VAL A 688     134.298  53.227   0.610  1.00106.14      A    C  
ANISOU 5226  CG1 VAL A 688    16184  11801  12341   -439   2748    114  A    C  
ATOM   5227  CG2 VAL A 688     131.973  54.076   0.144  1.00100.63      A    C  
ANISOU 5227  CG2 VAL A 688    15670  11075  11487   -312   2252    126  A    C  
ATOM   5228  N   GLY A 689     130.824  51.008  -0.065  1.00109.26      A    N  
ANISOU 5228  N   GLY A 689    16684  12223  12607   -292   2289    178  A    N  
ATOM   5229  CA  GLY A 689     130.472  50.172  -1.190  1.00106.79      A    C  
ANISOU 5229  CA  GLY A 689    16641  11762  12172   -349   2293    190  A    C  
ATOM   5230  C   GLY A 689     129.395  49.164  -0.867  1.00111.16      A    C  
ANISOU 5230  C   GLY A 689    17062  12406  12765   -284   2174    207  A    C  
ATOM   5231  O   GLY A 689     128.669  48.760  -1.775  1.00122.64      A    O  
ANISOU 5231  O   GLY A 689    18738  13744  14110   -299   2067    210  A    O  
ATOM   5232  N   ARG A 690     129.297  48.741   0.401  1.00109.48      A    N  
ANISOU 5232  N   ARG A 690    16509  12388  12697   -224   2189    218  A    N  
ATOM   5233  CA  ARG A 690     128.204  47.863   0.848  1.00112.58      A    C  
ANISOU 5233  CA  ARG A 690    16761  12886  13129   -175   2071    228  A    C  
ATOM   5234  C   ARG A 690     126.833  48.443   0.421  1.00118.45      A    C  
ANISOU 5234  C   ARG A 690    17590  13605  13810   -122   1800    187  A    C  
ATOM   5235  O   ARG A 690     126.428  49.546   0.826  1.00115.81      A    O  
ANISOU 5235  O   ARG A 690    17161  13333  13508    -64   1656    143  A    O  
ATOM   5236  CB  ARG A 690     128.248  47.664   2.364  1.00117.76      A    C  
ANISOU 5236  CB  ARG A 690    17062  13749  13930   -127   2095    238  A    C  
ATOM   5237  CG  ARG A 690     129.511  46.995   2.903  1.00124.12      A    C  
ANISOU 5237  CG  ARG A 690    17753  14579  14828   -159   2318    268  A    C  
ATOM   5238  CD  ARG A 690     129.515  46.918   4.438  1.00131.61      A    C  
ANISOU 5238  CD  ARG A 690    18384  15716  15904   -113   2302    280  A    C  
ATOM   5239  NE  ARG A 690     129.497  48.246   5.068  1.00143.37      A    N  
ANISOU 5239  NE  ARG A 690    19752  17291  17428    -73   2224    251  A    N  
ATOM   5240  CZ  ARG A 690     129.614  48.483   6.375  1.00146.19      A    C  
ANISOU 5240  CZ  ARG A 690    19863  17797  17882    -41   2211    255  A    C  
ATOM   5241  NH1 ARG A 690     129.774  47.483   7.233  1.00152.26      A    N1+
ANISOU 5241  NH1 ARG A 690    20485  18643  18721    -47   2261    289  A    N1+
ATOM   5242  NH2 ARG A 690     129.583  49.736   6.827  1.00147.87      A    N  
ANISOU 5242  NH2 ARG A 690    19994  18074  18116     -6   2139    223  A    N  
ATOM   5243  N   GLY A 691     126.117  47.695  -0.405  1.00119.80      A    N  
ANISOU 5243  N   GLY A 691    17933  13681  13902   -138   1720    190  A    N  
ATOM   5244  CA  GLY A 691     124.972  48.249  -1.112  1.00125.20      A    C  
ANISOU 5244  CA  GLY A 691    18768  14281  14519    -95   1458    139  A    C  
ATOM   5245  C   GLY A 691     125.183  48.145  -2.621  1.00140.93      A    C  
ANISOU 5245  C   GLY A 691    21178  16024  16345   -163   1451    157  A    C  
ATOM   5246  O   GLY A 691     126.311  47.969  -3.120  1.00130.10      A    O  
ANISOU 5246  O   GLY A 691    19981  14545  14904   -250   1664    193  A    O  
ATOM   5247  N   THR A 692     124.075  48.234  -3.349  1.00160.73      A    N  
ANISOU 5247  N   THR A 692    23845  18432  18791   -127   1204    118  A    N  
ATOM   5248  CA  THR A 692     124.055  48.087  -4.820  1.00151.03      A    C  
ANISOU 5248  CA  THR A 692    23047  16949  17388   -190   1145    132  A    C  
ATOM   5249  C   THR A 692     124.673  46.779  -5.339  1.00144.33      A    C  
ANISOU 5249  C   THR A 692    22341  16026  16468   -288   1375    192  A    C  
ATOM   5250  O   THR A 692     123.946  45.811  -5.597  1.00160.80      A    O  
ANISOU 5250  O   THR A 692    24444  18103  18545   -281   1308    198  A    O  
ATOM   5251  CB  THR A 692     124.698  49.288  -5.532  1.00140.79      A    C  
ANISOU 5251  CB  THR A 692    22046  15475  15970   -233   1120    125  A    C  
ATOM   5252  CG2 THR A 692     123.807  50.543  -5.375  1.00141.35      A    C  
ANISOU 5252  CG2 THR A 692    22070  15550  16084   -124    803     50  A    C  
ATOM   5253  OG1 THR A 692     126.022  49.502  -5.011  1.00126.56      A    O  
ANISOU 5253  OG1 THR A 692    20146  13740  14203   -293   1400    157  A    O  
ATOM   5254  N   SER A 693     125.996  46.739  -5.483  1.00124.24      A    N  
ANISOU 5254  N   SER A 693    19887  13432  13883   -378   1646    224  A    N  
ATOM   5255  CA  SER A 693     126.653  45.579  -6.095  1.00110.85      A    C  
ANISOU 5255  CA  SER A 693    18354  11644  12120   -477   1872    257  A    C  
ATOM   5256  C   SER A 693     128.104  45.545  -5.708  1.00104.89      A    C  
ANISOU 5256  C   SER A 693    17505  10928  11420   -545   2185    263  A    C  
ATOM   5257  O   SER A 693     128.525  46.246  -4.778  1.00102.76      A    O  
ANISOU 5257  O   SER A 693    16987  10792  11264   -503   2220    251  A    O  
ATOM   5258  CB  SER A 693     126.567  45.636  -7.625  1.00107.34      A    C  
ANISOU 5258  CB  SER A 693    18394  10929  11460   -567   1814    258  A    C  
ATOM   5259  OG  SER A 693     125.244  45.514  -8.091  1.00109.66      A    O  
ANISOU 5259  OG  SER A 693    18796  11160  11708   -506   1517    247  A    O  
ATOM   5260  N   THR A 694     128.846  44.687  -6.400  1.00101.68      A    N  
ANISOU 5260  N   THR A 694    17280  10407  10945   -648   2409    267  A    N  
ATOM   5261  CA  THR A 694     130.290  44.700  -6.344  1.00106.99      A    C  
ANISOU 5261  CA  THR A 694    17933  11064  11653   -737   2717    242  A    C  
ATOM   5262  C   THR A 694     130.853  45.263  -7.629  1.00111.58      A    C  
ANISOU 5262  C   THR A 694    18945  11415  12036   -882   2811    217  A    C  
ATOM   5263  O   THR A 694     132.062  45.404  -7.760  1.00110.95      A    O  
ANISOU 5263  O   THR A 694    18899  11295  11963   -985   3078    175  A    O  
ATOM   5264  CB  THR A 694     130.875  43.294  -6.162  1.00107.84      A    C  
ANISOU 5264  CB  THR A 694    17916  11209  11850   -763   2942    236  A    C  
ATOM   5265  CG2 THR A 694     130.435  42.709  -4.794  1.00107.49      A    C  
ANISOU 5265  CG2 THR A 694    17457  11386  11997   -637   2862    264  A    C  
ATOM   5266  OG1 THR A 694     130.484  42.463  -7.276  1.00108.02      A    O  
ANISOU 5266  OG1 THR A 694    18246  11070  11724   -829   2939    245  A    O  
ATOM   5267  N   PHE A 695     129.989  45.570  -8.589  1.00120.11      A    N  
ANISOU 5267  N   PHE A 695    20364  12332  12937   -899   2591    233  A    N  
ATOM   5268  CA  PHE A 695     130.449  46.232  -9.812  1.00130.57      A    C  
ANISOU 5268  CA  PHE A 695    22151  13417  14043  -1048   2644    215  A    C  
ATOM   5269  C   PHE A 695     130.536  47.718  -9.598  1.00131.49      A    C  
ANISOU 5269  C   PHE A 695    22292  13526  14141  -1031   2520    205  A    C  
ATOM   5270  O   PHE A 695     131.621  48.293  -9.536  1.00128.78      A    O  
ANISOU 5270  O   PHE A 695    21963  13168  13796  -1124   2735    176  A    O  
ATOM   5271  CB  PHE A 695     129.523  45.949 -10.994  1.00135.39      A    C  
ANISOU 5271  CB  PHE A 695    23167  13822  14453  -1080   2435    237  A    C  
ATOM   5272  CG  PHE A 695     130.002  44.834 -11.867  1.00143.35      A    C  
ANISOU 5272  CG  PHE A 695    24419  14697  15350  -1213   2665    229  A    C  
ATOM   5273  CD1 PHE A 695     130.801  43.823 -11.334  1.00148.14      A    C  
ANISOU 5273  CD1 PHE A 695    24754  15428  16101  -1229   2962    205  A    C  
ATOM   5274  CD2 PHE A 695     129.659  44.782 -13.207  1.00138.63      A    C  
ANISOU 5274  CD2 PHE A 695    24322  13843  14505  -1320   2575    237  A    C  
ATOM   5275  CE1 PHE A 695     131.258  42.794 -12.123  1.00141.06      A    C  
ANISOU 5275  CE1 PHE A 695    24066  14413  15116  -1348   3181    182  A    C  
ATOM   5276  CE2 PHE A 695     130.111  43.750 -13.999  1.00135.98      A    C  
ANISOU 5276  CE2 PHE A 695    24212  13388  14063  -1450   2801    222  A    C  
ATOM   5277  CZ  PHE A 695     130.910  42.755 -13.452  1.00140.22      A    C  
ANISOU 5277  CZ  PHE A 695    24456  14062  14758  -1462   3111    191  A    C  
ATOM   5278  N   ASP A 696     129.368  48.329  -9.461  1.00133.08      A    N  
ANISOU 5278  N   ASP A 696    22480  13741  14343   -908   2169    219  A    N  
ATOM   5279  CA  ASP A 696     129.283  49.755  -9.236  1.00123.98      A    C  
ANISOU 5279  CA  ASP A 696    21344  12579  13183   -868   2002    205  A    C  
ATOM   5280  C   ASP A 696     129.894  50.130  -7.887  1.00117.94      A    C  
ANISOU 5280  C   ASP A 696    20133  12050  12626   -801   2133    194  A    C  
ATOM   5281  O   ASP A 696     130.569  51.136  -7.778  1.00114.03      A    O  
ANISOU 5281  O   ASP A 696    19677  11534  12114   -845   2192    176  A    O  
ATOM   5282  CB  ASP A 696     127.832  50.223  -9.371  1.00129.60      A    C  
ANISOU 5282  CB  ASP A 696    22105  13255  13879   -736   1583    198  A    C  
ATOM   5283  CG  ASP A 696     126.849  49.343  -8.611  1.00140.09      A    C  
ANISOU 5283  CG  ASP A 696    23077  14775  15375   -598   1469    198  A    C  
ATOM   5284  OD1 ASP A 696     127.258  48.746  -7.588  1.00153.24      A    O  
ANISOU 5284  OD1 ASP A 696    24367  16651  17206   -567   1663    209  A    O  
ATOM   5285  OD2 ASP A 696     125.661  49.269  -9.021  1.00140.43      A    O1-
ANISOU 5285  OD2 ASP A 696    23217  14750  15388   -525   1174    181  A    O1-
ATOM   5286  N   GLY A 697     129.688  49.305  -6.862  1.00117.28      A    N  
ANISOU 5286  N   GLY A 697    19646  12183  12731   -703   2181    203  A    N  
ATOM   5287  CA  GLY A 697     130.299  49.548  -5.551  1.00112.01      A    C  
ANISOU 5287  CA  GLY A 697    18568  11730  12258   -646   2306    195  A    C  
ATOM   5288  C   GLY A 697     131.822  49.673  -5.616  1.00104.52      A    C  
ANISOU 5288  C   GLY A 697    17648  10746  11317   -770   2631    171  A    C  
ATOM   5289  O   GLY A 697     132.407  50.583  -5.051  1.00 89.68      A    O  
ANISOU 5289  O   GLY A 697    15640   8929   9503   -764   2677    153  A    O  
ATOM   5290  N   LEU A 698     132.461  48.722  -6.290  1.00107.94      A    N  
ANISOU 5290  N   LEU A 698    18235  11081  11696   -883   2867    159  A    N  
ATOM   5291  CA  LEU A 698     133.921  48.704  -6.400  1.00109.38      A    C  
ANISOU 5291  CA  LEU A 698    18426  11226  11907  -1012   3205    108  A    C  
ATOM   5292  C   LEU A 698     134.414  49.857  -7.234  1.00110.10      A    C  
ANISOU 5292  C   LEU A 698    18866  11142  11823  -1147   3243     83  A    C  
ATOM   5293  O   LEU A 698     135.483  50.397  -6.974  1.00110.15      A    O  
ANISOU 5293  O   LEU A 698    18796  11167  11887  -1220   3444     37  A    O  
ATOM   5294  CB  LEU A 698     134.409  47.391  -7.026  1.00110.80      A    C  
ANISOU 5294  CB  LEU A 698    18707  11327  12063  -1108   3442     79  A    C  
ATOM   5295  CG  LEU A 698     135.920  47.147  -7.258  1.00103.95      A    C  
ANISOU 5295  CG  LEU A 698    17844  10410  11242  -1255   3825     -8  A    C  
ATOM   5296  CD1 LEU A 698     136.331  47.539  -8.656  1.00101.84      A    C  
ANISOU 5296  CD1 LEU A 698    18063   9901  10729  -1459   3958    -45  A    C  
ATOM   5297  CD2 LEU A 698     136.804  47.800  -6.194  1.00 99.00      A    C  
ANISOU 5297  CD2 LEU A 698    16877   9926  10809  -1218   3929    -48  A    C  
ATOM   5298  N   ALA A 699     133.627  50.222  -8.240  1.00114.35      A    N  
ANISOU 5298  N   ALA A 699    19800  11499  12149  -1183   3036    111  A    N  
ATOM   5299  CA  ALA A 699     133.955  51.353  -9.119  1.00113.60      A    C  
ANISOU 5299  CA  ALA A 699    20110  11202  11849  -1318   3019     96  A    C  
ATOM   5300  C   ALA A 699     134.010  52.660  -8.333  1.00106.74      A    C  
ANISOU 5300  C   ALA A 699    19065  10426  11061  -1240   2890     96  A    C  
ATOM   5301  O   ALA A 699     134.933  53.441  -8.492  1.00 95.92      A    O  
ANISOU 5301  O   ALA A 699    17810   8992   9643  -1360   3048     64  A    O  
ATOM   5302  CB  ALA A 699     132.923  51.458 -10.229  1.00117.23      A    C  
ANISOU 5302  CB  ALA A 699    21009  11450  12083  -1335   2746    131  A    C  
ATOM   5303  N   LEU A 700     133.013  52.857  -7.464  1.00104.21      A    N  
ANISOU 5303  N   LEU A 700    18458  10265  10872  -1044   2613    124  A    N  
ATOM   5304  CA  LEU A 700     132.918  54.026  -6.591  1.00 93.54      A    C  
ANISOU 5304  CA  LEU A 700    16891   9028   9620   -944   2466    119  A    C  
ATOM   5305  C   LEU A 700     134.043  54.010  -5.559  1.00 85.80      A    C  
ANISOU 5305  C   LEU A 700    15544   8223   8830   -951   2734     95  A    C  
ATOM   5306  O   LEU A 700     134.734  54.991  -5.379  1.00 79.17      A    O  
ANISOU 5306  O   LEU A 700    14714   7373   7992  -1000   2798     73  A    O  
ATOM   5307  CB  LEU A 700     131.541  54.048  -5.899  1.00 91.68      A    C  
ANISOU 5307  CB  LEU A 700    16412   8930   9491   -744   2137    134  A    C  
ATOM   5308  CG  LEU A 700     130.327  54.280  -6.815  1.00 93.55      A    C  
ANISOU 5308  CG  LEU A 700    16970   8998   9577   -705   1806    138  A    C  
ATOM   5309  CD1 LEU A 700     129.018  53.844  -6.145  1.00 96.20      A    C  
ANISOU 5309  CD1 LEU A 700    17009   9491  10051   -529   1561    130  A    C  
ATOM   5310  CD2 LEU A 700     130.239  55.730  -7.270  1.00 91.42      A    C  
ANISOU 5310  CD2 LEU A 700    16975   8573   9187   -719   1601    120  A    C  
ATOM   5311  N   ALA A 701     134.215  52.888  -4.872  1.00 85.21      A    N  
ANISOU 5311  N   ALA A 701    15152   8302   8919   -899   2873     96  A    N  
ATOM   5312  CA  ALA A 701     135.238  52.802  -3.842  1.00 87.96      A    C  
ANISOU 5312  CA  ALA A 701    15142   8810   9467   -888   3088     67  A    C  
ATOM   5313  C   ALA A 701     136.602  53.002  -4.465  1.00 92.82      A    C  
ANISOU 5313  C   ALA A 701    15935   9302  10030  -1071   3398      7  A    C  
ATOM   5314  O   ALA A 701     137.536  53.467  -3.804  1.00 92.53      A    O  
ANISOU 5314  O   ALA A 701    15688   9345  10123  -1088   3545    -32  A    O  
ATOM   5315  CB  ALA A 701     135.169  51.476  -3.098  1.00 88.57      A    C  
ANISOU 5315  CB  ALA A 701    14901   9038   9713   -807   3161     77  A    C  
ATOM   5316  N   HIS A 702     136.707  52.659  -5.746  1.00101.08      A    N  
ANISOU 5316  N   HIS A 702    17374  10145  10884  -1219   3498     -7  A    N  
ATOM   5317  CA  HIS A 702     137.937  52.885  -6.512  1.00105.08      A    C  
ANISOU 5317  CA  HIS A 702    18116  10507  11300  -1433   3806    -79  A    C  
ATOM   5318  C   HIS A 702     138.171  54.390  -6.707  1.00103.13      A    C  
ANISOU 5318  C   HIS A 702    18068  10174  10941  -1502   3736    -82  A    C  
ATOM   5319  O   HIS A 702     139.275  54.882  -6.484  1.00100.32      A    O  
ANISOU 5319  O   HIS A 702    17634   9833  10651  -1600   3959   -144  A    O  
ATOM   5320  CB  HIS A 702     137.875  52.127  -7.849  1.00109.26      A    C  
ANISOU 5320  CB  HIS A 702    19051  10834  11627  -1582   3918    -93  A    C  
ATOM   5321  CG  HIS A 702     139.074  52.330  -8.731  1.00118.14      A    C  
ANISOU 5321  CG  HIS A 702    20460  11796  12631  -1833   4253   -181  A    C  
ATOM   5322  CD2 HIS A 702     140.337  52.737  -8.447  1.00118.96      A    C  
ANISOU 5322  CD2 HIS A 702    20430  11931  12836  -1943   4535   -271  A    C  
ATOM   5323  ND1 HIS A 702     139.033  52.125 -10.096  1.00124.90      A    N  
ANISOU 5323  ND1 HIS A 702    21811  12417  13225  -2015   4329   -193  A    N  
ATOM   5324  CE1 HIS A 702     140.215  52.404 -10.616  1.00126.04      A    C  
ANISOU 5324  CE1 HIS A 702    22123  12459  13305  -2239   4659   -289  A    C  
ATOM   5325  NE2 HIS A 702     141.023  52.777  -9.635  1.00125.10      A    N  
ANISOU 5325  NE2 HIS A 702    21616  12503  13414  -2198   4790   -343  A    N  
ATOM   5326  N   ALA A 703     137.107  55.110  -7.068  1.00100.96      A    N  
ANISOU 5326  N   ALA A 703    18031   9813  10515  -1440   3407    -21  A    N  
ATOM   5327  CA  ALA A 703     137.168  56.565  -7.316  1.00 96.32      A    C  
ANISOU 5327  CA  ALA A 703    17678   9117   9800  -1492   3278    -18  A    C  
ATOM   5328  C   ALA A 703     137.424  57.376  -6.025  1.00 92.02      A    C  
ANISOU 5328  C   ALA A 703    16733   8769   9458  -1369   3227    -23  A    C  
ATOM   5329  O   ALA A 703     138.206  58.334  -6.009  1.00 88.53      A    O  
ANISOU 5329  O   ALA A 703    16362   8285   8990  -1465   3324    -54  A    O  
ATOM   5330  CB  ALA A 703     135.873  57.036  -7.995  1.00 94.51      A    C  
ANISOU 5330  CB  ALA A 703    17781   8741   9387  -1427   2893     35  A    C  
ATOM   5331  N   ILE A 704     136.755  56.992  -4.943  1.00 87.26      A    N  
ANISOU 5331  N   ILE A 704    15726   8379   9047  -1166   3075      6  A    N  
ATOM   5332  CA  ILE A 704     136.848  57.753  -3.716  1.00 84.20      A    C  
ANISOU 5332  CA  ILE A 704    14984   8172   8834  -1044   2994      5  A    C  
ATOM   5333  C   ILE A 704     138.283  57.689  -3.200  1.00 83.89      A    C  
ANISOU 5333  C   ILE A 704    14727   8208   8940  -1132   3320    -50  A    C  
ATOM   5334  O   ILE A 704     138.838  58.666  -2.721  1.00 80.31      A    O  
ANISOU 5334  O   ILE A 704    14185   7790   8537  -1143   3340    -71  A    O  
ATOM   5335  CB  ILE A 704     135.844  57.246  -2.679  1.00 83.36      A    C  
ANISOU 5335  CB  ILE A 704    14511   8272   8889   -836   2791     38  A    C  
ATOM   5336  CG1 ILE A 704     134.408  57.487  -3.169  1.00 83.72      A    C  
ANISOU 5336  CG1 ILE A 704    14751   8243   8814   -745   2449     66  A    C  
ATOM   5337  CG2 ILE A 704     136.057  57.953  -1.347  1.00 84.82      A    C  
ANISOU 5337  CG2 ILE A 704    14325   8649   9254   -728   2746     32  A    C  
ATOM   5338  CD1 ILE A 704     133.363  56.625  -2.475  1.00 84.43      A    C  
ANISOU 5338  CD1 ILE A 704    14554   8498   9026   -592   2302     85  A    C  
ATOM   5339  N   ALA A 705     138.902  56.531  -3.312  1.00 87.71      A    N  
ANISOU 5339  N   ALA A 705    15121   8705   9497  -1195   3574    -86  A    N  
ATOM   5340  CA  ALA A 705     140.306  56.431  -2.968  1.00 92.95      A    C  
ANISOU 5340  CA  ALA A 705    15596   9410  10307  -1291   3890   -166  A    C  
ATOM   5341  C   ALA A 705     141.112  57.281  -3.930  1.00 99.27      A    C  
ANISOU 5341  C   ALA A 705    16754  10023  10938  -1508   4062   -220  A    C  
ATOM   5342  O   ALA A 705     142.041  57.963  -3.528  1.00100.91      A    O  
ANISOU 5342  O   ALA A 705    16841  10264  11235  -1569   4202   -275  A    O  
ATOM   5343  CB  ALA A 705     140.749  54.981  -3.017  1.00 96.31      A    C  
ANISOU 5343  CB  ALA A 705    15882   9864  10844  -1314   4112   -213  A    C  
ATOM   5344  N   GLU A 706     140.732  57.243  -5.206  1.00107.99      A    N  
ANISOU 5344  N   GLU A 706    18318  10922  11787  -1634   4042   -205  A    N  
ATOM   5345  CA  GLU A 706     141.359  58.071  -6.242  1.00118.61      A    C  
ANISOU 5345  CA  GLU A 706    20096  12056  12915  -1866   4179   -245  A    C  
ATOM   5346  C   GLU A 706     140.951  59.539  -6.125  1.00112.18      A    C  
ANISOU 5346  C   GLU A 706    19426  11196  12000  -1828   3917   -197  A    C  
ATOM   5347  O   GLU A 706     140.492  60.155  -7.091  1.00114.46      A    O  
ANISOU 5347  O   GLU A 706    20175  11279  12034  -1918   3767   -164  A    O  
ATOM   5348  CB  GLU A 706     140.999  57.553  -7.654  1.00133.26      A    C  
ANISOU 5348  CB  GLU A 706    22441  13686  14506  -2014   4209   -237  A    C  
ATOM   5349  CG  GLU A 706     141.750  56.296  -8.110  1.00142.84      A    C  
ANISOU 5349  CG  GLU A 706    23637  14875  15760  -2147   4563   -321  A    C  
ATOM   5350  CD  GLU A 706     143.240  56.535  -8.344  1.00139.45      A    C  
ANISOU 5350  CD  GLU A 706    23226  14396  15360  -2377   4966   -452  A    C  
ATOM   5351  OE1 GLU A 706     143.671  56.512  -9.511  1.00135.77      A    O  
ANISOU 5351  OE1 GLU A 706    23185  13727  14674  -2624   5173   -507  A    O  
ATOM   5352  OE2 GLU A 706     143.977  56.753  -7.358  1.00139.01      A    O1-
ANISOU 5352  OE2 GLU A 706    22766  14501  15549  -2319   5076   -507  A    O1-
ATOM   5353  N   HIS A 707     141.138  60.097  -4.942  1.00100.63      A    N  
ANISOU 5353  N   HIS A 707    17582   9914  10737  -1697   3854   -196  A    N  
ATOM   5354  CA  HIS A 707     140.692  61.440  -4.675  1.00 90.37      A    C  
ANISOU 5354  CA  HIS A 707    16356   8601   9380  -1627   3588   -155  A    C  
ATOM   5355  C   HIS A 707     141.371  61.902  -3.410  1.00 90.64      A    C  
ANISOU 5355  C   HIS A 707    15957   8828   9652  -1548   3658   -184  A    C  
ATOM   5356  O   HIS A 707     141.998  62.951  -3.384  1.00 89.93      A    O  
ANISOU 5356  O   HIS A 707    15948   8690   9528  -1636   3706   -210  A    O  
ATOM   5357  CB  HIS A 707     139.177  61.499  -4.522  1.00 83.58      A    C  
ANISOU 5357  CB  HIS A 707    15501   7770   8485  -1423   3188    -80  A    C  
ATOM   5358  CG  HIS A 707     138.624  62.846  -4.819  1.00 82.90      A    C  
ANISOU 5358  CG  HIS A 707    15688   7560   8248  -1402   2899    -53  A    C  
ATOM   5359  CD2 HIS A 707     138.788  64.037  -4.203  1.00 84.04      A    C  
ANISOU 5359  CD2 HIS A 707    15735   7754   8444  -1353   2790    -58  A    C  
ATOM   5360  ND1 HIS A 707     137.828  63.095  -5.907  1.00 86.05      A    N  
ANISOU 5360  ND1 HIS A 707    16543   7740   8411  -1439   2672    -24  A    N  
ATOM   5361  CE1 HIS A 707     137.504  64.377  -5.945  1.00 84.93      A    C  
ANISOU 5361  CE1 HIS A 707    16570   7512   8187  -1404   2422    -15  A    C  
ATOM   5362  NE2 HIS A 707     138.085  64.973  -4.927  1.00 84.75      A    N  
ANISOU 5362  NE2 HIS A 707    16217   7652   8331  -1356   2498    -34  A    N  
ATOM   5363  N   LEU A 708     141.242  61.106  -2.351  1.00 92.74      A    N  
ANISOU 5363  N   LEU A 708    15777   9307  10152  -1384   3657   -178  A    N  
ATOM   5364  CA  LEU A 708     141.951  61.362  -1.084  1.00 91.70      A    C  
ANISOU 5364  CA  LEU A 708    15214   9360  10266  -1306   3734   -210  A    C  
ATOM   5365  C   LEU A 708     143.474  61.408  -1.284  1.00 93.30      A    C  
ANISOU 5365  C   LEU A 708    15399   9513  10534  -1498   4095   -312  A    C  
ATOM   5366  O   LEU A 708     144.174  62.143  -0.571  1.00 88.48      A    O  
ANISOU 5366  O   LEU A 708    14589   8978  10052  -1495   4145   -348  A    O  
ATOM   5367  CB  LEU A 708     141.592  60.304  -0.029  1.00 90.54      A    C  
ANISOU 5367  CB  LEU A 708    14649   9416  10335  -1127   3687   -189  A    C  
ATOM   5368  CG  LEU A 708     140.352  60.514   0.854  1.00 87.90      A    C  
ANISOU 5368  CG  LEU A 708    14122   9227  10049   -913   3357   -115  A    C  
ATOM   5369  CD1 LEU A 708     139.242  61.241   0.102  1.00 87.97      A    C  
ANISOU 5369  CD1 LEU A 708    14466   9114   9843   -892   3086    -71  A    C  
ATOM   5370  CD2 LEU A 708     139.863  59.164   1.407  1.00 84.83      A    C  
ANISOU 5370  CD2 LEU A 708    13480   8967   9785   -800   3340    -92  A    C  
ATOM   5371  N   LEU A 709     143.970  60.614  -2.249  1.00 95.05      A    N  
ANISOU 5371  N   LEU A 709    15824   9610  10679  -1665   4350   -371  A    N  
ATOM   5372  CA  LEU A 709     145.393  60.539  -2.532  1.00 91.80      A    C  
ANISOU 5372  CA  LEU A 709    15395   9147  10339  -1865   4722   -499  A    C  
ATOM   5373  C   LEU A 709     145.811  61.738  -3.349  1.00 96.36      A    C  
ANISOU 5373  C   LEU A 709    16364   9548  10699  -2072   4789   -522  A    C  
ATOM   5374  O   LEU A 709     146.810  62.407  -3.045  1.00 92.35      A    O  
ANISOU 5374  O   LEU A 709    15749   9055  10281  -2170   4957   -598  A    O  
ATOM   5375  CB  LEU A 709     145.705  59.255  -3.271  1.00 90.65      A    C  
ANISOU 5375  CB  LEU A 709    15327   8932  10184  -1972   4970   -567  A    C  
ATOM   5376  CG  LEU A 709     145.660  58.011  -2.373  1.00 91.12      A    C  
ANISOU 5376  CG  LEU A 709    14951   9164  10507  -1795   4973   -578  A    C  
ATOM   5377  CD1 LEU A 709     144.938  56.882  -3.086  1.00 93.33      A    C  
ANISOU 5377  CD1 LEU A 709    15407   9379  10674  -1786   4951   -542  A    C  
ATOM   5378  CD2 LEU A 709     147.033  57.528  -1.892  1.00 91.18      A    C  
ANISOU 5378  CD2 LEU A 709    14621   9237  10786  -1850   5282   -729  A    C  
ATOM   5379  N   GLN A 710     145.014  62.030  -4.374  1.00102.71      A    N  
ANISOU 5379  N   GLN A 710    17635  10175  11214  -2138   4634   -454  A    N  
ATOM   5380  CA  GLN A 710     145.360  63.089  -5.338  1.00105.84      A    C  
ANISOU 5380  CA  GLN A 710    18505  10356  11351  -2366   4687   -470  A    C  
ATOM   5381  C   GLN A 710     144.764  64.449  -4.981  1.00103.87      A    C  
ANISOU 5381  C   GLN A 710    18342  10096  11026  -2264   4356   -389  A    C  
ATOM   5382  O   GLN A 710     145.445  65.312  -4.439  1.00102.41      A    O  
ANISOU 5382  O   GLN A 710    18023   9960  10928  -2295   4415   -424  A    O  
ATOM   5383  CB  GLN A 710     144.878  62.669  -6.726  1.00112.18      A    C  
ANISOU 5383  CB  GLN A 710    19825  10934  11861  -2514   4691   -447  A    C  
ATOM   5384  CG  GLN A 710     145.509  61.377  -7.222  1.00115.55      A    C  
ANISOU 5384  CG  GLN A 710    20224  11344  12333  -2646   5041   -540  A    C  
ATOM   5385  CD  GLN A 710     144.665  60.701  -8.263  1.00117.49      A    C  
ANISOU 5385  CD  GLN A 710    20856  11435  12350  -2682   4943   -486  A    C  
ATOM   5386  NE2 GLN A 710     145.295  59.852  -9.066  1.00120.10      A    N  
ANISOU 5386  NE2 GLN A 710    21346  11668  12616  -2883   5274   -577  A    N  
ATOM   5387  OE1 GLN A 710     143.449  60.923  -8.335  1.00115.75      A    O  
ANISOU 5387  OE1 GLN A 710    20776  11181  12020  -2528   4572   -373  A    O  
ATOM   5388  N   LYS A 711     143.467  64.598  -5.247  1.00105.27      A    N  
ANISOU 5388  N   LYS A 711    18718  10216  11064  -2129   4001   -291  A    N  
ATOM   5389  CA  LYS A 711     142.796  65.888  -5.228  1.00107.24      A    C  
ANISOU 5389  CA  LYS A 711    19165  10391  11189  -2056   3665   -230  A    C  
ATOM   5390  C   LYS A 711     142.352  66.414  -3.853  1.00105.56      A    C  
ANISOU 5390  C   LYS A 711    18509  10400  11197  -1801   3430   -198  A    C  
ATOM   5391  O   LYS A 711     141.609  67.405  -3.795  1.00109.70      A    O  
ANISOU 5391  O   LYS A 711    19167  10876  11638  -1703   3110   -153  A    O  
ATOM   5392  CB  LYS A 711     141.629  65.889  -6.227  1.00109.12      A    C  
ANISOU 5392  CB  LYS A 711    19847  10435  11176  -2038   3373   -164  A    C  
ATOM   5393  CG  LYS A 711     142.096  66.139  -7.664  1.00116.14      A    C  
ANISOU 5393  CG  LYS A 711    21347  11027  11753  -2334   3515   -185  A    C  
ATOM   5394  CD  LYS A 711     142.349  67.629  -7.908  1.00124.91      A    C  
ANISOU 5394  CD  LYS A 711    22772  11984  12704  -2438   3397   -180  A    C  
ATOM   5395  CE  LYS A 711     143.669  67.921  -8.614  1.00132.34      A    C  
ANISOU 5395  CE  LYS A 711    24011  12774  13498  -2777   3780   -254  A    C  
ATOM   5396  NZ  LYS A 711     143.775  67.212  -9.917  1.00140.18      A    N1+
ANISOU 5396  NZ  LYS A 711    25467  13550  14245  -3008   3956   -274  A    N1+
ATOM   5397  N   ASN A 712     142.793  65.779  -2.762  1.00 97.75      A    N  
ANISOU 5397  N   ASN A 712    17015   9641  10483  -1696   3574   -226  A    N  
ATOM   5398  CA  ASN A 712     142.756  66.439  -1.434  1.00 94.06      A    C  
ANISOU 5398  CA  ASN A 712    16154   9368  10216  -1520   3435   -214  A    C  
ATOM   5399  C   ASN A 712     143.625  65.728  -0.456  1.00 91.95      A    C  
ANISOU 5399  C   ASN A 712    15422   9291  10221  -1486   3673   -266  A    C  
ATOM   5400  O   ASN A 712     143.140  65.045   0.400  1.00 97.31      A    O  
ANISOU 5400  O   ASN A 712    15765  10142  11065  -1307   3580   -240  A    O  
ATOM   5401  CB  ASN A 712     141.327  66.610  -0.847  1.00 89.29      A    C  
ANISOU 5401  CB  ASN A 712    15419   8865   9642  -1269   3046   -147  A    C  
ATOM   5402  CG  ASN A 712     140.435  65.405  -1.060  1.00 86.91      A    C  
ANISOU 5402  CG  ASN A 712    15085   8596   9340  -1179   2972   -116  A    C  
ATOM   5403  ND2 ASN A 712     139.124  65.617  -1.086  1.00 82.86      A    N  
ANISOU 5403  ND2 ASN A 712    14635   8078   8767  -1027   2639    -75  A    N  
ATOM   5404  OD1 ASN A 712     140.915  64.298  -1.212  1.00 96.50      A    O  
ANISOU 5404  OD1 ASN A 712    16216   9834  10613  -1244   3209   -138  A    O  
ATOM   5405  N   LYS A 713     144.922  65.902  -0.597  1.00 95.88      A    N  
ANISOU 5405  N   LYS A 713    15913   9747  10768  -1665   3975   -350  A    N  
ATOM   5406  CA  LYS A 713     145.921  65.067   0.078  1.00100.62      A    C  
ANISOU 5406  CA  LYS A 713    16120  10481  11628  -1672   4245   -431  A    C  
ATOM   5407  C   LYS A 713     145.721  64.821   1.576  1.00100.45      A    C  
ANISOU 5407  C   LYS A 713    15604  10694  11869  -1438   4106   -405  A    C  
ATOM   5408  O   LYS A 713     146.538  65.242   2.395  1.00105.93      A    O  
ANISOU 5408  O   LYS A 713    16028  11478  12742  -1427   4185   -454  A    O  
ATOM   5409  CB  LYS A 713     147.304  65.676  -0.139  1.00104.73      A    C  
ANISOU 5409  CB  LYS A 713    16680  10931  12180  -1885   4536   -540  A    C  
ATOM   5410  CG  LYS A 713     147.615  65.986  -1.601  1.00108.82      A    C  
ANISOU 5410  CG  LYS A 713    17717  11207  12420  -2157   4707   -576  A    C  
ATOM   5411  CD  LYS A 713     149.098  66.206  -1.802  1.00111.90      A    C  
ANISOU 5411  CD  LYS A 713    18080  11549  12886  -2393   5083   -719  A    C  
ATOM   5412  CE  LYS A 713     149.480  66.074  -3.259  1.00114.02      A    C  
ANISOU 5412  CE  LYS A 713    18826  11592  12902  -2688   5334   -781  A    C  
ATOM   5413  NZ  LYS A 713     150.874  65.573  -3.335  1.00117.73      A    N1+
ANISOU 5413  NZ  LYS A 713    19110  12075  13546  -2876   5766   -961  A    N1+
ATOM   5414  N   SER A 714     144.675  64.080   1.922  1.00 98.18      A    N  
ANISOU 5414  N   SER A 714    15201  10497  11603  -1266   3913   -335  A    N  
ATOM   5415  CA  SER A 714     144.290  63.894   3.306  1.00 93.27      A    C  
ANISOU 5415  CA  SER A 714    14174  10082  11181  -1056   3747   -297  A    C  
ATOM   5416  C   SER A 714     144.819  62.590   3.843  1.00 95.12      A    C  
ANISOU 5416  C   SER A 714    14098  10412  11627  -1018   3911   -340  A    C  
ATOM   5417  O   SER A 714     144.832  61.577   3.164  1.00106.84      A    O  
ANISOU 5417  O   SER A 714    15679  11834  13079  -1078   4041   -362  A    O  
ATOM   5418  CB  SER A 714     142.765  63.902   3.428  1.00 93.25      A    C  
ANISOU 5418  CB  SER A 714    14227  10127  11078   -897   3430   -206  A    C  
ATOM   5419  OG  SER A 714     142.212  65.124   2.962  1.00 97.39      A    O  
ANISOU 5419  OG  SER A 714    15027  10552  11422   -908   3236   -178  A    O  
ATOM   5420  N   PHE A 715     145.225  62.610   5.096  1.00 97.36      A    N  
ANISOU 5420  N   PHE A 715    14014  10846  12130   -910   3882   -353  A    N  
ATOM   5421  CA  PHE A 715     145.618  61.391   5.800  1.00 91.90      A    C  
ANISOU 5421  CA  PHE A 715    13008  10250  11658   -837   3965   -386  A    C  
ATOM   5422  C   PHE A 715     144.377  60.578   6.010  1.00 84.94      A    C  
ANISOU 5422  C   PHE A 715    12108   9439  10725   -706   3773   -298  A    C  
ATOM   5423  O   PHE A 715     143.490  60.986   6.775  1.00 90.82      A    O  
ANISOU 5423  O   PHE A 715    12761  10291  11454   -574   3533   -225  A    O  
ATOM   5424  CB  PHE A 715     146.226  61.755   7.150  1.00 92.97      A    C  
ANISOU 5424  CB  PHE A 715    12792  10515  12016   -744   3918   -409  A    C  
ATOM   5425  CG  PHE A 715     147.600  62.343   7.035  1.00 95.45      A    C  
ANISOU 5425  CG  PHE A 715    13057  10771  12438   -874   4137   -520  A    C  
ATOM   5426  CD1 PHE A 715     147.821  63.479   6.260  1.00 94.30      A    C  
ANISOU 5426  CD1 PHE A 715    13182  10516  12131  -1014   4198   -536  A    C  
ATOM   5427  CD2 PHE A 715     148.667  61.747   7.680  1.00 94.96      A    C  
ANISOU 5427  CD2 PHE A 715    12686  10751  12643   -862   4275   -618  A    C  
ATOM   5428  CE1 PHE A 715     149.082  63.999   6.132  1.00 96.63      A    C  
ANISOU 5428  CE1 PHE A 715    13437  10756  12522  -1153   4418   -648  A    C  
ATOM   5429  CE2 PHE A 715     149.932  62.270   7.565  1.00 97.56      A    C  
ANISOU 5429  CE2 PHE A 715    12949  11027  13091   -985   4483   -742  A    C  
ATOM   5430  CZ  PHE A 715     150.141  63.396   6.785  1.00 98.85      A    C  
ANISOU 5430  CZ  PHE A 715    13381  11093  13085  -1141   4568   -757  A    C  
ATOM   5431  N   SER A 716     144.295  59.442   5.337  1.00 78.55      A    N  
ANISOU 5431  N   SER A 716    11386   8568   9889   -748   3883   -313  A    N  
ATOM   5432  CA  SER A 716     143.062  58.674   5.351  1.00 77.72      A    C  
ANISOU 5432  CA  SER A 716    11314   8509   9706   -646   3708   -231  A    C  
ATOM   5433  C   SER A 716     143.241  57.231   5.773  1.00 75.97      A    C  
ANISOU 5433  C   SER A 716    10883   8341   9639   -592   3778   -247  A    C  
ATOM   5434  O   SER A 716     144.210  56.604   5.388  1.00 75.62      A    O  
ANISOU 5434  O   SER A 716    10812   8229   9691   -677   4006   -335  A    O  
ATOM   5435  CB  SER A 716     142.454  58.717   3.967  1.00 78.17      A    C  
ANISOU 5435  CB  SER A 716    11762   8415   9522   -741   3709   -210  A    C  
ATOM   5436  OG  SER A 716     142.488  60.050   3.508  1.00 80.05      A    O  
ANISOU 5436  OG  SER A 716    12221   8570   9622   -812   3662   -210  A    O  
ATOM   5437  N   LEU A 717     142.303  56.709   6.562  1.00 75.35      A    N  
ANISOU 5437  N   LEU A 717    10664   8380   9586   -457   3580   -172  A    N  
ATOM   5438  CA  LEU A 717     142.232  55.259   6.794  1.00 77.23      A    C  
ANISOU 5438  CA  LEU A 717    10780   8645   9918   -412   3612   -170  A    C  
ATOM   5439  C   LEU A 717     141.019  54.709   6.032  1.00 80.65      A    C  
ANISOU 5439  C   LEU A 717    11434   9041  10169   -408   3515   -106  A    C  
ATOM   5440  O   LEU A 717     139.877  55.107   6.251  1.00 84.53      A    O  
ANISOU 5440  O   LEU A 717    11964   9596  10558   -339   3304    -39  A    O  
ATOM   5441  CB  LEU A 717     142.176  54.902   8.281  1.00 73.88      A    C  
ANISOU 5441  CB  LEU A 717    10041   8366   9663   -284   3478   -140  A    C  
ATOM   5442  CG  LEU A 717     143.105  55.674   9.222  1.00 73.88      A    C  
ANISOU 5442  CG  LEU A 717     9823   8421   9825   -259   3488   -182  A    C  
ATOM   5443  CD1 LEU A 717     143.201  55.012  10.582  1.00 75.18      A    C  
ANISOU 5443  CD1 LEU A 717     9712   8691  10163   -151   3377   -163  A    C  
ATOM   5444  CD2 LEU A 717     144.485  55.810   8.677  1.00 76.18      A    C  
ANISOU 5444  CD2 LEU A 717    10108   8611  10224   -364   3732   -298  A    C  
ATOM   5445  N   PHE A 718     141.291  53.795   5.116  1.00 84.66      A    N  
ANISOU 5445  N   PHE A 718    12079   9441  10645   -486   3675   -143  A    N  
ATOM   5446  CA  PHE A 718     140.301  53.314   4.180  1.00 84.89      A    C  
ANISOU 5446  CA  PHE A 718    12362   9398  10491   -508   3612    -96  A    C  
ATOM   5447  C   PHE A 718     140.193  51.810   4.359  1.00 87.40      A    C  
ANISOU 5447  C   PHE A 718    12574   9739  10894   -467   3647    -92  A    C  
ATOM   5448  O   PHE A 718     141.070  51.067   3.904  1.00 92.72      A    O  
ANISOU 5448  O   PHE A 718    13253  10333  11643   -536   3857   -167  A    O  
ATOM   5449  CB  PHE A 718     140.790  53.658   2.777  1.00 84.82      A    C  
ANISOU 5449  CB  PHE A 718    12681   9211  10336   -667   3790   -149  A    C  
ATOM   5450  CG  PHE A 718     139.718  53.695   1.755  1.00 85.50      A    C  
ANISOU 5450  CG  PHE A 718    13094   9200  10192   -696   3669    -96  A    C  
ATOM   5451  CD1 PHE A 718     139.281  52.533   1.164  1.00 89.38      A    C  
ANISOU 5451  CD1 PHE A 718    13693   9638  10627   -708   3695    -82  A    C  
ATOM   5452  CD2 PHE A 718     139.159  54.891   1.364  1.00 85.85      A    C  
ANISOU 5452  CD2 PHE A 718    13347   9193  10079   -708   3514    -65  A    C  
ATOM   5453  CE1 PHE A 718     138.279  52.553   0.219  1.00 92.06      A    C  
ANISOU 5453  CE1 PHE A 718    14341   9878  10761   -731   3564    -36  A    C  
ATOM   5454  CE2 PHE A 718     138.153  54.926   0.420  1.00 87.17      A    C  
ANISOU 5454  CE2 PHE A 718    13822   9252  10045   -724   3369    -24  A    C  
ATOM   5455  CZ  PHE A 718     137.716  53.755  -0.156  1.00 90.62      A    C  
ANISOU 5455  CZ  PHE A 718    14361   9639  10431   -737   3394    -10  A    C  
ATOM   5456  N   ALA A 719     139.146  51.356   5.050  1.00 85.99      A    N  
ANISOU 5456  N   ALA A 719    12292   9669  10712   -361   3446    -17  A    N  
ATOM   5457  CA  ALA A 719     138.905  49.910   5.218  1.00 87.30      A    C  
ANISOU 5457  CA  ALA A 719    12385   9850  10935   -324   3451     -1  A    C  
ATOM   5458  C   ALA A 719     137.905  49.472   4.174  1.00 86.45      A    C  
ANISOU 5458  C   ALA A 719    12540   9664  10641   -358   3397     38  A    C  
ATOM   5459  O   ALA A 719     136.985  50.239   3.813  1.00 82.14      A    O  
ANISOU 5459  O   ALA A 719    12145   9114   9947   -352   3248     77  A    O  
ATOM   5460  CB  ALA A 719     138.393  49.569   6.620  1.00 92.93      A    C  
ANISOU 5460  CB  ALA A 719    12843  10717  11747   -211   3276     54  A    C  
ATOM   5461  N   THR A 720     138.102  48.251   3.678  1.00 88.60      A    N  
ANISOU 5461  N   THR A 720    12867   9867  10931   -389   3511     19  A    N  
ATOM   5462  CA  THR A 720     137.311  47.730   2.564  1.00 91.99      A    C  
ANISOU 5462  CA  THR A 720    13568  10197  11186   -435   3489     46  A    C  
ATOM   5463  C   THR A 720     137.490  46.231   2.358  1.00 95.65      A    C  
ANISOU 5463  C   THR A 720    14018  10619  11707   -442   3588     29  A    C  
ATOM   5464  O   THR A 720     138.567  45.666   2.607  1.00 92.46      A    O  
ANISOU 5464  O   THR A 720    13470  10196  11463   -453   3755    -41  A    O  
ATOM   5465  CB  THR A 720     137.664  48.420   1.236  1.00 90.25      A    C  
ANISOU 5465  CB  THR A 720    13665   9814  10809   -562   3611      3  A    C  
ATOM   5466  CG2 THR A 720     139.102  48.169   0.881  1.00 85.97      A    C  
ANISOU 5466  CG2 THR A 720    13110   9189  10365   -661   3902    -99  A    C  
ATOM   5467  OG1 THR A 720     136.819  47.912   0.199  1.00 97.66      A    O  
ANISOU 5467  OG1 THR A 720    14880  10650  11573   -601   3556     35  A    O  
ATOM   5468  N   HIS A 721     136.410  45.599   1.907  1.00 99.23      A    N  
ANISOU 5468  N   HIS A 721    14613  11052  12037   -431   3473     85  A    N  
ATOM   5469  CA  HIS A 721     136.445  44.190   1.600  1.00106.55      A    C  
ANISOU 5469  CA  HIS A 721    15565  11927  12990   -439   3549     76  A    C  
ATOM   5470  C   HIS A 721     136.843  43.952   0.129  1.00104.69      A    C  
ANISOU 5470  C   HIS A 721    15633  11512  12631   -561   3734     22  A    C  
ATOM   5471  O   HIS A 721     137.194  42.825  -0.257  1.00 99.98      A    O  
ANISOU 5471  O   HIS A 721    15067  10847  12072   -590   3862    -16  A    O  
ATOM   5472  CB  HIS A 721     135.109  43.538   1.971  1.00109.63      A    C  
ANISOU 5472  CB  HIS A 721    15933  12394  13325   -371   3336    160  A    C  
ATOM   5473  CG  HIS A 721     135.056  43.075   3.390  1.00116.33      A    C  
ANISOU 5473  CG  HIS A 721    16488  13385  14324   -284   3243    191  A    C  
ATOM   5474  CD2 HIS A 721     135.665  42.039   4.014  1.00120.11      A    C  
ANISOU 5474  CD2 HIS A 721    16806  13875  14953   -251   3301    173  A    C  
ATOM   5475  ND1 HIS A 721     134.332  43.734   4.359  1.00132.56      A    N  
ANISOU 5475  ND1 HIS A 721    18401  15581  16383   -224   3063    238  A    N  
ATOM   5476  CE1 HIS A 721     134.483  43.117   5.517  1.00137.64      A    C  
ANISOU 5476  CE1 HIS A 721    18829  16316  17154   -171   3019    258  A    C  
ATOM   5477  NE2 HIS A 721     135.289  42.086   5.336  1.00139.35      A    N  
ANISOU 5477  NE2 HIS A 721    19032  16450  17462   -181   3147    222  A    N  
ATOM   5478  N   TYR A 722     136.796  45.024  -0.667  1.00105.26      A    N  
ANISOU 5478  N   TYR A 722    15941  11500  12553   -639   3743     15  A    N  
ATOM   5479  CA  TYR A 722     137.181  44.968  -2.087  1.00105.16      A    C  
ANISOU 5479  CA  TYR A 722    16265  11301  12387   -782   3918    -36  A    C  
ATOM   5480  C   TYR A 722     138.665  44.683  -2.201  1.00109.56      A    C  
ANISOU 5480  C   TYR A 722    16741  11807  13077   -868   4225   -156  A    C  
ATOM   5481  O   TYR A 722     139.468  45.596  -2.089  1.00105.92      A    O  
ANISOU 5481  O   TYR A 722    16240  11345  12661   -920   4333   -211  A    O  
ATOM   5482  CB  TYR A 722     136.863  46.281  -2.836  1.00 96.21      A    C  
ANISOU 5482  CB  TYR A 722    15419  10076  11060   -854   3842    -18  A    C  
ATOM   5483  CG  TYR A 722     135.390  46.592  -2.946  1.00 98.41      A    C  
ANISOU 5483  CG  TYR A 722    15816  10370  11205   -779   3537     70  A    C  
ATOM   5484  CD1 TYR A 722     134.466  45.584  -3.217  1.00109.73      A    C  
ANISOU 5484  CD1 TYR A 722    17311  11791  12587   -740   3427    112  A    C  
ATOM   5485  CD2 TYR A 722     134.906  47.877  -2.762  1.00 96.13      A    C  
ANISOU 5485  CD2 TYR A 722    15559  10107  10858   -742   3352     96  A    C  
ATOM   5486  CE1 TYR A 722     133.100  45.846  -3.283  1.00111.76      A    C  
ANISOU 5486  CE1 TYR A 722    17643  12069  12751   -668   3144    171  A    C  
ATOM   5487  CE2 TYR A 722     133.541  48.154  -2.840  1.00 98.08      A    C  
ANISOU 5487  CE2 TYR A 722    15882  10368  11016   -662   3063    149  A    C  
ATOM   5488  CZ  TYR A 722     132.641  47.128  -3.096  1.00104.60      A    C  
ANISOU 5488  CZ  TYR A 722    16751  11188  11803   -627   2963    181  A    C  
ATOM   5489  OH  TYR A 722     131.279  47.337  -3.170  1.00103.47      A    O  
ANISOU 5489  OH  TYR A 722    16655  11061  11595   -551   2681    213  A    O  
ATOM   5490  N   PHE A 723     139.027  43.413  -2.397  1.00111.15      A    N  
ANISOU 5490  N   PHE A 723    16904  11969  13357   -878   4362   -206  A    N  
ATOM   5491  CA  PHE A 723     140.433  43.030  -2.475  1.00109.24      A    C  
ANISOU 5491  CA  PHE A 723    16544  11681  13279   -949   4654   -351  A    C  
ATOM   5492  C   PHE A 723     141.068  43.678  -3.707  1.00112.36      A    C  
ANISOU 5492  C   PHE A 723    17250  11920  13521  -1142   4887   -435  A    C  
ATOM   5493  O   PHE A 723     142.293  43.866  -3.783  1.00105.59      A    O  
ANISOU 5493  O   PHE A 723    16306  11029  12782  -1232   5142   -570  A    O  
ATOM   5494  CB  PHE A 723     140.594  41.499  -2.507  1.00110.58      A    C  
ANISOU 5494  CB  PHE A 723    16630  11826  13558   -916   4732   -397  A    C  
ATOM   5495  CG  PHE A 723     142.018  41.038  -2.296  1.00115.71      A    C  
ANISOU 5495  CG  PHE A 723    17059  12455  14449   -943   4988   -565  A    C  
ATOM   5496  CD1 PHE A 723     142.494  40.777  -1.016  1.00113.92      A    C  
ANISOU 5496  CD1 PHE A 723    16457  12340  14486   -811   4916   -591  A    C  
ATOM   5497  CD2 PHE A 723     142.895  40.888  -3.377  1.00117.36      A    C  
ANISOU 5497  CD2 PHE A 723    17440  12525  14625  -1107   5299   -710  A    C  
ATOM   5498  CE1 PHE A 723     143.806  40.364  -0.818  1.00117.30      A    C  
ANISOU 5498  CE1 PHE A 723    16666  12739  15163   -823   5127   -765  A    C  
ATOM   5499  CE2 PHE A 723     144.206  40.481  -3.179  1.00115.78      A    C  
ANISOU 5499  CE2 PHE A 723    17007  12309  14672  -1133   5539   -894  A    C  
ATOM   5500  CZ  PHE A 723     144.665  40.222  -1.896  1.00116.14      A    C  
ANISOU 5500  CZ  PHE A 723    16659  12464  15003   -982   5443   -925  A    C  
ATOM   5501  N   GLU A 724     140.212  44.022  -4.667  1.00114.89      A    N  
ANISOU 5501  N   GLU A 724    17939  12138  13573  -1211   4790   -360  A    N  
ATOM   5502  CA  GLU A 724     140.640  44.641  -5.920  1.00116.74      A    C  
ANISOU 5502  CA  GLU A 724    18553  12198  13604  -1413   4975   -418  A    C  
ATOM   5503  C   GLU A 724     141.308  45.987  -5.679  1.00117.23      A    C  
ANISOU 5503  C   GLU A 724    18583  12275  13683  -1473   5034   -455  A    C  
ATOM   5504  O   GLU A 724     141.850  46.566  -6.587  1.00118.32      A    O  
ANISOU 5504  O   GLU A 724    19006  12274  13674  -1656   5217   -519  A    O  
ATOM   5505  CB  GLU A 724     139.437  44.828  -6.857  1.00120.77      A    C  
ANISOU 5505  CB  GLU A 724    19467  12593  13828  -1445   4773   -311  A    C  
ATOM   5506  CG  GLU A 724     138.873  43.545  -7.464  1.00125.22      A    C  
ANISOU 5506  CG  GLU A 724    20172  13088  14318  -1443   4765   -292  A    C  
ATOM   5507  CD  GLU A 724     137.938  42.785  -6.540  1.00130.11      A    C  
ANISOU 5507  CD  GLU A 724    20521  13855  15059  -1247   4519   -202  A    C  
ATOM   5508  OE1 GLU A 724     137.910  43.058  -5.312  1.00130.96      A    O  
ANISOU 5508  OE1 GLU A 724    20282  14132  15346  -1114   4402   -172  A    O  
ATOM   5509  OE2 GLU A 724     137.228  41.900  -7.052  1.00136.95      A    O1-
ANISOU 5509  OE2 GLU A 724    21537  14664  15832  -1237   4446   -161  A    O1-
ATOM   5510  N   LEU A 725     141.239  46.492  -4.449  1.00128.69      A    N  
ANISOU 5510  N   LEU A 725    19705  13889  15301  -1327   4876   -413  A    N  
ATOM   5511  CA  LEU A 725     141.831  47.792  -4.093  1.00125.89      A    C  
ANISOU 5511  CA  LEU A 725    19290  13563  14979  -1366   4905   -439  A    C  
ATOM   5512  C   LEU A 725     143.189  47.608  -3.435  1.00127.44      A    C  
ANISOU 5512  C   LEU A 725    19150  13823  15445  -1377   5143   -576  A    C  
ATOM   5513  O   LEU A 725     143.827  48.571  -3.023  1.00119.27      A    O  
ANISOU 5513  O   LEU A 725    18007  12825  14483  -1404   5191   -616  A    O  
ATOM   5514  CB  LEU A 725     140.904  48.564  -3.141  1.00121.79      A    C  
ANISOU 5514  CB  LEU A 725    18622  13181  14471  -1201   4575   -316  A    C  
ATOM   5515  CG  LEU A 725     139.679  49.229  -3.772  1.00124.90      A    C  
ANISOU 5515  CG  LEU A 725    19339  13502  14613  -1198   4325   -211  A    C  
ATOM   5516  CD1 LEU A 725     138.826  49.938  -2.723  1.00126.21      A    C  
ANISOU 5516  CD1 LEU A 725    19298  13821  14835  -1029   4023   -123  A    C  
ATOM   5517  CD2 LEU A 725     140.096  50.188  -4.865  1.00123.44      A    C  
ANISOU 5517  CD2 LEU A 725    19541  13139  14220  -1383   4436   -249  A    C  
ATOM   5518  N   THR A 726     143.607  46.358  -3.297  1.00132.37      A    N  
ANISOU 5518  N   THR A 726    19599  14460  16235  -1345   5270   -652  A    N  
ATOM   5519  CA  THR A 726     144.888  46.058  -2.705  1.00135.19      A    C  
ANISOU 5519  CA  THR A 726    19625  14862  16876  -1344   5477   -805  A    C  
ATOM   5520  C   THR A 726     146.007  46.648  -3.569  1.00143.55      A    C  
ANISOU 5520  C   THR A 726    20844  15802  17895  -1566   5810   -961  A    C  
ATOM   5521  O   THR A 726     147.056  47.029  -3.058  1.00138.72      A    O  
ANISOU 5521  O   THR A 726    19985  15232  17490  -1587   5955  -1082  A    O  
ATOM   5522  CB  THR A 726     145.039  44.536  -2.544  1.00134.32      A    C  
ANISOU 5522  CB  THR A 726    19345  14757  16930  -1269   5532   -865  A    C  
ATOM   5523  CG2 THR A 726     146.445  44.164  -2.146  1.00137.27      A    C  
ANISOU 5523  CG2 THR A 726    19408  15139  17607  -1285   5769  -1064  A    C  
ATOM   5524  OG1 THR A 726     144.121  44.073  -1.548  1.00137.12      A    O  
ANISOU 5524  OG1 THR A 726    19516  15235  17346  -1071   5227   -729  A    O  
ATOM   5525  N   TYR A 727     145.754  46.747  -4.870  1.00152.01      A    N  
ANISOU 5525  N   TYR A 727    22342  16720  18695  -1741   5923   -958  A    N  
ATOM   5526  CA  TYR A 727     146.760  47.157  -5.854  1.00160.06      A    C  
ANISOU 5526  CA  TYR A 727    23582  17601  19631  -1995   6272  -1114  A    C  
ATOM   5527  C   TYR A 727     147.193  48.647  -5.808  1.00149.92      A    C  
ANISOU 5527  C   TYR A 727    22376  16305  18280  -2098   6302  -1120  A    C  
ATOM   5528  O   TYR A 727     147.931  49.108  -6.684  1.00158.66      A    O  
ANISOU 5528  O   TYR A 727    23727  17284  19269  -2336   6581  -1235  A    O  
ATOM   5529  CB  TYR A 727     146.210  46.868  -7.257  1.00176.23      A    C  
ANISOU 5529  CB  TYR A 727    26127  19472  21359  -2155   6337  -1082  A    C  
ATOM   5530  CG  TYR A 727     145.337  47.998  -7.788  1.00190.45      A    C  
ANISOU 5530  CG  TYR A 727    28324  21192  22847  -2209   6124   -932  A    C  
ATOM   5531  CD1 TYR A 727     144.147  48.325  -7.151  1.00194.54      A    C  
ANISOU 5531  CD1 TYR A 727    28785  21803  23328  -2008   5732   -753  A    C  
ATOM   5532  CD2 TYR A 727     145.714  48.756  -8.904  1.00195.03      A    C  
ANISOU 5532  CD2 TYR A 727    29335  21594  23175  -2465   6307   -982  A    C  
ATOM   5533  CE1 TYR A 727     143.344  49.357  -7.607  1.00198.89      A    C  
ANISOU 5533  CE1 TYR A 727    29672  22273  23622  -2037   5513   -635  A    C  
ATOM   5534  CE2 TYR A 727     144.916  49.794  -9.369  1.00197.65      A    C  
ANISOU 5534  CE2 TYR A 727    30038  21831  23229  -2500   6075   -849  A    C  
ATOM   5535  CZ  TYR A 727     143.727  50.087  -8.715  1.00205.77      A    C  
ANISOU 5535  CZ  TYR A 727    30977  22955  24249  -2275   5669   -680  A    C  
ATOM   5536  OH  TYR A 727     142.894  51.102  -9.146  1.00220.59      A    O  
ANISOU 5536  OH  TYR A 727    33198  24737  25879  -2287   5408   -564  A    O  
ATOM   5537  N   LEU A 728     146.731  49.411  -4.823  1.00132.46      A    N  
ANISOU 5537  N   LEU A 728    19982  14219  16127  -1936   6025  -1002  A    N  
ATOM   5538  CA  LEU A 728     146.960  50.869  -4.836  1.00119.90      A    C  
ANISOU 5538  CA  LEU A 728    18514  12607  14436  -2024   6009   -983  A    C  
ATOM   5539  C   LEU A 728     148.362  51.277  -4.440  1.00117.18      A    C  
ANISOU 5539  C   LEU A 728    17911  12294  14314  -2114   6272  -1156  A    C  
ATOM   5540  O   LEU A 728     148.897  52.203  -5.003  1.00118.01      A    O  
ANISOU 5540  O   LEU A 728    18234  12308  14297  -2306   6433  -1213  A    O  
ATOM   5541  CB  LEU A 728     145.954  51.611  -3.953  1.00112.62      A    C  
ANISOU 5541  CB  LEU A 728    17496  11802  13491  -1826   5623   -808  A    C  
ATOM   5542  CG  LEU A 728     144.554  51.720  -4.546  1.00111.09      A    C  
ANISOU 5542  CG  LEU A 728    17646  11542  13021  -1787   5351   -651  A    C  
ATOM   5543  CD1 LEU A 728     143.656  52.491  -3.602  1.00109.05      A    C  
ANISOU 5543  CD1 LEU A 728    17243  11412  12780  -1596   4999   -517  A    C  
ATOM   5544  CD2 LEU A 728     144.559  52.336  -5.928  1.00110.10      A    C  
ANISOU 5544  CD2 LEU A 728    18042  11205  12586  -2014   5453   -662  A    C  
ATOM   5545  N   PRO A 729     148.959  50.608  -3.452  1.00122.37      A    N  
ANISOU 5545  N   PRO A 729    18111  13076  15307  -1978   6305  -1243  A    N  
ATOM   5546  CA  PRO A 729     150.332  50.980  -3.143  1.00122.76      A    C  
ANISOU 5546  CA  PRO A 729    17914  13142  15587  -2071   6562  -1432  A    C  
ATOM   5547  C   PRO A 729     151.267  50.787  -4.324  1.00121.67      A    C  
ANISOU 5547  C   PRO A 729    17987  12855  15386  -2349   6979  -1630  A    C  
ATOM   5548  O   PRO A 729     152.340  51.382  -4.350  1.00119.57      A    O  
ANISOU 5548  O   PRO A 729    17632  12570  15227  -2495   7221  -1789  A    O  
ATOM   5549  CB  PRO A 729     150.698  50.040  -1.991  1.00128.97      A    C  
ANISOU 5549  CB  PRO A 729    18209  14057  16737  -1863   6494  -1495  A    C  
ATOM   5550  CG  PRO A 729     149.399  49.733  -1.317  1.00133.52      A    C  
ANISOU 5550  CG  PRO A 729    18753  14727  17250  -1638   6114  -1280  A    C  
ATOM   5551  CD  PRO A 729     148.390  49.698  -2.438  1.00132.48      A    C  
ANISOU 5551  CD  PRO A 729    19075  14488  16770  -1726   6066  -1164  A    C  
ATOM   5552  N   GLU A 730     150.855  49.960  -5.279  1.00127.15      A    N  
ANISOU 5552  N   GLU A 730    18958  13443  15908  -2429   7065  -1627  A    N  
ATOM   5553  CA  GLU A 730     151.607  49.736  -6.512  1.00140.20      A    C  
ANISOU 5553  CA  GLU A 730    20880  14940  17449  -2715   7463  -1808  A    C  
ATOM   5554  C   GLU A 730     150.996  50.578  -7.636  1.00142.12      A    C  
ANISOU 5554  C   GLU A 730    21707  15025  17264  -2912   7443  -1693  A    C  
ATOM   5555  O   GLU A 730     150.783  50.095  -8.740  1.00165.46      A    O  
ANISOU 5555  O   GLU A 730    25032  17839  19996  -3069   7580  -1712  A    O  
ATOM   5556  CB  GLU A 730     151.572  48.245  -6.893  1.00144.64      A    C  
ANISOU 5556  CB  GLU A 730    21401  15470  18085  -2689   7579  -1889  A    C  
ATOM   5557  CG  GLU A 730     151.962  47.290  -5.776  1.00151.06      A    C  
ANISOU 5557  CG  GLU A 730    21676  16420  19299  -2460   7517  -1972  A    C  
ATOM   5558  CD  GLU A 730     151.385  45.892  -5.950  1.00159.16      A    C  
ANISOU 5558  CD  GLU A 730    22701  17431  20338  -2348   7448  -1943  A    C  
ATOM   5559  OE1 GLU A 730     151.959  44.939  -5.385  1.00164.11      A    O  
ANISOU 5559  OE1 GLU A 730    22957  18112  21283  -2234   7506  -2080  A    O  
ATOM   5560  OE2 GLU A 730     150.348  45.738  -6.631  1.00169.47      A    O1-
ANISOU 5560  OE2 GLU A 730    24374  18668  21348  -2367   7315  -1784  A    O1-
ATOM   5561  N   ALA A 731     150.711  51.837  -7.342  1.00133.71      A    N  
ANISOU 5561  N   ALA A 731    20737  13976  16087  -2899   7253  -1576  A    N  
ATOM   5562  CA  ALA A 731     150.084  52.749  -8.297  1.00133.20      A    C  
ANISOU 5562  CA  ALA A 731    21224  13754  15628  -3056   7165  -1457  A    C  
ATOM   5563  C   ALA A 731     150.141  54.195  -7.763  1.00140.34      A    C  
ANISOU 5563  C   ALA A 731    22113  14698  16508  -3042   7012  -1387  A    C  
ATOM   5564  O   ALA A 731     149.973  55.159  -8.516  1.00156.79      A    O  
ANISOU 5564  O   ALA A 731    24634  16637  18300  -3217   6997  -1336  A    O  
ATOM   5565  CB  ALA A 731     148.638  52.336  -8.553  1.00130.27      A    C  
ANISOU 5565  CB  ALA A 731    21083  13355  15057  -2908   6826  -1256  A    C  
ATOM   5566  N   HIS A 732     150.335  54.331  -6.447  1.00133.15      A    N  
ANISOU 5566  N   HIS A 732    20716  13975  15898  -2828   6876  -1380  A    N  
ATOM   5567  CA  HIS A 732     150.522  55.627  -5.787  1.00117.12      A    C  
ANISOU 5567  CA  HIS A 732    18592  12004  13903  -2799   6753  -1338  A    C  
ATOM   5568  C   HIS A 732     151.541  55.485  -4.665  1.00110.82      A    C  
ANISOU 5568  C   HIS A 732    17246  11362  13499  -2706   6869  -1474  A    C  
ATOM   5569  O   HIS A 732     151.564  54.469  -3.966  1.00104.75      A    O  
ANISOU 5569  O   HIS A 732    16113  10705  12983  -2526   6826  -1504  A    O  
ATOM   5570  CB  HIS A 732     149.206  56.116  -5.197  1.00110.76      A    C  
ANISOU 5570  CB  HIS A 732    17805  11273  13003  -2564   6297  -1113  A    C  
ATOM   5571  CG  HIS A 732     148.114  56.259  -6.201  1.00107.67      A    C  
ANISOU 5571  CG  HIS A 732    17917  10731  12258  -2615   6120   -981  A    C  
ATOM   5572  CD2 HIS A 732     147.582  57.353  -6.789  1.00106.20      A    C  
ANISOU 5572  CD2 HIS A 732    18145  10417  11787  -2699   5955   -885  A    C  
ATOM   5573  ND1 HIS A 732     147.425  55.177  -6.703  1.00106.49      A    N  
ANISOU 5573  ND1 HIS A 732    17889  10541  12028  -2570   6073   -939  A    N  
ATOM   5574  CE1 HIS A 732     146.520  55.595  -7.567  1.00107.46      A    C  
ANISOU 5574  CE1 HIS A 732    18477  10517  11834  -2627   5888   -825  A    C  
ATOM   5575  NE2 HIS A 732     146.588  56.914  -7.628  1.00110.55      A    N  
ANISOU 5575  NE2 HIS A 732    19056  10848  12098  -2699   5802   -791  A    N  
ATOM   5576  N   ALA A 733     152.378  56.504  -4.493  1.00108.89      A    N  
ANISOU 5576  N   ALA A 733    16956  11112  13305  -2828   7000  -1559  A    N  
ATOM   5577  CA  ALA A 733     153.413  56.481  -3.460  1.00109.26      A    C  
ANISOU 5577  CA  ALA A 733    16494  11289  13729  -2754   7105  -1703  A    C  
ATOM   5578  C   ALA A 733     152.806  56.512  -2.077  1.00109.67      A    C  
ANISOU 5578  C   ALA A 733    16188  11518  13963  -2438   6735  -1562  A    C  
ATOM   5579  O   ALA A 733     153.325  55.879  -1.147  1.00109.92      A    O  
ANISOU 5579  O   ALA A 733    15775  11662  14325  -2292   6736  -1649  A    O  
ATOM   5580  CB  ALA A 733     154.343  57.661  -3.619  1.00110.28      A    C  
ANISOU 5580  CB  ALA A 733    16692  11366  13841  -2963   7305  -1809  A    C  
ATOM   5581  N   ALA A 734     151.701  57.248  -1.956  1.00111.24      A    N  
ANISOU 5581  N   ALA A 734    16595  11728  13942  -2339   6412  -1355  A    N  
ATOM   5582  CA  ALA A 734     151.084  57.544  -0.660  1.00107.26      A    C  
ANISOU 5582  CA  ALA A 734    15801  11386  13567  -2073   6065  -1220  A    C  
ATOM   5583  C   ALA A 734     150.285  56.375  -0.074  1.00101.24      A    C  
ANISOU 5583  C   ALA A 734    14838  10724  12906  -1845   5861  -1135  A    C  
ATOM   5584  O   ALA A 734     150.121  56.285   1.133  1.00103.19      A    O  
ANISOU 5584  O   ALA A 734    14747  11112  13346  -1642   5659  -1084  A    O  
ATOM   5585  CB  ALA A 734     150.221  58.803  -0.766  1.00106.69      A    C  
ANISOU 5585  CB  ALA A 734    16015  11285  13235  -2060   5810  -1059  A    C  
ATOM   5586  N   ALA A 735     149.804  55.475  -0.916  1.00 98.54      A    N  
ANISOU 5586  N   ALA A 735    14713  10300  12426  -1890   5916  -1120  A    N  
ATOM   5587  CA  ALA A 735     149.045  54.327  -0.432  1.00 97.47      A    C  
ANISOU 5587  CA  ALA A 735    14414  10246  12372  -1694   5735  -1042  A    C  
ATOM   5588  C   ALA A 735     149.909  53.327   0.354  1.00 95.32      A    C  
ANISOU 5588  C   ALA A 735    13709  10054  12452  -1603   5847  -1176  A    C  
ATOM   5589  O   ALA A 735     151.092  53.183   0.125  1.00 95.77      A    O  
ANISOU 5589  O   ALA A 735    13652  10066  12670  -1728   6138  -1365  A    O  
ATOM   5590  CB  ALA A 735     148.339  53.627  -1.593  1.00 99.78      A    C  
ANISOU 5590  CB  ALA A 735    15067  10419  12424  -1775   5769   -998  A    C  
ATOM   5591  N   VAL A 736     149.279  52.642   1.290  1.00 96.14      A    N  
ANISOU 5591  N   VAL A 736    13581  10271  12673  -1386   5603  -1082  A    N  
ATOM   5592  CA  VAL A 736     149.919  51.621   2.098  1.00101.84      A    C  
ANISOU 5592  CA  VAL A 736    13923  11057  13715  -1270   5633  -1185  A    C  
ATOM   5593  C   VAL A 736     148.904  50.485   2.317  1.00107.38      A    C  
ANISOU 5593  C   VAL A 736    14622  11796  14380  -1121   5434  -1069  A    C  
ATOM   5594  O   VAL A 736     147.705  50.735   2.528  1.00119.49      A    O  
ANISOU 5594  O   VAL A 736    16279  13383  15736  -1032   5176   -892  A    O  
ATOM   5595  CB  VAL A 736     150.356  52.197   3.462  1.00 99.19      A    C  
ANISOU 5595  CB  VAL A 736    13239  10840  13609  -1137   5483  -1186  A    C  
ATOM   5596  CG1 VAL A 736     150.613  51.085   4.466  1.00103.35      A    C  
ANISOU 5596  CG1 VAL A 736    13413  11432  14423   -963   5379  -1229  A    C  
ATOM   5597  CG2 VAL A 736     151.578  53.073   3.319  1.00 97.49      A    C  
ANISOU 5597  CG2 VAL A 736    12951  10585  13504  -1280   5714  -1343  A    C  
ATOM   5598  N   ASN A 737     149.355  49.239   2.256  1.00105.49      A    N  
ANISOU 5598  N   ASN A 737    14243  11527  14312  -1098   5550  -1177  A    N  
ATOM   5599  CA  ASN A 737     148.472  48.148   2.597  1.00108.80      A    C  
ANISOU 5599  CA  ASN A 737    14630  11985  14723   -953   5352  -1073  A    C  
ATOM   5600  C   ASN A 737     148.754  47.674   4.007  1.00106.39      A    C  
ANISOU 5600  C   ASN A 737    13945  11778  14700   -768   5175  -1081  A    C  
ATOM   5601  O   ASN A 737     149.881  47.340   4.323  1.00111.92      A    O  
ANISOU 5601  O   ASN A 737    14392  12458  15674   -761   5306  -1251  A    O  
ATOM   5602  CB  ASN A 737     148.607  47.009   1.596  1.00114.85      A    C  
ANISOU 5602  CB  ASN A 737    15534  12641  15460  -1037   5552  -1164  A    C  
ATOM   5603  CG  ASN A 737     147.550  47.066   0.515  1.00121.87      A    C  
ANISOU 5603  CG  ASN A 737    16834  13461  16010  -1125   5526  -1043  A    C  
ATOM   5604  ND2 ASN A 737     147.952  46.857  -0.716  1.00122.55      A    N  
ANISOU 5604  ND2 ASN A 737    17163  13415  15985  -1306   5797  -1147  A    N  
ATOM   5605  OD1 ASN A 737     146.368  47.235   0.803  1.00135.13      A    O  
ANISOU 5605  OD1 ASN A 737    18606  15200  17534  -1028   5258   -865  A    O  
ATOM   5606  N   MET A 738     147.732  47.687   4.861  1.00 99.92      A    N  
ANISOU 5606  N   MET A 738    13090  11059  13813   -626   4872   -907  A    N  
ATOM   5607  CA  MET A 738     147.819  47.048   6.167  1.00 96.23      A    C  
ANISOU 5607  CA  MET A 738    12328  10668  13567   -457   4675   -892  A    C  
ATOM   5608  C   MET A 738     146.627  46.117   6.320  1.00 96.48      A    C  
ANISOU 5608  C   MET A 738    12453  10730  13475   -370   4480   -751  A    C  
ATOM   5609  O   MET A 738     145.632  46.253   5.603  1.00 99.71      A    O  
ANISOU 5609  O   MET A 738    13125  11132  13628   -420   4450   -645  A    O  
ATOM   5610  CB  MET A 738     147.839  48.080   7.296  1.00 92.52      A    C  
ANISOU 5610  CB  MET A 738    11697  10302  13153   -381   4496   -828  A    C  
ATOM   5611  CG  MET A 738     148.979  49.088   7.230  1.00 92.00      A    C  
ANISOU 5611  CG  MET A 738    11532  10213  13209   -464   4667   -958  A    C  
ATOM   5612  SD  MET A 738     150.501  48.567   8.063  1.00 88.55      A    S  
ANISOU 5612  SD  MET A 738    10696   9752  13194   -395   4730  -1164  A    S  
ATOM   5613  CE  MET A 738     151.247  50.159   8.439  1.00 86.16      A    C  
ANISOU 5613  CE  MET A 738    10294   9488  12953   -452   4776  -1212  A    C  
ATOM   5614  N   HIS A 739     146.731  45.164   7.245  1.00 96.78      A    N  
ANISOU 5614  N   HIS A 739    12284  10791  13694   -245   4339   -755  A    N  
ATOM   5615  CA  HIS A 739     145.629  44.249   7.506  1.00100.34      A    C  
ANISOU 5615  CA  HIS A 739    12812  11274  14039   -170   4148   -623  A    C  
ATOM   5616  C   HIS A 739     145.573  43.837   8.981  1.00103.06      A    C  
ANISOU 5616  C   HIS A 739    12936  11685  14534    -29   3900   -572  A    C  
ATOM   5617  O   HIS A 739     146.424  44.236   9.784  1.00 96.63      A    O  
ANISOU 5617  O   HIS A 739    11907  10885  13920     19   3866   -641  A    O  
ATOM   5618  CB  HIS A 739     145.721  43.011   6.594  1.00103.58      A    C  
ANISOU 5618  CB  HIS A 739    13324  11578  14453   -208   4291   -696  A    C  
ATOM   5619  CG  HIS A 739     146.745  42.008   7.031  1.00102.65      A    C  
ANISOU 5619  CG  HIS A 739    12969  11397  14634   -137   4329   -843  A    C  
ATOM   5620  CD2 HIS A 739     146.635  40.900   7.804  1.00104.34      A    C  
ANISOU 5620  CD2 HIS A 739    13064  11604  14977    -20   4152   -825  A    C  
ATOM   5621  ND1 HIS A 739     148.072  42.103   6.684  1.00102.00      A    N  
ANISOU 5621  ND1 HIS A 739    12746  11241  14765   -190   4559  -1050  A    N  
ATOM   5622  CE1 HIS A 739     148.739  41.102   7.228  1.00103.94      A    C  
ANISOU 5622  CE1 HIS A 739    12776  11437  15279    -92   4513  -1162  A    C  
ATOM   5623  NE2 HIS A 739     147.891  40.358   7.915  1.00104.71      A    N  
ANISOU 5623  NE2 HIS A 739    12895  11566  15323     15   4258  -1022  A    N  
ATOM   5624  N   LEU A 740     144.558  43.044   9.330  1.00106.71      A    N  
ANISOU 5624  N   LEU A 740    13469  12181  14893     26   3720   -449  A    N  
ATOM   5625  CA  LEU A 740     144.424  42.578  10.693  1.00112.48      A    C  
ANISOU 5625  CA  LEU A 740    14047  12960  15729    137   3480   -391  A    C  
ATOM   5626  C   LEU A 740     144.486  41.057  10.838  1.00119.48      A    C  
ANISOU 5626  C   LEU A 740    14908  13769  16720    195   3418   -417  A    C  
ATOM   5627  O   LEU A 740     144.014  40.281   9.996  1.00111.42      A    O  
ANISOU 5627  O   LEU A 740    14040  12699  15596    158   3491   -406  A    O  
ATOM   5628  CB  LEU A 740     143.191  43.201  11.350  1.00114.66      A    C  
ANISOU 5628  CB  LEU A 740    14399  13364  15802    146   3284   -224  A    C  
ATOM   5629  CG  LEU A 740     143.576  44.588  11.921  1.00117.64      A    C  
ANISOU 5629  CG  LEU A 740    14671  13811  16213    149   3262   -230  A    C  
ATOM   5630  CD1 LEU A 740     142.465  45.612  11.760  1.00121.79      A    C  
ANISOU 5630  CD1 LEU A 740    15336  14437  16497    106   3206   -120  A    C  
ATOM   5631  CD2 LEU A 740     144.012  44.513  13.383  1.00115.88      A    C  
ANISOU 5631  CD2 LEU A 740    14251  13619  16158    239   3074   -224  A    C  
ATOM   5632  N   SER A 741     145.109  40.664  11.940  1.00132.43      A    N  
ANISOU 5632  N   SER A 741    16357  15386  18571    290   3268   -456  A    N  
ATOM   5633  CA  SER A 741     145.509  39.294  12.176  1.00138.16      A    C  
ANISOU 5633  CA  SER A 741    17017  16010  19468    363   3198   -522  A    C  
ATOM   5634  C   SER A 741     144.343  38.385  12.522  1.00140.98      A    C  
ANISOU 5634  C   SER A 741    17521  16386  19658    380   3012   -374  A    C  
ATOM   5635  O   SER A 741     143.397  38.784  13.214  1.00140.30      A    O  
ANISOU 5635  O   SER A 741    17503  16402  19400    371   2851   -225  A    O  
ATOM   5636  CB  SER A 741     146.527  39.257  13.324  1.00140.04      A    C  
ANISOU 5636  CB  SER A 741    17016  16205  19985    465   3051   -609  A    C  
ATOM   5637  OG  SER A 741     146.513  38.008  13.999  1.00133.11      A    O  
ANISOU 5637  OG  SER A 741    16116  15247  19210    555   2848   -602  A    O  
ATOM   5638  N   ALA A 742     144.451  37.152  12.037  1.00143.03      A    N  
ANISOU 5638  N   ALA A 742    17823  16545  19977    399   3046   -428  A    N  
ATOM   5639  CA  ALA A 742     143.621  36.039  12.481  1.00140.71      A    C  
ANISOU 5639  CA  ALA A 742    17636  16233  19593    428   2854   -320  A    C  
ATOM   5640  C   ALA A 742     144.510  34.784  12.609  1.00143.84      A    C  
ANISOU 5640  C   ALA A 742    17930  16479  20244    517   2811   -453  A    C  
ATOM   5641  O   ALA A 742     145.207  34.423  11.669  1.00128.93      A    O  
ANISOU 5641  O   ALA A 742    16002  14504  18477    507   3013   -602  A    O  
ATOM   5642  CB  ALA A 742     142.482  35.815  11.501  1.00136.06      A    C  
ANISOU 5642  CB  ALA A 742    17273  15679  18742    343   2943   -226  A    C  
ATOM   5643  N   LEU A 743     144.494  34.144  13.779  1.00160.86      A    N  
ANISOU 5643  N   LEU A 743    20048  18593  22478    597   2542   -406  A    N  
ATOM   5644  CA  LEU A 743     145.387  33.008  14.093  1.00169.41      A    C  
ANISOU 5644  CA  LEU A 743    21018  19516  23831    703   2437   -538  A    C  
ATOM   5645  C   LEU A 743     144.597  31.717  14.353  1.00175.80      A    C  
ANISOU 5645  C   LEU A 743    21996  20266  24532    718   2252   -436  A    C  
ATOM   5646  O   LEU A 743     143.455  31.778  14.816  1.00164.18      A    O  
ANISOU 5646  O   LEU A 743    20686  18881  22811    660   2127   -253  A    O  
ATOM   5647  CB  LEU A 743     146.248  33.353  15.327  1.00177.50      A    C  
ANISOU 5647  CB  LEU A 743    21856  20503  25081    799   2236   -594  A    C  
ATOM   5648  CG  LEU A 743     146.894  32.227  16.163  1.00181.67      A    C  
ANISOU 5648  CG  LEU A 743    22305  20866  25853    927   1975   -674  A    C  
ATOM   5649  CD1 LEU A 743     148.082  31.624  15.429  1.00184.20      A    C  
ANISOU 5649  CD1 LEU A 743    22444  21052  26487    997   2124   -924  A    C  
ATOM   5650  CD2 LEU A 743     147.315  32.692  17.557  1.00175.55      A    C  
ANISOU 5650  CD2 LEU A 743    21435  20075  25190    997   1710   -652  A    C  
ATOM   5651  N   GLU A 744     145.207  30.562  14.059  1.00185.79      A    N  
ANISOU 5651  N   GLU A 744    23218  21382  25990    790   2242   -563  A    N  
ATOM   5652  CA  GLU A 744     144.621  29.246  14.381  1.00186.93      A    C  
ANISOU 5652  CA  GLU A 744    23514  21440  26071    819   2041   -485  A    C  
ATOM   5653  C   GLU A 744     145.109  28.678  15.717  1.00186.02      A    C  
ANISOU 5653  C   GLU A 744    23339  21206  26132    929   1708   -497  A    C  
ATOM   5654  O   GLU A 744     146.309  28.552  15.940  1.00183.83      A    O  
ANISOU 5654  O   GLU A 744    22859  20816  26169   1038   1665   -679  A    O  
ATOM   5655  CB  GLU A 744     144.883  28.239  13.254  1.00181.08      A    C  
ANISOU 5655  CB  GLU A 744    22797  20593  25410    830   2205   -609  A    C  
ATOM   5656  CG  GLU A 744     143.971  28.451  12.062  1.00183.12      A    C  
ANISOU 5656  CG  GLU A 744    23231  20944  25399    704   2439   -528  A    C  
ATOM   5657  CD  GLU A 744     142.629  29.034  12.483  1.00201.19      A    C  
ANISOU 5657  CD  GLU A 744    25687  23382  27372    615   2343   -302  A    C  
ATOM   5658  OE1 GLU A 744     142.423  30.254  12.275  1.00189.16      A    O  
ANISOU 5658  OE1 GLU A 744    24148  21982  25742    552   2465   -264  A    O  
ATOM   5659  OE2 GLU A 744     141.797  28.291  13.068  1.00218.23      A    O1-
ANISOU 5659  OE2 GLU A 744    27989  25530  29398    605   2139   -171  A    O1-
ATOM   5660  N   GLN A 745     144.162  28.332  16.591  1.00188.41      A    N  
ANISOU 5660  N   GLN A 745    23828  21528  26230    892   1469   -313  A    N  
ATOM   5661  CA  GLN A 745     144.471  27.891  17.956  1.00191.33      A    C  
ANISOU 5661  CA  GLN A 745    24207  21784  26704    971   1125   -289  A    C  
ATOM   5662  C   GLN A 745     144.168  26.407  18.166  1.00198.15      A    C  
ANISOU 5662  C   GLN A 745    25236  22497  27553   1003    918   -257  A    C  
ATOM   5663  O   GLN A 745     145.025  25.661  18.632  1.00206.80      A    O  
ANISOU 5663  O   GLN A 745    26260  23410  28902   1130    714   -375  A    O  
ATOM   5664  CB  GLN A 745     143.686  28.724  18.983  1.00182.98      A    C  
ANISOU 5664  CB  GLN A 745    23256  20853  25413    885    991   -107  A    C  
ATOM   5665  CG  GLN A 745     144.434  28.968  20.283  1.00176.55      A    C  
ANISOU 5665  CG  GLN A 745    22361  19953  24766    968    720   -135  A    C  
ATOM   5666  CD  GLN A 745     145.380  30.171  20.209  1.00171.04      A    C  
ANISOU 5666  CD  GLN A 745    21414  19311  24261   1017    851   -257  A    C  
ATOM   5667  NE2 GLN A 745     146.605  29.986  20.674  1.00171.03      A    N  
ANISOU 5667  NE2 GLN A 745    21234  19162  24586   1151    702   -416  A    N  
ATOM   5668  OE1 GLN A 745     145.004  31.251  19.764  1.00154.87      A    O  
ANISOU 5668  OE1 GLN A 745    19336  17432  22075    934   1066   -213  A    O  
ATOM   5669  N   GLY A 746     142.944  25.986  17.841  1.00194.34      A    N  
ANISOU 5669  N   GLY A 746    24977  22083  26781    891    955   -105  A    N  
ATOM   5670  CA  GLY A 746     142.526  24.593  18.024  1.00184.16      A    C  
ANISOU 5670  CA  GLY A 746    23876  20659  25436    899    766    -54  A    C  
ATOM   5671  C   GLY A 746     141.248  24.270  17.276  1.00172.24      A    C  
ANISOU 5671  C   GLY A 746    22562  19249  23632    768    908     76  A    C  
ATOM   5672  O   GLY A 746     140.194  24.078  17.892  1.00180.63      A    O  
ANISOU 5672  O   GLY A 746    23827  20360  24441    662    775    243  A    O  
ATOM   5673  N   ARG A 747     141.342  24.213  15.948  1.00158.74      A    N  
ANISOU 5673  N   ARG A 747    20798  17563  21952    766   1178    -12  A    N  
ATOM   5674  CA  ARG A 747     140.166  24.065  15.083  1.00174.27      A    C  
ANISOU 5674  CA  ARG A 747    22932  19631  23650    645   1337     94  A    C  
ATOM   5675  C   ARG A 747     139.295  25.334  15.113  1.00188.94      A    C  
ANISOU 5675  C   ARG A 747    24814  21698  25275    527   1448    215  A    C  
ATOM   5676  O   ARG A 747     138.326  25.449  14.358  1.00201.52      A    O  
ANISOU 5676  O   ARG A 747    26517  23390  26659    430   1587    289  A    O  
ATOM   5677  CB  ARG A 747     139.333  22.831  15.488  1.00173.45      A    C  
ANISOU 5677  CB  ARG A 747    23060  19448  23395    601   1132    211  A    C  
ATOM   5678  CG  ARG A 747     138.839  22.010  14.300  1.00171.55      A    C  
ANISOU 5678  CG  ARG A 747    22931  19180  23069    567   1280    203  A    C  
ATOM   5679  CD  ARG A 747     138.015  20.785  14.695  1.00168.67      A    C  
ANISOU 5679  CD  ARG A 747    22797  18735  22553    515   1079    315  A    C  
ATOM   5680  NE  ARG A 747     138.776  19.523  14.752  1.00170.53      A    N  
ANISOU 5680  NE  ARG A 747    23045  18753  22996    633    929    213  A    N  
ATOM   5681  CZ  ARG A 747     139.013  18.713  13.713  1.00165.66      A    C  
ANISOU 5681  CZ  ARG A 747    22436  18045  22461    678   1050    115  A    C  
ATOM   5682  NH1 ARG A 747     138.578  19.017  12.497  1.00176.64      A    N1+
ANISOU 5682  NH1 ARG A 747    23840  19535  23740    611   1326    108  A    N1+
ATOM   5683  NH2 ARG A 747     139.694  17.589  13.889  1.00151.79      A    N  
ANISOU 5683  NH2 ARG A 747    20681  16088  20903    792    884     13  A    N  
ATOM   5684  N   ASP A 748     139.662  26.287  15.970  1.00190.83      A    N  
ANISOU 5684  N   ASP A 748    24942  21996  25567    544   1377    221  A    N  
ATOM   5685  CA  ASP A 748     138.839  27.453  16.277  1.00179.79      A    C  
ANISOU 5685  CA  ASP A 748    23567  20785  23961    442   1424    334  A    C  
ATOM   5686  C   ASP A 748     139.643  28.715  15.989  1.00171.58      A    C  
ANISOU 5686  C   ASP A 748    22327  19811  23055    483   1586    238  A    C  
ATOM   5687  O   ASP A 748     140.753  28.854  16.491  1.00169.97      A    O  
ANISOU 5687  O   ASP A 748    21971  19524  23085    581   1514    137  A    O  
ATOM   5688  CB  ASP A 748     138.432  27.414  17.755  1.00177.43      A    C  
ANISOU 5688  CB  ASP A 748    23359  20492  23563    400   1161    448  A    C  
ATOM   5689  CG  ASP A 748     137.798  28.711  18.228  1.00176.10      A    C  
ANISOU 5689  CG  ASP A 748    23170  20508  23232    311   1202    530  A    C  
ATOM   5690  OD1 ASP A 748     137.060  29.348  17.450  1.00172.09      A    O  
ANISOU 5690  OD1 ASP A 748    22669  20138  22578    239   1390    558  A    O  
ATOM   5691  OD2 ASP A 748     138.033  29.091  19.392  1.00172.43      A    O1-
ANISOU 5691  OD2 ASP A 748    22690  20041  22783    314   1035    561  A    O1-
ATOM   5692  N   ILE A 749     139.086  29.630  15.192  1.00163.68      A    N  
ANISOU 5692  N   ILE A 749    21331  18948  21910    410   1792    263  A    N  
ATOM   5693  CA  ILE A 749     139.811  30.860  14.811  1.00155.04      A    C  
ANISOU 5693  CA  ILE A 749    20075  17913  20921    433   1962    175  A    C  
ATOM   5694  C   ILE A 749     139.778  31.881  15.940  1.00137.35      A    C  
ANISOU 5694  C   ILE A 749    17763  15767  18653    424   1843    233  A    C  
ATOM   5695  O   ILE A 749     138.833  31.910  16.734  1.00137.70      A    O  
ANISOU 5695  O   ILE A 749    17915  15887  18515    356   1702    361  A    O  
ATOM   5696  CB  ILE A 749     139.277  31.528  13.508  1.00152.04      A    C  
ANISOU 5696  CB  ILE A 749    19752  17624  20393    357   2209    177  A    C  
ATOM   5697  CG1 ILE A 749     137.966  32.304  13.770  1.00151.33      A    C  
ANISOU 5697  CG1 ILE A 749    19757  17696  20043    262   2172    315  A    C  
ATOM   5698  CG2 ILE A 749     139.106  30.489  12.410  1.00145.38      A    C  
ANISOU 5698  CG2 ILE A 749    19022  16690  19523    345   2315    142  A    C  
ATOM   5699  CD1 ILE A 749     137.477  33.136  12.600  1.00142.08      A    C  
ANISOU 5699  CD1 ILE A 749    18639  16604  18740    201   2367    312  A    C  
ATOM   5700  N   VAL A 750     140.829  32.695  16.011  1.00125.99      A    N  
ANISOU 5700  N   VAL A 750    16146  14321  17402    484   1909    130  A    N  
ATOM   5701  CA  VAL A 750     140.889  33.803  16.953  1.00128.07      A    C  
ANISOU 5701  CA  VAL A 750    16332  14678  17651    478   1825    171  A    C  
ATOM   5702  C   VAL A 750     141.489  35.028  16.278  1.00126.29      A    C  
ANISOU 5702  C   VAL A 750    15971  14512  17497    479   2037     84  A    C  
ATOM   5703  O   VAL A 750     142.080  34.934  15.208  1.00122.85      A    O  
ANISOU 5703  O   VAL A 750    15491  14022  17164    491   2233    -29  A    O  
ATOM   5704  CB  VAL A 750     141.745  33.483  18.193  1.00129.22      A    C  
ANISOU 5704  CB  VAL A 750    16390  14716  17990    567   1589    135  A    C  
ATOM   5705  CG1 VAL A 750     141.168  32.297  18.964  1.00126.87      A    C  
ANISOU 5705  CG1 VAL A 750    16260  14340  17604    553   1351    229  A    C  
ATOM   5706  CG2 VAL A 750     143.199  33.261  17.787  1.00132.66      A    C  
ANISOU 5706  CG2 VAL A 750    16635  15019  18750    679   1658    -55  A    C  
ATOM   5707  N   PHE A 751     141.334  36.175  16.928  1.00118.07      A    N  
ANISOU 5707  N   PHE A 751    14883  13582  16397    456   1997    133  A    N  
ATOM   5708  CA  PHE A 751     141.816  37.430  16.398  1.00109.49      A    C  
ANISOU 5708  CA  PHE A 751    13690  12558  15352    447   2174     67  A    C  
ATOM   5709  C   PHE A 751     142.633  38.150  17.465  1.00110.45      A    C  
ANISOU 5709  C   PHE A 751    13656  12681  15628    503   2058     32  A    C  
ATOM   5710  O   PHE A 751     142.099  38.631  18.461  1.00108.89      A    O  
ANISOU 5710  O   PHE A 751    13488  12565  15320    480   1908    130  A    O  
ATOM   5711  CB  PHE A 751     140.634  38.294  16.019  1.00106.15      A    C  
ANISOU 5711  CB  PHE A 751    13379  12282  14668    355   2245    168  A    C  
ATOM   5712  CG  PHE A 751     139.688  37.653  15.049  1.00100.53      A    C  
ANISOU 5712  CG  PHE A 751    12832  11575  13787    297   2325    214  A    C  
ATOM   5713  CD1 PHE A 751     139.883  37.788  13.693  1.00101.46      A    C  
ANISOU 5713  CD1 PHE A 751    12993  11658  13897    272   2538    146  A    C  
ATOM   5714  CD2 PHE A 751     138.572  36.959  15.501  1.00103.13      A    C  
ANISOU 5714  CD2 PHE A 751    13289  11941  13952    253   2189    324  A    C  
ATOM   5715  CE1 PHE A 751     138.992  37.236  12.785  1.00102.09      A    C  
ANISOU 5715  CE1 PHE A 751    13238  11735  13814    217   2598    190  A    C  
ATOM   5716  CE2 PHE A 751     137.676  36.395  14.608  1.00104.39      A    C  
ANISOU 5716  CE2 PHE A 751    13596  12107  13961    198   2255    362  A    C  
ATOM   5717  CZ  PHE A 751     137.887  36.541  13.242  1.00105.45      A    C  
ANISOU 5717  CZ  PHE A 751    13769  12201  14093    187   2453    297  A    C  
ATOM   5718  N   LEU A 752     143.935  38.226  17.265  1.00112.56      A    N  
ANISOU 5718  N   LEU A 752    13752  12857  16156    571   2131   -119  A    N  
ATOM   5719  CA  LEU A 752     144.795  38.854  18.253  1.00114.62      A    C  
ANISOU 5719  CA  LEU A 752    13854  13103  16592    633   2011   -168  A    C  
ATOM   5720  C   LEU A 752     144.710  40.365  18.148  1.00113.09      A    C  
ANISOU 5720  C   LEU A 752    13618  13037  16313    582   2125   -149  A    C  
ATOM   5721  O   LEU A 752     145.237  41.082  19.009  1.00113.17      A    O  
ANISOU 5721  O   LEU A 752    13516  13064  16421    617   2023   -165  A    O  
ATOM   5722  CB  LEU A 752     146.228  38.387  18.064  1.00121.71      A    C  
ANISOU 5722  CB  LEU A 752    14560  13856  17828    724   2049   -363  A    C  
ATOM   5723  CG  LEU A 752     146.411  36.868  17.970  1.00126.95      A    C  
ANISOU 5723  CG  LEU A 752    15253  14375  18606    786   1959   -416  A    C  
ATOM   5724  CD1 LEU A 752     147.897  36.543  18.008  1.00132.99      A    C  
ANISOU 5724  CD1 LEU A 752    15786  14998  19746    891   1957   -633  A    C  
ATOM   5725  CD2 LEU A 752     145.670  36.121  19.076  1.00127.39      A    C  
ANISOU 5725  CD2 LEU A 752    15457  14403  18540    801   1658   -272  A    C  
ATOM   5726  N   HIS A 753     144.036  40.831  17.091  1.00111.51      A    N  
ANISOU 5726  N   HIS A 753    13522  12917  15930    500   2318   -115  A    N  
ATOM   5727  CA  HIS A 753     143.805  42.253  16.834  1.00104.63      A    C  
ANISOU 5727  CA  HIS A 753    12650  12159  14946    445   2425    -90  A    C  
ATOM   5728  C   HIS A 753     145.119  43.013  16.796  1.00104.18      A    C  
ANISOU 5728  C   HIS A 753    12410  12062  15112    476   2524   -227  A    C  
ATOM   5729  O   HIS A 753     145.455  43.751  17.726  1.00 92.65      A    O  
ANISOU 5729  O   HIS A 753    10847  10638  13714    506   2410   -218  A    O  
ATOM   5730  CB  HIS A 753     142.878  42.837  17.884  1.00104.73      A    C  
ANISOU 5730  CB  HIS A 753    12714  12290  14784    425   2248     44  A    C  
ATOM   5731  CG  HIS A 753     141.577  42.110  18.007  1.00108.77      A    C  
ANISOU 5731  CG  HIS A 753    13393  12848  15086    380   2156    163  A    C  
ATOM   5732  CD2 HIS A 753     140.631  41.796  17.087  1.00106.75      A    C  
ANISOU 5732  CD2 HIS A 753    13279  12625  14656    321   2248    207  A    C  
ATOM   5733  ND1 HIS A 753     141.127  41.600  19.207  1.00115.33      A    N  
ANISOU 5733  ND1 HIS A 753    14266  13688  15863    381   1940    246  A    N  
ATOM   5734  CE1 HIS A 753     139.952  41.021  19.025  1.00112.50      A    C  
ANISOU 5734  CE1 HIS A 753    14059  13376  15308    318   1919    332  A    C  
ATOM   5735  NE2 HIS A 753     139.630  41.119  17.746  1.00104.66      A    N  
ANISOU 5735  NE2 HIS A 753    13119  12399  14249    288   2097    308  A    N  
ATOM   5736  N   GLN A 754     145.876  42.786  15.724  1.00112.01      A    N  
ANISOU 5736  N   GLN A 754    13361  12972  16226    457   2740   -361  A    N  
ATOM   5737  CA  GLN A 754     147.171  43.438  15.531  1.00115.25      A    C  
ANISOU 5737  CA  GLN A 754    13593  13337  16860    464   2878   -520  A    C  
ATOM   5738  C   GLN A 754     147.336  43.865  14.088  1.00115.15      A    C  
ANISOU 5738  C   GLN A 754    13660  13312  16778    361   3176   -595  A    C  
ATOM   5739  O   GLN A 754     147.119  43.058  13.163  1.00113.76      A    O  
ANISOU 5739  O   GLN A 754    13594  13079  16549    325   3298   -620  A    O  
ATOM   5740  CB  GLN A 754     148.316  42.503  15.928  1.00114.62      A    C  
ANISOU 5740  CB  GLN A 754    13323  13125  17100    557   2819   -673  A    C  
ATOM   5741  CG  GLN A 754     148.607  42.524  17.423  1.00116.46      A    C  
ANISOU 5741  CG  GLN A 754    13438  13348  17463    654   2531   -644  A    C  
ATOM   5742  CD  GLN A 754     149.499  41.391  17.897  1.00114.61      A    C  
ANISOU 5742  CD  GLN A 754    13057  12963  17525    764   2395   -773  A    C  
ATOM   5743  NE2 GLN A 754     149.339  40.222  17.299  1.00117.80      A    N  
ANISOU 5743  NE2 GLN A 754    13530  13290  17939    773   2439   -805  A    N  
ATOM   5744  OE1 GLN A 754     150.306  41.565  18.809  1.00107.80      A    O  
ANISOU 5744  OE1 GLN A 754    12029  12047  16881    845   2235   -845  A    O  
ATOM   5745  N   ILE A 755     147.685  45.141  13.906  1.00107.94      A    N  
ANISOU 5745  N   ILE A 755    12716  12446  15849    308   3283   -623  A    N  
ATOM   5746  CA  ILE A 755     148.001  45.659  12.587  1.00102.49      A    C  
ANISOU 5746  CA  ILE A 755    12116  11725  15100    193   3566   -708  A    C  
ATOM   5747  C   ILE A 755     149.208  44.911  12.072  1.00107.76      A    C  
ANISOU 5747  C   ILE A 755    12647  12272  16025    187   3748   -915  A    C  
ATOM   5748  O   ILE A 755     150.137  44.620  12.820  1.00104.33      A    O  
ANISOU 5748  O   ILE A 755    11979  11791  15869    270   3674  -1028  A    O  
ATOM   5749  CB  ILE A 755     148.284  47.181  12.556  1.00 98.44      A    C  
ANISOU 5749  CB  ILE A 755    11590  11268  14541    133   3639   -714  A    C  
ATOM   5750  CG1 ILE A 755     149.009  47.672  13.826  1.00102.44      A    C  
ANISOU 5750  CG1 ILE A 755    11863  11802  15257    217   3487   -749  A    C  
ATOM   5751  CG2 ILE A 755     146.996  47.939  12.368  1.00 94.81      A    C  
ANISOU 5751  CG2 ILE A 755    11344  10904  13776     93   3566   -546  A    C  
ATOM   5752  CD1 ILE A 755     150.518  47.445  13.845  1.00107.93      A    C  
ANISOU 5752  CD1 ILE A 755    12320  12402  16285    233   3607   -965  A    C  
ATOM   5753  N   GLN A 756     149.165  44.585  10.787  1.00119.86      A    N  
ANISOU 5753  N   GLN A 756    14329  13746  17465     88   3980   -972  A    N  
ATOM   5754  CA  GLN A 756     150.268  43.910  10.100  1.00127.73      A    C  
ANISOU 5754  CA  GLN A 756    15218  14629  18683     52   4210  -1191  A    C  
ATOM   5755  C   GLN A 756     150.348  44.485   8.704  1.00120.77      A    C  
ANISOU 5755  C   GLN A 756    14531  13716  17638   -121   4515  -1246  A    C  
ATOM   5756  O   GLN A 756     149.307  44.666   8.066  1.00123.51      A    O  
ANISOU 5756  O   GLN A 756    15147  14089  17690   -183   4514  -1104  A    O  
ATOM   5757  CB  GLN A 756     149.992  42.406   9.981  1.00136.98      A    C  
ANISOU 5757  CB  GLN A 756    16414  15733  19898    115   4151  -1200  A    C  
ATOM   5758  CG  GLN A 756     149.826  41.669  11.301  1.00140.95      A    C  
ANISOU 5758  CG  GLN A 756    16782  16240  20531    274   3832  -1136  A    C  
ATOM   5759  CD  GLN A 756     151.155  41.392  11.964  1.00139.61      A    C  
ANISOU 5759  CD  GLN A 756    16310  15994  20741    364   3796  -1332  A    C  
ATOM   5760  NE2 GLN A 756     151.208  40.328  12.755  1.00142.38      A    N  
ANISOU 5760  NE2 GLN A 756    16569  16282  21245    493   3566  -1338  A    N  
ATOM   5761  OE1 GLN A 756     152.129  42.115  11.753  1.00132.00      A    O  
ANISOU 5761  OE1 GLN A 756    15201  15016  19936    315   3968  -1487  A    O  
ATOM   5762  N   PRO A 757     151.567  44.784   8.220  1.00111.62      A    N  
ANISOU 5762  N   PRO A 757    13250  12495  16665   -208   4771  -1459  A    N  
ATOM   5763  CA  PRO A 757     151.714  45.255   6.831  1.00106.64      A    C  
ANISOU 5763  CA  PRO A 757    12840  11812  15865   -401   5085  -1526  A    C  
ATOM   5764  C   PRO A 757     151.270  44.205   5.804  1.00101.77      A    C  
ANISOU 5764  C   PRO A 757    12427  11118  15121   -458   5209  -1535  A    C  
ATOM   5765  O   PRO A 757     151.453  43.015   6.038  1.00107.87      A    O  
ANISOU 5765  O   PRO A 757    13072  11848  16065   -366   5160  -1604  A    O  
ATOM   5766  CB  PRO A 757     153.215  45.542   6.706  1.00104.38      A    C  
ANISOU 5766  CB  PRO A 757    12323  11470  15866   -473   5329  -1788  A    C  
ATOM   5767  CG  PRO A 757     153.704  45.718   8.105  1.00105.01      A    C  
ANISOU 5767  CG  PRO A 757    12088  11600  16209   -318   5099  -1806  A    C  
ATOM   5768  CD  PRO A 757     152.835  44.852   8.967  1.00108.12      A    C  
ANISOU 5768  CD  PRO A 757    12472  12027  16579   -145   4773  -1643  A    C  
ATOM   5769  N   GLY A 758     150.662  44.639   4.702  1.00 96.20      A    N  
ANISOU 5769  N   GLY A 758    12050  10389  14113   -602   5342  -1461  A    N  
ATOM   5770  CA  GLY A 758     150.201  43.732   3.665  1.00 99.88      A    C  
ANISOU 5770  CA  GLY A 758    12747  10775  14429   -669   5458  -1461  A    C  
ATOM   5771  C   GLY A 758     148.710  43.507   3.729  1.00107.13      A    C  
ANISOU 5771  C   GLY A 758    13876  11743  15085   -601   5210  -1222  A    C  
ATOM   5772  O   GLY A 758     148.041  44.033   4.611  1.00122.20      A    O  
ANISOU 5772  O   GLY A 758    15740  13752  16937   -503   4956  -1068  A    O  
ATOM   5773  N   PRO A 759     148.168  42.724   2.794  1.00113.13      A    N  
ANISOU 5773  N   PRO A 759    14867  12432  15684   -657   5285  -1200  A    N  
ATOM   5774  CA  PRO A 759     146.720  42.580   2.679  1.00121.23      A    C  
ANISOU 5774  CA  PRO A 759    16120  13495  16445   -617   5072   -989  A    C  
ATOM   5775  C   PRO A 759     146.082  41.227   3.050  1.00123.82      A    C  
ANISOU 5775  C   PRO A 759    16407  13829  16806   -498   4903   -923  A    C  
ATOM   5776  O   PRO A 759     145.158  40.783   2.365  1.00125.20      A    O  
ANISOU 5776  O   PRO A 759    16826  13973  16770   -530   4870   -829  A    O  
ATOM   5777  CB  PRO A 759     146.470  42.893   1.186  1.00120.19      A    C  
ANISOU 5777  CB  PRO A 759    16355  13262  16046   -799   5273   -996  A    C  
ATOM   5778  CG  PRO A 759     147.816  43.000   0.546  1.00117.32      A    C  
ANISOU 5778  CG  PRO A 759    15951  12807  15816   -940   5614  -1220  A    C  
ATOM   5779  CD  PRO A 759     148.809  42.451   1.513  1.00117.08      A    C  
ANISOU 5779  CD  PRO A 759    15523  12809  16151   -827   5618  -1363  A    C  
ATOM   5780  N   ALA A 760     146.544  40.588   4.120  1.00132.66      A    N  
ANISOU 5780  N   ALA A 760    17241  14980  18184   -365   4783   -968  A    N  
ATOM   5781  CA  ALA A 760     145.838  39.419   4.723  1.00144.27      A    C  
ANISOU 5781  CA  ALA A 760    18673  16467  19673   -242   4560   -875  A    C  
ATOM   5782  C   ALA A 760     145.690  38.107   3.890  1.00143.12      A    C  
ANISOU 5782  C   ALA A 760    18658  16222  19501   -266   4658   -923  A    C  
ATOM   5783  O   ALA A 760     145.147  37.118   4.396  1.00133.57      A    O  
ANISOU 5783  O   ALA A 760    17421  15016  18311   -169   4473   -851  A    O  
ATOM   5784  CB  ALA A 760     144.461  39.854   5.230  1.00144.24      A    C  
ANISOU 5784  CB  ALA A 760    18785  16571  19445   -200   4303   -652  A    C  
ATOM   5785  N   GLY A 761     146.155  38.098   2.638  1.00149.96      A    N  
ANISOU 5785  N   GLY A 761    19675  16990  20309   -402   4944  -1045  A    N  
ATOM   5786  CA  GLY A 761     146.024  36.927   1.734  1.00145.81      A    C  
ANISOU 5786  CA  GLY A 761    19302  16362  19736   -443   5062  -1100  A    C  
ATOM   5787  C   GLY A 761     144.567  36.485   1.575  1.00134.79      A    C  
ANISOU 5787  C   GLY A 761    18135  14993  18086   -418   4862   -897  A    C  
ATOM   5788  O   GLY A 761     143.654  37.247   1.893  1.00130.47      A    O  
ANISOU 5788  O   GLY A 761    17672  14534  17366   -404   4686   -732  A    O  
ATOM   5789  N   LYS A 762     144.354  35.261   1.084  1.00131.01      A    N  
ANISOU 5789  N   LYS A 762    17746  14436  17594   -412   4891   -921  A    N  
ATOM   5790  CA  LYS A 762     142.999  34.695   0.961  1.00123.50      A    C  
ANISOU 5790  CA  LYS A 762    16991  13503  16429   -385   4698   -743  A    C  
ATOM   5791  C   LYS A 762     142.843  33.401   1.770  1.00113.99      A    C  
ANISOU 5791  C   LYS A 762    15640  12298  15372   -253   4518   -724  A    C  
ATOM   5792  O   LYS A 762     143.360  32.349   1.446  1.00101.48      A    O  
ANISOU 5792  O   LYS A 762    14026  10617  13913   -239   4617   -841  A    O  
ATOM   5793  CB  LYS A 762     142.601  34.490  -0.499  1.00121.53      A    C  
ANISOU 5793  CB  LYS A 762    17073  13152  15949   -518   4865   -748  A    C  
ATOM   5794  N   SER A 763     142.095  33.516   2.848  1.00117.37      A    N  
ANISOU 5794  N   SER A 763    15990  12829  15774   -163   4246   -573  A    N  
ATOM   5795  CA  SER A 763     141.902  32.424   3.745  1.00114.02      A    C  
ANISOU 5795  CA  SER A 763    15452  12405  15466    -51   4045   -535  A    C  
ATOM   5796  C   SER A 763     140.447  32.423   4.176  1.00110.43      A    C  
ANISOU 5796  C   SER A 763    15120  12044  14795    -39   3807   -330  A    C  
ATOM   5797  O   SER A 763     140.139  32.226   5.338  1.00120.26      A    O  
ANISOU 5797  O   SER A 763    16248  13353  16091     38   3590   -250  A    O  
ATOM   5798  CB  SER A 763     142.855  32.553   4.933  1.00112.41      A    C  
ANISOU 5798  CB  SER A 763    14952  12220  15536     51   3958   -614  A    C  
ATOM   5799  N   TYR A 764     139.540  32.624   3.233  1.00108.48      A    N  
ANISOU 5799  N   TYR A 764    15115  11796  14305   -123   3847   -252  A    N  
ATOM   5800  CA  TYR A 764     138.144  32.302   3.505  1.00116.98      A    C  
ANISOU 5800  CA  TYR A 764    16304  12939  15202   -115   3637    -91  A    C  
ATOM   5801  C   TYR A 764     137.890  30.815   3.250  1.00115.52      A    C  
ANISOU 5801  C   TYR A 764    16201  12669  15022    -98   3606    -91  A    C  
ATOM   5802  O   TYR A 764     137.064  30.178   3.938  1.00101.05      A    O  
ANISOU 5802  O   TYR A 764    14370  10881  13143    -62   3405     15  A    O  
ATOM   5803  CB  TYR A 764     137.208  33.161   2.674  1.00123.98      A    C  
ANISOU 5803  CB  TYR A 764    17403  13858  15844   -198   3648    -15  A    C  
ATOM   5804  N   GLY A 765     138.611  30.287   2.253  1.00123.76      A    N  
ANISOU 5804  N   GLY A 765    17318  13587  16117   -134   3816   -217  A    N  
ATOM   5805  CA  GLY A 765     138.677  28.840   1.981  1.00114.39      A    C  
ANISOU 5805  CA  GLY A 765    16180  12297  14985   -108   3821   -260  A    C  
ATOM   5806  C   GLY A 765     139.374  28.113   3.127  1.00111.17      A    C  
ANISOU 5806  C   GLY A 765    15538  11871  14830      8   3699   -314  A    C  
ATOM   5807  O   GLY A 765     139.205  26.913   3.305  1.00121.27      A    O  
ANISOU 5807  O   GLY A 765    16838  13086  16151     55   3602   -307  A    O  
ATOM   5808  N   ILE A 766     140.092  28.856   3.955  1.00109.36      A    N  
ANISOU 5808  N   ILE A 766    15098  11693  14758     57   3674   -359  A    N  
ATOM   5809  CA  ILE A 766     140.535  28.333   5.229  1.00108.73      A    C  
ANISOU 5809  CA  ILE A 766    14819  11608  14884    169   3483   -372  A    C  
ATOM   5810  C   ILE A 766     139.388  28.083   6.176  1.00108.37      A    C  
ANISOU 5810  C   ILE A 766    14829  11642  14700    188   3210   -186  A    C  
ATOM   5811  O   ILE A 766     139.574  27.318   7.118  1.00115.99      A    O  
ANISOU 5811  O   ILE A 766    15712  12569  15791    267   3028   -180  A    O  
ATOM   5812  CB  ILE A 766     141.491  29.285   5.892  1.00113.08      A    C  
ANISOU 5812  CB  ILE A 766    15149  12198  15617    209   3507   -454  A    C  
ATOM   5813  N   ALA A 767     138.227  28.725   5.983  1.00100.83      A    N  
ANISOU 5813  N   ALA A 767    14015  10795  13500    114   3172    -48  A    N  
ATOM   5814  CA  ALA A 767     137.063  28.347   6.771  1.00 99.26      A    C  
ANISOU 5814  CA  ALA A 767    13881  10668  13164    108   2943    107  A    C  
ATOM   5815  C   ALA A 767     136.443  27.025   6.237  1.00 99.31      A    C  
ANISOU 5815  C   ALA A 767    14056  10592  13083     89   2910    141  A    C  
ATOM   5816  O   ALA A 767     135.237  26.807   6.312  1.00108.73      A    O  
ANISOU 5816  O   ALA A 767    15375  11845  14092     37   2797    263  A    O  
ATOM   5817  CB  ALA A 767     136.052  29.483   6.878  1.00 96.19      A    C  
ANISOU 5817  CB  ALA A 767    13541  10425  12581     45   2898    218  A    C  
ATOM   5818  N   VAL A 768     137.310  26.139   5.743  1.00 96.59      A    N  
ANISOU 5818  N   VAL A 768    13698  10111  12891    133   3008     17  A    N  
ATOM   5819  CA  VAL A 768     137.042  24.702   5.659  1.00 93.41      A    C  
ANISOU 5819  CA  VAL A 768    13393   9607  12488    153   2922     30  A    C  
ATOM   5820  C   VAL A 768     137.177  24.012   7.046  1.00 96.08      A    C  
ANISOU 5820  C   VAL A 768    13638   9920  12945    230   2672     67  A    C  
ATOM   5821  O   VAL A 768     136.962  22.813   7.165  1.00 92.04      A    O  
ANISOU 5821  O   VAL A 768    13210   9321  12440    252   2561     85  A    O  
ATOM   5822  CB  VAL A 768     137.969  24.055   4.643  1.00 86.74      A    C  
ANISOU 5822  CB  VAL A 768    12557   8621  11775    173   3123   -137  A    C  
ATOM   5823  N   ALA A 769     137.476  24.782   8.094  1.00100.14      A    N  
ANISOU 5823  N   ALA A 769    14008  10508  13534    263   2570     87  A    N  
ATOM   5824  CA  ALA A 769     137.574  24.245   9.449  1.00106.86      A    C  
ANISOU 5824  CA  ALA A 769    14805  11326  14469    321   2316    133  A    C  
ATOM   5825  C   ALA A 769     136.255  23.611   9.876  1.00116.90      A    C  
ANISOU 5825  C   ALA A 769    16258  12638  15522    247   2143    295  A    C  
ATOM   5826  O   ALA A 769     136.223  22.857  10.847  1.00130.17      A    O  
ANISOU 5826  O   ALA A 769    17966  14258  17236    273   1928    340  A    O  
ATOM   5827  CB  ALA A 769     137.976  25.326  10.449  1.00103.61      A    C  
ANISOU 5827  CB  ALA A 769    14237  10998  14130    346   2243    142  A    C  
ATOM   5828  N   LYS A 770     135.162  23.962   9.200  1.00114.44      A    N  
ANISOU 5828  N   LYS A 770    16070  12426  14986    147   2225    379  A    N  
ATOM   5829  CA  LYS A 770     133.941  23.152   9.229  1.00115.66      A    C  
ANISOU 5829  CA  LYS A 770    16404  12592  14948     70   2116    495  A    C  
ATOM   5830  C   LYS A 770     133.248  23.485   7.911  1.00117.91      A    C  
ANISOU 5830  C   LYS A 770    16796  12923  15080      2   2286    502  A    C  
ATOM   5831  O   LYS A 770     132.513  24.468   7.826  1.00126.39      A    O  
ANISOU 5831  O   LYS A 770    17874  14129  16020    -61   2313    556  A    O  
ATOM   5832  CB  LYS A 770     133.055  23.440  10.466  1.00107.82      A    C  
ANISOU 5832  CB  LYS A 770    15430  11714  13823     -2   1933    622  A    C  
ATOM   5833  N   LEU A 771     133.543  22.695   6.874  1.00115.41      A    N  
ANISOU 5833  N   LEU A 771    16566  12487  14794     20   2395    433  A    N  
ATOM   5834  CA  LEU A 771     132.892  22.847   5.550  1.00119.19      A    C  
ANISOU 5834  CA  LEU A 771    17193  12974  15118    -47   2537    440  A    C  
ATOM   5835  C   LEU A 771     132.625  21.491   4.931  1.00112.48      A    C  
ANISOU 5835  C   LEU A 771    16500  12006  14230    -56   2527    438  A    C  
ATOM   5836  O   LEU A 771     132.537  20.525   5.683  1.00119.96      A    O  
ANISOU 5836  O   LEU A 771    17462  12903  15214    -34   2368    475  A    O  
ATOM   5837  CB  LEU A 771     133.687  23.714   4.604  1.00120.39      A    C  
ANISOU 5837  CB  LEU A 771    17306  13108  15327    -38   2761    332  A    C  
ATOM   5838  N   ALA A 772     132.413  21.412   3.607  1.00103.67      A    N  
ANISOU 5838  N   ALA A 772    15525  10841  13023    -97   2676    406  A    N  
ATOM   5839  CA  ALA A 772     131.884  20.160   3.027  1.00106.30      A    C  
ANISOU 5839  CA  ALA A 772    16033  11078  13276   -121   2645    428  A    C  
ATOM   5840  C   ALA A 772     131.708  20.136   1.506  1.00 96.59      A    C  
ANISOU 5840  C   ALA A 772    14979   9782  11938   -171   2816    386  A    C  
ATOM   5841  O   ALA A 772     130.624  20.444   0.975  1.00 84.17      A    O  
ANISOU 5841  O   ALA A 772    13541   8263  10176   -246   2789    464  A    O  
ATOM   5842  CB  ALA A 772     130.545  19.779   3.698  1.00110.35      A    C  
ANISOU 5842  CB  ALA A 772    16621  11672  13632   -187   2443    571  A    C  
ATOM   5843  N   GLY A 773     132.724  19.655   0.810  1.00 96.86      A    N  
ANISOU 5843  N   GLY A 773    15025   9685  12091   -133   2979    256  A    N  
ATOM   5844  CA  GLY A 773     132.714  19.822  -0.620  1.00102.44      A    C  
ANISOU 5844  CA  GLY A 773    15907  10324  12689   -196   3169    203  A    C  
ATOM   5845  C   GLY A 773     134.006  19.230  -1.352  1.00104.51      A    C  
ANISOU 5845  C   GLY A 773    16163  10435  13110   -165   3386     22  A    C  
ATOM   5846  O   GLY A 773     134.808  18.592  -0.674  1.00104.19      A    O  
ANISOU 5846  O   GLY A 773    15965  10343  13276    -78   3350    -56  A    O  
ATOM   5847  N   LEU A 774     134.242  19.364  -2.673  1.00103.77      A    N  
ANISOU 5847  N   LEU A 774    16237  10258  12931   -234   3603    -58  A    N  
ATOM   5848  CA  LEU A 774     133.551  20.244  -3.644  1.00111.55      A    C  
ANISOU 5848  CA  LEU A 774    17429  11266  13688   -338   3672     -1  A    C  
ATOM   5849  C   LEU A 774     133.762  21.767  -3.305  1.00118.95      A    C  
ANISOU 5849  C   LEU A 774    18251  12315  14629   -351   3702      8  A    C  
ATOM   5850  O   LEU A 774     133.116  22.684  -3.866  1.00109.36      A    O  
ANISOU 5850  O   LEU A 774    17178  11135  13235   -421   3699     70  A    O  
ATOM   5851  CB  LEU A 774     132.074  19.852  -3.793  1.00113.63      A    C  
ANISOU 5851  CB  LEU A 774    17866  11558  13748   -376   3479    151  A    C  
ATOM   5852  N   PRO A 775     134.674  21.990  -2.346  1.00121.46      A    N  
ANISOU 5852  N   PRO A 775    18311  12676  15162   -276   3708    -57  A    N  
ATOM   5853  CA  PRO A 775     135.155  23.309  -1.930  1.00110.65      A    C  
ANISOU 5853  CA  PRO A 775    16794  11397  13849   -275   3757    -78  A    C  
ATOM   5854  C   PRO A 775     136.344  23.632  -2.815  1.00115.93      A    C  
ANISOU 5854  C   PRO A 775    17483  11971  14593   -324   4049   -251  A    C  
ATOM   5855  O   PRO A 775     136.953  24.667  -2.689  1.00118.55      A    O  
ANISOU 5855  O   PRO A 775    17714  12347  14982   -340   4147   -303  A    O  
ATOM   5856  CB  PRO A 775     135.584  23.293  -0.454  1.00101.30      A    C  
ANISOU 5856  CB  PRO A 775    15332  10290  12865   -172   3610    -71  A    C  
ATOM   5857  N   VAL A 776     136.696  22.704  -3.696  1.00130.66      A    N  
ANISOU 5857  N   VAL A 776    19476  13703  16463   -356   4198   -350  A    N  
ATOM   5858  CA  VAL A 776     137.749  22.917  -4.685  1.00135.79      A    C  
ANISOU 5858  CA  VAL A 776    20187  14251  17155   -436   4510   -531  A    C  
ATOM   5859  C   VAL A 776     137.218  23.854  -5.759  1.00140.30      A    C  
ANISOU 5859  C   VAL A 776    21041  14804  17459   -571   4602   -475  A    C  
ATOM   5860  O   VAL A 776     137.956  24.679  -6.296  1.00128.95      A    O  
ANISOU 5860  O   VAL A 776    19640  13338  16016   -657   4818   -578  A    O  
ATOM   5861  CB  VAL A 776     138.159  21.577  -5.290  1.00134.76      A    C  
ANISOU 5861  CB  VAL A 776    20124  13982  17094   -435   4628   -653  A    C  
ATOM   5862  N   ARG A 777     135.917  23.711  -6.041  1.00156.61      A    N  
ANISOU 5862  N   ARG A 777    23313  16883  19307   -590   4420   -317  A    N  
ATOM   5863  CA  ARG A 777     135.186  24.552  -7.006  1.00153.97      A    C  
ANISOU 5863  CA  ARG A 777    23269  16521  18708   -699   4424   -243  A    C  
ATOM   5864  C   ARG A 777     135.303  26.018  -6.618  1.00146.00      A    C  
ANISOU 5864  C   ARG A 777    22171  15609  17691   -710   4406   -216  A    C  
ATOM   5865  O   ARG A 777     135.285  26.911  -7.476  1.00121.59      A    O  
ANISOU 5865  O   ARG A 777    19296  12464  14437   -815   4501   -224  A    O  
ATOM   5866  CB  ARG A 777     133.714  24.136  -7.065  1.00155.54      A    C  
ANISOU 5866  CB  ARG A 777    23618  16743  18734   -685   4170    -82  A    C  
ATOM   5867  N   ALA A 778     135.377  26.244  -5.304  1.00155.27      A    N  
ANISOU 5867  N   ALA A 778    23047  16917  19029   -604   4266   -176  A    N  
ATOM   5868  CA  ALA A 778     135.675  27.558  -4.746  1.00152.10      A    C  
ANISOU 5868  CA  ALA A 778    22503  16615  18672   -596   4259   -169  A    C  
ATOM   5869  C   ALA A 778     137.153  27.847  -4.982  1.00141.08      A    C  
ANISOU 5869  C   ALA A 778    21013  15160  17430   -638   4538   -347  A    C  
ATOM   5870  O   ALA A 778     137.498  28.877  -5.563  1.00134.25      A    O  
ANISOU 5870  O   ALA A 778    20258  14270  16478   -732   4676   -388  A    O  
ATOM   5871  CB  ALA A 778     135.331  27.620  -3.254  1.00147.48      A    C  
ANISOU 5871  CB  ALA A 778    21639  16180  18213   -480   4030    -81  A    C  
ATOM   5872  N   LEU A 779     138.011  26.912  -4.560  1.00132.69      A    N  
ANISOU 5872  N   LEU A 779    19753  14065  16594   -574   4618   -463  A    N  
ATOM   5873  CA  LEU A 779     139.462  27.082  -4.672  1.00126.20      A    C  
ANISOU 5873  CA  LEU A 779    18784  13193  15970   -602   4880   -664  A    C  
ATOM   5874  C   LEU A 779     139.897  27.173  -6.138  1.00123.12      A    C  
ANISOU 5874  C   LEU A 779    18666  12667  15444   -765   5177   -782  A    C  
ATOM   5875  O   LEU A 779     141.046  27.483  -6.422  1.00109.24      A    O  
ANISOU 5875  O   LEU A 779    16832  10864  13808   -832   5437   -961  A    O  
ATOM   5876  CB  LEU A 779     140.203  25.959  -3.939  1.00121.63      A    C  
ANISOU 5876  CB  LEU A 779    17942  12591  15679   -485   4866   -776  A    C  
ATOM   5877  N   LYS A 780     138.959  26.905  -7.050  1.00130.47      A    N  
ANISOU 5877  N   LYS A 780    19924  13530  16118   -837   5134   -687  A    N  
ATOM   5878  CA  LYS A 780     139.190  26.994  -8.501  1.00129.54      A    C  
ANISOU 5878  CA  LYS A 780    20140  13267  15812  -1010   5384   -772  A    C  
ATOM   5879  C   LYS A 780     138.718  28.336  -9.064  1.00130.79      A    C  
ANISOU 5879  C   LYS A 780    20547  13421  15726  -1119   5363   -683  A    C  
ATOM   5880  O   LYS A 780     139.206  28.769 -10.100  1.00123.84      A    O  
ANISOU 5880  O   LYS A 780    19912  12427  14713  -1281   5600   -774  A    O  
ATOM   5881  CB  LYS A 780     138.469  25.856  -9.214  1.00128.90      A    C  
ANISOU 5881  CB  LYS A 780    20297  13088  15591  -1026   5336   -727  A    C  
ATOM   5882  N   ALA A 781     137.743  28.972  -8.407  1.00132.65      A    N  
ANISOU 5882  N   ALA A 781    20738  13770  15895  -1037   5076   -510  A    N  
ATOM   5883  CA  ALA A 781     137.281  30.308  -8.819  1.00132.56      A    C  
ANISOU 5883  CA  ALA A 781    20929  13757  15680  -1114   5014   -431  A    C  
ATOM   5884  C   ALA A 781     138.267  31.386  -8.353  1.00132.17      A    C  
ANISOU 5884  C   ALA A 781    20692  13766  15757  -1136   5149   -515  A    C  
ATOM   5885  O   ALA A 781     138.502  32.357  -9.053  1.00121.47      A    O  
ANISOU 5885  O   ALA A 781    19552  12344  14254  -1264   5264   -540  A    O  
ATOM   5886  CB  ALA A 781     135.889  30.578  -8.282  1.00130.30      A    C  
ANISOU 5886  CB  ALA A 781    20635  13572  15300  -1016   4667   -246  A    C  
ATOM   5887  N   ALA A 782     138.804  31.206  -7.146  1.00140.42      A    N  
ANISOU 5887  N   ALA A 782    21353  14931  17071  -1012   5114   -551  A    N  
ATOM   5888  CA  ALA A 782     140.024  31.879  -6.668  1.00141.36      A    C  
ANISOU 5888  CA  ALA A 782    21234  15089  17383  -1024   5289   -681  A    C  
ATOM   5889  C   ALA A 782     140.985  30.738  -6.362  1.00161.03      A    C  
ANISOU 5889  C   ALA A 782    23489  17553  20139   -972   5438   -842  A    C  
ATOM   5890  O   ALA A 782     140.726  30.017  -5.394  1.00187.26      A    O  
ANISOU 5890  O   ALA A 782    26585  20949  23614   -821   5245   -790  A    O  
ATOM   5891  CB  ALA A 782     139.740  32.650  -5.391  1.00126.88      A    C  
ANISOU 5891  CB  ALA A 782    19140  13418  15650   -900   5061   -579  A    C  
ATOM   5892  N   GLN A 783     142.091  30.531  -7.093  1.00156.59      A    N  
ANISOU 5892  N   GLN A 783    22959  16886  19650  -1088   5767  -1046  A    N  
ATOM   5893  CA  GLN A 783     142.810  31.489  -7.934  1.00143.20      A    C  
ANISOU 5893  CA  GLN A 783    21433  15119  17857  -1273   6045  -1158  A    C  
ATOM   5894  C   GLN A 783     142.027  32.231  -9.009  1.00149.59      A    C  
ANISOU 5894  C   GLN A 783    22685  15845  18304  -1421   6032  -1044  A    C  
ATOM   5895  O   GLN A 783     141.503  31.625  -9.939  1.00153.93      A    O  
ANISOU 5895  O   GLN A 783    23539  16285  18662  -1493   6054  -1016  A    O  
ATOM   5896  CB  GLN A 783     143.989  30.771  -8.583  1.00134.62      A    C  
ANISOU 5896  CB  GLN A 783    20317  13921  16908  -1376   6402  -1411  A    C  
ATOM   5897  N   LYS A 784     141.972  33.555  -8.858  1.00155.33      A    N  
ANISOU 5897  N   LYS A 784    23452  16619  18948  -1460   5980   -982  A    N  
ATOM   5898  CA  LYS A 784     141.419  34.473  -9.858  1.00147.57      A    C  
ANISOU 5898  CA  LYS A 784    22890  15539  17640  -1609   5971   -901  A    C  
ATOM   5899  C   LYS A 784     142.473  35.539 -10.164  1.00133.76      A    C  
ANISOU 5899  C   LYS A 784    21178  13751  15891  -1768   6234  -1029  A    C  
ATOM   5900  O   LYS A 784     142.688  36.440  -9.370  1.00118.71      A    O  
ANISOU 5900  O   LYS A 784    19064  11951  14089  -1709   6154  -1004  A    O  
ATOM   5901  CB  LYS A 784     140.132  35.117  -9.332  1.00146.14      A    C  
ANISOU 5901  CB  LYS A 784    22733  15450  17341  -1489   5592   -684  A    C  
ATOM   5902  N   HIS A 785     143.146  35.409 -11.299  1.00136.93      A    N  
ANISOU 5902  N   HIS A 785    21849  14000  16177  -1980   6557  -1175  A    N  
ATOM   5903  CA  HIS A 785     144.256  36.312 -11.646  1.00140.90      A    C  
ANISOU 5903  CA  HIS A 785    22395  14455  16686  -2166   6859  -1330  A    C  
ATOM   5904  C   HIS A 785     143.801  37.434 -12.595  1.00143.39      A    C  
ANISOU 5904  C   HIS A 785    23191  14647  16643  -2344   6834  -1237  A    C  
ATOM   5905  O   HIS A 785     142.694  37.392 -13.135  1.00149.38      A    O  
ANISOU 5905  O   HIS A 785    24273  15333  17150  -2336   6611  -1081  A    O  
ATOM   5906  CB  HIS A 785     145.413  35.522 -12.253  1.00136.24      A    C  
ANISOU 5906  CB  HIS A 785    21777  13774  16212  -2313   7269  -1585  A    C  
TER   
ATOM   5907  N   GLN B  -1     135.829  11.071  61.632  1.00165.61      B    N  
ATOM   5908  CA  GLN B  -1     134.505  11.745  61.470  1.00160.27      B    C  
ATOM   5909  C   GLN B  -1     133.468  11.349  62.526  1.00157.51      B    C  
ATOM   5910  O   GLN B  -1     132.439  10.776  62.185  1.00161.59      B    O  
ATOM   5911  N   SER B   0     133.747  11.645  63.799  1.00152.91      B    N  
ATOM   5912  CA  SER B   0     132.773  11.472  64.894  1.00132.79      B    C  
ATOM   5913  C   SER B   0     131.772  12.624  64.833  1.00137.49      B    C  
ATOM   5914  O   SER B   0     132.007  13.613  64.133  1.00164.23      B    O  
ATOM   5915  N   MET B   1     130.660  12.514  65.549  1.00170.44      B    N  
ANISOU 5915  N   MET B   1    18043  26408  20307   1676    336  -1660  B    N  
ATOM   5916  CA  MET B   1     129.608  13.518  65.441  1.00155.47      B    C  
ANISOU 5916  CA  MET B   1    16326  23988  18758   1207    388  -1675  B    C  
ATOM   5917  C   MET B   1     129.194  14.119  66.779  1.00152.09      B    C  
ANISOU 5917  C   MET B   1    15944  23350  18490    860    418  -1671  B    C  
ATOM   5918  O   MET B   1     129.995  14.255  67.705  1.00149.94      B    O  
ANISOU 5918  O   MET B   1    15458  23474  18038    776    441  -1632  B    O  
ATOM   5919  N   SER B   2     127.929  14.506  66.861  1.00145.50      B    N  
ANISOU 5919  N   SER B   2    15384  21916  17983    659    422  -1700  B    N  
ATOM   5920  CA  SER B   2     127.362  14.993  68.098  1.00144.68      B    C  
ANISOU 5920  CA  SER B   2    15373  21553  18043    392    451  -1697  B    C  
ATOM   5921  C   SER B   2     126.888  13.766  68.848  1.00152.10      B    C  
ANISOU 5921  C   SER B   2    16483  22272  19034    740    327  -1730  B    C  
ATOM   5922  O   SER B   2     127.699  13.037  69.413  1.00166.29      B    O  
ANISOU 5922  O   SER B   2    18160  24413  20607   1001    275  -1731  B    O  
ATOM   5923  N   LYS B   3     125.578  13.533  68.845  1.00145.44      B    N  
ANISOU 5923  N   LYS B   3    15923  20874  18463    743    272  -1741  B    N  
ATOM   5924  CA  LYS B   3     124.634  14.471  68.264  1.00136.81      B    C  
ANISOU 5924  CA  LYS B   3    14940  19430  17610    447    348  -1720  B    C  
ATOM   5925  C   LYS B   3     124.202  15.539  69.268  1.00132.30      B    C  
ANISOU 5925  C   LYS B   3    14385  18713  17168     78    456  -1692  B    C  
ATOM   5926  O   LYS B   3     123.068  15.999  69.223  1.00148.03      B    O  
ANISOU 5926  O   LYS B   3    16544  20309  19388    -62    490  -1664  B    O  
ATOM   5927  N   SER B   4     125.090  15.917  70.187  1.00122.52      B    N  
ANISOU 5927  N   SER B   4    12983  17807  15762    -63    506  -1691  B    N  
ATOM   5928  CA  SER B   4     124.783  16.982  71.133  1.00117.41      B    C  
ANISOU 5928  CA  SER B   4    12385  17031  15192   -413    607  -1672  B    C  
ATOM   5929  C   SER B   4     125.305  18.320  70.619  1.00114.28      B    C  
ANISOU 5929  C   SER B   4    11931  16785  14703   -777    725  -1657  B    C  
ATOM   5930  O   SER B   4     124.979  19.369  71.168  1.00118.41      B    O  
ANISOU 5930  O   SER B   4    12578  17135  15275  -1081    815  -1646  B    O  
ATOM   5931  CB  SER B   4     125.322  16.651  72.537  1.00115.93      B    C  
ANISOU 5931  CB  SER B   4    12107  17057  14881   -396    578  -1675  B    C  
ATOM   5932  OG  SER B   4     126.720  16.832  72.646  1.00112.05      B    O  
ANISOU 5932  OG  SER B   4    11355  17116  14100   -476    593  -1666  B    O  
ATOM   5933  N   ALA B   5     126.079  18.269  69.538  1.00115.23      B    N  
ANISOU 5933  N   ALA B   5    11899  17210  14671   -737    718  -1652  B    N  
ATOM   5934  CA  ALA B   5     126.614  19.466  68.885  1.00116.06      B    C  
ANISOU 5934  CA  ALA B   5    11962  17471  14665  -1094    809  -1622  B    C  
ATOM   5935  C   ALA B   5     125.636  20.047  67.845  1.00119.88      B    C  
ANISOU 5935  C   ALA B   5    12658  17536  15352  -1153    864  -1621  B    C  
ATOM   5936  O   ALA B   5     125.931  21.043  67.177  1.00120.55      B    O  
ANISOU 5936  O   ALA B   5    12771  17669  15364  -1433    937  -1596  B    O  
ATOM   5937  CB  ALA B   5     127.935  19.135  68.218  1.00113.95      B    C  
ANISOU 5937  CB  ALA B   5    11393  17789  14112  -1026    779  -1592  B    C  
ATOM   5938  N   VAL B   6     124.476  19.412  67.707  1.00121.04      B    N  
ANISOU 5938  N   VAL B   6    12959  17290  15738   -902    821  -1635  B    N  
ATOM   5939  CA  VAL B   6     123.490  19.805  66.712  1.00121.89      B    C  
ANISOU 5939  CA  VAL B   6    13238  17037  16035   -906    860  -1618  B    C  
ATOM   5940  C   VAL B   6     122.089  19.549  67.275  1.00119.30      B    C  
ANISOU 5940  C   VAL B   6    13096  16274  15957   -800    844  -1595  B    C  
ATOM   5941  O   VAL B   6     121.855  18.545  67.939  1.00123.05      B    O  
ANISOU 5941  O   VAL B   6    13560  16719  16475   -597    746  -1601  B    O  
ATOM   5942  CB  VAL B   6     123.728  19.041  65.381  1.00125.60      B    C  
ANISOU 5942  CB  VAL B   6    13622  17630  16468   -659    785  -1629  B    C  
ATOM   5943  CG1 VAL B   6     123.735  17.531  65.598  1.00130.61      B    C  
ANISOU 5943  CG1 VAL B   6    14224  18312  17088   -274    640  -1657  B    C  
ATOM   5944  CG2 VAL B   6     122.696  19.423  64.340  1.00127.42      B    C  
ANISOU 5944  CG2 VAL B   6    14019  17503  16890   -666    815  -1603  B    C  
ATOM   5945  N   SER B   7     121.163  20.466  67.019  1.00116.69      B    N  
ANISOU 5945  N   SER B   7    12938  15629  15767   -935    940  -1555  B    N  
ATOM   5946  CA  SER B   7     119.808  20.360  67.567  1.00117.97      B    C  
ANISOU 5946  CA  SER B   7    13239  15444  16137   -855    944  -1499  B    C  
ATOM   5947  C   SER B   7     118.975  19.339  66.841  1.00115.41      B    C  
ANISOU 5947  C   SER B   7    12927  14959  15962   -618    824  -1461  B    C  
ATOM   5948  O   SER B   7     119.169  19.109  65.645  1.00130.83      B    O  
ANISOU 5948  O   SER B   7    14853  16958  17898   -542    783  -1475  B    O  
ATOM   5949  CB  SER B   7     119.075  21.676  67.412  1.00125.11      B    C  
ANISOU 5949  CB  SER B   7    14324  16102  17108  -1016   1092  -1452  B    C  
ATOM   5950  OG  SER B   7     119.068  22.081  66.047  1.00125.21      B    O  
ANISOU 5950  OG  SER B   7    14366  16083  17124  -1036   1121  -1443  B    O  
ATOM   5951  N   PRO B   8     118.000  18.748  67.536  1.00104.63      B    N  
ANISOU 5951  N   PRO B   8    11619  13402  14734   -523    760  -1400  B    N  
ATOM   5952  CA  PRO B   8     117.234  17.748  66.800  1.00106.42      B    C  
ANISOU 5952  CA  PRO B   8    11886  13477  15071   -351    615  -1349  B    C  
ATOM   5953  C   PRO B   8     116.414  18.353  65.669  1.00 98.23      B    C  
ANISOU 5953  C   PRO B   8    10904  12274  14144   -390    671  -1281  B    C  
ATOM   5954  O   PRO B   8     116.042  17.648  64.734  1.00 95.51      B    O  
ANISOU 5954  O   PRO B   8    10587  11855  13847   -279    551  -1257  B    O  
ATOM   5955  CB  PRO B   8     116.355  17.099  67.876  1.00112.14      B    C  
ANISOU 5955  CB  PRO B   8    12660  14052  15896   -311    535  -1272  B    C  
ATOM   5956  CG  PRO B   8     117.091  17.349  69.148  1.00112.32      B    C  
ANISOU 5956  CG  PRO B   8    12632  14227  15815   -376    598  -1327  B    C  
ATOM   5957  CD  PRO B   8     117.721  18.707  68.972  1.00105.14      B    C  
ANISOU 5957  CD  PRO B   8    11703  13426  14821   -558    776  -1374  B    C  
ATOM   5958  N   MET B   9     116.141  19.644  65.723  1.00 98.36      B    N  
ANISOU 5958  N   MET B   9    10965  12226  14179   -533    844  -1250  B    N  
ATOM   5959  CA  MET B   9     115.413  20.248  64.611  1.00106.62      B    C  
ANISOU 5959  CA  MET B   9    12068  13135  15309   -539    904  -1182  B    C  
ATOM   5960  C   MET B   9     116.304  20.398  63.401  1.00 98.79      B    C  
ANISOU 5960  C   MET B   9    11046  12270  14219   -555    903  -1260  B    C  
ATOM   5961  O   MET B   9     115.838  20.364  62.263  1.00 96.03      B    O  
ANISOU 5961  O   MET B   9    10717  11838  13931   -499    878  -1220  B    O  
ATOM   5962  CB  MET B   9     114.797  21.590  64.994  1.00115.94      B    C  
ANISOU 5962  CB  MET B   9    13356  14186  16508   -632   1092  -1118  B    C  
ATOM   5963  CG  MET B   9     113.776  21.478  66.128  1.00123.17      B    C  
ANISOU 5963  CG  MET B   9    14283  15004  17512   -585   1108  -1012  B    C  
ATOM   5964  SD  MET B   9     112.282  22.485  65.897  1.00130.90      B    S  
ANISOU 5964  SD  MET B   9    15347  15813  18574   -517   1260   -841  B    S  
ATOM   5965  CE  MET B   9     111.603  21.860  64.343  1.00128.27      B    C  
ANISOU 5965  CE  MET B   9    14935  15449  18351   -436   1136   -754  B    C  
ATOM   5966  N   MET B  10     117.592  20.517  63.660  1.00 95.82      B    N  
ANISOU 5966  N   MET B  10    10603  12126  13676   -632    923  -1358  B    N  
ATOM   5967  CA  MET B  10     118.560  20.582  62.593  1.00 95.98      B    C  
ANISOU 5967  CA  MET B  10    10553  12346  13566   -650    917  -1418  B    C  
ATOM   5968  C   MET B  10     119.018  19.197  62.129  1.00 89.88      B    C  
ANISOU 5968  C   MET B  10     9685  11723  12740   -419    750  -1464  B    C  
ATOM   5969  O   MET B  10     119.311  18.987  60.948  1.00 79.23      B    O  
ANISOU 5969  O   MET B  10     8308  10451  11342   -339    714  -1482  B    O  
ATOM   5970  CB  MET B  10     119.761  21.373  63.064  1.00105.46      B    C  
ANISOU 5970  CB  MET B  10    11706  13791  14571   -868   1008  -1471  B    C  
ATOM   5971  CG  MET B  10     120.799  21.585  61.982  1.00106.03      B    C  
ANISOU 5971  CG  MET B  10    11680  14127  14480   -937   1016  -1503  B    C  
ATOM   5972  SD  MET B  10     120.023  22.294  60.531  1.00104.39      B    S  
ANISOU 5972  SD  MET B  10    11609  13675  14378   -958   1079  -1452  B    S  
ATOM   5973  CE  MET B  10     121.467  22.501  59.506  1.00115.39      B    C  
ANISOU 5973  CE  MET B  10    12853  15459  15531  -1075   1083  -1485  B    C  
ATOM   5974  N   GLN B  11     119.077  18.259  63.068  1.00 89.16      B    N  
ANISOU 5974  N   GLN B  11     9573  11664  12637   -294    648  -1481  B    N  
ATOM   5975  CA  GLN B  11     119.440  16.883  62.766  1.00 95.49      B    C  
ANISOU 5975  CA  GLN B  11    10363  12557  13361    -29    478  -1525  B    C  
ATOM   5976  C   GLN B  11     118.443  16.279  61.788  1.00 90.02      B    C  
ANISOU 5976  C   GLN B  11     9804  11604  12795     90    361  -1478  B    C  
ATOM   5977  O   GLN B  11     118.818  15.534  60.892  1.00 91.52      B    O  
ANISOU 5977  O   GLN B  11    10021  11861  12891    279    258  -1521  B    O  
ATOM   5978  CB  GLN B  11     119.485  16.049  64.057  1.00107.23      B    C  
ANISOU 5978  CB  GLN B  11    11867  14050  14825     73    388  -1537  B    C  
ATOM   5979  CG  GLN B  11     119.730  14.565  63.845  1.00125.98      B    C  
ANISOU 5979  CG  GLN B  11    14319  16444  17100    382    196  -1577  B    C  
ATOM   5980  CD  GLN B  11     121.102  14.265  63.258  1.00143.63      B    C  
ANISOU 5980  CD  GLN B  11    16427  19061  19084    567    194  -1657  B    C  
ATOM   5981  NE2 GLN B  11     121.132  13.758  62.026  1.00151.51      B    N  
ANISOU 5981  NE2 GLN B  11    17496  20039  20029    751    116  -1678  B    N  
ATOM   5982  OE1 GLN B  11     122.127  14.474  63.912  1.00154.45      B    O  
ANISOU 5982  OE1 GLN B  11    17627  20766  20292    551    260  -1689  B    O  
ATOM   5983  N   GLN B  12     117.172  16.615  61.963  1.00 88.50      B    N  
ANISOU 5983  N   GLN B  12     9694  11139  12793    -19    378  -1378  B    N  
ATOM   5984  CA  GLN B  12     116.122  16.132  61.088  1.00 89.44      B    C  
ANISOU 5984  CA  GLN B  12     9920  11031  13029     36    262  -1301  B    C  
ATOM   5985  C   GLN B  12     116.179  16.769  59.715  1.00 86.66      B    C  
ANISOU 5985  C   GLN B  12     9550  10698  12676      9    333  -1302  B    C  
ATOM   5986  O   GLN B  12     115.769  16.155  58.729  1.00 89.46      B    O  
ANISOU 5986  O   GLN B  12     9985  10953  13051    105    208  -1282  B    O  
ATOM   5987  CB  GLN B  12     114.764  16.402  61.700  1.00 94.40      B    C  
ANISOU 5987  CB  GLN B  12    10585  11450  13834    -82    277  -1160  B    C  
ATOM   5988  CG  GLN B  12     113.690  15.488  61.150  1.00106.11      B    C  
ANISOU 5988  CG  GLN B  12    12177  12738  15401    -43     83  -1056  B    C  
ATOM   5989  CD  GLN B  12     112.538  15.282  62.116  1.00116.21      B    C  
ANISOU 5989  CD  GLN B  12    13469  13890  16794   -140     33   -906  B    C  
ATOM   5990  NE2 GLN B  12     111.594  14.409  61.735  1.00124.32      B    N  
ANISOU 5990  NE2 GLN B  12    14597  14768  17870   -163   -168   -789  B    N  
ATOM   5991  OE1 GLN B  12     112.497  15.885  63.195  1.00114.49      B    O  
ANISOU 5991  OE1 GLN B  12    13179  13719  16601   -207    164   -886  B    O  
ATOM   5992  N   TYR B  13     116.684  17.993  59.648  1.00 82.39      B    N  
ANISOU 5992  N   TYR B  13     8934  10273  12097   -135    520  -1324  B    N  
ATOM   5993  CA  TYR B  13     116.927  18.630  58.365  1.00 81.53      B    C  
ANISOU 5993  CA  TYR B  13     8813  10211  11954   -171    590  -1333  B    C  
ATOM   5994  C   TYR B  13     118.011  17.937  57.571  1.00 84.77      B    C  
ANISOU 5994  C   TYR B  13     9164  10851  12191    -20    509  -1425  B    C  
ATOM   5995  O   TYR B  13     117.864  17.710  56.363  1.00 85.00      B    O  
ANISOU 5995  O   TYR B  13     9229  10847  12219     65    457  -1420  B    O  
ATOM   5996  CB  TYR B  13     117.353  20.062  58.551  1.00 81.33      B    C  
ANISOU 5996  CB  TYR B  13     8770  10253  11878   -383    789  -1338  B    C  
ATOM   5997  CG  TYR B  13     117.851  20.667  57.265  1.00 83.23      B    C  
ANISOU 5997  CG  TYR B  13     9001  10583  12037   -438    850  -1354  B    C  
ATOM   5998  CD1 TYR B  13     116.959  21.052  56.279  1.00 87.32      B    C  
ANISOU 5998  CD1 TYR B  13     9601  10910  12666   -426    873  -1282  B    C  
ATOM   5999  CD2 TYR B  13     119.202  20.850  57.028  1.00 83.16      B    C  
ANISOU 5999  CD2 TYR B  13     8885  10884  11828   -509    883  -1423  B    C  
ATOM   6000  CE1 TYR B  13     117.395  21.611  55.092  1.00 87.65      B    C  
ANISOU 6000  CE1 TYR B  13     9645  11024  12631   -478    928  -1292  B    C  
ATOM   6001  CE2 TYR B  13     119.649  21.403  55.841  1.00 84.49      B    C  
ANISOU 6001  CE2 TYR B  13     9039  11152  11912   -579    936  -1422  B    C  
ATOM   6002  CZ  TYR B  13     118.731  21.774  54.877  1.00 86.09      B    C  
ANISOU 6002  CZ  TYR B  13     9352  11118  12239   -560    958  -1363  B    C  
ATOM   6003  OH  TYR B  13     119.110  22.330  53.687  1.00 89.25      B    O  
ANISOU 6003  OH  TYR B  13     9754  11594  12560   -628   1009  -1355  B    O  
ATOM   6004  N   LEU B  14     119.111  17.615  58.247  1.00 88.02      B    N  
ANISOU 6004  N   LEU B  14     9475  11527  12439     27    506  -1498  B    N  
ATOM   6005  CA  LEU B  14     120.233  16.948  57.589  1.00 89.83      B    C  
ANISOU 6005  CA  LEU B  14     9618  12057  12457    222    445  -1571  B    C  
ATOM   6006  C   LEU B  14     119.806  15.579  57.067  1.00 92.71      B    C  
ANISOU 6006  C   LEU B  14    10132  12271  12821    514    247  -1589  B    C  
ATOM   6007  O   LEU B  14     120.388  15.089  56.101  1.00102.78      B    O  
ANISOU 6007  O   LEU B  14    11402  13700  13947    709    194  -1635  B    O  
ATOM   6008  CB  LEU B  14     121.432  16.826  58.532  1.00 89.32      B    C  
ANISOU 6008  CB  LEU B  14     9394  12346  12197    238    475  -1621  B    C  
ATOM   6009  CG  LEU B  14     121.983  18.176  59.005  1.00 90.08      B    C  
ANISOU 6009  CG  LEU B  14     9373  12609  12242    -96    646  -1600  B    C  
ATOM   6010  CD1 LEU B  14     122.839  18.042  60.252  1.00 93.51      B    C  
ANISOU 6010  CD1 LEU B  14     9677  13319  12532   -127    655  -1625  B    C  
ATOM   6011  CD2 LEU B  14     122.769  18.848  57.908  1.00 88.78      B    C  
ANISOU 6011  CD2 LEU B  14     9099  12700  11931   -209    725  -1593  B    C  
ATOM   6012  N   GLY B  15     118.801  14.965  57.698  1.00 89.72      B    N  
ANISOU 6012  N   GLY B  15     9907  11596  12583    535    131  -1548  B    N  
ATOM   6013  CA  GLY B  15     118.260  13.692  57.236  1.00 91.43      B    C  
ANISOU 6013  CA  GLY B  15    10341  11604  12792    748    -87  -1549  B    C  
ATOM   6014  C   GLY B  15     117.614  13.826  55.873  1.00 94.56      B    C  
ANISOU 6014  C   GLY B  15    10818  11847  13261    725   -123  -1507  B    C  
ATOM   6015  O   GLY B  15     117.727  12.928  55.028  1.00103.22      B    O  
ANISOU 6015  O   GLY B  15    12068  12901  14248    938   -271  -1548  B    O  
ATOM   6016  N   ILE B  16     116.944  14.955  55.658  1.00 92.85      B    N  
ANISOU 6016  N   ILE B  16    10521  11546  13211    486     13  -1426  B    N  
ATOM   6017  CA  ILE B  16     116.313  15.253  54.373  1.00 89.87      B    C  
ANISOU 6017  CA  ILE B  16    10190  11049  12907    448      4  -1371  B    C  
ATOM   6018  C   ILE B  16     117.330  15.812  53.410  1.00 90.86      B    C  
ANISOU 6018  C   ILE B  16    10204  11422  12896    485    119  -1439  B    C  
ATOM   6019  O   ILE B  16     117.335  15.437  52.246  1.00 94.77      B    O  
ANISOU 6019  O   ILE B  16    10769  11902  13336    604     42  -1455  B    O  
ATOM   6020  CB  ILE B  16     115.170  16.282  54.510  1.00 86.25      B    C  
ANISOU 6020  CB  ILE B  16     9693  10425  12653    221    115  -1240  B    C  
ATOM   6021  CG1 ILE B  16     113.859  15.583  54.813  1.00 81.60      B    C  
ANISOU 6021  CG1 ILE B  16     9217   9595  12192    187    -49  -1120  B    C  
ATOM   6022  CG2 ILE B  16     114.990  17.092  53.232  1.00 87.28      B    C  
ANISOU 6022  CG2 ILE B  16     9797  10553  12810    167    207  -1206  B    C  
ATOM   6023  CD1 ILE B  16     113.919  14.816  56.104  1.00 83.67      B    C  
ANISOU 6023  CD1 ILE B  16     9528   9827  12433    216   -144  -1134  B    C  
ATOM   6024  N   LYS B  17     118.187  16.708  53.889  1.00 90.95      B    N  
ANISOU 6024  N   LYS B  17    10052  11665  12837    362    291  -1470  B    N  
ATOM   6025  CA  LYS B  17     119.144  17.379  53.014  1.00 94.60      B    C  
ANISOU 6025  CA  LYS B  17    10393  12390  13158    323    406  -1503  B    C  
ATOM   6026  C   LYS B  17     120.112  16.402  52.379  1.00 90.99      B    C  
ANISOU 6026  C   LYS B  17     9903  12191  12475    605    309  -1581  B    C  
ATOM   6027  O   LYS B  17     120.531  16.624  51.251  1.00 83.65      B    O  
ANISOU 6027  O   LYS B  17     8926  11404  11450    640    343  -1588  B    O  
ATOM   6028  CB  LYS B  17     119.920  18.456  53.775  1.00 98.00      B    C  
ANISOU 6028  CB  LYS B  17    10683  13033  13516     89    578  -1507  B    C  
ATOM   6029  CG  LYS B  17     120.964  19.192  52.945  1.00 97.33      B    C  
ANISOU 6029  CG  LYS B  17    10469  13255  13255    -20    684  -1515  B    C  
ATOM   6030  CD  LYS B  17     120.372  19.835  51.704  1.00 94.63      B    C  
ANISOU 6030  CD  LYS B  17    10211  12742  12999    -95    730  -1466  B    C  
ATOM   6031  CE  LYS B  17     121.449  20.539  50.906  1.00 96.62      B    C  
ANISOU 6031  CE  LYS B  17    10342  13311  13056   -229    825  -1463  B    C  
ATOM   6032  NZ  LYS B  17     120.991  20.962  49.560  1.00 95.82      B    N1+
ANISOU 6032  NZ  LYS B  17    10320  13079  13007   -244    848  -1423  B    N1+
ATOM   6033  N   ALA B  18     120.456  15.337  53.108  1.00 95.37      B    N  
ANISOU 6033  N   ALA B  18    10498  12807  12929    824    194  -1635  B    N  
ATOM   6034  CA  ALA B  18     121.385  14.303  52.632  1.00100.74      B    C  
ANISOU 6034  CA  ALA B  18    11183  13740  13350   1177    100  -1709  B    C  
ATOM   6035  C   ALA B  18     120.900  13.570  51.385  1.00103.83      B    C  
ANISOU 6035  C   ALA B  18    11786  13939  13723   1385    -41  -1724  B    C  
ATOM   6036  O   ALA B  18     121.705  13.169  50.563  1.00118.78      B    O  
ANISOU 6036  O   ALA B  18    13651  16085  15396   1632    -55  -1771  B    O  
ATOM   6037  CB  ALA B  18     121.679  13.301  53.736  1.00102.97      B    C  
ANISOU 6037  CB  ALA B  18    11534  14056  13533   1394     -5  -1755  B    C  
ATOM   6038  N   GLN B  19     119.593  13.395  51.240  1.00102.91      B    N  
ANISOU 6038  N   GLN B  19    11875  13407  13817   1281   -149  -1672  B    N  
ATOM   6039  CA  GLN B  19     119.038  12.763  50.041  1.00104.79      B    C  
ANISOU 6039  CA  GLN B  19    12332  13441  14043   1418   -298  -1674  B    C  
ATOM   6040  C   GLN B  19     118.966  13.690  48.819  1.00 99.43      B    C  
ANISOU 6040  C   GLN B  19    11544  12823  13412   1285   -182  -1636  B    C  
ATOM   6041  O   GLN B  19     118.736  13.233  47.707  1.00 93.78      B    O  
ANISOU 6041  O   GLN B  19    10974  12014  12641   1418   -286  -1646  B    O  
ATOM   6042  CB  GLN B  19     117.628  12.275  50.321  1.00107.91      B    C  
ANISOU 6042  CB  GLN B  19    12963  13408  14628   1299   -470  -1598  B    C  
ATOM   6043  CG  GLN B  19     117.494  11.232  51.406  1.00109.10      B    C  
ANISOU 6043  CG  GLN B  19    13301  13417  14733   1411   -630  -1618  B    C  
ATOM   6044  CD  GLN B  19     116.036  11.045  51.757  1.00108.31      B    C  
ANISOU 6044  CD  GLN B  19    13355  12954  14843   1176   -766  -1497  B    C  
ATOM   6045  NE2 GLN B  19     115.741  10.886  53.029  1.00114.71      B    N  
ANISOU 6045  NE2 GLN B  19    14166  13690  15726   1082   -787  -1460  B    N  
ATOM   6046  OE1 GLN B  19     115.181  11.066  50.884  1.00106.10      B    O  
ANISOU 6046  OE1 GLN B  19    13170  12494  14648   1069   -849  -1423  B    O  
ATOM   6047  N   HIS B  20     119.116  14.992  49.038  1.00 98.20      B    N  
ANISOU 6047  N   HIS B  20    11170  12790  13349   1016     21  -1589  B    N  
ATOM   6048  CA  HIS B  20     118.990  15.987  47.972  1.00 97.37      B    C  
ANISOU 6048  CA  HIS B  20    10991  12708  13295    860    139  -1541  B    C  
ATOM   6049  C   HIS B  20     120.153  16.932  48.031  1.00101.02      B    C  
ANISOU 6049  C   HIS B  20    11222  13539  13623    732    326  -1553  B    C  
ATOM   6050  O   HIS B  20     120.006  18.134  48.201  1.00100.90      B    O  
ANISOU 6050  O   HIS B  20    11140  13496  13701    450    475  -1497  B    O  
ATOM   6051  CB  HIS B  20     117.683  16.740  48.116  1.00 95.34      B    C  
ANISOU 6051  CB  HIS B  20    10788  12139  13298    613    177  -1435  B    C  
ATOM   6052  CG  HIS B  20     116.511  15.831  48.208  1.00 91.16      B    C  
ANISOU 6052  CG  HIS B  20    10450  11297  12889    671    -19  -1386  B    C  
ATOM   6053  CD2 HIS B  20     115.854  15.323  49.273  1.00 88.05      B    C  
ANISOU 6053  CD2 HIS B  20    10132  10732  12590    634   -115  -1348  B    C  
ATOM   6054  ND1 HIS B  20     115.939  15.270  47.094  1.00 93.01      B    N  
ANISOU 6054  ND1 HIS B  20    10833  11383  13121    757   -164  -1363  B    N  
ATOM   6055  CE1 HIS B  20     114.958  14.471  47.468  1.00 93.64      B    C  
ANISOU 6055  CE1 HIS B  20    11080  11209  13286    742   -351  -1304  B    C  
ATOM   6056  NE2 HIS B  20     114.883  14.488  48.786  1.00 89.51      B    N  
ANISOU 6056  NE2 HIS B  20    10510  10673  12825    668   -322  -1291  B    N  
ATOM   6057  N   THR B  21     121.325  16.349  47.892  1.00108.45      B    N  
ANISOU 6057  N   THR B  21    12058  14838  14308    950    309  -1617  B    N  
ATOM   6058  CA  THR B  21     122.559  17.077  48.002  1.00114.36      B    C  
ANISOU 6058  CA  THR B  21    12553  16027  14872    825    460  -1607  B    C  
ATOM   6059  C   THR B  21     122.779  18.007  46.813  1.00110.31      B    C  
ANISOU 6059  C   THR B  21    11966  15624  14321    655    566  -1558  B    C  
ATOM   6060  O   THR B  21     123.548  18.950  46.897  1.00111.26      B    O  
ANISOU 6060  O   THR B  21    11917  16019  14335    403    699  -1514  B    O  
ATOM   6061  CB  THR B  21     123.736  16.098  48.133  1.00125.59      B    C  
ANISOU 6061  CB  THR B  21    13854  17869  15996   1160    407  -1664  B    C  
ATOM   6062  CG2 THR B  21     123.552  14.885  47.244  1.00129.53      B    C  
ANISOU 6062  CG2 THR B  21    14545  18272  16394   1569    250  -1721  B    C  
ATOM   6063  OG1 THR B  21     124.935  16.753  47.726  1.00150.89      B    O  
ANISOU 6063  OG1 THR B  21    16782  21577  18971   1055    536  -1623  B    O  
ATOM   6064  N   ASP B  22     122.095  17.756  45.709  1.00113.66      B    N  
ANISOU 6064  N   ASP B  22    12536  15827  14820    766    498  -1553  B    N  
ATOM   6065  CA  ASP B  22     122.280  18.564  44.511  1.00117.15      B    C  
ANISOU 6065  CA  ASP B  22    12927  16365  15218    634    588  -1506  B    C  
ATOM   6066  C   ASP B  22     121.252  19.670  44.379  1.00117.54      B    C  
ANISOU 6066  C   ASP B  22    13092  16059  15507    341    668  -1433  B    C  
ATOM   6067  O   ASP B  22     121.491  20.614  43.638  1.00143.62      B    O  
ANISOU 6067  O   ASP B  22    16359  19440  18768    155    774  -1382  B    O  
ATOM   6068  CB  ASP B  22     122.198  17.697  43.266  1.00118.86      B    C  
ANISOU 6068  CB  ASP B  22    13235  16579  15344    942    475  -1540  B    C  
ATOM   6069  CG  ASP B  22     120.903  16.899  43.206  1.00117.57      B    C  
ANISOU 6069  CG  ASP B  22    13341  15958  15372   1076    305  -1556  B    C  
ATOM   6070  OD1 ASP B  22     120.514  16.343  44.253  1.00112.03      B    O  
ANISOU 6070  OD1 ASP B  22    12723  15091  14751   1118    223  -1579  B    O  
ATOM   6071  OD2 ASP B  22     120.277  16.827  42.126  1.00122.49      B    O1-
ANISOU 6071  OD2 ASP B  22    14088  16400  16051   1118    246  -1535  B    O1-
ATOM   6072  N   LYS B  23     120.129  19.582  45.089  1.00105.45      B    N  
ANISOU 6072  N   LYS B  23    11699  14163  14201    309    620  -1416  B    N  
ATOM   6073  CA  LYS B  23     119.073  20.570  44.938  1.00104.79      B    C  
ANISOU 6073  CA  LYS B  23    11725  13769  14319    107    697  -1332  B    C  
ATOM   6074  C   LYS B  23     118.949  21.479  46.142  1.00111.31      B    C  
ANISOU 6074  C   LYS B  23    12559  14513  15220   -127    816  -1300  B    C  
ATOM   6075  O   LYS B  23     119.420  21.162  47.231  1.00128.41      B    O  
ANISOU 6075  O   LYS B  23    14658  16793  17339   -130    806  -1344  B    O  
ATOM   6076  CB  LYS B  23     117.749  19.880  44.769  1.00107.76      B    C  
ANISOU 6076  CB  LYS B  23    12244  13820  14878    237    558  -1296  B    C  
ATOM   6077  CG  LYS B  23     117.780  18.772  43.761  1.00116.59      B    C  
ANISOU 6077  CG  LYS B  23    13425  14961  15912    483    394  -1339  B    C  
ATOM   6078  CD  LYS B  23     116.864  17.631  44.174  1.00121.06      B    C  
ANISOU 6078  CD  LYS B  23    14142  15277  16575    612    193  -1334  B    C  
ATOM   6079  CE  LYS B  23     117.229  16.397  43.378  1.00130.90      B    C  
ANISOU 6079  CE  LYS B  23    15508  16573  17654    890     17  -1412  B    C  
ATOM   6080  NZ  LYS B  23     116.959  15.129  44.098  1.00140.12      B    N1+
ANISOU 6080  NZ  LYS B  23    16845  17594  18798   1045   -182  -1453  B    N1+
ATOM   6081  N   LEU B  24     118.308  22.622  45.943  1.00111.37      B    N  
ANISOU 6081  N   LEU B  24    12671  14315  15325   -301    931  -1224  B    N  
ATOM   6082  CA  LEU B  24     117.915  23.464  47.054  1.00103.82      B    C  
ANISOU 6082  CA  LEU B  24    11797  13199  14449   -468   1037  -1188  B    C  
ATOM   6083  C   LEU B  24     116.746  22.789  47.777  1.00101.71      B    C  
ANISOU 6083  C   LEU B  24    11568  12705  14371   -331    947  -1154  B    C  
ATOM   6084  O   LEU B  24     115.888  22.166  47.146  1.00 94.10      B    O  
ANISOU 6084  O   LEU B  24    10630  11613  13510   -190    839  -1110  B    O  
ATOM   6085  CB  LEU B  24     117.525  24.852  46.551  1.00100.65      B    C  
ANISOU 6085  CB  LEU B  24    11555  12626  14061   -633   1180  -1112  B    C  
ATOM   6086  CG  LEU B  24     118.665  25.723  45.994  1.00 99.16      B    C  
ANISOU 6086  CG  LEU B  24    11376  12633  13666   -859   1273  -1121  B    C  
ATOM   6087  CD1 LEU B  24     118.095  26.908  45.227  1.00 97.42      B    C  
ANISOU 6087  CD1 LEU B  24    11369  12182  13464   -954   1382  -1041  B    C  
ATOM   6088  CD2 LEU B  24     119.573  26.203  47.129  1.00103.28      B    C  
ANISOU 6088  CD2 LEU B  24    11887  13302  14051  -1094   1334  -1154  B    C  
ATOM   6089  N   VAL B  25     116.733  22.899  49.104  1.00 99.42      B    N  
ANISOU 6089  N   VAL B  25    11279  12388  14108   -398    982  -1163  B    N  
ATOM   6090  CA  VAL B  25     115.656  22.337  49.898  1.00 94.82      B    C  
ANISOU 6090  CA  VAL B  25    10717  11621  13685   -305    908  -1112  B    C  
ATOM   6091  C   VAL B  25     114.945  23.423  50.680  1.00 91.47      B    C  
ANISOU 6091  C   VAL B  25    10392  11024  13338   -408   1054  -1032  B    C  
ATOM   6092  O   VAL B  25     115.514  23.995  51.590  1.00 96.65      B    O  
ANISOU 6092  O   VAL B  25    11077  11724  13920   -535   1148  -1073  B    O  
ATOM   6093  CB  VAL B  25     116.181  21.295  50.884  1.00 95.49      B    C  
ANISOU 6093  CB  VAL B  25    10726  11826  13730   -233    799  -1189  B    C  
ATOM   6094  CG1 VAL B  25     115.051  20.790  51.775  1.00 93.05      B    C  
ANISOU 6094  CG1 VAL B  25    10452  11326  13576   -184    723  -1116  B    C  
ATOM   6095  CG2 VAL B  25     116.847  20.153  50.128  1.00 95.90      B    C  
ANISOU 6095  CG2 VAL B  25    10727  12040  13671    -57    652  -1265  B    C  
ATOM   6096  N   PHE B  26     113.709  23.701  50.284  1.00 93.11      B    N  
ANISOU 6096  N   PHE B  26    10656  11054  13667   -339   1070   -911  B    N  
ATOM   6097  CA  PHE B  26     112.783  24.536  51.039  1.00 92.64      B    C  
ANISOU 6097  CA  PHE B  26    10680  10840  13674   -342   1194   -808  B    C  
ATOM   6098  C   PHE B  26     112.230  23.723  52.207  1.00 98.39      B    C  
ANISOU 6098  C   PHE B  26    11327  11561  14494   -292   1104   -773  B    C  
ATOM   6099  O   PHE B  26     111.311  22.884  52.051  1.00 92.51      B    O  
ANISOU 6099  O   PHE B  26    10507  10786  13853   -209    968   -679  B    O  
ATOM   6100  CB  PHE B  26     111.613  24.955  50.161  1.00 91.58      B    C  
ANISOU 6100  CB  PHE B  26    10584  10593  13617   -240   1225   -664  B    C  
ATOM   6101  CG  PHE B  26     111.891  26.139  49.300  1.00 89.92      B    C  
ANISOU 6101  CG  PHE B  26    10524  10323  13314   -282   1369   -662  B    C  
ATOM   6102  CD1 PHE B  26     113.190  26.488  48.967  1.00 91.18      B    C  
ANISOU 6102  CD1 PHE B  26    10739  10567  13335   -434   1405   -783  B    C  
ATOM   6103  CD2 PHE B  26     110.837  26.886  48.788  1.00 87.88      B    C  
ANISOU 6103  CD2 PHE B  26    10351   9949  13091   -168   1460   -521  B    C  
ATOM   6104  CE1 PHE B  26     113.435  27.583  48.157  1.00 94.35      B    C  
ANISOU 6104  CE1 PHE B  26    11313  10900  13636   -506   1522   -768  B    C  
ATOM   6105  CE2 PHE B  26     111.075  27.974  47.973  1.00 88.13      B    C  
ANISOU 6105  CE2 PHE B  26    10566   9897  13021   -193   1585   -516  B    C  
ATOM   6106  CZ  PHE B  26     112.372  28.323  47.654  1.00 90.76      B    C  
ANISOU 6106  CZ  PHE B  26    10986  10276  13220   -379   1610   -643  B    C  
ATOM   6107  N   TYR B  27     112.798  23.977  53.379  1.00 95.01      B    N  
ANISOU 6107  N   TYR B  27    10923  11164  14010   -372   1171   -840  B    N  
ATOM   6108  CA  TYR B  27     112.388  23.312  54.587  1.00 90.52      B    C  
ANISOU 6108  CA  TYR B  27    10291  10593  13509   -341   1105   -814  B    C  
ATOM   6109  C   TYR B  27     111.352  24.202  55.210  1.00 93.07      B    C  
ANISOU 6109  C   TYR B  27    10684  10800  13877   -303   1246   -685  B    C  
ATOM   6110  O   TYR B  27     111.677  25.292  55.668  1.00 93.91      B    O  
ANISOU 6110  O   TYR B  27    10935  10851  13896   -360   1410   -716  B    O  
ATOM   6111  CB  TYR B  27     113.583  23.183  55.505  1.00 89.00      B    C  
ANISOU 6111  CB  TYR B  27    10083  10519  13212   -437   1113   -949  B    C  
ATOM   6112  CG  TYR B  27     113.479  22.115  56.561  1.00 91.05      B    C  
ANISOU 6112  CG  TYR B  27    10260  10815  13519   -390    988   -959  B    C  
ATOM   6113  CD1 TYR B  27     113.634  20.785  56.245  1.00 91.15      B    C  
ANISOU 6113  CD1 TYR B  27    10207  10882  13541   -299    791   -994  B    C  
ATOM   6114  CD2 TYR B  27     113.272  22.447  57.888  1.00 95.07      B    C  
ANISOU 6114  CD2 TYR B  27    10790  11292  14038   -431   1063   -939  B    C  
ATOM   6115  CE1 TYR B  27     113.567  19.815  57.219  1.00 96.53      B    C  
ANISOU 6115  CE1 TYR B  27    10861  11570  14243   -257    670  -1002  B    C  
ATOM   6116  CE2 TYR B  27     113.202  21.483  58.871  1.00 94.91      B    C  
ANISOU 6116  CE2 TYR B  27    10703  11303  14052   -397    949   -943  B    C  
ATOM   6117  CZ  TYR B  27     113.351  20.174  58.532  1.00 98.37      B    C  
ANISOU 6117  CZ  TYR B  27    11091  11784  14502   -315    750   -974  B    C  
ATOM   6118  OH  TYR B  27     113.285  19.218  59.516  1.00107.31      B    O  
ANISOU 6118  OH  TYR B  27    12204  12921  15648   -280    628   -977  B    O  
ATOM   6119  N   ARG B  28     110.094  23.760  55.202  1.00 93.36      B    N  
ANISOU 6119  N   ARG B  28    10634  10811  14025   -204   1179   -526  B    N  
ATOM   6120  CA  ARG B  28     109.020  24.557  55.782  1.00 91.94      B    C  
ANISOU 6120  CA  ARG B  28    10484  10584  13865   -115   1319   -372  B    C  
ATOM   6121  C   ARG B  28     109.340  24.778  57.240  1.00 96.43      B    C  
ANISOU 6121  C   ARG B  28    11100  11146  14391   -153   1396   -424  B    C  
ATOM   6122  O   ARG B  28     109.474  23.814  57.997  1.00121.08      B    O  
ANISOU 6122  O   ARG B  28    14119  14327  17556   -197   1269   -450  B    O  
ATOM   6123  CB  ARG B  28     107.668  23.856  55.676  1.00 90.79      B    C  
ANISOU 6123  CB  ARG B  28    10173  10498  13825    -41   1204   -166  B    C  
ATOM   6124  CG  ARG B  28     106.525  24.617  56.351  1.00 94.63      B    C  
ANISOU 6124  CG  ARG B  28    10637  11015  14302     91   1355     25  B    C  
ATOM   6125  CD  ARG B  28     105.921  25.747  55.491  1.00 91.97      B    C  
ANISOU 6125  CD  ARG B  28    10381  10652  13909    249   1518    135  B    C  
ATOM   6126  NE  ARG B  28     104.654  25.303  54.910  1.00 94.81      B    N  
ANISOU 6126  NE  ARG B  28    10538  11153  14330    320   1427    370  B    N  
ATOM   6127  CZ  ARG B  28     103.450  25.528  55.441  1.00 95.85      B    C  
ANISOU 6127  CZ  ARG B  28    10537  11432  14447    457   1493    605  B    C  
ATOM   6128  NH1 ARG B  28     103.325  26.245  56.542  1.00102.23      B    N1+
ANISOU 6128  NH1 ARG B  28    11425  12236  15182    580   1669    624  B    N1+
ATOM   6129  NH2 ARG B  28     102.348  25.051  54.863  1.00 92.63      B    N  
ANISOU 6129  NH2 ARG B  28     9910  11205  14079    473   1382    838  B    N  
ATOM   6130  N   MET B  29     109.450  26.036  57.646  1.00 92.57      B    N  
ANISOU 6130  N   MET B  29    10801  10570  13802   -131   1594   -439  B    N  
ATOM   6131  CA  MET B  29     109.689  26.355  59.038  1.00 93.94      B    C  
ANISOU 6131  CA  MET B  29    11054  10723  13915   -162   1675   -482  B    C  
ATOM   6132  C   MET B  29     108.637  27.366  59.491  1.00 96.03      B    C  
ANISOU 6132  C   MET B  29    11445  10914  14127     24   1856   -336  B    C  
ATOM   6133  O   MET B  29     108.821  28.566  59.360  1.00 85.50      B    O  
ANISOU 6133  O   MET B  29    10380   9445  12662     60   2017   -366  B    O  
ATOM   6134  CB  MET B  29     111.098  26.894  59.205  1.00 95.84      B    C  
ANISOU 6134  CB  MET B  29    11461  10932  14018   -347   1723   -669  B    C  
ATOM   6135  CG  MET B  29     111.808  26.435  60.458  1.00 99.39      B    C  
ANISOU 6135  CG  MET B  29    11866  11458  14439   -460   1676   -766  B    C  
ATOM   6136  SD  MET B  29     112.168  24.691  60.328  1.00119.29      B    S  
ANISOU 6136  SD  MET B  29    14107  14147  17067   -474   1435   -811  B    S  
ATOM   6137  CE  MET B  29     113.290  24.401  61.697  1.00123.19      B    C  
ANISOU 6137  CE  MET B  29    14584  14752  17470   -607   1411   -945  B    C  
ATOM   6138  N   GLY B  30     107.513  26.847  59.991  1.00106.64      B    N  
ANISOU 6138  N   GLY B  30    12601  12360  15554    149   1822   -162  B    N  
ATOM   6139  CA  GLY B  30     106.385  27.672  60.419  1.00110.19      B    C  
ANISOU 6139  CA  GLY B  30    13106  12821  15939    384   1992     17  B    C  
ATOM   6140  C   GLY B  30     105.685  28.315  59.234  1.00107.56      B    C  
ANISOU 6140  C   GLY B  30    12811  12478  15578    556   2071    143  B    C  
ATOM   6141  O   GLY B  30     105.214  27.610  58.331  1.00100.97      B    O  
ANISOU 6141  O   GLY B  30    11765  11751  14847    539   1939    240  B    O  
ATOM   6142  N   ASP B  31     105.600  29.645  59.241  1.00105.09      B    N  
ANISOU 6142  N   ASP B  31    12799  12026  15104    728   2279    146  B    N  
ATOM   6143  CA  ASP B  31     104.973  30.368  58.139  1.00107.28      B    C  
ANISOU 6143  CA  ASP B  31    13160  12279  15322    930   2374    262  B    C  
ATOM   6144  C   ASP B  31     106.020  30.781  57.111  1.00109.19      B    C  
ANISOU 6144  C   ASP B  31    13623  12338  15523    764   2360     88  B    C  
ATOM   6145  O   ASP B  31     105.832  31.750  56.377  1.00 99.48      B    O  
ANISOU 6145  O   ASP B  31    12629  10989  14180    910   2482    124  B    O  
ATOM   6146  CB  ASP B  31     104.232  31.602  58.641  1.00111.14      B    C  
ANISOU 6146  CB  ASP B  31    13900  12706  15619   1266   2609    379  B    C  
ATOM   6147  CG  ASP B  31     102.805  31.304  59.075  1.00119.28      B    C  
ANISOU 6147  CG  ASP B  31    14630  14023  16667   1528   2643    656  B    C  
ATOM   6148  OD1 ASP B  31     102.031  30.724  58.290  1.00128.59      B    O  
ANISOU 6148  OD1 ASP B  31    15501  15415  17942   1563   2549    833  B    O  
ATOM   6149  OD2 ASP B  31     102.444  31.654  60.210  1.00123.88      B    O1-
ANISOU 6149  OD2 ASP B  31    15279  14641  17148   1692   2760    713  B    O1-
ATOM   6150  N   PHE B  32     107.114  30.022  57.053  1.00118.81      B    N  
ANISOU 6150  N   PHE B  32    14759  13562  16818    471   2208    -86  B    N  
ATOM   6151  CA  PHE B  32     108.200  30.276  56.108  1.00118.75      B    C  
ANISOU 6151  CA  PHE B  32    14898  13454  16763    280   2177   -240  B    C  
ATOM   6152  C   PHE B  32     108.809  29.001  55.556  1.00117.27      B    C  
ANISOU 6152  C   PHE B  32    14438  13407  16711     95   1968   -321  B    C  
ATOM   6153  O   PHE B  32     108.760  27.944  56.192  1.00128.14      B    O  
ANISOU 6153  O   PHE B  32    15593  14903  18189     48   1840   -324  B    O  
ATOM   6154  CB  PHE B  32     109.321  31.024  56.808  1.00120.04      B    C  
ANISOU 6154  CB  PHE B  32    15369  13472  16769     94   2252   -407  B    C  
ATOM   6155  CG  PHE B  32     108.892  32.326  57.405  1.00120.66      B    C  
ANISOU 6155  CG  PHE B  32    15823  13354  16666    264   2449   -361  B    C  
ATOM   6156  CD1 PHE B  32     108.330  32.372  58.671  1.00120.90      B    C  
ANISOU 6156  CD1 PHE B  32    15859  13402  16673    408   2517   -304  B    C  
ATOM   6157  CD2 PHE B  32     109.048  33.493  56.699  1.00117.75      B    C  
ANISOU 6157  CD2 PHE B  32    15833  12776  16129    296   2562   -372  B    C  
ATOM   6158  CE1 PHE B  32     107.936  33.567  59.213  1.00119.39      B    C  
ANISOU 6158  CE1 PHE B  32    16055  13024  16283    610   2702   -266  B    C  
ATOM   6159  CE2 PHE B  32     108.660  34.691  57.233  1.00113.29      B    C  
ANISOU 6159  CE2 PHE B  32    15689  11994  15360    487   2736   -336  B    C  
ATOM   6160  CZ  PHE B  32     108.099  34.728  58.489  1.00117.80      B    C  
ANISOU 6160  CZ  PHE B  32    16271  12587  15900    661   2810   -284  B    C  
ATOM   6161  N   TYR B  33     109.384  29.106  54.366  1.00104.69      B    N  
ANISOU 6161  N   TYR B  33    12887  11792  15096      7   1934   -384  B    N  
ATOM   6162  CA  TYR B  33     110.281  28.088  53.888  1.00 98.20      B    C  
ANISOU 6162  CA  TYR B  33    11889  11091  14329   -160   1764   -502  B    C  
ATOM   6163  C   TYR B  33     111.663  28.671  54.067  1.00101.77      B    C  
ANISOU 6163  C   TYR B  33    12519  11518  14630   -382   1813   -664  B    C  
ATOM   6164  O   TYR B  33     111.963  29.731  53.546  1.00 94.61      B    O  
ANISOU 6164  O   TYR B  33    11857  10492  13597   -440   1922   -677  B    O  
ATOM   6165  CB  TYR B  33     110.034  27.763  52.424  1.00 93.61      B    C  
ANISOU 6165  CB  TYR B  33    11218  10546  13803   -113   1684   -455  B    C  
ATOM   6166  CG  TYR B  33     108.771  27.010  52.173  1.00 90.10      B    C  
ANISOU 6166  CG  TYR B  33    10568  10172  13493     36   1585   -289  B    C  
ATOM   6167  CD1 TYR B  33     108.680  25.648  52.428  1.00 89.89      B    C  
ANISOU 6167  CD1 TYR B  33    10336  10249  13567     -8   1387   -291  B    C  
ATOM   6168  CD2 TYR B  33     107.661  27.652  51.670  1.00 92.12      B    C  
ANISOU 6168  CD2 TYR B  33    10849  10402  13748    214   1677   -114  B    C  
ATOM   6169  CE1 TYR B  33     107.504  24.952  52.190  1.00 92.64      B    C  
ANISOU 6169  CE1 TYR B  33    10517  10665  14014     66   1270   -116  B    C  
ATOM   6170  CE2 TYR B  33     106.477  26.972  51.437  1.00 95.69      B    C  
ANISOU 6170  CE2 TYR B  33    11082  10975  14301    312   1573     73  B    C  
ATOM   6171  CZ  TYR B  33     106.402  25.627  51.696  1.00 94.29      B    C  
ANISOU 6171  CZ  TYR B  33    10711  10892  14223    210   1363     74  B    C  
ATOM   6172  OH  TYR B  33     105.222  24.973  51.442  1.00 89.77      B    O  
ANISOU 6172  OH  TYR B  33     9945  10440  13723    248   1237    277  B    O  
ATOM   6173  N   GLU B  34     112.495  27.973  54.826  1.00107.00      B    N  
ANISOU 6173  N   GLU B  34    13063  12304  15286   -514   1726   -770  B    N  
ATOM   6174  CA  GLU B  34     113.850  28.413  55.094  1.00101.07      B    C  
ANISOU 6174  CA  GLU B  34    12418  11609  14373   -758   1751   -900  B    C  
ATOM   6175  C   GLU B  34     114.826  27.489  54.366  1.00 97.47      B    C  
ANISOU 6175  C   GLU B  34    11745  11383  13907   -843   1613   -985  B    C  
ATOM   6176  O   GLU B  34     114.482  26.342  54.067  1.00 98.88      B    O  
ANISOU 6176  O   GLU B  34    11717  11645  14207   -703   1481   -971  B    O  
ATOM   6177  CB  GLU B  34     114.100  28.371  56.604  1.00101.16      B    C  
ANISOU 6177  CB  GLU B  34    12448  11638  14350   -825   1768   -945  B    C  
ATOM   6178  CG  GLU B  34     113.219  29.317  57.400  1.00107.25      B    C  
ANISOU 6178  CG  GLU B  34    13461  12197  15089   -717   1916   -870  B    C  
ATOM   6179  CD  GLU B  34     113.628  29.425  58.861  1.00118.02      B    C  
ANISOU 6179  CD  GLU B  34    14890  13569  16380   -819   1941   -929  B    C  
ATOM   6180  OE1 GLU B  34     114.276  28.500  59.377  1.00130.71      B    O  
ANISOU 6180  OE1 GLU B  34    16279  15362  18020   -909   1828  -1000  B    O  
ATOM   6181  OE2 GLU B  34     113.279  30.425  59.517  1.00133.04      B    O1-
ANISOU 6181  OE2 GLU B  34    17080  15290  18177   -786   2075   -904  B    O1-
ATOM   6182  N   LEU B  35     116.029  27.994  54.101  1.00 93.00      B    N  
ANISOU 6182  N   LEU B  35    11242  10925  13166  -1072   1637  -1061  B    N  
ATOM   6183  CA  LEU B  35     117.147  27.196  53.588  1.00 92.13      B    C  
ANISOU 6183  CA  LEU B  35    10911  11108  12984  -1146   1526  -1136  B    C  
ATOM   6184  C   LEU B  35     118.348  27.353  54.486  1.00 94.89      B    C  
ANISOU 6184  C   LEU B  35    11230  11660  13162  -1379   1529  -1208  B    C  
ATOM   6185  O   LEU B  35     118.595  28.433  55.000  1.00 97.42      B    O  
ANISOU 6185  O   LEU B  35    11777  11876  13359  -1593   1625  -1206  B    O  
ATOM   6186  CB  LEU B  35     117.562  27.652  52.204  1.00 93.65      B    C  
ANISOU 6186  CB  LEU B  35    11147  11348  13088  -1226   1545  -1125  B    C  
ATOM   6187  CG  LEU B  35     116.468  27.547  51.150  1.00101.18      B    C  
ANISOU 6187  CG  LEU B  35    12123  12133  14185  -1014   1538  -1048  B    C  
ATOM   6188  CD1 LEU B  35     115.650  28.833  51.054  1.00107.07      B    C  
ANISOU 6188  CD1 LEU B  35    13165  12589  14925  -1011   1683   -966  B    C  
ATOM   6189  CD2 LEU B  35     117.088  27.197  49.814  1.00 96.35      B    C  
ANISOU 6189  CD2 LEU B  35    11397  11700  13512  -1022   1476  -1069  B    C  
ATOM   6190  N   PHE B  36     119.111  26.280  54.660  1.00100.65      B    N  
ANISOU 6190  N   PHE B  36    11699  12684  13857  -1335   1418  -1267  B    N  
ATOM   6191  CA  PHE B  36     120.238  26.263  55.598  1.00101.21      B    C  
ANISOU 6191  CA  PHE B  36    11677  13016  13759  -1526   1406  -1319  B    C  
ATOM   6192  C   PHE B  36     121.584  25.973  54.911  1.00 98.92      B    C  
ANISOU 6192  C   PHE B  36    11174  13143  13265  -1634   1356  -1342  B    C  
ATOM   6193  O   PHE B  36     121.642  25.437  53.811  1.00 98.63      B    O  
ANISOU 6193  O   PHE B  36    11025  13209  13241  -1481   1306  -1340  B    O  
ATOM   6194  CB  PHE B  36     120.001  25.217  56.712  1.00102.57      B    C  
ANISOU 6194  CB  PHE B  36    11713  13227  14029  -1344   1326  -1352  B    C  
ATOM   6195  CG  PHE B  36     118.697  25.381  57.444  1.00101.31      B    C  
ANISOU 6195  CG  PHE B  36    11707  12733  14052  -1231   1369  -1308  B    C  
ATOM   6196  CD1 PHE B  36     118.495  26.447  58.298  1.00102.80      B    C  
ANISOU 6196  CD1 PHE B  36    12114  12748  14194  -1388   1483  -1291  B    C  
ATOM   6197  CD2 PHE B  36     117.683  24.458  57.290  1.00101.50      B    C  
ANISOU 6197  CD2 PHE B  36    11662  12635  14266   -974   1286  -1270  B    C  
ATOM   6198  CE1 PHE B  36     117.305  26.590  58.973  1.00103.06      B    C  
ANISOU 6198  CE1 PHE B  36    12262  12527  14366  -1245   1533  -1236  B    C  
ATOM   6199  CE2 PHE B  36     116.484  24.599  57.961  1.00 98.91      B    C  
ANISOU 6199  CE2 PHE B  36    11428  12069  14081   -882   1323  -1198  B    C  
ATOM   6200  CZ  PHE B  36     116.297  25.661  58.803  1.00 98.75      B    C  
ANISOU 6200  CZ  PHE B  36    11592  11916  14013   -995   1456  -1179  B    C  
ATOM   6201  N   LEU B  37     122.663  26.320  55.604  1.00 99.24      B    N  
ANISOU 6201  N   LEU B  37    11154  13451  13101  -1896   1365  -1354  B    N  
ATOM   6202  CA  LEU B  37     124.035  26.014  55.182  1.00 94.97      B    C  
ANISOU 6202  CA  LEU B  37    10347  13415  12322  -2009   1318  -1347  B    C  
ATOM   6203  C   LEU B  37     124.334  26.577  53.785  1.00 99.19      B    C  
ANISOU 6203  C   LEU B  37    10911  14018  12759  -2135   1349  -1297  B    C  
ATOM   6204  O   LEU B  37     124.087  27.747  53.516  1.00106.02      B    O  
ANISOU 6204  O   LEU B  37    12050  14634  13596  -2387   1425  -1258  B    O  
ATOM   6205  CB  LEU B  37     124.304  24.510  55.294  1.00 89.88      B    C  
ANISOU 6205  CB  LEU B  37     9413  13042  11694  -1654   1213  -1393  B    C  
ATOM   6206  CG  LEU B  37     124.023  23.920  56.691  1.00 91.85      B    C  
ANISOU 6206  CG  LEU B  37     9647  13222  12030  -1533   1173  -1435  B    C  
ATOM   6207  CD1 LEU B  37     123.920  22.405  56.701  1.00 90.16      B    C  
ANISOU 6207  CD1 LEU B  37     9274  13106  11873  -1123   1056  -1481  B    C  
ATOM   6208  CD2 LEU B  37     125.030  24.358  57.752  1.00 94.54      B    C  
ANISOU 6208  CD2 LEU B  37     9900  13859  12161  -1822   1193  -1425  B    C  
ATOM   6209  N   ASP B  38     124.859  25.765  52.886  1.00104.78      B    N  
ANISOU 6209  N   ASP B  38    11366  15049  13395  -1948   1290  -1297  B    N  
ATOM   6210  CA  ASP B  38     125.233  26.282  51.584  1.00109.70      B    C  
ANISOU 6210  CA  ASP B  38    11991  15787  13902  -2081   1319  -1242  B    C  
ATOM   6211  C   ASP B  38     124.017  26.643  50.750  1.00111.58      B    C  
ANISOU 6211  C   ASP B  38    12483  15554  14355  -1957   1358  -1238  B    C  
ATOM   6212  O   ASP B  38     124.074  27.557  49.932  1.00128.70      B    O  
ANISOU 6212  O   ASP B  38    14803  17644  16452  -2167   1414  -1184  B    O  
ATOM   6213  CB  ASP B  38     126.134  25.296  50.864  1.00113.31      B    C  
ANISOU 6213  CB  ASP B  38    12104  16750  14198  -1872   1254  -1238  B    C  
ATOM   6214  CG  ASP B  38     127.445  25.048  51.622  1.00128.02      B    C  
ANISOU 6214  CG  ASP B  38    13676  19174  15790  -2004   1228  -1209  B    C  
ATOM   6215  OD1 ASP B  38     127.910  25.951  52.366  1.00153.56      B    O  
ANISOU 6215  OD1 ASP B  38    16975  22470  18897  -2417   1263  -1163  B    O  
ATOM   6216  OD2 ASP B  38     128.016  23.954  51.492  1.00124.19      B    O1-
ANISOU 6216  OD2 ASP B  38    12913  19078  15196  -1690   1169  -1225  B    O1-
ATOM   6217  N   ASP B  39     122.899  25.971  50.995  1.00106.89      B    N  
ANISOU 6217  N   ASP B  39    11946  14655  14008  -1641   1323  -1278  B    N  
ATOM   6218  CA  ASP B  39     121.650  26.347  50.353  1.00103.96      B    C  
ANISOU 6218  CA  ASP B  39    11798  13865  13836  -1530   1360  -1248  B    C  
ATOM   6219  C   ASP B  39     121.327  27.790  50.648  1.00102.21      B    C  
ANISOU 6219  C   ASP B  39    11891  13354  13589  -1800   1478  -1204  B    C  
ATOM   6220  O   ASP B  39     120.814  28.496  49.770  1.00 97.83      B    O  
ANISOU 6220  O   ASP B  39    11527  12579  13062  -1819   1535  -1156  B    O  
ATOM   6221  CB  ASP B  39     120.487  25.466  50.833  1.00107.58      B    C  
ANISOU 6221  CB  ASP B  39    12262  14076  14538  -1219   1296  -1268  B    C  
ATOM   6222  CG  ASP B  39     120.444  24.149  50.131  1.00108.58      B    C  
ANISOU 6222  CG  ASP B  39    12219  14329  14706   -920   1169  -1301  B    C  
ATOM   6223  OD1 ASP B  39     121.482  23.784  49.551  1.00113.32      B    O  
ANISOU 6223  OD1 ASP B  39    12652  15276  15126   -905   1136  -1325  B    O  
ATOM   6224  OD2 ASP B  39     119.383  23.487  50.146  1.00109.45      B    O1-
ANISOU 6224  OD2 ASP B  39    12377  14205  15002   -705   1095  -1291  B    O1-
ATOM   6225  N   ALA B  40     121.588  28.200  51.894  1.00101.72      B    N  
ANISOU 6225  N   ALA B  40    11912  13273  13462  -1980   1509  -1221  B    N  
ATOM   6226  CA  ALA B  40     121.250  29.543  52.358  1.00115.39      B    C  
ANISOU 6226  CA  ALA B  40    14015  14686  15141  -2206   1612  -1189  B    C  
ATOM   6227  C   ALA B  40     122.100  30.573  51.617  1.00111.91      B    C  
ANISOU 6227  C   ALA B  40    13730  14328  14460  -2570   1647  -1143  B    C  
ATOM   6228  O   ALA B  40     121.613  31.608  51.149  1.00112.61      B    O  
ANISOU 6228  O   ALA B  40    14166  14097  14522  -2652   1724  -1101  B    O  
ATOM   6229  CB  ALA B  40     121.421  29.672  53.884  1.00120.64      B    C  
ANISOU 6229  CB  ALA B  40    14737  15334  15763  -2321   1622  -1223  B    C  
ATOM   6230  N   VAL B  41     123.378  30.282  51.511  1.00112.17      B    N  
ANISOU 6230  N   VAL B  41    13511  14813  14295  -2784   1587  -1138  B    N  
ATOM   6231  CA  VAL B  41     124.284  31.215  50.882  1.00121.58      B    C  
ANISOU 6231  CA  VAL B  41    14817  16151  15225  -3195   1600  -1070  B    C  
ATOM   6232  C   VAL B  41     123.902  31.340  49.405  1.00121.05      B    C  
ANISOU 6232  C   VAL B  41    14795  15986  15212  -3072   1622  -1032  B    C  
ATOM   6233  O   VAL B  41     123.932  32.426  48.834  1.00119.90      B    O  
ANISOU 6233  O   VAL B  41    14963  15650  14943  -3323   1669   -975  B    O  
ATOM   6234  CB  VAL B  41     125.752  30.777  51.083  1.00121.32      B    C  
ANISOU 6234  CB  VAL B  41    14421  16731  14945  -3435   1526  -1042  B    C  
ATOM   6235  CG1 VAL B  41     126.690  31.734  50.369  1.00124.18      B    C  
ANISOU 6235  CG1 VAL B  41    14877  17290  15013  -3909   1525   -941  B    C  
ATOM   6236  CG2 VAL B  41     126.081  30.722  52.577  1.00121.80      B    C  
ANISOU 6236  CG2 VAL B  41    14459  16869  14948  -3567   1503  -1074  B    C  
ATOM   6237  N   GLU B  42     123.500  30.222  48.814  1.00127.53      B    N  
ANISOU 6237  N   GLU B  42    15342  16904  16208  -2682   1579  -1065  B    N  
ATOM   6238  CA  GLU B  42     123.093  30.182  47.413  1.00130.17      B    C  
ANISOU 6238  CA  GLU B  42    15686  17164  16607  -2525   1587  -1035  B    C  
ATOM   6239  C   GLU B  42     121.846  30.989  47.171  1.00123.30      B    C  
ANISOU 6239  C   GLU B  42    15190  15773  15886  -2429   1667  -1009  B    C  
ATOM   6240  O   GLU B  42     121.813  31.824  46.282  1.00117.37      B    O  
ANISOU 6240  O   GLU B  42    14656  14888  15050  -2562   1714   -951  B    O  
ATOM   6241  CB  GLU B  42     122.813  28.739  46.999  1.00135.96      B    C  
ANISOU 6241  CB  GLU B  42    16103  18060  17495  -2108   1505  -1084  B    C  
ATOM   6242  CG  GLU B  42     124.034  28.010  46.484  1.00138.90      B    C  
ANISOU 6242  CG  GLU B  42    16126  18978  17671  -2109   1442  -1082  B    C  
ATOM   6243  CD  GLU B  42     124.440  28.507  45.116  1.00143.33      B    C  
ANISOU 6243  CD  GLU B  42    16697  19666  18096  -2242   1466  -1013  B    C  
ATOM   6244  OE1 GLU B  42     123.585  28.471  44.199  1.00130.65      B    O  
ANISOU 6244  OE1 GLU B  42    15204  17795  16640  -2039   1473  -1012  B    O  
ATOM   6245  OE2 GLU B  42     125.602  28.958  44.975  1.00151.88      B    O1-
ANISOU 6245  OE2 GLU B  42    17671  21126  18909  -2571   1474   -949  B    O1-
ATOM   6246  N   ALA B  43     120.825  30.710  47.972  1.00117.27      B    N  
ANISOU 6246  N   ALA B  43    14490  14744  15325  -2182   1681  -1038  B    N  
ATOM   6247  CA  ALA B  43     119.546  31.345  47.826  1.00116.97      B    C  
ANISOU 6247  CA  ALA B  43    14747  14273  15421  -2010   1762   -996  B    C  
ATOM   6248  C   ALA B  43     119.625  32.824  48.177  1.00124.16      B    C  
ANISOU 6248  C   ALA B  43    16108  14908  16157  -2281   1862   -961  B    C  
ATOM   6249  O   ALA B  43     118.868  33.629  47.641  1.00137.10      B    O  
ANISOU 6249  O   ALA B  43    18055  16230  17805  -2191   1941   -907  B    O  
ATOM   6250  CB  ALA B  43     118.524  30.654  48.714  1.00124.51      B    C  
ANISOU 6250  CB  ALA B  43    15616  15092  16597  -1710   1748  -1013  B    C  
ATOM   6251  N   ALA B  44     120.499  33.195  49.103  1.00125.07      B    N  
ANISOU 6251  N   ALA B  44    16299  15126  16095  -2598   1853   -990  B    N  
ATOM   6252  CA  ALA B  44     120.613  34.608  49.465  1.00137.96      B    C  
ANISOU 6252  CA  ALA B  44    18438  16459  17521  -2886   1925   -961  B    C  
ATOM   6253  C   ALA B  44     121.148  35.409  48.283  1.00137.76      B    C  
ANISOU 6253  C   ALA B  44    18617  16423  17303  -3153   1931   -898  B    C  
ATOM   6254  O   ALA B  44     120.709  36.530  48.043  1.00146.03      B    O  
ANISOU 6254  O   ALA B  44    20148  17086  18248  -3203   2004   -858  B    O  
ATOM   6255  CB  ALA B  44     121.480  34.794  50.709  1.00144.56      B    C  
ANISOU 6255  CB  ALA B  44    19312  17427  18186  -3214   1890   -997  B    C  
ATOM   6256  N   LYS B  45     122.085  34.824  47.547  1.00141.68      B    N  
ANISOU 6256  N   LYS B  45    18754  17346  17731  -3301   1854   -884  B    N  
ATOM   6257  CA  LYS B  45     122.649  35.460  46.350  1.00141.69      B    C  
ANISOU 6257  CA  LYS B  45    18879  17408  17547  -3562   1849   -810  B    C  
ATOM   6258  C   LYS B  45     121.626  35.569  45.224  1.00136.71      B    C  
ANISOU 6258  C   LYS B  45    18363  16508  17072  -3232   1906   -780  B    C  
ATOM   6259  O   LYS B  45     121.448  36.630  44.645  1.00142.00      B    O  
ANISOU 6259  O   LYS B  45    19449  16888  17615  -3361   1956   -723  B    O  
ATOM   6260  CB  LYS B  45     123.843  34.659  45.844  1.00140.91      B    C  
ANISOU 6260  CB  LYS B  45    18293  17905  17339  -3720   1762   -791  B    C  
ATOM   6261  CG  LYS B  45     125.201  35.196  46.281  1.00144.37      B    C  
ANISOU 6261  CG  LYS B  45    18745  18659  17449  -4282   1708   -734  B    C  
ATOM   6262  CD  LYS B  45     126.266  34.098  46.412  1.00143.03      B    C  
ANISOU 6262  CD  LYS B  45    17986  19155  17202  -4302   1629   -730  B    C  
ATOM   6263  CE  LYS B  45     126.144  32.951  45.396  1.00133.08      B    C  
ANISOU 6263  CE  LYS B  45    16310  18164  16088  -3887   1612   -750  B    C  
ATOM   6264  NZ  LYS B  45     126.280  33.357  43.976  1.00124.69      B    N1+
ANISOU 6264  NZ  LYS B  45    15303  17136  14935  -3973   1626   -672  B    N1+
ATOM   6265  N   LEU B  46     120.945  34.466  44.945  1.00129.87      B    N  
ANISOU 6265  N   LEU B  46    17150  15729  16465  -2813   1885   -814  B    N  
ATOM   6266  CA  LEU B  46     120.056  34.351  43.789  1.00121.02      B    C  
ANISOU 6266  CA  LEU B  46    16034  14455  15491  -2507   1911   -777  B    C  
ATOM   6267  C   LEU B  46     118.783  35.161  43.890  1.00120.34      B    C  
ANISOU 6267  C   LEU B  46    16344  13893  15486  -2281   2011   -735  B    C  
ATOM   6268  O   LEU B  46     118.268  35.640  42.891  1.00112.58      B    O  
ANISOU 6268  O   LEU B  46    15535  12734  14504  -2171   2056   -674  B    O  
ATOM   6269  CB  LEU B  46     119.653  32.892  43.604  1.00119.04      B    C  
ANISOU 6269  CB  LEU B  46    15338  14419  15473  -2151   1834   -820  B    C  
ATOM   6270  CG  LEU B  46     120.792  31.919  43.310  1.00122.25      B    C  
ANISOU 6270  CG  LEU B  46    15334  15317  15796  -2231   1737   -859  B    C  
ATOM   6271  CD1 LEU B  46     120.289  30.498  43.277  1.00120.95      B    C  
ANISOU 6271  CD1 LEU B  46    14846  15270  15840  -1850   1651   -913  B    C  
ATOM   6272  CD2 LEU B  46     121.437  32.269  41.991  1.00128.13      B    C  
ANISOU 6272  CD2 LEU B  46    16071  16233  16379  -2396   1735   -802  B    C  
ATOM   6273  N   LEU B  47     118.258  35.289  45.100  1.00130.54      B    N  
ANISOU 6273  N   LEU B  47    17763  15001  16834  -2181   2054   -762  B    N  
ATOM   6274  CA  LEU B  47     116.929  35.855  45.292  1.00139.35      B    C  
ANISOU 6274  CA  LEU B  47    19169  15740  18036  -1859   2156   -709  B    C  
ATOM   6275  C   LEU B  47     116.946  37.286  45.838  1.00138.13      B    C  
ANISOU 6275  C   LEU B  47    19613  15220  17650  -2017   2253   -690  B    C  
ATOM   6276  O   LEU B  47     115.887  37.905  45.986  1.00150.06      B    O  
ANISOU 6276  O   LEU B  47    21426  16415  19172  -1721   2357   -637  B    O  
ATOM   6277  CB  LEU B  47     116.106  34.931  46.215  1.00141.28      B    C  
ANISOU 6277  CB  LEU B  47    19134  16035  18511  -1552   2141   -728  B    C  
ATOM   6278  CG  LEU B  47     115.919  33.494  45.696  1.00133.67      B    C  
ANISOU 6278  CG  LEU B  47    17668  15356  17762  -1363   2027   -741  B    C  
ATOM   6279  CD1 LEU B  47     115.018  32.711  46.649  1.00133.24      B    C  
ANISOU 6279  CD1 LEU B  47    17418  15300  17904  -1101   2005   -735  B    C  
ATOM   6280  CD2 LEU B  47     115.368  33.477  44.273  1.00126.09      B    C  
ANISOU 6280  CD2 LEU B  47    16679  14366  16864  -1192   2025   -670  B    C  
ATOM   6281  N   ASP B  48     118.134  37.803  46.142  1.00125.97      B    N  
ANISOU 6281  N   ASP B  48    18253  13736  15872  -2478   2213   -722  B    N  
ATOM   6282  CA  ASP B  48     118.258  39.096  46.783  1.00126.31      B    C  
ANISOU 6282  CA  ASP B  48    18912  13418  15660  -2685   2272   -716  B    C  
ATOM   6283  C   ASP B  48     117.424  39.121  48.065  1.00132.52      B    C  
ANISOU 6283  C   ASP B  48    19816  14007  16526  -2400   2343   -745  B    C  
ATOM   6284  O   ASP B  48     116.666  40.071  48.317  1.00139.18      B    O  
ANISOU 6284  O   ASP B  48    21163  14454  17262  -2200   2451   -711  B    O  
ATOM   6285  CB  ASP B  48     117.823  40.205  45.831  1.00128.93      B    C  
ANISOU 6285  CB  ASP B  48    19754  13391  15843  -2625   2347   -641  B    C  
ATOM   6286  CG  ASP B  48     118.219  41.599  46.321  1.00144.08      B    C  
ANISOU 6286  CG  ASP B  48    22403  14922  17417  -2939   2374   -635  B    C  
ATOM   6287  OD1 ASP B  48     119.209  41.748  47.075  1.00153.83      B    O  
ANISOU 6287  OD1 ASP B  48    23712  16256  18481  -3384   2297   -676  B    O  
ATOM   6288  OD2 ASP B  48     117.528  42.566  45.954  1.00148.00      B    O1-
ANISOU 6288  OD2 ASP B  48    23435  15008  17790  -2736   2465   -584  B    O1-
ATOM   6289  N   ILE B  49     117.554  38.053  48.858  1.00132.62      B    N  
ANISOU 6289  N   ILE B  49    19368  14309  16711  -2355   2286   -801  B    N  
ATOM   6290  CA  ILE B  49     116.954  37.977  50.189  1.00133.30      B    C  
ANISOU 6290  CA  ILE B  49    19510  14277  16862  -2156   2336   -830  B    C  
ATOM   6291  C   ILE B  49     118.067  38.014  51.239  1.00131.00      B    C  
ANISOU 6291  C   ILE B  49    19246  14116  16410  -2571   2267   -903  B    C  
ATOM   6292  O   ILE B  49     119.193  37.590  50.975  1.00117.63      B    O  
ANISOU 6292  O   ILE B  49    17281  12758  14656  -2916   2163   -926  B    O  
ATOM   6293  CB  ILE B  49     116.100  36.701  50.380  1.00126.65      B    C  
ANISOU 6293  CB  ILE B  49    18141  13640  16338  -1765   2318   -822  B    C  
ATOM   6294  CG1 ILE B  49     116.953  35.447  50.200  1.00120.43      B    C  
ANISOU 6294  CG1 ILE B  49    16811  13282  15665  -1923   2181   -879  B    C  
ATOM   6295  CG2 ILE B  49     114.908  36.699  49.432  1.00125.08      B    C  
ANISOU 6295  CG2 ILE B  49    17917  13330  16277  -1367   2380   -727  B    C  
ATOM   6296  CD1 ILE B  49     116.311  34.204  50.764  1.00122.54      B    C  
ANISOU 6296  CD1 ILE B  49    16656  13714  16187  -1632   2133   -890  B    C  
ATOM   6297  N   THR B  50     117.734  38.494  52.437  1.00129.92      B    N  
ANISOU 6297  N   THR B  50    19413  13750  16197  -2517   2324   -929  B    N  
ATOM   6298  CA  THR B  50     118.728  38.691  53.479  1.00128.66      B    C  
ANISOU 6298  CA  THR B  50    19363  13669  15853  -2926   2260   -989  B    C  
ATOM   6299  C   THR B  50     119.242  37.337  54.006  1.00123.94      B    C  
ANISOU 6299  C   THR B  50    18123  13532  15434  -2958   2164  -1038  B    C  
ATOM   6300  O   THR B  50     118.455  36.433  54.303  1.00122.64      B    O  
ANISOU 6300  O   THR B  50    17618  13450  15527  -2580   2180  -1044  B    O  
ATOM   6301  CB  THR B  50     118.156  39.544  54.636  1.00130.67      B    C  
ANISOU 6301  CB  THR B  50    20142  13536  15971  -2810   2351  -1007  B    C  
ATOM   6302  CG2 THR B  50     117.468  40.800  54.121  1.00132.78      B    C  
ANISOU 6302  CG2 THR B  50    21062  13327  16058  -2638   2461   -955  B    C  
ATOM   6303  OG1 THR B  50     117.184  38.789  55.360  1.00135.81      B    O  
ANISOU 6303  OG1 THR B  50    20491  14242  16869  -2371   2408  -1010  B    O  
ATOM   6304  N   LEU B  51     120.561  37.210  54.113  1.00119.89      B    N  
ANISOU 6304  N   LEU B  51    17461  13331  14759  -3411   2059  -1059  B    N  
ATOM   6305  CA  LEU B  51     121.194  36.027  54.697  1.00120.06      B    C  
ANISOU 6305  CA  LEU B  51    16934  13801  14881  -3451   1968  -1102  B    C  
ATOM   6306  C   LEU B  51     121.456  36.242  56.185  1.00117.93      B    C  
ANISOU 6306  C   LEU B  51    16813  13490  14503  -3612   1959  -1148  B    C  
ATOM   6307  O   LEU B  51     121.845  37.321  56.586  1.00124.82      B    O  
ANISOU 6307  O   LEU B  51    18164  14149  15113  -3947   1964  -1143  B    O  
ATOM   6308  CB  LEU B  51     122.520  35.762  54.010  1.00121.49      B    C  
ANISOU 6308  CB  LEU B  51    16828  14426  14908  -3828   1865  -1076  B    C  
ATOM   6309  CG  LEU B  51     123.331  34.585  54.552  1.00126.51      B    C  
ANISOU 6309  CG  LEU B  51    16908  15579  15581  -3860   1771  -1108  B    C  
ATOM   6310  CD1 LEU B  51     122.685  33.235  54.270  1.00130.39      B    C  
ANISOU 6310  CD1 LEU B  51    16954  16208  16377  -3371   1759  -1141  B    C  
ATOM   6311  CD2 LEU B  51     124.719  34.622  53.978  1.00124.02      B    C  
ANISOU 6311  CD2 LEU B  51    16385  15718  15016  -4285   1686  -1050  B    C  
ATOM   6312  N   THR B  52     121.247  35.218  57.002  1.00114.47      B    N  
ANISOU 6312  N   THR B  52    15998  13242  14251  -3386   1936  -1192  B    N  
ATOM   6313  CA  THR B  52     121.330  35.372  58.442  1.00121.30      B    C  
ANISOU 6313  CA  THR B  52    16996  14046  15044  -3472   1938  -1234  B    C  
ATOM   6314  C   THR B  52     121.850  34.094  59.111  1.00118.43      B    C  
ANISOU 6314  C   THR B  52    16089  14116  14793  -3431   1850  -1273  B    C  
ATOM   6315  O   THR B  52     122.554  33.316  58.481  1.00104.30      B    O  
ANISOU 6315  O   THR B  52    13889  12719  13021  -3479   1771  -1264  B    O  
ATOM   6316  CB  THR B  52     119.956  35.784  59.026  1.00136.15      B    C  
ANISOU 6316  CB  THR B  52    19201  15492  17035  -3087   2062  -1234  B    C  
ATOM   6317  CG2 THR B  52     118.888  34.642  58.909  1.00138.40      B    C  
ANISOU 6317  CG2 THR B  52    19069  15852  17661  -2586   2083  -1217  B    C  
ATOM   6318  OG1 THR B  52     120.123  36.172  60.398  1.00160.51      B    O  
ANISOU 6318  OG1 THR B  52    22524  18476  19986  -3222   2071  -1275  B    O  
ATOM   6319  N   THR B  53     121.476  33.883  60.379  1.00124.10      B    N  
ANISOU 6319  N   THR B  53    16825  14757  15570  -3308   1869  -1311  B    N  
ATOM   6320  CA  THR B  53     121.939  32.751  61.181  1.00126.15      B    C  
ANISOU 6320  CA  THR B  53    16642  15379  15909  -3264   1787  -1348  B    C  
ATOM   6321  C   THR B  53     120.838  32.198  62.094  1.00127.77      B    C  
ANISOU 6321  C   THR B  53    16796  15413  16338  -2877   1833  -1367  B    C  
ATOM   6322  O   THR B  53     120.068  32.953  62.680  1.00143.69      B    O  
ANISOU 6322  O   THR B  53    19182  17076  18337  -2786   1928  -1360  B    O  
ATOM   6323  CB  THR B  53     123.117  33.207  62.069  1.00123.40      B    C  
ANISOU 6323  CB  THR B  53    16378  15229  15278  -3725   1725  -1362  B    C  
ATOM   6324  CG2 THR B  53     123.608  32.105  62.982  1.00125.88      B    C  
ANISOU 6324  CG2 THR B  53    16261  15922  15646  -3663   1649  -1394  B    C  
ATOM   6325  OG1 THR B  53     124.192  33.612  61.236  1.00117.83      B    O  
ANISOU 6325  OG1 THR B  53    15651  14772  14349  -4120   1665  -1315  B    O  
ATOM   6326  N   ARG B  54     120.772  30.885  62.242  1.00124.64      B    N  
ANISOU 6326  N   ARG B  54    15963  15268  16127  -2645   1762  -1381  B    N  
ATOM   6327  CA  ARG B  54     119.970  30.308  63.309  1.00143.86      B    C  
ANISOU 6327  CA  ARG B  54    18324  17610  18723  -2381   1776  -1389  B    C  
ATOM   6328  C   ARG B  54     120.731  29.151  63.930  1.00151.33      B    C  
ANISOU 6328  C   ARG B  54    18881  18933  19682  -2387   1662  -1430  B    C  
ATOM   6329  O   ARG B  54     120.956  28.137  63.284  1.00151.26      B    O  
ANISOU 6329  O   ARG B  54    18552  19157  19762  -2241   1578  -1433  B    O  
ATOM   6330  CB  ARG B  54     118.602  29.833  62.794  1.00154.58      B    C  
ANISOU 6330  CB  ARG B  54    19616  18779  20338  -1981   1811  -1332  B    C  
ATOM   6331  CG  ARG B  54     117.793  28.993  63.784  1.00156.66      B    C  
ANISOU 6331  CG  ARG B  54    19718  19025  20778  -1722   1793  -1314  B    C  
ATOM   6332  CD  ARG B  54     116.473  28.545  63.181  1.00157.04      B    C  
ANISOU 6332  CD  ARG B  54    19683  18938  21046  -1394   1806  -1226  B    C  
ATOM   6333  NE  ARG B  54     115.597  29.680  62.897  1.00162.39      B    N  
ANISOU 6333  NE  ARG B  54    20684  19326  21690  -1297   1949  -1157  B    N  
ATOM   6334  CZ  ARG B  54     114.303  29.578  62.608  1.00167.10      B    C  
ANISOU 6334  CZ  ARG B  54    21254  19803  22431  -1008   1996  -1046  B    C  
ATOM   6335  NH1 ARG B  54     113.705  28.393  62.569  1.00170.56      B    N1+
ANISOU 6335  NH1 ARG B  54    21377  20363  23062   -840   1896   -990  B    N1+
ATOM   6336  NH2 ARG B  54     113.592  30.673  62.374  1.00184.82      B    N  
ANISOU 6336  NH2 ARG B  54    23806  21815  24601   -887   2139   -980  B    N  
ATOM   6337  N   GLY B  55     121.100  29.297  65.196  1.00158.01      B    N  
ANISOU 6337  N   GLY B  55    19783  19828  20425  -2529   1658  -1460  B    N  
ATOM   6338  CA  GLY B  55     121.635  28.179  65.963  1.00153.44      B    C  
ANISOU 6338  CA  GLY B  55    18861  19569  19869  -2466   1560  -1490  B    C  
ATOM   6339  C   GLY B  55     123.063  27.802  65.627  1.00142.98      B    C  
ANISOU 6339  C   GLY B  55    17256  18713  18356  -2677   1467  -1502  B    C  
ATOM   6340  O   GLY B  55     123.734  28.464  64.840  1.00112.13      B    O  
ANISOU 6340  O   GLY B  55    13411  14911  14282  -2941   1471  -1478  B    O  
ATOM   6341  N   GLN B  56     123.509  26.711  66.240  1.00152.82      B    N  
ANISOU 6341  N   GLN B  56    18190  20259  19613  -2542   1382  -1523  B    N  
ATOM   6342  CA  GLN B  56     124.879  26.255  66.115  1.00154.58      B    C  
ANISOU 6342  CA  GLN B  56    18101  21005  19627  -2680   1298  -1518  B    C  
ATOM   6343  C   GLN B  56     124.973  24.785  65.708  1.00151.30      B    C  
ANISOU 6343  C   GLN B  56    17349  20833  19304  -2296   1210  -1533  B    C  
ATOM   6344  O   GLN B  56     124.206  23.938  66.190  1.00171.81      B    O  
ANISOU 6344  O   GLN B  56    19926  23261  22091  -1988   1177  -1556  B    O  
ATOM   6345  CB  GLN B  56     125.578  26.431  67.450  1.00161.31      B    C  
ANISOU 6345  CB  GLN B  56    18927  22059  20304  -2909   1273  -1525  B    C  
ATOM   6346  CG  GLN B  56     125.309  27.765  68.114  1.00168.01      B    C  
ANISOU 6346  CG  GLN B  56    20190  22580  21065  -3230   1348  -1527  B    C  
ATOM   6347  CD  GLN B  56     126.548  28.327  68.765  1.00179.03      B    C  
ANISOU 6347  CD  GLN B  56    21567  24310  22144  -3684   1298  -1500  B    C  
ATOM   6348  NE2 GLN B  56     126.738  29.637  68.648  1.00186.90      B    N  
ANISOU 6348  NE2 GLN B  56    22934  25121  22957  -4090   1331  -1479  B    N  
ATOM   6349  OE1 GLN B  56     127.333  27.590  69.364  1.00180.12      B    O  
ANISOU 6349  OE1 GLN B  56    21377  24877  22182  -3674   1223  -1493  B    O  
ATOM   6350  N   MET B  57     125.927  24.492  64.831  1.00133.19      B    N  
ANISOU 6350  N   MET B  57    14815  18941  16850  -2319   1165  -1509  B    N  
ATOM   6351  CA  MET B  57     126.203  23.124  64.429  1.00125.51      B    C  
ANISOU 6351  CA  MET B  57    13559  18241  15889  -1939   1079  -1524  B    C  
ATOM   6352  C   MET B  57     127.691  22.892  64.528  1.00122.15      B    C  
ANISOU 6352  C   MET B  57    12809  18452  15151  -2049   1034  -1485  B    C  
ATOM   6353  O   MET B  57     128.474  23.499  63.797  1.00116.24      B    O  
ANISOU 6353  O   MET B  57    11970  17990  14206  -2309   1053  -1426  B    O  
ATOM   6354  CB  MET B  57     125.751  22.861  63.000  1.00132.50      B    C  
ANISOU 6354  CB  MET B  57    14460  18999  16881  -1740   1074  -1522  B    C  
ATOM   6355  CG  MET B  57     125.908  21.402  62.599  1.00140.18      B    C  
ANISOU 6355  CG  MET B  57    15230  20170  17859  -1304    972  -1550  B    C  
ATOM   6356  SD  MET B  57     125.374  21.007  60.923  1.00139.06      B    S  
ANISOU 6356  SD  MET B  57    15135  19874  17828  -1060    947  -1554  B    S  
ATOM   6357  CE  MET B  57     126.746  21.637  59.983  1.00140.94      B    C  
ANISOU 6357  CE  MET B  57    15154  20634  17761  -1302    991  -1497  B    C  
ATOM   6358  N   ASP B  58     128.071  22.007  65.444  1.00124.80      B    N  
ANISOU 6358  N   ASP B  58    12963  19027  15424  -1848    972  -1501  B    N  
ATOM   6359  CA  ASP B  58     129.477  21.748  65.754  1.00118.27      B    C  
ANISOU 6359  CA  ASP B  58    11795  18863  14275  -1921    932  -1446  B    C  
ATOM   6360  C   ASP B  58     130.187  23.033  66.124  1.00119.31      B    C  
ANISOU 6360  C   ASP B  58    11949  19186  14196  -2498    969  -1376  B    C  
ATOM   6361  O   ASP B  58     131.295  23.266  65.702  1.00113.22      B    O  
ANISOU 6361  O   ASP B  58    10927  18948  13142  -2711    954  -1288  B    O  
ATOM   6362  CB  ASP B  58     130.172  21.074  64.578  1.00112.27      B    C  
ANISOU 6362  CB  ASP B  58    10769  18529  13359  -1667    900  -1411  B    C  
ATOM   6363  CG  ASP B  58     129.675  19.671  64.345  1.00112.31      B    C  
ANISOU 6363  CG  ASP B  58    10775  18408  13491  -1085    831  -1477  B    C  
ATOM   6364  OD1 ASP B  58     129.825  18.840  65.268  1.00111.94      B    O  
ANISOU 6364  OD1 ASP B  58    10654  18473  13405   -837    774  -1500  B    O  
ATOM   6365  OD2 ASP B  58     129.124  19.403  63.253  1.00110.34      B    O1-
ANISOU 6365  OD2 ASP B  58    10628  17928  13366   -886    825  -1504  B    O1-
ATOM   6366  N   GLY B  59     129.525  23.873  66.915  1.00133.38      B    N  
ANISOU 6366  N   GLY B  59    14053  20531  16096  -2755   1013  -1408  B    N  
ATOM   6367  CA  GLY B  59     130.118  25.134  67.383  1.00145.62      B    C  
ANISOU 6367  CA  GLY B  59    15731  22168  17427  -3327   1031  -1352  B    C  
ATOM   6368  C   GLY B  59     129.930  26.336  66.461  1.00149.03      B    C  
ANISOU 6368  C   GLY B  59    16451  22339  17834  -3675   1084  -1322  B    C  
ATOM   6369  O   GLY B  59     129.990  27.480  66.911  1.00153.57      B    O  
ANISOU 6369  O   GLY B  59    17326  22727  18295  -4113   1103  -1304  B    O  
ATOM   6370  N   VAL B  60     129.676  26.081  65.181  1.00143.11      B    N  
ANISOU 6370  N   VAL B  60    15650  21544  17178  -3469   1102  -1320  B    N  
ATOM   6371  CA  VAL B  60     129.586  27.131  64.173  1.00132.39      B    C  
ANISOU 6371  CA  VAL B  60    14532  19993  15776  -3768   1148  -1281  B    C  
ATOM   6372  C   VAL B  60     128.161  27.621  63.964  1.00142.55      B    C  
ANISOU 6372  C   VAL B  60    16244  20568  17349  -3625   1228  -1348  B    C  
ATOM   6373  O   VAL B  60     127.220  26.803  63.925  1.00159.96      B    O  
ANISOU 6373  O   VAL B  60    18428  22523  19825  -3178   1239  -1407  B    O  
ATOM   6374  CB  VAL B  60     130.070  26.584  62.839  1.00125.60      B    C  
ANISOU 6374  CB  VAL B  60    13377  19491  14855  -3598   1129  -1233  B    C  
ATOM   6375  CG1 VAL B  60     129.864  27.606  61.739  1.00124.14      B    C  
ANISOU 6375  CG1 VAL B  60    13453  19063  14651  -3866   1177  -1195  B    C  
ATOM   6376  CG2 VAL B  60     131.513  26.165  62.979  1.00127.53      B    C  
ANISOU 6376  CG2 VAL B  60    13171  20515  14767  -3723   1063  -1136  B    C  
ATOM   6377  N   PRO B  61     127.988  28.952  63.827  1.00137.45      B    N  
ANISOU 6377  N   PRO B  61    16002  19603  16618  -4001   1278  -1326  B    N  
ATOM   6378  CA  PRO B  61     126.654  29.464  63.552  1.00135.62      B    C  
ANISOU 6378  CA  PRO B  61    16164  18743  16619  -3824   1367  -1370  B    C  
ATOM   6379  C   PRO B  61     126.149  28.945  62.230  1.00130.86      B    C  
ANISOU 6379  C   PRO B  61    15442  18084  16195  -3504   1383  -1368  B    C  
ATOM   6380  O   PRO B  61     126.877  28.967  61.245  1.00119.95      B    O  
ANISOU 6380  O   PRO B  61    13897  17003  14674  -3633   1354  -1318  B    O  
ATOM   6381  CB  PRO B  61     126.862  30.978  63.503  1.00133.68      B    C  
ANISOU 6381  CB  PRO B  61    16372  18260  16156  -4306   1399  -1332  B    C  
ATOM   6382  CG  PRO B  61     127.964  31.203  64.460  1.00134.38      B    C  
ANISOU 6382  CG  PRO B  61    16384  18707  15966  -4716   1324  -1300  B    C  
ATOM   6383  CD  PRO B  61     128.889  30.027  64.268  1.00132.95      B    C  
ANISOU 6383  CD  PRO B  61    15603  19182  15728  -4588   1247  -1263  B    C  
ATOM   6384  N   ILE B  62     124.912  28.465  62.230  1.00132.07      B    N  
ANISOU 6384  N   ILE B  62    15665  17877  16637  -3101   1420  -1412  B    N  
ATOM   6385  CA  ILE B  62     124.305  27.892  61.039  1.00124.49      B    C  
ANISOU 6385  CA  ILE B  62    14607  16833  15860  -2783   1420  -1409  B    C  
ATOM   6386  C   ILE B  62     123.755  29.024  60.180  1.00115.04      B    C  
ANISOU 6386  C   ILE B  62    13761  15281  14668  -2910   1504  -1376  B    C  
ATOM   6387  O   ILE B  62     122.944  29.833  60.646  1.00111.75      B    O  
ANISOU 6387  O   ILE B  62    13702  14452  14303  -2925   1584  -1377  B    O  
ATOM   6388  CB  ILE B  62     123.159  26.920  61.409  1.00123.47      B    C  
ANISOU 6388  CB  ILE B  62    14421  16475  16016  -2349   1405  -1443  B    C  
ATOM   6389  CG1 ILE B  62     123.679  25.741  62.249  1.00124.34      B    C  
ANISOU 6389  CG1 ILE B  62    14230  16902  16110  -2193   1312  -1477  B    C  
ATOM   6390  CG2 ILE B  62     122.434  26.432  60.165  1.00117.07      B    C  
ANISOU 6390  CG2 ILE B  62    13567  15533  15380  -2069   1393  -1427  B    C  
ATOM   6391  CD1 ILE B  62     122.600  24.749  62.666  1.00121.13      B    C  
ANISOU 6391  CD1 ILE B  62    13796  16272  15954  -1819   1272  -1496  B    C  
ATOM   6392  N   LYS B  63     124.189  29.073  58.927  1.00111.35      B    N  
ANISOU 6392  N   LYS B  63    13200  14976  14130  -2968   1489  -1341  B    N  
ATOM   6393  CA  LYS B  63     123.687  30.085  58.000  1.00115.74      B    C  
ANISOU 6393  CA  LYS B  63    14084  15206  14685  -3062   1562  -1304  B    C  
ATOM   6394  C   LYS B  63     122.275  29.780  57.540  1.00113.76      B    C  
ANISOU 6394  C   LYS B  63    13912  14592  14718  -2655   1608  -1308  B    C  
ATOM   6395  O   LYS B  63     121.904  28.624  57.401  1.00114.17      B    O  
ANISOU 6395  O   LYS B  63    13694  14739  14945  -2334   1550  -1329  B    O  
ATOM   6396  CB  LYS B  63     124.639  30.264  56.816  1.00113.49      B    C  
ANISOU 6396  CB  LYS B  63    13668  15237  14216  -3284   1529  -1252  B    C  
ATOM   6397  CG  LYS B  63     125.730  31.267  57.173  1.00122.98      B    C  
ANISOU 6397  CG  LYS B  63    15021  16610  15092  -3832   1514  -1202  B    C  
ATOM   6398  CD  LYS B  63     126.725  31.520  56.072  1.00121.66      B    C  
ANISOU 6398  CD  LYS B  63    14716  16805  14703  -4117   1477  -1121  B    C  
ATOM   6399  CE  LYS B  63     127.911  30.596  56.225  1.00121.63      B    C  
ANISOU 6399  CE  LYS B  63    14194  17477  14544  -4147   1394  -1089  B    C  
ATOM   6400  NZ  LYS B  63     128.763  30.602  55.010  1.00122.41      B    N1+
ANISOU 6400  NZ  LYS B  63    14066  17991  14453  -4302   1366   -999  B    N1+
ATOM   6401  N   MET B  64     121.473  30.821  57.351  1.00115.88      B    N  
ANISOU 6401  N   MET B  64    14573  14449  15005  -2670   1704  -1279  B    N  
ATOM   6402  CA  MET B  64     120.055  30.641  57.064  1.00120.77      B    C  
ANISOU 6402  CA  MET B  64    15265  14754  15867  -2293   1757  -1254  B    C  
ATOM   6403  C   MET B  64     119.544  31.739  56.137  1.00117.54      B    C  
ANISOU 6403  C   MET B  64    15206  14042  15412  -2316   1849  -1201  B    C  
ATOM   6404  O   MET B  64     120.032  32.860  56.167  1.00122.45      B    O  
ANISOU 6404  O   MET B  64    16169  14541  15815  -2616   1893  -1193  B    O  
ATOM   6405  CB  MET B  64     119.239  30.622  58.380  1.00122.07      B    C  
ANISOU 6405  CB  MET B  64    15534  14714  16130  -2134   1803  -1261  B    C  
ATOM   6406  CG  MET B  64     117.759  30.272  58.221  1.00124.41      B    C  
ANISOU 6406  CG  MET B  64    15817  14787  16665  -1746   1841  -1203  B    C  
ATOM   6407  SD  MET B  64     116.630  31.688  58.081  1.00120.25      B    S  
ANISOU 6407  SD  MET B  64    15766  13823  16096  -1623   2009  -1126  B    S  
ATOM   6408  CE  MET B  64     116.275  31.937  59.829  1.00138.33      B    C  
ANISOU 6408  CE  MET B  64    18213  15992  18352  -1582   2070  -1139  B    C  
ATOM   6409  N   ALA B  65     118.547  31.399  55.331  1.00112.28      B    N  
ANISOU 6409  N   ALA B  65    14476  13251  14935  -2002   1866  -1157  B    N  
ATOM   6410  CA  ALA B  65     117.776  32.382  54.592  1.00112.53      B    C  
ANISOU 6410  CA  ALA B  65    14840  12964  14951  -1916   1967  -1092  B    C  
ATOM   6411  C   ALA B  65     116.391  31.821  54.287  1.00111.33      B    C  
ANISOU 6411  C   ALA B  65    14558  12700  15040  -1508   1984  -1025  B    C  
ATOM   6412  O   ALA B  65     116.218  30.613  54.195  1.00116.92      B    O  
ANISOU 6412  O   ALA B  65    14912  13597  15915  -1355   1885  -1031  B    O  
ATOM   6413  CB  ALA B  65     118.493  32.756  53.322  1.00108.78      B    C  
ANISOU 6413  CB  ALA B  65    14402  12579  14349  -2119   1947  -1079  B    C  
ATOM   6414  N   GLY B  66     115.393  32.686  54.169  1.00112.49      B    N  
ANISOU 6414  N   GLY B  66    15004  12552  15182  -1326   2102   -949  B    N  
ATOM   6415  CA  GLY B  66     114.028  32.211  53.990  1.00116.70      B    C  
ANISOU 6415  CA  GLY B  66    15390  13035  15917   -959   2119   -852  B    C  
ATOM   6416  C   GLY B  66     113.112  33.108  53.175  1.00113.11      B    C  
ANISOU 6416  C   GLY B  66    15191  12355  15429   -752   2233   -746  B    C  
ATOM   6417  O   GLY B  66     113.470  34.215  52.790  1.00 98.97      B    O  
ANISOU 6417  O   GLY B  66    13777  10377  13451   -872   2312   -756  B    O  
ATOM   6418  N   VAL B  67     111.906  32.594  52.937  1.00115.50      B    N  
ANISOU 6418  N   VAL B  67    15291  12690  15901   -443   2231   -632  B    N  
ATOM   6419  CA  VAL B  67     110.870  33.298  52.211  1.00110.89      B    C  
ANISOU 6419  CA  VAL B  67    14874  11962  15298   -176   2337   -499  B    C  
ATOM   6420  C   VAL B  67     109.536  32.963  52.846  1.00110.21      B    C  
ANISOU 6420  C   VAL B  67    14619  11930  15323    141   2375   -358  B    C  
ATOM   6421  O   VAL B  67     109.377  31.890  53.454  1.00110.46      B    O  
ANISOU 6421  O   VAL B  67    14326  12139  15504    129   2268   -355  B    O  
ATOM   6422  CB  VAL B  67     110.818  32.865  50.737  1.00109.31      B    C  
ANISOU 6422  CB  VAL B  67    14490  11859  15184   -163   2257   -464  B    C  
ATOM   6423  CG1 VAL B  67     112.128  33.190  50.058  1.00105.68      B    C  
ANISOU 6423  CG1 VAL B  67    14162  11394  14596   -474   2224   -580  B    C  
ATOM   6424  CG2 VAL B  67     110.508  31.369  50.622  1.00111.12      B    C  
ANISOU 6424  CG2 VAL B  67    14262  12328  15628   -117   2091   -444  B    C  
ATOM   6425  N   PRO B  68     108.564  33.868  52.712  1.00107.09      B    N  
ANISOU 6425  N   PRO B  68    14447  11403  14837    435   2524   -226  B    N  
ATOM   6426  CA  PRO B  68     107.244  33.589  53.273  1.00115.56      B    C  
ANISOU 6426  CA  PRO B  68    15321  12600  15985    751   2569    -51  B    C  
ATOM   6427  C   PRO B  68     106.446  32.624  52.411  1.00109.58      B    C  
ANISOU 6427  C   PRO B  68    14149  12074  15411    843   2449     87  B    C  
ATOM   6428  O   PRO B  68     106.603  32.623  51.197  1.00105.21      B    O  
ANISOU 6428  O   PRO B  68    13585  11512  14876    803   2404     84  B    O  
ATOM   6429  CB  PRO B  68     106.577  34.958  53.290  1.00119.91      B    C  
ANISOU 6429  CB  PRO B  68    16278  12956  16324   1066   2777     47  B    C  
ATOM   6430  CG  PRO B  68     107.261  35.701  52.193  1.00115.87      B    C  
ANISOU 6430  CG  PRO B  68    16083  12245  15696    940   2797    -30  B    C  
ATOM   6431  CD  PRO B  68     108.676  35.234  52.196  1.00106.30      B    C  
ANISOU 6431  CD  PRO B  68    14828  11039  14520    496   2663   -225  B    C  
ATOM   6432  N   PHE B  69     105.608  31.810  53.053  1.00106.29      B    N  
ANISOU 6432  N   PHE B  69    13409  11862  15112    941   2388    212  B    N  
ATOM   6433  CA  PHE B  69     104.767  30.849  52.355  1.00102.51      B    C  
ANISOU 6433  CA  PHE B  69    12555  11609  14783    986   2247    369  B    C  
ATOM   6434  C   PHE B  69     103.907  31.519  51.297  1.00107.85      B    C  
ANISOU 6434  C   PHE B  69    13270  12313  15395   1238   2338    540  B    C  
ATOM   6435  O   PHE B  69     103.721  30.955  50.219  1.00108.77      B    O  
ANISOU 6435  O   PHE B  69    13200  12526  15600   1181   2213    590  B    O  
ATOM   6436  CB  PHE B  69     103.863  30.107  53.339  1.00 99.95      B    C  
ANISOU 6436  CB  PHE B  69    11937  11498  14541   1055   2192    524  B    C  
ATOM   6437  CG  PHE B  69     103.018  29.054  52.697  1.00 98.52      B    C  
ANISOU 6437  CG  PHE B  69    11391  11551  14489   1026   2011    698  B    C  
ATOM   6438  CD1 PHE B  69     101.821  29.372  52.065  1.00 99.25      B    C  
ANISOU 6438  CD1 PHE B  69    11351  11814  14543   1256   2063    948  B    C  
ATOM   6439  CD2 PHE B  69     103.426  27.745  52.718  1.00103.97      B    C  
ANISOU 6439  CD2 PHE B  69    11894  12292  15317    770   1779    619  B    C  
ATOM   6440  CE1 PHE B  69     101.043  28.391  51.470  1.00 99.04      B    C  
ANISOU 6440  CE1 PHE B  69    10994  12017  14616   1175   1872   1124  B    C  
ATOM   6441  CE2 PHE B  69     102.655  26.758  52.127  1.00109.61      B    C  
ANISOU 6441  CE2 PHE B  69    12336  13186  16124    705   1585    779  B    C  
ATOM   6442  CZ  PHE B  69     101.459  27.078  51.503  1.00103.86      B    C  
ANISOU 6442  CZ  PHE B  69    11462  12637  15361    880   1624   1037  B    C  
ATOM   6443  N   HIS B  70     103.375  32.705  51.612  1.00114.55      B    N  
ANISOU 6443  N   HIS B  70    14378  13076  16067   1537   2552    633  B    N  
ATOM   6444  CA  HIS B  70     102.438  33.396  50.715  1.00120.64      B    C  
ANISOU 6444  CA  HIS B  70    15188  13905  16741   1855   2661    826  B    C  
ATOM   6445  C   HIS B  70     103.074  33.849  49.405  1.00115.87      B    C  
ANISOU 6445  C   HIS B  70    14803  13119  16100   1768   2654    726  B    C  
ATOM   6446  O   HIS B  70     102.365  34.149  48.460  1.00120.27      B    O  
ANISOU 6446  O   HIS B  70    15320  13757  16620   1976   2691    879  B    O  
ATOM   6447  CB  HIS B  70     101.771  34.598  51.405  1.00126.99      B    C  
ANISOU 6447  CB  HIS B  70    16281  14648  17320   2257   2903    941  B    C  
ATOM   6448  CG  HIS B  70     102.688  35.775  51.624  1.00134.97      B    C  
ANISOU 6448  CG  HIS B  70    17879  15267  18134   2244   3042    749  B    C  
ATOM   6449  CD2 HIS B  70     103.261  36.255  52.755  1.00134.79      B    C  
ANISOU 6449  CD2 HIS B  70    18172  15044  17997   2189   3120    613  B    C  
ATOM   6450  ND1 HIS B  70     103.093  36.619  50.607  1.00138.08      B    N  
ANISOU 6450  ND1 HIS B  70    18633  15425  18405   2264   3101    690  B    N  
ATOM   6451  CE1 HIS B  70     103.884  37.561  51.099  1.00129.72      B    C  
ANISOU 6451  CE1 HIS B  70    18102  14031  17157   2195   3198    531  B    C  
ATOM   6452  NE2 HIS B  70     104.005  37.360  52.401  1.00129.84      B    N  
ANISOU 6452  NE2 HIS B  70    18099  14061  17172   2148   3210    479  B    N  
ATOM   6453  N   ALA B  71     104.400  33.900  49.358  1.00113.47      B    N  
ANISOU 6453  N   ALA B  71    14713  12605  15794   1458   2607    486  B    N  
ATOM   6454  CA  ALA B  71     105.120  34.288  48.142  1.00117.95      B    C  
ANISOU 6454  CA  ALA B  71    15476  13023  16315   1325   2590    390  B    C  
ATOM   6455  C   ALA B  71     106.114  33.212  47.694  1.00118.77      B    C  
ANISOU 6455  C   ALA B  71    15351  13205  16570    962   2389    232  B    C  
ATOM   6456  O   ALA B  71     107.114  33.499  47.027  1.00118.42      B    O  
ANISOU 6456  O   ALA B  71    15485  13043  16465    757   2372     98  B    O  
ATOM   6457  CB  ALA B  71     105.858  35.584  48.393  1.00123.62      B    C  
ANISOU 6457  CB  ALA B  71    16740  13419  16809   1294   2739    271  B    C  
ATOM   6458  N   ALA B  72     105.850  31.970  48.073  1.00111.36      B    N  
ANISOU 6458  N   ALA B  72    14035  12474  15801    888   2234    258  B    N  
ATOM   6459  CA  ALA B  72     106.794  30.914  47.809  1.00103.16      B    C  
ANISOU 6459  CA  ALA B  72    12819  11505  14869    606   2050    104  B    C  
ATOM   6460  C   ALA B  72     106.794  30.590  46.335  1.00100.53      B    C  
ANISOU 6460  C   ALA B  72    12393  11225  14577    584   1954    125  B    C  
ATOM   6461  O   ALA B  72     107.838  30.350  45.768  1.00 99.08      B    O  
ANISOU 6461  O   ALA B  72    12241  11025  14380    390   1885    -23  B    O  
ATOM   6462  CB  ALA B  72     106.452  29.676  48.626  1.00109.29      B    C  
ANISOU 6462  CB  ALA B  72    13288  12449  15788    556   1901    132  B    C  
ATOM   6463  N   GLU B  73     105.620  30.554  45.716  1.00108.34      B    N  
ANISOU 6463  N   GLU B  73    13247  12312  15604    784   1947    321  B    N  
ATOM   6464  CA  GLU B  73     105.521  30.187  44.309  1.00115.61      B    C  
ANISOU 6464  CA  GLU B  73    14067  13294  16566    766   1842    356  B    C  
ATOM   6465  C   GLU B  73     106.230  31.242  43.474  1.00121.20      B    C  
ANISOU 6465  C   GLU B  73    15079  13829  17141    750   1964    273  B    C  
ATOM   6466  O   GLU B  73     106.748  30.946  42.394  1.00125.43      B    O  
ANISOU 6466  O   GLU B  73    15588  14382  17687    640   1878    209  B    O  
ATOM   6467  CB  GLU B  73     104.058  30.025  43.860  1.00121.97      B    C  
ANISOU 6467  CB  GLU B  73    14660  14271  17410    974   1813    614  B    C  
ATOM   6468  CG  GLU B  73     103.515  28.593  43.917  1.00128.51      B    C  
ANISOU 6468  CG  GLU B  73    15154  15297  18376    860   1574    695  B    C  
ATOM   6469  CD  GLU B  73     101.984  28.517  43.781  1.00138.26      B    C  
ANISOU 6469  CD  GLU B  73    16152  16762  19617   1030   1553    996  B    C  
ATOM   6470  OE1 GLU B  73     101.294  29.515  44.118  1.00134.52      B    O  
ANISOU 6470  OE1 GLU B  73    15734  16332  19045   1289   1750   1146  B    O  
ATOM   6471  OE2 GLU B  73     101.465  27.456  43.344  1.00129.00      B    O1-
ANISOU 6471  OE2 GLU B  73    14747  15744  18523    906   1333   1097  B    O1-
ATOM   6472  N   GLN B  74     106.271  32.468  43.983  1.00118.45      B    N  
ANISOU 6472  N   GLN B  74    15050  13306  16648    852   2158    276  B    N  
ATOM   6473  CA  GLN B  74     106.909  33.554  43.257  1.00119.66      B    C  
ANISOU 6473  CA  GLN B  74    15563  13258  16643    812   2268    214  B    C  
ATOM   6474  C   GLN B  74     108.423  33.370  43.212  1.00112.60      B    C  
ANISOU 6474  C   GLN B  74    14743  12326  15712    459   2201      4  B    C  
ATOM   6475  O   GLN B  74     109.028  33.506  42.162  1.00113.32      B    O  
ANISOU 6475  O   GLN B  74    14896  12404  15755    336   2173    -43  B    O  
ATOM   6476  CB  GLN B  74     106.548  34.875  43.900  1.00128.36      B    C  
ANISOU 6476  CB  GLN B  74    17055  14150  17564   1016   2474    271  B    C  
ATOM   6477  CG  GLN B  74     105.049  35.072  44.062  1.00139.95      B    C  
ANISOU 6477  CG  GLN B  74    18418  15727  19030   1416   2561    500  B    C  
ATOM   6478  CD  GLN B  74     104.724  36.381  44.757  1.00162.40      B    C  
ANISOU 6478  CD  GLN B  74    21693  18355  21654   1680   2776    548  B    C  
ATOM   6479  NE2 GLN B  74     103.577  36.436  45.428  1.00171.16      B    N  
ANISOU 6479  NE2 GLN B  74    22678  19610  22746   2015   2859    726  B    N  
ATOM   6480  OE1 GLN B  74     105.504  37.331  44.702  1.00171.36      B    O  
ANISOU 6480  OE1 GLN B  74    23293  19203  22614   1579   2859    433  B    O  
ATOM   6481  N   TYR B  75     109.032  33.044  44.345  1.00109.67      B    N  
ANISOU 6481  N   TYR B  75    14341  11974  15353    300   2175   -106  B    N  
ATOM   6482  CA  TYR B  75     110.475  32.773  44.387  1.00108.48      B    C  
ANISOU 6482  CA  TYR B  75    14193  11873  15152    -28   2104   -282  B    C  
ATOM   6483  C   TYR B  75     110.827  31.456  43.699  1.00107.44      B    C  
ANISOU 6483  C   TYR B  75    13708  11970  15144   -100   1922   -333  B    C  
ATOM   6484  O   TYR B  75     111.896  31.323  43.124  1.00106.67      B    O  
ANISOU 6484  O   TYR B  75    13597  11957  14975   -297   1873   -432  B    O  
ATOM   6485  CB  TYR B  75     110.992  32.732  45.827  1.00110.40      B    C  
ANISOU 6485  CB  TYR B  75    14475  12107  15365   -160   2120   -372  B    C  
ATOM   6486  CG  TYR B  75     111.063  34.083  46.472  1.00116.23      B    C  
ANISOU 6486  CG  TYR B  75    15652  12595  15915   -175   2281   -371  B    C  
ATOM   6487  CD1 TYR B  75     112.173  34.898  46.304  1.00111.41      B    C  
ANISOU 6487  CD1 TYR B  75    15351  11872  15106   -465   2315   -458  B    C  
ATOM   6488  CD2 TYR B  75     110.012  34.549  47.255  1.00127.81      B    C  
ANISOU 6488  CD2 TYR B  75    17246  13944  17372    100   2393   -270  B    C  
ATOM   6489  CE1 TYR B  75     112.245  36.145  46.895  1.00113.57      B    C  
ANISOU 6489  CE1 TYR B  75    16108  11868  15174   -502   2442   -459  B    C  
ATOM   6490  CE2 TYR B  75     110.070  35.794  47.847  1.00135.54      B    C  
ANISOU 6490  CE2 TYR B  75    18694  14661  18145    124   2540   -276  B    C  
ATOM   6491  CZ  TYR B  75     111.193  36.589  47.658  1.00128.37      B    C  
ANISOU 6491  CZ  TYR B  75    18145  13590  17038   -188   2556   -378  B    C  
ATOM   6492  OH  TYR B  75     111.251  37.823  48.260  1.00141.38      B    O  
ANISOU 6492  OH  TYR B  75    20332  14934  18451   -185   2679   -386  B    O  
ATOM   6493  N   LEU B  76     109.948  30.468  43.783  1.00108.68      B    N  
ANISOU 6493  N   LEU B  76    13593  12236  15462     53   1814   -258  B    N  
ATOM   6494  CA  LEU B  76     110.185  29.212  43.086  1.00110.92      B    C  
ANISOU 6494  CA  LEU B  76    13619  12688  15835     14   1628   -303  B    C  
ATOM   6495  C   LEU B