binder.pdb

ATOM      1  N   GLN A   1     -66.560  28.798   3.241  1.00 54.53           N  
ANISOU    1  N   GLN A   1     5767   7937   7015    263  -2217    107       N  
ATOM      2  CA  GLN A   1     -65.382  28.108   2.736  1.00 54.52           C  
ANISOU    2  CA  GLN A   1     5943   7841   6930     61  -2198    240       C  
ATOM      3  C   GLN A   1     -65.230  26.739   3.378  1.00 57.69           C  
ANISOU    3  C   GLN A   1     6269   8363   7288   -112  -1981    271       C  
ATOM      4  O   GLN A   1     -65.470  26.574   4.575  1.00 70.21           O  
ANISOU    4  O   GLN A   1     7780  10044   8852    -83  -1828    209       O  
ATOM      5  CB  GLN A   1     -64.126  28.935   3.007  1.00 38.26           C  
ANISOU    5  CB  GLN A   1     4141   5606   4791     89  -2248    282       C  
ATOM      6  CG  GLN A   1     -64.110  29.590   4.374  1.00 48.03           C  
ANISOU    6  CG  GLN A   1     5393   6855   6002    227  -2162    200       C  
ATOM      7  CD  GLN A   1     -65.017  30.803   4.437  1.00 72.49           C  
ANISOU    7  CD  GLN A   1     8429   9942   9170    466  -2287     85       C  
ATOM      8  NE2 GLN A   1     -65.366  31.223   5.647  1.00 66.42           N  
ANISOU    8  NE2 GLN A   1     7608   9232   8398    596  -2181    -19       N  
ATOM      9  OE1 GLN A   1     -65.397  31.360   3.404  1.00 93.80           O  
ANISOU    9  OE1 GLN A   1    11138  12574  11927    534  -2483     87       O  
ATOM     10  N   VAL A   2     -64.829  25.759   2.577  1.00 45.79           N  
ANISOU   10  N   VAL A   2     4798   6841   5760   -297  -1973    365       N  
ATOM     11  CA  VAL A   2     -64.527  24.433   3.097  1.00 41.07           C  
ANISOU   11  CA  VAL A   2     4172   6320   5114   -470  -1793    409       C  
ATOM     12  C   VAL A   2     -63.312  24.512   4.010  1.00 45.43           C  
ANISOU   12  C   VAL A   2     4896   6778   5587   -494  -1714    443       C  
ATOM     13  O   VAL A   2     -62.281  25.067   3.634  1.00 55.57           O  
ANISOU   13  O   VAL A   2     6362   7910   6844   -490  -1802    495       O  
ATOM     14  CB  VAL A   2     -64.231  23.438   1.969  1.00 37.69           C  
ANISOU   14  CB  VAL A   2     3779   5864   4679   -653  -1818    500       C  
ATOM     15  CG1 VAL A   2     -63.649  22.155   2.533  1.00 35.43           C  
ANISOU   15  CG1 VAL A   2     3520   5606   4334   -821  -1654    552       C  
ATOM     16  CG2 VAL A   2     -65.492  23.164   1.159  1.00 43.85           C  
ANISOU   16  CG2 VAL A   2     4380   6753   5529   -661  -1885    474       C  
ATOM     17  N   THR A   3     -63.435  23.968   5.216  1.00 43.18           N  
ANISOU   17  N   THR A   3     4558   6583   5263   -528  -1552    413       N  
ATOM     18  CA  THR A   3     -62.311  23.931   6.142  1.00 49.36           C  
ANISOU   18  CA  THR A   3     5504   7278   5972   -566  -1484    451       C  
ATOM     19  C   THR A   3     -62.063  22.515   6.640  1.00 48.92           C  
ANISOU   19  C   THR A   3     5440   7276   5873   -746  -1345    501       C  
ATOM     20  O   THR A   3     -62.933  21.656   6.564  1.00 66.85           O  
ANISOU   20  O   THR A   3     7566   9679   8155   -828  -1271    484       O  
ATOM     21  CB  THR A   3     -62.511  24.883   7.342  1.00 59.31           C  
ANISOU   21  CB  THR A   3     6781   8550   7204   -419  -1444    367       C  
ATOM     22  CG2 THR A   3     -62.716  26.316   6.861  1.00 51.67           C  
ANISOU   22  CG2 THR A   3     5846   7507   6279   -229  -1601    316       C  
ATOM     23  OG1 THR A   3     -63.650  24.468   8.104  1.00 74.92           O  
ANISOU   23  OG1 THR A   3     8579  10705   9183   -416  -1308    279       O  
ATOM     24  N   LEU A   4     -60.861  22.277   7.141  1.00 49.31           N  
ANISOU   24  N   LEU A   4     5649   7215   5870   -812  -1322    564       N  
ATOM     25  CA  LEU A   4     -60.488  20.973   7.667  1.00 49.75           C  
ANISOU   25  CA  LEU A   4     5732   7288   5885   -974  -1217    615       C  
ATOM     26  C   LEU A   4     -59.522  21.184   8.825  1.00 52.77           C  
ANISOU   26  C   LEU A   4     6267   7578   6206   -972  -1188    637       C  
ATOM     27  O   LEU A   4     -58.595  21.987   8.734  1.00 54.73           O  
ANISOU   27  O   LEU A   4     6639   7699   6458   -907  -1274    663       O  
ATOM     28  CB  LEU A   4     -59.824  20.122   6.581  1.00 42.15           C  
ANISOU   28  CB  LEU A   4     4813   6252   4952  -1095  -1260    697       C  
ATOM     29  CG  LEU A   4     -60.549  20.006   5.241  1.00 49.44           C  
ANISOU   29  CG  LEU A   4     5633   7224   5929  -1109  -1321    693       C  
ATOM     30  CD1 LEU A   4     -59.568  20.037   4.082  1.00 62.44           C  
ANISOU   30  CD1 LEU A   4     7390   8736   7600  -1152  -1411    754       C  
ATOM     31  CD2 LEU A   4     -61.396  18.752   5.188  1.00 56.48           C  
ANISOU   31  CD2 LEU A   4     6405   8241   6813  -1239  -1234    695       C  
ATOM     32  N   ARG A   5     -59.753  20.475   9.922  1.00 51.42           N  
ANISOU   32  N   ARG A   5     6095   7469   5971  -1055  -1074    628       N  
ATOM     33  CA  ARG A   5     -58.877  20.563  11.078  1.00 45.86           C  
ANISOU   33  CA  ARG A   5     5549   6675   5201  -1075  -1055    655       C  
ATOM     34  C   ARG A   5     -58.487  19.172  11.551  1.00 37.71           C  
ANISOU   34  C   ARG A   5     4573   5627   4128  -1250   -996    719       C  
ATOM     35  O   ARG A   5     -59.332  18.394  11.985  1.00 45.80           O  
ANISOU   35  O   ARG A   5     5526   6769   5106  -1345   -895    694       O  
ATOM     36  CB  ARG A   5     -59.560  21.320  12.214  1.00 57.84           C  
ANISOU   36  CB  ARG A   5     7056   8266   6655   -991   -980    566       C  
ATOM     37  CG  ARG A   5     -58.629  21.688  13.363  1.00 79.13           C  
ANISOU   37  CG  ARG A   5     9941  10849   9276   -992   -986    592       C  
ATOM     38  CD  ARG A   5     -59.394  21.830  14.671  1.00 93.89           C  
ANISOU   38  CD  ARG A   5    11809  12816  11049   -996   -857    510       C  
ATOM     39  NE  ARG A   5     -60.794  22.176  14.445  1.00105.05           N  
ANISOU   39  NE  ARG A   5    13026  14398  12492   -912   -781    396       N  
ATOM     40  CZ  ARG A   5     -61.209  23.350  13.980  1.00106.54           C  
ANISOU   40  CZ  ARG A   5    13147  14594  12740   -729   -842    324       C  
ATOM     41  NH1 ARG A   5     -60.328  24.296  13.680  1.00 96.74           N1+
ANISOU   41  NH1 ARG A   5    12037  13202  11520   -624   -974    360       N1+
ATOM     42  NH2 ARG A   5     -62.505  23.574  13.805  1.00111.13           N  
ANISOU   42  NH2 ARG A   5    13531  15333  13363   -652   -779    216       N  
ATOM     43  N   GLU A   6     -57.202  18.861  11.454  1.00 37.97           N  
ANISOU   43  N   GLU A   6     4733   5511   4181  -1294  -1067    799       N  
ATOM     44  CA  GLU A   6     -56.678  17.608  11.974  1.00 42.26           C  
ANISOU   44  CA  GLU A   6     5359   6004   4695  -1441  -1043    861       C  
ATOM     45  C   GLU A   6     -56.501  17.727  13.482  1.00 44.05           C  
ANISOU   45  C   GLU A   6     5708   6205   4825  -1469  -1006    859       C  
ATOM     46  O   GLU A   6     -56.311  18.821  14.012  1.00 46.97           O  
ANISOU   46  O   GLU A   6     6135   6544   5167  -1368  -1027    829       O  
ATOM     47  CB  GLU A   6     -55.328  17.272  11.329  1.00 51.62           C  
ANISOU   47  CB  GLU A   6     6622   7036   5956  -1462  -1138    935       C  
ATOM     48  CG  GLU A   6     -55.302  17.340   9.813  1.00 57.38           C  
ANISOU   48  CG  GLU A   6     7267   7765   6770  -1435  -1180    936       C  
ATOM     49  CD  GLU A   6     -55.023  18.737   9.288  1.00 58.83           C  
ANISOU   49  CD  GLU A   6     7457   7911   6984  -1305  -1253    912       C  
ATOM     50  OE1 GLU A   6     -55.029  19.692  10.093  1.00 47.52           O  
ANISOU   50  OE1 GLU A   6     6077   6471   5509  -1220  -1265    886       O  
ATOM     51  OE2 GLU A   6     -54.795  18.876   8.067  1.00 64.09           O1-
ANISOU   51  OE2 GLU A   6     8093   8550   7709  -1296  -1301    920       O1-
ATOM     52  N   SER A   7     -56.557  16.596  14.173  1.00 44.43           N  
ANISOU   52  N   SER A   7     5816   6257   4811  -1616   -959    891       N  
ATOM     53  CA  SER A   7     -56.328  16.572  15.613  1.00 43.58           C  
ANISOU   53  CA  SER A   7     5856   6107   4595  -1676   -934    900       C  
ATOM     54  C   SER A   7     -55.838  15.198  16.051  1.00 45.73           C  
ANISOU   54  C   SER A   7     6242   6298   4834  -1842   -957    976       C  
ATOM     55  O   SER A   7     -56.193  14.180  15.462  1.00 40.00           O  
ANISOU   55  O   SER A   7     5455   5612   4130  -1932   -936    994       O  
ATOM     56  CB  SER A   7     -57.599  16.949  16.377  1.00 33.31           C  
ANISOU   56  CB  SER A   7     4496   4968   3194  -1681   -797    807       C  
ATOM     57  OG  SER A   7     -58.636  16.018  16.125  1.00 45.52           O  
ANISOU   57  OG  SER A   7     5923   6656   4716  -1795   -701    782       O  
ATOM     58  N   GLY A   8     -55.011  15.180  17.088  1.00 52.37           N  
ANISOU   58  N   GLY A   8     7262   7013   5621  -1883  -1016   1023       N  
ATOM     59  CA  GLY A   8     -54.432  13.948  17.581  1.00 51.94           C  
ANISOU   59  CA  GLY A   8     7345   6849   5540  -2028  -1074   1099       C  
ATOM     60  C   GLY A   8     -53.305  14.247  18.547  1.00 51.83           C  
ANISOU   60  C   GLY A   8     7519   6669   5503  -2026  -1185   1154       C  
ATOM     61  O   GLY A   8     -53.023  15.411  18.831  1.00 55.05           O  
ANISOU   61  O   GLY A   8     7952   7059   5907  -1920  -1203   1132       O  
ATOM     62  N   PRO A   9     -52.655  13.197  19.065  1.00 53.70           N  
ANISOU   62  N   PRO A   9     7900   6776   5726  -2144  -1273   1229       N  
ATOM     63  CA  PRO A   9     -51.544  13.374  20.003  1.00 60.48           C  
ANISOU   63  CA  PRO A   9     8945   7463   6572  -2154  -1405   1291       C  
ATOM     64  C   PRO A   9     -50.372  14.087  19.342  1.00 64.96           C  
ANISOU   64  C   PRO A   9     9461   7928   7293  -2009  -1521   1313       C  
ATOM     65  O   PRO A   9     -50.125  13.882  18.152  1.00 56.82           O  
ANISOU   65  O   PRO A   9     8292   6903   6392  -1947  -1533   1308       O  
ATOM     66  CB  PRO A   9     -51.149  11.931  20.340  1.00 54.10           C  
ANISOU   66  CB  PRO A   9     8262   6537   5757  -2298  -1494   1363       C  
ATOM     67  CG  PRO A   9     -51.677  11.124  19.179  1.00 53.86           C  
ANISOU   67  CG  PRO A   9     8079   6586   5798  -2311  -1436   1344       C  
ATOM     68  CD  PRO A   9     -52.984  11.774  18.891  1.00 54.02           C  
ANISOU   68  CD  PRO A   9     7955   6818   5750  -2285  -1264   1259       C  
ATOM     69  N   ALA A  10     -49.665  14.917  20.103  1.00 60.90           N  
ANISOU   69  N   ALA A  10     9063   7322   6753  -1969  -1600   1336       N  
ATOM     70  CA  ALA A  10     -48.448  15.540  19.603  1.00 49.96           C  
ANISOU   70  CA  ALA A  10     7647   5831   5506  -1860  -1722   1365       C  
ATOM     71  C   ALA A  10     -47.264  14.621  19.877  1.00 46.79           C  
ANISOU   71  C   ALA A  10     7333   5253   5192  -1915  -1884   1445       C  
ATOM     72  O   ALA A  10     -46.275  14.625  19.151  1.00 52.73           O  
ANISOU   72  O   ALA A  10     8004   5929   6101  -1846  -1972   1462       O  
ATOM     73  CB  ALA A  10     -48.236  16.894  20.251  1.00 44.18           C  
ANISOU   73  CB  ALA A  10     6998   5082   4707  -1793  -1742   1353       C  
ATOM     74  N   LEU A  11     -47.382  13.823  20.929  1.00 48.71           N  
ANISOU   74  N   LEU A  11     7743   5429   5334  -2044  -1924   1487       N  
ATOM     75  CA  LEU A  11     -46.317  12.915  21.319  1.00 56.62           C  
ANISOU   75  CA  LEU A  11     8852   6245   6414  -2097  -2102   1564       C  
ATOM     76  C   LEU A  11     -46.843  11.490  21.400  1.00 52.22           C  
ANISOU   76  C   LEU A  11     8349   5678   5815  -2223  -2090   1582       C  
ATOM     77  O   LEU A  11     -47.954  11.258  21.864  1.00 63.89           O  
ANISOU   77  O   LEU A  11     9886   7258   7130  -2329  -1971   1559       O  
ATOM     78  CB  LEU A  11     -45.725  13.335  22.669  1.00 57.51           C  
ANISOU   78  CB  LEU A  11     9178   6232   6440  -2149  -2226   1621       C  
ATOM     79  CG  LEU A  11     -44.504  12.555  23.166  1.00 49.13           C  
ANISOU   79  CG  LEU A  11     8235   4957   5474  -2189  -2451   1705       C  
ATOM     80  CD1 LEU A  11     -43.412  12.534  22.110  1.00 43.90           C  
ANISOU   80  CD1 LEU A  11     7392   4236   5050  -2062  -2540   1704       C  
ATOM     81  CD2 LEU A  11     -43.987  13.161  24.455  1.00 51.10           C  
ANISOU   81  CD2 LEU A  11     8696   5095   5627  -2240  -2571   1760       C  
ATOM     82  N   VAL A  12     -46.042  10.540  20.938  1.00 43.36           N  
ANISOU   82  N   VAL A  12     7205   4430   4838  -2213  -2211   1617       N  
ATOM     83  CA  VAL A  12     -46.419   9.136  20.988  1.00 41.98           C  
ANISOU   83  CA  VAL A  12     7105   4215   4632  -2330  -2229   1640       C  
ATOM     84  C   VAL A  12     -45.172   8.260  21.009  1.00 49.88           C  
ANISOU   84  C   VAL A  12     8161   5001   5789  -2310  -2440   1695       C  
ATOM     85  O   VAL A  12     -44.253   8.451  20.213  1.00 56.40           O  
ANISOU   85  O   VAL A  12     8843   5779   6807  -2181  -2497   1678       O  
ATOM     86  CB  VAL A  12     -47.338   8.744  19.804  1.00 38.39           C  
ANISOU   86  CB  VAL A  12     6478   3913   4196  -2321  -2070   1580       C  
ATOM     87  CG1 VAL A  12     -46.614   8.922  18.483  1.00 48.71           C  
ANISOU   87  CG1 VAL A  12     7590   5210   5708  -2175  -2082   1548       C  
ATOM     88  CG2 VAL A  12     -47.813   7.318  19.955  1.00 57.56           C  
ANISOU   88  CG2 VAL A  12     9009   6300   6560  -2464  -2086   1608       C  
ATOM     89  N   LYS A  13     -45.140   7.313  21.940  1.00 52.87           N  
ANISOU   89  N   LYS A  13     8754   5249   6085  -2442  -2559   1755       N  
ATOM     90  CA  LYS A  13     -44.001   6.418  22.087  1.00 47.90           C  
ANISOU   90  CA  LYS A  13     8201   4397   5603  -2424  -2787   1808       C  
ATOM     91  C   LYS A  13     -43.885   5.484  20.886  1.00 51.04           C  
ANISOU   91  C   LYS A  13     8456   4781   6154  -2363  -2772   1770       C  
ATOM     92  O   LYS A  13     -44.868   5.239  20.184  1.00 56.77           O  
ANISOU   92  O   LYS A  13     9099   5653   6818  -2398  -2603   1726       O  
ATOM     93  CB  LYS A  13     -44.137   5.612  23.378  1.00 48.88           C  
ANISOU   93  CB  LYS A  13     8620   4381   5572  -2600  -2923   1884       C  
ATOM     94  CG  LYS A  13     -44.036   6.459  24.640  1.00 53.87           C  
ANISOU   94  CG  LYS A  13     9426   4981   6060  -2666  -2973   1927       C  
ATOM     95  CD  LYS A  13     -44.551   5.710  25.856  1.00 57.64           C  
ANISOU   95  CD  LYS A  13    10208   5374   6318  -2886  -3038   1988       C  
ATOM     96  CE  LYS A  13     -44.368   6.525  27.125  1.00 67.35           C  
ANISOU   96  CE  LYS A  13    11636   6553   7402  -2960  -3098   2031       C  
ATOM     97  NZ  LYS A  13     -42.927   6.721  27.460  1.00 77.27           N1+
ANISOU   97  NZ  LYS A  13    12936   7601   8822  -2869  -3359   2093       N1+
ATOM     98  N   PRO A  14     -42.674   4.972  20.632  1.00 46.66           N  
ANISOU   98  N   PRO A  14     7868   4052   5808  -2270  -2950   1781       N  
ATOM     99  CA  PRO A  14     -42.480   4.009  19.545  1.00 43.41           C  
ANISOU   99  CA  PRO A  14     7343   3604   5547  -2210  -2945   1737       C  
ATOM    100  C   PRO A  14     -43.380   2.793  19.732  1.00 52.17           C  
ANISOU  100  C   PRO A  14     8612   4691   6519  -2359  -2933   1761       C  
ATOM    101  O   PRO A  14     -43.761   2.487  20.860  1.00 58.18           O  
ANISOU  101  O   PRO A  14     9603   5394   7111  -2506  -3006   1825       O  
ATOM    102  CB  PRO A  14     -41.012   3.607  19.693  1.00 45.37           C  
ANISOU  102  CB  PRO A  14     7588   3633   6017  -2108  -3179   1755       C  
ATOM    103  CG  PRO A  14     -40.368   4.768  20.370  1.00 47.61           C  
ANISOU  103  CG  PRO A  14     7870   3909   6312  -2066  -3248   1785       C  
ATOM    104  CD  PRO A  14     -41.408   5.325  21.298  1.00 49.88           C  
ANISOU  104  CD  PRO A  14     8323   4296   6332  -2205  -3159   1826       C  
ATOM    105  N   THR A  15     -43.705   2.117  18.634  1.00 54.45           N  
ANISOU  105  N   THR A  15     8792   5025   6870  -2335  -2843   1710       N  
ATOM    106  CA  THR A  15     -44.581   0.940  18.637  1.00 48.20           C  
ANISOU  106  CA  THR A  15     8138   4222   5954  -2480  -2822   1727       C  
ATOM    107  C   THR A  15     -46.043   1.270  18.929  1.00 51.87           C  
ANISOU  107  C   THR A  15     8642   4893   6172  -2634  -2633   1730       C  
ATOM    108  O   THR A  15     -46.935   0.484  18.607  1.00 59.66           O  
ANISOU  108  O   THR A  15     9669   5940   7061  -2748  -2554   1725       O  
ATOM    109  CB  THR A  15     -44.110  -0.163  19.611  1.00 46.38           C  
ANISOU  109  CB  THR A  15     8170   3749   5704  -2568  -3064   1800       C  
ATOM    110  CG2 THR A  15     -42.591  -0.276  19.617  1.00 43.50           C  
ANISOU  110  CG2 THR A  15     7765   3176   5587  -2406  -3280   1800       C  
ATOM    111  OG1 THR A  15     -44.593   0.120  20.929  1.00 50.12           O  
ANISOU  111  OG1 THR A  15     8853   4228   5962  -2726  -3094   1867       O  
ATOM    112  N   GLN A  16     -46.292   2.429  19.528  1.00 43.84           N  
ANISOU  112  N   GLN A  16     7609   3986   5062  -2637  -2560   1733       N  
ATOM    113  CA  GLN A  16     -47.661   2.833  19.817  1.00 46.67           C  
ANISOU  113  CA  GLN A  16     7977   4551   5206  -2763  -2371   1717       C  
ATOM    114  C   GLN A  16     -48.425   3.233  18.558  1.00 52.83           C  
ANISOU  114  C   GLN A  16     8518   5538   6018  -2699  -2170   1643       C  
ATOM    115  O   GLN A  16     -47.831   3.495  17.509  1.00 51.45           O  
ANISOU  115  O   GLN A  16     8171   5358   6019  -2549  -2163   1603       O  
ATOM    116  CB  GLN A  16     -47.693   3.966  20.840  1.00 49.87           C  
ANISOU  116  CB  GLN A  16     8442   5003   5503  -2774  -2352   1730       C  
ATOM    117  CG  GLN A  16     -47.388   3.510  22.259  1.00 65.09           C  
ANISOU  117  CG  GLN A  16    10658   6764   7308  -2915  -2515   1808       C  
ATOM    118  CD  GLN A  16     -47.644   4.593  23.285  1.00 66.28           C  
ANISOU  118  CD  GLN A  16    10891   6984   7310  -2958  -2460   1812       C  
ATOM    119  NE2 GLN A  16     -47.852   4.182  24.533  1.00 65.86           N  
ANISOU  119  NE2 GLN A  16    11107   6847   7071  -3144  -2531   1868       N  
ATOM    120  OE1 GLN A  16     -47.654   5.788  22.963  1.00 52.17           O  
ANISOU  120  OE1 GLN A  16     8941   5315   5565  -2833  -2357   1764       O  
ATOM    121  N   THR A  17     -49.747   3.277  18.676  1.00 44.56           N  
ANISOU  121  N   THR A  17     7464   4671   4797  -2823  -2009   1623       N  
ATOM    122  CA  THR A  17     -50.612   3.596  17.551  1.00 44.15           C  
ANISOU  122  CA  THR A  17     7200   4816   4759  -2784  -1833   1559       C  
ATOM    123  C   THR A  17     -50.994   5.067  17.531  1.00 51.02           C  
ANISOU  123  C   THR A  17     7925   5850   5608  -2689  -1710   1509       C  
ATOM    124  O   THR A  17     -51.315   5.654  18.566  1.00 52.94           O  
ANISOU  124  O   THR A  17     8252   6138   5724  -2741  -1678   1513       O  
ATOM    125  CB  THR A  17     -51.905   2.763  17.590  1.00 53.09           C  
ANISOU  125  CB  THR A  17     8377   6065   5729  -2973  -1730   1557       C  
ATOM    126  CG2 THR A  17     -52.868   3.223  16.506  1.00 51.64           C  
ANISOU  126  CG2 THR A  17     7966   6096   5558  -2933  -1557   1492       C  
ATOM    127  OG1 THR A  17     -51.589   1.381  17.391  1.00 58.31           O  
ANISOU  127  OG1 THR A  17     9166   6571   6418  -3051  -1844   1598       O  
ATOM    128  N   LEU A  18     -50.952   5.657  16.342  1.00 49.89           N  
ANISOU  128  N   LEU A  18     7582   5788   5587  -2554  -1644   1459       N  
ATOM    129  CA  LEU A  18     -51.375   7.034  16.149  1.00 42.69           C  
ANISOU  129  CA  LEU A  18     6530   5027   4664  -2456  -1537   1408       C  
ATOM    130  C   LEU A  18     -52.821   7.066  15.676  1.00 52.06           C  
ANISOU  130  C   LEU A  18     7597   6424   5761  -2517  -1376   1358       C  
ATOM    131  O   LEU A  18     -53.204   6.325  14.772  1.00 59.58           O  
ANISOU  131  O   LEU A  18     8483   7409   6745  -2556  -1346   1351       O  
ATOM    132  CB  LEU A  18     -50.487   7.715  15.113  1.00 41.83           C  
ANISOU  132  CB  LEU A  18     6285   4878   4730  -2286  -1572   1383       C  
ATOM    133  CG  LEU A  18     -50.958   9.084  14.617  1.00 43.78           C  
ANISOU  133  CG  LEU A  18     6385   5273   4978  -2179  -1474   1328       C  
ATOM    134  CD1 LEU A  18     -50.883  10.102  15.743  1.00 55.65           C  
ANISOU  134  CD1 LEU A  18     7963   6781   6399  -2151  -1483   1331       C  
ATOM    135  CD2 LEU A  18     -50.120   9.533  13.430  1.00 33.89           C  
ANISOU  135  CD2 LEU A  18     5015   3978   3885  -2052  -1505   1307       C  
ATOM    136  N   THR A  19     -53.627   7.921  16.291  1.00 49.90           N  
ANISOU  136  N   THR A  19     7293   6289   5377  -2524  -1276   1320       N  
ATOM    137  CA  THR A  19     -55.015   8.057  15.884  1.00 51.31           C  
ANISOU  137  CA  THR A  19     7328   6678   5487  -2567  -1126   1262       C  
ATOM    138  C   THR A  19     -55.333   9.510  15.548  1.00 51.73           C  
ANISOU  138  C   THR A  19     7229   6848   5578  -2410  -1060   1196       C  
ATOM    139  O   THR A  19     -55.455  10.355  16.436  1.00 48.64           O  
ANISOU  139  O   THR A  19     6877   6488   5115  -2379  -1028   1170       O  
ATOM    140  CB  THR A  19     -55.976   7.510  16.957  1.00 54.29           C  
ANISOU  140  CB  THR A  19     7801   7145   5681  -2756  -1042   1258       C  
ATOM    141  CG2 THR A  19     -57.425   7.747  16.553  1.00 45.20           C  
ANISOU  141  CG2 THR A  19     6466   6231   4476  -2790   -883   1185       C  
ATOM    142  OG1 THR A  19     -55.762   6.101  17.107  1.00 62.34           O  
ANISOU  142  OG1 THR A  19     8969   8055   6664  -2911  -1115   1322       O  
ATOM    143  N   LEU A  20     -55.457   9.788  14.253  1.00 46.48           N  
ANISOU  143  N   LEU A  20     6407   6233   5019  -2317  -1049   1169       N  
ATOM    144  CA  LEU A  20     -55.724  11.138  13.778  1.00 46.15           C  
ANISOU  144  CA  LEU A  20     6232   6279   5022  -2165  -1014   1112       C  
ATOM    145  C   LEU A  20     -57.185  11.322  13.395  1.00 47.62           C  
ANISOU  145  C   LEU A  20     6257   6671   5167  -2183   -898   1046       C  
ATOM    146  O   LEU A  20     -57.835  10.393  12.924  1.00 50.81           O  
ANISOU  146  O   LEU A  20     6609   7141   5553  -2292   -860   1052       O  
ATOM    147  CB  LEU A  20     -54.824  11.469  12.588  1.00 49.96           C  
ANISOU  147  CB  LEU A  20     6663   6671   5649  -2050  -1094   1124       C  
ATOM    148  CG  LEU A  20     -53.326  11.486  12.894  1.00 58.58           C  
ANISOU  148  CG  LEU A  20     7873   7574   6810  -2007  -1209   1173       C  
ATOM    149  CD1 LEU A  20     -52.518  11.625  11.618  1.00 58.41           C  
ANISOU  149  CD1 LEU A  20     7784   7483   6925  -1926  -1261   1173       C  
ATOM    150  CD2 LEU A  20     -52.994  12.605  13.870  1.00 59.55           C  
ANISOU  150  CD2 LEU A  20     8063   7673   6889  -1933  -1232   1167       C  
ATOM    151  N   THR A  21     -57.692  12.532  13.602  1.00 50.37           N  
ANISOU  151  N   THR A  21     6522   7114   5501  -2072   -850    981       N  
ATOM    152  CA  THR A  21     -59.077  12.855  13.296  1.00 49.73           C  
ANISOU  152  CA  THR A  21     6265   7231   5400  -2060   -750    905       C  
ATOM    153  C   THR A  21     -59.162  14.124  12.461  1.00 49.44           C  
ANISOU  153  C   THR A  21     6111   7220   5455  -1875   -787    858       C  
ATOM    154  O   THR A  21     -58.550  15.140  12.790  1.00 55.78           O  
ANISOU  154  O   THR A  21     6974   7948   6271  -1755   -833    848       O  
ATOM    155  CB  THR A  21     -59.910  13.043  14.580  1.00 55.79           C  
ANISOU  155  CB  THR A  21     7040   8118   6041  -2121   -632    846       C  
ATOM    156  CG2 THR A  21     -61.327  13.488  14.237  1.00 64.25           C  
ANISOU  156  CG2 THR A  21     7893   9401   7118  -2083   -530    750       C  
ATOM    157  OG1 THR A  21     -59.968  11.806  15.298  1.00 48.39           O  
ANISOU  157  OG1 THR A  21     6221   7166   5000  -2324   -598    891       O  
ATOM    158  N   CYS A  22     -59.927  14.056  11.377  1.00 51.76           N  
ANISOU  158  N   CYS A  22     6250   7611   5805  -1862   -780    832       N  
ATOM    159  CA  CYS A  22     -60.120  15.193  10.490  1.00 50.15           C  
ANISOU  159  CA  CYS A  22     5943   7429   5684  -1701   -833    790       C  
ATOM    160  C   CYS A  22     -61.559  15.677  10.585  1.00 60.75           C  
ANISOU  160  C   CYS A  22     7106   8961   7015  -1656   -756    697       C  
ATOM    161  O   CYS A  22     -62.476  15.007  10.116  1.00 72.28           O  
ANISOU  161  O   CYS A  22     8441  10542   8479  -1743   -714    684       O  
ATOM    162  CB  CYS A  22     -59.807  14.790   9.046  1.00 45.19           C  
ANISOU  162  CB  CYS A  22     5288   6744   5137  -1717   -908    834       C  
ATOM    163  SG  CYS A  22     -59.786  16.156   7.857  1.00 86.48           S  
ANISOU  163  SG  CYS A  22    10451  11951  10456  -1545  -1009    803       S  
ATOM    164  N   THR A  23     -61.761  16.837  11.199  1.00 57.77           N  
ANISOU  164  N   THR A  23     6712   8611   6627  -1520   -741    628       N  
ATOM    165  CA  THR A  23     -63.098  17.412  11.285  1.00 59.16           C  
ANISOU  165  CA  THR A  23     6700   8963   6815  -1446   -673    521       C  
ATOM    166  C   THR A  23     -63.245  18.537  10.269  1.00 48.67           C  
ANISOU  166  C   THR A  23     5291   7613   5590  -1263   -786    488       C  
ATOM    167  O   THR A  23     -62.442  19.463  10.240  1.00 46.37           O  
ANISOU  167  O   THR A  23     5110   7193   5315  -1144   -871    500       O  
ATOM    168  CB  THR A  23     -63.407  17.930  12.704  1.00 58.37           C  
ANISOU  168  CB  THR A  23     6626   8923   6629  -1416   -564    443       C  
ATOM    169  CG2 THR A  23     -64.773  18.598  12.742  1.00 44.72           C  
ANISOU  169  CG2 THR A  23     4679   7378   4935  -1313   -491    312       C  
ATOM    170  OG1 THR A  23     -63.394  16.831  13.625  1.00 63.47           O  
ANISOU  170  OG1 THR A  23     7354   9597   7164  -1612   -462    473       O  
ATOM    171  N   PHE A  24     -64.266  18.451   9.427  1.00 36.13           N  
ANISOU  171  N   PHE A  24     3520   6144   4066  -1252   -799    450       N  
ATOM    172  CA  PHE A  24     -64.423  19.425   8.356  1.00 49.59           C  
ANISOU  172  CA  PHE A  24     5165   7811   5865  -1098   -934    430       C  
ATOM    173  C   PHE A  24     -65.796  20.080   8.314  1.00 51.46           C  
ANISOU  173  C   PHE A  24     5183   8207   6162   -978   -921    314       C  
ATOM    174  O   PHE A  24     -66.718  19.682   9.025  1.00 62.90           O  
ANISOU  174  O   PHE A  24     6493   9822   7585  -1031   -789    243       O  
ATOM    175  CB  PHE A  24     -64.122  18.781   7.003  1.00 51.71           C  
ANISOU  175  CB  PHE A  24     5452   8018   6178  -1185  -1026    514       C  
ATOM    176  CG  PHE A  24     -64.946  17.560   6.713  1.00 57.53           C  
ANISOU  176  CG  PHE A  24     6067   8884   6907  -1347   -960    526       C  
ATOM    177  CD1 PHE A  24     -66.200  17.673   6.135  1.00 66.89           C  
ANISOU  177  CD1 PHE A  24     7048  10212   8154  -1319   -980    469       C  
ATOM    178  CD2 PHE A  24     -64.464  16.296   7.015  1.00 47.60           C  
ANISOU  178  CD2 PHE A  24     4905   7598   5584  -1528   -890    595       C  
ATOM    179  CE1 PHE A  24     -66.957  16.548   5.869  1.00 63.39           C  
ANISOU  179  CE1 PHE A  24     6497   9891   7699  -1482   -924    484       C  
ATOM    180  CE2 PHE A  24     -65.214  15.172   6.748  1.00 44.62           C  
ANISOU  180  CE2 PHE A  24     4435   7330   5187  -1687   -837    610       C  
ATOM    181  CZ  PHE A  24     -66.463  15.297   6.177  1.00 52.19           C  
ANISOU  181  CZ  PHE A  24     5190   8441   6200  -1671   -849    556       C  
ATOM    182  N   SER A  25     -65.917  21.094   7.466  1.00 44.10           N  
ANISOU  182  N   SER A  25     4222   7220   5312   -819  -1064    291       N  
ATOM    183  CA  SER A  25     -67.179  21.784   7.258  1.00 52.57           C  
ANISOU  183  CA  SER A  25     5083   8419   6471   -679  -1094    180       C  
ATOM    184  C   SER A  25     -67.172  22.416   5.876  1.00 51.34           C  
ANISOU  184  C   SER A  25     4935   8171   6403   -587  -1297    210       C  
ATOM    185  O   SER A  25     -66.130  22.479   5.222  1.00 45.56           O  
ANISOU  185  O   SER A  25     4386   7275   5648   -622  -1393    303       O  
ATOM    186  CB  SER A  25     -67.386  22.858   8.324  1.00 53.35           C  
ANISOU  186  CB  SER A  25     5173   8537   6562   -506  -1042     68       C  
ATOM    187  OG  SER A  25     -66.342  23.815   8.289  1.00 53.78           O  
ANISOU  187  OG  SER A  25     5435   8402   6598   -396  -1152    104       O  
ATOM    188  N   GLY A  26     -68.335  22.880   5.433  1.00 49.12           N  
ANISOU  188  N   GLY A  26     4452   7992   6218   -476  -1364    128       N  
ATOM    189  CA  GLY A  26     -68.451  23.490   4.122  1.00 55.79           C  
ANISOU  189  CA  GLY A  26     5308   8747   7142   -394  -1576    154       C  
ATOM    190  C   GLY A  26     -68.928  22.504   3.075  1.00 53.79           C  
ANISOU  190  C   GLY A  26     4965   8554   6918   -550  -1618    215       C  
ATOM    191  O   GLY A  26     -69.468  22.897   2.037  1.00 48.29           O  
ANISOU  191  O   GLY A  26     4206   7840   6301   -493  -1785    214       O  
ATOM    192  N   PHE A  27     -68.721  21.219   3.349  1.00 47.72           N  
ANISOU  192  N   PHE A  27     4206   7845   6079   -753  -1477    273       N  
ATOM    193  CA  PHE A  27     -69.173  20.158   2.456  1.00 58.65           C  
ANISOU  193  CA  PHE A  27     5518   9290   7474   -923  -1496    332       C  
ATOM    194  C   PHE A  27     -69.493  18.893   3.245  1.00 66.27           C  
ANISOU  194  C   PHE A  27     6405  10399   8375  -1103  -1304    334       C  
ATOM    195  O   PHE A  27     -69.079  18.750   4.397  1.00 72.35           O  
ANISOU  195  O   PHE A  27     7235  11179   9073  -1121  -1165    316       O  
ATOM    196  CB  PHE A  27     -68.119  19.857   1.387  1.00 53.40           C  
ANISOU  196  CB  PHE A  27     5071   8446   6771  -1023  -1595    449       C  
ATOM    197  CG  PHE A  27     -66.968  19.022   1.880  1.00 52.84           C  
ANISOU  197  CG  PHE A  27     5175   8296   6605  -1160  -1475    521       C  
ATOM    198  CD1 PHE A  27     -66.918  17.663   1.618  1.00 42.64           C  
ANISOU  198  CD1 PHE A  27     3899   7034   5270  -1361  -1404    585       C  
ATOM    199  CD2 PHE A  27     -65.931  19.598   2.599  1.00 56.40           C  
ANISOU  199  CD2 PHE A  27     5781   8635   7015  -1086  -1447    525       C  
ATOM    200  CE1 PHE A  27     -65.856  16.892   2.066  1.00 45.53           C  
ANISOU  200  CE1 PHE A  27     4425   7313   5562  -1472  -1314    646       C  
ATOM    201  CE2 PHE A  27     -64.868  18.834   3.048  1.00 49.84           C  
ANISOU  201  CE2 PHE A  27     5100   7724   6113  -1203  -1358    590       C  
ATOM    202  CZ  PHE A  27     -64.832  17.478   2.780  1.00 45.29           C  
ANISOU  202  CZ  PHE A  27     4531   7173   5503  -1389  -1294    648       C  
ATOM    203  N   SER A  28     -70.236  17.981   2.625  1.00 61.91           N  
ANISOU  203  N   SER A  28     5734   9951   7839  -1246  -1307    360       N  
ATOM    204  CA  SER A  28     -70.528  16.694   3.246  1.00 64.58           C  
ANISOU  204  CA  SER A  28     6023  10411   8102  -1448  -1142    376       C  
ATOM    205  C   SER A  28     -69.834  15.555   2.504  1.00 73.65           C  
ANISOU  205  C   SER A  28     7340  11457   9188  -1643  -1162    498       C  
ATOM    206  O   SER A  28     -69.747  15.559   1.273  1.00 79.56           O  
ANISOU  206  O   SER A  28     8133  12124   9973  -1659  -1299    551       O  
ATOM    207  CB  SER A  28     -72.033  16.444   3.300  1.00 64.87           C  
ANISOU  207  CB  SER A  28     5771  10679   8197  -1481  -1102    296       C  
ATOM    208  OG  SER A  28     -72.316  15.239   3.989  1.00 70.11           O  
ANISOU  208  OG  SER A  28     6404  11465   8770  -1692   -935    309       O  
ATOM    209  N   LEU A  29     -69.345  14.580   3.262  1.00 63.71           N  
ANISOU  209  N   LEU A  29     6184  10192   7831  -1793  -1029    537       N  
ATOM    210  CA  LEU A  29     -68.645  13.437   2.696  1.00 53.74           C  
ANISOU  210  CA  LEU A  29     5088   8822   6509  -1969  -1036    641       C  
ATOM    211  C   LEU A  29     -69.635  12.450   2.090  1.00 61.63           C  
ANISOU  211  C   LEU A  29     5967   9945   7503  -2140  -1035    661       C  
ATOM    212  O   LEU A  29     -69.261  11.605   1.280  1.00 70.71           O  
ANISOU  212  O   LEU A  29     7235  11009   8623  -2273  -1077    740       O  
ATOM    213  CB  LEU A  29     -67.831  12.738   3.779  1.00 54.93           C  
ANISOU  213  CB  LEU A  29     5392   8916   6562  -2062   -915    672       C  
ATOM    214  CG  LEU A  29     -66.433  12.236   3.417  1.00 52.77           C  
ANISOU  214  CG  LEU A  29     5356   8435   6258  -2112   -951    761       C  
ATOM    215  CD1 LEU A  29     -65.898  11.346   4.533  1.00 35.37           C  
ANISOU  215  CD1 LEU A  29     3276   6201   3963  -2229   -844    790       C  
ATOM    216  CD2 LEU A  29     -66.430  11.505   2.083  1.00 45.88           C  
ANISOU  216  CD2 LEU A  29     4524   7510   5399  -2223  -1026    822       C  
ATOM    217  N   SER A  30     -70.900  12.551   2.488  1.00 53.32           N  
ANISOU  217  N   SER A  30     4679   9100   6482  -2142   -985    584       N  
ATOM    218  CA  SER A  30     -71.928  11.659   1.963  1.00 61.05           C  
ANISOU  218  CA  SER A  30     5520  10217   7459  -2312   -987    599       C  
ATOM    219  C   SER A  30     -72.356  12.081   0.563  1.00 63.52           C  
ANISOU  219  C   SER A  30     5765  10504   7867  -2257  -1167    616       C  
ATOM    220  O   SER A  30     -73.066  11.349  -0.126  1.00 61.04           O  
ANISOU  220  O   SER A  30     5374  10265   7554  -2403  -1208    649       O  
ATOM    221  CB  SER A  30     -73.138  11.611   2.899  1.00 62.51           C  
ANISOU  221  CB  SER A  30     5458  10648   7647  -2347   -860    502       C  
ATOM    222  OG  SER A  30     -73.629  12.913   3.167  1.00 69.03           O  
ANISOU  222  OG  SER A  30     6108  11544   8575  -2121   -886    393       O  
ATOM    223  N   THR A  31     -71.919  13.267   0.151  1.00 63.52           N  
ANISOU  223  N   THR A  31     5808  10389   7937  -2057  -1284    598       N  
ATOM    224  CA  THR A  31     -72.212  13.768  -1.186  1.00 57.18           C  
ANISOU  224  CA  THR A  31     4985   9528   7212  -2002  -1477    621       C  
ATOM    225  C   THR A  31     -71.394  13.005  -2.221  1.00 50.88           C  
ANISOU  225  C   THR A  31     4418   8566   6350  -2150  -1534    730       C  
ATOM    226  O   THR A  31     -70.200  12.765  -2.027  1.00 47.53           O  
ANISOU  226  O   THR A  31     4203   7996   5859  -2172  -1478    774       O  
ATOM    227  CB  THR A  31     -71.919  15.273  -1.301  1.00 60.85           C  
ANISOU  227  CB  THR A  31     5467   9899   7754  -1756  -1594    572       C  
ATOM    228  CG2 THR A  31     -72.163  15.760  -2.721  1.00 62.48           C  
ANISOU  228  CG2 THR A  31     5694  10021   8024  -1722  -1812    606       C  
ATOM    229  OG1 THR A  31     -72.769  15.997  -0.402  1.00 61.67           O  
ANISOU  229  OG1 THR A  31     5345  10157   7929  -1606  -1545    456       O  
ATOM    230  N   ALA A  32     -72.041  12.614  -3.313  1.00 52.54           N  
ANISOU  230  N   ALA A  32     4584   8798   6581  -2252  -1646    768       N  
ATOM    231  CA  ALA A  32     -71.375  11.854  -4.363  1.00 57.86           C  
ANISOU  231  CA  ALA A  32     5474   9324   7188  -2405  -1695    862       C  
ATOM    232  C   ALA A  32     -70.192  12.625  -4.940  1.00 72.48           C  
ANISOU  232  C   ALA A  32     7539  10966   9035  -2304  -1773    887       C  
ATOM    233  O   ALA A  32     -70.291  13.821  -5.218  1.00 82.88           O  
ANISOU  233  O   ALA A  32     8826  12247  10418  -2141  -1894    853       O  
ATOM    234  CB  ALA A  32     -72.359  11.503  -5.460  1.00 58.42           C  
ANISOU  234  CB  ALA A  32     5458   9452   7286  -2517  -1826    892       C  
ATOM    235  N   GLY A  33     -69.072  11.932  -5.115  1.00 69.98           N  
ANISOU  235  N   GLY A  33     7438  10509   8640  -2403  -1704    941       N  
ATOM    236  CA  GLY A  33     -67.890  12.536  -5.697  1.00 61.97           C  
ANISOU  236  CA  GLY A  33     6627   9305   7613  -2341  -1756    963       C  
ATOM    237  C   GLY A  33     -66.894  13.043  -4.674  1.00 53.91           C  
ANISOU  237  C   GLY A  33     5670   8225   6590  -2218  -1666    936       C  
ATOM    238  O   GLY A  33     -65.751  13.352  -5.007  1.00 49.82           O  
ANISOU  238  O   GLY A  33     5324   7553   6051  -2194  -1675    955       O  
ATOM    239  N   MET A  34     -67.325  13.120  -3.421  1.00 56.57           N  
ANISOU  239  N   MET A  34     5868   8684   6940  -2152  -1575    889       N  
ATOM    240  CA  MET A  34     -66.513  13.722  -2.373  1.00 51.86           C  
ANISOU  240  CA  MET A  34     5323   8040   6341  -2027  -1505    860       C  
ATOM    241  C   MET A  34     -65.581  12.703  -1.710  1.00 47.02           C  
ANISOU  241  C   MET A  34     4838   7364   5664  -2129  -1375    896       C  
ATOM    242  O   MET A  34     -65.941  11.541  -1.524  1.00 49.17           O  
ANISOU  242  O   MET A  34     5092   7697   5893  -2278  -1303    919       O  
ATOM    243  CB  MET A  34     -67.414  14.394  -1.336  1.00 55.68           C  
ANISOU  243  CB  MET A  34     5612   8678   6866  -1900  -1471    781       C  
ATOM    244  CG  MET A  34     -66.990  15.807  -0.979  1.00 67.71           C  
ANISOU  244  CG  MET A  34     7163  10136   8428  -1695  -1527    736       C  
ATOM    245  SD  MET A  34     -67.050  16.952  -2.377  1.00 63.60           S  
ANISOU  245  SD  MET A  34     6691   9509   7965  -1593  -1745    742       S  
ATOM    246  CE  MET A  34     -68.804  17.006  -2.703  1.00 58.68           C  
ANISOU  246  CE  MET A  34     5802   9070   7423  -1573  -1826    691       C  
ATOM    247  N   SER A  35     -64.380  13.152  -1.363  1.00 42.21           N  
ANISOU  247  N   SER A  35     4362   6625   5049  -2051  -1359    901       N  
ATOM    248  CA  SER A  35     -63.366  12.285  -0.783  1.00 43.27           C  
ANISOU  248  CA  SER A  35     4626   6673   5142  -2126  -1265    934       C  
ATOM    249  C   SER A  35     -62.481  13.039   0.201  1.00 43.30           C  
ANISOU  249  C   SER A  35     4689   6611   5152  -2000  -1239    915       C  
ATOM    250  O   SER A  35     -62.344  14.260   0.119  1.00 48.89           O  
ANISOU  250  O   SER A  35     5391   7293   5892  -1863  -1305    888       O  
ATOM    251  CB  SER A  35     -62.489  11.683  -1.886  1.00 43.05           C  
ANISOU  251  CB  SER A  35     4749   6501   5106  -2219  -1290    979       C  
ATOM    252  OG  SER A  35     -61.339  11.050  -1.333  1.00 47.85           O  
ANISOU  252  OG  SER A  35     5479   7000   5700  -2248  -1220    999       O  
ATOM    253  N   VAL A  35A    -61.877  12.305   1.129  1.00 34.59           N  
ANISOU  253  N   VAL A  35A    3657   5472   4014  -2053  -1156    934       N  
ATOM    254  CA  VAL A  35A    -60.901  12.890   2.036  1.00 42.70           C  
ANISOU  254  CA  VAL A  35A    4766   6416   5044  -1956  -1141    929       C  
ATOM    255  C   VAL A  35A    -59.635  12.047   2.047  1.00 46.76           C  
ANISOU  255  C   VAL A  35A    5426   6784   5557  -2025  -1121    973       C  
ATOM    256  O   VAL A  35A    -59.695  10.822   2.130  1.00 48.11           O  
ANISOU  256  O   VAL A  35A    5630   6949   5699  -2150  -1078   1000       O  
ATOM    257  CB  VAL A  35A    -61.451  13.029   3.469  1.00 41.65           C  
ANISOU  257  CB  VAL A  35A    4569   6387   4870  -1927  -1068    895       C  
ATOM    258  CG1 VAL A  35A    -60.312  13.209   4.459  1.00 38.84           C  
ANISOU  258  CG1 VAL A  35A    4338   5921   4499  -1882  -1050    910       C  
ATOM    259  CG2 VAL A  35A    -62.420  14.194   3.553  1.00 31.48           C  
ANISOU  259  CG2 VAL A  35A    3140   5215   3606  -1799  -1094    830       C  
ATOM    260  N   GLY A  35B    -58.489  12.711   1.949  1.00 45.43           N  
ANISOU  260  N   GLY A  35B    5344   6494   5425  -1943  -1158    976       N  
ATOM    261  CA  GLY A  35B    -57.212  12.027   1.929  1.00 27.22           C  
ANISOU  261  CA  GLY A  35B    3153   4047   3142  -1986  -1147   1005       C  
ATOM    262  C   GLY A  35B    -56.287  12.541   3.014  1.00 48.21           C  
ANISOU  262  C   GLY A  35B    5871   6634   5812  -1903  -1153   1008       C  
ATOM    263  O   GLY A  35B    -56.421  13.680   3.468  1.00 44.54           O  
ANISOU  263  O   GLY A  35B    5383   6201   5340  -1799  -1178    986       O  
ATOM    264  N   TRP A  36     -55.353  11.693   3.436  1.00 43.82           N  
ANISOU  264  N   TRP A  36     5400   5975   5276  -1948  -1140   1034       N  
ATOM    265  CA  TRP A  36     -54.364  12.069   4.432  1.00 38.94           C  
ANISOU  265  CA  TRP A  36     4847   5271   4676  -1884  -1164   1045       C  
ATOM    266  C   TRP A  36     -52.982  12.134   3.812  1.00 49.01           C  
ANISOU  266  C   TRP A  36     6176   6413   6034  -1860  -1197   1046       C  
ATOM    267  O   TRP A  36     -52.623  11.309   2.976  1.00 50.73           O  
ANISOU  267  O   TRP A  36     6409   6575   6291  -1923  -1181   1044       O  
ATOM    268  CB  TRP A  36     -54.369  11.093   5.606  1.00 44.07           C  
ANISOU  268  CB  TRP A  36     5555   5902   5288  -1952  -1143   1073       C  
ATOM    269  CG  TRP A  36     -55.523  11.290   6.525  1.00 50.39           C  
ANISOU  269  CG  TRP A  36     6313   6834   6000  -1967  -1099   1061       C  
ATOM    270  CD1 TRP A  36     -56.765  10.740   6.407  1.00 55.81           C  
ANISOU  270  CD1 TRP A  36     6928   7647   6629  -2054  -1044   1051       C  
ATOM    271  CD2 TRP A  36     -55.550  12.096   7.708  1.00 51.12           C  
ANISOU  271  CD2 TRP A  36     6427   6949   6047  -1903  -1096   1051       C  
ATOM    272  CE2 TRP A  36     -56.843  11.985   8.258  1.00 51.37           C  
ANISOU  272  CE2 TRP A  36     6392   7130   5997  -1953  -1025   1025       C  
ATOM    273  CE3 TRP A  36     -54.608  12.898   8.355  1.00 48.43           C  
ANISOU  273  CE3 TRP A  36     6158   6518   5724  -1816  -1144   1058       C  
ATOM    274  NE1 TRP A  36     -57.565  11.151   7.446  1.00 58.38           N  
ANISOU  274  NE1 TRP A  36     7215   8083   6882  -2047   -997   1027       N  
ATOM    275  CZ2 TRP A  36     -57.215  12.648   9.426  1.00 44.69           C  
ANISOU  275  CZ2 TRP A  36     5553   6343   5084  -1914   -989    997       C  
ATOM    276  CZ3 TRP A  36     -54.980  13.555   9.513  1.00 49.49           C  
ANISOU  276  CZ3 TRP A  36     6314   6702   5787  -1779  -1122   1041       C  
ATOM    277  CH2 TRP A  36     -56.271  13.425  10.037  1.00 49.00           C  
ANISOU  277  CH2 TRP A  36     6188   6787   5641  -1826  -1039   1006       C  
ATOM    278  N   ILE A  37     -52.209  13.124   4.240  1.00 50.83           N  
ANISOU  278  N   ILE A  37     6434   6593   6288  -1773  -1238   1044       N  
ATOM    279  CA  ILE A  37     -50.893  13.384   3.683  1.00 43.15           C  
ANISOU  279  CA  ILE A  37     5491   5511   5392  -1751  -1266   1037       C  
ATOM    280  C   ILE A  37     -49.993  13.866   4.807  1.00 42.22           C  
ANISOU  280  C   ILE A  37     5422   5323   5296  -1690  -1314   1056       C  
ATOM    281  O   ILE A  37     -50.420  14.644   5.658  1.00 46.88           O  
ANISOU  281  O   ILE A  37     6027   5958   5828  -1636  -1333   1063       O  
ATOM    282  CB  ILE A  37     -50.976  14.472   2.604  1.00 44.51           C  
ANISOU  282  CB  ILE A  37     5644   5709   5558  -1722  -1283   1012       C  
ATOM    283  CG1 ILE A  37     -51.982  14.063   1.528  1.00 39.44           C  
ANISOU  283  CG1 ILE A  37     4962   5138   4884  -1786  -1254    999       C  
ATOM    284  CG2 ILE A  37     -49.604  14.740   2.005  1.00 43.29           C  
ANISOU  284  CG2 ILE A  37     5520   5456   5474  -1724  -1295    998       C  
ATOM    285  CD1 ILE A  37     -52.893  15.179   1.093  1.00 41.09           C  
ANISOU  285  CD1 ILE A  37     5140   5426   5044  -1738  -1295    986       C  
ATOM    286  N   ARG A  38     -48.750  13.405   4.821  1.00 36.33           N  
ANISOU  286  N   ARG A  38     4701   4466   4637  -1697  -1336   1060       N  
ATOM    287  CA  ARG A  38     -47.843  13.779   5.893  1.00 42.93           C  
ANISOU  287  CA  ARG A  38     5584   5226   5502  -1649  -1399   1084       C  
ATOM    288  C   ARG A  38     -46.541  14.307   5.330  1.00 49.22           C  
ANISOU  288  C   ARG A  38     6365   5947   6390  -1624  -1427   1065       C  
ATOM    289  O   ARG A  38     -46.196  14.028   4.182  1.00 48.52           O  
ANISOU  289  O   ARG A  38     6235   5846   6354  -1658  -1385   1029       O  
ATOM    290  CB  ARG A  38     -47.563  12.587   6.806  1.00 43.15           C  
ANISOU  290  CB  ARG A  38     5659   5180   5555  -1685  -1426   1114       C  
ATOM    291  CG  ARG A  38     -46.596  11.590   6.213  1.00 33.78           C  
ANISOU  291  CG  ARG A  38     4456   3892   4489  -1709  -1432   1096       C  
ATOM    292  CD  ARG A  38     -46.227  10.508   7.200  1.00 30.35           C  
ANISOU  292  CD  ARG A  38     4088   3358   4086  -1731  -1494   1130       C  
ATOM    293  NE  ARG A  38     -45.290   9.561   6.608  1.00 43.09           N  
ANISOU  293  NE  ARG A  38     5676   4865   5830  -1732  -1507   1100       N  
ATOM    294  CZ  ARG A  38     -44.847   8.464   7.208  1.00 50.34           C  
ANISOU  294  CZ  ARG A  38     6651   5669   6805  -1744  -1576   1118       C  
ATOM    295  NH1 ARG A  38     -45.258   8.162   8.432  1.00 53.50           N1+
ANISOU  295  NH1 ARG A  38     7153   6048   7127  -1777  -1638   1175       N1+
ATOM    296  NH2 ARG A  38     -43.993   7.669   6.580  1.00 51.10           N  
ANISOU  296  NH2 ARG A  38     6711   5669   7035  -1727  -1584   1074       N  
ATOM    297  N   GLN A  39     -45.823  15.071   6.146  1.00 54.94           N  
ANISOU  297  N   GLN A  39     7125   6624   7126  -1576  -1494   1086       N  
ATOM    298  CA  GLN A  39     -44.530  15.607   5.748  1.00 50.69           C  
ANISOU  298  CA  GLN A  39     6565   6020   6673  -1564  -1525   1070       C  
ATOM    299  C   GLN A  39     -43.494  15.449   6.848  1.00 43.29           C  
ANISOU  299  C   GLN A  39     5656   4986   5806  -1539  -1611   1102       C  
ATOM    300  O   GLN A  39     -43.536  16.153   7.855  1.00 48.72           O  
ANISOU  300  O   GLN A  39     6410   5665   6435  -1507  -1672   1139       O  
ATOM    301  CB  GLN A  39     -44.646  17.078   5.356  1.00 54.00           C  
ANISOU  301  CB  GLN A  39     7005   6484   7027  -1538  -1539   1062       C  
ATOM    302  CG  GLN A  39     -43.307  17.722   5.050  1.00 56.94           C  
ANISOU  302  CG  GLN A  39     7367   6798   7471  -1546  -1574   1050       C  
ATOM    303  CD  GLN A  39     -43.450  19.043   4.331  1.00 60.71           C  
ANISOU  303  CD  GLN A  39     7879   7312   7876  -1551  -1581   1037       C  
ATOM    304  NE2 GLN A  39     -42.474  19.368   3.493  1.00 74.75           N  
ANISOU  304  NE2 GLN A  39     9632   9065   9705  -1604  -1567   1007       N  
ATOM    305  OE1 GLN A  39     -44.424  19.765   4.525  1.00 55.87           O  
ANISOU  305  OE1 GLN A  39     7318   6749   7161  -1509  -1601   1049       O  
ATOM    306  N   PRO A  40     -42.560  14.511   6.658  1.00 40.24           N  
ANISOU  306  N   PRO A  40     5222   4519   5550  -1553  -1622   1083       N  
ATOM    307  CA  PRO A  40     -41.458  14.312   7.602  1.00 42.05           C  
ANISOU  307  CA  PRO A  40     5462   4642   5874  -1527  -1725   1110       C  
ATOM    308  C   PRO A  40     -40.543  15.523   7.590  1.00 49.48           C  
ANISOU  308  C   PRO A  40     6385   5573   6843  -1508  -1769   1109       C  
ATOM    309  O   PRO A  40     -40.517  16.251   6.597  1.00 54.98           O  
ANISOU  309  O   PRO A  40     7045   6327   7519  -1527  -1709   1072       O  
ATOM    310  CB  PRO A  40     -40.719  13.099   7.027  1.00 43.66           C  
ANISOU  310  CB  PRO A  40     5588   4773   6226  -1534  -1709   1065       C  
ATOM    311  CG  PRO A  40     -41.713  12.422   6.141  1.00 47.71           C  
ANISOU  311  CG  PRO A  40     6094   5348   6684  -1575  -1605   1036       C  
ATOM    312  CD  PRO A  40     -42.534  13.528   5.564  1.00 41.94           C  
ANISOU  312  CD  PRO A  40     5373   4732   5832  -1590  -1544   1033       C  
ATOM    313  N   PRO A  41     -39.799  15.742   8.680  1.00 51.28           N  
ANISOU  313  N   PRO A  41     6653   5724   7108  -1485  -1883   1152       N  
ATOM    314  CA  PRO A  41     -38.892  16.892   8.749  1.00 50.84           C  
ANISOU  314  CA  PRO A  41     6587   5654   7075  -1480  -1938   1158       C  
ATOM    315  C   PRO A  41     -37.959  16.929   7.542  1.00 51.40           C  
ANISOU  315  C   PRO A  41     6529   5735   7265  -1508  -1880   1090       C  
ATOM    316  O   PRO A  41     -37.343  15.917   7.201  1.00 45.74           O  
ANISOU  316  O   PRO A  41     5719   4973   6689  -1505  -1864   1048       O  
ATOM    317  CB  PRO A  41     -38.100  16.630  10.031  1.00 46.54           C  
ANISOU  317  CB  PRO A  41     6084   5001   6598  -1461  -2079   1211       C  
ATOM    318  CG  PRO A  41     -39.012  15.791  10.862  1.00 50.09           C  
ANISOU  318  CG  PRO A  41     6629   5430   6972  -1461  -2095   1250       C  
ATOM    319  CD  PRO A  41     -39.746  14.915   9.896  1.00 42.76           C  
ANISOU  319  CD  PRO A  41     5644   4558   6046  -1477  -1978   1202       C  
ATOM    320  N   GLY A  42     -37.874  18.087   6.896  1.00 57.55           N  
ANISOU  320  N   GLY A  42     7313   6570   7982  -1538  -1847   1074       N  
ATOM    321  CA  GLY A  42     -36.992  18.270   5.757  1.00 57.37           C  
ANISOU  321  CA  GLY A  42     7186   6567   8044  -1591  -1781   1007       C  
ATOM    322  C   GLY A  42     -37.153  17.237   4.654  1.00 57.45           C  
ANISOU  322  C   GLY A  42     7112   6600   8117  -1616  -1661    935       C  
ATOM    323  O   GLY A  42     -36.174  16.836   4.026  1.00 55.42           O  
ANISOU  323  O   GLY A  42     6739   6326   7993  -1643  -1613    867       O  
ATOM    324  N   LYS A  43     -38.388  16.804   4.416  1.00 56.41           N  
ANISOU  324  N   LYS A  43     7036   6507   7891  -1611  -1608    944       N  
ATOM    325  CA  LYS A  43     -38.669  15.855   3.343  1.00 57.22           C  
ANISOU  325  CA  LYS A  43     7085   6629   8027  -1645  -1497    882       C  
ATOM    326  C   LYS A  43     -39.900  16.280   2.555  1.00 52.75           C  
ANISOU  326  C   LYS A  43     6587   6144   7311  -1684  -1433    884       C  
ATOM    327  O   LYS A  43     -40.671  17.126   3.005  1.00 51.47           O  
ANISOU  327  O   LYS A  43     6506   6020   7030  -1661  -1480    934       O  
ATOM    328  CB  LYS A  43     -38.845  14.435   3.896  1.00 64.84           C  
ANISOU  328  CB  LYS A  43     8038   7533   9067  -1604  -1518    888       C  
ATOM    329  CG  LYS A  43     -37.583  13.862   4.531  1.00 75.12           C  
ANISOU  329  CG  LYS A  43     9263   8735  10543  -1560  -1596    875       C  
ATOM    330  CD  LYS A  43     -37.701  12.368   4.807  1.00 82.27           C  
ANISOU  330  CD  LYS A  43    10166   9564  11530  -1527  -1615    866       C  
ATOM    331  CE  LYS A  43     -36.442  11.849   5.494  1.00 96.70           C  
ANISOU  331  CE  LYS A  43    11921  11277  13542  -1469  -1724    854       C  
ATOM    332  NZ  LYS A  43     -36.475  10.378   5.736  1.00104.57           N1+
ANISOU  332  NZ  LYS A  43    12929  12176  14627  -1432  -1763    842       N1+
ATOM    333  N   ALA A  44     -40.078  15.690   1.377  1.00 51.26           N  
ANISOU  333  N   ALA A  44     6366   5977   7132  -1740  -1330    826       N  
ATOM    334  CA  ALA A  44     -41.208  16.023   0.517  1.00 49.14           C  
ANISOU  334  CA  ALA A  44     6160   5779   6733  -1786  -1282    827       C  
ATOM    335  C   ALA A  44     -42.513  15.477   1.086  1.00 52.96           C  
ANISOU  335  C   ALA A  44     6685   6291   7146  -1748  -1304    875       C  
ATOM    336  O   ALA A  44     -42.518  14.792   2.109  1.00 62.44           O  
ANISOU  336  O   ALA A  44     7881   7454   8388  -1699  -1347    906       O  
ATOM    337  CB  ALA A  44     -40.981  15.490  -0.888  1.00 45.14           C  
ANISOU  337  CB  ALA A  44     5622   5279   6252  -1873  -1168    751       C  
ATOM    338  N   LEU A  45     -43.617  15.782   0.414  1.00 40.49           N  
ANISOU  338  N   LEU A  45     5148   4780   5458  -1779  -1279    880       N  
ATOM    339  CA  LEU A  45     -44.927  15.331   0.851  1.00 39.74           C  
ANISOU  339  CA  LEU A  45     5074   4734   5294  -1756  -1289    916       C  
ATOM    340  C   LEU A  45     -45.173  13.886   0.439  1.00 50.19           C  
ANISOU  340  C   LEU A  45     6372   6041   6656  -1801  -1227    895       C  
ATOM    341  O   LEU A  45     -44.819  13.477  -0.667  1.00 54.06           O  
ANISOU  341  O   LEU A  45     6848   6513   7178  -1864  -1159    844       O  
ATOM    342  CB  LEU A  45     -46.016  16.238   0.277  1.00 46.60           C  
ANISOU  342  CB  LEU A  45     5981   5679   6047  -1764  -1304    926       C  
ATOM    343  CG  LEU A  45     -46.010  17.686   0.774  1.00 47.02           C  
ANISOU  343  CG  LEU A  45     6081   5743   6043  -1704  -1381    949       C  
ATOM    344  CD1 LEU A  45     -46.664  18.622  -0.237  1.00 49.70           C  
ANISOU  344  CD1 LEU A  45     6467   6120   6295  -1730  -1403    939       C  
ATOM    345  CD2 LEU A  45     -46.683  17.796   2.137  1.00 36.82           C  
ANISOU  345  CD2 LEU A  45     4797   4478   4714  -1622  -1426    988       C  
ATOM    346  N   GLU A  46     -45.785  13.121   1.337  1.00 53.50           N  
ANISOU  346  N   GLU A  46     6799   6464   7063  -1779  -1248    931       N  
ATOM    347  CA  GLU A  46     -46.095  11.719   1.078  1.00 48.26           C  
ANISOU  347  CA  GLU A  46     6135   5778   6422  -1827  -1205    920       C  
ATOM    348  C   GLU A  46     -47.577  11.444   1.305  1.00 45.25           C  
ANISOU  348  C   GLU A  46     5773   5484   5935  -1855  -1202    956       C  
ATOM    349  O   GLU A  46     -48.108  11.707   2.387  1.00 52.07           O  
ANISOU  349  O   GLU A  46     6650   6385   6748  -1819  -1242    996       O  
ATOM    350  CB  GLU A  46     -45.248  10.812   1.980  1.00 48.52           C  
ANISOU  350  CB  GLU A  46     6170   5710   6556  -1794  -1245    926       C  
ATOM    351  CG  GLU A  46     -45.514   9.324   1.799  1.00 50.78           C  
ANISOU  351  CG  GLU A  46     6478   5950   6866  -1840  -1219    916       C  
ATOM    352  CD  GLU A  46     -44.755   8.464   2.792  1.00 57.99           C  
ANISOU  352  CD  GLU A  46     7413   6748   7871  -1800  -1291    930       C  
ATOM    353  OE1 GLU A  46     -44.482   8.945   3.910  1.00 69.29           O  
ANISOU  353  OE1 GLU A  46     8864   8160   9303  -1754  -1369    973       O  
ATOM    354  OE2 GLU A  46     -44.434   7.304   2.458  1.00 56.35           O1-
ANISOU  354  OE2 GLU A  46     7217   6459   7734  -1817  -1278    897       O1-
ATOM    355  N   TRP A  47     -48.245  10.918   0.283  1.00 34.02           N  
ANISOU  355  N   TRP A  47     4350   4097   4477  -1926  -1150    938       N  
ATOM    356  CA  TRP A  47     -49.642  10.527   0.418  1.00 38.02           C  
ANISOU  356  CA  TRP A  47     4859   4692   4896  -1968  -1145    968       C  
ATOM    357  C   TRP A  47     -49.742   9.239   1.222  1.00 47.69           C  
ANISOU  357  C   TRP A  47     6115   5876   6131  -2000  -1148    991       C  
ATOM    358  O   TRP A  47     -48.880   8.365   1.122  1.00 47.78           O  
ANISOU  358  O   TRP A  47     6152   5781   6221  -2009  -1143    972       O  
ATOM    359  CB  TRP A  47     -50.300  10.352  -0.949  1.00 38.77           C  
ANISOU  359  CB  TRP A  47     4953   4829   4948  -2048  -1105    947       C  
ATOM    360  CG  TRP A  47     -51.694   9.812  -0.865  1.00 43.58           C  
ANISOU  360  CG  TRP A  47     5548   5529   5479  -2105  -1102    975       C  
ATOM    361  CD1 TRP A  47     -52.823  10.504  -0.540  1.00 43.38           C  
ANISOU  361  CD1 TRP A  47     5475   5620   5386  -2082  -1129    995       C  
ATOM    362  CD2 TRP A  47     -52.107   8.463  -1.110  1.00 50.80           C  
ANISOU  362  CD2 TRP A  47     6492   6431   6379  -2197  -1071    981       C  
ATOM    363  CE2 TRP A  47     -53.503   8.409  -0.911  1.00 52.90           C  
ANISOU  363  CE2 TRP A  47     6720   6817   6563  -2241  -1079   1010       C  
ATOM    364  CE3 TRP A  47     -51.434   7.293  -1.478  1.00 54.53           C  
ANISOU  364  CE3 TRP A  47     7020   6798   6901  -2246  -1039    960       C  
ATOM    365  NE1 TRP A  47     -53.916   9.670  -0.564  1.00 50.62           N  
ANISOU  365  NE1 TRP A  47     6373   6609   6251  -2162  -1111   1013       N  
ATOM    366  CZ2 TRP A  47     -54.237   7.232  -1.066  1.00 46.01           C  
ANISOU  366  CZ2 TRP A  47     5869   5967   5646  -2349  -1058   1028       C  
ATOM    367  CZ3 TRP A  47     -52.164   6.125  -1.632  1.00 47.94           C  
ANISOU  367  CZ3 TRP A  47     6223   5971   6021  -2343  -1024    977       C  
ATOM    368  CH2 TRP A  47     -53.551   6.104  -1.426  1.00 50.20           C  
ANISOU  368  CH2 TRP A  47     6477   6382   6214  -2401  -1034   1015       C  
ATOM    369  N   LEU A  48     -50.798   9.128   2.020  1.00 48.05           N  
ANISOU  369  N   LEU A  48     6160   6003   6095  -2019  -1159   1028       N  
ATOM    370  CA  LEU A  48     -50.932   8.026   2.965  1.00 45.61           C  
ANISOU  370  CA  LEU A  48     5904   5655   5769  -2063  -1173   1059       C  
ATOM    371  C   LEU A  48     -52.162   7.168   2.688  1.00 50.00           C  
ANISOU  371  C   LEU A  48     6465   6290   6244  -2172  -1138   1074       C  
ATOM    372  O   LEU A  48     -52.087   5.937   2.664  1.00 49.44           O  
ANISOU  372  O   LEU A  48     6457   6151   6177  -2243  -1138   1083       O  
ATOM    373  CB  LEU A  48     -51.005   8.573   4.391  1.00 39.22           C  
ANISOU  373  CB  LEU A  48     5114   4868   4921  -2017  -1212   1091       C  
ATOM    374  CG  LEU A  48     -49.717   8.730   5.199  1.00 44.98           C  
ANISOU  374  CG  LEU A  48     5888   5474   5726  -1950  -1278   1102       C  
ATOM    375  CD1 LEU A  48     -48.544   9.150   4.328  1.00 57.03           C  
ANISOU  375  CD1 LEU A  48     7376   6927   7364  -1893  -1282   1063       C  
ATOM    376  CD2 LEU A  48     -49.939   9.721   6.331  1.00 40.52           C  
ANISOU  376  CD2 LEU A  48     5336   4959   5101  -1900  -1305   1125       C  
ATOM    377  N   ALA A  49     -53.297   7.825   2.483  1.00 42.62           N  
ANISOU  377  N   ALA A  49     5462   5495   5237  -2183  -1115   1074       N  
ATOM    378  CA  ALA A  49     -54.567   7.121   2.397  1.00 44.51           C  
ANISOU  378  CA  ALA A  49     5683   5834   5394  -2290  -1086   1090       C  
ATOM    379  C   ALA A  49     -55.689   8.053   1.959  1.00 45.37           C  
ANISOU  379  C   ALA A  49     5686   6093   5459  -2274  -1075   1076       C  
ATOM    380  O   ALA A  49     -55.548   9.273   2.005  1.00 43.77           O  
ANISOU  380  O   ALA A  49     5440   5915   5274  -2171  -1096   1058       O  
ATOM    381  CB  ALA A  49     -54.905   6.494   3.746  1.00 31.07           C  
ANISOU  381  CB  ALA A  49     4029   4146   3630  -2344  -1087   1122       C  
ATOM    382  N   ASP A  50     -56.801   7.471   1.524  1.00 42.16           N  
ANISOU  382  N   ASP A  50     5241   5780   4998  -2375  -1053   1083       N  
ATOM    383  CA  ASP A  50     -58.014   8.247   1.308  1.00 50.99           C  
ANISOU  383  CA  ASP A  50     6239   7053   6081  -2360  -1055   1068       C  
ATOM    384  C   ASP A  50     -59.273   7.386   1.405  1.00 53.82           C  
ANISOU  384  C   ASP A  50     6548   7532   6370  -2491  -1023   1082       C  
ATOM    385  O   ASP A  50     -59.200   6.170   1.597  1.00 50.17           O  
ANISOU  385  O   ASP A  50     6165   7023   5873  -2606  -1003   1109       O  
ATOM    386  CB  ASP A  50     -57.964   9.025  -0.012  1.00 57.39           C  
ANISOU  386  CB  ASP A  50     7025   7853   6929  -2317  -1095   1049       C  
ATOM    387  CG  ASP A  50     -58.144   8.140  -1.229  1.00 59.30           C  
ANISOU  387  CG  ASP A  50     7308   8064   7160  -2435  -1094   1058       C  
ATOM    388  OD1 ASP A  50     -58.125   6.902  -1.081  1.00 58.37           O  
ANISOU  388  OD1 ASP A  50     7250   7910   7018  -2538  -1062   1078       O  
ATOM    389  OD2 ASP A  50     -58.298   8.694  -2.340  1.00 58.28           O1-
ANISOU  389  OD2 ASP A  50     7169   7935   7039  -2431  -1131   1047       O1-
ATOM    390  N   ILE A  51     -60.425   8.034   1.279  1.00 50.07           N  
ANISOU  390  N   ILE A  51     5939   7208   5878  -2475  -1026   1061       N  
ATOM    391  CA  ILE A  51     -61.705   7.366   1.447  1.00 46.11           C  
ANISOU  391  CA  ILE A  51     5354   6851   5315  -2599   -992   1065       C  
ATOM    392  C   ILE A  51     -62.772   8.153   0.693  1.00 44.86           C  
ANISOU  392  C   ILE A  51     5042   6821   5181  -2561  -1031   1037       C  
ATOM    393  O   ILE A  51     -62.646   9.364   0.520  1.00 50.86           O  
ANISOU  393  O   ILE A  51     5755   7581   5990  -2419  -1075   1007       O  
ATOM    394  CB  ILE A  51     -62.064   7.238   2.945  1.00 44.48           C  
ANISOU  394  CB  ILE A  51     5126   6726   5049  -2622   -927   1057       C  
ATOM    395  CG1 ILE A  51     -63.376   6.475   3.134  1.00 49.17           C  
ANISOU  395  CG1 ILE A  51     5632   7480   5571  -2779   -878   1058       C  
ATOM    396  CG2 ILE A  51     -62.123   8.608   3.609  1.00 42.56           C  
ANISOU  396  CG2 ILE A  51     4799   6540   4832  -2463   -922   1010       C  
ATOM    397  CD1 ILE A  51     -63.763   6.298   4.587  1.00 47.94           C  
ANISOU  397  CD1 ILE A  51     5467   7412   5337  -2834   -799   1044       C  
ATOM    398  N   TRP A  52     -63.808   7.466   0.226  1.00 36.71           N  
ANISOU  398  N   TRP A  52     3941   5892   4116  -2691  -1029   1048       N  
ATOM    399  CA  TRP A  52     -64.816   8.117  -0.601  1.00 41.00           C  
ANISOU  399  CA  TRP A  52     4340   6544   4693  -2664  -1091   1026       C  
ATOM    400  C   TRP A  52     -66.212   7.982  -0.010  1.00 57.67           C  
ANISOU  400  C   TRP A  52     6268   8864   6780  -2724  -1049    998       C  
ATOM    401  O   TRP A  52     -66.406   7.319   1.008  1.00 68.93           O  
ANISOU  401  O   TRP A  52     7697  10349   8143  -2813   -961    999       O  
ATOM    402  CB  TRP A  52     -64.756   7.585  -2.037  1.00 39.97           C  
ANISOU  402  CB  TRP A  52     4286   6337   4563  -2760  -1155   1063       C  
ATOM    403  CG  TRP A  52     -63.400   7.785  -2.658  1.00 47.35           C  
ANISOU  403  CG  TRP A  52     5384   7084   5524  -2704  -1179   1073       C  
ATOM    404  CD1 TRP A  52     -62.252   7.122  -2.335  1.00 49.99           C  
ANISOU  404  CD1 TRP A  52     5864   7282   5850  -2724  -1129   1088       C  
ATOM    405  CD2 TRP A  52     -63.047   8.714  -3.695  1.00 45.70           C  
ANISOU  405  CD2 TRP A  52     5205   6803   5354  -2626  -1259   1063       C  
ATOM    406  CE2 TRP A  52     -61.667   8.552  -3.947  1.00 45.28           C  
ANISOU  406  CE2 TRP A  52     5308   6584   5311  -2613  -1233   1068       C  
ATOM    407  CE3 TRP A  52     -63.760   9.663  -4.437  1.00 49.43           C  
ANISOU  407  CE3 TRP A  52     5594   7330   5855  -2572  -1358   1050       C  
ATOM    408  NE1 TRP A  52     -61.208   7.575  -3.104  1.00 46.53           N  
ANISOU  408  NE1 TRP A  52     5523   6706   5450  -2662  -1157   1081       N  
ATOM    409  CZ2 TRP A  52     -60.985   9.305  -4.907  1.00 46.96           C  
ANISOU  409  CZ2 TRP A  52     5597   6698   5547  -2566  -1284   1058       C  
ATOM    410  CZ3 TRP A  52     -63.079  10.413  -5.393  1.00 56.88           C  
ANISOU  410  CZ3 TRP A  52     6639   8159   6816  -2524  -1428   1048       C  
ATOM    411  CH2 TRP A  52     -61.705  10.228  -5.617  1.00 50.54           C  
ANISOU  411  CH2 TRP A  52     5992   7202   6008  -2530  -1382   1052       C  
ATOM    412  N   TRP A  53     -67.182   8.628  -0.644  1.00 55.68           N  
ANISOU  412  N   TRP A  53     5857   8721   6578  -2680  -1116    969       N  
ATOM    413  CA  TRP A  53     -68.540   8.646  -0.122  1.00 53.36           C  
ANISOU  413  CA  TRP A  53     5348   8642   6285  -2716  -1077    924       C  
ATOM    414  C   TRP A  53     -69.158   7.253  -0.154  1.00 57.56           C  
ANISOU  414  C   TRP A  53     5880   9249   6740  -2948  -1028    963       C  
ATOM    415  O   TRP A  53     -70.072   6.953   0.614  1.00 60.09           O  
ANISOU  415  O   TRP A  53     6061   9743   7027  -3030   -948    931       O  
ATOM    416  CB  TRP A  53     -69.403   9.640  -0.904  1.00 55.32           C  
ANISOU  416  CB  TRP A  53     5423   8972   6624  -2606  -1188    884       C  
ATOM    417  CG  TRP A  53     -69.863   9.131  -2.231  1.00 56.55           C  
ANISOU  417  CG  TRP A  53     5584   9117   6786  -2724  -1290    931       C  
ATOM    418  CD1 TRP A  53     -71.099   8.649  -2.533  1.00 51.91           C  
ANISOU  418  CD1 TRP A  53     4833   8686   6204  -2842  -1312    929       C  
ATOM    419  CD2 TRP A  53     -69.095   9.051  -3.439  1.00 54.04           C  
ANISOU  419  CD2 TRP A  53     5448   8622   6464  -2747  -1382    987       C  
ATOM    420  CE2 TRP A  53     -69.934   8.511  -4.433  1.00 47.35           C  
ANISOU  420  CE2 TRP A  53     4554   7826   5612  -2883  -1462   1019       C  
ATOM    421  CE3 TRP A  53     -67.780   9.382  -3.776  1.00 60.34           C  
ANISOU  421  CE3 TRP A  53     6441   9228   7257  -2677  -1399   1007       C  
ATOM    422  NE1 TRP A  53     -71.152   8.275  -3.852  1.00 56.29           N  
ANISOU  422  NE1 TRP A  53     5469   9164   6755  -2937  -1424    986       N  
ATOM    423  CZ2 TRP A  53     -69.507   8.295  -5.741  1.00 41.26           C  
ANISOU  423  CZ2 TRP A  53     3943   6914   4822  -2952  -1555   1071       C  
ATOM    424  CZ3 TRP A  53     -67.354   9.167  -5.078  1.00 67.18           C  
ANISOU  424  CZ3 TRP A  53     7451   9966   8110  -2747  -1479   1050       C  
ATOM    425  CH2 TRP A  53     -68.218   8.628  -6.045  1.00 55.39           C  
ANISOU  425  CH2 TRP A  53     5924   8520   6601  -2884  -1554   1082       C  
ATOM    426  N   ASP A  54     -68.651   6.402  -1.041  1.00 62.29           N  
ANISOU  426  N   ASP A  54     6643   9719   7307  -3062  -1071   1029       N  
ATOM    427  CA  ASP A  54     -69.149   5.035  -1.155  1.00 75.25           C  
ANISOU  427  CA  ASP A  54     8324  11403   8866  -3290  -1040   1074       C  
ATOM    428  C   ASP A  54     -68.313   4.065  -0.323  1.00 71.81           C  
ANISOU  428  C   ASP A  54     8078  10859   8346  -3380   -959   1108       C  
ATOM    429  O   ASP A  54     -68.411   2.849  -0.481  1.00 76.80           O  
ANISOU  429  O   ASP A  54     8817  11462   8901  -3565   -948   1155       O  
ATOM    430  CB  ASP A  54     -69.206   4.593  -2.621  1.00 81.73           C  
ANISOU  430  CB  ASP A  54     9221  12145   9690  -3379  -1138   1123       C  
ATOM    431  CG  ASP A  54     -67.860   4.676  -3.311  1.00 78.61           C  
ANISOU  431  CG  ASP A  54     9035  11523   9309  -3309  -1175   1147       C  
ATOM    432  OD1 ASP A  54     -66.838   4.834  -2.612  1.00 78.83           O  
ANISOU  432  OD1 ASP A  54     9161  11450   9342  -3219  -1123   1137       O  
ATOM    433  OD2 ASP A  54     -67.825   4.576  -4.556  1.00 75.51           O1-
ANISOU  433  OD2 ASP A  54     8711  11057   8922  -3354  -1254   1173       O1-
ATOM    434  N   ASP A  55     -67.493   4.627   0.560  1.00 66.54           N  
ANISOU  434  N   ASP A  55     7464  10125   7694  -3248   -918   1084       N  
ATOM    435  CA  ASP A  55     -66.686   3.864   1.513  1.00 64.41           C  
ANISOU  435  CA  ASP A  55     7367   9751   7356  -3309   -859   1111       C  
ATOM    436  C   ASP A  55     -65.484   3.147   0.884  1.00 49.70           C  
ANISOU  436  C   ASP A  55     5725   7663   5497  -3327   -904   1159       C  
ATOM    437  O   ASP A  55     -64.842   2.318   1.528  1.00 54.17           O  
ANISOU  437  O   ASP A  55     6447   8122   6012  -3393   -882   1188       O  
ATOM    438  CB  ASP A  55     -67.550   2.884   2.313  1.00 80.16           C  
ANISOU  438  CB  ASP A  55     9342  11873   9241  -3514   -786   1123       C  
ATOM    439  CG  ASP A  55     -66.930   2.518   3.661  1.00 94.50           C  
ANISOU  439  CG  ASP A  55    11296  13626  10985  -3545   -724   1131       C  
ATOM    440  OD1 ASP A  55     -66.282   3.388   4.293  1.00 76.98           O  
ANISOU  440  OD1 ASP A  55     9084  11358   8805  -3385   -712   1102       O  
ATOM    441  OD2 ASP A  55     -67.099   1.356   4.094  1.00103.44           O1-
ANISOU  441  OD2 ASP A  55    12543  14748  12013  -3739   -698   1171       O1-
ATOM    442  N   LYS A  56     -65.177   3.474  -0.367  1.00 38.10           N  
ANISOU  442  N   LYS A  56     4271   6117   4089  -3268   -971   1162       N  
ATOM    443  CA  LYS A  56     -63.960   2.980  -1.002  1.00 42.94           C  
ANISOU  443  CA  LYS A  56     5073   6520   4722  -3258   -997   1185       C  
ATOM    444  C   LYS A  56     -62.719   3.578  -0.340  1.00 47.58           C  
ANISOU  444  C   LYS A  56     5726   6989   5363  -3101   -986   1166       C  
ATOM    445  O   LYS A  56     -62.663   4.781  -0.082  1.00 49.04           O  
ANISOU  445  O   LYS A  56     5816   7219   5595  -2957   -993   1134       O  
ATOM    446  CB  LYS A  56     -63.957   3.309  -2.494  1.00 59.26           C  
ANISOU  446  CB  LYS A  56     7141   8544   6829  -3243  -1059   1183       C  
ATOM    447  CG  LYS A  56     -64.507   2.212  -3.377  1.00 78.04           C  
ANISOU  447  CG  LYS A  56     9585  10918   9150  -3426  -1081   1218       C  
ATOM    448  CD  LYS A  56     -64.343   2.580  -4.837  1.00 96.84           C  
ANISOU  448  CD  LYS A  56    12004  13229  11561  -3413  -1142   1215       C  
ATOM    449  CE  LYS A  56     -64.350   1.349  -5.722  1.00115.48           C  
ANISOU  449  CE  LYS A  56    14514  15501  13861  -3583  -1151   1247       C  
ATOM    450  NZ  LYS A  56     -63.907   1.678  -7.106  1.00126.82           N1+
ANISOU  450  NZ  LYS A  56    16035  16834  15317  -3572  -1193   1236       N1+
ATOM    451  N   LYS A  57     -61.724   2.735  -0.082  1.00 45.55           N  
ANISOU  451  N   LYS A  57     5633   6573   5101  -3128   -980   1186       N  
ATOM    452  CA  LYS A  57     -60.516   3.159   0.615  1.00 41.89           C  
ANISOU  452  CA  LYS A  57     5234   5990   4691  -2996   -981   1173       C  
ATOM    453  C   LYS A  57     -59.248   2.816  -0.165  1.00 42.90           C  
ANISOU  453  C   LYS A  57     5487   5928   4887  -2953  -1003   1166       C  
ATOM    454  O   LYS A  57     -59.191   1.796  -0.851  1.00 44.45           O  
ANISOU  454  O   LYS A  57     5777   6049   5064  -3055  -1007   1177       O  
ATOM    455  CB  LYS A  57     -60.451   2.511   2.002  1.00 37.91           C  
ANISOU  455  CB  LYS A  57     4802   5473   4127  -3056   -960   1196       C  
ATOM    456  CG  LYS A  57     -61.695   2.703   2.866  1.00 48.20           C  
ANISOU  456  CG  LYS A  57     5994   6972   5349  -3128   -912   1193       C  
ATOM    457  CD  LYS A  57     -61.550   1.971   4.204  1.00 56.39           C  
ANISOU  457  CD  LYS A  57     7147   7975   6305  -3220   -893   1220       C  
ATOM    458  CE  LYS A  57     -62.778   2.145   5.101  1.00 64.37           C  
ANISOU  458  CE  LYS A  57     8047   9189   7221  -3312   -821   1204       C  
ATOM    459  NZ  LYS A  57     -63.991   1.453   4.580  1.00 72.42           N1+
ANISOU  459  NZ  LYS A  57     8995  10346   8175  -3486   -795   1214       N1+
ATOM    460  N   HIS A  58     -58.231   3.668  -0.045  1.00 39.21           N  
ANISOU  460  N   HIS A  58     5017   5383   4496  -2807  -1013   1141       N  
ATOM    461  CA  HIS A  58     -56.923   3.405  -0.642  1.00 43.64           C  
ANISOU  461  CA  HIS A  58     5674   5773   5134  -2757  -1021   1119       C  
ATOM    462  C   HIS A  58     -55.804   3.699   0.347  1.00 54.04           C  
ANISOU  462  C   HIS A  58     7025   6995   6514  -2646  -1037   1113       C  
ATOM    463  O   HIS A  58     -55.936   4.577   1.197  1.00 56.13           O  
ANISOU  463  O   HIS A  58     7228   7328   6771  -2573  -1043   1118       O  
ATOM    464  CB  HIS A  58     -56.728   4.240  -1.905  1.00 38.17           C  
ANISOU  464  CB  HIS A  58     4943   5080   4481  -2710  -1021   1087       C  
ATOM    465  CG  HIS A  58     -57.774   3.997  -2.950  1.00 50.84           C  
ANISOU  465  CG  HIS A  58     6527   6763   6028  -2821  -1026   1096       C  
ATOM    466  CD2 HIS A  58     -57.861   3.056  -3.916  1.00 57.29           C  
ANISOU  466  CD2 HIS A  58     7430   7521   6818  -2935  -1016   1097       C  
ATOM    467  ND1 HIS A  58     -58.901   4.778  -3.063  1.00 56.74           N  
ANISOU  467  ND1 HIS A  58     7156   7661   6741  -2821  -1052   1105       N  
ATOM    468  CE1 HIS A  58     -59.642   4.330  -4.063  1.00 63.00           C  
ANISOU  468  CE1 HIS A  58     7959   8489   7492  -2935  -1068   1117       C  
ATOM    469  NE2 HIS A  58     -59.035   3.288  -4.597  1.00 67.45           N  
ANISOU  469  NE2 HIS A  58     8653   8926   8050  -3012  -1043   1115       N  
ATOM    470  N   TYR A  59     -54.705   2.961   0.232  1.00 55.01           N  
ANISOU  470  N   TYR A  59     7243   6956   6702  -2631  -1048   1099       N  
ATOM    471  CA  TYR A  59     -53.570   3.132   1.133  1.00 47.46           C  
ANISOU  471  CA  TYR A  59     6318   5893   5820  -2529  -1083   1095       C  
ATOM    472  C   TYR A  59     -52.247   3.091   0.381  1.00 53.41           C  
ANISOU  472  C   TYR A  59     7093   6509   6691  -2456  -1079   1044       C  
ATOM    473  O   TYR A  59     -52.119   2.408  -0.636  1.00 54.82           O  
ANISOU  473  O   TYR A  59     7312   6630   6885  -2507  -1048   1014       O  
ATOM    474  CB  TYR A  59     -53.555   2.043   2.201  1.00 40.56           C  
ANISOU  474  CB  TYR A  59     5551   4948   4912  -2592  -1125   1133       C  
ATOM    475  CG  TYR A  59     -54.827   1.914   3.004  1.00 48.41           C  
ANISOU  475  CG  TYR A  59     6538   6078   5779  -2696  -1114   1177       C  
ATOM    476  CD1 TYR A  59     -55.037   2.686   4.141  1.00 49.77           C  
ANISOU  476  CD1 TYR A  59     6673   6324   5913  -2656  -1117   1193       C  
ATOM    477  CD2 TYR A  59     -55.807   1.004   2.640  1.00 42.15           C  
ANISOU  477  CD2 TYR A  59     5779   5339   4898  -2844  -1094   1197       C  
ATOM    478  CE1 TYR A  59     -56.193   2.562   4.882  1.00 44.48           C  
ANISOU  478  CE1 TYR A  59     5988   5787   5125  -2759  -1087   1218       C  
ATOM    479  CE2 TYR A  59     -56.963   0.871   3.375  1.00 47.83           C  
ANISOU  479  CE2 TYR A  59     6477   6196   5501  -2955  -1072   1229       C  
ATOM    480  CZ  TYR A  59     -57.152   1.651   4.495  1.00 55.13           C  
ANISOU  480  CZ  TYR A  59     7353   7199   6392  -2911  -1061   1234       C  
ATOM    481  OH  TYR A  59     -58.310   1.517   5.230  1.00 65.83           O  
ANISOU  481  OH  TYR A  59     8680   8703   7630  -3030  -1020   1252       O  
ATOM    482  N   ASN A  60     -51.262   3.815   0.901  1.00 57.55           N  
ANISOU  482  N   ASN A  60     7589   6983   7296  -2343  -1105   1030       N  
ATOM    483  CA  ASN A  60     -49.924   3.814   0.328  1.00 59.49           C  
ANISOU  483  CA  ASN A  60     7831   7108   7666  -2271  -1096    974       C  
ATOM    484  C   ASN A  60     -49.136   2.582   0.766  1.00 61.51           C  
ANISOU  484  C   ASN A  60     8167   7204   7999  -2261  -1142    964       C  
ATOM    485  O   ASN A  60     -48.842   2.417   1.949  1.00 60.87           O  
ANISOU  485  O   ASN A  60     8123   7071   7935  -2227  -1216   1000       O  
ATOM    486  CB  ASN A  60     -49.180   5.089   0.724  1.00 58.46           C  
ANISOU  486  CB  ASN A  60     7632   6989   7592  -2164  -1116    965       C  
ATOM    487  CG  ASN A  60     -47.853   5.232   0.013  1.00 59.63           C  
ANISOU  487  CG  ASN A  60     7750   7043   7864  -2107  -1090    897       C  
ATOM    488  ND2 ASN A  60     -47.359   6.460  -0.072  1.00 54.87           N  
ANISOU  488  ND2 ASN A  60     7086   6475   7286  -2048  -1087    883       N  
ATOM    489  OD1 ASN A  60     -47.275   4.249  -0.455  1.00 64.16           O  
ANISOU  489  OD1 ASN A  60     8355   7513   8509  -2118  -1070    852       O  
ATOM    490  N   PRO A  61     -48.793   1.714  -0.198  1.00 63.71           N  
ANISOU  490  N   PRO A  61     8485   7399   8324  -2291  -1103    911       N  
ATOM    491  CA  PRO A  61     -48.109   0.434   0.033  1.00 58.19           C  
ANISOU  491  CA  PRO A  61     7871   6534   7704  -2277  -1150    888       C  
ATOM    492  C   PRO A  61     -46.874   0.561   0.927  1.00 50.61           C  
ANISOU  492  C   PRO A  61     6888   5462   6879  -2156  -1230    876       C  
ATOM    493  O   PRO A  61     -46.552  -0.379   1.651  1.00 53.89           O  
ANISOU  493  O   PRO A  61     7390   5750   7334  -2143  -1321    893       O  
ATOM    494  CB  PRO A  61     -47.706  -0.001  -1.377  1.00 57.69           C  
ANISOU  494  CB  PRO A  61     7811   6417   7693  -2292  -1065    803       C  
ATOM    495  CG  PRO A  61     -48.714   0.639  -2.268  1.00 54.79           C  
ANISOU  495  CG  PRO A  61     7414   6195   7207  -2381   -993    817       C  
ATOM    496  CD  PRO A  61     -49.060   1.951  -1.627  1.00 56.62           C  
ANISOU  496  CD  PRO A  61     7561   6552   7398  -2342  -1015    866       C  
ATOM    497  N   SER A  62     -46.200   1.704   0.877  1.00 40.79           N  
ANISOU  497  N   SER A  62     5539   4259   5702  -2075  -1210    851       N  
ATOM    498  CA  SER A  62     -45.034   1.943   1.722  1.00 53.61           C  
ANISOU  498  CA  SER A  62     7127   5789   7455  -1966  -1293    843       C  
ATOM    499  C   SER A  62     -45.375   1.803   3.201  1.00 70.61           C  
ANISOU  499  C   SER A  62     9359   7920   9548  -1974  -1409    932       C  
ATOM    500  O   SER A  62     -44.626   1.196   3.965  1.00 84.80           O  
ANISOU  500  O   SER A  62    11207   9578  11436  -1923  -1518    939       O  
ATOM    501  CB  SER A  62     -44.453   3.334   1.460  1.00 62.55           C  
ANISOU  501  CB  SER A  62     8142   6995   8630  -1907  -1252    817       C  
ATOM    502  OG  SER A  62     -44.064   3.481   0.105  1.00 79.20           O  
ANISOU  502  OG  SER A  62    10190   9118  10784  -1917  -1142    731       O  
ATOM    503  N   LEU A  63     -46.507   2.373   3.600  1.00 73.28           N  
ANISOU  503  N   LEU A  63     9713   8395   9735  -2041  -1388    994       N  
ATOM    504  CA  LEU A  63     -46.939   2.336   4.994  1.00 74.70           C  
ANISOU  504  CA  LEU A  63     9975   8577   9831  -2072  -1472   1071       C  
ATOM    505  C   LEU A  63     -47.999   1.266   5.223  1.00 85.09           C  
ANISOU  505  C   LEU A  63    11405   9902  11022  -2200  -1477   1114       C  
ATOM    506  O   LEU A  63     -48.974   1.485   5.942  1.00 96.00           O  
ANISOU  506  O   LEU A  63    12821  11387  12268  -2277  -1470   1167       O  
ATOM    507  CB  LEU A  63     -47.477   3.702   5.420  1.00 66.70           C  
ANISOU  507  CB  LEU A  63     8901   7710   8732  -2059  -1439   1101       C  
ATOM    508  CG  LEU A  63     -46.489   4.848   5.227  1.00 83.66           C  
ANISOU  508  CG  LEU A  63    10952   9854  10980  -1951  -1440   1067       C  
ATOM    509  CD1 LEU A  63     -47.135   6.176   5.568  1.00 83.18           C  
ANISOU  509  CD1 LEU A  63    10850   9931  10821  -1940  -1411   1093       C  
ATOM    510  CD2 LEU A  63     -45.241   4.616   6.068  1.00100.19           C  
ANISOU  510  CD2 LEU A  63    13075  11797  13196  -1878  -1556   1074       C  
ATOM    511  N   LYS A  64     -47.803   0.108   4.606  1.00 80.70           N  
ANISOU  511  N   LYS A  64    10910   9240  10511  -2227  -1485   1084       N  
ATOM    512  CA  LYS A  64     -48.747  -0.990   4.725  1.00 81.26           C  
ANISOU  512  CA  LYS A  64    11105   9307  10464  -2363  -1496   1123       C  
ATOM    513  C   LYS A  64     -48.040  -2.158   5.387  1.00 71.54           C  
ANISOU  513  C   LYS A  64    10018   7870   9295  -2353  -1629   1136       C  
ATOM    514  O   LYS A  64     -46.842  -2.343   5.191  1.00 79.48           O  
ANISOU  514  O   LYS A  64    10998   8734  10465  -2234  -1681   1083       O  
ATOM    515  CB  LYS A  64     -49.254  -1.390   3.339  1.00 95.31           C  
ANISOU  515  CB  LYS A  64    12861  11132  12221  -2420  -1399   1080       C  
ATOM    516  CG  LYS A  64     -50.637  -2.023   3.336  1.00101.99           C  
ANISOU  516  CG  LYS A  64    13782  12068  12900  -2587  -1374   1130       C  
ATOM    517  CD  LYS A  64     -51.662  -1.081   3.948  1.00 94.96           C  
ANISOU  517  CD  LYS A  64    12821  11370  11891  -2637  -1333   1176       C  
ATOM    518  CE  LYS A  64     -52.962  -1.799   4.256  1.00 77.16           C  
ANISOU  518  CE  LYS A  64    10641   9202   9475  -2813  -1321   1228       C  
ATOM    519  NZ  LYS A  64     -53.858  -0.940   5.077  1.00 72.85           N1+
ANISOU  519  NZ  LYS A  64    10022   8831   8825  -2851  -1284   1260       N1+
ATOM    520  N   ASP A  65     -48.767  -2.941   6.177  1.00 64.67           N  
ANISOU  520  N   ASP A  65     9299   6978   8295  -2481  -1690   1202       N  
ATOM    521  CA  ASP A  65     -50.189  -2.730   6.417  1.00 70.41           C  
ANISOU  521  CA  ASP A  65    10033   7887   8834  -2628  -1616   1252       C  
ATOM    522  C   ASP A  65     -50.443  -2.104   7.784  1.00 66.64           C  
ANISOU  522  C   ASP A  65     9584   7468   8269  -2656  -1653   1309       C  
ATOM    523  O   ASP A  65     -51.007  -2.741   8.679  1.00 59.74           O  
ANISOU  523  O   ASP A  65     8854   6578   7266  -2789  -1703   1366       O  
ATOM    524  CB  ASP A  65     -50.950  -4.054   6.290  1.00 88.86           C  
ANISOU  524  CB  ASP A  65    12520  10184  11060  -2788  -1635   1282       C  
ATOM    525  CG  ASP A  65     -50.308  -5.183   7.084  1.00 93.77           C  
ANISOU  525  CG  ASP A  65    13341  10582  11705  -2805  -1794   1312       C  
ATOM    526  OD1 ASP A  65     -49.433  -4.902   7.931  1.00 85.71           O  
ANISOU  526  OD1 ASP A  65    12344   9458  10764  -2712  -1895   1323       O  
ATOM    527  OD2 ASP A  65     -50.684  -6.355   6.861  1.00 99.71           O1-
ANISOU  527  OD2 ASP A  65    14238  11254  12393  -2916  -1831   1326       O1-
ATOM    528  N   ARG A  66     -50.032  -0.848   7.934  1.00 60.82           N  
ANISOU  528  N   ARG A  66     8722   6797   7589  -2542  -1625   1292       N  
ATOM    529  CA  ARG A  66     -50.102  -0.168   9.221  1.00 55.60           C  
ANISOU  529  CA  ARG A  66     8095   6171   6858  -2549  -1662   1336       C  
ATOM    530  C   ARG A  66     -51.212   0.873   9.254  1.00 53.63           C  
ANISOU  530  C   ARG A  66     7734   6148   6494  -2584  -1538   1334       C  
ATOM    531  O   ARG A  66     -51.408   1.551  10.263  1.00 59.83           O  
ANISOU  531  O   ARG A  66     8537   6989   7208  -2591  -1541   1358       O  
ATOM    532  CB  ARG A  66     -48.769   0.514   9.517  1.00 52.59           C  
ANISOU  532  CB  ARG A  66     7671   5683   6626  -2392  -1741   1321       C  
ATOM    533  CG  ARG A  66     -47.547  -0.342   9.240  1.00 57.62           C  
ANISOU  533  CG  ARG A  66     8354   6109   7430  -2312  -1853   1296       C  
ATOM    534  CD  ARG A  66     -46.294   0.510   9.247  1.00 57.44           C  
ANISOU  534  CD  ARG A  66     8226   6028   7570  -2155  -1897   1263       C  
ATOM    535  NE  ARG A  66     -46.263   1.397  10.407  1.00 58.65           N  
ANISOU  535  NE  ARG A  66     8407   6215   7662  -2150  -1944   1313       N  
ATOM    536  CZ  ARG A  66     -45.650   2.577  10.429  1.00 60.69           C  
ANISOU  536  CZ  ARG A  66     8558   6513   7990  -2049  -1934   1296       C  
ATOM    537  NH1 ARG A  66     -45.019   3.024   9.348  1.00 59.63           N1+
ANISOU  537  NH1 ARG A  66     8275   6396   7987  -1952  -1875   1229       N1+
ATOM    538  NH2 ARG A  66     -45.677   3.319  11.531  1.00 55.34           N  
ANISOU  538  NH2 ARG A  66     7932   5856   7240  -2057  -1981   1343       N  
ATOM    539  N   LEU A  67     -51.937   0.996   8.150  1.00 46.25           N  
ANISOU  539  N   LEU A  67     6691   5338   5545  -2605  -1436   1301       N  
ATOM    540  CA  LEU A  67     -52.918   2.063   7.997  1.00 44.85           C  
ANISOU  540  CA  LEU A  67     6379   5367   5294  -2606  -1332   1285       C  
ATOM    541  C   LEU A  67     -54.353   1.572   8.074  1.00 53.10           C  
ANISOU  541  C   LEU A  67     7426   6557   6192  -2767  -1264   1301       C  
ATOM    542  O   LEU A  67     -54.698   0.533   7.519  1.00 63.61           O  
ANISOU  542  O   LEU A  67     8811   7862   7496  -2869  -1264   1310       O  
ATOM    543  CB  LEU A  67     -52.704   2.785   6.667  1.00 40.26           C  
ANISOU  543  CB  LEU A  67     5657   4830   4808  -2505  -1279   1234       C  
ATOM    544  CG  LEU A  67     -51.691   3.928   6.641  1.00 48.05           C  
ANISOU  544  CG  LEU A  67     6578   5779   5901  -2351  -1302   1208       C  
ATOM    545  CD1 LEU A  67     -50.648   3.781   7.739  1.00 53.39           C  
ANISOU  545  CD1 LEU A  67     7350   6308   6627  -2305  -1403   1235       C  
ATOM    546  CD2 LEU A  67     -51.043   4.009   5.268  1.00 48.32           C  
ANISOU  546  CD2 LEU A  67     6546   5766   6047  -2288  -1278   1159       C  
ATOM    547  N   THR A  68     -55.189   2.343   8.758  1.00 49.26           N  
ANISOU  547  N   THR A  68     6877   6228   5612  -2791  -1202   1299       N  
ATOM    548  CA  THR A  68     -56.613   2.059   8.833  1.00 54.04           C  
ANISOU  548  CA  THR A  68     7438   7007   6088  -2938  -1119   1300       C  
ATOM    549  C   THR A  68     -57.389   3.364   8.746  1.00 55.83           C  
ANISOU  549  C   THR A  68     7485   7425   6303  -2865  -1034   1256       C  
ATOM    550  O   THR A  68     -57.252   4.234   9.607  1.00 55.92           O  
ANISOU  550  O   THR A  68     7486   7464   6298  -2796  -1024   1244       O  
ATOM    551  CB  THR A  68     -56.974   1.349  10.147  1.00 65.42           C  
ANISOU  551  CB  THR A  68     9028   8439   7390  -3097  -1131   1341       C  
ATOM    552  CG2 THR A  68     -58.403   0.831  10.094  1.00 62.40           C  
ANISOU  552  CG2 THR A  68     8602   8231   6877  -3279  -1043   1340       C  
ATOM    553  OG1 THR A  68     -56.074   0.254  10.363  1.00 74.32           O  
ANISOU  553  OG1 THR A  68    10345   9352   8543  -3135  -1245   1384       O  
ATOM    554  N   ILE A  69     -58.196   3.503   7.699  1.00 59.40           N  
ANISOU  554  N   ILE A  69     7805   7999   6767  -2877   -984   1230       N  
ATOM    555  CA  ILE A  69     -58.979   4.720   7.496  1.00 62.29           C  
ANISOU  555  CA  ILE A  69     7993   8536   7138  -2795   -924   1182       C  
ATOM    556  C   ILE A  69     -60.481   4.436   7.542  1.00 63.14           C  
ANISOU  556  C   ILE A  69     7996   8842   7150  -2930   -846   1166       C  
ATOM    557  O   ILE A  69     -60.955   3.456   6.972  1.00 71.98           O  
ANISOU  557  O   ILE A  69     9134   9977   8236  -3063   -844   1189       O  
ATOM    558  CB  ILE A  69     -58.613   5.417   6.163  1.00 58.83           C  
ANISOU  558  CB  ILE A  69     7467   8075   6812  -2668   -951   1157       C  
ATOM    559  CG1 ILE A  69     -59.083   6.872   6.167  1.00 56.51           C  
ANISOU  559  CG1 ILE A  69     7030   7903   6539  -2540   -927   1111       C  
ATOM    560  CG2 ILE A  69     -59.196   4.663   4.974  1.00 60.54           C  
ANISOU  560  CG2 ILE A  69     7653   8323   7027  -2765   -946   1164       C  
ATOM    561  CD1 ILE A  69     -58.716   7.629   4.914  1.00 52.98           C  
ANISOU  561  CD1 ILE A  69     6524   7422   6183  -2429   -968   1091       C  
ATOM    562  N   SER A  70     -61.222   5.293   8.237  1.00 54.77           N  
ANISOU  562  N   SER A  70     6826   7934   6049  -2897   -779   1122       N  
ATOM    563  CA  SER A  70     -62.670   5.148   8.350  1.00 56.46           C  
ANISOU  563  CA  SER A  70     6905   8361   6188  -3013   -693   1090       C  
ATOM    564  C   SER A  70     -63.335   6.516   8.426  1.00 63.86           C  
ANISOU  564  C   SER A  70     7651   9450   7163  -2873   -645   1015       C  
ATOM    565  O   SER A  70     -62.671   7.524   8.660  1.00 58.36           O  
ANISOU  565  O   SER A  70     6965   8689   6519  -2709   -672    995       O  
ATOM    566  CB  SER A  70     -63.038   4.325   9.586  1.00 50.90           C  
ANISOU  566  CB  SER A  70     6305   7692   5341  -3199   -634   1107       C  
ATOM    567  OG  SER A  70     -62.801   5.058  10.776  1.00 52.56           O  
ANISOU  567  OG  SER A  70     6551   7909   5511  -3138   -597   1079       O  
ATOM    568  N   LYS A  71     -64.649   6.550   8.236  1.00 69.24           N  
ANISOU  568  N   LYS A  71     8155  10331   7821  -2937   -580    971       N  
ATOM    569  CA  LYS A  71     -65.377   7.813   8.241  1.00 65.78           C  
ANISOU  569  CA  LYS A  71     7518  10041   7436  -2792   -545    888       C  
ATOM    570  C   LYS A  71     -66.638   7.749   9.093  1.00 60.14           C  
ANISOU  570  C   LYS A  71     6664   9545   6639  -2897   -418    822       C  
ATOM    571  O   LYS A  71     -67.121   6.671   9.429  1.00 65.57           O  
ANISOU  571  O   LYS A  71     7389  10296   7229  -3108   -361    846       O  
ATOM    572  CB  LYS A  71     -65.751   8.217   6.815  1.00 62.20           C  
ANISOU  572  CB  LYS A  71     6930   9618   7087  -2710   -619    879       C  
ATOM    573  CG  LYS A  71     -66.838   7.356   6.206  1.00 65.84           C  
ANISOU  573  CG  LYS A  71     7283  10211   7523  -2875   -602    888       C  
ATOM    574  CD  LYS A  71     -67.105   7.745   4.769  1.00 66.26           C  
ANISOU  574  CD  LYS A  71     7237  10264   7674  -2801   -698    890       C  
ATOM    575  CE  LYS A  71     -68.182   6.873   4.156  1.00 70.21           C  
ANISOU  575  CE  LYS A  71     7635  10893   8148  -2975   -693    904       C  
ATOM    576  NZ  LYS A  71     -68.504   7.329   2.781  1.00 76.66           N1+
ANISOU  576  NZ  LYS A  71     8360  11710   9057  -2905   -801    906       N1+
ATOM    577  N   ASP A  72     -67.156   8.922   9.437  1.00 56.93           N  
ANISOU  577  N   ASP A  72     6103   9254   6273  -2751   -372    732       N  
ATOM    578  CA  ASP A  72     -68.427   9.045  10.134  1.00 68.23           C  
ANISOU  578  CA  ASP A  72     7352  10917   7654  -2818   -239    641       C  
ATOM    579  C   ASP A  72     -69.117  10.322   9.662  1.00 64.11           C  
ANISOU  579  C   ASP A  72     6595  10508   7254  -2609   -256    546       C  
ATOM    580  O   ASP A  72     -68.924  11.395  10.236  1.00 49.27           O  
ANISOU  580  O   ASP A  72     4704   8619   5399  -2442   -236    482       O  
ATOM    581  CB  ASP A  72     -68.217   9.069  11.648  1.00 77.56           C  
ANISOU  581  CB  ASP A  72     8652  12104   8714  -2879   -129    613       C  
ATOM    582  CG  ASP A  72     -69.507   8.855  12.423  1.00 85.80           C  
ANISOU  582  CG  ASP A  72     9538  13391   9670  -3023     37    523       C  
ATOM    583  OD1 ASP A  72     -70.597   9.091  11.858  1.00 84.54           O  
ANISOU  583  OD1 ASP A  72     9123  13414   9583  -2999     67    455       O  
ATOM    584  OD2 ASP A  72     -69.429   8.454  13.603  1.00 86.46           O1-
ANISOU  584  OD2 ASP A  72     9754  13484   9613  -3167    136    518       O1-
ATOM    585  N   THR A  73     -69.909  10.195   8.602  1.00 65.82           N  
ANISOU  585  N   THR A  73     6640  10821   7549  -2620   -308    540       N  
ATOM    586  CA  THR A  73     -70.580  11.333   7.985  1.00 69.37           C  
ANISOU  586  CA  THR A  73     6871  11358   8129  -2422   -364    459       C  
ATOM    587  C   THR A  73     -71.477  12.086   8.968  1.00 77.02           C  
ANISOU  587  C   THR A  73     7651  12514   9101  -2345   -236    322       C  
ATOM    588  O   THR A  73     -71.747  13.271   8.786  1.00 79.18           O  
ANISOU  588  O   THR A  73     7795  12811   9478  -2128   -283    242       O  
ATOM    589  CB  THR A  73     -71.419  10.889   6.768  1.00 79.97           C  
ANISOU  589  CB  THR A  73     8056  12789   9540  -2491   -441    478       C  
ATOM    590  CG2 THR A  73     -71.998  12.094   6.047  1.00 85.35           C  
ANISOU  590  CG2 THR A  73     8541  13522  10367  -2274   -542    407       C  
ATOM    591  OG1 THR A  73     -70.594  10.146   5.862  1.00 81.43           O  
ANISOU  591  OG1 THR A  73     8430  12799   9711  -2573   -544    596       O  
ATOM    592  N   SER A  74     -71.939  11.395  10.006  1.00 81.64           N  
ANISOU  592  N   SER A  74     8227  13227   9567  -2529    -75    291       N  
ATOM    593  CA  SER A  74     -72.774  12.017  11.030  1.00 82.54           C  
ANISOU  593  CA  SER A  74     8170  13527   9664  -2484     80    148       C  
ATOM    594  C   SER A  74     -72.055  13.188  11.686  1.00 80.82           C  
ANISOU  594  C   SER A  74     8058  13194   9457  -2271     77    101       C  
ATOM    595  O   SER A  74     -72.633  14.258  11.872  1.00 74.45           O  
ANISOU  595  O   SER A  74     7076  12481   8730  -2085    106    -22       O  
ATOM    596  CB  SER A  74     -73.161  10.998  12.104  1.00 87.97           C  
ANISOU  596  CB  SER A  74     8905  14335  10184  -2756    257    139       C  
ATOM    597  OG  SER A  74     -73.841   9.890  11.542  1.00100.10           O  
ANISOU  597  OG  SER A  74    10358  15980  11697  -2973    260    184       O  
ATOM    598  N   LYS A  75     -70.790  12.970  12.034  1.00 78.71           N  
ANISOU  598  N   LYS A  75     8076  12718   9111  -2298     34    198       N  
ATOM    599  CA  LYS A  75     -69.998  13.966  12.745  1.00 74.98           C  
ANISOU  599  CA  LYS A  75     7741  12122   8625  -2133     28    171       C  
ATOM    600  C   LYS A  75     -69.063  14.726  11.810  1.00 68.58           C  
ANISOU  600  C   LYS A  75     7019  11115   7924  -1935   -157    232       C  
ATOM    601  O   LYS A  75     -68.223  15.503  12.265  1.00 65.33           O  
ANISOU  601  O   LYS A  75     6753  10567   7501  -1808   -192    235       O  
ATOM    602  CB  LYS A  75     -69.178  13.298  13.850  1.00 79.12           C  
ANISOU  602  CB  LYS A  75     8529  12542   8991  -2296     94    235       C  
ATOM    603  CG  LYS A  75     -69.962  12.332  14.717  1.00 85.26           C  
ANISOU  603  CG  LYS A  75     9281  13484   9629  -2551    263    203       C  
ATOM    604  CD  LYS A  75     -69.029  11.446  15.526  1.00 92.97           C  
ANISOU  604  CD  LYS A  75    10561  14310  10455  -2738    266    305       C  
ATOM    605  CE  LYS A  75     -69.759  10.222  16.051  1.00106.56           C  
ANISOU  605  CE  LYS A  75    12286  16167  12034  -3035    390    309       C  
ATOM    606  NZ  LYS A  75     -68.811   9.202  16.582  1.00105.65           N1+
ANISOU  606  NZ  LYS A  75    12483  15870  11789  -3221    338    433       N1+
ATOM    607  N   ASN A  76     -69.208  14.496  10.507  1.00 67.01           N  
ANISOU  607  N   ASN A  76     6742  10899   7818  -1924   -276    282       N  
ATOM    608  CA  ASN A  76     -68.338  15.120   9.513  1.00 58.70           C  
ANISOU  608  CA  ASN A  76     5784   9664   6854  -1774   -448    344       C  
ATOM    609  C   ASN A  76     -66.858  14.901   9.793  1.00 60.33           C  
ANISOU  609  C   ASN A  76     6263   9656   7003  -1801   -493    442       C  
ATOM    610  O   ASN A  76     -66.067  15.845   9.735  1.00 60.72           O  
ANISOU  610  O   ASN A  76     6410   9573   7089  -1645   -574    448       O  
ATOM    611  CB  ASN A  76     -68.612  16.623   9.414  1.00 62.05           C  
ANISOU  611  CB  ASN A  76     6107  10097   7372  -1521   -506    250       C  
ATOM    612  CG  ASN A  76     -69.511  16.977   8.249  1.00 68.91           C  
ANISOU  612  CG  ASN A  76     6769  11048   8366  -1435   -609    214       C  
ATOM    613  ND2 ASN A  76     -69.854  18.257   8.134  1.00 64.04           N  
ANISOU  613  ND2 ASN A  76     6057  10437   7838  -1212   -676    127       N  
ATOM    614  OD1 ASN A  76     -69.890  16.115   7.457  1.00 77.94           O  
ANISOU  614  OD1 ASN A  76     7850  12238   9525  -1568   -639    266       O  
ATOM    615  N   GLN A  77     -66.473  13.666  10.097  1.00 55.57           N  
ANISOU  615  N   GLN A  77     5786   9014   6313  -2000   -450    518       N  
ATOM    616  CA  GLN A  77     -65.065  13.406  10.375  1.00 58.19           C  
ANISOU  616  CA  GLN A  77     6361   9140   6609  -2021   -504    607       C  
ATOM    617  C   GLN A  77     -64.533  12.078   9.849  1.00 52.93           C  
ANISOU  617  C   GLN A  77     5810   8380   5922  -2187   -545    708       C  
ATOM    618  O   GLN A  77     -65.277  11.117   9.663  1.00 48.21           O  
ANISOU  618  O   GLN A  77     5147   7883   5286  -2345   -497    717       O  
ATOM    619  CB  GLN A  77     -64.750  13.573  11.864  1.00 55.03           C  
ANISOU  619  CB  GLN A  77     6081   8722   6105  -2044   -418    583       C  
ATOM    620  CG  GLN A  77     -65.527  12.672  12.791  1.00 65.41           C  
ANISOU  620  CG  GLN A  77     7381  10174   7298  -2245   -277    558       C  
ATOM    621  CD  GLN A  77     -65.279  13.009  14.252  1.00 78.26           C  
ANISOU  621  CD  GLN A  77     9135  11786   8815  -2262   -191    523       C  
ATOM    622  NE2 GLN A  77     -65.236  11.986  15.099  1.00 84.05           N  
ANISOU  622  NE2 GLN A  77    10002  12516   9416  -2475   -125    562       N  
ATOM    623  OE1 GLN A  77     -65.124  14.178  14.613  1.00 72.71           O  
ANISOU  623  OE1 GLN A  77     8425  11064   8136  -2092   -192    463       O  
ATOM    624  N   VAL A  78     -63.228  12.065   9.601  1.00 50.66           N  
ANISOU  624  N   VAL A  78     5689   7895   5663  -2145   -636    777       N  
ATOM    625  CA  VAL A  78     -62.513  10.894   9.124  1.00 47.47           C  
ANISOU  625  CA  VAL A  78     5413   7368   5256  -2268   -684    863       C  
ATOM    626  C   VAL A  78     -61.369  10.615  10.081  1.00 47.51           C  
ANISOU  626  C   VAL A  78     5620   7219   5215  -2293   -702    911       C  
ATOM    627  O   VAL A  78     -60.741  11.541  10.595  1.00 48.19           O  
ANISOU  627  O   VAL A  78     5759   7237   5314  -2171   -728    898       O  
ATOM    628  CB  VAL A  78     -61.924  11.134   7.722  1.00 48.25           C  
ANISOU  628  CB  VAL A  78     5511   7365   5458  -2185   -788    893       C  
ATOM    629  CG1 VAL A  78     -61.030   9.972   7.308  1.00 44.80           C  
ANISOU  629  CG1 VAL A  78     5217   6781   5025  -2291   -830    968       C  
ATOM    630  CG2 VAL A  78     -63.035  11.362   6.707  1.00 49.06           C  
ANISOU  630  CG2 VAL A  78     5434   7601   5605  -2172   -798    857       C  
ATOM    631  N   VAL A  79     -61.095   9.339  10.320  1.00 52.04           N  
ANISOU  631  N   VAL A  79     6312   7726   5733  -2454   -703    970       N  
ATOM    632  CA  VAL A  79     -60.038   8.957  11.246  1.00 52.35           C  
ANISOU  632  CA  VAL A  79     6549   7608   5734  -2489   -744   1020       C  
ATOM    633  C   VAL A  79     -59.008   8.058  10.578  1.00 53.09           C  
ANISOU  633  C   VAL A  79     6757   7525   5891  -2519   -838   1088       C  
ATOM    634  O   VAL A  79     -59.360   7.119   9.866  1.00 63.12           O  
ANISOU  634  O   VAL A  79     8013   8808   7161  -2621   -837   1108       O  
ATOM    635  CB  VAL A  79     -60.612   8.232  12.477  1.00 52.79           C  
ANISOU  635  CB  VAL A  79     6686   7727   5644  -2666   -666   1023       C  
ATOM    636  CG1 VAL A  79     -59.491   7.662  13.329  1.00 54.80           C  
ANISOU  636  CG1 VAL A  79     7170   7791   5860  -2721   -743   1090       C  
ATOM    637  CG2 VAL A  79     -61.485   9.179  13.286  1.00 46.64           C  
ANISOU  637  CG2 VAL A  79     5807   7112   4801  -2627   -558    941       C  
ATOM    638  N   LEU A  80     -57.733   8.355  10.809  1.00 50.47           N  
ANISOU  638  N   LEU A  80     6533   7027   5617  -2430   -919   1117       N  
ATOM    639  CA  LEU A  80     -56.643   7.529  10.303  1.00 43.24           C  
ANISOU  639  CA  LEU A  80     5720   5934   4776  -2442  -1007   1166       C  
ATOM    640  C   LEU A  80     -55.835   6.960  11.459  1.00 43.93           C  
ANISOU  640  C   LEU A  80     5988   5878   4825  -2497  -1070   1214       C  
ATOM    641  O   LEU A  80     -55.439   7.691  12.364  1.00 47.40           O  
ANISOU  641  O   LEU A  80     6480   6288   5243  -2440  -1089   1214       O  
ATOM    642  CB  LEU A  80     -55.732   8.348   9.391  1.00 40.95           C  
ANISOU  642  CB  LEU A  80     5380   5565   4613  -2287  -1061   1153       C  
ATOM    643  CG  LEU A  80     -54.515   7.608   8.830  1.00 36.91           C  
ANISOU  643  CG  LEU A  80     4949   4877   4200  -2280  -1138   1184       C  
ATOM    644  CD1 LEU A  80     -54.930   6.665   7.717  1.00 31.14           C  
ANISOU  644  CD1 LEU A  80     4188   4160   3484  -2361  -1116   1183       C  
ATOM    645  CD2 LEU A  80     -53.470   8.589   8.332  1.00 29.59           C  
ANISOU  645  CD2 LEU A  80     3990   3873   3380  -2137  -1184   1167       C  
ATOM    646  N   LYS A  81     -55.600   5.653  11.432  1.00 53.14           N  
ANISOU  646  N   LYS A  81     7265   6946   5980  -2611  -1115   1257       N  
ATOM    647  CA  LYS A  81     -54.789   4.999  12.455  1.00 49.17           C  
ANISOU  647  CA  LYS A  81     6951   6279   5450  -2667  -1208   1308       C  
ATOM    648  C   LYS A  81     -53.489   4.485  11.851  1.00 57.99           C  
ANISOU  648  C   LYS A  81     8121   7202   6713  -2591  -1321   1330       C  
ATOM    649  O   LYS A  81     -53.489   3.869  10.784  1.00 65.28           O  
ANISOU  649  O   LYS A  81     9001   8105   7696  -2599  -1316   1319       O  
ATOM    650  CB  LYS A  81     -55.545   3.830  13.088  1.00 43.03           C  
ANISOU  650  CB  LYS A  81     6293   5524   4532  -2873  -1190   1340       C  
ATOM    651  CG  LYS A  81     -56.727   4.218  13.960  1.00 54.06           C  
ANISOU  651  CG  LYS A  81     7665   7104   5773  -2976  -1074   1314       C  
ATOM    652  CD  LYS A  81     -57.583   2.994  14.271  1.00 72.07           C  
ANISOU  652  CD  LYS A  81    10035   9431   7915  -3204  -1039   1340       C  
ATOM    653  CE  LYS A  81     -58.712   3.311  15.243  1.00 89.47           C  
ANISOU  653  CE  LYS A  81    12219  11820   9955  -3330   -910   1304       C  
ATOM    654  NZ  LYS A  81     -58.218   3.513  16.639  1.00 94.89           N1+
ANISOU  654  NZ  LYS A  81    13089  12416  10549  -3371   -947   1328       N1+
ATOM    655  N   VAL A  82     -52.382   4.743  12.537  1.00 54.24           N  
ANISOU  655  N   VAL A  82     7733   6583   6294  -2520  -1421   1354       N  
ATOM    656  CA  VAL A  82     -51.088   4.219  12.124  1.00 43.99           C  
ANISOU  656  CA  VAL A  82     6475   5095   5144  -2447  -1535   1366       C  
ATOM    657  C   VAL A  82     -50.508   3.376  13.248  1.00 54.22           C  
ANISOU  657  C   VAL A  82     7968   6220   6411  -2518  -1667   1423       C  
ATOM    658  O   VAL A  82     -50.252   3.877  14.342  1.00 62.77           O  
ANISOU  658  O   VAL A  82     9135   7271   7443  -2519  -1716   1451       O  
ATOM    659  CB  VAL A  82     -50.107   5.346  11.774  1.00 41.13           C  
ANISOU  659  CB  VAL A  82     6015   4700   4911  -2281  -1561   1339       C  
ATOM    660  CG1 VAL A  82     -48.853   4.776  11.124  1.00 41.26           C  
ANISOU  660  CG1 VAL A  82     6027   4551   5098  -2206  -1648   1329       C  
ATOM    661  CG2 VAL A  82     -50.767   6.351  10.847  1.00 37.05           C  
ANISOU  661  CG2 VAL A  82     5335   4350   4393  -2221  -1446   1290       C  
ATOM    662  N   THR A  82A    -50.310   2.090  12.986  1.00 52.63           N  
ANISOU  662  N   THR A  82A    7858   5900   6238  -2581  -1734   1441       N  
ATOM    663  CA  THR A  82A    -49.807   1.192  14.019  1.00 53.63           C  
ANISOU  663  CA  THR A  82A    8196   5846   6334  -2657  -1883   1499       C  
ATOM    664  C   THR A  82A    -48.285   1.157  14.024  1.00 47.74           C  
ANISOU  664  C   THR A  82A    7462   4901   5778  -2515  -2036   1500       C  
ATOM    665  O   THR A  82A    -47.641   1.573  13.060  1.00 39.03           O  
ANISOU  665  O   THR A  82A    6204   3796   4829  -2378  -2010   1449       O  
ATOM    666  CB  THR A  82A    -50.360  -0.243  13.861  1.00 55.80           C  
ANISOU  666  CB  THR A  82A    8598   6070   6535  -2807  -1906   1522       C  
ATOM    667  CG2 THR A  82A    -51.883  -0.226  13.797  1.00 54.73           C  
ANISOU  667  CG2 THR A  82A    8424   6149   6221  -2958  -1750   1516       C  
ATOM    668  OG1 THR A  82A    -49.838  -0.839  12.665  1.00 55.44           O  
ANISOU  668  OG1 THR A  82A    8485   5942   6637  -2724  -1923   1484       O  
ATOM    669  N   ASN A  82B    -47.721   0.668  15.125  1.00 49.01           N  
ANISOU  669  N   ASN A  82B    7807   4893   5921  -2558  -2198   1557       N  
ATOM    670  CA  ASN A  82B    -46.278   0.497  15.255  1.00 48.01           C  
ANISOU  670  CA  ASN A  82B    7699   4561   5982  -2433  -2373   1562       C  
ATOM    671  C   ASN A  82B    -45.494   1.728  14.815  1.00 53.18           C  
ANISOU  671  C   ASN A  82B    8164   5263   6779  -2267  -2339   1518       C  
ATOM    672  O   ASN A  82B    -44.724   1.673  13.853  1.00 58.30           O  
ANISOU  672  O   ASN A  82B    8677   5867   7607  -2146  -2340   1464       O  
ATOM    673  CB  ASN A  82B    -45.817  -0.721  14.457  1.00 35.71           C  
ANISOU  673  CB  ASN A  82B    6154   2862   4554  -2398  -2442   1534       C  
ATOM    674  CG  ASN A  82B    -44.379  -1.094  14.749  1.00 57.30           C  
ANISOU  674  CG  ASN A  82B    8923   5364   7482  -2279  -2646   1536       C  
ATOM    675  ND2 ASN A  82B    -43.695  -1.643  13.752  1.00 70.06           N  
ANISOU  675  ND2 ASN A  82B   10440   6896   9284  -2167  -2661   1470       N  
ATOM    676  OD1 ASN A  82B    -43.887  -0.892  15.860  1.00 58.35           O  
ANISOU  676  OD1 ASN A  82B    9171   5395   7603  -2288  -2792   1592       O  
ATOM    677  N   MET A  82C    -45.687   2.837  15.518  1.00 49.59           N  
ANISOU  677  N   MET A  82C    7707   4898   6236  -2270  -2306   1539       N  
ATOM    678  CA  MET A  82C    -45.040   4.084  15.133  1.00 44.29           C  
ANISOU  678  CA  MET A  82C    6875   4281   5672  -2133  -2272   1503       C  
ATOM    679  C   MET A  82C    -43.529   4.048  15.352  1.00 47.26           C  
ANISOU  679  C   MET A  82C    7244   4475   6239  -2025  -2447   1511       C  
ATOM    680  O   MET A  82C    -43.030   3.412  16.287  1.00 36.85           O  
ANISOU  680  O   MET A  82C    6083   2989   4929  -2060  -2621   1565       O  
ATOM    681  CB  MET A  82C    -45.667   5.266  15.868  1.00 42.49           C  
ANISOU  681  CB  MET A  82C    6666   4184   5293  -2163  -2198   1520       C  
ATOM    682  CG  MET A  82C    -47.087   5.567  15.423  1.00 51.34           C  
ANISOU  682  CG  MET A  82C    7718   5516   6273  -2226  -2008   1487       C  
ATOM    683  SD  MET A  82C    -47.168   6.340  13.787  1.00 59.28           S  
ANISOU  683  SD  MET A  82C    8482   6657   7387  -2106  -1873   1410       S  
ATOM    684  CE  MET A  82C    -46.659   8.009  14.183  1.00 38.51           C  
ANISOU  684  CE  MET A  82C    5800   4063   4768  -2000  -1880   1404       C  
ATOM    685  N   ASP A  83     -42.810   4.737  14.473  1.00 40.89           N  
ANISOU  685  N   ASP A  83     6253   3702   5583  -1901  -2404   1455       N  
ATOM    686  CA  ASP A  83     -41.359   4.772  14.519  1.00 34.51           C  
ANISOU  686  CA  ASP A  83     5387   2749   4979  -1792  -2547   1444       C  
ATOM    687  C   ASP A  83     -40.924   6.230  14.491  1.00 38.77           C  
ANISOU  687  C   ASP A  83     5819   3373   5541  -1726  -2510   1433       C  
ATOM    688  O   ASP A  83     -41.640   7.072  13.960  1.00 40.90           O  
ANISOU  688  O   ASP A  83     6015   3806   5719  -1732  -2355   1407       O  
ATOM    689  CB  ASP A  83     -40.795   4.013  13.316  1.00 44.03           C  
ANISOU  689  CB  ASP A  83     6461   3902   6364  -1716  -2521   1367       C  
ATOM    690  CG  ASP A  83     -39.289   3.864  13.369  1.00 60.76           C  
ANISOU  690  CG  ASP A  83     8504   5867   8717  -1602  -2672   1341       C  
ATOM    691  OD1 ASP A  83     -38.816   2.752  13.694  1.00 69.47           O  
ANISOU  691  OD1 ASP A  83     9686   6795   9913  -1587  -2822   1349       O  
ATOM    692  OD2 ASP A  83     -38.578   4.857  13.092  1.00 61.88           O1-
ANISOU  692  OD2 ASP A  83     8505   6058   8951  -1530  -2649   1311       O1-
ATOM    693  N   PRO A  84     -39.762   6.542  15.086  1.00 54.90           N  
ANISOU  693  N   PRO A  84     7859   5297   7702  -1667  -2665   1456       N  
ATOM    694  CA  PRO A  84     -39.234   7.910  15.051  1.00 56.95           C  
ANISOU  694  CA  PRO A  84     8025   5623   7990  -1612  -2646   1449       C  
ATOM    695  C   PRO A  84     -39.250   8.503  13.645  1.00 48.95           C  
ANISOU  695  C   PRO A  84     6819   4744   7035  -1558  -2478   1367       C  
ATOM    696  O   PRO A  84     -39.398   9.711  13.496  1.00 45.13           O  
ANISOU  696  O   PRO A  84     6293   4367   6488  -1548  -2407   1363       O  
ATOM    697  CB  PRO A  84     -37.794   7.734  15.532  1.00 56.69           C  
ANISOU  697  CB  PRO A  84     7971   5423   8148  -1547  -2847   1464       C  
ATOM    698  CG  PRO A  84     -37.861   6.579  16.459  1.00 61.85           C  
ANISOU  698  CG  PRO A  84     8806   5918   8778  -1600  -3006   1523       C  
ATOM    699  CD  PRO A  84     -38.938   5.657  15.928  1.00 65.53           C  
ANISOU  699  CD  PRO A  84     9315   6435   9147  -1661  -2887   1500       C  
ATOM    700  N   ALA A  85     -39.102   7.656  12.633  1.00 46.50           N  
ANISOU  700  N   ALA A  85     6414   4419   6836  -1532  -2422   1303       N  
ATOM    701  CA  ALA A  85     -39.131   8.102  11.250  1.00 45.14           C  
ANISOU  701  CA  ALA A  85     6082   4362   6707  -1503  -2262   1224       C  
ATOM    702  C   ALA A  85     -40.546   8.483  10.819  1.00 52.24           C  
ANISOU  702  C   ALA A  85     7011   5420   7419  -1565  -2108   1226       C  
ATOM    703  O   ALA A  85     -40.742   9.108   9.776  1.00 65.82           O  
ANISOU  703  O   ALA A  85     8629   7247   9131  -1555  -1984   1176       O  
ATOM    704  CB  ALA A  85     -38.560   7.032  10.334  1.00 42.21           C  
ANISOU  704  CB  ALA A  85     5616   3918   6502  -1462  -2244   1148       C  
ATOM    705  N   ASP A  86     -41.531   8.100  11.625  1.00 40.37           N  
ANISOU  705  N   ASP A  86     5646   3929   5765  -1635  -2121   1282       N  
ATOM    706  CA  ASP A  86     -42.922   8.462  11.363  1.00 45.95           C  
ANISOU  706  CA  ASP A  86     6368   4792   6299  -1693  -1986   1282       C  
ATOM    707  C   ASP A  86     -43.221   9.865  11.878  1.00 45.35           C  
ANISOU  707  C   ASP A  86     6306   4805   6119  -1678  -1965   1303       C  
ATOM    708  O   ASP A  86     -44.294  10.415  11.622  1.00 46.90           O  
ANISOU  708  O   ASP A  86     6488   5137   6194  -1699  -1858   1291       O  
ATOM    709  CB  ASP A  86     -43.878   7.454  12.002  1.00 43.96           C  
ANISOU  709  CB  ASP A  86     6247   4529   5924  -1790  -1993   1322       C  
ATOM    710  CG  ASP A  86     -43.891   6.125  11.274  1.00 58.40           C  
ANISOU  710  CG  ASP A  86     8069   6297   7822  -1816  -1983   1294       C  
ATOM    711  OD1 ASP A  86     -44.144   6.119  10.047  1.00 49.55           O  
ANISOU  711  OD1 ASP A  86     6843   5252   6731  -1804  -1871   1239       O  
ATOM    712  OD2 ASP A  86     -43.652   5.086  11.928  1.00 68.55           O1-
ANISOU  712  OD2 ASP A  86     9472   7449   9124  -1852  -2096   1328       O1-
ATOM    713  N   THR A  87     -42.266  10.432  12.611  1.00 36.14           N  
ANISOU  713  N   THR A  87     5169   3555   5006  -1638  -2077   1333       N  
ATOM    714  CA  THR A  87     -42.368  11.803  13.094  1.00 36.82           C  
ANISOU  714  CA  THR A  87     5281   3702   5005  -1616  -2074   1350       C  
ATOM    715  C   THR A  87     -42.587  12.749  11.920  1.00 42.04           C  
ANISOU  715  C   THR A  87     5823   4482   5668  -1576  -1961   1296       C  
ATOM    716  O   THR A  87     -41.786  12.776  10.988  1.00 55.27           O  
ANISOU  716  O   THR A  87     7391   6139   7472  -1544  -1951   1255       O  
ATOM    717  CB  THR A  87     -41.083  12.222  13.837  1.00 41.29           C  
ANISOU  717  CB  THR A  87     5877   4147   5662  -1581  -2224   1386       C  
ATOM    718  CG2 THR A  87     -41.052  13.721  14.048  1.00 38.74           C  
ANISOU  718  CG2 THR A  87     5567   3886   5267  -1552  -2214   1392       C  
ATOM    719  OG1 THR A  87     -41.024  11.562  15.107  1.00 44.63           O  
ANISOU  719  OG1 THR A  87     6455   4461   6043  -1630  -2346   1449       O  
ATOM    720  N   ALA A  88     -43.668  13.523  11.965  1.00 34.68           N  
ANISOU  720  N   ALA A  88     4913   3668   4594  -1580  -1880   1291       N  
ATOM    721  CA  ALA A  88     -44.023  14.390  10.845  1.00 38.76           C  
ANISOU  721  CA  ALA A  88     5339   4289   5098  -1547  -1791   1244       C  
ATOM    722  C   ALA A  88     -45.250  15.258  11.120  1.00 44.21           C  
ANISOU  722  C   ALA A  88     6064   5095   5637  -1535  -1729   1238       C  
ATOM    723  O   ALA A  88     -45.883  15.149  12.170  1.00 53.64           O  
ANISOU  723  O   ALA A  88     7344   6305   6731  -1560  -1731   1262       O  
ATOM    724  CB  ALA A  88     -44.250  13.557   9.591  1.00 34.48           C  
ANISOU  724  CB  ALA A  88     4706   3779   4617  -1573  -1711   1201       C  
ATOM    725  N   THR A  89     -45.571  16.120  10.160  1.00 34.32           N  
ANISOU  725  N   THR A  89     4749   3920   4372  -1500  -1677   1201       N  
ATOM    726  CA  THR A  89     -46.783  16.925  10.208  1.00 35.70           C  
ANISOU  726  CA  THR A  89     4929   4205   4428  -1469  -1622   1179       C  
ATOM    727  C   THR A  89     -47.832  16.272   9.319  1.00 43.79           C  
ANISOU  727  C   THR A  89     5874   5325   5437  -1503  -1534   1148       C  
ATOM    728  O   THR A  89     -47.572  15.993   8.149  1.00 45.55           O  
ANISOU  728  O   THR A  89     6033   5545   5728  -1521  -1512   1128       O  
ATOM    729  CB  THR A  89     -46.519  18.365   9.731  1.00 37.74           C  
ANISOU  729  CB  THR A  89     5190   4474   4676  -1406  -1650   1161       C  
ATOM    730  CG2 THR A  89     -47.825  19.097   9.470  1.00 36.43           C  
ANISOU  730  CG2 THR A  89     5004   4419   4417  -1360  -1599   1124       C  
ATOM    731  OG1 THR A  89     -45.781  19.075  10.734  1.00 43.48           O  
ANISOU  731  OG1 THR A  89     6009   5127   5386  -1379  -1731   1193       O  
ATOM    732  N   TYR A  90     -49.014  16.019   9.873  1.00 45.11           N  
ANISOU  732  N   TYR A  90     6047   5580   5512  -1523  -1481   1142       N  
ATOM    733  CA  TYR A  90     -50.049  15.287   9.145  1.00 40.82           C  
ANISOU  733  CA  TYR A  90     5428   5131   4952  -1573  -1405   1119       C  
ATOM    734  C   TYR A  90     -51.194  16.186   8.696  1.00 47.51           C  
ANISOU  734  C   TYR A  90     6208   6102   5741  -1520  -1363   1076       C  
ATOM    735  O   TYR A  90     -51.726  16.975   9.475  1.00 57.80           O  
ANISOU  735  O   TYR A  90     7532   7454   6975  -1467  -1356   1059       O  
ATOM    736  CB  TYR A  90     -50.576  14.129   9.987  1.00 37.66           C  
ANISOU  736  CB  TYR A  90     5067   4745   4498  -1660  -1373   1141       C  
ATOM    737  CG  TYR A  90     -49.565  13.021  10.171  1.00 38.69           C  
ANISOU  737  CG  TYR A  90     5256   4743   4701  -1714  -1429   1179       C  
ATOM    738  CD1 TYR A  90     -48.518  13.151  11.076  1.00 36.53           C  
ANISOU  738  CD1 TYR A  90     5070   4351   4457  -1695  -1517   1214       C  
ATOM    739  CD2 TYR A  90     -49.650  11.850   9.434  1.00 36.91           C  
ANISOU  739  CD2 TYR A  90     5001   4503   4520  -1780  -1405   1178       C  
ATOM    740  CE1 TYR A  90     -47.589  12.144  11.239  1.00 37.26           C  
ANISOU  740  CE1 TYR A  90     5208   4314   4635  -1729  -1588   1244       C  
ATOM    741  CE2 TYR A  90     -48.730  10.836   9.594  1.00 27.02           C  
ANISOU  741  CE2 TYR A  90     3804   3119   3346  -1812  -1466   1203       C  
ATOM    742  CZ  TYR A  90     -47.702  10.987  10.493  1.00 35.53           C  
ANISOU  742  CZ  TYR A  90     4956   4080   4466  -1781  -1561   1234       C  
ATOM    743  OH  TYR A  90     -46.784   9.972  10.649  1.00 39.65           O  
ANISOU  743  OH  TYR A  90     5522   4461   5081  -1799  -1640   1254       O  
ATOM    744  N   TYR A  91     -51.561  16.061   7.427  1.00 36.13           N  
ANISOU  744  N   TYR A  91     4691   4703   4332  -1534  -1341   1056       N  
ATOM    745  CA  TYR A  91     -52.595  16.900   6.841  1.00 29.17           C  
ANISOU  745  CA  TYR A  91     3744   3924   3416  -1480  -1330   1016       C  
ATOM    746  C   TYR A  91     -53.773  16.060   6.366  1.00 40.98           C  
ANISOU  746  C   TYR A  91     5152   5526   4891  -1547  -1270   1002       C  
ATOM    747  O   TYR A  91     -53.607  14.913   5.944  1.00 43.91           O  
ANISOU  747  O   TYR A  91     5522   5874   5289  -1639  -1245   1022       O  
ATOM    748  CB  TYR A  91     -52.052  17.666   5.629  1.00 29.31           C  
ANISOU  748  CB  TYR A  91     3764   3895   3478  -1449  -1381   1007       C  
ATOM    749  CG  TYR A  91     -50.870  18.574   5.879  1.00 35.12           C  
ANISOU  749  CG  TYR A  91     4578   4532   4234  -1399  -1445   1020       C  
ATOM    750  CD1 TYR A  91     -49.571  18.119   5.696  1.00 44.07           C  
ANISOU  750  CD1 TYR A  91     5741   5566   5438  -1446  -1460   1042       C  
ATOM    751  CD2 TYR A  91     -51.050  19.898   6.257  1.00 34.49           C  
ANISOU  751  CD2 TYR A  91     4539   4458   4109  -1307  -1495   1005       C  
ATOM    752  CE1 TYR A  91     -48.483  18.953   5.903  1.00 45.18           C  
ANISOU  752  CE1 TYR A  91     5941   5626   5601  -1414  -1520   1054       C  
ATOM    753  CE2 TYR A  91     -49.967  20.738   6.465  1.00 35.58           C  
ANISOU  753  CE2 TYR A  91     4759   4504   4255  -1277  -1560   1022       C  
ATOM    754  CZ  TYR A  91     -48.689  20.257   6.286  1.00 36.94           C  
ANISOU  754  CZ  TYR A  91     4950   4589   4497  -1338  -1572   1048       C  
ATOM    755  OH  TYR A  91     -47.607  21.075   6.495  1.00 33.57           O  
ANISOU  755  OH  TYR A  91     4591   4081   4083  -1321  -1637   1065       O  
ATOM    756  N   CYS A  92     -54.965  16.641   6.424  1.00 42.56           N  
ANISOU  756  N   CYS A  92     5278   5844   5048  -1498  -1251    962       N  
ATOM    757  CA  CYS A  92     -56.104  16.067   5.729  1.00 33.84           C  
ANISOU  757  CA  CYS A  92     4071   4849   3939  -1554  -1213    945       C  
ATOM    758  C   CYS A  92     -56.494  17.026   4.616  1.00 34.82           C  
ANISOU  758  C   CYS A  92     4147   4994   4088  -1483  -1275    918       C  
ATOM    759  O   CYS A  92     -56.134  18.205   4.655  1.00 43.63           O  
ANISOU  759  O   CYS A  92     5305   6065   5208  -1381  -1335    903       O  
ATOM    760  CB  CYS A  92     -57.272  15.774   6.683  1.00 30.31           C  
ANISOU  760  CB  CYS A  92     3553   4536   3429  -1577  -1138    916       C  
ATOM    761  SG  CYS A  92     -58.086  17.205   7.428  1.00 91.47           S  
ANISOU  761  SG  CYS A  92    11240  12372  11141  -1430  -1134    844       S  
ATOM    762  N   ALA A  93     -57.200  16.522   3.610  1.00 37.62           N  
ANISOU  762  N   ALA A  93     4432   5406   4456  -1544  -1274    915       N  
ATOM    763  CA  ALA A  93     -57.535  17.349   2.460  1.00 35.96           C  
ANISOU  763  CA  ALA A  93     4199   5197   4267  -1496  -1355    898       C  
ATOM    764  C   ALA A  93     -58.703  16.773   1.687  1.00 41.50           C  
ANISOU  764  C   ALA A  93     4797   6000   4971  -1562  -1352    890       C  
ATOM    765  O   ALA A  93     -58.846  15.557   1.579  1.00 52.78           O  
ANISOU  765  O   ALA A  93     6212   7452   6390  -1681  -1293    913       O  
ATOM    766  CB  ALA A  93     -56.321  17.515   1.549  1.00 34.44           C  
ANISOU  766  CB  ALA A  93     4115   4872   4099  -1528  -1399    925       C  
ATOM    767  N   ARG A  94     -59.533  17.659   1.148  1.00 34.03           N  
ANISOU  767  N   ARG A  94     3785   5105   4038  -1483  -1430    858       N  
ATOM    768  CA  ARG A  94     -60.691  17.252   0.362  1.00 30.08           C  
ANISOU  768  CA  ARG A  94     3177   4702   3551  -1537  -1454    849       C  
ATOM    769  C   ARG A  94     -60.266  16.855  -1.044  1.00 46.47           C  
ANISOU  769  C   ARG A  94     5336   6693   5629  -1642  -1504    889       C  
ATOM    770  O   ARG A  94     -59.230  17.298  -1.541  1.00 58.29           O  
ANISOU  770  O   ARG A  94     6958   8068   7123  -1639  -1541    906       O  
ATOM    771  CB  ARG A  94     -61.719  18.385   0.317  1.00 37.47           C  
ANISOU  771  CB  ARG A  94     4008   5712   4516  -1400  -1540    795       C  
ATOM    772  CG  ARG A  94     -63.083  18.002  -0.239  1.00 45.49           C  
ANISOU  772  CG  ARG A  94     4869   6857   5559  -1439  -1567    776       C  
ATOM    773  CD  ARG A  94     -63.199  18.314  -1.726  1.00 51.96           C  
ANISOU  773  CD  ARG A  94     5736   7611   6396  -1466  -1706    801       C  
ATOM    774  NE  ARG A  94     -63.202  19.749  -2.002  1.00 50.52           N  
ANISOU  774  NE  ARG A  94     5592   7365   6239  -1317  -1842    773       N  
ATOM    775  CZ  ARG A  94     -64.269  20.533  -1.877  1.00 53.06           C  
ANISOU  775  CZ  ARG A  94     5782   7766   6613  -1183  -1925    714       C  
ATOM    776  NH1 ARG A  94     -65.424  20.025  -1.476  1.00 52.12           N1+
ANISOU  776  NH1 ARG A  94     5464   7809   6530  -1187  -1871    674       N1+
ATOM    777  NH2 ARG A  94     -64.183  21.825  -2.158  1.00 57.10           N  
ANISOU  777  NH2 ARG A  94     6360   8193   7143  -1048  -2066    692       N  
ATOM    778  N   ASP A  95     -61.074  16.012  -1.676  1.00 51.09           N  
ANISOU  778  N   ASP A  95     5855   7347   6211  -1747  -1499    901       N  
ATOM    779  CA  ASP A  95     -60.799  15.536  -3.023  1.00 48.10           C  
ANISOU  779  CA  ASP A  95     5561   6894   5820  -1864  -1537    934       C  
ATOM    780  C   ASP A  95     -62.126  15.271  -3.717  1.00 50.31           C  
ANISOU  780  C   ASP A  95     5735   7276   6106  -1918  -1597    934       C  
ATOM    781  O   ASP A  95     -63.132  15.014  -3.062  1.00 62.91           O  
ANISOU  781  O   ASP A  95     7183   9008   7714  -1905  -1565    912       O  
ATOM    782  CB  ASP A  95     -59.965  14.252  -2.964  1.00 49.12           C  
ANISOU  782  CB  ASP A  95     5771   6962   5932  -1988  -1434    964       C  
ATOM    783  CG  ASP A  95     -59.399  13.850  -4.317  1.00 52.55           C  
ANISOU  783  CG  ASP A  95     6322   7295   6351  -2100  -1452    984       C  
ATOM    784  OD1 ASP A  95     -59.509  14.642  -5.277  1.00 51.04           O  
ANISOU  784  OD1 ASP A  95     6173   7067   6152  -2091  -1547    982       O  
ATOM    785  OD2 ASP A  95     -58.836  12.738  -4.421  1.00 45.95           O1-
ANISOU  785  OD2 ASP A  95     5545   6406   5507  -2200  -1374    998       O1-
ATOM    786  N   MET A  96     -62.134  15.348  -5.040  1.00 46.04           N  
ANISOU  786  N   MET A  96     5270   6671   5553  -1988  -1685    955       N  
ATOM    787  CA  MET A  96     -63.318  14.986  -5.807  1.00 48.50           C  
ANISOU  787  CA  MET A  96     5498   7061   5867  -2064  -1756    966       C  
ATOM    788  C   MET A  96     -62.930  14.122  -6.993  1.00 54.75           C  
ANISOU  788  C   MET A  96     6424   7768   6612  -2237  -1752   1007       C  
ATOM    789  O   MET A  96     -61.801  14.191  -7.478  1.00 61.09           O  
ANISOU  789  O   MET A  96     7383   8441   7388  -2272  -1730   1015       O  
ATOM    790  CB  MET A  96     -64.063  16.225  -6.301  1.00 46.29           C  
ANISOU  790  CB  MET A  96     5167   6796   5624  -1953  -1922    944       C  
ATOM    791  CG  MET A  96     -64.498  17.183  -5.211  1.00 46.11           C  
ANISOU  791  CG  MET A  96     5016   6850   5653  -1765  -1934    889       C  
ATOM    792  SD  MET A  96     -65.438  18.558  -5.904  1.00 67.78           S  
ANISOU  792  SD  MET A  96     7704   9594   8454  -1629  -2157    858       S  
ATOM    793  CE  MET A  96     -65.091  19.838  -4.707  1.00191.17           C  
ANISOU  793  CE  MET A  96    23317  25208  24112  -1406  -2150    797       C  
ATOM    794  N   ILE A  97     -63.872  13.310  -7.458  1.00 51.49           N  
ANISOU  794  N   ILE A  97     5947   7429   6187  -2350  -1770   1027       N  
ATOM    795  CA  ILE A  97     -63.633  12.446  -8.606  1.00 58.01           C  
ANISOU  795  CA  ILE A  97     6906   8176   6959  -2524  -1769   1063       C  
ATOM    796  C   ILE A  97     -63.687  13.234  -9.914  1.00 52.87           C  
ANISOU  796  C   ILE A  97     6360   7441   6287  -2549  -1917   1075       C  
ATOM    797  O   ILE A  97     -63.232  12.761 -10.955  1.00 57.46           O  
ANISOU  797  O   ILE A  97     7098   7923   6810  -2687  -1914   1096       O  
ATOM    798  CB  ILE A  97     -64.617  11.263  -8.612  1.00 61.85           C  
ANISOU  798  CB  ILE A  97     7303   8768   7428  -2654  -1742   1086       C  
ATOM    799  CG1 ILE A  97     -64.886  10.770 -10.028  1.00 66.22           C  
ANISOU  799  CG1 ILE A  97     7966   9263   7931  -2815  -1816   1122       C  
ATOM    800  CG2 ILE A  97     -65.913  11.667  -7.963  1.00 61.02           C  
ANISOU  800  CG2 ILE A  97     6976   8833   7376  -2574  -1793   1064       C  
ATOM    801  CD1 ILE A  97     -65.874   9.632 -10.079  1.00 69.58           C  
ANISOU  801  CD1 ILE A  97     8314   9790   8333  -2956  -1803   1150       C  
ATOM    802  N   PHE A  98     -64.233  14.445  -9.852  1.00 48.72           N  
ANISOU  802  N   PHE A  98     5763   6946   5805  -2416  -2048   1058       N  
ATOM    803  CA  PHE A  98     -64.193  15.353 -10.994  1.00 52.28           C  
ANISOU  803  CA  PHE A  98     6340   7294   6230  -2427  -2210   1071       C  
ATOM    804  C   PHE A  98     -62.758  15.812 -11.192  1.00 55.98           C  
ANISOU  804  C   PHE A  98     6995   7620   6653  -2429  -2157   1064       C  
ATOM    805  O   PHE A  98     -62.362  16.225 -12.280  1.00 60.52           O  
ANISOU  805  O   PHE A  98     7742   8082   7169  -2512  -2237   1079       O  
ATOM    806  CB  PHE A  98     -65.063  16.585 -10.749  1.00 47.87           C  
ANISOU  806  CB  PHE A  98     5662   6788   5738  -2258  -2373   1046       C  
ATOM    807  CG  PHE A  98     -66.491  16.270 -10.443  1.00 51.59           C  
ANISOU  807  CG  PHE A  98     5907   7419   6276  -2232  -2421   1035       C  
ATOM    808  CD1 PHE A  98     -67.340  15.808 -11.432  1.00 51.94           C  
ANISOU  808  CD1 PHE A  98     5942   7483   6310  -2358  -2533   1071       C  
ATOM    809  CD2 PHE A  98     -66.988  16.447  -9.164  1.00 49.58           C  
ANISOU  809  CD2 PHE A  98     5448   7298   6090  -2090  -2353    985       C  
ATOM    810  CE1 PHE A  98     -68.658  15.518 -11.146  1.00 55.13           C  
ANISOU  810  CE1 PHE A  98     6118   8046   6783  -2341  -2578   1057       C  
ATOM    811  CE2 PHE A  98     -68.302  16.160  -8.873  1.00 45.92           C  
ANISOU  811  CE2 PHE A  98     4759   6998   5691  -2075  -2381    963       C  
ATOM    812  CZ  PHE A  98     -69.140  15.695  -9.865  1.00 53.24           C  
ANISOU  812  CZ  PHE A  98     5659   7952   6618  -2199  -2496    999       C  
ATOM    813  N   ASN A  99     -61.985  15.740 -10.116  1.00 57.28           N  
ANISOU  813  N   ASN A  99     7127   7794   6843  -2348  -2024   1040       N  
ATOM    814  CA  ASN A  99     -60.621  16.238 -10.115  1.00 59.50           C  
ANISOU  814  CA  ASN A  99     7548   7960   7099  -2333  -1971   1028       C  
ATOM    815  C   ASN A  99     -59.799  15.580  -9.024  1.00 59.89           C  
ANISOU  815  C   ASN A  99     7556   8023   7177  -2301  -1804   1012       C  
ATOM    816  O   ASN A  99     -59.901  15.945  -7.852  1.00 82.52           O  
ANISOU  816  O   ASN A  99    10319  10949  10086  -2168  -1782    996       O  
ATOM    817  CB  ASN A  99     -60.615  17.758  -9.945  1.00 65.13           C  
ANISOU  817  CB  ASN A  99     8281   8641   7826  -2191  -2100   1014       C  
ATOM    818  CG  ASN A  99     -61.461  18.225  -8.770  1.00 53.59           C  
ANISOU  818  CG  ASN A  99     6633   7294   6435  -2014  -2128    988       C  
ATOM    819  ND2 ASN A  99     -60.888  19.054  -7.918  1.00 55.14           N  
ANISOU  819  ND2 ASN A  99     6836   7466   6648  -1882  -2114    964       N  
ATOM    820  OD1 ASN A  99     -62.618  17.854  -8.644  1.00 72.96           O  
ANISOU  820  OD1 ASN A  99     8941   9858   8925  -2003  -2159    985       O  
ATOM    821  N   PHE A 100     -58.993  14.599  -9.414  1.00 43.43           N  
ANISOU  821  N   PHE A 100     5559   5874   5067  -2423  -1692   1013       N  
ATOM    822  CA  PHE A 100     -58.220  13.806  -8.459  1.00 37.83           C  
ANISOU  822  CA  PHE A 100     4821   5161   4392  -2404  -1551   1001       C  
ATOM    823  C   PHE A 100     -57.011  14.567  -7.911  1.00 43.25           C  
ANISOU  823  C   PHE A 100     5551   5778   5103  -2314  -1519    980       C  
ATOM    824  O   PHE A 100     -55.866  14.166  -8.122  1.00 50.19           O  
ANISOU  824  O   PHE A 100     6507   6573   5988  -2366  -1433    962       O  
ATOM    825  CB  PHE A 100     -57.765  12.496  -9.106  1.00 40.17           C  
ANISOU  825  CB  PHE A 100     5197   5399   4665  -2552  -1454   1000       C  
ATOM    826  CG  PHE A 100     -58.865  11.486  -9.275  1.00 43.38           C  
ANISOU  826  CG  PHE A 100     5551   5881   5052  -2642  -1459   1026       C  
ATOM    827  CD1 PHE A 100     -59.941  11.746 -10.110  1.00 49.59           C  
ANISOU  827  CD1 PHE A 100     6328   6711   5803  -2699  -1572   1048       C  
ATOM    828  CD2 PHE A 100     -58.819  10.269  -8.608  1.00 37.05           C  
ANISOU  828  CD2 PHE A 100     4718   5098   4262  -2679  -1363   1030       C  
ATOM    829  CE1 PHE A 100     -60.960  10.813 -10.271  1.00 48.06           C  
ANISOU  829  CE1 PHE A 100     6079   6592   5590  -2795  -1581   1075       C  
ATOM    830  CE2 PHE A 100     -59.828   9.338  -8.762  1.00 40.46           C  
ANISOU  830  CE2 PHE A 100     5111   5598   4663  -2780  -1370   1057       C  
ATOM    831  CZ  PHE A 100     -60.901   9.610  -9.598  1.00 45.97           C  
ANISOU  831  CZ  PHE A 100     5785   6353   5329  -2841  -1474   1079       C  
ATOM    832  N   TYR A 100A    -57.278  15.676  -7.229  1.00 44.02           N  
ANISOU  832  N   TYR A 100A    5596   5911   5218  -2178  -1593    977       N  
ATOM    833  CA  TYR A 100A    -56.248  16.430  -6.525  1.00 49.08           C  
ANISOU  833  CA  TYR A 100A    6269   6499   5880  -2087  -1574    963       C  
ATOM    834  C   TYR A 100A    -56.849  17.042  -5.272  1.00 51.48           C  
ANISOU  834  C   TYR A 100A    6467   6882   6211  -1936  -1607    958       C  
ATOM    835  O   TYR A 100A    -58.070  17.104  -5.129  1.00 54.85           O  
ANISOU  835  O   TYR A 100A    6794   7403   6641  -1897  -1657    956       O  
ATOM    836  CB  TYR A 100A    -55.643  17.523  -7.404  1.00 27.20           C  
ANISOU  836  CB  TYR A 100A    3627   3638   3069  -2107  -1651    957       C  
ATOM    837  CG  TYR A 100A    -56.661  18.402  -8.084  1.00 45.68           C  
ANISOU  837  CG  TYR A 100A    5988   5994   5375  -2086  -1805    967       C  
ATOM    838  CD1 TYR A 100A    -56.949  18.241  -9.431  1.00 42.88           C  
ANISOU  838  CD1 TYR A 100A    5726   5599   4966  -2218  -1861    979       C  
ATOM    839  CD2 TYR A 100A    -57.339  19.390  -7.385  1.00 46.77           C  
ANISOU  839  CD2 TYR A 100A    6059   6177   5534  -1933  -1905    961       C  
ATOM    840  CE1 TYR A 100A    -57.873  19.035 -10.064  1.00 38.27           C  
ANISOU  840  CE1 TYR A 100A    5170   5016   4357  -2200  -2028    993       C  
ATOM    841  CE2 TYR A 100A    -58.270  20.195  -8.015  1.00 44.38           C  
ANISOU  841  CE2 TYR A 100A    5770   5877   5215  -1898  -2066    965       C  
ATOM    842  CZ  TYR A 100A    -58.535  20.007  -9.356  1.00 45.04           C  
ANISOU  842  CZ  TYR A 100A    5948   5916   5251  -2033  -2136    985       C  
ATOM    843  OH  TYR A 100A    -59.467  20.787 -10.002  1.00 49.30           O  
ANISOU  843  OH  TYR A 100A    6509   6445   5780  -2001  -2321    993       O  
ATOM    844  N   PHE A 100B    -55.990  17.499  -4.371  1.00 36.32           N  
ANISOU  844  N   PHE A 100B    4566   4925   4310  -1856  -1577    950       N  
ATOM    845  CA  PHE A 100B    -56.443  18.036  -3.101  1.00 29.30           C  
ANISOU  845  CA  PHE A 100B    3596   4100   3436  -1722  -1589    940       C  
ATOM    846  C   PHE A 100B    -56.579  19.550  -3.174  1.00 33.39           C  
ANISOU  846  C   PHE A 100B    4156   4592   3939  -1612  -1708    925       C  
ATOM    847  O   PHE A 100B    -55.597  20.279  -3.074  1.00 41.48           O  
ANISOU  847  O   PHE A 100B    5276   5532   4954  -1585  -1729    927       O  
ATOM    848  CB  PHE A 100B    -55.490  17.602  -1.982  1.00 32.60           C  
ANISOU  848  CB  PHE A 100B    4024   4486   3877  -1704  -1501    945       C  
ATOM    849  CG  PHE A 100B    -55.432  16.109  -1.789  1.00 38.01           C  
ANISOU  849  CG  PHE A 100B    4678   5187   4577  -1798  -1404    958       C  
ATOM    850  CD1 PHE A 100B    -54.338  15.376  -2.229  1.00 37.75           C  
ANISOU  850  CD1 PHE A 100B    4712   5063   4569  -1881  -1349    962       C  
ATOM    851  CD2 PHE A 100B    -56.490  15.431  -1.192  1.00 37.26           C  
ANISOU  851  CD2 PHE A 100B    4490   5197   4471  -1810  -1369    960       C  
ATOM    852  CE1 PHE A 100B    -54.291  13.991  -2.060  1.00 27.00           C  
ANISOU  852  CE1 PHE A 100B    3338   3698   3223  -1959  -1276    971       C  
ATOM    853  CE2 PHE A 100B    -56.450  14.055  -1.027  1.00 31.33           C  
ANISOU  853  CE2 PHE A 100B    3734   4448   3720  -1909  -1294    976       C  
ATOM    854  CZ  PHE A 100B    -55.349  13.336  -1.462  1.00 30.73           C  
ANISOU  854  CZ  PHE A 100B    3740   4264   3671  -1977  -1255    983       C  
ATOM    855  N   ASP A 101     -57.810  20.017  -3.344  1.00 32.15           N  
ANISOU  855  N   ASP A 101     3925   4506   3785  -1547  -1793    909       N  
ATOM    856  CA  ASP A 101     -58.070  21.441  -3.528  1.00 37.71           C  
ANISOU  856  CA  ASP A 101     4675   5172   4479  -1435  -1932    891       C  
ATOM    857  C   ASP A 101     -58.086  22.228  -2.217  1.00 45.47           C  
ANISOU  857  C   ASP A 101     5625   6177   5474  -1278  -1928    860       C  
ATOM    858  O   ASP A 101     -57.708  23.402  -2.187  1.00 44.73           O  
ANISOU  858  O   ASP A 101     5629   6006   5361  -1197  -2020    853       O  
ATOM    859  CB  ASP A 101     -59.368  21.672  -4.323  1.00 39.11           C  
ANISOU  859  CB  ASP A 101     4788   5402   4670  -1418  -2050    880       C  
ATOM    860  CG  ASP A 101     -60.587  21.024  -3.678  1.00 53.35           C  
ANISOU  860  CG  ASP A 101     6396   7357   6517  -1379  -1997    854       C  
ATOM    861  OD1 ASP A 101     -60.467  19.902  -3.137  1.00 61.44           O  
ANISOU  861  OD1 ASP A 101     7363   8440   7542  -1454  -1859    864       O  
ATOM    862  OD2 ASP A 101     -61.678  21.631  -3.731  1.00 45.43           O1-
ANISOU  862  OD2 ASP A 101     5295   6415   5550  -1277  -2098    819       O1-
ATOM    863  N   VAL A 102     -58.521  21.585  -1.137  1.00 44.60           N  
ANISOU  863  N   VAL A 102     5396   6166   5384  -1248  -1823    842       N  
ATOM    864  CA  VAL A 102     -58.540  22.233   0.173  1.00 45.03           C  
ANISOU  864  CA  VAL A 102     5430   6244   5437  -1117  -1800    809       C  
ATOM    865  C   VAL A 102     -57.849  21.383   1.235  1.00 50.42           C  
ANISOU  865  C   VAL A 102     6116   6932   6108  -1169  -1667    827       C  
ATOM    866  O   VAL A 102     -58.107  20.188   1.348  1.00 50.29           O  
ANISOU  866  O   VAL A 102     6032   6979   6097  -1265  -1577    841       O  
ATOM    867  CB  VAL A 102     -59.968  22.562   0.630  1.00 40.24           C  
ANISOU  867  CB  VAL A 102     4670   5762   4859  -1001  -1817    747       C  
ATOM    868  CG1 VAL A 102     -59.930  23.315   1.949  1.00 30.73           C  
ANISOU  868  CG1 VAL A 102     3468   4568   3642   -866  -1786    702       C  
ATOM    869  CG2 VAL A 102     -60.682  23.379  -0.430  1.00 39.40           C  
ANISOU  869  CG2 VAL A 102     4555   5636   4777   -940  -1977    729       C  
ATOM    870  N   TRP A 103     -56.976  22.016   2.012  1.00 50.95           N  
ANISOU  870  N   TRP A 103     6276   6926   6157  -1111  -1669    831       N  
ATOM    871  CA  TRP A 103     -56.170  21.322   3.009  1.00 40.72           C  
ANISOU  871  CA  TRP A 103     5011   5607   4852  -1160  -1576    856       C  
ATOM    872  C   TRP A 103     -56.439  21.839   4.413  1.00 47.98           C  
ANISOU  872  C   TRP A 103     5925   6563   5743  -1059  -1546    823       C  
ATOM    873  O   TRP A 103     -56.831  22.991   4.600  1.00 55.41           O  
ANISOU  873  O   TRP A 103     6878   7504   6671   -935  -1610    783       O  
ATOM    874  CB  TRP A 103     -54.687  21.531   2.711  1.00 40.80           C  
ANISOU  874  CB  TRP A 103     5149   5486   4868  -1205  -1605    895       C  
ATOM    875  CG  TRP A 103     -54.214  20.917   1.440  1.00 43.50           C  
ANISOU  875  CG  TRP A 103     5511   5785   5232  -1322  -1603    919       C  
ATOM    876  CD1 TRP A 103     -54.668  21.177   0.183  1.00 43.27           C  
ANISOU  876  CD1 TRP A 103     5487   5757   5198  -1352  -1664    913       C  
ATOM    877  CD2 TRP A 103     -53.175  19.946   1.302  1.00 37.06           C  
ANISOU  877  CD2 TRP A 103     4721   4910   4448  -1425  -1539    945       C  
ATOM    878  CE2 TRP A 103     -53.053  19.657  -0.069  1.00 38.59           C  
ANISOU  878  CE2 TRP A 103     4935   5079   4649  -1517  -1546    947       C  
ATOM    879  CE3 TRP A 103     -52.337  19.287   2.207  1.00 38.80           C  
ANISOU  879  CE3 TRP A 103     4955   5091   4695  -1447  -1485    964       C  
ATOM    880  NE1 TRP A 103     -53.981  20.419  -0.731  1.00 43.66           N  
ANISOU  880  NE1 TRP A 103     5572   5757   5261  -1479  -1626    932       N  
ATOM    881  CZ2 TRP A 103     -52.130  18.740  -0.559  1.00 35.28           C  
ANISOU  881  CZ2 TRP A 103     4535   4603   4265  -1621  -1483    955       C  
ATOM    882  CZ3 TRP A 103     -51.419  18.380   1.721  1.00 38.39           C  
ANISOU  882  CZ3 TRP A 103     4917   4978   4691  -1539  -1441    977       C  
ATOM    883  CH2 TRP A 103     -51.324  18.112   0.349  1.00 35.54           C  
ANISOU  883  CH2 TRP A 103     4564   4600   4340  -1621  -1432    966       C  
ATOM    884  N   GLY A 104     -56.213  20.982   5.402  1.00 39.35           N  
ANISOU  884  N   GLY A 104     4828   5490   4632  -1117  -1454    839       N  
ATOM    885  CA  GLY A 104     -56.218  21.409   6.785  1.00 37.17           C  
ANISOU  885  CA  GLY A 104     4588   5223   4312  -1052  -1420    816       C  
ATOM    886  C   GLY A 104     -54.898  22.092   7.092  1.00 47.82           C  
ANISOU  886  C   GLY A 104     6081   6435   5653  -1026  -1483    851       C  
ATOM    887  O   GLY A 104     -54.005  22.123   6.245  1.00 49.53           O  
ANISOU  887  O   GLY A 104     6351   6566   5903  -1069  -1536    888       O  
ATOM    888  N   GLN A 105     -54.767  22.639   8.296  1.00 51.83           N  
ANISOU  888  N   GLN A 105     6655   6926   6112   -966  -1473    836       N  
ATOM    889  CA  GLN A 105     -53.546  23.341   8.673  1.00 65.09           C  
ANISOU  889  CA  GLN A 105     8474   8478   7778   -945  -1542    872       C  
ATOM    890  C   GLN A 105     -52.453  22.372   9.114  1.00 58.98           C  
ANISOU  890  C   GLN A 105     7752   7633   7025  -1054  -1522    934       C  
ATOM    891  O   GLN A 105     -51.284  22.739   9.223  1.00 64.04           O  
ANISOU  891  O   GLN A 105     8485   8167   7680  -1064  -1585    973       O  
ATOM    892  CB  GLN A 105     -53.833  24.372   9.766  1.00 88.03           C  
ANISOU  892  CB  GLN A 105    11448  11380  10618   -837  -1551    830       C  
ATOM    893  CG  GLN A 105     -54.606  25.589   9.271  1.00105.75           C  
ANISOU  893  CG  GLN A 105    13674  13647  12858   -701  -1614    767       C  
ATOM    894  CD  GLN A 105     -54.893  26.595  10.373  1.00117.28           C  
ANISOU  894  CD  GLN A 105    15210  15097  14254   -585  -1616    713       C  
ATOM    895  NE2 GLN A 105     -55.249  27.814   9.982  1.00121.22           N  
ANISOU  895  NE2 GLN A 105    15741  15567  14752   -455  -1705    667       N  
ATOM    896  OE1 GLN A 105     -54.798  26.280  11.559  1.00119.20           O  
ANISOU  896  OE1 GLN A 105    15496  15349  14444   -615  -1542    712       O  
ATOM    897  N   GLY A 106     -52.842  21.128   9.363  1.00 53.60           N  
ANISOU  897  N   GLY A 106     7010   7009   6348  -1139  -1444    943       N  
ATOM    898  CA  GLY A 106     -51.900  20.106   9.769  1.00 50.62           C  
ANISOU  898  CA  GLY A 106     6681   6556   5998  -1235  -1440    999       C  
ATOM    899  C   GLY A 106     -51.710  20.052  11.271  1.00 48.88           C  
ANISOU  899  C   GLY A 106     6556   6305   5713  -1247  -1430   1014       C  
ATOM    900  O   GLY A 106     -51.922  21.042  11.971  1.00 50.94           O  
ANISOU  900  O   GLY A 106     6874   6570   5912  -1172  -1441    988       O  
ATOM    901  N   THR A 107     -51.319  18.882  11.763  1.00 39.48           N  
ANISOU  901  N   THR A 107     5395   5074   4531  -1345  -1417   1056       N  
ATOM    902  CA  THR A 107     -51.002  18.700  13.169  1.00 41.26           C  
ANISOU  902  CA  THR A 107     5739   5246   4692  -1383  -1428   1084       C  
ATOM    903  C   THR A 107     -49.697  17.917  13.249  1.00 46.70           C  
ANISOU  903  C   THR A 107     6487   5800   5458  -1445  -1508   1149       C  
ATOM    904  O   THR A 107     -49.445  17.042  12.418  1.00 48.87           O  
ANISOU  904  O   THR A 107     6696   6059   5813  -1489  -1506   1161       O  
ATOM    905  CB  THR A 107     -52.127  17.955  13.917  1.00 49.42           C  
ANISOU  905  CB  THR A 107     6763   6380   5634  -1458  -1329   1061       C  
ATOM    906  CG2 THR A 107     -52.174  16.489  13.507  1.00 45.38           C  
ANISOU  906  CG2 THR A 107     6214   5869   5160  -1570  -1308   1093       C  
ATOM    907  OG1 THR A 107     -51.912  18.054  15.330  1.00 54.68           O  
ANISOU  907  OG1 THR A 107     7570   6997   6210  -1493  -1338   1079       O  
ATOM    908  N   THR A 108     -48.865  18.241  14.235  1.00 41.66           N  
ANISOU  908  N   THR A 108     5970   5059   4800  -1446  -1585   1187       N  
ATOM    909  CA  THR A 108     -47.517  17.688  14.295  1.00 35.68           C  
ANISOU  909  CA  THR A 108     5253   4165   4139  -1482  -1686   1244       C  
ATOM    910  C   THR A 108     -47.423  16.516  15.257  1.00 43.39           C  
ANISOU  910  C   THR A 108     6320   5080   5088  -1578  -1712   1287       C  
ATOM    911  O   THR A 108     -47.924  16.580  16.380  1.00 58.74           O  
ANISOU  911  O   THR A 108     8370   7036   6911  -1619  -1694   1294       O  
ATOM    912  CB  THR A 108     -46.483  18.768  14.675  1.00 44.87           C  
ANISOU  912  CB  THR A 108     6492   5237   5319  -1430  -1786   1268       C  
ATOM    913  CG2 THR A 108     -45.067  18.218  14.593  1.00 39.81           C  
ANISOU  913  CG2 THR A 108     5851   4468   4807  -1459  -1892   1315       C  
ATOM    914  OG1 THR A 108     -46.605  19.880  13.780  1.00 58.88           O  
ANISOU  914  OG1 THR A 108     8208   7062   7102  -1353  -1770   1230       O  
ATOM    915  N   VAL A 109     -46.774  15.447  14.807  1.00 39.72           N  
ANISOU  915  N   VAL A 109     5820   4540   4729  -1618  -1757   1312       N  
ATOM    916  CA  VAL A 109     -46.626  14.235  15.607  1.00 39.09           C  
ANISOU  916  CA  VAL A 109     5838   4379   4636  -1711  -1808   1357       C  
ATOM    917  C   VAL A 109     -45.167  13.827  15.738  1.00 43.54           C  
ANISOU  917  C   VAL A 109     6432   4778   5335  -1701  -1954   1402       C  
ATOM    918  O   VAL A 109     -44.471  13.634  14.744  1.00 52.15           O  
ANISOU  918  O   VAL A 109     7410   5838   6565  -1658  -1969   1383       O  
ATOM    919  CB  VAL A 109     -47.396  13.053  14.990  1.00 37.79           C  
ANISOU  919  CB  VAL A 109     5614   4273   4471  -1777  -1731   1341       C  
ATOM    920  CG1 VAL A 109     -47.106  11.779  15.759  1.00 31.35           C  
ANISOU  920  CG1 VAL A 109     4920   3344   3648  -1875  -1810   1392       C  
ATOM    921  CG2 VAL A 109     -48.890  13.347  14.966  1.00 35.39           C  
ANISOU  921  CG2 VAL A 109     5269   4139   4039  -1799  -1594   1296       C  
ATOM    922  N   THR A 110     -44.711  13.691  16.973  1.00 42.82           N  
ANISOU  922  N   THR A 110     6489   4579   5200  -1746  -2061   1456       N  
ATOM    923  CA  THR A 110     -43.342  13.285  17.244  1.00 36.22           C  
ANISOU  923  CA  THR A 110     5685   3578   4498  -1736  -2225   1501       C  
ATOM    924  C   THR A 110     -43.325  11.917  17.912  1.00 46.03           C  
ANISOU  924  C   THR A 110     7043   4715   5732  -1825  -2307   1545       C  
ATOM    925  O   THR A 110     -44.060  11.673  18.864  1.00 60.12           O  
ANISOU  925  O   THR A 110     8975   6508   7359  -1918  -2293   1571       O  
ATOM    926  CB  THR A 110     -42.646  14.306  18.158  1.00 40.38           C  
ANISOU  926  CB  THR A 110     6311   4036   4996  -1716  -2329   1540       C  
ATOM    927  CG2 THR A 110     -41.251  13.834  18.537  1.00 33.71           C  
ANISOU  927  CG2 THR A 110     5494   3018   4297  -1712  -2518   1590       C  
ATOM    928  OG1 THR A 110     -42.559  15.565  17.480  1.00 47.36           O  
ANISOU  928  OG1 THR A 110     7100   5001   5895  -1636  -2271   1501       O  
ATOM    929  N   VAL A 111     -42.497  11.017  17.398  1.00 43.28           N  
ANISOU  929  N   VAL A 111     6633   4262   5549  -1801  -2392   1546       N  
ATOM    930  CA  VAL A 111     -42.364   9.695  17.989  1.00 37.05           C  
ANISOU  930  CA  VAL A 111     5966   3342   4768  -1875  -2502   1589       C  
ATOM    931  C   VAL A 111     -41.067   9.610  18.773  1.00 48.27           C  
ANISOU  931  C   VAL A 111     7466   4578   6297  -1854  -2719   1644       C  
ATOM    932  O   VAL A 111     -39.975   9.623  18.204  1.00 52.45           O  
ANISOU  932  O   VAL A 111     7865   5040   7021  -1764  -2794   1623       O  
ATOM    933  CB  VAL A 111     -42.410   8.590  16.930  1.00 39.72           C  
ANISOU  933  CB  VAL A 111     6204   3673   5216  -1861  -2463   1549       C  
ATOM    934  CG1 VAL A 111     -41.976   7.268  17.532  1.00 49.82           C  
ANISOU  934  CG1 VAL A 111     7616   4773   6540  -1914  -2625   1595       C  
ATOM    935  CG2 VAL A 111     -43.812   8.481  16.345  1.00 43.54           C  
ANISOU  935  CG2 VAL A 111     6649   4326   5570  -1916  -2276   1512       C  
ATOM    936  N   SER A 112     -41.196   9.530  20.091  1.00 53.79           N  
ANISOU  936  N   SER A 112    10988   4572   4878  -1981  -2271    -84       N  
ATOM    937  CA  SER A 112     -40.040   9.580  20.969  1.00 54.76           C  
ANISOU  937  CA  SER A 112    11069   4746   4990  -1712  -2054    -92       C  
ATOM    938  C   SER A 112     -40.368   8.948  22.310  1.00 63.14           C  
ANISOU  938  C   SER A 112    12080   5798   6114  -1855  -2013    -25       C  
ATOM    939  O   SER A 112     -41.522   8.946  22.738  1.00 73.09           O  
ANISOU  939  O   SER A 112    13156   7118   7496  -2143  -2110     48       O  
ATOM    940  CB  SER A 112     -39.603  11.031  21.172  1.00 57.54           C  
ANISOU  940  CB  SER A 112    11002   5373   5487  -1544  -1903    -95       C  
ATOM    941  OG  SER A 112     -38.515  11.118  22.070  1.00 58.51           O  
ANISOU  941  OG  SER A 112    11056   5575   5601  -1318  -1711    -96       O  
ATOM    942  N   SER A 113     -39.351   8.403  22.968  1.00 58.81           N  
ANISOU  942  N   SER A 113    11683   5193   5471  -1640  -1864    -32       N  
ATOM    943  CA  SER A 113     -39.535   7.825  24.290  1.00 53.03           C  
ANISOU  943  CA  SER A 113    10893   4467   4788  -1728  -1798     37       C  
ATOM    944  C   SER A 113     -39.427   8.911  25.353  1.00 53.86           C  
ANISOU  944  C   SER A 113    10519   4878   5068  -1660  -1645     62       C  
ATOM    945  O   SER A 113     -39.819   8.709  26.499  1.00 63.67           O  
ANISOU  945  O   SER A 113    11603   6198   6392  -1758  -1597    130       O  
ATOM    946  CB  SER A 113     -38.510   6.725  24.550  1.00 59.48           C  
ANISOU  946  CB  SER A 113    12094   5097   5409  -1513  -1699     29       C  
ATOM    947  OG  SER A 113     -37.211   7.265  24.714  1.00 67.74           O  
ANISOU  947  OG  SER A 113    13040   6297   6401  -1168  -1507      1       O  
TER     948      SER A 113 
ATOM    949  N   ASP B   1     -45.479   1.454  -9.247  1.00 98.01           N  
ANISOU  949  N   ASP B   1    14764  11810  10666  -3369    564  -1311       N  
ATOM    950  CA  ASP B   1     -46.047   2.764  -8.946  1.00 94.72           C  
ANISOU  950  CA  ASP B   1    14256  11564  10168  -3396    503  -1168       C  
ATOM    951  C   ASP B   1     -45.378   3.865  -9.768  1.00 93.64           C  
ANISOU  951  C   ASP B   1    14038  11545   9996  -3313    629  -1122       C  
ATOM    952  O   ASP B   1     -44.465   3.597 -10.553  1.00104.65           O  
ANISOU  952  O   ASP B   1    15444  12893  11427  -3237    777  -1202       O  
ATOM    953  CB  ASP B   1     -45.951   3.068  -7.447  1.00 92.24           C  
ANISOU  953  CB  ASP B   1    13860  11169  10019  -3389    381  -1041       C  
ATOM    954  CG  ASP B   1     -44.523   3.285  -6.978  1.00 91.69           C  
ANISOU  954  CG  ASP B   1    13695  10956  10185  -3261    434   -985       C  
ATOM    955  OD1 ASP B   1     -43.745   3.946  -7.699  1.00 92.28           O  
ANISOU  955  OD1 ASP B   1    13703  11085  10274  -3171    557   -971       O  
ATOM    956  OD2 ASP B   1     -44.183   2.805  -5.876  1.00 88.07           O1-
ANISOU  956  OD2 ASP B   1    13231  10331   9902  -3259    344   -948       O1-
ATOM    957  N   ILE B   2     -45.829   5.103  -9.578  1.00 74.83           N  
ANISOU  957  N   ILE B   2    11572   9312   7547  -3328    573   -994       N  
ATOM    958  CA  ILE B   2     -45.348   6.228 -10.381  1.00 64.91           C  
ANISOU  958  CA  ILE B   2    10246   8185   6231  -3272    668   -936       C  
ATOM    959  C   ILE B   2     -44.527   7.229  -9.574  1.00 66.38           C  
ANISOU  959  C   ILE B   2    10292   8342   6589  -3179    650   -789       C  
ATOM    960  O   ILE B   2     -45.050   7.895  -8.682  1.00 60.47           O  
ANISOU  960  O   ILE B   2     9488   7627   5859  -3203    528   -680       O  
ATOM    961  CB  ILE B   2     -46.515   6.997 -11.029  1.00 60.40           C  
ANISOU  961  CB  ILE B   2     9696   7822   5432  -3366    611   -901       C  
ATOM    962  CG1 ILE B   2     -47.388   6.064 -11.868  1.00 60.16           C  
ANISOU  962  CG1 ILE B   2     9812   7826   5219  -3473    610  -1033       C  
ATOM    963  CG2 ILE B   2     -45.991   8.139 -11.884  1.00 59.26           C  
ANISOU  963  CG2 ILE B   2     9489   7804   5221  -3319    697   -837       C  
ATOM    964  CD1 ILE B   2     -48.546   6.770 -12.538  1.00 50.73           C  
ANISOU  964  CD1 ILE B   2     8637   6824   3813  -3574    538   -993       C  
ATOM    965  N   GLN B   3     -43.246   7.346  -9.902  1.00 78.03           N  
ANISOU  965  N   GLN B   3    11707   9753   8187  -3076    775   -787       N  
ATOM    966  CA  GLN B   3     -42.367   8.285  -9.211  1.00 88.06           C  
ANISOU  966  CA  GLN B   3    12845  10987   9628  -2988    758   -641       C  
ATOM    967  C   GLN B   3     -42.209   9.579 -10.006  1.00 80.22           C  
ANISOU  967  C   GLN B   3    11786  10166   8526  -2970    812   -557       C  
ATOM    968  O   GLN B   3     -42.451   9.610 -11.212  1.00 69.46           O  
ANISOU  968  O   GLN B   3    10481   8925   6985  -3007    904   -628       O  
ATOM    969  CB  GLN B   3     -41.001   7.649  -8.931  1.00106.12           C  
ANISOU  969  CB  GLN B   3    15083  13080  12159  -2885    841   -666       C  
ATOM    970  CG  GLN B   3     -41.043   6.508  -7.918  1.00121.51           C  
ANISOU  970  CG  GLN B   3    17080  14832  14257  -2901    748   -711       C  
ATOM    971  CD  GLN B   3     -39.659   6.032  -7.519  1.00132.14           C  
ANISOU  971  CD  GLN B   3    18353  15973  15882  -2794    800   -705       C  
ATOM    972  NE2 GLN B   3     -39.605   5.003  -6.678  1.00132.21           N  
ANISOU  972  NE2 GLN B   3    18406  15792  16036  -2809    711   -743       N  
ATOM    973  OE1 GLN B   3     -38.650   6.584  -7.960  1.00135.20           O  
ANISOU  973  OE1 GLN B   3    18641  16371  16360  -2704    912   -661       O  
ATOM    974  N   MET B   4     -41.809  10.646  -9.319  1.00 84.37           N  
ANISOU  974  N   MET B   4    12204  10697   9155  -2921    746   -403       N  
ATOM    975  CA  MET B   4     -41.688  11.964  -9.937  1.00 84.05           C  
ANISOU  975  CA  MET B   4    12098  10812   9023  -2909    765   -301       C  
ATOM    976  C   MET B   4     -40.314  12.570  -9.672  1.00 77.06           C  
ANISOU  976  C   MET B   4    11094   9856   8331  -2806    815   -192       C  
ATOM    977  O   MET B   4     -39.907  12.730  -8.523  1.00 74.76           O  
ANISOU  977  O   MET B   4    10744   9441   8220  -2763    724   -100       O  
ATOM    978  CB  MET B   4     -42.745  12.912  -9.375  1.00 92.30           C  
ANISOU  978  CB  MET B   4    13127  11960   9982  -2962    604   -201       C  
ATOM    979  CG  MET B   4     -44.056  12.253  -8.980  1.00 94.83           C  
ANISOU  979  CG  MET B   4    13532  12291  10209  -3054    508   -274       C  
ATOM    980  SD  MET B   4     -45.205  12.130 -10.358  1.00 71.30           S  
ANISOU  980  SD  MET B   4    10645   9492   6953  -3161    531   -369       S  
ATOM    981  CE  MET B   4     -45.001  13.745 -11.098  1.00 91.02           C  
ANISOU  981  CE  MET B   4    13064  12153   9367  -3141    530   -241       C  
ATOM    982  N   THR B   5     -39.601  12.918 -10.733  1.00 77.54           N  
ANISOU  982  N   THR B   5    11120   9993   8349  -2776    957   -195       N  
ATOM    983  CA  THR B   5     -38.308  13.568 -10.577  1.00 74.41           C  
ANISOU  983  CA  THR B   5    10597   9547   8130  -2686   1008    -80       C  
ATOM    984  C   THR B   5     -38.432  15.041 -10.929  1.00 71.09           C  
ANISOU  984  C   THR B   5    10124   9287   7602  -2705    957     60       C  
ATOM    985  O   THR B   5     -38.833  15.395 -12.038  1.00 70.21           O  
ANISOU  985  O   THR B   5    10056   9335   7285  -2763   1015     29       O  
ATOM    986  CB  THR B   5     -37.228  12.912 -11.448  1.00 79.19           C  
ANISOU  986  CB  THR B   5    11179  10109   8802  -2630   1222   -175       C  
ATOM    987  CG2 THR B   5     -35.870  13.543 -11.167  1.00 74.95           C  
ANISOU  987  CG2 THR B   5    10490   9506   8483  -2536   1265    -42       C  
ATOM    988  OG1 THR B   5     -37.173  11.507 -11.165  1.00 83.39           O  
ANISOU  988  OG1 THR B   5    11768  10482   9432  -2611   1260   -316       O  
ATOM    989  N   GLN B   6     -38.087  15.897  -9.978  1.00 67.61           N  
ANISOU  989  N   GLN B   6     9597   8795   7298  -2663    836    217       N  
ATOM    990  CA  GLN B   6     -38.294  17.325 -10.139  1.00 65.02           C  
ANISOU  990  CA  GLN B   6     9223   8598   6882  -2680    750    358       C  
ATOM    991  C   GLN B   6     -36.965  18.061 -10.205  1.00 61.77           C  
ANISOU  991  C   GLN B   6     8693   8161   6617  -2611    799    490       C  
ATOM    992  O   GLN B   6     -36.060  17.783  -9.419  1.00 71.08           O  
ANISOU  992  O   GLN B   6     9804   9180   8024  -2542    796    538       O  
ATOM    993  CB  GLN B   6     -39.130  17.852  -8.975  1.00 70.93           C  
ANISOU  993  CB  GLN B   6     9982   9321   7646  -2697    552    435       C  
ATOM    994  CG  GLN B   6     -39.780  19.190  -9.231  1.00 73.65           C  
ANISOU  994  CG  GLN B   6    10312   9816   7855  -2731    446    537       C  
ATOM    995  CD  GLN B   6     -40.939  19.446  -8.300  1.00 69.84           C  
ANISOU  995  CD  GLN B   6     9865   9334   7339  -2763    285    550       C  
ATOM    996  NE2 GLN B   6     -41.362  20.701  -8.217  1.00 68.61           N  
ANISOU  996  NE2 GLN B   6     9676   9264   7129  -2768    169    658       N  
ATOM    997  OE1 GLN B   6     -41.454  18.526  -7.663  1.00 68.51           O  
ANISOU  997  OE1 GLN B   6     9751   9086   7194  -2785    266    461       O  
ATOM    998  N   SER B   7     -36.843  18.994 -11.144  1.00 51.04           N  
ANISOU  998  N   SER B   7     7307   6956   5131  -2637    837    556       N  
ATOM    999  CA  SER B   7     -35.632  19.806 -11.243  1.00 57.70           C  
ANISOU  999  CA  SER B   7     8032   7793   6099  -2585    874    699       C  
ATOM   1000  C   SER B   7     -35.937  21.226 -11.708  1.00 58.30           C  
ANISOU 1000  C   SER B   7     8091   8025   6033  -2631    781    831       C  
ATOM   1001  O   SER B   7     -36.877  21.446 -12.472  1.00 70.66           O  
ANISOU 1001  O   SER B   7     9735   9735   7377  -2710    765    782       O  
ATOM   1002  CB  SER B   7     -34.616  19.160 -12.185  1.00 64.45           C  
ANISOU 1002  CB  SER B   7     8847   8648   6992  -2558   1107    620       C  
ATOM   1003  OG  SER B   7     -34.915  19.467 -13.535  1.00 75.42           O  
ANISOU 1003  OG  SER B   7    10289  10222   8143  -2632   1209    575       O  
ATOM   1004  N   PRO B   8     -35.138  22.198 -11.246  1.00 45.68           N  
ANISOU 1004  N   PRO B   8     6393   6392   4571  -2588    706   1006       N  
ATOM   1005  CA  PRO B   8     -34.023  21.973 -10.322  1.00 48.16           C  
ANISOU 1005  CA  PRO B   8     6614   6526   5158  -2503    704   1081       C  
ATOM   1006  C   PRO B   8     -34.550  21.724  -8.916  1.00 54.06           C  
ANISOU 1006  C   PRO B   8     7402   7130   6007  -2483    539   1087       C  
ATOM   1007  O   PRO B   8     -35.704  22.050  -8.643  1.00 65.33           O  
ANISOU 1007  O   PRO B   8     8906   8616   7300  -2527    417   1070       O  
ATOM   1008  CB  PRO B   8     -33.261  23.306 -10.349  1.00 36.74           C  
ANISOU 1008  CB  PRO B   8     5071   5119   3771  -2490    636   1283       C  
ATOM   1009  CG  PRO B   8     -33.945  24.165 -11.367  1.00 42.15           C  
ANISOU 1009  CG  PRO B   8     5800   6005   4208  -2568    617   1303       C  
ATOM   1010  CD  PRO B   8     -35.322  23.626 -11.537  1.00 46.85           C  
ANISOU 1010  CD  PRO B   8     6518   6661   4620  -2623    589   1154       C  
ATOM   1011  N   SER B   9     -33.729  21.157  -8.040  1.00 54.85           N  
ANISOU 1011  N   SER B   9     7453   7043   6344  -2423    533   1113       N  
ATOM   1012  CA  SER B   9     -34.152  20.947  -6.663  1.00 64.32           C  
ANISOU 1012  CA  SER B   9     8703   8099   7637  -2418    372   1131       C  
ATOM   1013  C   SER B   9     -34.134  22.274  -5.910  1.00 63.88           C  
ANISOU 1013  C   SER B   9     8626   8033   7612  -2413    188   1312       C  
ATOM   1014  O   SER B   9     -34.899  22.475  -4.968  1.00 63.04           O  
ANISOU 1014  O   SER B   9     8589   7882   7479  -2433     43   1323       O  
ATOM   1015  CB  SER B   9     -33.263  19.914  -5.969  1.00 68.88           C  
ANISOU 1015  CB  SER B   9     9243   8467   8460  -2367    405   1110       C  
ATOM   1016  OG  SER B   9     -31.894  20.250  -6.097  1.00 82.66           O  
ANISOU 1016  OG  SER B   9    10859  10150  10397  -2309    456   1229       O  
ATOM   1017  N   THR B  10     -33.261  23.181  -6.338  1.00 58.82           N  
ANISOU 1017  N   THR B  10     7893   7434   7023  -2389    197   1450       N  
ATOM   1018  CA  THR B  10     -33.171  24.500  -5.724  1.00 63.26           C  
ANISOU 1018  CA  THR B  10     8437   7987   7613  -2385     19   1628       C  
ATOM   1019  C   THR B  10     -33.060  25.560  -6.802  1.00 59.42           C  
ANISOU 1019  C   THR B  10     7903   7674   6999  -2407     43   1709       C  
ATOM   1020  O   THR B  10     -32.753  25.258  -7.952  1.00 74.28           O  
ANISOU 1020  O   THR B  10     9750   9663   8812  -2422    212   1650       O  
ATOM   1021  CB  THR B  10     -31.957  24.615  -4.795  1.00 73.48           C  
ANISOU 1021  CB  THR B  10     9658   9090   9169  -2335    -54   1773       C  
ATOM   1022  CG2 THR B  10     -32.263  25.555  -3.639  1.00 71.62           C  
ANISOU 1022  CG2 THR B  10     9477   8779   8957  -2340   -278   1899       C  
ATOM   1023  OG1 THR B  10     -31.620  23.320  -4.284  1.00 86.86           O  
ANISOU 1023  OG1 THR B  10    11359  10629  11017  -2313      4   1683       O  
ATOM   1024  N   LEU B  11     -33.298  26.808  -6.424  1.00 48.51           N  
ANISOU 1024  N   LEU B  11     6529   6318   5585  -2415   -127   1844       N  
ATOM   1025  CA  LEU B  11     -33.368  27.877  -7.401  1.00 41.23           C  
ANISOU 1025  CA  LEU B  11     5580   5562   4523  -2450   -141   1924       C  
ATOM   1026  C   LEU B  11     -33.278  29.243  -6.738  1.00 55.65           C  
ANISOU 1026  C   LEU B  11     7398   7352   6393  -2438   -350   2105       C  
ATOM   1027  O   LEU B  11     -33.808  29.454  -5.649  1.00 72.45           O  
ANISOU 1027  O   LEU B  11     9589   9385   8555  -2421   -496   2116       O  
ATOM   1028  CB  LEU B  11     -34.670  27.755  -8.186  1.00 44.48           C  
ANISOU 1028  CB  LEU B  11     6073   6134   4695  -2508   -112   1789       C  
ATOM   1029  CG  LEU B  11     -34.951  28.732  -9.321  1.00 58.40           C  
ANISOU 1029  CG  LEU B  11     7831   8080   6280  -2566   -130   1847       C  
ATOM   1030  CD1 LEU B  11     -33.685  29.048 -10.105  1.00 79.47           C  
ANISOU 1030  CD1 LEU B  11    10406  10791   8998  -2572    -23   1952       C  
ATOM   1031  CD2 LEU B  11     -36.012  28.138 -10.225  1.00 52.67           C  
ANISOU 1031  CD2 LEU B  11     7181   7487   5344  -2630    -46   1683       C  
ATOM   1032  N   SER B  12     -32.591  30.166  -7.398  1.00 57.20           N  
ANISOU 1032  N   SER B  12     7524   7623   6584  -2453   -362   2245       N  
ATOM   1033  CA  SER B  12     -32.515  31.543  -6.938  1.00 58.40           C  
ANISOU 1033  CA  SER B  12     7675   7756   6759  -2449   -567   2421       C  
ATOM   1034  C   SER B  12     -32.665  32.462  -8.145  1.00 57.06           C  
ANISOU 1034  C   SER B  12     7484   7769   6425  -2507   -573   2484       C  
ATOM   1035  O   SER B  12     -31.945  32.318  -9.133  1.00 70.78           O  
ANISOU 1035  O   SER B  12     9154   9595   8143  -2538   -426   2504       O  
ATOM   1036  CB  SER B  12     -31.182  31.794  -6.232  1.00 65.81           C  
ANISOU 1036  CB  SER B  12     8535   8541   7929  -2409   -621   2587       C  
ATOM   1037  OG  SER B  12     -31.236  32.962  -5.429  1.00 70.95           O  
ANISOU 1037  OG  SER B  12     9220   9121   8619  -2398   -848   2736       O  
ATOM   1038  N   ALA B  13     -33.608  33.394  -8.075  1.00 39.71           N  
ANISOU 1038  N   ALA B  13     5347   5628   4112  -2526   -740   2512       N  
ATOM   1039  CA  ALA B  13     -33.851  34.298  -9.195  1.00 44.06           C  
ANISOU 1039  CA  ALA B  13     5892   6344   4504  -2591   -777   2577       C  
ATOM   1040  C   ALA B  13     -34.303  35.675  -8.736  1.00 48.03           C  
ANISOU 1040  C   ALA B  13     6425   6830   4996  -2584  -1025   2702       C  
ATOM   1041  O   ALA B  13     -34.918  35.816  -7.679  1.00 54.26           O  
ANISOU 1041  O   ALA B  13     7268   7516   5834  -2535  -1148   2675       O  
ATOM   1042  CB  ALA B  13     -34.870  33.699 -10.160  1.00 35.17           C  
ANISOU 1042  CB  ALA B  13     4821   5365   3177  -2650   -671   2409       C  
ATOM   1043  N   SER B  14     -33.994  36.684  -9.545  1.00 41.50           N  
ANISOU 1043  N   SER B  14     5566   6101   4101  -2637  -1095   2838       N  
ATOM   1044  CA  SER B  14     -34.348  38.062  -9.232  1.00 46.93           C  
ANISOU 1044  CA  SER B  14     6279   6770   4780  -2634  -1339   2969       C  
ATOM   1045  C   SER B  14     -35.803  38.339  -9.579  1.00 55.16           C  
ANISOU 1045  C   SER B  14     7388   7905   5667  -2658  -1425   2869       C  
ATOM   1046  O   SER B  14     -36.356  37.735 -10.500  1.00 65.67           O  
ANISOU 1046  O   SER B  14     8735   9362   6855  -2716  -1306   2752       O  
ATOM   1047  CB  SER B  14     -33.443  39.030  -9.998  1.00 48.07           C  
ANISOU 1047  CB  SER B  14     6365   6985   4915  -2693  -1393   3162       C  
ATOM   1048  OG  SER B  14     -32.075  38.757  -9.740  1.00 63.22           O  
ANISOU 1048  OG  SER B  14     8202   8826   6991  -2673  -1304   3259       O  
ATOM   1049  N   VAL B  15     -36.422  39.251  -8.834  1.00 49.83           N  
ANISOU 1049  N   VAL B  15     6750   7159   5024  -2614  -1635   2915       N  
ATOM   1050  CA  VAL B  15     -37.775  39.695  -9.137  1.00 41.80           C  
ANISOU 1050  CA  VAL B  15     5775   6217   3889  -2631  -1745   2844       C  
ATOM   1051  C   VAL B  15     -37.858  40.142 -10.592  1.00 53.61           C  
ANISOU 1051  C   VAL B  15     7257   7879   5232  -2734  -1754   2898       C  
ATOM   1052  O   VAL B  15     -37.100  41.016 -11.024  1.00 53.81           O  
ANISOU 1052  O   VAL B  15     7254   7929   5263  -2774  -1837   3066       O  
ATOM   1053  CB  VAL B  15     -38.195  40.864  -8.239  1.00 43.83           C  
ANISOU 1053  CB  VAL B  15     6061   6372   4221  -2568  -1983   2922       C  
ATOM   1054  CG1 VAL B  15     -39.416  41.571  -8.819  1.00 43.53           C  
ANISOU 1054  CG1 VAL B  15     6039   6425   4076  -2595  -2120   2893       C  
ATOM   1055  CG2 VAL B  15     -38.467  40.373  -6.826  1.00 28.63           C  
ANISOU 1055  CG2 VAL B  15     4177   4299   2402  -2481  -1973   2830       C  
ATOM   1056  N   GLY B  16     -38.770  39.533 -11.345  1.00 48.52           N  
ANISOU 1056  N   GLY B  16     6640   7348   4449  -2788  -1673   2762       N  
ATOM   1057  CA  GLY B  16     -38.925  39.851 -12.752  1.00 46.68           C  
ANISOU 1057  CA  GLY B  16     6415   7272   4050  -2904  -1678   2800       C  
ATOM   1058  C   GLY B  16     -38.435  38.744 -13.670  1.00 58.62           C  
ANISOU 1058  C   GLY B  16     7931   8883   5461  -2976  -1428   2716       C  
ATOM   1059  O   GLY B  16     -38.806  38.700 -14.851  1.00 54.88           O  
ANISOU 1059  O   GLY B  16     7491   8545   4815  -3084  -1397   2693       O  
ATOM   1060  N   ASP B  17     -37.602  37.852 -13.136  1.00 54.09           N  
ANISOU 1060  N   ASP B  17     7326   8231   4993  -2920  -1254   2670       N  
ATOM   1061  CA  ASP B  17     -37.044  36.762 -13.933  1.00 49.57           C  
ANISOU 1061  CA  ASP B  17     6752   7733   4350  -2971  -1001   2581       C  
ATOM   1062  C   ASP B  17     -38.127  35.757 -14.311  1.00 55.19           C  
ANISOU 1062  C   ASP B  17     7530   8502   4935  -3002   -908   2383       C  
ATOM   1063  O   ASP B  17     -39.103  35.578 -13.577  1.00 54.40           O  
ANISOU 1063  O   ASP B  17     7457   8345   4868  -2952   -991   2297       O  
ATOM   1064  CB  ASP B  17     -35.917  36.050 -13.176  1.00 46.91           C  
ANISOU 1064  CB  ASP B  17     6355   7275   4193  -2891   -858   2579       C  
ATOM   1065  CG  ASP B  17     -34.642  36.883 -13.087  1.00 66.38           C  
ANISOU 1065  CG  ASP B  17     8743   9706   6771  -2885   -904   2780       C  
ATOM   1066  OD1 ASP B  17     -34.649  38.049 -13.542  1.00 77.66           O  
ANISOU 1066  OD1 ASP B  17    10172  11200   8137  -2941  -1058   2923       O  
ATOM   1067  OD2 ASP B  17     -33.628  36.368 -12.558  1.00 51.57           O1-
ANISOU 1067  OD2 ASP B  17     6805   7733   5055  -2829   -796   2801       O1-
ATOM   1068  N   ARG B  18     -37.958  35.112 -15.462  1.00 53.75           N  
ANISOU 1068  N   ARG B  18     7381   8436   4605  -3092   -734   2312       N  
ATOM   1069  CA  ARG B  18     -38.814  33.992 -15.837  1.00 58.35           C  
ANISOU 1069  CA  ARG B  18     8034   9061   5074  -3125   -620   2121       C  
ATOM   1070  C   ARG B  18     -38.236  32.723 -15.222  1.00 56.47           C  
ANISOU 1070  C   ARG B  18     7776   8723   4956  -3047   -423   2003       C  
ATOM   1071  O   ARG B  18     -37.040  32.457 -15.346  1.00 65.22           O  
ANISOU 1071  O   ARG B  18     8833   9810   6139  -3029   -276   2039       O  
ATOM   1072  CB  ARG B  18     -38.898  33.855 -17.360  1.00 65.40           C  
ANISOU 1072  CB  ARG B  18     8993  10114   5740  -3265   -526   2093       C  
ATOM   1073  CG  ARG B  18     -39.957  32.877 -17.852  1.00 64.47           C  
ANISOU 1073  CG  ARG B  18     8968  10048   5478  -3322   -460   1912       C  
ATOM   1074  CD  ARG B  18     -39.859  32.668 -19.355  1.00 73.44           C  
ANISOU 1074  CD  ARG B  18    10187  11330   6384  -3467   -344   1883       C  
ATOM   1075  NE  ARG B  18     -41.001  31.921 -19.881  1.00 89.26           N  
ANISOU 1075  NE  ARG B  18    12294  13385   8234  -3541   -335   1736       N  
ATOM   1076  CZ  ARG B  18     -42.114  32.486 -20.340  1.00 98.21           C  
ANISOU 1076  CZ  ARG B  18    13480  14585   9249  -3627   -526   1764       C  
ATOM   1077  NH1 ARG B  18     -42.235  33.808 -20.338  1.00104.47           N1+
ANISOU 1077  NH1 ARG B  18    14232  15398  10061  -3645   -739   1928       N1+
ATOM   1078  NH2 ARG B  18     -43.107  31.734 -20.801  1.00 88.19           N  
ANISOU 1078  NH2 ARG B  18    12302  13355   7852  -3696   -514   1632       N  
ATOM   1079  N   VAL B  19     -39.079  31.946 -14.552  1.00 46.62           N  
ANISOU 1079  N   VAL B  19     6564   7411   3738  -3004   -426   1866       N  
ATOM   1080  CA  VAL B  19     -38.617  30.735 -13.885  1.00 46.41           C  
ANISOU 1080  CA  VAL B  19     6527   7274   3833  -2934   -269   1756       C  
ATOM   1081  C   VAL B  19     -39.418  29.519 -14.332  1.00 54.39           C  
ANISOU 1081  C   VAL B  19     7619   8324   4724  -2978   -153   1563       C  
ATOM   1082  O   VAL B  19     -40.648  29.546 -14.333  1.00 62.11           O  
ANISOU 1082  O   VAL B  19     8647   9342   5611  -3013   -257   1504       O  
ATOM   1083  CB  VAL B  19     -38.685  30.876 -12.349  1.00 49.40           C  
ANISOU 1083  CB  VAL B  19     6872   7496   4401  -2831   -388   1788       C  
ATOM   1084  CG1 VAL B  19     -38.707  29.516 -11.690  1.00 53.57           C  
ANISOU 1084  CG1 VAL B  19     7422   7920   5011  -2786   -265   1642       C  
ATOM   1085  CG2 VAL B  19     -37.517  31.701 -11.839  1.00 51.86           C  
ANISOU 1085  CG2 VAL B  19     7107   7730   4869  -2778   -446   1963       C  
ATOM   1086  N   THR B  20     -38.713  28.454 -14.710  1.00 55.45           N  
ANISOU 1086  N   THR B  20     7762   8442   4866  -2976     61   1465       N  
ATOM   1087  CA  THR B  20     -39.363  27.233 -15.176  1.00 48.09           C  
ANISOU 1087  CA  THR B  20     6917   7536   3819  -3020    181   1279       C  
ATOM   1088  C   THR B  20     -38.946  26.007 -14.377  1.00 51.01           C  
ANISOU 1088  C   THR B  20     7275   7762   4342  -2941    301   1169       C  
ATOM   1089  O   THR B  20     -37.765  25.687 -14.282  1.00 62.87           O  
ANISOU 1089  O   THR B  20     8718   9196   5973  -2887    430   1187       O  
ATOM   1090  CB  THR B  20     -39.072  26.968 -16.657  1.00 54.10           C  
ANISOU 1090  CB  THR B  20     7737   8427   4392  -3118    340   1228       C  
ATOM   1091  CG2 THR B  20     -39.634  25.619 -17.070  1.00 62.34           C  
ANISOU 1091  CG2 THR B  20     8881   9473   5332  -3156    470   1029       C  
ATOM   1092  OG1 THR B  20     -39.675  27.994 -17.455  1.00 54.37           O  
ANISOU 1092  OG1 THR B  20     7807   8595   4256  -3217    207   1316       O  
ATOM   1093  N   ILE B  21     -39.934  25.319 -13.815  1.00 53.38           N  
ANISOU 1093  N   ILE B  21     7631   8017   4635  -2938    251   1058       N  
ATOM   1094  CA  ILE B  21     -39.707  24.111 -13.032  1.00 47.25           C  
ANISOU 1094  CA  ILE B  21     6861   7102   3992  -2879    338    949       C  
ATOM   1095  C   ILE B  21     -40.201  22.887 -13.796  1.00 55.67           C  
ANISOU 1095  C   ILE B  21     8024   8205   4921  -2939    470    767       C  
ATOM   1096  O   ILE B  21     -41.285  22.906 -14.375  1.00 56.12           O  
ANISOU 1096  O   ILE B  21     8156   8365   4803  -3022    413    714       O  
ATOM   1097  CB  ILE B  21     -40.429  24.194 -11.676  1.00 39.71           C  
ANISOU 1097  CB  ILE B  21     5900   6050   3138  -2837    180    962       C  
ATOM   1098  CG1 ILE B  21     -39.884  25.370 -10.858  1.00 34.77           C  
ANISOU 1098  CG1 ILE B  21     5195   5366   2650  -2775     48   1136       C  
ATOM   1099  CG2 ILE B  21     -40.297  22.881 -10.916  1.00 36.81           C  
ANISOU 1099  CG2 ILE B  21     5558   5542   2885  -2800    255    847       C  
ATOM   1100  CD1 ILE B  21     -40.521  25.518  -9.504  1.00 40.17           C  
ANISOU 1100  CD1 ILE B  21     5883   5952   3426  -2736    -95   1150       C  
ATOM   1101  N   THR B  22     -39.409  21.820 -13.792  1.00 56.79           N  
ANISOU 1101  N   THR B  22     8168   8257   5155  -2898    637    673       N  
ATOM   1102  CA  THR B  22     -39.741  20.634 -14.572  1.00 57.92           C  
ANISOU 1102  CA  THR B  22     8411   8422   5172  -2950    775    496       C  
ATOM   1103  C   THR B  22     -40.012  19.398 -13.712  1.00 66.60           C  
ANISOU 1103  C   THR B  22     9546   9379   6380  -2913    784    375       C  
ATOM   1104  O   THR B  22     -39.317  19.149 -12.725  1.00 78.54           O  
ANISOU 1104  O   THR B  22    10991  10746   8105  -2829    780    409       O  
ATOM   1105  CB  THR B  22     -38.628  20.313 -15.588  1.00 66.63           C  
ANISOU 1105  CB  THR B  22     9508   9556   6253  -2947    995    453       C  
ATOM   1106  CG2 THR B  22     -38.966  19.055 -16.371  1.00 79.01           C  
ANISOU 1106  CG2 THR B  22    11198  11134   7689  -2998   1141    257       C  
ATOM   1107  OG1 THR B  22     -38.483  21.410 -16.500  1.00 68.70           O  
ANISOU 1107  OG1 THR B  22     9759   9968   6376  -3010    987    559       O  
ATOM   1108  N   CYS B  23     -41.031  18.632 -14.094  1.00 57.28           N  
ANISOU 1108  N   CYS B  23     8475   8237   5052  -2986    783    244       N  
ATOM   1109  CA  CYS B  23     -41.338  17.364 -13.441  1.00 66.50           C  
ANISOU 1109  CA  CYS B  23     9693   9279   6294  -2972    797    118       C  
ATOM   1110  C   CYS B  23     -41.398  16.252 -14.483  1.00 72.32           C  
ANISOU 1110  C   CYS B  23    10542  10036   6900  -3023    952    -52       C  
ATOM   1111  O   CYS B  23     -42.097  16.374 -15.489  1.00 73.70           O  
ANISOU 1111  O   CYS B  23    10803  10343   6857  -3118    955    -94       O  
ATOM   1112  CB  CYS B  23     -42.668  17.448 -12.688  1.00 66.59           C  
ANISOU 1112  CB  CYS B  23     9732   9301   6267  -3016    620    124       C  
ATOM   1113  SG  CYS B  23     -42.834  16.250 -11.347  1.00215.26           S  
ANISOU 1113  SG  CYS B  23    28581  27947  25260  -2983    585     46       S  
ATOM   1114  N   SER B  24     -40.660  15.173 -14.242  1.00 71.38           N  
ANISOU 1114  N   SER B  24    10426   9777   6916  -2962   1073   -151       N  
ATOM   1115  CA  SER B  24     -40.615  14.058 -15.181  1.00 73.25           C  
ANISOU 1115  CA  SER B  24    10775  10009   7048  -2996   1231   -326       C  
ATOM   1116  C   SER B  24     -41.035  12.755 -14.513  1.00 66.89           C  
ANISOU 1116  C   SER B  24    10036   9062   6318  -2992   1202   -449       C  
ATOM   1117  O   SER B  24     -40.338  12.244 -13.634  1.00 69.19           O  
ANISOU 1117  O   SER B  24    10265   9190   6832  -2907   1213   -449       O  
ATOM   1118  CB  SER B  24     -39.216  13.919 -15.785  1.00 88.00           C  
ANISOU 1118  CB  SER B  24    12591  11846   9001  -2926   1443   -353       C  
ATOM   1119  OG  SER B  24     -38.240  13.713 -14.778  1.00100.27           O  
ANISOU 1119  OG  SER B  24    14025  13234  10838  -2811   1452   -303       O  
ATOM   1120  N   ALA B  25     -42.177  12.223 -14.939  1.00 62.73           N  
ANISOU 1120  N   ALA B  25     9636   8593   5606  -3092   1153   -545       N  
ATOM   1121  CA  ALA B  25     -42.737  11.015 -14.339  1.00 64.17           C  
ANISOU 1121  CA  ALA B  25     9893   8655   5834  -3111   1102   -654       C  
ATOM   1122  C   ALA B  25     -42.178   9.740 -14.970  1.00 72.58           C  
ANISOU 1122  C   ALA B  25    11049   9624   6904  -3091   1271   -829       C  
ATOM   1123  O   ALA B  25     -41.836   9.715 -16.156  1.00 74.06           O  
ANISOU 1123  O   ALA B  25    11296   9886   6957  -3111   1420   -901       O  
ATOM   1124  CB  ALA B  25     -44.258  11.030 -14.435  1.00 57.49           C  
ANISOU 1124  CB  ALA B  25     9131   7910   4804  -3230    957   -665       C  
ATOM   1125  N   SER B  26     -42.095   8.684 -14.166  1.00 70.43           N  
ANISOU 1125  N   SER B  26    10794   9181   6784  -3057   1244   -900       N  
ATOM   1126  CA  SER B  26     -41.568   7.402 -14.621  1.00 75.65           C  
ANISOU 1126  CA  SER B  26    11538   9719   7486  -3026   1385  -1073       C  
ATOM   1127  C   SER B  26     -42.499   6.724 -15.626  1.00 73.97           C  
ANISOU 1127  C   SER B  26    11505   9579   7020  -3139   1406  -1215       C  
ATOM   1128  O   SER B  26     -42.056   5.929 -16.462  1.00 68.05           O  
ANISOU 1128  O   SER B  26    10848   8785   6224  -3127   1564  -1365       O  
ATOM   1129  CB  SER B  26     -41.311   6.477 -13.428  1.00 76.01           C  
ANISOU 1129  CB  SER B  26    11559   9553   7767  -2972   1314  -1097       C  
ATOM   1130  OG  SER B  26     -42.496   6.254 -12.683  1.00 72.27           O  
ANISOU 1130  OG  SER B  26    11138   9081   7239  -3061   1128  -1073       O  
ATOM   1131  N   SER B  27     -43.788   7.042 -15.541  1.00 64.38           N  
ANISOU 1131  N   SER B  27    10341   8472   5648  -3250   1246  -1166       N  
ATOM   1132  CA  SER B  27     -44.778   6.497 -16.469  1.00 62.29           C  
ANISOU 1132  CA  SER B  27    10246   8282   5138  -3375   1231  -1275       C  
ATOM   1133  C   SER B  27     -45.781   7.558 -16.924  1.00 61.30           C  
ANISOU 1133  C   SER B  27    10125   8353   4813  -3479   1117  -1171       C  
ATOM   1134  O   SER B  27     -45.915   8.612 -16.298  1.00 54.73           O  
ANISOU 1134  O   SER B  27     9165   7582   4047  -3457   1017  -1020       O  
ATOM   1135  CB  SER B  27     -45.501   5.300 -15.845  1.00 65.88           C  
ANISOU 1135  CB  SER B  27    10787   8617   5627  -3423   1125  -1361       C  
ATOM   1136  OG  SER B  27     -45.735   5.510 -14.462  1.00 73.51           O  
ANISOU 1136  OG  SER B  27    11644   9524   6762  -3398    980  -1252       O  
TER    1137      SER B  27 
HETATM 1138  O   HOH B  28     -45.218  11.217  -2.842  1.00 45.37           O  
ATOM   1139  N   ARG B  29     -46.481   7.266 -18.015  1.00 67.78           N  
ANISOU 1139  N   ARG B  29    11097   9260   5395  -3595   1124  -1253       N  
ATOM   1140  CA  ARG B  29     -47.407   8.212 -18.638  1.00 70.67           C  
ANISOU 1140  CA  ARG B  29    11482   9804   5563  -3706   1016  -1163       C  
ATOM   1141  C   ARG B  29     -48.558   8.616 -17.715  1.00 67.94           C  
ANISOU 1141  C   ARG B  29    11058   9495   5258  -3752    799  -1055       C  
ATOM   1142  O   ARG B  29     -49.114   7.786 -16.995  1.00 72.09           O  
ANISOU 1142  O   ARG B  29    11608   9934   5849  -3772    720  -1100       O  
ATOM   1143  CB  ARG B  29     -47.951   7.623 -19.944  1.00 84.76           C  
ANISOU 1143  CB  ARG B  29    13471  11646   7090  -3835   1052  -1284       C  
ATOM   1144  CG  ARG B  29     -48.696   8.607 -20.835  1.00 94.01           C  
ANISOU 1144  CG  ARG B  29    14678  12995   8045  -3957    962  -1195       C  
ATOM   1145  CD  ARG B  29     -48.410   8.327 -22.304  1.00105.84           C  
ANISOU 1145  CD  ARG B  29    16359  14545   9310  -4038   1103  -1303       C  
ATOM   1146  NE  ARG B  29     -48.440   6.899 -22.607  1.00119.46           N  
ANISOU 1146  NE  ARG B  29    18252  16155  10982  -4064   1181  -1488       N  
ATOM   1147  CZ  ARG B  29     -49.496   6.262 -23.103  1.00128.04           C  
ANISOU 1147  CZ  ARG B  29    19503  17253  11894  -4203   1075  -1553       C  
ATOM   1148  NH1 ARG B  29     -50.613   6.928 -23.357  1.00132.11           N1+
ANISOU 1148  NH1 ARG B  29    20026  17891  12281  -4328    887  -1444       N1+
ATOM   1149  NH2 ARG B  29     -49.435   4.960 -23.347  1.00127.69           N  
ANISOU 1149  NH2 ARG B  29    19616  17090  11813  -4217   1148  -1724       N  
ATOM   1150  N   VAL B  30     -48.911   9.898 -17.751  1.00 65.93           N  
ANISOU 1150  N   VAL B  30    10712   9371   4967  -3769    708   -913       N  
ATOM   1151  CA  VAL B  30     -49.946  10.445 -16.877  1.00 70.26           C  
ANISOU 1151  CA  VAL B  30    11163   9962   5569  -3797    519   -806       C  
ATOM   1152  C   VAL B  30     -50.887  11.389 -17.632  1.00 70.43           C  
ANISOU 1152  C   VAL B  30    11189  10146   5423  -3900    399   -722       C  
ATOM   1153  O   VAL B  30     -50.467  12.085 -18.562  1.00 72.21           O  
ANISOU 1153  O   VAL B  30    11437  10459   5541  -3917    452   -686       O  
ATOM   1154  CB  VAL B  30     -49.314  11.186 -15.669  1.00 77.89           C  
ANISOU 1154  CB  VAL B  30    11961  10879   6756  -3672    502   -693       C  
ATOM   1155  CG1 VAL B  30     -50.230  12.285 -15.162  1.00 73.17           C  
ANISOU 1155  CG1 VAL B  30    11256  10379   6167  -3695    336   -559       C  
ATOM   1156  CG2 VAL B  30     -48.969  10.198 -14.560  1.00 78.21           C  
ANISOU 1156  CG2 VAL B  30    11990  10752   6974  -3610    522   -751       C  
ATOM   1157  N   GLY B  31     -52.158  11.408 -17.231  1.00 60.00           N  
ANISOU 1157  N   GLY B  31     9844   8865   4087  -3975    235   -687       N  
ATOM   1158  CA  GLY B  31     -53.160  12.231 -17.889  1.00 58.01           C  
ANISOU 1158  CA  GLY B  31     9587   8753   3703  -4077     97   -606       C  
ATOM   1159  C   GLY B  31     -53.075  13.715 -17.564  1.00 65.26           C  
ANISOU 1159  C   GLY B  31    10352   9747   4699  -4015     24   -454       C  
ATOM   1160  O   GLY B  31     -53.158  14.557 -18.464  1.00 61.92           O  
ANISOU 1160  O   GLY B  31     9941   9426   4159  -4067    -17   -388       O  
ATOM   1161  N   TYR B  32     -52.915  14.034 -16.279  1.00 61.93           N  
ANISOU 1161  N   TYR B  32     9795   9268   4469  -3912      0   -398       N  
ATOM   1162  CA  TYR B  32     -52.831  15.421 -15.824  1.00 56.65           C  
ANISOU 1162  CA  TYR B  32     8981   8651   3891  -3843    -75   -259       C  
ATOM   1163  C   TYR B  32     -51.744  15.577 -14.771  1.00 59.30           C  
ANISOU 1163  C   TYR B  32     9233   8884   4413  -3705      6   -228       C  
ATOM   1164  O   TYR B  32     -51.528  14.680 -13.959  1.00 66.15           O  
ANISOU 1164  O   TYR B  32    10113   9640   5380  -3669     54   -294       O  
ATOM   1165  CB  TYR B  32     -54.159  15.875 -15.212  1.00 58.41           C  
ANISOU 1165  CB  TYR B  32     9111   8926   4158  -3879   -244   -199       C  
ATOM   1166  CG  TYR B  32     -55.382  15.629 -16.070  1.00 65.04           C  
ANISOU 1166  CG  TYR B  32    10015   9850   4847  -4022   -352   -221       C  
ATOM   1167  CD1 TYR B  32     -55.859  16.609 -16.932  1.00 69.64           C  
ANISOU 1167  CD1 TYR B  32    10580  10542   5337  -4083   -462   -135       C  
ATOM   1168  CD2 TYR B  32     -56.068  14.422 -16.008  1.00 68.50           C  
ANISOU 1168  CD2 TYR B  32    10532  10252   5243  -4103   -361   -318       C  
ATOM   1169  CE1 TYR B  32     -56.976  16.390 -17.713  1.00 78.85           C  
ANISOU 1169  CE1 TYR B  32    11806  11776   6377  -4221   -579   -144       C  
ATOM   1170  CE2 TYR B  32     -57.187  14.194 -16.786  1.00 75.13           C  
ANISOU 1170  CE2 TYR B  32    11432  11163   5952  -4241   -474   -328       C  
ATOM   1171  CZ  TYR B  32     -57.636  15.181 -17.636  1.00 86.30           C  
ANISOU 1171  CZ  TYR B  32    12825  12682   7281  -4300   -584   -240       C  
ATOM   1172  OH  TYR B  32     -58.751  14.959 -18.412  1.00 94.61           O  
ANISOU 1172  OH  TYR B  32    13937  13796   8213  -4445   -713   -239       O  
ATOM   1173  N   MET B  33     -51.066  16.720 -14.777  1.00 60.09           N  
ANISOU 1173  N   MET B  33     9252   9015   4563  -3635      5   -120       N  
ATOM   1174  CA  MET B  33     -50.111  17.042 -13.718  1.00 51.60           C  
ANISOU 1174  CA  MET B  33     8088   7845   3674  -3510     47    -65       C  
ATOM   1175  C   MET B  33     -50.624  18.232 -12.905  1.00 47.28           C  
ANISOU 1175  C   MET B  33     7419   7330   3216  -3468    -93     56       C  
ATOM   1176  O   MET B  33     -51.170  19.185 -13.461  1.00 46.38           O  
ANISOU 1176  O   MET B  33     7272   7322   3030  -3504   -191    129       O  
ATOM   1177  CB  MET B  33     -48.721  17.337 -14.296  1.00 45.93           C  
ANISOU 1177  CB  MET B  33     7373   7114   2965  -3453    175    -37       C  
ATOM   1178  CG  MET B  33     -47.613  17.390 -13.253  1.00 50.78           C  
ANISOU 1178  CG  MET B  33     7910   7602   3782  -3331    231      6       C  
ATOM   1179  SD  MET B  33     -47.452  15.844 -12.322  1.00 62.39           S  
ANISOU 1179  SD  MET B  33     9427   8906   5372  -3306    295   -117       S  
ATOM   1180  CE  MET B  33     -47.077  14.703 -13.654  1.00180.80           C  
ANISOU 1180  CE  MET B  33    24557  23905  20232  -3360    456   -267       C  
ATOM   1181  N   HIS B  34     -50.456  18.165 -11.588  1.00 52.79           N  
ANISOU 1181  N   HIS B  34     8058   7930   4071  -3395   -106     73       N  
ATOM   1182  CA  HIS B  34     -50.967  19.198 -10.696  1.00 43.73           C  
ANISOU 1182  CA  HIS B  34     6808   6798   3011  -3352   -226    168       C  
ATOM   1183  C   HIS B  34     -49.815  19.757  -9.876  1.00 45.38           C  
ANISOU 1183  C   HIS B  34     6962   6911   3368  -3242   -199    249       C  
ATOM   1184  O   HIS B  34     -48.833  19.055  -9.633  1.00 49.23           O  
ANISOU 1184  O   HIS B  34     7483   7296   3927  -3204    -99    216       O  
ATOM   1185  CB  HIS B  34     -52.052  18.618  -9.783  1.00 32.95           C  
ANISOU 1185  CB  HIS B  34     5431   5408   1679  -3389   -281    112       C  
ATOM   1186  CG  HIS B  34     -53.073  17.798 -10.512  1.00 44.82           C  
ANISOU 1186  CG  HIS B  34     6998   6979   3053  -3504   -297     24       C  
ATOM   1187  CD2 HIS B  34     -53.198  17.483 -11.819  1.00 52.23           C  
ANISOU 1187  CD2 HIS B  34     8015   7986   3843  -3581   -277    -17       C  
ATOM   1188  ND1 HIS B  34     -54.139  17.201  -9.872  1.00 58.49           N  
ANISOU 1188  ND1 HIS B  34     8721   8707   4795  -3560   -346    -26       N  
ATOM   1189  CE1 HIS B  34     -54.867  16.543 -10.756  1.00 58.94           C  
ANISOU 1189  CE1 HIS B  34     8844   8825   4727  -3665   -363    -91       C  
ATOM   1190  NE2 HIS B  34     -54.320  16.700 -11.948  1.00 58.39           N  
ANISOU 1190  NE2 HIS B  34     8836   8797   4553  -3681   -324    -89       N  
ATOM   1191  N   TRP B  35     -49.935  21.014  -9.453  1.00 45.55           N  
ANISOU 1191  N   TRP B  35     6901   6960   3444  -3192   -298    357       N  
ATOM   1192  CA  TRP B  35     -48.844  21.688  -8.753  1.00 37.60           C  
ANISOU 1192  CA  TRP B  35     5849   5867   2570  -3096   -295    453       C  
ATOM   1193  C   TRP B  35     -49.281  22.348  -7.450  1.00 48.85           C  
ANISOU 1193  C   TRP B  35     7218   7244   4099  -3047   -393    506       C  
ATOM   1194  O   TRP B  35     -50.349  22.958  -7.370  1.00 53.59           O  
ANISOU 1194  O   TRP B  35     7775   7918   4668  -3065   -488    517       O  
ATOM   1195  CB  TRP B  35     -48.201  22.727  -9.662  1.00 38.81           C  
ANISOU 1195  CB  TRP B  35     5972   6091   2683  -3077   -309    553       C  
ATOM   1196  CG  TRP B  35     -47.525  22.140 -10.858  1.00 51.41           C  
ANISOU 1196  CG  TRP B  35     7627   7722   4184  -3117   -185    507       C  
ATOM   1197  CD1 TRP B  35     -48.086  21.890 -12.075  1.00 54.11           C  
ANISOU 1197  CD1 TRP B  35     8028   8174   4358  -3210   -170    452       C  
ATOM   1198  CD2 TRP B  35     -46.154  21.731 -10.955  1.00 52.99           C  
ANISOU 1198  CD2 TRP B  35     7835   7844   4453  -3069    -55    508       C  
ATOM   1199  CE2 TRP B  35     -45.956  21.240 -12.259  1.00 50.56           C  
ANISOU 1199  CE2 TRP B  35     7594   7611   4008  -3131     53    442       C  
ATOM   1200  CE3 TRP B  35     -45.077  21.732 -10.065  1.00 50.95           C  
ANISOU 1200  CE3 TRP B  35     7535   7456   4367  -2982    -21    561       C  
ATOM   1201  NE1 TRP B  35     -47.149  21.347 -12.924  1.00 57.97           N  
ANISOU 1201  NE1 TRP B  35     8572   8662   4793  -3222    -25    410       N  
ATOM   1202  CZ2 TRP B  35     -44.727  20.756 -12.696  1.00 50.02           C  
ANISOU 1202  CZ2 TRP B  35     7538   7495   3972  -3100    209    417       C  
ATOM   1203  CZ3 TRP B  35     -43.859  21.251 -10.499  1.00 54.48           C  
ANISOU 1203  CZ3 TRP B  35     7984   7853   4861  -2952    119    548       C  
ATOM   1204  CH2 TRP B  35     -43.693  20.770 -11.804  1.00 53.78           C  
ANISOU 1204  CH2 TRP B  35     7950   7845   4637  -3006    241    472       C  
ATOM   1205  N   TYR B  36     -48.433  22.226  -6.434  1.00 46.89           N  
ANISOU 1205  N   TYR B  36     6973   6864   3980  -2986   -369    537       N  
ATOM   1206  CA  TYR B  36     -48.722  22.759  -5.113  1.00 40.45           C  
ANISOU 1206  CA  TYR B  36     6131   5983   3257  -2946   -448    580       C  
ATOM   1207  C   TYR B  36     -47.637  23.730  -4.681  1.00 43.29           C  
ANISOU 1207  C   TYR B  36     6461   6267   3721  -2863   -488    706       C  
ATOM   1208  O   TYR B  36     -46.450  23.470  -4.862  1.00 55.35           O  
ANISOU 1208  O   TYR B  36     7998   7724   5308  -2834   -426    741       O  
ATOM   1209  CB  TYR B  36     -48.828  21.622  -4.090  1.00 36.80           C  
ANISOU 1209  CB  TYR B  36     5723   5412   2848  -2974   -406    502       C  
ATOM   1210  CG  TYR B  36     -50.097  20.821  -4.207  1.00 34.84           C  
ANISOU 1210  CG  TYR B  36     5495   5233   2510  -3059   -398    393       C  
ATOM   1211  CD1 TYR B  36     -51.219  21.157  -3.464  1.00 35.39           C  
ANISOU 1211  CD1 TYR B  36     5532   5339   2576  -3079   -461    379       C  
ATOM   1212  CD2 TYR B  36     -50.181  19.738  -5.070  1.00 41.07           C  
ANISOU 1212  CD2 TYR B  36     6335   6049   3219  -3121   -327    303       C  
ATOM   1213  CE1 TYR B  36     -52.387  20.436  -3.574  1.00 43.62           C  
ANISOU 1213  CE1 TYR B  36     6580   6449   3545  -3162   -456    289       C  
ATOM   1214  CE2 TYR B  36     -51.350  19.009  -5.188  1.00 36.30           C  
ANISOU 1214  CE2 TYR B  36     5753   5506   2534  -3208   -333    212       C  
ATOM   1215  CZ  TYR B  36     -52.448  19.364  -4.439  1.00 43.68           C  
ANISOU 1215  CZ  TYR B  36     6642   6482   3475  -3230   -400    211       C  
ATOM   1216  OH  TYR B  36     -53.614  18.643  -4.552  1.00 54.81           O  
ANISOU 1216  OH  TYR B  36     8059   7954   4813  -3321   -408    131       O  
ATOM   1217  N   GLN B  37     -48.049  24.852  -4.110  1.00 40.00           N  
ANISOU 1217  N   GLN B  37     6003   5860   3334  -2824   -593    774       N  
ATOM   1218  CA  GLN B  37     -47.108  25.796  -3.532  1.00 41.61           C  
ANISOU 1218  CA  GLN B  37     6191   5978   3640  -2750   -652    897       C  
ATOM   1219  C   GLN B  37     -47.182  25.632  -2.033  1.00 33.51           C  
ANISOU 1219  C   GLN B  37     5206   4828   2700  -2735   -679    889       C  
ATOM   1220  O   GLN B  37     -48.264  25.464  -1.478  1.00 44.30           O  
ANISOU 1220  O   GLN B  37     6579   6219   4032  -2764   -693    817       O  
ATOM   1221  CB  GLN B  37     -47.463  27.228  -3.936  1.00 29.83           C  
ANISOU 1221  CB  GLN B  37     4642   4569   2122  -2717   -763    983       C  
ATOM   1222  CG  GLN B  37     -46.613  28.300  -3.284  1.00 32.81           C  
ANISOU 1222  CG  GLN B  37     5010   4856   2601  -2644   -848   1114       C  
ATOM   1223  CD  GLN B  37     -47.100  29.701  -3.620  1.00 47.98           C  
ANISOU 1223  CD  GLN B  37     6879   6850   4500  -2612   -975   1189       C  
ATOM   1224  NE2 GLN B  37     -46.181  30.567  -4.039  1.00 39.15           N  
ANISOU 1224  NE2 GLN B  37     5740   5723   3412  -2580  -1031   1316       N  
ATOM   1225  OE1 GLN B  37     -48.292  29.997  -3.513  1.00 48.64           O  
ANISOU 1225  OE1 GLN B  37     6937   6995   4548  -2619  -1027   1135       O  
ATOM   1226  N   GLN B  38     -46.032  25.657  -1.376  1.00 35.44           N  
ANISOU 1226  N   GLN B  38     5476   4935   3053  -2697   -685    965       N  
ATOM   1227  CA  GLN B  38     -46.014  25.570   0.075  1.00 41.55           C  
ANISOU 1227  CA  GLN B  38     6308   5578   3901  -2694   -725    972       C  
ATOM   1228  C   GLN B  38     -45.112  26.614   0.699  1.00 42.20           C  
ANISOU 1228  C   GLN B  38     6396   5558   4081  -2632   -817   1110       C  
ATOM   1229  O   GLN B  38     -43.936  26.719   0.357  1.00 49.12           O  
ANISOU 1229  O   GLN B  38     7253   6380   5030  -2602   -813   1199       O  
ATOM   1230  CB  GLN B  38     -45.589  24.182   0.543  1.00 42.04           C  
ANISOU 1230  CB  GLN B  38     6431   5532   4011  -2740   -653    912       C  
ATOM   1231  CG  GLN B  38     -45.499  24.092   2.047  1.00 40.45           C  
ANISOU 1231  CG  GLN B  38     6306   5186   3879  -2754   -705    932       C  
ATOM   1232  CD  GLN B  38     -45.155  22.704   2.526  1.00 45.12           C  
ANISOU 1232  CD  GLN B  38     6960   5664   4518  -2812   -655    875       C  
ATOM   1233  NE2 GLN B  38     -45.776  22.291   3.622  1.00 37.58           N  
ANISOU 1233  NE2 GLN B  38     6079   4652   3546  -2872   -674    827       N  
ATOM   1234  OE1 GLN B  38     -44.336  22.010   1.922  1.00 48.95           O  
ANISOU 1234  OE1 GLN B  38     7431   6109   5058  -2804   -598    873       O  
ATOM   1235  N   LYS B  39     -45.683  27.388   1.613  1.00 50.40           N  
ANISOU 1235  N   LYS B  39     7460   6569   5119  -2613   -898   1125       N  
ATOM   1236  CA  LYS B  39     -44.925  28.339   2.405  1.00 52.99           C  
ANISOU 1236  CA  LYS B  39     7822   6779   5533  -2564   -999   1247       C  
ATOM   1237  C   LYS B  39     -44.434  27.617   3.652  1.00 53.33           C  
ANISOU 1237  C   LYS B  39     7961   6654   5648  -2600   -999   1248       C  
ATOM   1238  O   LYS B  39     -44.955  26.560   3.999  1.00 59.20           O  
ANISOU 1238  O   LYS B  39     8745   7391   6359  -2662   -932   1145       O  
ATOM   1239  CB  LYS B  39     -45.814  29.520   2.788  1.00 56.27           C  
ANISOU 1239  CB  LYS B  39     8231   7239   5911  -2526  -1084   1250       C  
ATOM   1240  CG  LYS B  39     -46.234  30.385   1.614  1.00 54.55           C  
ANISOU 1240  CG  LYS B  39     7920   7165   5641  -2491  -1121   1273       C  
ATOM   1241  CD  LYS B  39     -45.095  31.279   1.173  1.00 62.61           C  
ANISOU 1241  CD  LYS B  39     8917   8150   6721  -2444  -1200   1425       C  
ATOM   1242  CE  LYS B  39     -45.575  32.343   0.200  1.00 66.33           C  
ANISOU 1242  CE  LYS B  39     9314   8747   7141  -2415  -1274   1463       C  
ATOM   1243  NZ  LYS B  39     -44.516  33.357  -0.052  1.00 64.61           N1+
ANISOU 1243  NZ  LYS B  39     9083   8485   6983  -2374  -1373   1623       N1+
ATOM   1244  N   PRO B  40     -43.432  28.183   4.334  1.00 51.61           N  
ANISOU 1244  N   PRO B  40     7786   6294   5527  -2571  -1087   1373       N  
ATOM   1245  CA  PRO B  40     -42.856  27.543   5.524  1.00 58.89           C  
ANISOU 1245  CA  PRO B  40     8810   7038   6527  -2615  -1112   1396       C  
ATOM   1246  C   PRO B  40     -43.875  27.366   6.647  1.00 57.44           C  
ANISOU 1246  C   PRO B  40     8722   6831   6272  -2669  -1113   1305       C  
ATOM   1247  O   PRO B  40     -44.587  28.309   6.983  1.00 54.71           O  
ANISOU 1247  O   PRO B  40     8388   6529   5870  -2640  -1155   1294       O  
ATOM   1248  CB  PRO B  40     -41.769  28.532   5.963  1.00 60.56           C  
ANISOU 1248  CB  PRO B  40     9046   7125   6841  -2570  -1234   1560       C  
ATOM   1249  CG  PRO B  40     -41.492  29.369   4.753  1.00 57.34           C  
ANISOU 1249  CG  PRO B  40     8526   6832   6428  -2507  -1243   1626       C  
ATOM   1250  CD  PRO B  40     -42.789  29.470   4.030  1.00 47.40           C  
ANISOU 1250  CD  PRO B  40     7216   5756   5039  -2505  -1184   1508       C  
ATOM   1251  N   GLY B  41     -43.938  26.167   7.220  1.00 58.37           N  
ANISOU 1251  N   GLY B  41     8906   6878   6394  -2747  -1067   1241       N  
ATOM   1252  CA  GLY B  41     -44.846  25.892   8.319  1.00 59.66           C  
ANISOU 1252  CA  GLY B  41     9167   7017   6485  -2817  -1058   1158       C  
ATOM   1253  C   GLY B  41     -46.310  26.082   7.964  1.00 70.92           C  
ANISOU 1253  C   GLY B  41    10536   8622   7790  -2817   -988   1037       C  
ATOM   1254  O   GLY B  41     -47.169  26.155   8.843  1.00 74.85           O  
ANISOU 1254  O   GLY B  41    11094   9123   8221  -2859   -975    971       O  
ATOM   1255  N   LYS B  42     -46.597  26.167   6.670  1.00 68.76           N  
ANISOU 1255  N   LYS B  42    10143   8494   7488  -2774   -945   1009       N  
ATOM   1256  CA  LYS B  42     -47.967  26.301   6.196  1.00 58.86           C  
ANISOU 1256  CA  LYS B  42     8818   7409   6138  -2777   -892    904       C  
ATOM   1257  C   LYS B  42     -48.375  25.064   5.413  1.00 56.13           C  
ANISOU 1257  C   LYS B  42     8433   7149   5746  -2836   -801    811       C  
ATOM   1258  O   LYS B  42     -47.529  24.274   4.998  1.00 60.00           O  
ANISOU 1258  O   LYS B  42     8934   7583   6282  -2852   -776    830       O  
ATOM   1259  CB  LYS B  42     -48.120  27.540   5.315  1.00 64.88           C  
ANISOU 1259  CB  LYS B  42     9482   8273   6894  -2688   -942    952       C  
ATOM   1260  CG  LYS B  42     -48.486  28.812   6.059  1.00 70.71           C  
ANISOU 1260  CG  LYS B  42    10242   8986   7637  -2633  -1017    981       C  
ATOM   1261  CD  LYS B  42     -48.790  29.920   5.068  1.00 86.50           C  
ANISOU 1261  CD  LYS B  42    12135  11099   9632  -2556  -1074   1017       C  
ATOM   1262  CE  LYS B  42     -49.490  31.099   5.721  1.00 97.37           C  
ANISOU 1262  CE  LYS B  42    13515  12473  11010  -2498  -1135   1007       C  
ATOM   1263  NZ  LYS B  42     -49.837  32.136   4.704  1.00 97.55           N1+
ANISOU 1263  NZ  LYS B  42    13429  12601  11037  -2428  -1206   1042       N1+
ATOM   1264  N   ALA B  43     -49.677  24.896   5.217  1.00 51.94           N  
ANISOU 1264  N   ALA B  43     7856   6748   5132  -2870   -754    709       N  
ATOM   1265  CA  ALA B  43     -50.180  23.780   4.434  1.00 46.72           C  
ANISOU 1265  CA  ALA B  43     7161   6173   4416  -2932   -680    620       C  
ATOM   1266  C   ALA B  43     -50.075  24.131   2.966  1.00 47.64           C  
ANISOU 1266  C   ALA B  43     7187   6403   4512  -2885   -681    641       C  
ATOM   1267  O   ALA B  43     -50.213  25.297   2.597  1.00 51.39           O  
ANISOU 1267  O   ALA B  43     7601   6937   4988  -2818   -737    693       O  
ATOM   1268  CB  ALA B  43     -51.623  23.470   4.805  1.00 46.04           C  
ANISOU 1268  CB  ALA B  43     7056   6183   4256  -2996   -637    515       C  
ATOM   1269  N   PRO B  44     -49.821  23.121   2.123  1.00 44.77           N  
ANISOU 1269  N   PRO B  44     6824   6062   4125  -2924   -623    600       N  
ATOM   1270  CA  PRO B  44     -49.698  23.317   0.674  1.00 38.00           C  
ANISOU 1270  CA  PRO B  44     5901   5311   3226  -2899   -611    610       C  
ATOM   1271  C   PRO B  44     -50.980  23.882   0.064  1.00 46.26           C  
ANISOU 1271  C   PRO B  44     6870   6515   4193  -2907   -637    571       C  
ATOM   1272  O   PRO B  44     -52.087  23.479   0.438  1.00 54.34           O  
ANISOU 1272  O   PRO B  44     7883   7588   5175  -2962   -620    491       O  
ATOM   1273  CB  PRO B  44     -49.456  21.899   0.147  1.00 32.33           C  
ANISOU 1273  CB  PRO B  44     5224   4577   2483  -2961   -529    535       C  
ATOM   1274  CG  PRO B  44     -48.895  21.157   1.301  1.00 40.25           C  
ANISOU 1274  CG  PRO B  44     6308   5422   3563  -2988   -521    534       C  
ATOM   1275  CD  PRO B  44     -49.569  21.725   2.515  1.00 45.34           C  
ANISOU 1275  CD  PRO B  44     6970   6046   4209  -2998   -570    542       C  
ATOM   1276  N   LYS B  45     -50.820  24.816  -0.864  1.00 40.92           N  
ANISOU 1276  N   LYS B  45     6133   5913   3501  -2858   -684    635       N  
ATOM   1277  CA  LYS B  45     -51.946  25.382  -1.584  1.00 44.33           C  
ANISOU 1277  CA  LYS B  45     6487   6486   3872  -2868   -730    613       C  
ATOM   1278  C   LYS B  45     -51.886  24.916  -3.031  1.00 42.92           C  
ANISOU 1278  C   LYS B  45     6302   6398   3608  -2914   -701    594       C  
ATOM   1279  O   LYS B  45     -50.807  24.787  -3.599  1.00 47.73           O  
ANISOU 1279  O   LYS B  45     6941   6976   4218  -2899   -666    637       O  
ATOM   1280  CB  LYS B  45     -51.894  26.910  -1.526  1.00 51.92           C  
ANISOU 1280  CB  LYS B  45     7393   7456   4877  -2785   -832    706       C  
ATOM   1281  CG  LYS B  45     -53.050  27.595  -2.245  1.00 65.07           C  
ANISOU 1281  CG  LYS B  45     8968   9253   6504  -2789   -902    694       C  
ATOM   1282  CD  LYS B  45     -52.903  29.109  -2.249  1.00 56.75           C  
ANISOU 1282  CD  LYS B  45     7866   8194   5504  -2704  -1017    791       C  
ATOM   1283  CE  LYS B  45     -51.965  29.572  -3.343  1.00 61.80           C  
ANISOU 1283  CE  LYS B  45     8508   8858   6117  -2695  -1057    889       C  
ATOM   1284  NZ  LYS B  45     -51.869  31.060  -3.388  1.00 72.86           N1+
ANISOU 1284  NZ  LYS B  45     9862  10253   7567  -2622  -1188    991       N1+
ATOM   1285  N   LEU B  46     -53.047  24.669  -3.625  1.00 36.57           N  
ANISOU 1285  N   LEU B  46     5459   5705   2729  -2974   -713    530       N  
ATOM   1286  CA  LEU B  46     -53.114  24.246  -5.016  1.00 41.53           C  
ANISOU 1286  CA  LEU B  46     6099   6423   3258  -3033   -696    509       C  
ATOM   1287  C   LEU B  46     -52.875  25.429  -5.949  1.00 45.66           C  
ANISOU 1287  C   LEU B  46     6578   7014   3759  -3000   -778    604       C  
ATOM   1288  O   LEU B  46     -53.614  26.408  -5.907  1.00 51.58           O  
ANISOU 1288  O   LEU B  46     7253   7813   4531  -2975   -879    641       O  
ATOM   1289  CB  LEU B  46     -54.478  23.622  -5.304  1.00 40.17           C  
ANISOU 1289  CB  LEU B  46     5905   6339   3020  -3120   -705    422       C  
ATOM   1290  CG  LEU B  46     -54.650  22.932  -6.654  1.00 44.72           C  
ANISOU 1290  CG  LEU B  46     6523   6994   3475  -3205   -685    380       C  
ATOM   1291  CD1 LEU B  46     -53.777  21.691  -6.727  1.00 52.52           C  
ANISOU 1291  CD1 LEU B  46     7613   7905   4439  -3233   -569    321       C  
ATOM   1292  CD2 LEU B  46     -56.108  22.579  -6.883  1.00 42.14           C  
ANISOU 1292  CD2 LEU B  46     6154   6756   3101  -3288   -731    321       C  
ATOM   1293  N   LEU B  47     -51.840  25.332  -6.784  1.00 45.09           N  
ANISOU 1293  N   LEU B  47     6548   6940   3646  -3003   -733    642       N  
ATOM   1294  CA  LEU B  47     -51.500  26.389  -7.743  1.00 44.80           C  
ANISOU 1294  CA  LEU B  47     6483   6969   3571  -2991   -804    739       C  
ATOM   1295  C   LEU B  47     -52.078  26.126  -9.131  1.00 50.39           C  
ANISOU 1295  C   LEU B  47     7210   7796   4140  -3086   -816    709       C  
ATOM   1296  O   LEU B  47     -52.850  26.925  -9.665  1.00 48.72           O  
ANISOU 1296  O   LEU B  47     6948   7666   3897  -3109   -934    751       O  
ATOM   1297  CB  LEU B  47     -49.986  26.516  -7.889  1.00 35.87           C  
ANISOU 1297  CB  LEU B  47     5381   5774   2472  -2947   -743    810       C  
ATOM   1298  CG  LEU B  47     -49.234  27.625  -7.173  1.00 44.61           C  
ANISOU 1298  CG  LEU B  47     6452   6806   3690  -2857   -812    929       C  
ATOM   1299  CD1 LEU B  47     -47.949  27.883  -7.931  1.00 40.49           C  
ANISOU 1299  CD1 LEU B  47     5942   6285   3157  -2849   -769   1013       C  
ATOM   1300  CD2 LEU B  47     -50.066  28.889  -7.097  1.00 51.26           C  
ANISOU 1300  CD2 LEU B  47     7230   7699   4548  -2830   -962    988       C  
ATOM   1301  N   ILE B  48     -51.660  25.011  -9.720  1.00 42.27           N  
ANISOU 1301  N   ILE B  48     6260   6767   3032  -3143   -700    637       N  
ATOM   1302  CA  ILE B  48     -52.108  24.613 -11.043  1.00 42.97           C  
ANISOU 1302  CA  ILE B  48     6399   6956   2971  -3246   -696    597       C  
ATOM   1303  C   ILE B  48     -52.746  23.231 -10.970  1.00 47.55           C  
ANISOU 1303  C   ILE B  48     7037   7527   3503  -3314   -628    467       C  
ATOM   1304  O   ILE B  48     -52.219  22.331 -10.315  1.00 45.89           O  
ANISOU 1304  O   ILE B  48     6866   7225   3346  -3289   -526    405       O  
ATOM   1305  CB  ILE B  48     -50.932  24.556 -12.041  1.00 44.62           C  
ANISOU 1305  CB  ILE B  48     6670   7180   3101  -3263   -606    624       C  
ATOM   1306  CG1 ILE B  48     -50.223  25.906 -12.116  1.00 48.80           C  
ANISOU 1306  CG1 ILE B  48     7145   7719   3679  -3204   -675    764       C  
ATOM   1307  CG2 ILE B  48     -51.421  24.143 -13.418  1.00 46.75           C  
ANISOU 1307  CG2 ILE B  48     7016   7552   3194  -3383   -601    577       C  
ATOM   1308  CD1 ILE B  48     -50.913  26.907 -13.008  1.00 51.28           C  
ANISOU 1308  CD1 ILE B  48     7435   8141   3909  -3262   -820    839       C  
ATOM   1309  N   TYR B  49     -53.885  23.069 -11.633  1.00 33.54           N  
ANISOU 1309  N   TYR B  49     5268   5840   1637  -3406   -699    434       N  
ATOM   1310  CA  TYR B  49     -54.522  21.767 -11.731  1.00 35.51           C  
ANISOU 1310  CA  TYR B  49     5581   6088   1823  -3488   -650    319       C  
ATOM   1311  C   TYR B  49     -54.822  21.458 -13.186  1.00 41.13           C  
ANISOU 1311  C   TYR B  49     6378   6886   2365  -3603   -665    294       C  
ATOM   1312  O   TYR B  49     -54.791  22.351 -14.031  1.00 43.94           O  
ANISOU 1312  O   TYR B  49     6725   7314   2658  -3627   -739    373       O  
ATOM   1313  CB  TYR B  49     -55.801  21.718 -10.897  1.00 40.16           C  
ANISOU 1313  CB  TYR B  49     6092   6689   2480  -3502   -729    295       C  
ATOM   1314  CG  TYR B  49     -56.904  22.617 -11.403  1.00 49.97           C  
ANISOU 1314  CG  TYR B  49     7251   8030   3706  -3540   -880    352       C  
ATOM   1315  CD1 TYR B  49     -57.936  22.109 -12.183  1.00 42.04           C  
ANISOU 1315  CD1 TYR B  49     6269   7097   2607  -3657   -942    314       C  
ATOM   1316  CD2 TYR B  49     -56.912  23.975 -11.103  1.00 56.43           C  
ANISOU 1316  CD2 TYR B  49     7970   8859   4613  -3460   -974    449       C  
ATOM   1317  CE1 TYR B  49     -58.947  22.926 -12.645  1.00 50.30           C  
ANISOU 1317  CE1 TYR B  49     7231   8223   3660  -3694  -1095    374       C  
ATOM   1318  CE2 TYR B  49     -57.917  24.801 -11.561  1.00 55.48           C  
ANISOU 1318  CE2 TYR B  49     7765   8815   4499  -3489  -1124    502       C  
ATOM   1319  CZ  TYR B  49     -58.932  24.272 -12.332  1.00 63.43           C  
ANISOU 1319  CZ  TYR B  49     8787   9892   5423  -3607  -1185    467       C  
ATOM   1320  OH  TYR B  49     -59.937  25.093 -12.794  1.00 71.17           O  
ANISOU 1320  OH  TYR B  49     9674  10939   6429  -3639  -1349    528       O  
ATOM   1321  N   ASP B  50     -55.106  20.191 -13.472  1.00 48.87           N  
ANISOU 1321  N   ASP B  50     7451   7853   3265  -3681   -601    187       N  
ATOM   1322  CA  ASP B  50     -55.351  19.744 -14.840  1.00 43.40           C  
ANISOU 1322  CA  ASP B  50     6869   7226   2393  -3801   -604    148       C  
ATOM   1323  C   ASP B  50     -54.250  20.193 -15.806  1.00 51.18           C  
ANISOU 1323  C   ASP B  50     7919   8238   3289  -3797   -535    187       C  
ATOM   1324  O   ASP B  50     -54.524  20.513 -16.964  1.00 67.30           O  
ANISOU 1324  O   ASP B  50    10020  10364   5188  -3892   -593    215       O  
ATOM   1325  CB  ASP B  50     -56.719  20.223 -15.332  1.00 48.15           C  
ANISOU 1325  CB  ASP B  50     7428   7922   2945  -3893   -775    191       C  
ATOM   1326  CG  ASP B  50     -57.869  19.486 -14.671  1.00 57.07           C  
ANISOU 1326  CG  ASP B  50     8520   9041   4125  -3935   -821    131       C  
ATOM   1327  OD1 ASP B  50     -57.635  18.797 -13.656  1.00 64.01           O  
ANISOU 1327  OD1 ASP B  50     9391   9840   5090  -3883   -734     72       O  
ATOM   1328  OD2 ASP B  50     -59.010  19.597 -15.167  1.00 62.52           O1-
ANISOU 1328  OD2 ASP B  50     9186   9799   4768  -4029   -950    150       O1-
ATOM   1329  N   THR B  51     -53.013  20.224 -15.315  1.00 42.22           N  
ANISOU 1329  N   THR B  51     6771   7030   2242  -3695   -416    195       N  
ATOM   1330  CA  THR B  51     -51.836  20.495 -16.143  1.00 40.89           C  
ANISOU 1330  CA  THR B  51     6655   6878   2004  -3685   -314    221       C  
ATOM   1331  C   THR B  51     -51.575  21.976 -16.439  1.00 52.57           C  
ANISOU 1331  C   THR B  51     8061   8422   3490  -3663   -407    366       C  
ATOM   1332  O   THR B  51     -50.424  22.427 -16.390  1.00 44.36           O  
ANISOU 1332  O   THR B  51     6997   7358   2501  -3594   -331    422       O  
ATOM   1333  CB  THR B  51     -51.862  19.700 -17.466  1.00 39.77           C  
ANISOU 1333  CB  THR B  51     6667   6784   1661  -3805   -239    132       C  
ATOM   1334  CG2 THR B  51     -50.634  20.017 -18.304  1.00 40.60           C  
ANISOU 1334  CG2 THR B  51     6819   6915   1692  -3797   -114    157       C  
ATOM   1335  OG1 THR B  51     -51.878  18.297 -17.179  1.00 60.00           O  
ANISOU 1335  OG1 THR B  51     9304   9265   4229  -3811   -138     -5       O  
ATOM   1336  N   SER B  52     -52.630  22.727 -16.746  1.00 60.32           N  
ANISOU 1336  N   SER B  52     9005   9483   4433  -3722   -580    431       N  
ATOM   1337  CA  SER B  52     -52.467  24.125 -17.149  1.00 57.78           C  
ANISOU 1337  CA  SER B  52     8626   9222   4106  -3718   -694    569       C  
ATOM   1338  C   SER B  52     -53.556  25.055 -16.619  1.00 54.95           C  
ANISOU 1338  C   SER B  52     8150   8883   3844  -3696   -892    645       C  
ATOM   1339  O   SER B  52     -53.568  26.243 -16.930  1.00 66.24           O  
ANISOU 1339  O   SER B  52     9531  10357   5282  -3695  -1016    761       O  
ATOM   1340  CB  SER B  52     -52.395  24.236 -18.675  1.00 49.95           C  
ANISOU 1340  CB  SER B  52     7747   8325   2906  -3851   -700    587       C  
ATOM   1341  OG  SER B  52     -53.510  23.605 -19.283  1.00 46.27           O  
ANISOU 1341  OG  SER B  52     7357   7902   2322  -3974   -768    521       O  
ATOM   1342  N   LYS B  53     -54.470  24.518 -15.823  1.00 50.04           N  
ANISOU 1342  N   LYS B  53     7483   8230   3301  -3682   -920    579       N  
ATOM   1343  CA  LYS B  53     -55.570  25.315 -15.293  1.00 56.93           C  
ANISOU 1343  CA  LYS B  53     8233   9121   4277  -3657  -1087    633       C  
ATOM   1344  C   LYS B  53     -55.156  26.055 -14.024  1.00 58.05           C  
ANISOU 1344  C   LYS B  53     8269   9190   4596  -3513  -1091    683       C  
ATOM   1345  O   LYS B  53     -54.547  25.475 -13.123  1.00 60.68           O  
ANISOU 1345  O   LYS B  53     8611   9442   5002  -3443   -970    632       O  
ATOM   1346  CB  LYS B  53     -56.787  24.432 -15.010  1.00 68.16           C  
ANISOU 1346  CB  LYS B  53     9644  10549   5704  -3715  -1111    543       C  
ATOM   1347  CG  LYS B  53     -57.446  23.847 -16.250  1.00 82.30           C  
ANISOU 1347  CG  LYS B  53    11532  12410   7327  -3870  -1159    509       C  
ATOM   1348  CD  LYS B  53     -58.484  24.793 -16.835  1.00 94.19           C  
ANISOU 1348  CD  LYS B  53    12968  13988   8833  -3932  -1369    599       C  
ATOM   1349  CE  LYS B  53     -59.224  24.149 -18.001  1.00101.54           C  
ANISOU 1349  CE  LYS B  53    14003  14977   9601  -4100  -1434    569       C  
ATOM   1350  NZ  LYS B  53     -59.778  22.809 -17.644  1.00103.67           N1+
ANISOU 1350  NZ  LYS B  53    14313  15220   9857  -4144  -1361    452       N1+
ATOM   1351  N   LEU B  54     -55.495  27.338 -13.960  1.00 53.00           N  
ANISOU 1351  N   LEU B  54     7539   8574   4027  -3474  -1242    784       N  
ATOM   1352  CA  LEU B  54     -55.182  28.162 -12.799  1.00 52.32           C  
ANISOU 1352  CA  LEU B  54     7361   8416   4100  -3342  -1267    836       C  
ATOM   1353  C   LEU B  54     -56.206  28.002 -11.686  1.00 49.89           C  
ANISOU 1353  C   LEU B  54     6967   8079   3912  -3296  -1291    775       C  
ATOM   1354  O   LEU B  54     -57.386  28.294 -11.874  1.00 49.37           O  
ANISOU 1354  O   LEU B  54     6828   8063   3866  -3332  -1407    776       O  
ATOM   1355  CB  LEU B  54     -55.111  29.635 -13.196  1.00 55.31           C  
ANISOU 1355  CB  LEU B  54     7685   8823   4509  -3317  -1426    967       C  
ATOM   1356  CG  LEU B  54     -53.792  30.114 -13.787  1.00 61.93           C  
ANISOU 1356  CG  LEU B  54     8581   9663   5287  -3315  -1392   1056       C  
ATOM   1357  CD1 LEU B  54     -53.922  31.557 -14.227  1.00 66.91           C  
ANISOU 1357  CD1 LEU B  54     9158  10324   5941  -3310  -1581   1189       C  
ATOM   1358  CD2 LEU B  54     -52.683  29.959 -12.759  1.00 64.15           C  
ANISOU 1358  CD2 LEU B  54     8864   9845   5666  -3208  -1270   1054       C  
ATOM   1359  N   ALA B  55     -55.750  27.550 -10.522  1.00 45.05           N  
ANISOU 1359  N   ALA B  55     6357   7379   3379  -3223  -1182    728       N  
ATOM   1360  CA  ALA B  55     -56.618  27.467  -9.358  1.00 48.04           C  
ANISOU 1360  CA  ALA B  55     6660   7727   3866  -3179  -1188    674       C  
ATOM   1361  C   ALA B  55     -57.113  28.864  -8.992  1.00 57.34           C  
ANISOU 1361  C   ALA B  55     7727   8906   5153  -3100  -1326    746       C  
ATOM   1362  O   ALA B  55     -56.520  29.867  -9.390  1.00 65.09           O  
ANISOU 1362  O   ALA B  55     8704   9885   6143  -3062  -1406    845       O  
ATOM   1363  CB  ALA B  55     -55.881  26.838  -8.192  1.00 49.70           C  
ANISOU 1363  CB  ALA B  55     6915   7834   4134  -3123  -1059    627       C  
ATOM   1364  N   SER B  56     -58.202  28.927  -8.234  1.00 60.01           N  
ANISOU 1364  N   SER B  56     7974   9248   5578  -3078  -1352    696       N  
ATOM   1365  CA  SER B  56     -58.798  30.206  -7.864  1.00 59.47           C  
ANISOU 1365  CA  SER B  56     7791   9175   5628  -2997  -1477    746       C  
ATOM   1366  C   SER B  56     -57.893  30.997  -6.925  1.00 58.95           C  
ANISOU 1366  C   SER B  56     7741   9014   5645  -2879  -1465    794       C  
ATOM   1367  O   SER B  56     -57.297  30.436  -6.002  1.00 46.86           O  
ANISOU 1367  O   SER B  56     6271   7410   4125  -2852  -1348    753       O  
ATOM   1368  CB  SER B  56     -60.175  30.000  -7.223  1.00 60.97           C  
ANISOU 1368  CB  SER B  56     7874   9393   5901  -2999  -1480    667       C  
ATOM   1369  OG  SER B  56     -60.063  29.387  -5.954  1.00 66.58           O  
ANISOU 1369  OG  SER B  56     8609  10043   6647  -2966  -1346    590       O  
ATOM   1370  N   GLY B  57     -57.794  32.301  -7.170  1.00 67.56           N  
ANISOU 1370  N   GLY B  57     8782  10095   6791  -2819  -1602    886       N  
ATOM   1371  CA  GLY B  57     -56.977  33.179  -6.352  1.00 72.97           C  
ANISOU 1371  CA  GLY B  57     9485  10686   7555  -2711  -1620    944       C  
ATOM   1372  C   GLY B  57     -55.500  33.091  -6.683  1.00 76.18           C  
ANISOU 1372  C   GLY B  57     9994  11055   7897  -2718  -1577   1019       C  
ATOM   1373  O   GLY B  57     -54.649  33.481  -5.880  1.00 81.21           O  
ANISOU 1373  O   GLY B  57    10669  11598   8590  -2644  -1559   1060       O  
ATOM   1374  N   VAL B  58     -55.191  32.576  -7.867  1.00 66.06           N  
ANISOU 1374  N   VAL B  58     8759   9844   6499  -2811  -1558   1038       N  
ATOM   1375  CA  VAL B  58     -53.805  32.409  -8.281  1.00 59.16           C  
ANISOU 1375  CA  VAL B  58     7969   8945   5564  -2824  -1495   1101       C  
ATOM   1376  C   VAL B  58     -53.473  33.312  -9.461  1.00 57.46           C  
ANISOU 1376  C   VAL B  58     7752   8790   5292  -2860  -1615   1217       C  
ATOM   1377  O   VAL B  58     -54.087  33.202 -10.521  1.00 76.00           O  
ANISOU 1377  O   VAL B  58    10096  11229   7552  -2949  -1669   1214       O  
ATOM   1378  CB  VAL B  58     -53.500  30.946  -8.650  1.00 47.61           C  
ANISOU 1378  CB  VAL B  58     6583   7504   4002  -2904  -1337   1016       C  
ATOM   1379  CG1 VAL B  58     -52.124  30.838  -9.293  1.00 40.99           C  
ANISOU 1379  CG1 VAL B  58     5815   6657   3104  -2922  -1270   1080       C  
ATOM   1380  CG2 VAL B  58     -53.595  30.061  -7.416  1.00 37.20           C  
ANISOU 1380  CG2 VAL B  58     5282   6108   2742  -2874  -1223    920       C  
ATOM   1381  N   PRO B  59     -52.493  34.207  -9.276  1.00 48.95           N  
ANISOU 1381  N   PRO B  59     6683   7656   4261  -2800  -1665   1326       N  
ATOM   1382  CA  PRO B  59     -52.100  35.202 -10.278  1.00 44.73           C  
ANISOU 1382  CA  PRO B  59     6147   7169   3681  -2833  -1794   1455       C  
ATOM   1383  C   PRO B  59     -51.809  34.556 -11.622  1.00 44.47           C  
ANISOU 1383  C   PRO B  59     6176   7233   3488  -2957  -1730   1456       C  
ATOM   1384  O   PRO B  59     -51.132  33.528 -11.669  1.00 56.26           O  
ANISOU 1384  O   PRO B  59     7730   8720   4925  -2982  -1560   1399       O  
ATOM   1385  CB  PRO B  59     -50.811  35.795  -9.694  1.00 41.03           C  
ANISOU 1385  CB  PRO B  59     5701   6609   3279  -2758  -1789   1553       C  
ATOM   1386  CG  PRO B  59     -50.921  35.580  -8.233  1.00 43.11           C  
ANISOU 1386  CG  PRO B  59     5957   6767   3657  -2664  -1736   1487       C  
ATOM   1387  CD  PRO B  59     -51.647  34.273  -8.072  1.00 54.86           C  
ANISOU 1387  CD  PRO B  59     7454   8286   5103  -2708  -1606   1341       C  
ATOM   1388  N   SER B  60     -52.318  35.151 -12.696  1.00 45.95           N  
ANISOU 1388  N   SER B  60     6354   7503   3603  -3035  -1867   1517       N  
ATOM   1389  CA  SER B  60     -52.088  34.643 -14.046  1.00 53.51           C  
ANISOU 1389  CA  SER B  60     7388   8556   4385  -3170  -1820   1522       C  
ATOM   1390  C   SER B  60     -50.592  34.608 -14.366  1.00 49.46           C  
ANISOU 1390  C   SER B  60     6935   8039   3818  -3179  -1707   1588       C  
ATOM   1391  O   SER B  60     -50.169  34.095 -15.401  1.00 38.29           O  
ANISOU 1391  O   SER B  60     5596   6697   2255  -3281  -1619   1581       O  
ATOM   1392  CB  SER B  60     -52.844  35.500 -15.059  1.00 58.78           C  
ANISOU 1392  CB  SER B  60     8038   9297   4998  -3255  -2024   1604       C  
ATOM   1393  OG  SER B  60     -52.964  36.833 -14.590  1.00 68.38           O  
ANISOU 1393  OG  SER B  60     9178  10461   6344  -3172  -2204   1704       O  
ATOM   1394  N   ARG B  61     -49.804  35.171 -13.458  1.00 52.13           N  
ANISOU 1394  N   ARG B  61     7240   8288   4279  -3072  -1710   1652       N  
ATOM   1395  CA  ARG B  61     -48.350  35.100 -13.501  1.00 51.81           C  
ANISOU 1395  CA  ARG B  61     7232   8220   4233  -3059  -1595   1715       C  
ATOM   1396  C   ARG B  61     -47.887  33.646 -13.635  1.00 54.84           C  
ANISOU 1396  C   ARG B  61     7673   8609   4554  -3090  -1367   1597       C  
ATOM   1397  O   ARG B  61     -46.893  33.362 -14.303  1.00 56.42           O  
ANISOU 1397  O   ARG B  61     7914   8842   4683  -3135  -1250   1624       O  
ATOM   1398  CB  ARG B  61     -47.799  35.727 -12.220  1.00 55.76           C  
ANISOU 1398  CB  ARG B  61     7687   8598   4901  -2932  -1638   1775       C  
ATOM   1399  CG  ARG B  61     -46.303  35.637 -12.011  1.00 67.88           C  
ANISOU 1399  CG  ARG B  61     9237  10078   6476  -2902  -1531   1845       C  
ATOM   1400  CD  ARG B  61     -46.000  35.878 -10.537  1.00 59.88           C  
ANISOU 1400  CD  ARG B  61     8200   8924   5629  -2782  -1555   1860       C  
ATOM   1401  NE  ARG B  61     -47.014  36.746  -9.947  1.00 60.83           N  
ANISOU 1401  NE  ARG B  61     8284   9013   5815  -2727  -1727   1865       N  
ATOM   1402  CZ  ARG B  61     -47.284  36.809  -8.649  1.00 58.54           C  
ANISOU 1402  CZ  ARG B  61     7984   8616   5641  -2636  -1746   1823       C  
ATOM   1403  NH1 ARG B  61     -46.616  36.050  -7.798  1.00 46.92           N1+
ANISOU 1403  NH1 ARG B  61     6543   7056   4229  -2598  -1620   1783       N1+
ATOM   1404  NH2 ARG B  61     -48.227  37.629  -8.203  1.00 64.41           N  
ANISOU 1404  NH2 ARG B  61     8691   9339   6442  -2585  -1891   1820       N  
ATOM   1405  N   PHE B  62     -48.623  32.733 -13.005  1.00 49.68           N  
ANISOU 1405  N   PHE B  62     7021   7923   3932  -3067  -1304   1464       N  
ATOM   1406  CA  PHE B  62     -48.339  31.300 -13.083  1.00 44.21           C  
ANISOU 1406  CA  PHE B  62     6386   7222   3188  -3096  -1107   1340       C  
ATOM   1407  C   PHE B  62     -48.992  30.658 -14.302  1.00 47.49           C  
ANISOU 1407  C   PHE B  62     6868   7747   3431  -3222  -1077   1267       C  
ATOM   1408  O   PHE B  62     -50.039  31.112 -14.770  1.00 53.63           O  
ANISOU 1408  O   PHE B  62     7633   8589   4156  -3279  -1219   1281       O  
ATOM   1409  CB  PHE B  62     -48.839  30.583 -11.827  1.00 31.87           C  
ANISOU 1409  CB  PHE B  62     4806   5571   1731  -3029  -1064   1237       C  
ATOM   1410  CG  PHE B  62     -48.125  30.979 -10.577  1.00 34.99           C  
ANISOU 1410  CG  PHE B  62     5167   5846   2284  -2918  -1069   1291       C  
ATOM   1411  CD1 PHE B  62     -48.525  32.096  -9.863  1.00 46.70           C  
ANISOU 1411  CD1 PHE B  62     6596   7290   3860  -2852  -1222   1362       C  
ATOM   1412  CD2 PHE B  62     -47.055  30.234 -10.108  1.00 35.45           C  
ANISOU 1412  CD2 PHE B  62     5251   5818   2400  -2883   -929   1271       C  
ATOM   1413  CE1 PHE B  62     -47.868  32.465  -8.703  1.00 44.83           C  
ANISOU 1413  CE1 PHE B  62     6346   6933   3754  -2759  -1235   1413       C  
ATOM   1414  CE2 PHE B  62     -46.394  30.600  -8.951  1.00 41.09           C  
ANISOU 1414  CE2 PHE B  62     5943   6411   3258  -2794   -952   1332       C  
ATOM   1415  CZ  PHE B  62     -46.802  31.716  -8.249  1.00 39.70           C  
ANISOU 1415  CZ  PHE B  62     5729   6200   3156  -2736  -1105   1403       C  
ATOM   1416  N   SER B  63     -48.378  29.588 -14.799  1.00 43.73           N  
ANISOU 1416  N   SER B  63     6463   7280   2872  -3266   -896   1187       N  
ATOM   1417  CA  SER B  63     -48.914  28.858 -15.943  1.00 48.72           C  
ANISOU 1417  CA  SER B  63     7183   8002   3326  -3391   -850   1105       C  
ATOM   1418  C   SER B  63     -48.362  27.438 -15.985  1.00 45.62           C  
ANISOU 1418  C   SER B  63     6861   7571   2900  -3396   -637    974       C  
ATOM   1419  O   SER B  63     -47.317  27.152 -15.397  1.00 35.58           O  
ANISOU 1419  O   SER B  63     5568   6218   1732  -3315   -519    973       O  
ATOM   1420  CB  SER B  63     -48.601  29.593 -17.252  1.00 55.15           C  
ANISOU 1420  CB  SER B  63     8041   8919   3994  -3491   -899   1200       C  
ATOM   1421  OG  SER B  63     -47.264  29.366 -17.663  1.00 57.08           O  
ANISOU 1421  OG  SER B  63     8320   9165   4203  -3491   -731   1216       O  
ATOM   1422  N   GLY B  64     -49.069  26.553 -16.683  1.00 47.28           N  
ANISOU 1422  N   GLY B  64     7156   7832   2976  -3494   -599    866       N  
ATOM   1423  CA  GLY B  64     -48.681  25.157 -16.751  1.00 48.66           C  
ANISOU 1423  CA  GLY B  64     7409   7964   3117  -3503   -412    728       C  
ATOM   1424  C   GLY B  64     -48.693  24.602 -18.159  1.00 58.18           C  
ANISOU 1424  C   GLY B  64     8742   9254   4110  -3631   -330    663       C  
ATOM   1425  O   GLY B  64     -49.395  25.115 -19.035  1.00 63.41           O  
ANISOU 1425  O   GLY B  64     9445  10011   4637  -3738   -449    707       O  
ATOM   1426  N   SER B  65     -47.920  23.543 -18.376  1.00 59.16           N  
ANISOU 1426  N   SER B  65     8935   9336   4206  -3624   -131    557       N  
ATOM   1427  CA  SER B  65     -47.804  22.950 -19.702  1.00 57.57           C  
ANISOU 1427  CA  SER B  65     8872   9206   3796  -3742    -22    478       C  
ATOM   1428  C   SER B  65     -47.115  21.593 -19.644  1.00 64.43           C  
ANISOU 1428  C   SER B  65     9805   9993   4681  -3705    194    329       C  
ATOM   1429  O   SER B  65     -46.249  21.365 -18.796  1.00 69.52           O  
ANISOU 1429  O   SER B  65    10375  10540   5501  -3586    286    325       O  
ATOM   1430  CB  SER B  65     -47.028  23.892 -20.626  1.00 57.69           C  
ANISOU 1430  CB  SER B  65     8897   9309   3713  -3789      0    586       C  
ATOM   1431  OG  SER B  65     -46.707  23.263 -21.852  1.00 67.25           O  
ANISOU 1431  OG  SER B  65    10250  10579   4722  -3896    149    499       O  
ATOM   1432  N   GLY B  66     -47.504  20.693 -20.544  1.00 62.77           N  
ANISOU 1432  N   GLY B  66     9739   9816   4295  -3810    264    207       N  
ATOM   1433  CA  GLY B  66     -46.874  19.389 -20.633  1.00 64.70           C  
ANISOU 1433  CA  GLY B  66    10060   9982   4541  -3782    469     53       C  
ATOM   1434  C   GLY B  66     -47.833  18.259 -20.956  1.00 69.01           C  
ANISOU 1434  C   GLY B  66    10739  10515   4969  -3871    456    -87       C  
ATOM   1435  O   GLY B  66     -49.049  18.452 -21.006  1.00 69.21           O  
ANISOU 1435  O   GLY B  66    10781  10588   4928  -3952    281    -60       O  
ATOM   1436  N   SER B  67     -47.275  17.072 -21.178  1.00 73.70           N  
ANISOU 1436  N   SER B  67    11422  11036   5544  -3856    639   -235       N  
ATOM   1437  CA  SER B  67     -48.068  15.875 -21.449  1.00 79.43           C  
ANISOU 1437  CA  SER B  67    12286  11728   6166  -3934    639   -379       C  
ATOM   1438  C   SER B  67     -47.194  14.627 -21.357  1.00 78.35           C  
ANISOU 1438  C   SER B  67    12206  11470   6092  -3864    847   -534       C  
ATOM   1439  O   SER B  67     -45.963  14.719 -21.332  1.00 83.76           O  
ANISOU 1439  O   SER B  67    12835  12120   6871  -3772   1008   -534       O  
ATOM   1440  CB  SER B  67     -48.723  15.954 -22.831  1.00 74.37           C  
ANISOU 1440  CB  SER B  67    11807  11201   5250  -4106    598   -399       C  
ATOM   1441  OG  SER B  67     -47.766  15.791 -23.862  1.00 68.53           O  
ANISOU 1441  OG  SER B  67    11171  10493   4376  -4136    796   -462       O  
ATOM   1442  N   GLY B  68     -47.831  13.461 -21.306  1.00 63.30           N  
ANISOU 1442  N   GLY B  68    10406   9498   4146  -3908    838   -663       N  
ATOM   1443  CA  GLY B  68     -47.104  12.210 -21.207  1.00 61.62           C  
ANISOU 1443  CA  GLY B  68    10255   9156   4000  -3844   1014   -819       C  
ATOM   1444  C   GLY B  68     -46.335  12.091 -19.906  1.00 61.78           C  
ANISOU 1444  C   GLY B  68    10122   9047   4303  -3687   1046   -790       C  
ATOM   1445  O   GLY B  68     -46.925  11.835 -18.853  1.00 56.71           O  
ANISOU 1445  O   GLY B  68     9425   8338   3785  -3663    920   -769       O  
ATOM   1446  N   THR B  69     -45.019  12.283 -19.975  1.00 63.88           N  
ANISOU 1446  N   THR B  69    10320   9278   4671  -3589   1212   -782       N  
ATOM   1447  CA  THR B  69     -44.164  12.156 -18.799  1.00 68.92           C  
ANISOU 1447  CA  THR B  69    10818   9781   5586  -3444   1244   -749       C  
ATOM   1448  C   THR B  69     -43.426  13.453 -18.475  1.00 69.53           C  
ANISOU 1448  C   THR B  69    10739   9906   5775  -3373   1231   -580       C  
ATOM   1449  O   THR B  69     -42.693  13.525 -17.486  1.00 70.13           O  
ANISOU 1449  O   THR B  69    10691   9874   6081  -3260   1236   -523       O  
ATOM   1450  CB  THR B  69     -43.123  11.026 -18.973  1.00 75.77           C  
ANISOU 1450  CB  THR B  69    11724  10516   6548  -3367   1453   -899       C  
ATOM   1451  CG2 THR B  69     -43.800   9.739 -19.430  1.00 75.98           C  
ANISOU 1451  CG2 THR B  69    11928  10494   6447  -3443   1472  -1075       C  
ATOM   1452  OG1 THR B  69     -42.133  11.419 -19.936  1.00 70.74           O  
ANISOU 1452  OG1 THR B  69    11082   9945   5850  -3351   1642   -906       O  
ATOM   1453  N   GLU B  70     -43.617  14.474 -19.307  1.00 70.49           N  
ANISOU 1453  N   GLU B  70    10871  10180   5731  -3448   1201   -493       N  
ATOM   1454  CA  GLU B  70     -42.917  15.745 -19.119  1.00 73.31           C  
ANISOU 1454  CA  GLU B  70    11091  10589   6173  -3394   1182   -327       C  
ATOM   1455  C   GLU B  70     -43.867  16.923 -18.927  1.00 69.68           C  
ANISOU 1455  C   GLU B  70    10589  10233   5652  -3450    962   -182       C  
ATOM   1456  O   GLU B  70     -44.699  17.218 -19.785  1.00 65.18           O  
ANISOU 1456  O   GLU B  70    10110   9781   4875  -3571    889   -179       O  
ATOM   1457  CB  GLU B  70     -41.963  16.024 -20.284  1.00 75.32           C  
ANISOU 1457  CB  GLU B  70    11372  10924   6320  -3416   1370   -337       C  
ATOM   1458  CG  GLU B  70     -40.804  15.046 -20.381  1.00 84.17           C  
ANISOU 1458  CG  GLU B  70    12489  11935   7555  -3329   1607   -462       C  
ATOM   1459  CD  GLU B  70     -39.938  15.043 -19.136  1.00 90.36           C  
ANISOU 1459  CD  GLU B  70    13108  12575   8649  -3181   1605   -396       C  
ATOM   1460  OE1 GLU B  70     -39.721  16.129 -18.555  1.00 93.16           O  
ANISOU 1460  OE1 GLU B  70    13338  12953   9104  -3143   1494   -225       O  
ATOM   1461  OE2 GLU B  70     -39.471  13.953 -18.744  1.00 90.18           O1-
ANISOU 1461  OE2 GLU B  70    13086  12408   8772  -3105   1705   -512       O1-
ATOM   1462  N   PHE B  71     -43.729  17.594 -17.790  1.00 68.63           N  
ANISOU 1462  N   PHE B  71    10321  10048   5708  -3363    851    -61       N  
ATOM   1463  CA  PHE B  71     -44.545  18.754 -17.478  1.00 59.75           C  
ANISOU 1463  CA  PHE B  71     9138   9001   4563  -3392    647     75       C  
ATOM   1464  C   PHE B  71     -43.665  19.851 -16.909  1.00 58.38           C  
ANISOU 1464  C   PHE B  71     8829   8811   4542  -3303    617    232       C  
ATOM   1465  O   PHE B  71     -42.632  19.570 -16.303  1.00 59.15           O  
ANISOU 1465  O   PHE B  71     8860   8800   4816  -3204    711    237       O  
ATOM   1466  CB  PHE B  71     -45.637  18.382 -16.476  1.00 47.55           C  
ANISOU 1466  CB  PHE B  71     7583   7399   3083  -3390    504     49       C  
ATOM   1467  CG  PHE B  71     -46.527  17.271 -16.942  1.00 48.22           C  
ANISOU 1467  CG  PHE B  71     7796   7491   3034  -3481    515    -95       C  
ATOM   1468  CD1 PHE B  71     -47.751  17.547 -17.528  1.00 47.10           C  
ANISOU 1468  CD1 PHE B  71     7710   7456   2728  -3595    386    -86       C  
ATOM   1469  CD2 PHE B  71     -46.136  15.948 -16.806  1.00 48.21           C  
ANISOU 1469  CD2 PHE B  71     7859   7379   3079  -3456    644   -234       C  
ATOM   1470  CE1 PHE B  71     -48.574  16.524 -17.963  1.00 50.35           C  
ANISOU 1470  CE1 PHE B  71     8244   7870   3017  -3688    383   -209       C  
ATOM   1471  CE2 PHE B  71     -46.953  14.923 -17.241  1.00 55.55           C  
ANISOU 1471  CE2 PHE B  71     8916   8308   3882  -3545    644   -363       C  
ATOM   1472  CZ  PHE B  71     -48.174  15.211 -17.820  1.00 56.74           C  
ANISOU 1472  CZ  PHE B  71     9126   8571   3862  -3664    513   -349       C  
ATOM   1473  N   THR B  72     -44.070  21.100 -17.119  1.00 53.99           N  
ANISOU 1473  N   THR B  72     8234   8354   3925  -3340    474    363       N  
ATOM   1474  CA  THR B  72     -43.347  22.236 -16.565  1.00 54.30           C  
ANISOU 1474  CA  THR B  72     8153   8377   4100  -3264    413    523       C  
ATOM   1475  C   THR B  72     -44.299  23.267 -15.962  1.00 53.91           C  
ANISOU 1475  C   THR B  72     8051   8358   4075  -3264    187    629       C  
ATOM   1476  O   THR B  72     -45.398  23.491 -16.471  1.00 47.68           O  
ANISOU 1476  O   THR B  72     7309   7658   3149  -3351     79    619       O  
ATOM   1477  CB  THR B  72     -42.461  22.928 -17.622  1.00 58.96           C  
ANISOU 1477  CB  THR B  72     8740   9063   4601  -3302    499    601       C  
ATOM   1478  CG2 THR B  72     -41.754  21.899 -18.492  1.00 61.24           C  
ANISOU 1478  CG2 THR B  72     9104   9354   4811  -3327    735    469       C  
ATOM   1479  OG1 THR B  72     -43.263  23.784 -18.446  1.00 60.58           O  
ANISOU 1479  OG1 THR B  72     8989   9403   4624  -3411    367    667       O  
ATOM   1480  N   LEU B  73     -43.866  23.873 -14.863  1.00 57.73           N  
ANISOU 1480  N   LEU B  73     8437   8758   4742  -3166    116    729       N  
ATOM   1481  CA  LEU B  73     -44.549  25.008 -14.259  1.00 54.90           C  
ANISOU 1481  CA  LEU B  73     8017   8416   4426  -3148    -84    840       C  
ATOM   1482  C   LEU B  73     -43.716  26.242 -14.555  1.00 56.77           C  
ANISOU 1482  C   LEU B  73     8194   8690   4686  -3129   -127    999       C  
ATOM   1483  O   LEU B  73     -42.490  26.199 -14.460  1.00 68.00           O  
ANISOU 1483  O   LEU B  73     9577  10059   6200  -3078    -21   1041       O  
ATOM   1484  CB  LEU B  73     -44.658  24.813 -12.746  1.00 56.48           C  
ANISOU 1484  CB  LEU B  73     8169   8484   4807  -3057   -137    836       C  
ATOM   1485  CG  LEU B  73     -44.999  26.039 -11.893  1.00 43.93           C  
ANISOU 1485  CG  LEU B  73     6507   6875   3308  -3005   -315    958       C  
ATOM   1486  CD1 LEU B  73     -46.367  26.582 -12.264  1.00 49.94           C  
ANISOU 1486  CD1 LEU B  73     7275   7739   3963  -3066   -456    956       C  
ATOM   1487  CD2 LEU B  73     -44.946  25.689 -10.412  1.00 42.33           C  
ANISOU 1487  CD2 LEU B  73     6281   6532   3269  -2927   -333    941       C  
ATOM   1488  N   THR B  74     -44.365  27.342 -14.920  1.00 50.86           N  
ANISOU 1488  N   THR B  74     7432   8029   3863  -3174   -289   1092       N  
ATOM   1489  CA  THR B  74     -43.621  28.553 -15.251  1.00 55.28           C  
ANISOU 1489  CA  THR B  74     7943   8628   4434  -3170   -350   1251       C  
ATOM   1490  C   THR B  74     -44.168  29.811 -14.592  1.00 56.74           C  
ANISOU 1490  C   THR B  74     8066   8798   4696  -3130   -572   1370       C  
ATOM   1491  O   THR B  74     -45.343  30.143 -14.739  1.00 71.66           O  
ANISOU 1491  O   THR B  74     9967  10739   6522  -3171   -707   1357       O  
ATOM   1492  CB  THR B  74     -43.519  28.767 -16.772  1.00 50.46           C  
ANISOU 1492  CB  THR B  74     7395   8156   3622  -3293   -308   1270       C  
ATOM   1493  CG2 THR B  74     -43.206  30.216 -17.081  1.00 52.38           C  
ANISOU 1493  CG2 THR B  74     7592   8453   3856  -3313   -448   1449       C  
ATOM   1494  OG1 THR B  74     -42.467  27.948 -17.297  1.00 54.91           O  
ANISOU 1494  OG1 THR B  74     7987   8718   4159  -3301    -80   1207       O  
ATOM   1495  N   ILE B  75     -43.298  30.502 -13.863  1.00 43.41           N  
ANISOU 1495  N   ILE B  75     6311   7031   3152  -3047   -610   1486       N  
ATOM   1496  CA  ILE B  75     -43.634  31.789 -13.279  1.00 47.57           C  
ANISOU 1496  CA  ILE B  75     6788   7534   3754  -3003   -816   1608       C  
ATOM   1497  C   ILE B  75     -43.084  32.887 -14.175  1.00 45.97           C  
ANISOU 1497  C   ILE B  75     6571   7412   3484  -3058   -889   1758       C  
ATOM   1498  O   ILE B  75     -41.873  33.102 -14.220  1.00 48.90           O  
ANISOU 1498  O   ILE B  75     6911   7759   3910  -3038   -822   1846       O  
ATOM   1499  CB  ILE B  75     -43.032  31.939 -11.874  1.00 41.35           C  
ANISOU 1499  CB  ILE B  75     5952   6597   3161  -2888   -838   1654       C  
ATOM   1500  CG1 ILE B  75     -43.289  30.678 -11.048  1.00 33.31           C  
ANISOU 1500  CG1 ILE B  75     4959   5492   2205  -2851   -731   1511       C  
ATOM   1501  CG2 ILE B  75     -43.607  33.160 -11.177  1.00 44.03           C  
ANISOU 1501  CG2 ILE B  75     6259   6902   3571  -2839  -1050   1745       C  
ATOM   1502  CD1 ILE B  75     -42.673  30.719  -9.670  1.00 36.63           C  
ANISOU 1502  CD1 ILE B  75     5353   5757   2807  -2756   -751   1554       C  
ATOM   1503  N   SER B  76     -43.971  33.572 -14.893  1.00 52.02           N  
ANISOU 1503  N   SER B  76     7356   8272   4138  -3132  -1034   1792       N  
ATOM   1504  CA  SER B  76     -43.550  34.581 -15.863  1.00 63.36           C  
ANISOU 1504  CA  SER B  76     8794   9796   5483  -3211  -1117   1933       C  
ATOM   1505  C   SER B  76     -42.603  35.621 -15.262  1.00 69.98           C  
ANISOU 1505  C   SER B  76     9568  10564   6456  -3140  -1205   2096       C  
ATOM   1506  O   SER B  76     -41.429  35.671 -15.627  1.00 85.89           O  
ANISOU 1506  O   SER B  76    11569  12594   8470  -3159  -1103   2171       O  
ATOM   1507  CB  SER B  76     -44.758  35.256 -16.523  1.00 70.43           C  
ANISOU 1507  CB  SER B  76     9715  10774   6273  -3292  -1309   1957       C  
ATOM   1508  OG  SER B  76     -45.543  35.955 -15.576  1.00 85.09           O  
ANISOU 1508  OG  SER B  76    11516  12557   8260  -3206  -1493   1982       O  
ATOM   1509  N   SER B  77     -43.105  36.449 -14.349  1.00 60.04           N  
ANISOU 1509  N   SER B  77     8271   9227   5315  -3062  -1391   2151       N  
ATOM   1510  CA  SER B  77     -42.261  37.451 -13.696  1.00 62.52           C  
ANISOU 1510  CA  SER B  77     8537   9457   5760  -2994  -1495   2305       C  
ATOM   1511  C   SER B  77     -42.233  37.271 -12.178  1.00 60.14           C  
ANISOU 1511  C   SER B  77     8212   9004   5633  -2866  -1504   2268       C  
ATOM   1512  O   SER B  77     -43.124  37.730 -11.460  1.00 59.81           O  
ANISOU 1512  O   SER B  77     8165   8911   5650  -2810  -1642   2245       O  
ATOM   1513  CB  SER B  77     -42.684  38.876 -14.078  1.00 60.43           C  
ANISOU 1513  CB  SER B  77     8262   9228   5469  -3027  -1739   2441       C  
ATOM   1514  OG  SER B  77     -43.960  39.196 -13.557  1.00 66.43           O  
ANISOU 1514  OG  SER B  77     9014   9954   6271  -2980  -1887   2382       O  
ATOM   1515  N   LEU B  78     -41.186  36.602 -11.708  1.00 51.98           N  
ANISOU 1515  N   LEU B  78     7166   7898   4685  -2825  -1356   2263       N  
ATOM   1516  CA  LEU B  78     -41.053  36.217 -10.306  1.00 50.18           C  
ANISOU 1516  CA  LEU B  78     6934   7522   4610  -2725  -1341   2221       C  
ATOM   1517  C   LEU B  78     -41.181  37.383  -9.322  1.00 58.32           C  
ANISOU 1517  C   LEU B  78     7956   8451   5751  -2651  -1545   2323       C  
ATOM   1518  O   LEU B  78     -40.644  38.473  -9.554  1.00 58.03           O  
ANISOU 1518  O   LEU B  78     7900   8416   5734  -2658  -1671   2479       O  
ATOM   1519  CB  LEU B  78     -39.710  35.525 -10.104  1.00 49.40           C  
ANISOU 1519  CB  LEU B  78     6813   7357   4601  -2705  -1182   2245       C  
ATOM   1520  CG  LEU B  78     -39.422  34.925  -8.735  1.00 44.96           C  
ANISOU 1520  CG  LEU B  78     6256   6633   4192  -2622  -1150   2202       C  
ATOM   1521  CD1 LEU B  78     -40.461  33.871  -8.397  1.00 46.69           C  
ANISOU 1521  CD1 LEU B  78     6519   6850   4370  -2621  -1075   2017       C  
ATOM   1522  CD2 LEU B  78     -38.036  34.328  -8.752  1.00 56.30           C  
ANISOU 1522  CD2 LEU B  78     7654   8012   5726  -2612  -1008   2246       C  
ATOM   1523  N   GLN B  79     -41.884  37.147  -8.217  1.00 52.50           N  
ANISOU 1523  N   GLN B  79     7240   7624   5082  -2586  -1575   2233       N  
ATOM   1524  CA  GLN B  79     -42.090  38.195  -7.223  1.00 48.64           C  
ANISOU 1524  CA  GLN B  79     6759   7031   4690  -2512  -1754   2305       C  
ATOM   1525  C   GLN B  79     -41.866  37.712  -5.792  1.00 52.73           C  
ANISOU 1525  C   GLN B  79     7313   7397   5327  -2443  -1718   2259       C  
ATOM   1526  O   GLN B  79     -41.886  36.512  -5.533  1.00 63.38           O  
ANISOU 1526  O   GLN B  79     8677   8728   6676  -2451  -1567   2146       O  
ATOM   1527  CB  GLN B  79     -43.466  38.833  -7.399  1.00 44.85           C  
ANISOU 1527  CB  GLN B  79     6273   6610   4158  -2509  -1886   2256       C  
ATOM   1528  CG  GLN B  79     -43.570  39.605  -8.702  1.00 63.53           C  
ANISOU 1528  CG  GLN B  79     8614   9097   6427  -2581  -1985   2346       C  
ATOM   1529  CD  GLN B  79     -44.553  40.744  -8.629  1.00 79.78           C  
ANISOU 1529  CD  GLN B  79    10656  11153   8503  -2551  -2195   2374       C  
ATOM   1530  NE2 GLN B  79     -44.366  41.740  -9.486  1.00 84.51           N  
ANISOU 1530  NE2 GLN B  79    11241  11808   9060  -2600  -2339   2507       N  
ATOM   1531  OE1 GLN B  79     -45.473  40.733  -7.811  1.00 89.67           O  
ANISOU 1531  OE1 GLN B  79    11907  12353   9811  -2487  -2227   2278       O  
ATOM   1532  N   PRO B  80     -41.632  38.652  -4.863  1.00 43.74           N  
ANISOU 1532  N   PRO B  80     6197   6140   4283  -2381  -1865   2351       N  
ATOM   1533  CA  PRO B  80     -41.282  38.338  -3.476  1.00 40.42           C  
ANISOU 1533  CA  PRO B  80     5829   5560   3971  -2328  -1855   2337       C  
ATOM   1534  C   PRO B  80     -42.156  37.253  -2.851  1.00 48.21           C  
ANISOU 1534  C   PRO B  80     6848   6533   4935  -2326  -1741   2157       C  
ATOM   1535  O   PRO B  80     -41.636  36.348  -2.197  1.00 54.58           O  
ANISOU 1535  O   PRO B  80     7687   7252   5798  -2328  -1645   2123       O  
ATOM   1536  CB  PRO B  80     -41.505  39.670  -2.758  1.00 44.89           C  
ANISOU 1536  CB  PRO B  80     6428   6039   4590  -2270  -2054   2418       C  
ATOM   1537  CG  PRO B  80     -41.203  40.695  -3.793  1.00 33.34           C  
ANISOU 1537  CG  PRO B  80     4918   4655   3093  -2295  -2170   2554       C  
ATOM   1538  CD  PRO B  80     -41.663  40.107  -5.104  1.00 43.37           C  
ANISOU 1538  CD  PRO B  80     6138   6097   4243  -2366  -2063   2483       C  
ATOM   1539  N   ASP B  81     -43.465  37.342  -3.052  1.00 51.14           N  
ANISOU 1539  N   ASP B  81     7207   6988   5235  -2327  -1759   2051       N  
ATOM   1540  CA  ASP B  81     -44.390  36.421  -2.402  1.00 50.14           C  
ANISOU 1540  CA  ASP B  81     7108   6855   5090  -2329  -1665   1888       C  
ATOM   1541  C   ASP B  81     -44.306  35.005  -2.962  1.00 40.49           C  
ANISOU 1541  C   ASP B  81     5878   5694   3812  -2390  -1489   1792       C  
ATOM   1542  O   ASP B  81     -45.020  34.111  -2.511  1.00 43.79           O  
ANISOU 1542  O   ASP B  81     6318   6111   4208  -2407  -1405   1661       O  
ATOM   1543  CB  ASP B  81     -45.826  36.936  -2.508  1.00 60.78           C  
ANISOU 1543  CB  ASP B  81     8423   8277   6391  -2313  -1735   1808       C  
ATOM   1544  CG  ASP B  81     -46.767  36.227  -1.555  1.00 78.81           C  
ANISOU 1544  CG  ASP B  81    10735  10531   8678  -2305  -1659   1659       C  
ATOM   1545  OD1 ASP B  81     -46.300  35.774  -0.487  1.00 82.71           O  
ANISOU 1545  OD1 ASP B  81    11297  10907   9224  -2294  -1613   1646       O  
ATOM   1546  OD2 ASP B  81     -47.971  36.122  -1.871  1.00 89.61           O1-
ANISOU 1546  OD2 ASP B  81    12057  11993   9998  -2318  -1651   1561       O1-
ATOM   1547  N   ASP B  82     -43.433  34.798  -3.941  1.00 35.79           N  
ANISOU 1547  N   ASP B  82     5254   5152   3193  -2427  -1432   1856       N  
ATOM   1548  CA  ASP B  82     -43.333  33.495  -4.594  1.00 33.76           C  
ANISOU 1548  CA  ASP B  82     4995   4955   2878  -2482  -1263   1759       C  
ATOM   1549  C   ASP B  82     -42.324  32.584  -3.918  1.00 43.96           C  
ANISOU 1549  C   ASP B  82     6314   6123   4267  -2471  -1163   1757       C  
ATOM   1550  O   ASP B  82     -42.202  31.416  -4.279  1.00 49.12           O  
ANISOU 1550  O   ASP B  82     6973   6796   4896  -2506  -1022   1666       O  
ATOM   1551  CB  ASP B  82     -42.995  33.647  -6.075  1.00 37.77           C  
ANISOU 1551  CB  ASP B  82     5464   5593   3294  -2536  -1228   1806       C  
ATOM   1552  CG  ASP B  82     -44.116  34.289  -6.857  1.00 46.04           C  
ANISOU 1552  CG  ASP B  82     6492   6767   4234  -2570  -1321   1788       C  
ATOM   1553  OD1 ASP B  82     -45.218  34.444  -6.287  1.00 42.93           O  
ANISOU 1553  OD1 ASP B  82     6100   6367   3844  -2547  -1386   1717       O  
ATOM   1554  OD2 ASP B  82     -43.897  34.634  -8.037  1.00 55.96           O1-
ANISOU 1554  OD2 ASP B  82     7730   8127   5404  -2625  -1329   1846       O1-
ATOM   1555  N   PHE B  83     -41.598  33.119  -2.942  1.00 42.39           N  
ANISOU 1555  N   PHE B  83     6135   5786   4184  -2424  -1247   1860       N  
ATOM   1556  CA  PHE B  83     -40.720  32.284  -2.143  1.00 32.67           C  
ANISOU 1556  CA  PHE B  83     4933   4414   3065  -2417  -1183   1865       C  
ATOM   1557  C   PHE B  83     -41.541  31.143  -1.573  1.00 38.40           C  
ANISOU 1557  C   PHE B  83     5709   5119   3760  -2442  -1100   1705       C  
ATOM   1558  O   PHE B  83     -42.505  31.368  -0.841  1.00 42.68           O  
ANISOU 1558  O   PHE B  83     6293   5651   4274  -2436  -1156   1646       O  
ATOM   1559  CB  PHE B  83     -40.083  33.070  -0.998  1.00 34.82           C  
ANISOU 1559  CB  PHE B  83     5245   4531   3455  -2374  -1317   1990       C  
ATOM   1560  CG  PHE B  83     -39.506  32.194   0.076  1.00 34.46           C  
ANISOU 1560  CG  PHE B  83     5253   4322   3516  -2377  -1282   1977       C  
ATOM   1561  CD1 PHE B  83     -38.226  31.690  -0.043  1.00 39.73           C  
ANISOU 1561  CD1 PHE B  83     5885   4910   4299  -2378  -1230   2052       C  
ATOM   1562  CD2 PHE B  83     -40.256  31.850   1.190  1.00 40.49           C  
ANISOU 1562  CD2 PHE B  83     6102   5012   4270  -2386  -1301   1888       C  
ATOM   1563  CE1 PHE B  83     -37.696  30.870   0.935  1.00 46.79           C  
ANISOU 1563  CE1 PHE B  83     6828   5643   5307  -2387  -1217   2047       C  
ATOM   1564  CE2 PHE B  83     -39.731  31.037   2.169  1.00 46.04           C  
ANISOU 1564  CE2 PHE B  83     6867   5561   5065  -2405  -1285   1883       C  
ATOM   1565  CZ  PHE B  83     -38.450  30.545   2.042  1.00 44.58           C  
ANISOU 1565  CZ  PHE B  83     6646   5287   5004  -2405  -1252   1965       C  
ATOM   1566  N   ALA B  84     -41.154  29.919  -1.905  1.00 39.44           N  
ANISOU 1566  N   ALA B  84     5838   5244   3904  -2472   -964   1634       N  
ATOM   1567  CA  ALA B  84     -41.913  28.750  -1.492  1.00 34.71           C  
ANISOU 1567  CA  ALA B  84     5286   4632   3269  -2509   -885   1484       C  
ATOM   1568  C   ALA B  84     -41.224  27.497  -1.983  1.00 38.44           C  
ANISOU 1568  C   ALA B  84     5749   5081   3775  -2532   -745   1428       C  
ATOM   1569  O   ALA B  84     -40.194  27.565  -2.653  1.00 43.83           O  
ANISOU 1569  O   ALA B  84     6381   5765   4508  -2515   -698   1499       O  
ATOM   1570  CB  ALA B  84     -43.332  28.815  -2.047  1.00 33.06           C  
ANISOU 1570  CB  ALA B  84     5070   4574   2918  -2540   -880   1379       C  
ATOM   1571  N   THR B  85     -41.795  26.351  -1.638  1.00 41.35           N  
ANISOU 1571  N   THR B  85     6166   5425   4120  -2570   -679   1298       N  
ATOM   1572  CA  THR B  85     -41.346  25.080  -2.180  1.00 45.57           C  
ANISOU 1572  CA  THR B  85     6700   5943   4672  -2593   -545   1216       C  
ATOM   1573  C   THR B  85     -42.465  24.534  -3.059  1.00 47.90           C  
ANISOU 1573  C   THR B  85     7007   6386   4808  -2646   -474   1079       C  
ATOM   1574  O   THR B  85     -43.621  24.465  -2.645  1.00 55.65           O  
ANISOU 1574  O   THR B  85     8022   7407   5717  -2679   -514   1009       O  
ATOM   1575  CB  THR B  85     -40.999  24.070  -1.066  1.00 40.50           C  
ANISOU 1575  CB  THR B  85     6113   5128   4145  -2605   -538   1182       C  
ATOM   1576  CG2 THR B  85     -40.612  22.726  -1.661  1.00 32.19           C  
ANISOU 1576  CG2 THR B  85     5061   4054   3116  -2624   -405   1082       C  
ATOM   1577  OG1 THR B  85     -39.908  24.576  -0.288  1.00 51.80           O  
ANISOU 1577  OG1 THR B  85     7537   6413   5731  -2564   -617   1321       O  
ATOM   1578  N   TYR B  86     -42.124  24.161  -4.283  1.00 37.69           N  
ANISOU 1578  N   TYR B  86     5689   5174   3458  -2660   -369   1043       N  
ATOM   1579  CA  TYR B  86     -43.134  23.730  -5.236  1.00 36.96           C  
ANISOU 1579  CA  TYR B  86     5618   5222   3203  -2720   -316    928       C  
ATOM   1580  C   TYR B  86     -43.092  22.222  -5.452  1.00 45.59           C  
ANISOU 1580  C   TYR B  86     6759   6273   4289  -2755   -194    794       C  
ATOM   1581  O   TYR B  86     -42.021  21.626  -5.558  1.00 67.37           O  
ANISOU 1581  O   TYR B  86     9508   8943   7144  -2726   -106    794       O  
ATOM   1582  CB  TYR B  86     -42.977  24.496  -6.555  1.00 31.46           C  
ANISOU 1582  CB  TYR B  86     4882   4665   2405  -2730   -300    980       C  
ATOM   1583  CG  TYR B  86     -43.197  25.985  -6.396  1.00 38.86           C  
ANISOU 1583  CG  TYR B  86     5778   5649   3338  -2704   -441   1104       C  
ATOM   1584  CD1 TYR B  86     -42.211  26.801  -5.858  1.00 37.34           C  
ANISOU 1584  CD1 TYR B  86     5548   5371   3269  -2644   -503   1244       C  
ATOM   1585  CD2 TYR B  86     -44.401  26.570  -6.762  1.00 42.03           C  
ANISOU 1585  CD2 TYR B  86     6176   6168   3624  -2738   -525   1085       C  
ATOM   1586  CE1 TYR B  86     -42.414  28.159  -5.700  1.00 30.37           C  
ANISOU 1586  CE1 TYR B  86     4636   4519   2384  -2620   -642   1355       C  
ATOM   1587  CE2 TYR B  86     -44.611  27.926  -6.610  1.00 43.79           C  
ANISOU 1587  CE2 TYR B  86     6362   6421   3857  -2708   -663   1194       C  
ATOM   1588  CZ  TYR B  86     -43.617  28.714  -6.080  1.00 40.88           C  
ANISOU 1588  CZ  TYR B  86     5967   5965   3602  -2648   -720   1326       C  
ATOM   1589  OH  TYR B  86     -43.834  30.063  -5.930  1.00 52.62           O  
ANISOU 1589  OH  TYR B  86     7424   7471   5098  -2618   -867   1431       O  
ATOM   1590  N   TYR B  87     -44.269  21.609  -5.495  1.00 36.47           N  
ANISOU 1590  N   TYR B  87     5652   5176   3030  -2816   -195    682       N  
ATOM   1591  CA  TYR B  87     -44.383  20.170  -5.683  1.00 39.13           C  
ANISOU 1591  CA  TYR B  87     6047   5472   3348  -2859   -100    550       C  
ATOM   1592  C   TYR B  87     -45.342  19.867  -6.827  1.00 51.82           C  
ANISOU 1592  C   TYR B  87     7687   7227   4774  -2931    -65    455       C  
ATOM   1593  O   TYR B  87     -46.386  20.505  -6.966  1.00 56.96           O  
ANISOU 1593  O   TYR B  87     8325   7987   5332  -2965   -147    466       O  
ATOM   1594  CB  TYR B  87     -44.908  19.495  -4.412  1.00 37.49           C  
ANISOU 1594  CB  TYR B  87     5885   5161   3200  -2885   -150    504       C  
ATOM   1595  CG  TYR B  87     -44.024  19.627  -3.183  1.00 44.06           C  
ANISOU 1595  CG  TYR B  87     6712   5825   4203  -2835   -198    590       C  
ATOM   1596  CD1 TYR B  87     -44.227  20.646  -2.266  1.00 43.46           C  
ANISOU 1596  CD1 TYR B  87     6620   5730   4162  -2812   -308    684       C  
ATOM   1597  CD2 TYR B  87     -43.010  18.715  -2.927  1.00 47.98           C  
ANISOU 1597  CD2 TYR B  87     7225   6174   4831  -2815   -142    574       C  
ATOM   1598  CE1 TYR B  87     -43.437  20.767  -1.141  1.00 43.73           C  
ANISOU 1598  CE1 TYR B  87     6669   5605   4341  -2781   -365    766       C  
ATOM   1599  CE2 TYR B  87     -42.211  18.824  -1.804  1.00 38.12           C  
ANISOU 1599  CE2 TYR B  87     5977   4763   3745  -2782   -206    663       C  
ATOM   1600  CZ  TYR B  87     -42.429  19.854  -0.914  1.00 42.45           C  
ANISOU 1600  CZ  TYR B  87     6523   5297   4309  -2770   -320    762       C  
ATOM   1601  OH  TYR B  87     -41.641  19.973   0.207  1.00 48.54           O  
ANISOU 1601  OH  TYR B  87     7312   5900   5230  -2750   -395    855       O  
ATOM   1602  N   CYS B  88     -44.987  18.893  -7.654  1.00 53.28           N  
ANISOU 1602  N   CYS B  88     7918   7410   4916  -2955     54    361       N  
ATOM   1603  CA  CYS B  88     -45.933  18.361  -8.622  1.00 47.91           C  
ANISOU 1603  CA  CYS B  88     7298   6842   4064  -3040     82    255       C  
ATOM   1604  C   CYS B  88     -46.686  17.208  -7.974  1.00 46.25           C  
ANISOU 1604  C   CYS B  88     7149   6568   3858  -3091     69    150       C  
ATOM   1605  O   CYS B  88     -46.220  16.620  -6.996  1.00 52.26           O  
ANISOU 1605  O   CYS B  88     7918   7187   4750  -3061     74    141       O  
ATOM   1606  CB  CYS B  88     -45.228  17.905  -9.903  1.00 56.23           C  
ANISOU 1606  CB  CYS B  88     8391   7931   5045  -3050    221    197       C  
ATOM   1607  SG  CYS B  88     -43.831  16.788  -9.665  1.00 68.92           S  
ANISOU 1607  SG  CYS B  88    10007   9365   6813  -2983    365    137       S  
ATOM   1608  N   PHE B  89     -47.857  16.893  -8.507  1.00 39.21           N  
ANISOU 1608  N   PHE B  89     6300   5776   2823  -3176     40     78       N  
ATOM   1609  CA  PHE B  89     -48.684  15.847  -7.924  1.00 40.59           C  
ANISOU 1609  CA  PHE B  89     6529   5906   2990  -3240     16    -13       C  
ATOM   1610  C   PHE B  89     -49.473  15.129  -9.007  1.00 46.15           C  
ANISOU 1610  C   PHE B  89     7309   6697   3530  -3334     40   -117       C  
ATOM   1611  O   PHE B  89     -50.105  15.765  -9.851  1.00 48.71           O  
ANISOU 1611  O   PHE B  89     7622   7153   3730  -3378     -1    -94       O  
ATOM   1612  CB  PHE B  89     -49.633  16.443  -6.880  1.00 38.38           C  
ANISOU 1612  CB  PHE B  89     6196   5649   2738  -3252    -99     39       C  
ATOM   1613  CG  PHE B  89     -50.637  15.464  -6.330  1.00 36.39           C  
ANISOU 1613  CG  PHE B  89     5988   5379   2459  -3336   -128    -45       C  
ATOM   1614  CD1 PHE B  89     -51.839  15.243  -6.984  1.00 32.79           C  
ANISOU 1614  CD1 PHE B  89     5547   5038   1872  -3425   -164    -99       C  
ATOM   1615  CD2 PHE B  89     -50.388  14.783  -5.146  1.00 38.53           C  
ANISOU 1615  CD2 PHE B  89     6288   5515   2836  -3336   -131    -61       C  
ATOM   1616  CE1 PHE B  89     -52.772  14.354  -6.477  1.00 39.04           C  
ANISOU 1616  CE1 PHE B  89     6373   5819   2642  -3510   -195   -166       C  
ATOM   1617  CE2 PHE B  89     -51.317  13.887  -4.630  1.00 33.69           C  
ANISOU 1617  CE2 PHE B  89     5719   4891   2193  -3425   -161   -131       C  
ATOM   1618  CZ  PHE B  89     -52.511  13.674  -5.296  1.00 36.48           C  
ANISOU 1618  CZ  PHE B  89     6078   5367   2418  -3511   -189   -183       C  
ATOM   1619  N   GLN B  90     -49.417  13.803  -8.992  1.00 43.91           N  
ANISOU 1619  N   GLN B  90     7109   6327   3246  -3371     96   -226       N  
ATOM   1620  CA  GLN B  90     -50.210  13.005  -9.916  1.00 41.36           C  
ANISOU 1620  CA  GLN B  90     6878   6068   2769  -3471    106   -330       C  
ATOM   1621  C   GLN B  90     -51.263  12.233  -9.142  1.00 49.01           C  
ANISOU 1621  C   GLN B  90     7873   7009   3739  -3548     29   -378       C  
ATOM   1622  O   GLN B  90     -51.007  11.749  -8.036  1.00 52.44           O  
ANISOU 1622  O   GLN B  90     8303   7324   4295  -3527     20   -380       O  
ATOM   1623  CB  GLN B  90     -49.327  12.049 -10.725  1.00 36.61           C  
ANISOU 1623  CB  GLN B  90     6370   5396   2145  -3460    238   -433       C  
ATOM   1624  CG  GLN B  90     -48.630  10.966  -9.901  1.00 49.36           C  
ANISOU 1624  CG  GLN B  90     8015   6830   3909  -3419    285   -493       C  
ATOM   1625  CD  GLN B  90     -49.478   9.722  -9.735  1.00 54.83           C  
ANISOU 1625  CD  GLN B  90     8803   7478   4551  -3513    244   -598       C  
ATOM   1626  NE2 GLN B  90     -49.048   8.830  -8.848  1.00 60.90           N  
ANISOU 1626  NE2 GLN B  90     9596   8087   5455  -3493    245   -635       N  
ATOM   1627  OE1 GLN B  90     -50.505   9.559 -10.399  1.00 56.31           O  
ANISOU 1627  OE1 GLN B  90     9046   7768   4582  -3609    201   -639       O  
ATOM   1628  N   GLY B  91     -52.453  12.139  -9.724  1.00 54.01           N  
ANISOU 1628  N   GLY B  91     8532   7752   4236  -3648    -35   -407       N  
ATOM   1629  CA  GLY B  91     -53.541  11.383  -9.135  1.00 50.08           C  
ANISOU 1629  CA  GLY B  91     8056   7248   3725  -3738   -106   -451       C  
ATOM   1630  C   GLY B  91     -54.110  10.410 -10.148  1.00 50.40           C  
ANISOU 1630  C   GLY B  91     8212   7317   3621  -3844   -103   -551       C  
ATOM   1631  O   GLY B  91     -55.186   9.842  -9.950  1.00 45.04           O  
ANISOU 1631  O   GLY B  91     7553   6664   2897  -3943   -178   -582       O  
ATOM   1632  N   SER B  92     -53.370  10.215 -11.236  1.00 60.82           N  
ANISOU 1632  N   SER B  92     9613   8631   4867  -3827    -15   -602       N  
ATOM   1633  CA  SER B  92     -53.799   9.351 -12.332  1.00 62.92           C  
ANISOU 1633  CA  SER B  92    10012   8920   4975  -3927     -3   -702       C  
ATOM   1634  C   SER B  92     -53.709   7.869 -11.974  1.00 62.81           C  
ANISOU 1634  C   SER B  92    10102   8769   4992  -3961     23   -815       C  
ATOM   1635  O   SER B  92     -54.359   7.032 -12.599  1.00 73.96           O  
ANISOU 1635  O   SER B  92    11627  10190   6285  -4064     -6   -895       O  
ATOM   1636  CB  SER B  92     -52.970   9.637 -13.585  1.00 65.81           C  
ANISOU 1636  CB  SER B  92    10441   9320   5243  -3899    102   -728       C  
ATOM   1637  OG  SER B  92     -52.959  11.022 -13.881  1.00 67.90           O  
ANISOU 1637  OG  SER B  92    10612   9699   5487  -3869     69   -615       O  
ATOM   1638  N   GLY B  93     -52.900   7.548 -10.970  1.00 64.18           N  
ANISOU 1638  N   GLY B  93    10244   8809   5331  -3879     64   -814       N  
ATOM   1639  CA  GLY B  93     -52.752   6.174 -10.524  1.00 60.42           C  
ANISOU 1639  CA  GLY B  93     9860   8185   4911  -3907     72   -910       C  
ATOM   1640  C   GLY B  93     -52.325   6.076  -9.074  1.00 58.04           C  
ANISOU 1640  C   GLY B  93     9491   7765   4795  -3853     47   -861       C  
ATOM   1641  O   GLY B  93     -51.697   6.996  -8.543  1.00 59.59           O  
ANISOU 1641  O   GLY B  93     9588   7960   5096  -3761     65   -770       O  
ATOM   1642  N   TYR B  94     -52.667   4.959  -8.435  1.00 58.53           N  
ANISOU 1642  N   TYR B  94     9620   7724   4894  -3921     -6   -915       N  
ATOM   1643  CA  TYR B  94     -52.298   4.716  -7.040  1.00 57.72           C  
ANISOU 1643  CA  TYR B  94     9482   7494   4956  -3897    -45   -872       C  
ATOM   1644  C   TYR B  94     -50.970   3.974  -6.924  1.00 63.72           C  
ANISOU 1644  C   TYR B  94    10289   8062   5857  -3812     26   -928       C  
ATOM   1645  O   TYR B  94     -50.684   3.073  -7.714  1.00 65.82           O  
ANISOU 1645  O   TYR B  94    10657   8264   6088  -3817     80  -1041       O  
ATOM   1646  CB  TYR B  94     -53.390   3.920  -6.324  1.00 44.21           C  
ANISOU 1646  CB  TYR B  94     7812   5770   3215  -4030   -152   -888       C  
ATOM   1647  CG  TYR B  94     -54.615   4.728  -5.976  1.00 43.88           C  
ANISOU 1647  CG  TYR B  94     7680   5889   3102  -4098   -226   -809       C  
ATOM   1648  CD1 TYR B  94     -54.650   5.509  -4.828  1.00 42.37           C  
ANISOU 1648  CD1 TYR B  94     7389   5708   2999  -4069   -254   -713       C  
ATOM   1649  CD2 TYR B  94     -55.740   4.708  -6.793  1.00 44.85           C  
ANISOU 1649  CD2 TYR B  94     7817   6148   3075  -4193   -269   -831       C  
ATOM   1650  CE1 TYR B  94     -55.769   6.250  -4.502  1.00 42.77           C  
ANISOU 1650  CE1 TYR B  94     7349   5902   2998  -4121   -307   -653       C  
ATOM   1651  CE2 TYR B  94     -56.864   5.444  -6.475  1.00 46.31           C  
ANISOU 1651  CE2 TYR B  94     7901   6474   3220  -4249   -335   -760       C  
ATOM   1652  CZ  TYR B  94     -56.873   6.213  -5.327  1.00 54.07           C  
ANISOU 1652  CZ  TYR B  94     8778   7467   4300  -4207   -346   -676       C  
ATOM   1653  OH  TYR B  94     -57.987   6.951  -5.006  1.00 55.96           O  
ANISOU 1653  OH  TYR B  94     8909   7842   4512  -4252   -399   -616       O  
ATOM   1654  N   PRO B  95     -50.156   4.341  -5.923  1.00 66.60           N  
ANISOU 1654  N   PRO B  95    10584   8328   6391  -3735     21   -851       N  
ATOM   1655  CA  PRO B  95     -50.451   5.386  -4.936  1.00 61.79           C  
ANISOU 1655  CA  PRO B  95     9875   7781   5823  -3729    -41   -725       C  
ATOM   1656  C   PRO B  95     -50.298   6.780  -5.531  1.00 62.85           C  
ANISOU 1656  C   PRO B  95     9914   8057   5909  -3654      6   -652       C  
ATOM   1657  O   PRO B  95     -49.639   6.942  -6.561  1.00 63.21           O  
ANISOU 1657  O   PRO B  95     9966   8124   5929  -3591     98   -685       O  
ATOM   1658  CB  PRO B  95     -49.367   5.182  -3.869  1.00 56.93           C  
ANISOU 1658  CB  PRO B  95     9246   6978   5408  -3666    -54   -679       C  
ATOM   1659  CG  PRO B  95     -48.666   3.905  -4.222  1.00 64.60           C  
ANISOU 1659  CG  PRO B  95    10306   7787   6454  -3651    -16   -785       C  
ATOM   1660  CD  PRO B  95     -48.850   3.711  -5.681  1.00 70.29           C  
ANISOU 1660  CD  PRO B  95    11073   8601   7034  -3649     72   -884       C  
ATOM   1661  N   PHE B  96     -50.902   7.776  -4.891  1.00 58.63           N  
ANISOU 1661  N   PHE B  96     9297   7617   5363  -3664    -55   -557       N  
ATOM   1662  CA  PHE B  96     -50.685   9.157  -5.290  1.00 46.62           C  
ANISOU 1662  CA  PHE B  96     7683   6208   3824  -3588    -32   -474       C  
ATOM   1663  C   PHE B  96     -49.267   9.516  -4.907  1.00 46.86           C  
ANISOU 1663  C   PHE B  96     7675   6118   4011  -3473     14   -414       C  
ATOM   1664  O   PHE B  96     -48.736   8.999  -3.927  1.00 55.65           O  
ANISOU 1664  O   PHE B  96     8809   7080   5258  -3463    -13   -402       O  
ATOM   1665  CB  PHE B  96     -51.663  10.101  -4.590  1.00 50.89           C  
ANISOU 1665  CB  PHE B  96     8144   6855   4335  -3618   -113   -393       C  
ATOM   1666  CG  PHE B  96     -53.090   9.939  -5.030  1.00 51.32           C  
ANISOU 1666  CG  PHE B  96     8204   7046   4250  -3725   -162   -433       C  
ATOM   1667  CD1 PHE B  96     -53.392   9.385  -6.261  1.00 48.58           C  
ANISOU 1667  CD1 PHE B  96     7922   6755   3783  -3776   -138   -511       C  
ATOM   1668  CD2 PHE B  96     -54.130  10.363  -4.219  1.00 56.20           C  
ANISOU 1668  CD2 PHE B  96     8760   7734   4859  -3777   -231   -391       C  
ATOM   1669  CE1 PHE B  96     -54.705   9.238  -6.667  1.00 50.02           C  
ANISOU 1669  CE1 PHE B  96     8106   7053   3845  -3881   -200   -535       C  
ATOM   1670  CE2 PHE B  96     -55.447  10.224  -4.623  1.00 54.93           C  
ANISOU 1670  CE2 PHE B  96     8584   7696   4591  -3875   -279   -419       C  
ATOM   1671  CZ  PHE B  96     -55.733   9.662  -5.848  1.00 52.32           C  
ANISOU 1671  CZ  PHE B  96     8317   7414   4148  -3929   -273   -485       C  
ATOM   1672  N   THR B  97     -48.648  10.403  -5.674  1.00 45.36           N  
ANISOU 1672  N   THR B  97     7430   5995   3810  -3394     73   -370       N  
ATOM   1673  CA  THR B  97     -47.264  10.761  -5.413  1.00 49.40           C  
ANISOU 1673  CA  THR B  97     7893   6399   4476  -3286    120   -306       C  
ATOM   1674  C   THR B  97     -46.985  12.232  -5.683  1.00 45.60           C  
ANISOU 1674  C   THR B  97     7320   6021   3984  -3221    118   -195       C  
ATOM   1675  O   THR B  97     -47.623  12.852  -6.532  1.00 53.04           O  
ANISOU 1675  O   THR B  97     8247   7119   4786  -3247    117   -191       O  
ATOM   1676  CB  THR B  97     -46.300   9.892  -6.246  1.00 60.93           C  
ANISOU 1676  CB  THR B  97     9398   7773   5978  -3244    237   -397       C  
ATOM   1677  CG2 THR B  97     -46.250   8.467  -5.688  1.00 51.95           C  
ANISOU 1677  CG2 THR B  97     8343   6473   4921  -3283    220   -485       C  
ATOM   1678  OG1 THR B  97     -46.743   9.856  -7.612  1.00 57.27           O  
ANISOU 1678  OG1 THR B  97     8977   7444   5338  -3280    304   -471       O  
ATOM   1679  N   PHE B  98     -46.036  12.783  -4.932  1.00 45.70           N  
ANISOU 1679  N   PHE B  98     7276   5938   4150  -3143    102    -96       N  
ATOM   1680  CA  PHE B  98     -45.558  14.137  -5.141  1.00 40.07           C  
ANISOU 1680  CA  PHE B  98     6479   5294   3452  -3074     97     19       C  
ATOM   1681  C   PHE B  98     -44.142  14.049  -5.684  1.00 47.44           C  
ANISOU 1681  C   PHE B  98     7380   6154   4490  -2993    199     33       C  
ATOM   1682  O   PHE B  98     -43.497  13.008  -5.579  1.00 55.28           O  
ANISOU 1682  O   PHE B  98     8406   7013   5585  -2977    256    -32       O  
ATOM   1683  CB  PHE B  98     -45.518  14.907  -3.819  1.00 42.94           C  
ANISOU 1683  CB  PHE B  98     6803   5596   3915  -3050     -8    132       C  
ATOM   1684  CG  PHE B  98     -46.854  15.087  -3.171  1.00 39.18           C  
ANISOU 1684  CG  PHE B  98     6343   5189   3354  -3121    -94    121       C  
ATOM   1685  CD1 PHE B  98     -47.434  14.059  -2.446  1.00 36.06           C  
ANISOU 1685  CD1 PHE B  98     6015   4727   2961  -3197   -121     51       C  
ATOM   1686  CD2 PHE B  98     -47.520  16.297  -3.261  1.00 44.76           C  
ANISOU 1686  CD2 PHE B  98     6993   6026   3988  -3112   -150    184       C  
ATOM   1687  CE1 PHE B  98     -48.667  14.228  -1.839  1.00 39.29           C  
ANISOU 1687  CE1 PHE B  98     6427   5207   3295  -3267   -186     42       C  
ATOM   1688  CE2 PHE B  98     -48.749  16.475  -2.651  1.00 44.44           C  
ANISOU 1688  CE2 PHE B  98     6951   6048   3887  -3170   -216    169       C  
ATOM   1689  CZ  PHE B  98     -49.324  15.438  -1.940  1.00 41.82           C  
ANISOU 1689  CZ  PHE B  98     6679   5658   3552  -3248   -226     97       C  
ATOM   1690  N   GLY B  99     -43.657  15.146  -6.252  1.00 47.25           N  
ANISOU 1690  N   GLY B  99     7287   6214   4450  -2943    221    121       N  
ATOM   1691  CA  GLY B  99     -42.270  15.230  -6.663  1.00 44.93           C  
ANISOU 1691  CA  GLY B  99     6941   5858   4273  -2864    318    159       C  
ATOM   1692  C   GLY B  99     -41.379  15.567  -5.481  1.00 46.56           C  
ANISOU 1692  C   GLY B  99     7091   5912   4689  -2801    249    277       C  
ATOM   1693  O   GLY B  99     -41.864  15.996  -4.431  1.00 44.09           O  
ANISOU 1693  O   GLY B  99     6785   5569   4399  -2819    126    341       O  
ATOM   1694  N   GLY B 100     -40.074  15.372  -5.651  1.00 43.12           N  
ANISOU 1694  N   GLY B 100     6600   5376   4407  -2731    331    304       N  
ATOM   1695  CA  GLY B 100     -39.110  15.682  -4.611  1.00 43.45           C  
ANISOU 1695  CA  GLY B 100     6584   5261   4663  -2674    260    428       C  
ATOM   1696  C   GLY B 100     -39.221  17.102  -4.092  1.00 46.56           C  
ANISOU 1696  C   GLY B 100     6937   5709   5045  -2662    142    580       C  
ATOM   1697  O   GLY B 100     -38.929  17.369  -2.929  1.00 46.63           O  
ANISOU 1697  O   GLY B 100     6944   5594   5180  -2651     31    674       O  
ATOM   1698  N   GLY B 101     -39.644  18.016  -4.959  1.00 53.40           N  
ANISOU 1698  N   GLY B 101     7779   6752   5757  -2671    158    604       N  
ATOM   1699  CA  GLY B 101     -39.831  19.403  -4.578  1.00 55.53           C  
ANISOU 1699  CA  GLY B 101     8013   7080   6005  -2659     42    739       C  
ATOM   1700  C   GLY B 101     -38.776  20.335  -5.139  1.00 51.18           C  
ANISOU 1700  C   GLY B 101     7374   6561   5513  -2604     70    862       C  
ATOM   1701  O   GLY B 101     -37.646  19.925  -5.401  1.00 55.36           O  
ANISOU 1701  O   GLY B 101     7850   7012   6173  -2560    164    875       O  
ATOM   1702  N   THR B 102     -39.152  21.596  -5.326  1.00 44.58           N  
ANISOU 1702  N   THR B 102     6514   5836   4588  -2608    -12    955       N  
ATOM   1703  CA  THR B 102     -38.221  22.622  -5.783  1.00 46.75           C  
ANISOU 1703  CA  THR B 102     6708   6146   4910  -2568    -13   1093       C  
ATOM   1704  C   THR B 102     -38.311  23.839  -4.869  1.00 55.89           C  
ANISOU 1704  C   THR B 102     7854   7269   6114  -2546   -186   1236       C  
ATOM   1705  O   THR B 102     -39.394  24.373  -4.641  1.00 61.76           O  
ANISOU 1705  O   THR B 102     8636   8084   6747  -2573   -280   1223       O  
ATOM   1706  CB  THR B 102     -38.502  23.041  -7.240  1.00 44.70           C  
ANISOU 1706  CB  THR B 102     6436   6076   4470  -2604     63   1069       C  
ATOM   1707  CG2 THR B 102     -37.690  24.269  -7.615  1.00 42.96           C  
ANISOU 1707  CG2 THR B 102     6138   5903   4281  -2579     30   1231       C  
ATOM   1708  OG1 THR B 102     -38.156  21.969  -8.126  1.00 48.55           O  
ANISOU 1708  OG1 THR B 102     6936   6581   4928  -2617    241    947       O  
ATOM   1709  N   LYS B 103     -37.168  24.265  -4.343  1.00 62.26           N  
ANISOU 1709  N   LYS B 103     8606   7959   7090  -2498   -229   1371       N  
ATOM   1710  CA  LYS B 103     -37.117  25.379  -3.406  1.00 53.31           C  
ANISOU 1710  CA  LYS B 103     7475   6765   6014  -2477   -398   1511       C  
ATOM   1711  C   LYS B 103     -36.748  26.661  -4.140  1.00 50.18           C  
ANISOU 1711  C   LYS B 103     7016   6474   5576  -2464   -438   1640       C  
ATOM   1712  O   LYS B 103     -35.668  26.761  -4.712  1.00 65.78           O  
ANISOU 1712  O   LYS B 103     8914   8448   7630  -2445   -368   1715       O  
ATOM   1713  CB  LYS B 103     -36.097  25.083  -2.304  1.00 51.84           C  
ANISOU 1713  CB  LYS B 103     7282   6369   6045  -2445   -451   1595       C  
ATOM   1714  CG  LYS B 103     -36.452  25.657  -0.945  1.00 78.19           C  
ANISOU 1714  CG  LYS B 103    10691   9601   9417  -2449   -622   1664       C  
ATOM   1715  CD  LYS B 103     -35.724  24.909   0.166  1.00100.50           C  
ANISOU 1715  CD  LYS B 103    13547  12211  12427  -2448   -662   1694       C  
ATOM   1716  CE  LYS B 103     -36.299  25.245   1.535  1.00114.23           C  
ANISOU 1716  CE  LYS B 103    15393  13852  14157  -2476   -811   1721       C  
ATOM   1717  NZ  LYS B 103     -35.736  24.377   2.609  1.00116.99           N1+
ANISOU 1717  NZ  LYS B 103    15796  13994  14662  -2500   -856   1735       N1+
ATOM   1718  N   VAL B 104     -37.649  27.638  -4.125  1.00 43.09           N  
ANISOU 1718  N   VAL B 104     6145   5665   4561  -2478   -551   1666       N  
ATOM   1719  CA  VAL B 104     -37.409  28.916  -4.799  1.00 45.12           C  
ANISOU 1719  CA  VAL B 104     6353   6020   4770  -2475   -618   1793       C  
ATOM   1720  C   VAL B 104     -36.984  30.025  -3.835  1.00 49.28           C  
ANISOU 1720  C   VAL B 104     6880   6441   5404  -2437   -792   1954       C  
ATOM   1721  O   VAL B 104     -37.730  30.379  -2.924  1.00 55.61           O  
ANISOU 1721  O   VAL B 104     7744   7194   6193  -2428   -906   1941       O  
ATOM   1722  CB  VAL B 104     -38.663  29.396  -5.566  1.00 44.11           C  
ANISOU 1722  CB  VAL B 104     6250   6063   4448  -2516   -650   1731       C  
ATOM   1723  CG1 VAL B 104     -38.419  30.772  -6.176  1.00 45.96           C  
ANISOU 1723  CG1 VAL B 104     6442   6381   4641  -2519   -749   1875       C  
ATOM   1724  CG2 VAL B 104     -39.062  28.387  -6.638  1.00 35.41           C  
ANISOU 1724  CG2 VAL B 104     5161   5072   3222  -2567   -491   1585       C  
ATOM   1725  N   GLU B 105     -35.788  30.570  -4.046  1.00 54.25           N  
ANISOU 1725  N   GLU B 105     7441   7036   6136  -2418   -807   2103       N  
ATOM   1726  CA  GLU B 105     -35.316  31.731  -3.291  1.00 54.57           C  
ANISOU 1726  CA  GLU B 105     7483   6983   6267  -2390   -984   2274       C  
ATOM   1727  C   GLU B 105     -35.293  32.952  -4.200  1.00 57.17           C  
ANISOU 1727  C   GLU B 105     7769   7443   6509  -2405  -1052   2382       C  
ATOM   1728  O   GLU B 105     -35.064  32.821  -5.402  1.00 72.31           O  
ANISOU 1728  O   GLU B 105     9632   9492   8352  -2438   -937   2370       O  
ATOM   1729  CB  GLU B 105     -33.912  31.487  -2.729  1.00 68.08           C  
ANISOU 1729  CB  GLU B 105     9146   8534   8187  -2364   -984   2391       C  
ATOM   1730  CG  GLU B 105     -33.336  32.696  -1.987  1.00 84.78           C  
ANISOU 1730  CG  GLU B 105    11268  10545  10398  -2344  -1178   2583       C  
ATOM   1731  CD  GLU B 105     -31.813  32.720  -1.952  1.00 90.39           C  
ANISOU 1731  CD  GLU B 105    11889  11156  11301  -2332  -1173   2739       C  
ATOM   1732  OE1 GLU B 105     -31.177  31.875  -2.614  1.00100.44           O  
ANISOU 1732  OE1 GLU B 105    13076  12454  12632  -2332  -1004   2699       O  
ATOM   1733  OE2 GLU B 105     -31.251  33.595  -1.262  1.00 83.77           O1-
ANISOU 1733  OE2 GLU B 105    11061  10207  10560  -2321  -1339   2904       O1-
ATOM   1734  N   ILE B 106     -35.516  34.135  -3.630  1.00 53.68           N  
ANISOU 1734  N   ILE B 106     7361   6962   6074  -2386  -1239   2487       N  
ATOM   1735  CA  ILE B 106     -35.554  35.371  -4.419  1.00 51.76           C  
ANISOU 1735  CA  ILE B 106     7086   6828   5752  -2404  -1337   2598       C  
ATOM   1736  C   ILE B 106     -34.286  36.209  -4.279  1.00 51.22           C  
ANISOU 1736  C   ILE B 106     6967   6684   5809  -2395  -1433   2808       C  
ATOM   1737  O   ILE B 106     -34.011  36.743  -3.209  1.00 62.20           O  
ANISOU 1737  O   ILE B 106     8400   7930   7304  -2361  -1579   2900       O  
ATOM   1738  CB  ILE B 106     -36.752  36.256  -4.029  1.00 47.89           C  
ANISOU 1738  CB  ILE B 106     6660   6357   5178  -2389  -1497   2574       C  
ATOM   1739  CG1 ILE B 106     -38.039  35.443  -4.005  1.00 46.96           C  
ANISOU 1739  CG1 ILE B 106     6585   6299   4958  -2398  -1416   2376       C  
ATOM   1740  CG2 ILE B 106     -36.903  37.409  -5.000  1.00 52.70           C  
ANISOU 1740  CG2 ILE B 106     7236   7090   5696  -2417  -1596   2671       C  
ATOM   1741  CD1 ILE B 106     -38.537  35.094  -5.377  1.00 45.96           C  
ANISOU 1741  CD1 ILE B 106     6425   6352   4686  -2453  -1310   2295       C  
TER    1742      ILE B 106