multi.pdb

MODEL 1             
ATOM      1  N   GLU A 172     -49.847  -6.027  32.848  1.00 42.47           N  
ATOM      2  CA  GLU A 172     -50.553  -4.786  32.493  1.00 56.33           C  
ATOM      3  C   GLU A 172     -49.853  -3.635  33.213  1.00 51.50           C  
ATOM      4  O   GLU A 172     -49.035  -2.930  32.621  1.00 49.32           O  
ATOM      5  CB  GLU A 172     -52.069  -4.869  32.780  1.00 60.53           C  
ATOM      6  CG  GLU A 172     -52.523  -5.253  34.204  1.00 69.49           C  
ATOM      7  CD  GLU A 172     -52.173  -6.685  34.619  1.00 65.19           C  
ATOM      8  OE1 GLU A 172     -51.698  -7.474  33.772  1.00 61.98           O  
ATOM      9  OE2 GLU A 172     -52.382  -7.014  35.804  1.00 66.14           O  
ATOM     10  N   LEU A 173     -50.118  -3.488  34.506  1.00 81.91           N  
ANISOU   10  N   LEU A 173    11865  10053   9205   1989    608    954       N  
ATOM     11  CA  LEU A 173     -49.147  -2.827  35.364  1.00 72.60           C  
ANISOU   11  CA  LEU A 173    10734   8950   7902   2070    541    774       C  
ATOM     12  C   LEU A 173     -47.895  -3.726  35.431  1.00 64.44           C  
ANISOU   12  C   LEU A 173     9752   8113   6619   2132    478    689       C  
ATOM     13  O   LEU A 173     -46.797  -3.216  35.599  1.00 58.42           O  
ANISOU   13  O   LEU A 173     8981   7456   5761   2125    365    557       O  
ATOM     14  CB  LEU A 173     -49.726  -2.533  36.756  1.00 73.90           C  
ANISOU   14  CB  LEU A 173    11012   9018   8048   2248    664    709       C  
ATOM     15  CG  LEU A 173     -50.408  -1.168  37.002  1.00 79.24           C  
ANISOU   15  CG  LEU A 173    11642   9541   8925   2202    672    699       C  
ATOM     16  CD1 LEU A 173     -49.432  -0.084  37.482  1.00 80.70           C  
ANISOU   16  CD1 LEU A 173    11819   9784   9061   2204    560    532       C  
ATOM     17  CD2 LEU A 173     -51.175  -0.679  35.777  1.00 77.58           C  
ANISOU   17  CD2 LEU A 173    11293   9223   8963   2001    641    844       C  
ATOM     18  N   ASP A 174     -48.060  -5.051  35.266  1.00 59.88           N  
ANISOU   18  N   ASP A 174     9226   7586   5941   2189    547    768       N  
ATOM     19  CA  ASP A 174     -46.910  -5.979  35.190  1.00 55.93           C  
ANISOU   19  CA  ASP A 174     8767   7272   5214   2233    485    704       C  
ATOM     20  C   ASP A 174     -45.930  -5.539  34.077  1.00 63.48           C  
ANISOU   20  C   ASP A 174     9597   8334   6190   2050    308    682       C  
ATOM     21  O   ASP A 174     -44.726  -5.389  34.308  1.00 62.84           O  
ANISOU   21  O   ASP A 174     9530   8388   5958   2073    207    548       O  
ATOM     22  CB  ASP A 174     -47.345  -7.445  34.912  1.00 65.32           C  
ANISOU   22  CB  ASP A 174    10003   8486   6330   2282    577    821       C  
ATOM     23  CG  ASP A 174     -48.374  -7.995  35.919  1.00 71.39           C  
ANISOU   23  CG  ASP A 174    10892   9150   7082   2456    757    860       C  
ATOM     24  OD1 ASP A 174     -49.029  -7.192  36.620  1.00 77.99           O  
ANISOU   24  OD1 ASP A 174    11753   9861   8019   2507    820    836       O  
ATOM     25  OD2 ASP A 174     -48.547  -9.250  35.981  1.00 63.38           O  
ANISOU   25  OD2 ASP A 174     9946   8178   5955   2540    836    920       O  
ATOM     26  N   SER A 175     -46.461  -5.338  32.868  1.00 56.94           N  
ANISOU   26  N   SER A 175     8644   7441   5548   1868    272    815       N  
ATOM     27  CA  SER A 175     -45.652  -4.964  31.700  1.00 55.00           C  
ANISOU   27  CA  SER A 175     8271   7286   5342   1681    110    816       C  
ATOM     28  C   SER A 175     -44.986  -3.613  31.930  1.00 56.22           C  
ANISOU   28  C   SER A 175     8379   7449   5532   1631     -2    686       C  
ATOM     29  O   SER A 175     -43.787  -3.445  31.662  1.00 53.47           O  
ANISOU   29  O   SER A 175     7998   7240   5077   1583   -133    590       O  
ATOM     30  CB  SER A 175     -46.533  -4.934  30.452  1.00 52.33           C  
ANISOU   30  CB  SER A 175     7814   6850   5220   1504    111    991       C  
ATOM     31  OG  SER A 175     -45.809  -5.309  29.299  1.00 62.85           O  
ANISOU   31  OG  SER A 175     9057   8300   6524   1364     -6   1027       O  
ATOM     32  N   LEU A 176     -45.769  -2.663  32.445  1.00 53.03           N  
ANISOU   32  N   LEU A 176     7977   6897   5277   1647     53    683       N  
ATOM     33  CA  LEU A 176     -45.247  -1.378  32.914  1.00 58.91           C  
ANISOU   33  CA  LEU A 176     8701   7635   6049   1635    -29    550       C  
ATOM     34  C   LEU A 176     -43.944  -1.507  33.720  1.00 62.97           C  
ANISOU   34  C   LEU A 176     9298   8306   6322   1756    -89    375       C  
ATOM     35  O   LEU A 176     -42.949  -0.839  33.417  1.00 62.07           O  
ANISOU   35  O   LEU A 176     9123   8281   6180   1672   -230    282       O  
ATOM     36  CB  LEU A 176     -46.309  -0.665  33.758  1.00 64.87           C  
ANISOU   36  CB  LEU A 176     9498   8216   6933   1712     82    556       C  
ATOM     37  CG  LEU A 176     -46.907   0.636  33.212  1.00 74.39           C  
ANISOU   37  CG  LEU A 176    10586   9287   8390   1557     37    602       C  
ATOM     38  CD1 LEU A 176     -48.313   0.849  33.767  1.00 71.94           C  
ANISOU   38  CD1 LEU A 176    10316   8790   8226   1624    185    679       C  
ATOM     39  CD2 LEU A 176     -45.994   1.832  33.537  1.00 80.02           C  
ANISOU   39  CD2 LEU A 176    11271  10046   9086   1530    -85    449       C  
ATOM     40  N   LEU A 177     -43.947  -2.380  34.732  1.00 66.37           N  
ANISOU   40  N   LEU A 177     9867   8772   6579   1951     16    330       N  
ATOM     41  CA  LEU A 177     -42.775  -2.554  35.594  1.00 66.56           C  
ANISOU   41  CA  LEU A 177     9981   8938   6369   2082    -27    164       C  
ATOM     42  C   LEU A 177     -41.587  -3.075  34.799  1.00 58.23           C  
ANISOU   42  C   LEU A 177     8879   8062   5185   2001   -156    135       C  
ATOM     43  O   LEU A 177     -40.450  -2.726  35.091  1.00 58.98           O  
ANISOU   43  O   LEU A 177     8984   8273   5151   2020   -257     -4       O  
ATOM     44  CB  LEU A 177     -43.090  -3.494  36.765  1.00 76.51           C  
ANISOU   44  CB  LEU A 177    11399  10198   7474   2303    119    139       C  
ATOM     45  CG  LEU A 177     -44.487  -3.332  37.380  1.00 85.38           C  
ANISOU   45  CG  LEU A 177    12570  11139   8731   2381    274    214       C  
ATOM     46  CD1 LEU A 177     -44.853  -4.457  38.350  1.00 90.74           C  
ANISOU   46  CD1 LEU A 177    13396  11822   9258   2584    421    216       C  
ATOM     47  CD2 LEU A 177     -44.704  -1.967  38.033  1.00 88.09           C  
ANISOU   47  CD2 LEU A 177    12906  11381   9185   2391    266    132       C  
ATOM     48  N   GLY A 178     -41.868  -3.908  33.795  1.00 56.51           N  
ANISOU   48  N   GLY A 178     8609   7862   5002   1910   -152    269       N  
ATOM     49  CA  GLY A 178     -40.845  -4.430  32.894  1.00 56.96           C  
ANISOU   49  CA  GLY A 178     8607   8078   4957   1814   -272    263       C  
ATOM     50  C   GLY A 178     -39.897  -3.377  32.344  1.00 53.25           C  
ANISOU   50  C   GLY A 178     8033   7675   4524   1672   -442    178       C  
ATOM     51  O   GLY A 178     -38.686  -3.595  32.262  1.00 50.83           O  
ANISOU   51  O   GLY A 178     7730   7528   4055   1673   -545     81       O  
ATOM     52  N   GLN A 179     -40.440  -2.216  31.984  1.00 51.67           N  
ANISOU   52  N   GLN A 179     7741   7353   4538   1551   -473    212       N  
ATOM     53  CA  GLN A 179     -39.641  -1.156  31.386  1.00 46.37           C  
ANISOU   53  CA  GLN A 179     6961   6731   3926   1402   -634    145       C  
ATOM     54  C   GLN A 179     -38.863  -0.323  32.411  1.00 45.91           C  
ANISOU   54  C   GLN A 179     6958   6714   3771   1496   -682    -35       C  
ATOM     55  CB  GLN A 179     -40.546  -0.235  30.575  1.00 58.07           C  
ANISOU   55  CB  GLN A 179     8319   8063   5680   1232   -649    256       C  
ATOM     56  CG  GLN A 179     -41.720  -0.938  29.898  1.00 70.92           C  
ANISOU   56  CG  GLN A 179     9918   9591   7438   1179   -550    441       C  
ATOM     57  CD  GLN A 179     -41.297  -2.007  28.907  1.00 76.76           C  
ANISOU   57  CD  GLN A 179    10617  10447   8100   1104   -596    518       C  
ATOM     58  OE1 GLN A 179     -40.247  -1.916  28.268  1.00 78.00           O  
ANISOU   58  OE1 GLN A 179    10711  10735   8192   1007   -733    466       O  
ATOM     59  NE2 GLN A 179     -42.124  -3.031  28.774  1.00 80.51           N  
ANISOU   59  NE2 GLN A 179    11131  10875   8585   1148   -479    642       N  
ATOM     60  N   ARG A 183     -41.706   6.758  29.305  1.00 37.81           N  
ANISOU   60  N   ARG A 183     5285   5008   4071    626   -982    199       N  
ATOM     61  CA  ARG A 183     -41.788   7.095  27.882  1.00 39.60           C  
ANISOU   61  CA  ARG A 183     5362   5221   4462    402  -1081    303       C  
ATOM     62  C   ARG A 183     -42.675   6.113  27.127  1.00 44.05           C  
ANISOU   62  C   ARG A 183     5903   5734   5099    355   -997    478       C  
ATOM     63  O   ARG A 183     -42.695   6.131  25.887  1.00 44.22           O  
ANISOU   63  O   ARG A 183     5808   5765   5229    176  -1073    574       O  
ATOM     64  CB  ARG A 183     -40.404   7.107  27.256  1.00 50.70           C  
ANISOU   64  CB  ARG A 183     6709   6803   5751    310  -1243    225       C  
ATOM     65  CG  ARG A 183     -39.395   7.961  28.024  1.00 58.31           C  
ANISOU   65  CG  ARG A 183     7703   7839   6613    366  -1331     44       C  
ATOM     66  CD  ARG A 183     -38.216   8.290  27.129  1.00 60.38           C  
ANISOU   66  CD  ARG A 183     7865   8239   6838    217  -1508     -7       C  
ATOM     67  NE  ARG A 183     -37.592   7.081  26.590  1.00 52.02           N  
ANISOU   67  NE  ARG A 183     6816   7325   5625    213  -1533     22       N  
ATOM     68  CZ  ARG A 183     -36.631   6.404  27.204  1.00 48.20           C  
ANISOU   68  CZ  ARG A 183     6424   6988   4902    342  -1545    -88       C  
ATOM     69  NH1 ARG A 183     -36.198   6.806  28.381  1.00 49.96           N  
ANISOU   69  NH1 ARG A 183     6738   7231   5015    485  -1532   -231       N  
ATOM     70  NH2 ARG A 183     -36.111   5.323  26.646  1.00 56.81           N  
ANISOU   70  NH2 ARG A 183     7515   8204   5866    327  -1570    -53       N  
ATOM     71  N   PHE A 184     -43.374   5.241  27.852  1.00 40.43           N  
ANISOU   71  N   PHE A 184     5557   5228   4578    512   -844    518       N  
ATOM     72  CA  PHE A 184     -44.208   4.215  27.179  1.00 44.52           C  
ANISOU   72  CA  PHE A 184     6062   5703   5151    480   -758    684       C  
ATOM     73  C   PHE A 184     -45.601   4.340  27.707  1.00 49.01           C  
ANISOU   73  C   PHE A 184     6673   6089   5858    549   -608    765       C  
ATOM     74  O   PHE A 184     -45.800   4.891  28.782  1.00 47.04           O  
ANISOU   74  O   PHE A 184     6497   5777   5599    669   -553    680       O  
ATOM     75  CB  PHE A 184     -43.697   2.774  27.425  1.00 36.60           C  
ANISOU   75  CB  PHE A 184     5154   4836   3918    603   -714    672       C  
ATOM     76  CG  PHE A 184     -42.322   2.494  26.817  1.00 43.56           C  
ANISOU   76  CG  PHE A 184     5992   5905   4652    532   -860    604       C  
ATOM     77  CD1 PHE A 184     -41.165   2.646  27.565  1.00 46.47           C  
ANISOU   77  CD1 PHE A 184     6423   6401   4831    628   -925    436       C  
ATOM     78  CD2 PHE A 184     -42.202   2.110  25.482  1.00 39.51           C  
ANISOU   78  CD2 PHE A 184     5373   5441   4199    365   -933    709       C  
ATOM     79  CE1 PHE A 184     -39.913   2.425  26.995  1.00 49.92           C  
ANISOU   79  CE1 PHE A 184     6819   7010   5140    559  -1060    373       C  
ATOM     80  CE2 PHE A 184     -40.961   1.893  24.903  1.00 38.13           C  
ANISOU   80  CE2 PHE A 184     5154   5436   3898    295  -1068    648       C  
ATOM     81  CZ  PHE A 184     -39.809   2.033  25.661  1.00 43.05           C  
ANISOU   81  CZ  PHE A 184     5842   6186   4330    393  -1131    480       C  
ATOM     82  N   GLN A 185     -46.582   3.830  26.967  1.00 37.95           N  
ANISOU   82  N   GLN A 185     5720   4674   4024   -134   -616    404       N  
ATOM     83  CA  GLN A 185     -47.914   3.683  27.539  1.00 34.03           C  
ANISOU   83  CA  GLN A 185     5302   4236   3393   -251   -608    494       C  
ATOM     84  C   GLN A 185     -48.362   2.291  27.208  1.00 37.64           C  
ANISOU   84  C   GLN A 185     5916   4602   3784   -293   -650    570       C  
ATOM     85  O   GLN A 185     -48.422   1.938  26.039  1.00 36.52           O  
ANISOU   85  O   GLN A 185     5789   4402   3684   -299   -602    567       O  
ATOM     86  CB  GLN A 185     -48.890   4.664  26.908  1.00 38.62           C  
ANISOU   86  CB  GLN A 185     5800   4905   3967   -337   -484    498       C  
ATOM     87  CG  GLN A 185     -48.883   6.074  27.470  1.00 46.29           C  
ANISOU   87  CG  GLN A 185     6634   5992   4961   -334   -439    450       C  
ATOM     88  CD  GLN A 185     -50.067   6.880  26.936  1.00 56.13           C  
ANISOU   88  CD  GLN A 185     7827   7326   6173   -438   -323    473       C  
ATOM     89  OE1 GLN A 185     -51.221   6.585  27.243  1.00 64.94           O  
ANISOU   89  OE1 GLN A 185     9023   8476   7177   -539   -314    554       O  
ATOM     90  NE2 GLN A 185     -49.783   7.888  26.125  1.00 56.24           N  
ANISOU   90  NE2 GLN A 185     7708   7374   6285   -412   -233    402       N  
ATOM     91  N   VAL A 186     -48.684   1.493  28.220  1.00 36.56           N  
ANISOU   91  N   VAL A 186     5897   4450   3542   -322   -738    638       N  
ATOM     92  CA  VAL A 186     -49.138   0.128  27.970  1.00 42.41           C  
ANISOU   92  CA  VAL A 186     6795   5104   4215   -364   -783    715       C  
ATOM     93  C   VAL A 186     -50.644   0.104  27.901  1.00 43.33           C  
ANISOU   93  C   VAL A 186     6966   5275   4223   -499   -726    799       C  
ATOM     94  O   VAL A 186     -51.317   0.612  28.807  1.00 42.97           O  
ANISOU   94  O   VAL A 186     6908   5318   4099   -557   -722    833       O  
ATOM     95  CB  VAL A 186     -48.668  -0.805  29.082  1.00 42.57           C  
ANISOU   95  CB  VAL A 186     6922   5073   4179   -322   -913    746       C  
ATOM     96  CG1 VAL A 186     -49.160  -2.233  28.806  1.00 40.73           C  
ANISOU   96  CG1 VAL A 186     6853   4747   3874   -369   -959    828       C  
ATOM     97  CG2 VAL A 186     -47.144  -0.721  29.193  1.00 44.86           C  
ANISOU   97  CG2 VAL A 186     7151   5313   4579   -186   -970    659       C  
ATOM     98  N   LEU A 187     -51.191  -0.465  26.825  1.00 38.30           N  
ANISOU   98  N   LEU A 187     6385   4584   3581   -549   -680    833       N  
ATOM     99  CA  LEU A 187     -52.618  -0.312  26.581  1.00 41.65           C  
ANISOU   99  CA  LEU A 187     6838   5067   3921   -676   -607    902       C  
ATOM    100  C   LEU A 187     -53.187  -1.671  26.356  1.00 46.97           C  
ANISOU  100  C   LEU A 187     7671   5657   4519   -729   -651    985       C  
ATOM    101  O   LEU A 187     -52.585  -2.463  25.629  1.00 44.48           O  
ANISOU  101  O   LEU A 187     7405   5239   4258   -676   -679    969       O  
ATOM    102  CB  LEU A 187     -52.884   0.508  25.322  1.00 38.01           C  
ANISOU  102  CB  LEU A 187     6273   4636   3532   -697   -484    859       C  
ATOM    103  CG  LEU A 187     -52.130   1.832  25.197  1.00 41.91           C  
ANISOU  103  CG  LEU A 187     6598   5193   4132   -628   -430    760       C  
ATOM    104  CD1 LEU A 187     -52.570   2.484  23.901  1.00 44.85           C  
ANISOU  104  CD1 LEU A 187     6892   5590   4561   -665   -308    734       C  
ATOM    105  CD2 LEU A 187     -52.450   2.715  26.379  1.00 39.44           C  
ANISOU  105  CD2 LEU A 187     6227   4992   3766   -655   -434    764       C  
ATOM    106  N   PRO A 188     -54.351  -1.937  26.974  1.00 55.99           N  
ANISOU  106  N   PRO A 188     8893   6842   5537   -834   -657   1073       N  
ATOM    107  CA  PRO A 188     -55.068  -3.202  26.827  1.00 57.44           C  
ANISOU  107  CA  PRO A 188     9177   6962   5685   -879   -676   1126       C  
ATOM    108  C   PRO A 188     -55.769  -3.193  25.480  1.00 50.35           C  
ANISOU  108  C   PRO A 188     8234   6055   4841   -921   -573   1110       C  
ATOM    109  O   PRO A 188     -56.355  -2.167  25.091  1.00 49.25           O  
ANISOU  109  O   PRO A 188     7986   6000   4728   -960   -474   1082       O  
ATOM    110  CB  PRO A 188     -56.112  -3.134  27.950  1.00 60.44           C  
ANISOU  110  CB  PRO A 188     9508   7428   6029   -927   -660   1137       C  
ATOM    111  CG  PRO A 188     -56.410  -1.668  28.083  1.00 65.59           C  
ANISOU  111  CG  PRO A 188    10038   8195   6690   -952   -583   1107       C  
ATOM    112  CD  PRO A 188     -55.079  -0.986  27.839  1.00 62.08           C  
ANISOU  112  CD  PRO A 188     9604   7738   6246   -896   -621   1091       C  
ATOM    113  N   GLY A 189     -55.697  -4.311  24.774  1.00 48.08           N  
ANISOU  113  N   GLY A 189     8026   5669   4574   -909   -597   1123       N  
ATOM    114  CA  GLY A 189     -56.423  -4.447  23.524  1.00 44.64           C  
ANISOU  114  CA  GLY A 189     7550   5222   4188   -945   -509   1106       C  
ATOM    115  C   GLY A 189     -57.609  -5.394  23.637  1.00 51.04           C  
ANISOU  115  C   GLY A 189     8368   6034   4990   -990   -500   1119       C  
ATOM    116  O   GLY A 189     -57.569  -6.397  24.377  1.00 46.15           O  
ANISOU  116  O   GLY A 189     7829   5372   4333   -982   -579   1149       O  
ATOM    117  N   ARG A 190     -58.657  -5.074  22.885  1.00 47.95           N  
ANISOU  117  N   ARG A 190     7892   5691   4638  -1031   -407   1095       N  
ATOM    118  CA  ARG A 190     -59.830  -5.926  22.742  1.00 50.94           C  
ANISOU  118  CA  ARG A 190     8270   6066   5018  -1067   -393   1101       C  
ATOM    119  C   ARG A 190     -59.539  -7.324  22.193  1.00 56.56           C  
ANISOU  119  C   ARG A 190     9088   6672   5731  -1051   -447   1121       C  
ATOM    120  O   ARG A 190     -60.416  -8.184  22.230  1.00 58.96           O  
ANISOU  120  O   ARG A 190     9409   6967   6025  -1080   -452   1132       O  
ATOM    121  CB  ARG A 190     -60.850  -5.235  21.847  1.00 49.15           C  
ANISOU  121  CB  ARG A 190     7931   5901   4843  -1094   -291   1062       C  
ATOM    122  CG  ARG A 190     -61.419  -3.975  22.456  1.00 47.30           C  
ANISOU  122  CG  ARG A 190     7587   5773   4613  -1110   -238   1040       C  
ATOM    123  CD  ARG A 190     -62.478  -3.387  21.537  1.00 53.37           C  
ANISOU  123  CD  ARG A 190     8249   6590   5439  -1123   -148    998       C  
ATOM    124  NE  ARG A 190     -61.942  -3.231  20.188  1.00 54.53           N  
ANISOU  124  NE  ARG A 190     8386   6699   5636  -1103   -107    974       N  
ATOM    125  CZ  ARG A 190     -61.429  -2.097  19.713  1.00 53.65           C  
ANISOU  125  CZ  ARG A 190     8204   6621   5560  -1086    -52    942       C  
ATOM    126  NH1 ARG A 190     -61.399  -1.013  20.472  1.00 51.29           N  
ANISOU  126  NH1 ARG A 190     7836   6399   5253  -1089    -33    929       N  
ATOM    127  NH2 ARG A 190     -60.955  -2.052  18.473  1.00 54.98           N  
ANISOU  127  NH2 ARG A 190     8367   6746   5775  -1067    -14    923       N  
ATOM    128  N   ASP A 191     -58.337  -7.536  21.659  1.00 56.51           N  
ANISOU  128  N   ASP A 191     9150   6583   5739  -1003   -486   1122       N  
ATOM    129  CA  ASP A 191     -57.931  -8.849  21.161  1.00 53.94           C  
ANISOU  129  CA  ASP A 191     8928   6148   5417   -978   -544   1137       C  
ATOM    130  C   ASP A 191     -57.162  -9.609  22.241  1.00 58.85           C  
ANISOU  130  C   ASP A 191     9652   6714   5992   -942   -657   1169       C  
ATOM    131  O   ASP A 191     -56.422 -10.549  21.947  1.00 60.16           O  
ANISOU  131  O   ASP A 191     9913   6780   6165   -898   -723   1178       O  
ATOM    132  CB  ASP A 191     -57.041  -8.688  19.927  1.00 52.69           C  
ANISOU  132  CB  ASP A 191     8789   5920   5312   -933   -525   1117       C  
ATOM    133  CG  ASP A 191     -55.799  -7.835  20.196  1.00 45.71           C  
ANISOU  133  CG  ASP A 191     7916   5019   4432   -879   -554   1112       C  
ATOM    134  OD1 ASP A 191     -55.632  -7.312  21.331  1.00 43.91           O  
ANISOU  134  OD1 ASP A 191     7676   4846   4163   -878   -587   1123       O  
ATOM    135  OD2 ASP A 191     -54.975  -7.686  19.261  1.00 47.35           O  
ANISOU  135  OD2 ASP A 191     8146   5158   4688   -832   -544   1096       O  
ATOM    136  N   LYS A 192     -57.305  -9.156  23.485  1.00 60.32           N  
ANISOU  136  N   LYS A 192     9815   6967   6136   -954   -679   1182       N  
ATOM    137  CA  LYS A 192     -56.511  -9.665  24.600  1.00 66.78           C  
ANISOU  137  CA  LYS A 192    10717   7746   6912   -912   -786   1206       C  
ATOM    138  C   LYS A 192     -54.980  -9.483  24.489  1.00 69.40           C  
ANISOU  138  C   LYS A 192    11108   8004   7258   -827   -856   1199       C  
ATOM    139  O   LYS A 192     -54.239 -10.061  25.290  1.00 77.54           O  
ANISOU  139  O   LYS A 192    12215   8985   8262   -777   -956   1213       O  
ATOM    140  CB  LYS A 192     -56.851 -11.135  24.876  1.00 67.89           C  
ANISOU  140  CB  LYS A 192    10940   7826   7029   -923   -842   1232       C  
ATOM    141  CG  LYS A 192     -58.333 -11.367  25.144  1.00 79.15           C  
ANISOU  141  CG  LYS A 192    12315   9318   8438   -996   -788   1240       C  
ATOM    142  CD  LYS A 192     -58.805 -10.575  26.358  1.00 84.92           C  
ANISOU  142  CD  LYS A 192    12985  10146   9134  -1020   -775   1247       C  
ATOM    143  CE  LYS A 192     -60.060 -11.192  26.967  1.00 89.13           C  
ANISOU  143  CE  LYS A 192    13509  10714   9642  -1073   -763   1266       C  
ATOM    144  NZ  LYS A 192     -60.446 -10.508  28.232  1.00 88.16           N  
ANISOU  144  NZ  LYS A 192    13337  10675   9485  -1089   -759   1274       N  
ATOM    145  N   MET A 193     -54.496  -8.701  23.520  1.00 55.10           N  
ANISOU  145  N   MET A 193     9260   6181   5492   -804   -809   1174       N  
ATOM    146  CA  MET A 193     -53.066  -8.367  23.490  1.00 51.80           C  
ANISOU  146  CA  MET A 193     8889   5699   5094   -712   -877   1163       C  
ATOM    147  C   MET A 193     -52.781  -7.150  24.371  1.00 47.09           C  
ANISOU  147  C   MET A 193     8218   5194   4481   -699   -877   1147       C  
ATOM    148  O   MET A 193     -53.685  -6.374  24.710  1.00 50.43           O  
ANISOU  148  O   MET A 193     8565   5724   4871   -772   -808   1154       O  
ATOM    149  CB  MET A 193     -52.547  -8.135  22.061  1.00 48.73           C  
ANISOU  149  CB  MET A 193     8478   5248   4787   -672   -825   1127       C  
ATOM    150  CG  MET A 193     -52.457  -9.391  21.202  1.00 53.18           C  
ANISOU  150  CG  MET A 193     9136   5698   5371   -657   -853   1141       C  
ATOM    151  SD  MET A 193     -51.311 -10.652  21.854  1.00 74.95           S  
ANISOU  151  SD  MET A 193    12021   8334   8122   -560  -1006   1152       S  
ATOM    152  CE  MET A 193     -49.697 -10.068  21.328  1.00 57.42           C  
ANISOU  152  CE  MET A 193     9678   6083   6056   -411  -1002   1031       C  
ATOM    153  N   LEU A 194     -51.527  -7.015  24.773  1.00 49.37           N  
ANISOU  153  N   LEU A 194     8458   5459   4841   -586   -935   1079       N  
ATOM    154  CA  LEU A 194     -51.067  -5.796  25.434  1.00 50.58           C  
ANISOU  154  CA  LEU A 194     8479   5705   5035   -544   -914   1016       C  
ATOM    155  C   LEU A 194     -50.272  -5.025  24.406  1.00 45.77           C  
ANISOU  155  C   LEU A 194     7738   5092   4561   -469   -844    920       C  
ATOM    156  O   LEU A 194     -49.377  -5.585  23.752  1.00 43.24           O  
ANISOU  156  O   LEU A 194     7433   4678   4317   -388   -873    880       O  
ATOM    157  CB  LEU A 194     -50.176  -6.097  26.649  1.00 51.15           C  
ANISOU  157  CB  LEU A 194     8577   5759   5097   -466  -1028   1002       C  
ATOM    158  CG  LEU A 194     -50.889  -6.449  27.963  1.00 54.67           C  
ANISOU  158  CG  LEU A 194     9113   6245   5413   -532  -1091   1082       C  
ATOM    159  CD1 LEU A 194     -49.878  -6.871  29.033  1.00 52.06           C  
ANISOU  159  CD1 LEU A 194     8817   5878   5084   -441  -1208   1063       C  
ATOM    160  CD2 LEU A 194     -51.758  -5.293  28.466  1.00 53.47           C  
ANISOU  160  CD2 LEU A 194     8877   6225   5213   -608  -1019   1094       C  
ATOM    161  N   TYR A 195     -50.586  -3.737  24.280  1.00 43.80           N  
ANISOU  161  N   TYR A 195     7359   4944   4339   -496   -752    883       N  
ATOM    162  CA  TYR A 195     -49.959  -2.894  23.293  1.00 37.52           C  
ANISOU  162  CA  TYR A 195     6431   4156   3667   -437   -672    796       C  
ATOM    163  C   TYR A 195     -49.076  -1.886  24.007  1.00 41.77           C  
ANISOU  163  C   TYR A 195     6845   4757   4269   -358   -684    720       C  
ATOM    164  O   TYR A 195     -49.552  -1.129  24.844  1.00 40.84           O  
ANISOU  164  O   TYR A 195     6680   4737   4101   -401   -669    731       O  
ATOM    165  CB  TYR A 195     -51.039  -2.172  22.471  1.00 33.30           C  
ANISOU  165  CB  TYR A 195     5842   3690   3122   -531   -549    811       C  
ATOM    166  CG  TYR A 195     -51.651  -3.110  21.465  1.00 33.54           C  
ANISOU  166  CG  TYR A 195     5974   3643   3126   -584   -529    863       C  
ATOM    167  CD1 TYR A 195     -51.057  -3.283  20.221  1.00 34.58           C  
ANISOU  167  CD1 TYR A 195     6081   3703   3356   -526   -493    813       C  
ATOM    168  CD2 TYR A 195     -52.786  -3.877  21.774  1.00 40.58           C  
ANISOU  168  CD2 TYR A 195     6992   4529   3896   -688   -551    962       C  
ATOM    169  CE1 TYR A 195     -51.586  -4.198  19.283  1.00 38.53           C  
ANISOU  169  CE1 TYR A 195     6680   4127   3834   -570   -480    860       C  
ATOM    170  CE2 TYR A 195     -53.317  -4.782  20.842  1.00 40.74           C  
ANISOU  170  CE2 TYR A 195     7111   4475   3896   -733   -537   1009       C  
ATOM    171  CZ  TYR A 195     -52.696  -4.933  19.612  1.00 39.52           C  
ANISOU  171  CZ  TYR A 195     6928   4248   3840   -672   -503    957       C  
ATOM    172  OH  TYR A 195     -53.186  -5.814  18.675  1.00 43.75           O  
ANISOU  172  OH  TYR A 195     7558   4707   4358   -712   -491   1000       O  
ATOM    173  N   VAL A 196     -47.798  -1.896  23.672  1.00 36.40           N  
ANISOU  173  N   VAL A 196     6113   4018   3698   -243   -711    643       N  
ATOM    174  CA  VAL A 196     -46.869  -0.944  24.263  1.00 37.87           C  
ANISOU  174  CA  VAL A 196     6176   4256   3957   -161   -722    564       C  
ATOM    175  C   VAL A 196     -46.627   0.206  23.267  1.00 34.34           C  
ANISOU  175  C   VAL A 196     5576   3853   3619   -137   -610    488       C  
ATOM    176  O   VAL A 196     -45.954   0.008  22.272  1.00 31.01           O  
ANISOU  176  O   VAL A 196     5131   3363   3289    -75   -589    441       O  
ATOM    177  CB  VAL A 196     -45.552  -1.662  24.601  1.00 35.34           C  
ANISOU  177  CB  VAL A 196     5891   3846   3691    -43   -828    526       C  
ATOM    178  CG1 VAL A 196     -44.509  -0.704  25.195  1.00 35.14           C  
ANISOU  178  CG1 VAL A 196     5737   3868   3748     49   -843    440       C  
ATOM    179  CG2 VAL A 196     -45.832  -2.825  25.569  1.00 36.98           C  
ANISOU  179  CG2 VAL A 196     6254   4009   3787    -70   -937    605       C  
ATOM    180  N   ALA A 197     -47.130   1.404  23.549  1.00 34.80           N  
ANISOU  180  N   ALA A 197     5531   4023   3669   -182   -540    473       N  
ATOM    181  CA  ALA A 197     -46.906   2.555  22.643  1.00 31.45           C  
ANISOU  181  CA  ALA A 197     4957   3645   3347   -160   -432    399       C  
ATOM    182  C   ALA A 197     -45.596   3.264  22.955  1.00 37.88           C  
ANISOU  182  C   ALA A 197     5653   4470   4270    -45   -455    305       C  
ATOM    183  O   ALA A 197     -45.410   3.750  24.074  1.00 32.65           O  
ANISOU  183  O   ALA A 197     4954   3867   3584    -30   -498    294       O  
ATOM    184  CB  ALA A 197     -48.049   3.560  22.762  1.00 34.95           C  
ANISOU  184  CB  ALA A 197     5338   4206   3735   -262   -343    423       C  
ATOM    185  N   ALA A 198     -44.684   3.316  21.981  1.00 32.92           N  
ANISOU  185  N   ALA A 198     4965   3783   3761     38   -429    237       N  
ATOM    186  CA  ALA A 198     -43.397   3.977  22.174  1.00 34.59           C  
ANISOU  186  CA  ALA A 198     5060   3997   4085    151   -447    144       C  
ATOM    187  C   ALA A 198     -43.384   5.270  21.338  1.00 36.00           C  
ANISOU  187  C   ALA A 198     5083   4241   4354    153   -327     80       C  
ATOM    188  O   ALA A 198     -44.166   5.439  20.375  1.00 33.24           O  
ANISOU  188  O   ALA A 198     4728   3905   3998     86   -235    100       O  
ATOM    189  CB  ALA A 198     -42.254   3.057  21.740  1.00 28.79           C  
ANISOU  189  CB  ALA A 198     4370   3143   3424    254   -513    111       C  
ATOM    190  N   GLN A 199     -42.482   6.163  21.675  1.00 38.12           N  
ANISOU  190  N   GLN A 199     5227   4547   4709    231   -327      2       N  
ATOM    191  CA  GLN A 199     -42.462   7.483  21.085  1.00 37.84           C  
ANISOU  191  CA  GLN A 199     5039   4585   4754    232   -220    -60       C  
ATOM    192  C   GLN A 199     -41.595   7.554  19.837  1.00 43.29           C  
ANISOU  192  C   GLN A 199     5662   5211   5574    311   -172   -128       C  
ATOM    193  O   GLN A 199     -41.634   8.550  19.092  1.00 38.93           O  
ANISOU  193  O   GLN A 199     4991   4707   5093    308    -71   -175       O  
ATOM    194  CB  GLN A 199     -41.896   8.467  22.116  1.00 34.88           C  
ANISOU  194  CB  GLN A 199     4557   4286   4410    279   -246   -113       C  
ATOM    195  CG  GLN A 199     -42.761   8.615  23.353  1.00 38.10           C  
ANISOU  195  CG  GLN A 199     5008   4773   4695    202   -281    -53       C  
ATOM    196  CD  GLN A 199     -42.217   9.653  24.331  1.00 51.24           C  
ANISOU  196  CD  GLN A 199     6560   6515   6393    249   -302   -108       C  
ATOM    197  OE1 GLN A 199     -40.994   9.783  24.545  1.00 49.09           O  
ANISOU  197  OE1 GLN A 199     6230   6211   6212    356   -350   -176       O  
ATOM    198  NE2 GLN A 199     -43.126  10.395  24.934  1.00 52.03           N  
ANISOU  198  NE2 GLN A 199     6630   6718   6419    170   -266    -79       N  
ATOM    199  N   ASN A 200     -40.766   6.538  19.628  1.00 36.78           N  
ANISOU  199  N   ASN A 200     4908   4279   4785    386   -244   -136       N  
ATOM    200  CA  ASN A 200     -39.820   6.578  18.512  1.00 36.71           C  
ANISOU  200  CA  ASN A 200     4836   4207   4905    473   -208   -204       C  
ATOM    201  C   ASN A 200     -39.162   5.221  18.252  1.00 40.60           C  
ANISOU  201  C   ASN A 200     5442   4574   5408    534   -291   -192       C  
ATOM    202  O   ASN A 200     -39.369   4.250  18.996  1.00 38.80           O  
ANISOU  202  O   ASN A 200     5342   4309   5091    515   -383   -133       O  
ATOM    203  CB  ASN A 200     -38.726   7.614  18.782  1.00 46.23           C  
ANISOU  203  CB  ASN A 200     5891   5450   6223    566   -202   -298       C  
ATOM    204  CG  ASN A 200     -38.007   7.349  20.094  1.00 48.69           C  
ANISOU  204  CG  ASN A 200     6226   5754   6519    625   -320   -307       C  
ATOM    205  OD1 ASN A 200     -37.332   6.322  20.250  1.00 52.52           O  
ANISOU  205  OD1 ASN A 200     6797   6148   7009    686   -409   -302       O  
ATOM    206  ND2 ASN A 200     -38.189   8.232  21.057  1.00 51.21           N  
ANISOU  206  ND2 ASN A 200     6478   6168   6813    606   -323   -317       N  
ATOM    207  N   GLU A 201     -38.332   5.183  17.214  1.00 44.17           N  
ANISOU  207  N   GLU A 201     5845   4964   5972    611   -259   -249       N  
ATOM    208  CA  GLU A 201     -37.710   3.940  16.775  1.00 45.66           C  
ANISOU  208  CA  GLU A 201     6135   5034   6182    672   -325   -242       C  
ATOM    209  C   GLU A 201     -36.786   3.315  17.812  1.00 41.02           C  
ANISOU  209  C   GLU A 201     5596   4399   5592    750   -453   -253       C  
ATOM    210  O   GLU A 201     -36.874   2.135  18.085  1.00 39.52           O  
ANISOU  210  O   GLU A 201     5543   4138   5336    744   -534   -200       O  
ATOM    211  CB  GLU A 201     -36.905   4.192  15.506  1.00 50.82           C  
ANISOU  211  CB  GLU A 201     6703   5639   6966    748   -261   -312       C  
ATOM    212  CG  GLU A 201     -36.062   2.994  15.102  1.00 60.91           C  
ANISOU  212  CG  GLU A 201     8069   6793   8280    829   -334   -318       C  
ATOM    213  CD  GLU A 201     -35.209   3.313  13.913  1.00 70.02           C  
ANISOU  213  CD  GLU A 201     9130   7905   9567    910   -271   -391       C  
ATOM    214  OE1 GLU A 201     -34.506   4.346  13.960  1.00 77.57           O  
ANISOU  214  OE1 GLU A 201     9945   8909  10618    969   -236   -465       O  
ATOM    215  OE2 GLU A 201     -35.264   2.555  12.925  1.00 73.05           O  
ANISOU  215  OE2 GLU A 201     9582   8212   9962    915   -255   -375       O  
ATOM    216  N   ARG A 202     -35.884   4.108  18.375  1.00 45.57           N  
ANISOU  216  N   ARG A 202     6637   4885   5794    614  -1811   -563       N  
ATOM    217  CA  ARG A 202     -34.917   3.588  19.340  1.00 39.82           C  
ANISOU  217  CA  ARG A 202     5889   4214   5027    707  -1869   -597       C  
ATOM    218  C   ARG A 202     -35.631   2.892  20.478  1.00 50.66           C  
ANISOU  218  C   ARG A 202     7371   5576   6299    766  -1892   -607       C  
ATOM    219  O   ARG A 202     -35.236   1.787  20.875  1.00 49.37           O  
ANISOU  219  O   ARG A 202     7255   5439   6064    853  -1898   -599       O  
ATOM    220  CB  ARG A 202     -34.033   4.724  19.879  1.00 50.12           C  
ANISOU  220  CB  ARG A 202     7072   5562   6410    689  -1940   -656       C  
ATOM    221  CG  ARG A 202     -32.924   4.282  20.823  1.00 60.97           C  
ANISOU  221  CG  ARG A 202     8411   6999   7755    780  -2003   -693       C  
ATOM    222  CD  ARG A 202     -31.969   5.440  21.153  1.00 72.85           C  
ANISOU  222  CD  ARG A 202     9785   8548   9347    755  -2066   -746       C  
ATOM    223  NE  ARG A 202     -32.469   6.292  22.236  1.00 79.92           N  
ANISOU  223  NE  ARG A 202    10681   9437  10247    732  -2123   -794       N  
ATOM    224  CZ  ARG A 202     -31.928   7.455  22.613  1.00 81.58           C  
ANISOU  224  CZ  ARG A 202    10791   9675  10533    696  -2178   -842       C  
ATOM    225  NH1 ARG A 202     -32.470   8.135  23.621  1.00 78.91           N  
ANISOU  225  NH1 ARG A 202    10465   9328  10190    677  -2226   -883       N  
ATOM    226  NH2 ARG A 202     -30.856   7.946  21.991  1.00 72.23           N  
ANISOU  226  NH2 ARG A 202     9493   8526   9426    677  -2184   -850       N  
ATOM    227  N   ASP A 203     -36.695   3.512  20.998  1.00 44.98           N  
ANISOU  227  N   ASP A 203     6696   4819   5574    719  -1904   -623       N  
ATOM    228  CA  ASP A 203     -37.414   2.917  22.130  1.00 42.06           C  
ANISOU  228  CA  ASP A 203     6431   4440   5111    771  -1929   -635       C  
ATOM    229  C   ASP A 203     -38.194   1.693  21.740  1.00 38.78           C  
ANISOU  229  C   ASP A 203     6137   3988   4607    802  -1866   -581       C  
ATOM    230  O   ASP A 203     -38.398   0.790  22.575  1.00 41.08           O  
ANISOU  230  O   ASP A 203     6512   4288   4808    875  -1883   -584       O  
ATOM    231  CB  ASP A 203     -38.349   3.923  22.803  1.00 37.64           C  
ANISOU  231  CB  ASP A 203     5883   3849   4568    712  -1960   -668       C  
ATOM    232  CG  ASP A 203     -37.583   5.009  23.585  1.00 49.99           C  
ANISOU  232  CG  ASP A 203     7342   5455   6198    702  -2037   -732       C  
ATOM    233  OD1 ASP A 203     -36.350   4.849  23.838  1.00 44.64           O  
ANISOU  233  OD1 ASP A 203     6593   4833   5534    756  -2076   -754       O  
ATOM    234  OD2 ASP A 203     -38.240   6.019  23.933  1.00 52.40           O  
ANISOU  234  OD2 ASP A 203     7636   5736   6539    640  -2059   -758       O  
ATOM    235  N   THR A 204     -38.694   1.687  20.499  1.00 40.67           N  
ANISOU  235  N   THR A 204     6393   4188   4873    742  -1794   -531       N  
ATOM    236  CA  THR A 204     -39.472   0.552  19.999  1.00 36.38           C  
ANISOU  236  CA  THR A 204     5966   3607   4251    763  -1728   -475       C  
ATOM    237  C   THR A 204     -38.601  -0.693  19.958  1.00 38.81           C  
ANISOU  237  C   THR A 204     6290   3953   4503    857  -1721   -457       C  
ATOM    238  O   THR A 204     -38.996  -1.731  20.452  1.00 40.28           O  
ANISOU  238  O   THR A 204     6576   4133   4594    920  -1714   -442       O  
ATOM    239  CB  THR A 204     -40.044   0.817  18.580  1.00 32.33           C  
ANISOU  239  CB  THR A 204     5453   3047   3785    680  -1651   -424       C  
ATOM    240  OG1 THR A 204     -40.954   1.935  18.620  1.00 40.67           O  
ANISOU  240  OG1 THR A 204     6503   4064   4887    593  -1655   -438       O  
ATOM    241  CG2 THR A 204     -40.789  -0.380  18.116  1.00 36.05           C  
ANISOU  241  CG2 THR A 204     6043   3483   4171    706  -1585   -367       C  
ATOM    242  N   LEU A 205     -37.414  -0.572  19.368  1.00 45.34           N  
ANISOU  242  N   LEU A 205     7019   4819   5391    864  -1723   -458       N  
ATOM    243  CA  LEU A 205     -36.455  -1.688  19.285  1.00 42.27           C  
ANISOU  243  CA  LEU A 205     6631   4470   4958    952  -1718   -444       C  
ATOM    244  C   LEU A 205     -36.011  -2.129  20.684  1.00 40.42           C  
ANISOU  244  C   LEU A 205     6415   4278   4663   1040  -1788   -486       C  
ATOM    245  O   LEU A 205     -35.921  -3.337  20.985  1.00 40.43           O  
ANISOU  245  O   LEU A 205     6491   4291   4580   1121  -1780   -469       O  
ATOM    246  CB  LEU A 205     -35.228  -1.247  18.468  1.00 42.25           C  
ANISOU  246  CB  LEU A 205     6502   4504   5045    934  -1717   -446       C  
ATOM    247  CG  LEU A 205     -35.562  -0.881  17.019  1.00 44.10           C  
ANISOU  247  CG  LEU A 205     6715   4701   5341    850  -1646   -402       C  
ATOM    248  CD1 LEU A 205     -34.326  -0.526  16.181  1.00 41.83           C  
ANISOU  248  CD1 LEU A 205     6307   4451   5138    836  -1643   -403       C  
ATOM    249  CD2 LEU A 205     -36.338  -2.034  16.368  1.00 41.05           C  
ANISOU  249  CD2 LEU A 205     6445   4274   4880    866  -1571   -340       C  
ATOM    250  N   TRP A 206     -35.759  -1.159  21.555  1.00 38.54           N  
ANISOU  250  N   TRP A 206     6113   4063   4468   1025  -1857   -543       N  
ATOM    251  CA  TRP A 206     -35.348  -1.490  22.918  1.00 48.18           C  
ANISOU  251  CA  TRP A 206     7348   5324   5635   1105  -1926   -586       C  
ATOM    252  C   TRP A 206     -36.419  -2.316  23.633  1.00 46.76           C  
ANISOU  252  C   TRP A 206     7305   5113   5349   1143  -1919   -574       C  
ATOM    253  O   TRP A 206     -36.111  -3.351  24.233  1.00 44.07           O  
ANISOU  253  O   TRP A 206     7017   4796   4930   1231  -1935   -574       O  
ATOM    254  CB  TRP A 206     -34.984  -0.236  23.734  1.00 48.21           C  
ANISOU  254  CB  TRP A 206     7261   5353   5703   1075  -2000   -649       C  
ATOM    255  CG  TRP A 206     -34.541  -0.597  25.127  1.00 47.63           C  
ANISOU  255  CG  TRP A 206     7201   5321   5574   1156  -2072   -692       C  
ATOM    256  CD1 TRP A 206     -33.293  -1.023  25.500  1.00 49.89           C  
ANISOU  256  CD1 TRP A 206     7433   5666   5856   1230  -2111   -712       C  
ATOM    257  CD2 TRP A 206     -35.345  -0.610  26.327  1.00 47.97           C  
ANISOU  257  CD2 TRP A 206     7320   5350   5556   1174  -2110   -720       C  
ATOM    258  NE1 TRP A 206     -33.268  -1.267  26.854  1.00 53.30           N  
ANISOU  258  NE1 TRP A 206     7900   6121   6230   1291  -2173   -751       N  
ATOM    259  CE2 TRP A 206     -34.511  -1.026  27.383  1.00 56.13           C  
ANISOU  259  CE2 TRP A 206     8338   6436   6552   1258  -2174   -757       C  
ATOM    260  CE3 TRP A 206     -36.675  -0.290  26.611  1.00 50.31           C  
ANISOU  260  CE3 TRP A 206     7694   5596   5827   1127  -2099   -718       C  
ATOM    261  CZ2 TRP A 206     -34.970  -1.137  28.701  1.00 53.04           C  
ANISOU  261  CZ2 TRP A 206     8007   6047   6099   1295  -2225   -791       C  
ATOM    262  CZ3 TRP A 206     -37.127  -0.397  27.918  1.00 51.40           C  
ANISOU  262  CZ3 TRP A 206     7890   5736   5903   1163  -2149   -753       C  
ATOM    263  CH2 TRP A 206     -36.279  -0.817  28.942  1.00 51.91           C  
ANISOU  263  CH2 TRP A 206     7939   5853   5932   1246  -2211   -789       C  
ATOM    264  N   ALA A 207     -37.680  -1.887  23.547  1.00 40.63           N  
ANISOU  264  N   ALA A 207     6589   4283   4568   1079  -1893   -563       N  
ATOM    265  CA  ALA A 207     -38.736  -2.578  24.280  1.00 43.44           C  
ANISOU  265  CA  ALA A 207     7072   4609   4825   1110  -1890   -555       C  
ATOM    266  C   ALA A 207     -38.958  -3.936  23.674  1.00 46.73           C  
ANISOU  266  C   ALA A 207     7581   5010   5166   1157  -1827   -499       C  
ATOM    267  O   ALA A 207     -39.313  -4.911  24.372  1.00 46.67           O  
ANISOU  267  O   ALA A 207     7670   5001   5061   1224  -1834   -493       O  
ATOM    268  CB  ALA A 207     -40.011  -1.810  24.241  1.00 40.55           C  
ANISOU  268  CB  ALA A 207     6746   4189   4474   1028  -1873   -553       C  
ATOM    269  N   ARG A 208     -38.766  -4.011  22.362  1.00 35.38           N  
ANISOU  269  N   ARG A 208     6113   3559   3770   1121  -1766   -455       N  
ATOM    270  CA  ARG A 208     -38.852  -5.335  21.715  1.00 38.65           C  
ANISOU  270  CA  ARG A 208     6608   3962   4116   1168  -1705   -400       C  
ATOM    271  C   ARG A 208     -37.748  -6.304  22.205  1.00 44.12           C  
ANISOU  271  C   ARG A 208     7293   4710   4763   1273  -1736   -410       C  
ATOM    272  O   ARG A 208     -38.049  -7.470  22.491  1.00 50.66           O  
ANISOU  272  O   ARG A 208     8220   5532   5496   1338  -1719   -387       O  
ATOM    273  CB  ARG A 208     -38.833  -5.213  20.188  1.00 37.06           C  
ANISOU  273  CB  ARG A 208     6373   3736   3973   1107  -1632   -352       C  
ATOM    274  CG  ARG A 208     -40.209  -4.860  19.623  1.00 35.89           C  
ANISOU  274  CG  ARG A 208     6289   3522   3825   1024  -1579   -319       C  
ATOM    275  CD  ARG A 208     -40.185  -4.724  18.107  1.00 42.77           C  
ANISOU  275  CD  ARG A 208     7127   4370   4755    962  -1508   -271       C  
ATOM    276  NE  ARG A 208     -41.474  -4.207  17.632  1.00 45.34           N  
ANISOU  276  NE  ARG A 208     7501   4634   5091    876  -1464   -247       N  
ATOM    277  CZ  ARG A 208     -41.620  -3.430  16.557  1.00 44.32           C  
ANISOU  277  CZ  ARG A 208     7316   4480   5044    789  -1425   -227       C  
ATOM    278  NH1 ARG A 208     -42.829  -2.981  16.237  1.00 38.18           N  
ANISOU  278  NH1 ARG A 208     6588   3646   4271    716  -1390   -207       N  
ATOM    279  NH2 ARG A 208     -40.563  -3.082  15.822  1.00 42.22           N  
ANISOU  279  NH2 ARG A 208     6943   4243   4855    774  -1421   -227       N  
ATOM    280  N   GLN A 209     -36.506  -5.826  22.233  1.00 47.34           N  
ANISOU  280  N   GLN A 209     7583   5167   5237   1286  -1776   -441       N  
ATOM    281  CA  GLN A 209     -35.350  -6.558  22.788  1.00 44.56           C  
ANISOU  281  CA  GLN A 209     7205   4872   4853   1381  -1816   -460       C  
ATOM    282  C   GLN A 209     -35.694  -7.055  24.182  1.00 49.29           C  
ANISOU  282  C   GLN A 209     7882   5481   5365   1447  -1868   -489       C  
ATOM    283  O   GLN A 209     -35.630  -8.267  24.457  1.00 45.21           O  
ANISOU  283  O   GLN A 209     7443   4974   4763   1526  -1858   -470       O  
ATOM    284  CB  GLN A 209     -34.119  -5.647  22.890  1.00 49.70           C  
ANISOU  284  CB  GLN A 209     7715   5574   5596   1372  -1869   -503       C  
ATOM    285  CG  GLN A 209     -33.533  -5.109  21.573  1.00 56.83           C  
ANISOU  285  CG  GLN A 209     8522   6479   6592   1313  -1829   -481       C  
ATOM    286  CD  GLN A 209     -32.757  -6.179  20.826  1.00 72.45           C  
ANISOU  286  CD  GLN A 209    10501   8479   8548   1370  -1789   -443       C  
ATOM    287  OE1 GLN A 209     -31.806  -6.766  21.362  1.00 81.02           O  
ANISOU  287  OE1 GLN A 209    11564   9613   9606   1452  -1826   -461       O  
ATOM    288  NE2 GLN A 209     -33.169  -6.459  19.595  1.00 75.04           N  
ANISOU  288  NE2 GLN A 209    10857   8771   8886   1329  -1712   -389       N  
ATOM    289  N   VAL A 210     -36.065  -6.122  25.063  1.00 42.78           N  
ANISOU  289  N   VAL A 210     7038   4653   4562   1415  -1921   -535       N  
ATOM    290  CA  VAL A 210     -36.502  -6.467  26.423  1.00 46.59           C  
ANISOU  290  CA  VAL A 210     7595   5142   4967   1467  -1972   -566       C  
ATOM    291  C   VAL A 210     -37.634  -7.499  26.536  1.00 43.68           C  
ANISOU  291  C   VAL A 210     7373   4731   4494   1493  -1930   -529       C  
ATOM    292  O   VAL A 210     -37.484  -8.514  27.244  1.00 41.04           O  
ANISOU  292  O   VAL A 210     7104   4416   4074   1578  -1949   -531       O  
ATOM    293  CB  VAL A 210     -36.808  -5.215  27.272  1.00 48.95           C  
ANISOU  293  CB  VAL A 210     7849   5439   5310   1417  -2031   -620       C  
ATOM    294  CG1 VAL A 210     -37.349  -5.609  28.632  1.00 49.31           C  
ANISOU  294  CG1 VAL A 210     7979   5485   5272   1468  -2078   -649       C  
ATOM    295  CG2 VAL A 210     -35.561  -4.387  27.408  1.00 53.71           C  
ANISOU  295  CG2 VAL A 210     8315   6093   5999   1414  -2084   -662       C  
ATOM    296  N   LEU A 211     -38.749  -7.281  25.841  1.00 44.10           N  
ANISOU  296  N   LEU A 211     7479   4727   4549   1423  -1873   -495       N  
ATOM    297  CA  LEU A 211     -39.887  -8.208  25.925  1.00 43.53           C  
ANISOU  297  CA  LEU A 211     7547   4613   4380   1441  -1832   -459       C  
ATOM    298  C   LEU A 211     -39.559  -9.606  25.401  1.00 46.42           C  
ANISOU  298  C   LEU A 211     7972   4987   4680   1510  -1786   -412       C  
ATOM    299  O   LEU A 211     -40.192 -10.580  25.787  1.00 44.96           O  
ANISOU  299  O   LEU A 211     7900   4784   4398   1557  -1771   -392       O  
ATOM    300  CB  LEU A 211     -41.087  -7.703  25.118  1.00 45.37           C  
ANISOU  300  CB  LEU A 211     7819   4784   4636   1349  -1773   -426       C  
ATOM    301  CG  LEU A 211     -41.866  -6.493  25.654  1.00 56.05           C  
ANISOU  301  CG  LEU A 211     9157   6112   6029   1277  -1805   -462       C  
ATOM    302  CD1 LEU A 211     -42.925  -6.106  24.658  1.00 46.73           C  
ANISOU  302  CD1 LEU A 211     8009   4873   4874   1189  -1738   -421       C  
ATOM    303  CD2 LEU A 211     -42.520  -6.847  26.979  1.00 54.00           C  
ANISOU  303  CD2 LEU A 211     8986   5849   5683   1322  -1848   -489       C  
ATOM    304  N   ALA A 212     -38.607  -9.678  24.478  1.00 40.44           N  
ANISOU  304  N   ALA A 212     7138   4251   3975   1512  -1760   -393       N  
ATOM    305  CA  ALA A 212     -38.290 -10.958  23.800  1.00 41.93           C  
ANISOU  305  CA  ALA A 212     7377   4445   4111   1569  -1708   -344       C  
ATOM    306  C   ALA A 212     -37.463 -11.861  24.713  1.00 43.66           C  
ANISOU  306  C   ALA A 212     7610   4713   4267   1676  -1756   -365       C  
ATOM    307  O   ALA A 212     -37.313 -13.058  24.456  1.00 42.46           O  
ANISOU  307  O   ALA A 212     7521   4565   4048   1738  -1722   -330       O  
ATOM    308  CB  ALA A 212     -37.499 -10.682  22.552  1.00 38.81           C  
ANISOU  308  CB  ALA A 212     6889   4060   3798   1534  -1669   -320       C  
ATOM    309  N   ARG A 213     -36.886 -11.266  25.749  1.00 47.82           N  
ANISOU  309  N   ARG A 213     8073   5278   4817   1698  -1834   -423       N  
ATOM    310  CA  ARG A 213     -35.971 -11.998  26.646  1.00 48.31           C  
ANISOU  310  CA  ARG A 213     8133   5393   4831   1798  -1886   -449       C  
ATOM    311  C   ARG A 213     -36.723 -12.685  27.771  1.00 52.48           C  
ANISOU  311  C   ARG A 213     8775   5910   5254   1850  -1912   -459       C  
ATOM    312  O   ARG A 213     -36.117 -13.385  28.575  1.00 54.36           O  
ANISOU  312  O   ARG A 213     9029   6186   5440   1935  -1954   -478       O  
ATOM    313  CB  ARG A 213     -34.981 -11.032  27.298  1.00 57.90           C  
ANISOU  313  CB  ARG A 213     9225   6657   6118   1797  -1962   -508       C  
ATOM    314  CG  ARG A 213     -33.914 -10.481  26.390  1.00 63.90           C  
ANISOU  314  CG  ARG A 213     9860   7445   6975   1769  -1952   -506       C  
ATOM    315  CD  ARG A 213     -32.797  -9.854  27.208  1.00 71.26           C  
ANISOU  315  CD  ARG A 213    10686   8435   7955   1797  -2032   -564       C  
ATOM    316  NE  ARG A 213     -32.060  -8.908  26.381  1.00 79.54           N  
ANISOU  316  NE  ARG A 213    11610   9500   9114   1739  -2027   -570       N  
ATOM    317  CZ  ARG A 213     -31.812  -7.650  26.725  1.00 84.97           C  
ANISOU  317  CZ  ARG A 213    12205  10201   9878   1688  -2075   -615       C  
ATOM    318  NH1 ARG A 213     -32.219  -7.191  27.902  1.00 83.72           N  
ANISOU  318  NH1 ARG A 213    12065  10044   9700   1689  -2133   -658       N  
ATOM    319  NH2 ARG A 213     -31.151  -6.854  25.894  1.00 86.47           N  
ANISOU  319  NH2 ARG A 213    12285  10404  10165   1635  -2065   -616       N  
ATOM    320  N   GLY A 214     -38.029 -12.463  27.850  1.00 46.03           N  
ANISOU  320  N   GLY A 214     8038   5042   4409   1799  -1889   -449       N  
ATOM    321  CA  GLY A 214     -38.813 -12.930  28.972  1.00 47.69           C  
ANISOU  321  CA  GLY A 214     8308   5235   4576   1802  -1865   -473       C  
ATOM    322  C   GLY A 214     -40.160 -13.498  28.570  1.00 48.40           C  
ANISOU  322  C   GLY A 214     8484   5264   4642   1749  -1760   -436       C  
ATOM    323  O   GLY A 214     -40.396 -13.769  27.392  1.00 49.34           O  
ANISOU  323  O   GLY A 214     8626   5360   4763   1722  -1701   -388       O  
ATOM    324  N   ASP A 215     -41.056 -13.623  29.552  1.00 56.31           N  
ANISOU  324  N   ASP A 215     8883   6291   6223    221    750   1099       N  
ATOM    325  CA  ASP A 215     -42.335 -14.334  29.428  1.00 55.35           C  
ANISOU  325  CA  ASP A 215     8725   5986   6319    271    763    930       C  
ATOM    326  C   ASP A 215     -43.484 -13.565  28.778  1.00 56.59           C  
ANISOU  326  C   ASP A 215     8920   5988   6592    234    555    781       C  
ATOM    327  O   ASP A 215     -44.556 -14.138  28.493  1.00 54.12           O  
ANISOU  327  O   ASP A 215     8589   5519   6454    274    548    635       O  
ATOM    328  CB  ASP A 215     -42.783 -14.791  30.814  1.00 66.64           C  
ANISOU  328  CB  ASP A 215    10053   7374   7893    301    914    908       C  
ATOM    329  CG  ASP A 215     -41.782 -15.707  31.467  1.00 72.71           C  
ANISOU  329  CG  ASP A 215    10775   8276   8574    347   1133   1037       C  
ATOM    330  OD1 ASP A 215     -41.816 -16.917  31.151  1.00 71.88           O  
ANISOU  330  OD1 ASP A 215    10655   8145   8511    417   1253   1010       O  
ATOM    331  OD2 ASP A 215     -40.962 -15.213  32.277  1.00 76.83           O  
ANISOU  331  OD2 ASP A 215    11278   8928   8985    313   1182   1166       O  
ATOM    332  N   TYR A 216     -43.276 -12.272  28.564  1.00 49.90           N  
ANISOU  332  N   TYR A 216     8125   5183   5652    158    388    816       N  
ATOM    333  CA  TYR A 216     -44.270 -11.447  27.881  1.00 62.05           C  
ANISOU  333  CA  TYR A 216     9708   6588   7281    116    178    685       C  
ATOM    334  C   TYR A 216     -44.021 -11.477  26.366  1.00 66.38           C  
ANISOU  334  C   TYR A 216    10348   7142   7730    114     65    674       C  
ATOM    335  O   TYR A 216     -44.810 -10.931  25.588  1.00 73.11           O  
ANISOU  335  O   TYR A 216    11246   7883   8649     86   -107    563       O  
ATOM    336  CB  TYR A 216     -44.263 -10.013  28.459  1.00 60.03           C  
ANISOU  336  CB  TYR A 216     9457   6363   6990     34     51    719       C  
ATOM    337  CG  TYR A 216     -44.633 -10.022  29.920  1.00 61.63           C  
ANISOU  337  CG  TYR A 216     9568   6542   7309     38    159    713       C  
ATOM    338  CD1 TYR A 216     -45.950  -9.867  30.331  1.00 67.10           C  
ANISOU  338  CD1 TYR A 216    10216   7067   8212     39    109    565       C  
ATOM    339  CD2 TYR A 216     -43.668 -10.252  30.892  1.00 67.73           C  
ANISOU  339  CD2 TYR A 216    10295   7457   7983     46    318    855       C  
ATOM    340  CE1 TYR A 216     -46.290  -9.917  31.684  1.00 70.23           C  
ANISOU  340  CE1 TYR A 216    10526   7441   8717     45    214    560       C  
ATOM    341  CE2 TYR A 216     -43.993 -10.309  32.236  1.00 70.07           C  
ANISOU  341  CE2 TYR A 216    10505   7732   8387     52    423    851       C  
ATOM    342  CZ  TYR A 216     -45.300 -10.144  32.631  1.00 69.41           C  
ANISOU  342  CZ  TYR A 216    10378   7483   8511     52    372    703       C  
ATOM    343  OH  TYR A 216     -45.586 -10.199  33.983  1.00 62.14           O  
ANISOU  343  OH  TYR A 216     9372   6546   7691     57    480    705       O  
ATOM    344  N   ASP A 217     -42.942 -12.170  25.972  1.00 64.11           N  
ANISOU  344  N   ASP A 217    10085   6982   7291    146    171    787       N  
ATOM    345  CA  ASP A 217     -42.410 -12.178  24.598  1.00 57.46           C  
ANISOU  345  CA  ASP A 217     9333   6187   6312    141     82    814       C  
ATOM    346  C   ASP A 217     -43.408 -12.432  23.494  1.00 64.65           C  
ANISOU  346  C   ASP A 217    10284   6942   7340    160    -31    660       C  
ATOM    347  O   ASP A 217     -43.096 -12.213  22.326  1.00 67.60           O  
ANISOU  347  O   ASP A 217    10737   7339   7610    143   -142    668       O  
ATOM    348  CB  ASP A 217     -41.205 -13.127  24.437  1.00 52.90           C  
ANISOU  348  CB  ASP A 217     8762   5755   5584    188    245    946       C  
ATOM    349  CG  ASP A 217     -41.571 -14.615  24.578  1.00 50.23           C  
ANISOU  349  CG  ASP A 217     8369   5349   5368    276    424    889       C  
ATOM    350  OD1 ASP A 217     -42.539 -14.970  25.286  1.00 51.96           O  
ANISOU  350  OD1 ASP A 217     8519   5447   5777    304    479    785       O  
ATOM    351  OD2 ASP A 217     -40.849 -15.435  23.978  1.00 50.85           O  
ANISOU  351  OD2 ASP A 217     8474   5502   5345    318    510    951       O  
ATOM    352  N   LYS A 218     -44.595 -12.892  23.868  1.00 71.48           N  
ANISOU  352  N   LYS A 218    11092   7648   8419    195     -1    520       N  
ATOM    353  CA  LYS A 218     -45.665 -13.110  22.914  1.00 81.54           C  
ANISOU  353  CA  LYS A 218    12397   8758   9825    212   -108    362       C  
ATOM    354  C   LYS A 218     -46.994 -12.696  23.521  1.00 76.42           C  
ANISOU  354  C   LYS A 218    11700   7949   9387    197   -173    222       C  
ATOM    355  O   LYS A 218     -48.061 -13.064  23.032  1.00 73.38           O  
ANISOU  355  O   LYS A 218    11316   7408   9160    224   -223     76       O  
ATOM    356  CB  LYS A 218     -45.678 -14.569  22.449  1.00 91.91           C  
ANISOU  356  CB  LYS A 218    13699  10041  11180    295     33    332       C  
ATOM    357  CG  LYS A 218     -44.771 -14.809  21.245  1.00 97.79           C  
ANISOU  357  CG  LYS A 218    14526  10883  11749    300      5    406       C  
ATOM    358  CD  LYS A 218     -44.033 -16.133  21.315  1.00102.51           C  
ANISOU  358  CD  LYS A 218    15097  11561  12290    372    212    483       C  
ATOM    359  CE  LYS A 218     -43.176 -16.326  20.069  1.00103.82           C  
ANISOU  359  CE  LYS A 218    15348  11817  12283    375    173    551       C  
ATOM    360  NZ  LYS A 218     -42.546 -17.675  20.015  1.00104.37           N  
ANISOU  360  NZ  LYS A 218    15397  11951  12309    449    368    611       N  
ATOM    361  N   ASN A 219     -46.926 -11.919  24.596  1.00 69.10           N  
ANISOU  361  N   ASN A 219    10732   7061   8463    155   -175    268       N  
ATOM    362  CA  ASN A 219     -48.138 -11.325  25.137  1.00 62.38           C  
ANISOU  362  CA  ASN A 219     9843   6065   7794    129   -262    142       C  
ATOM    363  C   ASN A 219     -48.258  -9.850  24.755  1.00 48.80           C  
ANISOU  363  C   ASN A 219     8182   4342   6018     44   -482    135       C  
ATOM    364  O   ASN A 219     -49.315  -9.243  24.908  1.00 45.94           O  
ANISOU  364  O   ASN A 219     7807   3849   5799     15   -596     18       O  
ATOM    365  CB  ASN A 219     -48.189 -11.449  26.649  1.00 68.53           C  
ANISOU  365  CB  ASN A 219    10529   6863   8647    140   -121    175       C  
ATOM    366  CG  ASN A 219     -49.597 -11.596  27.154  1.00 78.18           C  
ANISOU  366  CG  ASN A 219    11692   7902  10109    158   -130     17       C  
ATOM    367  OD1 ASN A 219     -49.908 -12.555  27.863  1.00 81.55           O  
ANISOU  367  OD1 ASN A 219    12046   8287  10650    218     33    -13       O  
ATOM    368  ND2 ASN A 219     -50.476 -10.664  26.763  1.00 72.24           N  
ANISOU  368  ND2 ASN A 219    10972   7039   9439    109   -321    -89       N  
ATOM    369  N   ALA A 220     -47.167  -9.275  24.274  1.00 40.98           N  
ANISOU  369  N   ALA A 220     7254   3498   4819      2   -541    260       N  
ATOM    370  CA  ALA A 220     -47.188  -7.836  24.033  1.00 44.09           C  
ANISOU  370  CA  ALA A 220     7699   3905   5149    -82   -740    268       C  
ATOM    371  C   ALA A 220     -46.754  -7.508  22.616  1.00 47.87           C  
ANISOU  371  C   ALA A 220     8276   4421   5491   -107   -880    285       C  
ATOM    372  O   ALA A 220     -46.031  -8.273  22.003  1.00 46.68           O  
ANISOU  372  O   ALA A 220     8155   4346   5236    -68   -803    348       O  
ATOM    373  CB  ALA A 220     -46.304  -7.141  25.042  1.00 43.17           C  
ANISOU  373  CB  ALA A 220     7559   3934   4910   -125   -696    410       C  
ATOM    374  N   ARG A 221     -47.197  -6.365  22.089  1.00 42.49           N  
ANISOU  374  N   ARG A 221     7647   3687   4810   -172  -1089    230       N  
ATOM    375  CA  ARG A 221     -46.729  -5.921  20.779  1.00 42.16           C  
ANISOU  375  CA  ARG A 221     7701   3692   4627   -204  -1233    256       C  
ATOM    376  C   ARG A 221     -46.339  -4.450  20.956  1.00 35.89           C  
ANISOU  376  C   ARG A 221     6941   2974   3721   -291  -1381    325       C  
ATOM    377  O   ARG A 221     -47.077  -3.732  21.575  1.00 37.17           O  
ANISOU  377  O   ARG A 221     7073   3059   3992   -327  -1453    261       O  
ATOM    378  CB  ARG A 221     -47.844  -6.006  19.737  1.00 43.63           C  
ANISOU  378  CB  ARG A 221     7924   3708   4945   -197  -1366     93       C  
ATOM    379  CG  ARG A 221     -48.296  -7.453  19.419  1.00 51.19           C  
ANISOU  379  CG  ARG A 221     8855   4579   6016   -111  -1236     13       C  
ATOM    380  CD  ARG A 221     -48.666  -7.625  17.932  1.00 65.44           C  
ANISOU  380  CD  ARG A 221    10734   6304   7824   -105  -1360    -73       C  
ATOM    381  NE  ARG A 221     -49.425  -8.846  17.636  1.00 70.97           N  
ANISOU  381  NE  ARG A 221    11408   6881   8678    -31  -1271   -185       N  
ATOM    382  CZ  ARG A 221     -50.724  -8.875  17.328  1.00 77.31           C  
ANISOU  382  CZ  ARG A 221    12204   7503   9667    -24  -1357   -350       C  
ATOM    383  NH1 ARG A 221     -51.322 -10.036  17.070  1.00 78.49           N  
ANISOU  383  NH1 ARG A 221    12329   7551   9943     46  -1265   -441       N  
ATOM    384  NH2 ARG A 221     -51.432  -7.751  17.277  1.00 73.17           N  
ANISOU  384  NH2 ARG A 221    11698   6899   9205    -85  -1535   -423       N  
ATOM    385  N   VAL A 222     -45.181  -4.056  20.445  1.00 36.73           N  
ANISOU  385  N   VAL A 222     5024   4168   4763   -393   -634    879       N  
ATOM    386  CA  VAL A 222     -44.730  -2.681  20.641  1.00 34.02           C  
ANISOU  386  CA  VAL A 222     4706   3861   4358   -410   -632    868       C  
ATOM    387  C   VAL A 222     -45.159  -1.930  19.367  1.00 38.14           C  
ANISOU  387  C   VAL A 222     5227   4387   4875   -350   -574    824       C  
ATOM    388  O   VAL A 222     -44.934  -2.414  18.226  1.00 33.26           O  
ANISOU  388  O   VAL A 222     4547   3749   4342   -282   -548    797       O  
ATOM    389  CB  VAL A 222     -43.215  -2.589  20.872  1.00 35.17           C  
ANISOU  389  CB  VAL A 222     4801   3997   4564   -412   -689    906       C  
ATOM    390  CG1 VAL A 222     -42.826  -1.142  21.268  1.00 34.95           C  
ANISOU  390  CG1 VAL A 222     4808   4012   4461   -439   -685    894       C  
ATOM    391  CG2 VAL A 222     -42.800  -3.597  21.969  1.00 36.68           C  
ANISOU  391  CG2 VAL A 222     4980   4173   4783   -467   -756    957       C  
ATOM    392  N   ILE A 223     -45.812  -0.789  19.557  1.00 30.94           N  
ANISOU  392  N   ILE A 223     4367   3519   3870   -372   -532    781       N  
ATOM    393  CA  ILE A 223     -46.262  -0.013  18.372  1.00 29.71           C  
ANISOU  393  CA  ILE A 223     4189   3390   3710   -308   -461    702       C  
ATOM    394  C   ILE A 223     -45.706   1.389  18.447  1.00 30.42           C  
ANISOU  394  C   ILE A 223     4292   3510   3755   -317   -459    698       C  
ATOM    395  O   ILE A 223     -45.330   1.844  19.522  1.00 30.55           O  
ANISOU  395  O   ILE A 223     4350   3537   3722   -382   -496    741       O  
ATOM    396  CB  ILE A 223     -47.771   0.114  18.309  1.00 32.06           C  
ANISOU  396  CB  ILE A 223     4521   3706   3954   -312   -398    638       C  
ATOM    397  CG1 ILE A 223     -48.285   0.870  19.530  1.00 36.04           C  
ANISOU  397  CG1 ILE A 223     5096   4231   4365   -394   -393    640       C  
ATOM    398  CG2 ILE A 223     -48.465  -1.315  18.155  1.00 30.40           C  
ANISOU  398  CG2 ILE A 223     4297   3467   3787   -296   -391    632       C  
ATOM    399  CD1 ILE A 223     -49.794   1.034  19.562  1.00 36.96           C  
ANISOU  399  CD1 ILE A 223     5245   4355   4441   -406   -326    573       C  
ATOM    400  N   ASN A 224     -45.642   2.065  17.306  1.00 26.53           N  
ANISOU  400  N   ASN A 224     3766   3035   3280   -256   -416    649       N  
ATOM    401  CA  ASN A 224     -45.330   3.507  17.330  1.00 30.04           C  
ANISOU  401  CA  ASN A 224     4224   3514   3677   -262   -402    634       C  
ATOM    402  C   ASN A 224     -46.055   4.120  16.152  1.00 28.67           C  
ANISOU  402  C   ASN A 224     4032   3362   3501   -209   -338    562       C  
ATOM    403  O   ASN A 224     -46.642   3.400  15.323  1.00 27.42           O  
ANISOU  403  O   ASN A 224     3850   3190   3377   -171   -313    530       O  
ATOM    404  CB  ASN A 224     -43.822   3.737  17.281  1.00 36.83           C  
ANISOU  404  CB  ASN A 224     5053   4361   4581   -250   -449    680       C  
ATOM    405  CG  ASN A 224     -43.182   3.191  16.020  1.00 37.85           C  
ANISOU  405  CG  ASN A 224     5118   4460   4802   -179   -442    666       C  
ATOM    406  OD1 ASN A 224     -43.650   3.463  14.932  1.00 29.34           O  
ANISOU  406  OD1 ASN A 224     4024   3397   3728   -133   -389    607       O  
ATOM    407  ND2 ASN A 224     -42.100   2.433  16.163  1.00 39.17           N  
ANISOU  407  ND2 ASN A 224     5250   4582   5049   -178   -494    719       N  
ATOM    408  N   GLU A 225     -46.039   5.445  16.089  1.00 25.87           N  
ANISOU  408  N   GLU A 225     3686   3040   3105   -212   -314    539       N  
ATOM    409  CA  GLU A 225     -46.870   6.155  15.110  1.00 23.68           C  
ANISOU  409  CA  GLU A 225     3396   2783   2820   -176   -260    477       C  
ATOM    410  C   GLU A 225     -46.418   5.846  13.682  1.00 23.72           C  
ANISOU  410  C   GLU A 225     3354   2779   2881   -109   -253    458       C  
ATOM    411  O   GLU A 225     -47.238   5.798  12.763  1.00 23.48           O  
ANISOU  411  O   GLU A 225     3312   2752   2856    -81   -219    414       O  
ATOM    412  CB  GLU A 225     -46.773   7.681  15.391  1.00 21.60           C  
ANISOU  412  CB  GLU A 225     3143   2553   2512   -196   -240    464       C  
ATOM    413  CG  GLU A 225     -47.584   8.497  14.334  1.00 29.87           C  
ANISOU  413  CG  GLU A 225     4170   3618   3563   -159   -192    408       C  
ATOM    414  CD  GLU A 225     -47.924   9.944  14.743  1.00 45.77           C  
ANISOU  414  CD  GLU A 225     6192   5657   5540   -189   -160    387       C  
ATOM    415  OE1 GLU A 225     -48.335  10.223  15.918  1.00 33.25           O  
ANISOU  415  OE1 GLU A 225     4641   4074   3917   -253   -147    389       O  
ATOM    416  OE2 GLU A 225     -47.824  10.799  13.837  1.00 39.98           O  
ANISOU  416  OE2 GLU A 225     5431   4941   4820   -152   -144    365       O  
ATOM    417  N   ASN A 226     -45.116   5.658  13.474  1.00 22.61           N  
ANISOU  417  N   ASN A 226     3187   2623   2782    -90   -283    489       N  
ATOM    418  CA  ASN A 226     -44.632   5.458  12.118  1.00 22.25           C  
ANISOU  418  CA  ASN A 226     3102   2566   2788    -37   -266    462       C  
ATOM    419  C   ASN A 226     -45.109   4.098  11.610  1.00 23.75           C  
ANISOU  419  C   ASN A 226     3274   2727   3023    -23   -255    449       C  
ATOM    420  O   ASN A 226     -45.632   3.985  10.488  1.00 22.93           O  
ANISOU  420  O   ASN A 226     3158   2629   2927      5   -219    404       O  
ATOM    421  CB  ASN A 226     -43.136   5.544  12.056  1.00 31.43           C  
ANISOU  421  CB  ASN A 226     4237   3707   3998    -24   -294    493       C  
ATOM    422  CG  ASN A 226     -42.597   5.274  10.670  1.00 39.65           C  
ANISOU  422  CG  ASN A 226     5240   4729   5096     20   -267    459       C  
ATOM    423  OD1 ASN A 226     -42.262   4.142  10.345  1.00 40.26           O  
ANISOU  423  OD1 ASN A 226     5288   4766   5243     30   -269    463       O  
ATOM    424  ND2 ASN A 226     -42.501   6.323   9.843  1.00 39.81           N  
ANISOU  424  ND2 ASN A 226     5259   4775   5090     42   -238    423       N  
ATOM    425  N   GLU A 227     -44.929   3.054  12.430  1.00 24.09           N  
ANISOU  425  N   GLU A 227     3316   2740   3096    -45   -289    491       N  
ATOM    426  CA  GLU A 227     -45.362   1.718  11.998  1.00 22.33           C  
ANISOU  426  CA  GLU A 227     3072   2489   2923    -31   -276    479       C  
ATOM    427  C   GLU A 227     -46.872   1.622  11.832  1.00 27.82           C  
ANISOU  427  C   GLU A 227     3792   3204   3573    -33   -241    437       C  
ATOM    428  O   GLU A 227     -47.379   0.909  10.942  1.00 20.79           O  
ANISOU  428  O   GLU A 227     2883   2305   2712     -8   -212    402       O  
ATOM    429  CB  GLU A 227     -44.944   0.647  13.024  1.00 26.59           C  
ANISOU  429  CB  GLU A 227     3606   2991   3505    -60   -325    539       C  
ATOM    430  CG  GLU A 227     -43.466   0.524  13.159  1.00 41.05           C  
ANISOU  430  CG  GLU A 227     5402   4788   5407    -58   -366    586       C  
ATOM    431  CD  GLU A 227     -43.062  -0.764  13.894  1.00 52.51           C  
ANISOU  431  CD  GLU A 227     6830   6191   6930    -81   -416    645       C  
ATOM    432  OE1 GLU A 227     -43.976  -1.528  14.306  1.00 58.11           O  
ANISOU  432  OE1 GLU A 227     7558   6900   7622    -98   -414    647       O  
ATOM    433  OE2 GLU A 227     -41.834  -0.993  14.036  1.00 48.42           O  
ANISOU  433  OE2 GLU A 227     6274   5631   6491    -82   -457    690       O  
ATOM    434  N   GLU A 228     -47.621   2.249  12.733  1.00 22.64           N  
ANISOU  434  N   GLU A 228     3179   2569   2853    -68   -242    440       N  
ATOM    435  CA  GLU A 228     -49.062   2.055  12.658  1.00 25.51           C  
ANISOU  435  CA  GLU A 228     3563   2939   3191    -72   -209    400       C  
ATOM    436  C   GLU A 228     -49.615   2.792  11.421  1.00 26.14           C  
ANISOU  436  C   GLU A 228     3630   3040   3263    -40   -173    349       C  
ATOM    437  O   GLU A 228     -50.518   2.285  10.722  1.00 21.22           O  
ANISOU  437  O   GLU A 228     3001   2412   2651    -22   -148    314       O  
ATOM    438  CB  GLU A 228     -49.778   2.551  13.915  1.00 23.40           C  
ANISOU  438  CB  GLU A 228     3343   2680   2867   -125   -209    407       C  
ATOM    439  CG  GLU A 228     -49.651   1.615  15.135  1.00 22.91           C  
ANISOU  439  CG  GLU A 228     3306   2596   2802   -170   -242    453       C  
ATOM    440  CD  GLU A 228     -50.385   0.286  14.918  1.00 32.32           C  
ANISOU  440  CD  GLU A 228     4489   3763   4029   -154   -231    439       C  
ATOM    441  OE1 GLU A 228     -49.791  -0.596  14.279  1.00 33.45           O  
ANISOU  441  OE1 GLU A 228     4591   3887   4233   -119   -243    452       O  
ATOM    442  OE2 GLU A 228     -51.565   0.155  15.359  1.00 33.61           O  
ANISOU  442  OE2 GLU A 228     4685   3923   4163   -178   -204    412       O  
ATOM    443  N   ASN A 229     -49.072   3.981  11.143  1.00 20.99           N  
ANISOU  443  N   ASN A 229     2975   2410   2591    -34   -173    347       N  
ATOM    444  CA  ASN A 229     -49.431   4.633   9.862  1.00 22.30           C  
ANISOU  444  CA  ASN A 229     3126   2593   2753     -6   -148    307       C  
ATOM    445  C   ASN A 229     -49.164   3.748   8.653  1.00 21.57           C  
ANISOU  445  C   ASN A 229     3007   2488   2702     24   -137    288       C  
ATOM    446  O   ASN A 229     -49.992   3.692   7.748  1.00 21.31           O  
ANISOU  446  O   ASN A 229     2972   2460   2664     33   -117    253       O  
ATOM    447  CB  ASN A 229     -48.684   5.942   9.710  1.00 19.22           C  
ANISOU  447  CB  ASN A 229     2732   2228   2344     -3   -152    312       C  
ATOM    448  CG  ASN A 229     -49.498   7.087  10.258  1.00 25.42           C  
ANISOU  448  CG  ASN A 229     3536   3032   3093    -28   -139    301       C  
ATOM    449  OD1 ASN A 229     -50.456   7.470   9.616  1.00 25.12           O  
ANISOU  449  OD1 ASN A 229     3493   2999   3054    -22   -121    270       O  
ATOM    450  ND2 ASN A 229     -49.148   7.627  11.457  1.00 22.93           N  
ANISOU  450  ND2 ASN A 229     3238   2723   2751    -62   -148    326       N  
ATOM    451  N   LYS A 230     -47.991   3.112   8.619  1.00 22.17           N  
ANISOU  451  N   LYS A 230     3061   2542   2820     33   -149    310       N  
ATOM    452  CA  LYS A 230     -47.656   2.187   7.519  1.00 23.75           C  
ANISOU  452  CA  LYS A 230     3232   2722   3070     52   -128    286       C  
ATOM    453  C   LYS A 230     -48.671   1.065   7.430  1.00 21.79           C  
ANISOU  453  C   LYS A 230     2983   2461   2835     52   -112    269       C  
ATOM    454  O   LYS A 230     -49.113   0.731   6.318  1.00 21.29           O  
ANISOU  454  O   LYS A 230     2912   2400   2777     61    -84    230       O  
ATOM    455  CB  LYS A 230     -46.257   1.599   7.680  1.00 25.84           C  
ANISOU  455  CB  LYS A 230     3465   2952   3400     57   -141    314       C  
ATOM    456  CG  LYS A 230     -45.139   2.626   7.390  1.00 26.53           C  
ANISOU  456  CG  LYS A 230     3546   3047   3488     64   -146    319       C  
ATOM    457  CD  LYS A 230     -43.771   2.051   7.882  1.00 33.89           C  
ANISOU  457  CD  LYS A 230     4444   3934   4498     64   -171    358       C  
ATOM    458  CE  LYS A 230     -42.678   3.077   7.531  1.00 43.13           C  
ANISOU  458  CE  LYS A 230     5608   5107   5671     75   -171    356       C  
ATOM    459  NZ  LYS A 230     -41.379   2.674   8.141  1.00 38.44           N  
ANISOU  459  NZ  LYS A 230     4981   4466   5157     73   -204    400       N  
ATOM    460  N   ARG A 231     -49.079   0.526   8.595  1.00 20.86           N  
ANISOU  460  N   ARG A 231     2878   2331   2717     37   -131    297       N  
ATOM    461  CA  ARG A 231     -49.975  -0.682   8.622  1.00 20.76           C  
ANISOU  461  CA  ARG A 231     2862   2301   2725     38   -116    283       C  
ATOM    462  C   ARG A 231     -51.358  -0.298   8.127  1.00 22.90           C  
ANISOU  462  C   ARG A 231     3154   2592   2956     41    -93    241       C  
ATOM    463  O   ARG A 231     -51.922  -0.980   7.264  1.00 20.27           O  
ANISOU  463  O   ARG A 231     2809   2254   2639     53    -69    209       O  
ATOM    464  CB  ARG A 231     -50.077  -1.253  10.045  1.00 23.84           C  
ANISOU  464  CB  ARG A 231     3267   2673   3117     14   -145    324       C  
ATOM    465  CG  ARG A 231     -51.047  -2.439  10.149  1.00 25.34           C  
ANISOU  465  CG  ARG A 231     3457   2846   3326     17   -128    309       C  
ATOM    466  CD  ARG A 231     -50.924  -3.121  11.527  1.00 26.84           C  
ANISOU  466  CD  ARG A 231     3660   3014   3524    -13   -161    358       C  
ATOM    467  NE  ARG A 231     -51.510  -2.306  12.581  1.00 24.79           N  
ANISOU  467  NE  ARG A 231     3452   2769   3197    -50   -171    366       N  
ATOM    468  CZ  ARG A 231     -52.801  -2.323  12.891  1.00 26.62           C  
ANISOU  468  CZ  ARG A 231     3715   3002   3397    -63   -147    335       C  
ATOM    469  NH1 ARG A 231     -53.242  -1.527  13.869  1.00 25.16           N  
ANISOU  469  NH1 ARG A 231     3575   2825   3158   -106   -148    338       N  
ATOM    470  NH2 ARG A 231     -53.645  -3.133  12.224  1.00 26.36           N  
ANISOU  470  NH2 ARG A 231     3667   2958   3390    -36   -117    298       N  
ATOM    471  N   ILE A 232     -51.848   0.876   8.569  1.00 21.60           N  
ANISOU  471  N   ILE A 232     3016   2447   2745     26   -100    241       N  
ATOM    472  CA  ILE A 232     -53.199   1.316   8.204  1.00 19.32           C  
ANISOU  472  CA  ILE A 232     2741   2166   2434     24    -83    206       C  
ATOM    473  C   ILE A 232     -53.135   1.726   6.735  1.00 22.30           C  
ANISOU  473  C   ILE A 232     3103   2559   2809     40    -74    180       C  
ATOM    474  O   ILE A 232     -54.092   1.483   5.997  1.00 18.96           O  
ANISOU  474  O   ILE A 232     2681   2135   2389     44    -63    152       O  
ATOM    475  CB  ILE A 232     -53.712   2.497   9.111  1.00 23.54           C  
ANISOU  475  CB  ILE A 232     3300   2708   2935     -2    -86    210       C  
ATOM    476  CG1 ILE A 232     -53.872   2.041  10.575  1.00 24.05           C  
ANISOU  476  CG1 ILE A 232     3390   2756   2990    -33    -90    231       C  
ATOM    477  CG2 ILE A 232     -55.075   3.056   8.585  1.00 24.78           C  
ANISOU  477  CG2 ILE A 232     3460   2864   3092     -3    -70    174       C  
ATOM    478  CD1 ILE A 232     -54.542   0.704  10.728  1.00 31.19           C  
ANISOU  478  CD1 ILE A 232     4297   3636   3918    -29    -81    222       C  
ATOM    479  N   SER A 233     -52.040   2.393   6.304  1.00 19.69           N  
ANISOU  479  N   SER A 233     2764   2243   2473     45    -81    191       N  
ATOM    480  CA  SER A 233     -51.951   2.792   4.874  1.00 20.60           C  
ANISOU  480  CA  SER A 233     2873   2375   2580     50    -72    166       C  
ATOM    481  C   SER A 233     -52.012   1.598   3.964  1.00 21.20           C  
ANISOU  481  C   SER A 233     2938   2439   2681     53    -50    140       C  
ATOM    482  O   SER A 233     -52.614   1.648   2.914  1.00 19.69           O  
ANISOU  482  O   SER A 233     2751   2256   2474     46    -42    114       O  
ATOM    483  CB  SER A 233     -50.702   3.658   4.564  1.00 24.51           C  
ANISOU  483  CB  SER A 233     3363   2884   3066     53    -78    177       C  
ATOM    484  OG  SER A 233     -50.907   5.019   5.119  1.00 25.90           O  
ANISOU  484  OG  SER A 233     3550   3079   3213     46    -94    191       O  
ATOM    485  N   ILE A 234     -51.406   0.487   4.348  1.00 17.84           N  
ANISOU  485  N   ILE A 234     2494   1989   2297     60    -40    149       N  
ATOM    486  CA  ILE A 234     -51.531  -0.707   3.490  1.00 15.91           C  
ANISOU  486  CA  ILE A 234     2231   1729   2083     60     -9    119       C  
ATOM    487  C   ILE A 234     -52.967  -1.201   3.378  1.00 20.34           C  
ANISOU  487  C   ILE A 234     2803   2291   2633     60     -3     99       C  
ATOM    488  O   ILE A 234     -53.427  -1.594   2.312  1.00 20.32           O  
ANISOU  488  O   ILE A 234     2800   2293   2626     52     17     66       O  
ATOM    489  CB  ILE A 234     -50.537  -1.820   4.002  1.00 21.15           C  
ANISOU  489  CB  ILE A 234     2862   2360   2815     67      0    137       C  
ATOM    490  CG1 ILE A 234     -49.086  -1.383   3.726  1.00 23.11           C  
ANISOU  490  CG1 ILE A 234     3093   2599   3089     66      2    145       C  
ATOM    491  CG2 ILE A 234     -50.802  -3.175   3.295  1.00 21.46           C  
ANISOU  491  CG2 ILE A 234     2877   2380   2898     66     39    104       C  
ATOM    492  CD1 ILE A 234     -47.992  -2.191   4.508  1.00 26.62           C  
ANISOU  492  CD1 ILE A 234     3500   3002   3612     71     -8    180       C  
ATOM    493  N   TRP A 235     -53.688  -1.188   4.489  1.00 21.48           N  
ANISOU  493  N   TRP A 235     2960   2428   2772     64    -19    115       N  
ATOM    494  CA  TRP A 235     -55.087  -1.601   4.461  1.00 21.60           C  
ANISOU  494  CA  TRP A 235     2986   2438   2784     65    -12     94       C  
ATOM    495  C   TRP A 235     -55.905  -0.630   3.551  1.00 21.14           C  
ANISOU  495  C   TRP A 235     2941   2396   2693     55    -22     75       C  
ATOM    496  O   TRP A 235     -56.673  -1.000   2.650  1.00 21.36           O  
ANISOU  496  O   TRP A 235     2970   2425   2720     50    -14     49       O  
ATOM    497  CB  TRP A 235     -55.612  -1.609   5.906  1.00 18.44           C  
ANISOU  497  CB  TRP A 235     2600   2022   2383     62    -23    113       C  
ATOM    498  CG  TRP A 235     -57.034  -2.154   6.074  1.00 21.05           C  
ANISOU  498  CG  TRP A 235     2941   2335   2722     65    -10     88       C  
ATOM    499  CD1 TRP A 235     -57.426  -3.499   6.254  1.00 25.67           C  
ANISOU  499  CD1 TRP A 235     3516   2900   3336     75      9     77       C  
ATOM    500  CD2 TRP A 235     -58.245  -1.396   6.067  1.00 20.65           C  
ANISOU  500  CD2 TRP A 235     2906   2280   2661     57    -14     70       C  
ATOM    501  NE1 TRP A 235     -58.788  -3.571   6.383  1.00 24.15           N  
ANISOU  501  NE1 TRP A 235     3338   2693   3145     76     17     52       N  
ATOM    502  CE2 TRP A 235     -59.323  -2.304   6.245  1.00 27.40           C  
ANISOU  502  CE2 TRP A 235     3762   3109   3537     64      4     47       C  
ATOM    503  CE3 TRP A 235     -58.537  -0.031   5.935  1.00 24.70           C  
ANISOU  503  CE3 TRP A 235     3426   2802   3158     44    -29     71       C  
ATOM    504  CZ2 TRP A 235     -60.639  -1.889   6.319  1.00 27.08           C  
ANISOU  504  CZ2 TRP A 235     3732   3049   3508     58      6     24       C  
ATOM    505  CZ3 TRP A 235     -59.824   0.377   5.992  1.00 28.07           C  
ANISOU  505  CZ3 TRP A 235     3857   3207   3600     36    -27     51       C  
ATOM    506  CH2 TRP A 235     -60.882  -0.555   6.176  1.00 28.47           C  
ANISOU  506  CH2 TRP A 235     3911   3230   3678     43    -10     27       C  
ATOM    507  N   LEU A 236     -55.700   0.649   3.744  1.00 18.01           N  
ANISOU  507  N   LEU A 236     2554   2014   2274     48    -42     91       N  
ATOM    508  CA  LEU A 236     -56.458   1.592   2.946  1.00 17.83           C  
ANISOU  508  CA  LEU A 236     2539   2003   2234     35    -59     81       C  
ATOM    509  C   LEU A 236     -56.118   1.537   1.464  1.00 20.38           C  
ANISOU  509  C   LEU A 236     2861   2343   2538     22    -57     66       C  
ATOM    510  O   LEU A 236     -56.988   1.868   0.617  1.00 21.97           O  
ANISOU  510  O   LEU A 236     3070   2549   2728      5    -74     56       O  
ATOM    511  CB  LEU A 236     -56.111   3.017   3.439  1.00 18.97           C  
ANISOU  511  CB  LEU A 236     2685   2159   2362     29    -77    103       C  
ATOM    512  CG  LEU A 236     -56.590   3.368   4.835  1.00 18.49           C  
ANISOU  512  CG  LEU A 236     2631   2083   2313     26    -75    113       C  
ATOM    513  CD1 LEU A 236     -55.920   4.781   5.245  1.00 19.30           C  
ANISOU  513  CD1 LEU A 236     2731   2202   2398     17    -86    133       C  
ATOM    514  CD2 LEU A 236     -58.119   3.402   4.936  1.00 19.75           C  
ANISOU  514  CD2 LEU A 236     2790   2216   2497     18    -74     93       C  
ATOM    515  N   ASP A 237     -54.888   1.166   1.137  1.00 18.50           N  
ANISOU  515  N   ASP A 237     2617   2112   2300     22    -38     64       N  
ATOM    516  CA  ASP A 237     -54.438   1.035  -0.286  1.00 21.67           C  
ANISOU  516  CA  ASP A 237     3024   2527   2682     -2    -23     41       C  
ATOM    517  C   ASP A 237     -55.405   0.130  -1.039  1.00 26.35           C  
ANISOU  517  C   ASP A 237     3622   3115   3275    -17    -12     13       C  
ATOM    518  O   ASP A 237     -55.629   0.296  -2.231  1.00 24.61           O  
ANISOU  518  O   ASP A 237     3418   2910   3024    -50    -15     -2       O  
ATOM    519  CB  ASP A 237     -53.059   0.312  -0.394  1.00 27.55           C  
ANISOU  519  CB  ASP A 237     3753   3262   3455      1     13     31       C  
ATOM    520  CG  ASP A 237     -51.856   1.203  -0.127  1.00 38.10           C  
ANISOU  520  CG  ASP A 237     5086   4603   4788      6      6     50       C  
ATOM    521  OD1 ASP A 237     -51.967   2.461  -0.214  1.00 37.19           O  
ANISOU  521  OD1 ASP A 237     4985   4509   4637      2    -22     64       O  
ATOM    522  OD2 ASP A 237     -50.760   0.615   0.175  1.00 35.56           O  
ANISOU  522  OD2 ASP A 237     4742   4261   4509     15     28     51       O  
ATOM    523  N   THR A 238     -55.882  -0.920  -0.362  1.00 22.16           N  
ANISOU  523  N   THR A 238     3077   2564   2778      4      5      7       N  
ATOM    524  CA  THR A 238     -56.846  -1.847  -1.013  1.00 20.47           C  
ANISOU  524  CA  THR A 238     2865   2344   2568     -7     19    -21       C  
ATOM    525  C   THR A 238     -58.314  -1.431  -0.790  1.00 21.32           C  
ANISOU  525  C   THR A 238     2984   2444   2674     -4    -14    -15       C  
ATOM    526  O   THR A 238     -59.110  -1.460  -1.733  1.00 23.47           O  
ANISOU  526  O   THR A 238     3267   2721   2931    -27    -27    -29       O  
ATOM    527  CB  THR A 238     -56.640  -3.300  -0.485  1.00 25.55           C  
ANISOU  527  CB  THR A 238     3484   2966   3258     13     59    -34       C  
ATOM    528  OG1 THR A 238     -55.373  -3.767  -0.943  1.00 23.37           O  
ANISOU  528  OG1 THR A 238     3191   2688   3001      2     94    -46       O  
ATOM    529  CG2 THR A 238     -57.776  -4.206  -1.018  1.00 23.93           C  
ANISOU  529  CG2 THR A 238     3279   2754   3058      7     73    -63       C  
ATOM    530  N   TYR A 239     -58.700  -1.007   0.412  1.00 17.81           N  
ANISOU  530  N   TYR A 239     2535   1983   2248     19    -29      3       N  
ATOM    531  CA  TYR A 239     -60.136  -0.878   0.700  1.00 19.06           C  
ANISOU  531  CA  TYR A 239     2697   2120   2426     22    -46     -2       C  
ATOM    532  C   TYR A 239     -60.675   0.509   0.444  1.00 25.98           C  
ANISOU  532  C   TYR A 239     3577   2996   3298      5    -86     15       C  
ATOM    533  O   TYR A 239     -61.877   0.664   0.243  1.00 24.13           O  
ANISOU  533  O   TYR A 239     3341   2740   3087     -2   -107      9       O  
ATOM    534  CB  TYR A 239     -60.446  -1.258   2.122  1.00 19.33           C  
ANISOU  534  CB  TYR A 239     2727   2128   2489     44    -31      1       C  
ATOM    535  CG  TYR A 239     -60.294  -2.800   2.274  1.00 20.73           C  
ANISOU  535  CG  TYR A 239     2896   2297   2685     60      4    -16       C  
ATOM    536  CD1 TYR A 239     -59.264  -3.352   3.035  1.00 21.99           C  
ANISOU  536  CD1 TYR A 239     3045   2455   2854     72     21     -1       C  
ATOM    537  CD2 TYR A 239     -61.087  -3.616   1.541  1.00 20.01           C  
ANISOU  537  CD2 TYR A 239     2801   2199   2603     60     16    -43       C  
ATOM    538  CE1 TYR A 239     -59.127  -4.758   3.130  1.00 28.73           C  
ANISOU  538  CE1 TYR A 239     3882   3296   3737     85     51    -13       C  
ATOM    539  CE2 TYR A 239     -60.940  -5.060   1.595  1.00 19.95           C  
ANISOU  539  CE2 TYR A 239     2777   2183   2618     74     53    -61       C  
ATOM    540  CZ  TYR A 239     -59.980  -5.593   2.397  1.00 26.79           C  
ANISOU  540  CZ  TYR A 239     3631   3045   3503     87     71    -45       C  
ATOM    541  OH  TYR A 239     -59.828  -7.004   2.487  1.00 27.51           O  
ANISOU  541  OH  TYR A 239     3699   3124   3630    101    106    -59       O  
ATOM    542  N   TYR A 240     -59.799   1.506   0.540  1.00 22.35           N  
ANISOU  542  N   TYR A 240     3118   2555   2818      0    -98     36       N  
ATOM    543  CA  TYR A 240     -60.194   2.924   0.227  1.00 19.41           C  
ANISOU  543  CA  TYR A 240     2744   2185   2446    -18   -137     55       C  
ATOM    544  C   TYR A 240     -59.112   3.534  -0.636  1.00 19.61           C  
ANISOU  544  C   TYR A 240     2778   2245   2429    -35   -148     67       C  
ATOM    545  O   TYR A 240     -58.384   4.444  -0.182  1.00 22.47           O  
ANISOU  545  O   TYR A 240     3136   2618   2783    -30   -151     85       O  
ATOM    546  CB  TYR A 240     -60.215   3.757   1.533  1.00 21.72           C  
ANISOU  546  CB  TYR A 240     3027   2463   2764     -8   -133     68       C  
ATOM    547  CG  TYR A 240     -61.451   3.470   2.426  1.00 22.81           C  
ANISOU  547  CG  TYR A 240     3159   2558   2951     -2   -121     53       C  
ATOM    548  CD1 TYR A 240     -62.567   4.298   2.404  1.00 24.94           C  
ANISOU  548  CD1 TYR A 240     3412   2795   3268    -16   -142     53       C  
ATOM    549  CD2 TYR A 240     -61.503   2.332   3.267  1.00 22.27           C  
ANISOU  549  CD2 TYR A 240     3098   2475   2888     14    -88     37       C  
ATOM    550  CE1 TYR A 240     -63.685   4.016   3.211  1.00 24.73           C  
ANISOU  550  CE1 TYR A 240     3379   2721   3295    -15   -123     32       C  
ATOM    551  CE2 TYR A 240     -62.577   2.081   4.071  1.00 21.68           C  
ANISOU  551  CE2 TYR A 240     3023   2360   2854     15    -72     19       C  
ATOM    552  CZ  TYR A 240     -63.676   2.887   4.025  1.00 25.97           C  
ANISOU  552  CZ  TYR A 240     3553   2870   3446      1    -86     13       C  
ATOM    553  OH  TYR A 240     -64.749   2.632   4.869  1.00 27.14           O  
ANISOU  553  OH  TYR A 240     3700   2969   3644     -2    -62    -13       O  
ATOM    554  N   PRO A 241     -58.900   3.000  -1.835  1.00 19.73           N  
ANISOU  554  N   PRO A 241     2808   2277   2413    -59   -146     54       N  
ATOM    555  CA  PRO A 241     -57.709   3.287  -2.659  1.00 19.91           C  
ANISOU  555  CA  PRO A 241     2844   2328   2392    -80   -139     54       C  
ATOM    556  C   PRO A 241     -57.657   4.731  -3.180  1.00 30.56           C  
ANISOU  556  C   PRO A 241     4199   3692   3721   -103   -182     80       C  
ATOM    557  O   PRO A 241     -56.607   5.169  -3.639  1.00 30.89           O  
ANISOU  557  O   PRO A 241     4251   3756   3730   -115   -174     81       O  
ATOM    558  CB  PRO A 241     -57.920   2.406  -3.893  1.00 28.11           C  
ANISOU  558  CB  PRO A 241     3901   3374   3404   -116   -129     29       C  
ATOM    559  CG  PRO A 241     -59.420   2.091  -3.901  1.00 34.16           C  
ANISOU  559  CG  PRO A 241     4664   4120   4196   -118   -155     29       C  
ATOM    560  CD  PRO A 241     -59.786   1.969  -2.459  1.00 25.80           C  
ANISOU  560  CD  PRO A 241     3582   3035   3187    -72   -143     33       C  
ATOM    561  N   GLN A 242     -58.780   5.415  -3.172  1.00 24.96           N  
ANISOU  561  N   GLN A 242     3480   2968   3037   -111   -225     99       N  
ATOM    562  CA  GLN A 242     -58.778   6.797  -3.688  1.00 28.60           C  
ANISOU  562  CA  GLN A 242     3939   3439   3489   -135   -270    129       C  
ATOM    563  C   GLN A 242     -58.877   7.813  -2.574  1.00 30.55           C  
ANISOU  563  C   GLN A 242     4157   3672   3780   -109   -274    147       C  
ATOM    564  O   GLN A 242     -59.073   9.002  -2.853  1.00 27.49           O  
ANISOU  564  O   GLN A 242     3755   3284   3405   -125   -311    174       O  
ATOM    565  CB  GLN A 242     -59.958   7.013  -4.652  1.00 36.65           C  
ANISOU  565  CB  GLN A 242     4962   4445   4517   -176   -326    146       C  
ATOM    566  CG  GLN A 242     -59.889   6.116  -5.873  1.00 51.83           C  
ANISOU  566  CG  GLN A 242     6921   6387   6386   -218   -324    128       C  
ATOM    567  CD  GLN A 242     -58.632   6.388  -6.671  1.00 67.96           C  
ANISOU  567  CD  GLN A 242     8992   8465   8363   -248   -309    123       C  
ATOM    568  OE1 GLN A 242     -58.449   7.488  -7.200  1.00 74.40           O  
ANISOU  568  OE1 GLN A 242     9815   9293   9159   -276   -349    151       O  
ATOM    569  NE2 GLN A 242     -57.743   5.399  -6.742  1.00 73.90           N  
ANISOU  569  NE2 GLN A 242     9760   9229   9091   -244   -249     86       N  
ATOM    570  N   LEU A 243     -58.759   7.375  -1.322  1.00 22.15           N  
ANISOU  570  N   LEU A 243     3082   2595   2741    -74   -236    134       N  
ATOM    571  CA  LEU A 243     -58.965   8.247  -0.169  1.00 23.19           C  
ANISOU  571  CA  LEU A 243     3189   2709   2913    -60   -231    144       C  
ATOM    572  C   LEU A 243     -57.886   9.333  -0.088  1.00 23.45           C  
ANISOU  572  C   LEU A 243     3218   2770   2923    -57   -231    162       C  
ATOM    573  O   LEU A 243     -56.681   9.048  -0.201  1.00 25.91           O  
ANISOU  573  O   LEU A 243     3545   3106   3191    -48   -211    157       O  
ATOM    574  CB  LEU A 243     -59.031   7.435   1.113  1.00 22.14           C  
ANISOU  574  CB  LEU A 243     3057   2558   2798    -36   -190    127       C  
ATOM    575  CG  LEU A 243     -59.379   8.265   2.346  1.00 22.87           C  
ANISOU  575  CG  LEU A 243     3130   2628   2929    -36   -176    130       C  
ATOM    576  CD1 LEU A 243     -60.845   8.692   2.382  1.00 27.31           C  
ANISOU  576  CD1 LEU A 243     3670   3147   3561    -51   -191    125       C  
ATOM    577  CD2 LEU A 243     -59.050   7.381   3.567  1.00 23.74           C  
ANISOU  577  CD2 LEU A 243     3256   2733   3032    -22   -137    117       C  
ATOM    578  N   ALA A 244     -58.317  10.593   0.090  1.00 22.21           N  
ANISOU  578  N   ALA A 244     3034   2602   2802    -67   -252    180       N  
ATOM    579  CA  ALA A 244     -57.382  11.701   0.197  1.00 19.30           C  
ANISOU  579  CA  ALA A 244     2657   2258   2416    -64   -251    195       C  
ATOM    580  C   ALA A 244     -57.159  11.954   1.676  1.00 22.22           C  
ANISOU  580  C   ALA A 244     3015   2620   2808    -48   -213    189       C  
ATOM    581  O   ALA A 244     -57.978  12.589   2.329  1.00 23.73           O  
ANISOU  581  O   ALA A 244     3178   2783   3053    -57   -207    188       O  
ATOM    582  CB  ALA A 244     -58.030  12.995  -0.454  1.00 21.66           C  
ANISOU  582  CB  ALA A 244     2928   2549   2755    -88   -296    222       C  
ATOM    583  N   TYR A 245     -56.049  11.466   2.215  1.00 20.95           N  
ANISOU  583  N   TYR A 245     2872   2479   2607    -29   -185    183       N  
ATOM    584  CA  TYR A 245     -55.797  11.611   3.639  1.00 26.37           C  
ANISOU  584  CA  TYR A 245     3556   3160   3302    -25   -154    180       C  
ATOM    585  C   TYR A 245     -54.379  12.079   3.865  1.00 21.03           C  
ANISOU  585  C   TYR A 245     2885   2515   2590    -12   -145    192       C  
ATOM    586  O   TYR A 245     -53.533  12.059   2.931  1.00 20.91           O  
ANISOU  586  O   TYR A 245     2879   2522   2545     -3   -157    196       O  
ATOM    587  CB  TYR A 245     -56.130  10.323   4.431  1.00 26.19           C  
ANISOU  587  CB  TYR A 245     3551   3117   3282    -21   -132    165       C  
ATOM    588  CG  TYR A 245     -55.235   9.143   4.137  1.00 20.41           C  
ANISOU  588  CG  TYR A 245     2840   2398   2516     -4   -129    164       C  
ATOM    589  CD1 TYR A 245     -54.138   8.863   4.972  1.00 21.45           C  
ANISOU  589  CD1 TYR A 245     2981   2540   2629      5   -115    175       C  
ATOM    590  CD2 TYR A 245     -55.506   8.297   3.062  1.00 20.40           C  
ANISOU  590  CD2 TYR A 245     2846   2396   2510     -2   -138    153       C  
ATOM    591  CE1 TYR A 245     -53.309   7.749   4.732  1.00 24.48           C  
ANISOU  591  CE1 TYR A 245     3374   2925   3003     19   -111    175       C  
ATOM    592  CE2 TYR A 245     -54.670   7.169   2.783  1.00 20.43           C  
ANISOU  592  CE2 TYR A 245     2861   2405   2496     10   -125    147       C  
ATOM    593  CZ  TYR A 245     -53.595   6.917   3.666  1.00 23.16           C  
ANISOU  593  CZ  TYR A 245     3208   2753   2837     22   -111    158       C  
ATOM    594  OH  TYR A 245     -52.761   5.857   3.435  1.00 23.88           O  
ANISOU  594  OH  TYR A 245     3301   2841   2932     32    -98    154       O  
ATOM    595  N   TYR A 246     -54.103  12.448   5.103  1.00 17.49           N  
ANISOU  595  N   TYR A 246     2434   2066   2144    -17   -123    195       N  
ATOM    596  CA  TYR A 246     -52.775  12.891   5.444  1.00 15.29           C  
ANISOU  596  CA  TYR A 246     2160   1813   1836     -6   -117    208       C  
ATOM    597  C   TYR A 246     -52.065  11.803   6.284  1.00 19.69           C  
ANISOU  597  C   TYR A 246     2740   2366   2374     -1   -108    213       C  
ATOM    598  O   TYR A 246     -51.194  11.106   5.775  1.00 20.32           O  
ANISOU  598  O   TYR A 246     2828   2451   2440     17   -115    216       O  
ATOM    599  CB  TYR A 246     -52.935  14.139   6.282  1.00 15.17           C  
ANISOU  599  CB  TYR A 246     2126   1802   1838    -24   -100    210       C  
ATOM    600  CG  TYR A 246     -53.308  15.336   5.373  1.00 18.20           C  
ANISOU  600  CG  TYR A 246     2478   2190   2247    -25   -115    214       C  
ATOM    601  CD1 TYR A 246     -52.351  15.890   4.561  1.00 18.15           C  
ANISOU  601  CD1 TYR A 246     2469   2212   2214     -8   -130    226       C  
ATOM    602  CD2 TYR A 246     -54.567  15.860   5.372  1.00 20.55           C  
ANISOU  602  CD2 TYR A 246     2748   2460   2600    -46   -115    207       C  
ATOM    603  CE1 TYR A 246     -52.628  16.957   3.725  1.00 22.67           C  
ANISOU  603  CE1 TYR A 246     3015   2790   2806    -12   -149    235       C  
ATOM    604  CE2 TYR A 246     -54.879  16.973   4.536  1.00 19.68           C  
ANISOU  604  CE2 TYR A 246     2603   2351   2523    -50   -137    219       C  
ATOM    605  CZ  TYR A 246     -53.896  17.474   3.694  1.00 23.89           C  
ANISOU  605  CZ  TYR A 246     3139   2919   3019    -34   -157    235       C  
ATOM    606  OH  TYR A 246     -54.123  18.582   2.858  1.00 23.50           O  
ANISOU  606  OH  TYR A 246     3059   2873   2999    -41   -183    252       O  
ATOM    607  N   ARG A 247     -52.485  11.649   7.521  1.00 18.77           N  
ANISOU  607  N   ARG A 247     2633   2236   2263    -23    -92    212       N  
ATOM    608  CA  ARG A 247     -51.708  10.846   8.464  1.00 23.42           C  
ANISOU  608  CA  ARG A 247     3243   2823   2832    -27    -92    228       C  
ATOM    609  C   ARG A 247     -52.565  10.606   9.688  1.00 23.61           C  
ANISOU  609  C   ARG A 247     3284   2827   2860    -63    -74    221       C  
ATOM    610  O   ARG A 247     -53.438  11.397   9.962  1.00 23.50           O  
ANISOU  610  O   ARG A 247     3262   2805   2864    -86    -53    204       O  
ATOM    611  CB  ARG A 247     -50.496  11.696   8.906  1.00 26.25           C  
ANISOU  611  CB  ARG A 247     3599   3205   3170    -27    -96    248       C  
ATOM    612  CG  ARG A 247     -49.490  10.910   9.652  1.00 38.32           C  
ANISOU  612  CG  ARG A 247     5145   4729   4686    -29   -110    274       C  
ATOM    613  CD  ARG A 247     -48.101  11.427   9.454  1.00 34.40           C  
ANISOU  613  CD  ARG A 247     4639   4249   4183    -10   -123    292       C  
ATOM    614  NE  ARG A 247     -47.099  10.517  10.048  1.00 36.49           N  
ANISOU  614  NE  ARG A 247     4913   4498   4454    -11   -146    322       N  
ATOM    615  CZ  ARG A 247     -46.646   9.405   9.473  1.00 39.25           C  
ANISOU  615  CZ  ARG A 247     5254   4827   4834     11   -156    326       C  
ATOM    616  NH1 ARG A 247     -47.112   8.988   8.282  1.00 38.40           N  
ANISOU  616  NH1 ARG A 247     5135   4713   4740     31   -143    297       N  
ATOM    617  NH2 ARG A 247     -45.712   8.691  10.109  1.00 42.28           N  
ANISOU  617  NH2 ARG A 247     5637   5190   5238      6   -181    359       N  
ATOM    618  N   ILE A 248     -52.260   9.557  10.474  1.00 19.79           N  
ANISOU  618  N   ILE A 248     2824   2332   2363    -74    -79    236       N  
ATOM    619  CA  ILE A 248     -52.950   9.370  11.732  1.00 16.60           C  
ANISOU  619  CA  ILE A 248     2447   1911   1952   -120    -60    230       C  
ATOM    620  C   ILE A 248     -52.001   9.763  12.832  1.00 19.89           C  
ANISOU  620  C   ILE A 248     2883   2342   2333   -153    -66    258       C  
ATOM    621  O   ILE A 248     -50.821   9.456  12.765  1.00 24.26           O  
ANISOU  621  O   ILE A 248     3435   2906   2876   -135    -96    290       O  
ATOM    622  CB  ILE A 248     -53.252   7.847  11.958  1.00 22.71           C  
ANISOU  622  CB  ILE A 248     3238   2661   2730   -118    -68    234       C  
ATOM    623  CG1 ILE A 248     -54.126   7.336  10.826  1.00 27.87           C  
ANISOU  623  CG1 ILE A 248     3874   3301   3416    -86    -64    207       C  
ATOM    624  CG2 ILE A 248     -53.985   7.649  13.298  1.00 27.04           C  
ANISOU  624  CG2 ILE A 248     3821   3188   3264   -174    -46    226       C  
ATOM    625  CD1 ILE A 248     -54.204   5.804  10.855  1.00 28.40           C  
ANISOU  625  CD1 ILE A 248     3950   3350   3492    -74    -72    212       C  
ATOM    626  N   HIS A 249     -52.509  10.459  13.839  1.00 21.86           N  
ANISOU  626  N   HIS A 249     3149   2588   2568   -206    -36    245       N  
ATOM    627  CA  HIS A 249     -51.696  10.961  14.941  1.00 21.52           C  
ANISOU  627  CA  HIS A 249     3131   2562   2485   -251    -38    269       C  
ATOM    628  C   HIS A 249     -52.076  10.284  16.249  1.00 25.05           C  
ANISOU  628  C   HIS A 249     3626   2991   2901   -317    -30    275       C  
ATOM    629  O   HIS A 249     -53.246  10.028  16.500  1.00 27.32           O  
ANISOU  629  O   HIS A 249     3926   3252   3203   -342      4    241       O  
ATOM    630  CB  HIS A 249     -51.863  12.475  15.073  1.00 26.94           C  
ANISOU  630  CB  HIS A 249     3799   3263   3174   -273     -2    247       C  
ATOM    631  CG  HIS A 249     -51.230  13.219  13.953  1.00 30.83           C  
ANISOU  631  CG  HIS A 249     4251   3779   3684   -217    -16    252       C  
ATOM    632  ND1 HIS A 249     -49.867  13.237  13.766  1.00 38.65           N  
ANISOU  632  ND1 HIS A 249     5239   4792   4654   -190    -50    285       N  
ATOM    633  CD2 HIS A 249     -51.771  13.873  12.895  1.00 28.35           C  
ANISOU  633  CD2 HIS A 249     3898   3464   3409   -184     -6    230       C  
ATOM    634  CE1 HIS A 249     -49.585  13.956  12.692  1.00 39.36           C  
ANISOU  634  CE1 HIS A 249     5295   4897   4764   -145    -52    278       C  
ATOM    635  NE2 HIS A 249     -50.721  14.361  12.150  1.00 32.19           N  
ANISOU  635  NE2 HIS A 249     4365   3977   3888   -143    -29    248       N  
ATOM    636  N   PHE A 250     -51.075   9.965  17.053  1.00 27.57           N  
ANISOU  636  N   PHE A 250     3973   3320   3182   -346    -65    319       N  
ATOM    637  CA  PHE A 250     -51.253   9.110  18.231  1.00 24.73           C  
ANISOU  637  CA  PHE A 250     3664   2943   2787   -411    -74    338       C  
ATOM    638  C   PHE A 250     -50.898   9.774  19.559  1.00 32.85           C  
ANISOU  638  C   PHE A 250     4737   3986   3757   -499    -66    353       C  
ATOM    639  O   PHE A 250     -50.613   9.076  20.532  1.00 38.51           O  
ANISOU  639  O   PHE A 250     5500   4696   4435   -556    -96    389       O  
ATOM    640  CB  PHE A 250     -50.456   7.834  18.074  1.00 31.22           C  
ANISOU  640  CB  PHE A 250     4486   3757   3621   -380   -135    388       C  
ATOM    641  CG  PHE A 250     -50.989   6.904  17.025  1.00 32.61           C  
ANISOU  641  CG  PHE A 250     4631   3913   3846   -317   -134    369       C  
ATOM    642  CD1 PHE A 250     -50.546   6.993  15.693  1.00 30.86           C  
ANISOU  642  CD1 PHE A 250     4362   3700   3664   -243   -143    363       C  
ATOM    643  CD2 PHE A 250     -51.930   5.950  17.354  1.00 31.23           C  
ANISOU  643  CD2 PHE A 250     4478   3713   3676   -335   -121    355       C  
ATOM    644  CE1 PHE A 250     -51.009   6.135  14.724  1.00 33.35           C  
ANISOU  644  CE1 PHE A 250     4653   4000   4019   -194   -139    344       C  
ATOM    645  CE2 PHE A 250     -52.423   5.086  16.391  1.00 31.29           C  
ANISOU  645  CE2 PHE A 250     4457   3704   3727   -279   -119    336       C  
ATOM    646  CZ  PHE A 250     -51.960   5.157  15.066  1.00 34.03           C  
ANISOU  646  CZ  PHE A 250     4757   4061   4111   -210   -128    331       C  
ATOM    647  N   ASP A 251     -50.921  11.110  19.586  1.00 33.27           N  
ANISOU  647  N   ASP A 251     4777   4059   3806   -514    -26    326       N  
ATOM    648  CA  ASP A 251     -50.727  11.874  20.815  1.00 43.25           C  
ANISOU  648  CA  ASP A 251     6082   5337   5015   -607     -2    327       C  
ATOM    649  C   ASP A 251     -51.438  11.229  22.006  1.00 45.19           C  
ANISOU  649  C   ASP A 251     6392   5559   5219   -701     18    319       C  
ATOM    650  O   ASP A 251     -50.846  11.018  23.068  1.00 37.91           O  
ANISOU  650  O   ASP A 251     5522   4646   4234   -777    -11    358       O  
ATOM    651  CB  ASP A 251     -51.208  13.308  20.629  1.00 44.89           C  
ANISOU  651  CB  ASP A 251     6258   5554   5245   -615     65    275       C  
ATOM    652  CG  ASP A 251     -50.451  14.024  19.536  1.00 55.74           C  
ANISOU  652  CG  ASP A 251     7574   6953   6650   -532     45    285       C  
ATOM    653  OD1 ASP A 251     -49.344  13.572  19.200  1.00 59.68           O  
ANISOU  653  OD1 ASP A 251     8069   7467   7142   -488    -16    333       O  
ATOM    654  OD2 ASP A 251     -50.956  15.039  19.019  1.00 66.50           O  
ANISOU  654  OD2 ASP A 251     8897   8318   8054   -515     90    246       O  
ATOM    655  N   GLU A 252     -52.707  10.903  21.830  1.00 42.08           N  
ANISOU  655  N   GLU A 252     5997   5133   4859   -701     65    269       N  
ATOM    656  CA  GLU A 252     -53.353  10.017  22.771  1.00 41.30           C  
ANISOU  656  CA  GLU A 252     5958   5006   4727   -774     76    264       C  
ATOM    657  C   GLU A 252     -53.631   8.673  22.078  1.00 36.62           C  
ANISOU  657  C   GLU A 252     5350   4392   4171   -704     37    279       C  
ATOM    658  O   GLU A 252     -54.591   8.561  21.323  1.00 33.35           O  
ANISOU  658  O   GLU A 252     4903   3955   3813   -656     71    234       O  
ATOM    659  CB  GLU A 252     -54.624  10.650  23.331  1.00 43.62           C  
ANISOU  659  CB  GLU A 252     6271   5272   5032   -847    170    189       C  
ATOM    660  CG  GLU A 252     -55.377   9.737  24.310  1.00 52.81           C  
ANISOU  660  CG  GLU A 252     7487   6410   6167   -909    184    165       C  
ATOM    661  CD  GLU A 252     -54.443   9.027  25.305  1.00 63.56           C  
ANISOU  661  CD  GLU A 252     8893   7801   7457   -948    111    218       C  
ATOM    662  OE1 GLU A 252     -53.836   9.735  26.144  1.00 72.73           O  
ANISOU  662  OE1 GLU A 252    10066   8995   8574   -996    103    214       O  
ATOM    663  OE2 GLU A 252     -54.317   7.765  25.256  1.00 48.57           O  
ANISOU  663  OE2 GLU A 252     7013   5888   5553   -932     59    262       O  
ATOM    664  N   PRO A 253     -52.783   7.659  22.348  1.00 38.22           N  
ANISOU  664  N   PRO A 253     5573   4600   4349   -702    -35    344       N  
ATOM    665  CA  PRO A 253     -52.869   6.375  21.631  1.00 35.36           C  
ANISOU  665  CA  PRO A 253     5186   4219   4030   -632    -72    362       C  
ATOM    666  C   PRO A 253     -54.185   5.671  21.844  1.00 33.61           C  
ANISOU  666  C   PRO A 253     4989   3963   3820   -652    -30    318       C  
ATOM    667  O   PRO A 253     -54.580   4.951  20.940  1.00 33.61           O  
ANISOU  667  O   PRO A 253     4951   3947   3870   -579    -35    306       O  
ATOM    668  CB  PRO A 253     -51.723   5.540  22.196  1.00 38.71           C  
ANISOU  668  CB  PRO A 253     5632   4648   4429   -653   -153    442       C  
ATOM    669  CG  PRO A 253     -50.934   6.421  23.050  1.00 40.91           C  
ANISOU  669  CG  PRO A 253     5943   4951   4650   -723   -167    471       C  
ATOM    670  CD  PRO A 253     -51.675   7.693  23.322  1.00 36.11           C  
ANISOU  670  CD  PRO A 253     5348   4353   4020   -769    -87    406       C  
ATOM    671  N   ARG A 254     -54.876   5.884  22.963  1.00 32.37           N  
ANISOU  671  N   ARG A 254     4890   3789   3619   -750     16    289       N  
ATOM    672  CA  ARG A 254     -56.280   5.378  23.077  1.00 35.88           C  
ANISOU  672  CA  ARG A 254     5353   4193   4088   -766     73    231       C  
ATOM    673  C   ARG A 254     -57.273   6.060  22.162  1.00 32.53           C  
ANISOU  673  C   ARG A 254     4877   3750   3735   -713    133    162       C  
ATOM    674  O   ARG A 254     -58.386   5.561  21.975  1.00 37.96           O  
ANISOU  674  O   ARG A 254     5563   4400   4462   -701    170    118       O  
ATOM    675  CB  ARG A 254     -56.825   5.529  24.515  1.00 38.96           C  
ANISOU  675  CB  ARG A 254     5820   4566   4418   -893    121    204       C  
ATOM    676  CG  ARG A 254     -56.100   4.682  25.542  1.00 55.75           C  
ANISOU  676  CG  ARG A 254     7985   6714   6482   -936     53    255       C  
ATOM    677  CD  ARG A 254     -56.436   5.118  26.974  1.00 66.88           C  
ANISOU  677  CD  ARG A 254     9439   8141   7831  -1028     85    205       C  
ATOM    678  NE  ARG A 254     -55.468   4.590  27.941  1.00 76.66           N  
ANISOU  678  NE  ARG A 254    10711   9408   9010  -1076      6    262       N  
ATOM    679  CZ  ARG A 254     -54.240   5.074  28.118  1.00 79.65           C  
ANISOU  679  CZ  ARG A 254    11075   9821   9366  -1082    -52    310       C  
ATOM    680  NH1 ARG A 254     -53.435   4.531  29.017  1.00 81.09           N  
ANISOU  680  NH1 ARG A 254    11283  10021   9507  -1129   -128    358       N  
ATOM    681  NH2 ARG A 254     -53.812   6.098  27.393  1.00 80.49           N  
ANISOU  681  NH2 ARG A 254    11141   9943   9499  -1040    -36    309       N  
ATOM    682  N   LYS A 255     -56.923   7.240  21.651  1.00 34.04           N  
ANISOU  682  N   LYS A 255     5026   3963   3944   -688    144    154       N  
ATOM    683  CA  LYS A 255     -57.842   7.994  20.806  1.00 35.31           C  
ANISOU  683  CA  LYS A 255     5135   4104   4178   -647    193     97       C  
ATOM    684  C   LYS A 255     -57.103   8.606  19.604  1.00 27.87           C  
ANISOU  684  C   LYS A 255     4129   3195   3264   -562    155    121       C  
ATOM    685  O   LYS A 255     -56.944   9.870  19.499  1.00 30.61           O  
ANISOU  685  O   LYS A 255     4450   3556   3624   -572    181    106       O  
ATOM    686  CB  LYS A 255     -58.482   9.111  21.634  1.00 40.72           C  
ANISOU  686  CB  LYS A 255     5836   4767   4867   -736    273     43       C  
ATOM    687  CG  LYS A 255     -59.747   9.716  21.020  1.00 59.00           C  
ANISOU  687  CG  LYS A 255     8102   7038   7278   -715    333    -23       C  
ATOM    688  CD  LYS A 255     -60.294  10.802  21.937  1.00 64.42           C  
ANISOU  688  CD  LYS A 255     8791   7709   7977   -796    412    -80       C  
ATOM    689  CE  LYS A 255     -61.742  11.153  21.634  1.00 72.26           C  
ANISOU  689  CE  LYS A 255     9724   8661   9071   -764    464   -147       C  
ATOM    690  NZ  LYS A 255     -61.912  11.988  20.403  1.00 77.01           N  
ANISOU  690  NZ  LYS A 255    10254   9244   9762   -711    460   -149       N  
ATOM    691  N   PRO A 256     -56.647   7.736  18.692  1.00 29.58           N  
ANISOU  691  N   PRO A 256     4322   3423   3494   -484    100    154       N  
ATOM    692  CA  PRO A 256     -55.938   8.202  17.500  1.00 30.18           C  
ANISOU  692  CA  PRO A 256     4346   3529   3593   -409     67    173       C  
ATOM    693  C   PRO A 256     -56.838   9.182  16.734  1.00 28.94           C  
ANISOU  693  C   PRO A 256     4144   3357   3495   -388    105    127       C  
ATOM    694  O   PRO A 256     -58.086   9.080  16.762  1.00 28.62           O  
ANISOU  694  O   PRO A 256     4101   3276   3498   -402    145     83       O  
ATOM    695  CB  PRO A 256     -55.720   6.909  16.679  1.00 23.54           C  
ANISOU  695  CB  PRO A 256     3490   2685   2768   -344     23    196       C  
ATOM    696  CG  PRO A 256     -55.838   5.777  17.726  1.00 30.77           C  
ANISOU  696  CG  PRO A 256     4456   3583   3654   -390     16    213       C  
ATOM    697  CD  PRO A 256     -56.937   6.286  18.626  1.00 25.09           C  
ANISOU  697  CD  PRO A 256     3768   2835   2929   -462     78    165       C  
ATOM    698  N   VAL A 257     -56.206  10.168  16.103  1.00 25.10           N  
ANISOU  698  N   VAL A 257     3621   2899   3016   -358     93    139       N  
ATOM    699  CA  VAL A 257     -56.910  11.145  15.248  1.00 24.24           C  
ANISOU  699  CA  VAL A 257     3463   2779   2969   -334    115    108       C  
ATOM    700  C   VAL A 257     -56.429  11.017  13.807  1.00 26.68           C  
ANISOU  700  C   VAL A 257     3736   3110   3292   -258     68    131       C  
ATOM    701  O   VAL A 257     -55.214  11.086  13.548  1.00 22.23           O  
ANISOU  701  O   VAL A 257     3172   2582   2693   -232     35    165       O  
ATOM    702  CB  VAL A 257     -56.630  12.599  15.693  1.00 27.14           C  
ANISOU  702  CB  VAL A 257     3814   3159   3338   -372    148     99       C  
ATOM    703  CG1 VAL A 257     -57.495  13.555  14.837  1.00 28.91           C  
ANISOU  703  CG1 VAL A 257     3980   3361   3644   -352    168     70       C  
ATOM    704  CG2 VAL A 257     -56.950  12.743  17.165  1.00 36.42           C  
ANISOU  704  CG2 VAL A 257     5033   4318   4488   -462    200     76       C  
ATOM    705  N   PHE A 258     -57.364  10.751  12.903  1.00 22.46           N  
ANISOU  705  N   PHE A 258     3176   2550   2806   -227     65    111       N  
ATOM    706  CA  PHE A 258     -57.047  10.487  11.512  1.00 21.65           C  
ANISOU  706  CA  PHE A 258     3048   2465   2711   -168     23    127       C  
ATOM    707  C   PHE A 258     -57.306  11.787  10.759  1.00 25.43           C  
ANISOU  707  C   PHE A 258     3484   2946   3230   -161     23    121       C  
ATOM    708  O   PHE A 258     -58.439  12.217  10.703  1.00 24.42           O  
ANISOU  708  O   PHE A 258     3334   2782   3163   -178     43     96       O  
ATOM    709  CB  PHE A 258     -58.012   9.435  10.935  1.00 23.98           C  
ANISOU  709  CB  PHE A 258     3343   2731   3036   -148     17    110       C  
ATOM    710  CG  PHE A 258     -57.559   8.874   9.594  1.00 33.35           C  
ANISOU  710  CG  PHE A 258     4518   3939   4214    -99    -22    126       C  
ATOM    711  CD1 PHE A 258     -56.275   9.158   9.096  1.00 36.23           C  
ANISOU  711  CD1 PHE A 258     4879   4343   4546    -76    -46    153       C  
ATOM    712  CD2 PHE A 258     -58.397   8.121   8.823  1.00 44.71           C  
ANISOU  712  CD2 PHE A 258     5950   5357   5680    -80    -31    111       C  
ATOM    713  CE1 PHE A 258     -55.872   8.643   7.851  1.00 38.82           C  
ANISOU  713  CE1 PHE A 258     5199   4686   4867    -42    -71    159       C  
ATOM    714  CE2 PHE A 258     -58.004   7.604   7.581  1.00 35.50           C  
ANISOU  714  CE2 PHE A 258     4776   4210   4501    -47    -60    121       C  
ATOM    715  CZ  PHE A 258     -56.775   7.851   7.095  1.00 27.79           C  
ANISOU  715  CZ  PHE A 258     3798   3269   3491    -31    -76    142       C  
ATOM    716  N   TRP A 259     -56.267  12.397  10.191  1.00 23.15           N  
ANISOU  716  N   TRP A 259     3184   2697   2917   -136     -1    145       N  
ATOM    717  CA  TRP A 259     -56.460  13.595   9.377  1.00 22.24           C  
ANISOU  717  CA  TRP A 259     3026   2585   2838   -128     -8    146       C  
ATOM    718  C   TRP A 259     -56.793  13.274   7.939  1.00 20.69           C  
ANISOU  718  C   TRP A 259     2816   2388   2659    -95    -47    152       C  
ATOM    719  O   TRP A 259     -55.985  12.671   7.253  1.00 20.66           O  
ANISOU  719  O   TRP A 259     2827   2410   2613    -67    -73    167       O  
ATOM    720  CB  TRP A 259     -55.174  14.440   9.355  1.00 21.37           C  
ANISOU  720  CB  TRP A 259     2911   2517   2691   -117    -15    168       C  
ATOM    721  CG  TRP A 259     -54.862  15.081  10.634  1.00 23.87           C  
ANISOU  721  CG  TRP A 259     3235   2839   2995   -156     21    163       C  
ATOM    722  CD1 TRP A 259     -55.522  14.945  11.822  1.00 27.29           C  
ANISOU  722  CD1 TRP A 259     3687   3245   3437   -206     62    141       C  
ATOM    723  CD2 TRP A 259     -53.752  15.957  10.873  1.00 21.47           C  
ANISOU  723  CD2 TRP A 259     2927   2571   2661   -155     23    179       C  
ATOM    724  NE1 TRP A 259     -54.897  15.731  12.789  1.00 29.34           N  
ANISOU  724  NE1 TRP A 259     3954   3523   3670   -243     90    142       N  
ATOM    725  CE2 TRP A 259     -53.825  16.362  12.223  1.00 25.95           C  
ANISOU  725  CE2 TRP A 259     3508   3133   3219   -209     65    166       C  
ATOM    726  CE3 TRP A 259     -52.753  16.492  10.057  1.00 22.03           C  
ANISOU  726  CE3 TRP A 259     2982   2674   2714   -117     -3    199       C  
ATOM    727  CZ2 TRP A 259     -52.877  17.259  12.807  1.00 25.45           C  
ANISOU  727  CZ2 TRP A 259     3444   3100   3125   -225     79    177       C  
ATOM    728  CZ3 TRP A 259     -51.797  17.389  10.634  1.00 23.61           C  
ANISOU  728  CZ3 TRP A 259     3179   2902   2889   -126     11    209       C  
ATOM    729  CH2 TRP A 259     -51.880  17.740  11.997  1.00 28.72           C  
ANISOU  729  CH2 TRP A 259     3840   3547   3525   -179     50    199       C  
ATOM    730  N   LEU A 260     -57.963  13.744   7.483  1.00 19.47           N  
ANISOU  730  N   LEU A 260     2629   2199   2569   -106    -51    141       N  
ATOM    731  CA ALEU A 260     -58.438  13.566   6.123  0.37 22.47           C  
ANISOU  731  CA ALEU A 260     2995   2574   2968    -89    -94    150       C  
ATOM    732  CA BLEU A 260     -58.411  13.563   6.130  0.63 21.00           C  
ANISOU  732  CA BLEU A 260     2809   2389   2781    -89    -93    151       C  
ATOM    733  C   LEU A 260     -58.478  14.962   5.530  1.00 25.35           C  
ANISOU  733  C   LEU A 260     3319   2943   3371    -96   -112    167       C  
ATOM    734  O   LEU A 260     -58.539  15.915   6.255  1.00 28.10           O  
ANISOU  734  O   LEU A 260     3641   3281   3754   -115    -83    160       O  
ATOM    735  CB ALEU A 260     -59.886  13.043   6.098  0.37 25.93           C  
ANISOU  735  CB ALEU A 260     3424   2961   3469   -101    -92    130       C  
ATOM    736  CB BLEU A 260     -59.852  13.086   6.160  0.63 22.83           C  
ANISOU  736  CB BLEU A 260     3030   2567   3075   -102    -90    130       C  
ATOM    737  CG ALEU A 260     -60.232  11.612   6.488  0.37 33.54           C  
ANISOU  737  CG ALEU A 260     4421   3909   4414    -95    -78    112       C  
ATOM    738  CG BLEU A 260     -60.160  11.920   5.289  0.63 32.28           C  
ANISOU  738  CG BLEU A 260     4246   3763   4254    -84   -119    131       C  
ATOM    739  CD1ALEU A 260     -61.431  11.102   5.667  0.37 33.38           C  
ANISOU  739  CD1ALEU A 260     4387   3851   4443    -92   -103    104       C  
ATOM    740  CD1BLEU A 260     -59.519  10.776   6.031  0.63 36.74           C  
ANISOU  740  CD1BLEU A 260     4851   4345   4764    -72    -94    122       C  
ATOM    741  CD2ALEU A 260     -59.042  10.745   6.266  0.37 36.33           C  
ANISOU  741  CD2ALEU A 260     4808   4306   4690    -70    -88    126       C  
ATOM    742  CD2BLEU A 260     -61.656  11.823   5.327  0.63 37.13           C  
ANISOU  742  CD2BLEU A 260     4839   4319   4950   -100   -117    112       C  
ATOM    743  N   SER A 261     -58.473  15.041   4.212  1.00 21.12           N  
ANISOU  743  N   SER A 261     2777   2419   2829    -85   -160    187       N  
ATOM    744  CA  SER A 261     -58.589  16.322   3.503  1.00 20.65           C  
ANISOU  744  CA  SER A 261     2677   2359   2808    -95   -189    210       C  
ATOM    745  C   SER A 261     -60.028  16.759   3.454  1.00 25.56           C  
ANISOU  745  C   SER A 261     3254   2922   3534   -120   -200    208       C  
ATOM    746  O   SER A 261     -60.881  15.991   3.042  1.00 24.87           O  
ANISOU  746  O   SER A 261     3174   2807   3470   -124   -222    204       O  
ATOM    747  CB  SER A 261     -58.014  16.221   2.093  1.00 21.36           C  
ANISOU  747  CB  SER A 261     2786   2484   2845    -86   -238    234       C  
ATOM    748  OG  SER A 261     -58.429  17.396   1.299  1.00 21.23           O  
ANISOU  748  OG  SER A 261     2730   2458   2879   -105   -280    262       O  
ATOM    749  N   ARG A 262     -60.327  17.986   3.887  1.00 23.82           N  
ANISOU  749  N   ARG A 262     2983   2679   3388   -139   -183    209       N  
ATOM    750  CA  ARG A 262     -61.673  18.530   3.745  1.00 27.64           C  
ANISOU  750  CA  ARG A 262     3410   3097   3994   -165   -197    211       C  
ATOM    751  C   ARG A 262     -62.019  18.695   2.277  1.00 28.13           C  
ANISOU  751  C   ARG A 262     3459   3156   4072   -169   -279    253       C  
ATOM    752  O   ARG A 262     -63.096  18.268   1.826  1.00 28.47           O  
ANISOU  752  O   ARG A 262     3490   3153   4174   -182   -313    258       O  
ATOM    753  CB  ARG A 262     -61.818  19.916   4.457  1.00 28.42           C  
ANISOU  753  CB  ARG A 262     3447   3169   4180   -189   -157    204       C  
ATOM    754  CG  ARG A 262     -63.293  20.400   4.466  1.00 26.35           C  
ANISOU  754  CG  ARG A 262     3118   2821   4072   -220   -161    199       C  
ATOM    755  CD  ARG A 262     -63.412  21.760   5.089  1.00 33.10           C  
ANISOU  755  CD  ARG A 262     3906   3647   5025   -247   -116    189       C  
ATOM    756  NE  ARG A 262     -62.988  22.767   4.128  1.00 34.54           N  
ANISOU  756  NE  ARG A 262     4051   3853   5220   -241   -172    238       N  
ATOM    757  CZ  ARG A 262     -62.050  23.674   4.346  1.00 39.23           C  
ANISOU  757  CZ  ARG A 262     4631   4490   5784   -235   -148    244       C  
ATOM    758  NH1 ARG A 262     -61.414  23.731   5.518  1.00 42.88           N  
ANISOU  758  NH1 ARG A 262     5115   4977   6200   -239    -71    206       N  
ATOM    759  NH2 ARG A 262     -61.790  24.553   3.382  1.00 33.57           N  
ANISOU  759  NH2 ARG A 262     3879   3788   5087   -232   -205    290       N  
ATOM    760  N   GLN A 263     -61.134  19.344   1.506  1.00 24.45           N  
ANISOU  760  N   GLN A 263     2997   2738   3556   -163   -312    285       N  
ATOM    761  CA  GLN A 263     -61.454  19.665   0.097  1.00 27.88           C  
ANISOU  761  CA  GLN A 263     3420   3169   4002   -180   -394    330       C  
ATOM    762  C   GLN A 263     -61.599  18.437  -0.770  1.00 32.59           C  
ANISOU  762  C   GLN A 263     4072   3780   4532   -182   -433    333       C  
ATOM    763  O   GLN A 263     -62.406  18.403  -1.699  1.00 26.67           O  
ANISOU  763  O   GLN A 263     3311   3003   3818   -208   -498    363       O  
ATOM    764  CB  GLN A 263     -60.357  20.517  -0.499  1.00 28.42           C  
ANISOU  764  CB  GLN A 263     3494   3291   4015   -176   -414    357       C  
ATOM    765  CG  GLN A 263     -60.393  21.926   0.053  1.00 29.09           C  
ANISOU  765  CG  GLN A 263     3510   3356   4185   -183   -392    365       C  
ATOM    766  CD  GLN A 263     -59.479  22.147   1.250  1.00 25.82           C  
ANISOU  766  CD  GLN A 263     3104   2973   3735   -160   -313    330       C  
ATOM    767  OE1 GLN A 263     -59.061  21.192   1.928  1.00 25.03           O  
ANISOU  767  OE1 GLN A 263     3051   2891   3568   -143   -271    298       O  
ATOM    768  NE2 GLN A 263     -59.171  23.440   1.536  1.00 24.35           N  
ANISOU  768  NE2 GLN A 263     2866   2789   3596   -164   -294    338       N  
ATOM    769  N   ARG A 264     -60.742  17.444  -0.538  1.00 26.46           N  
ANISOU  769  N   ARG A 264     3352   3046   3655   -157   -396    306       N  
ATOM    770  CA  ARG A 264     -60.727  16.291  -1.433  1.00 28.86           C  
ANISOU  770  CA  ARG A 264     3706   3368   3890   -161   -424    306       C  
ATOM    771  C   ARG A 264     -61.478  15.062  -0.903  1.00 29.15           C  
ANISOU  771  C   ARG A 264     3757   3375   3944   -152   -399    274       C  
ATOM    772  O   ARG A 264     -61.459  14.042  -1.558  1.00 25.56           O  
ANISOU  772  O   ARG A 264     3342   2935   3435   -154   -413    269       O  
ATOM    773  CB  ARG A 264     -59.291  15.936  -1.823  1.00 25.94           C  
ANISOU  773  CB  ARG A 264     3387   3059   3408   -147   -407    299       C  
ATOM    774  CG  ARG A 264     -58.575  17.105  -2.576  1.00 26.37           C  
ANISOU  774  CG  ARG A 264     3435   3144   3440   -161   -439    330       C  
ATOM    775  CD  ARG A 264     -57.045  16.941  -2.642  1.00 30.48           C  
ANISOU  775  CD  ARG A 264     3995   3715   3869   -141   -404    314       C  
ATOM    776  NE  ARG A 264     -56.413  17.101  -1.313  1.00 28.03           N  
ANISOU  776  NE  ARG A 264     3672   3412   3567   -105   -345    293       N  
ATOM    777  CZ  ARG A 264     -55.583  16.209  -0.747  1.00 28.50           C  
ANISOU  777  CZ  ARG A 264     3762   3488   3577    -80   -301    266       C  
ATOM    778  NH1 ARG A 264     -55.229  15.092  -1.373  1.00 27.52           N  
ANISOU  778  NH1 ARG A 264     3680   3376   3401    -82   -300    252       N  
ATOM    779  NH2 ARG A 264     -55.100  16.440   0.468  1.00 24.23           N  
ANISOU  779  NH2 ARG A 264     3210   2950   3046    -58   -259    255       N  
ATOM    780  N   ASN A 265     -62.096  15.171   0.270  1.00 29.97           N  
ANISOU  780  N   ASN A 265     3830   3436   4119   -145   -357    251       N  
ATOM    781  CA  ASN A 265     -63.078  14.187   0.771  1.00 36.13           C  
ANISOU  781  CA  ASN A 265     4616   4174   4940   -142   -336    223       C  
ATOM    782  C   ASN A 265     -64.297  14.040  -0.176  1.00 37.38           C  
ANISOU  782  C   ASN A 265     4755   4288   5160   -165   -399    242       C  
ATOM    783  O   ASN A 265     -64.901  15.022  -0.615  1.00 31.79           O  
ANISOU  783  O   ASN A 265     4000   3546   4532   -190   -444    273       O  
ATOM    784  CB  ASN A 265     -63.578  14.636   2.171  1.00 32.46           C  
ANISOU  784  CB  ASN A 265     4117   3663   4554   -146   -278    194       C  
ATOM    785  CG  ASN A 265     -64.744  13.786   2.714  1.00 34.90           C  
ANISOU  785  CG  ASN A 265     4425   3914   4923   -149   -255    161       C  
ATOM    786  OD1 ASN A 265     -64.682  12.559   2.705  1.00 35.42           O  
ANISOU  786  OD1 ASN A 265     4531   3993   4932   -132   -245    145       O  
ATOM    787  ND2 ASN A 265     -65.804  14.447   3.177  1.00 44.16           N  
ANISOU  787  ND2 ASN A 265     5546   5017   6217   -172   -241    150       N  
ATOM    788  N   THR A 266     -64.679  12.796  -0.457  1.00 28.35           N  
ANISOU  788  N   THR A 266     3644   3141   3986   -159   -401    226       N  
ATOM    789  CA  THR A 266     -65.809  12.549  -1.330  1.00 26.87           C  
ANISOU  789  CA  THR A 266     3444   2915   3852   -183   -461    244       C  
ATOM    790  C   THR A 266     -66.885  11.795  -0.537  1.00 33.03           C  
ANISOU  790  C   THR A 266     4213   3635   4703   -171   -426    206       C  
ATOM    791  O   THR A 266     -67.871  11.369  -1.109  1.00 29.81           O  
ANISOU  791  O   THR A 266     3797   3189   4341   -185   -466    213       O  
ATOM    792  CB  THR A 266     -65.378  11.651  -2.498  1.00 34.11           C  
ANISOU  792  CB  THR A 266     4414   3880   4667   -193   -494    253       C  
ATOM    793  OG1 THR A 266     -64.702  10.459  -1.981  1.00 27.77           O  
ANISOU  793  OG1 THR A 266     3653   3110   3790   -161   -431    213       O  
ATOM    794  CG2 THR A 266     -64.467  12.430  -3.447  1.00 32.88           C  
ANISOU  794  CG2 THR A 266     4272   3773   4447   -216   -534    290       C  
ATOM    795  N   MET A 267     -66.631  11.560   0.749  1.00 34.88           N  
ANISOU  795  N   MET A 267     4008   4526   4718     26   -196   -360       N  
ATOM    796  CA  MET A 267     -67.499  10.747   1.596  1.00 33.87           C  
ANISOU  796  CA  MET A 267     3847   4366   4658     18   -106   -335       C  
ATOM    797  C   MET A 267     -68.582  11.529   2.321  1.00 40.23           C  
ANISOU  797  C   MET A 267     4660   5140   5484     39     -4   -336       C  
ATOM    798  O   MET A 267     -68.346  12.633   2.818  1.00 35.81           O  
ANISOU  798  O   MET A 267     4182   4584   4841     46     25   -339       O  
ATOM    799  CB  MET A 267     -66.667   9.992   2.647  1.00 38.69           C  
ANISOU  799  CB  MET A 267     4527   4980   5194    -22    -81   -296       C  
ATOM    800  CG  MET A 267     -65.567   9.162   2.051  1.00 45.15           C  
ANISOU  800  CG  MET A 267     5341   5827   5985    -46   -175   -290       C  
ATOM    801  SD  MET A 267     -65.012   7.727   3.045  1.00 46.85           S  
ANISOU  801  SD  MET A 267     5582   6039   6179    -90   -145   -244       S  
ATOM    802  CE  MET A 267     -65.013   6.630   1.629  1.00 78.21           C  
ANISOU  802  CE  MET A 267     9441  10023  10252    -88   -244   -261       C  
ATOM    803  N   SER A 268     -69.750  10.912   2.449  1.00 32.18           N  
ANISOU  803  N   SER A 268     3561   4090   4575     48     54   -331       N  
ATOM    804  CA  SER A 268     -70.851  11.485   3.223  1.00 31.25           C  
ANISOU  804  CA  SER A 268     3447   3940   4489     67    159   -327       C  
ATOM    805  C   SER A 268     -70.537  11.317   4.679  1.00 34.93           C  
ANISOU  805  C   SER A 268     3998   4395   4879     41    239   -290       C  
ATOM    806  O   SER A 268     -69.611  10.614   5.046  1.00 28.04           O  
ANISOU  806  O   SER A 268     3167   3537   3949      9    215   -267       O  
ATOM    807  CB  SER A 268     -72.138  10.710   2.950  1.00 32.04           C  
ANISOU  807  CB  SER A 268     3433   4010   4731     81    194   -328       C  
ATOM    808  OG  SER A 268     -72.030   9.410   3.540  1.00 29.64           O  
ANISOU  808  OG  SER A 268     3115   3697   4449     52    218   -296       O  
ATOM    809  N   LYS A 269     -71.338  11.935   5.537  1.00 36.99           N  
ANISOU  809  N   LYS A 269     4284   4629   5141     54    336   -283       N  
ATOM    810  CA  LYS A 269     -71.120  11.814   6.981  1.00 39.01           C  
ANISOU  810  CA  LYS A 269     4622   4872   5327     31    420   -248       C  
ATOM    811  C   LYS A 269     -71.178  10.350   7.440  1.00 30.50           C  
ANISOU  811  C   LYS A 269     3508   3783   4298      4    442   -217       C  
ATOM    812  O   LYS A 269     -70.431   9.918   8.306  1.00 33.41           O  
ANISOU  812  O   LYS A 269     3945   4157   4592    -27    461   -188       O  
ATOM    813  CB  LYS A 269     -72.189  12.615   7.722  1.00 47.77           C  
ANISOU  813  CB  LYS A 269     5744   5950   6455     54    524   -247       C  
ATOM    814  CG  LYS A 269     -71.957  12.706   9.214  1.00 58.52           C  
ANISOU  814  CG  LYS A 269     7201   7299   7735     33    612   -213       C  
ATOM    815  CD  LYS A 269     -73.033  13.569   9.897  1.00 71.82           C  
ANISOU  815  CD  LYS A 269     8898   8953   9439     59    713   -214       C  
ATOM    816  CE  LYS A 269     -72.786  13.673  11.403  1.00 79.70           C  
ANISOU  816  CE  LYS A 269     9993   9937  10352     38    801   -181       C  
ATOM    817  NZ  LYS A 269     -73.994  14.153  12.146  1.00 84.05           N  
ANISOU  817  NZ  LYS A 269    10538  10453  10945     60    911   -175       N  
ATOM    818  N   LYS A 270     -72.105   9.601   6.856  1.00 33.82           N  
ANISOU  818  N   LYS A 270     3818   4186   4844     16    440   -224       N  
ATOM    819  CA  LYS A 270     -72.293   8.200   7.199  1.00 32.99           C  
ANISOU  819  CA  LYS A 270     3666   4069   4799     -6    460   -197       C  
ATOM    820  C   LYS A 270     -71.064   7.383   6.755  1.00 25.98           C  
ANISOU  820  C   LYS A 270     2790   3212   3869    -36    369   -191       C  
ATOM    821  O   LYS A 270     -70.613   6.487   7.465  1.00 29.02           O  
ANISOU  821  O   LYS A 270     3200   3597   4228    -67    388   -160       O  
ATOM    822  CB  LYS A 270     -73.573   7.690   6.511  1.00 39.78           C  
ANISOU  822  CB  LYS A 270     4401   4906   5806     17    469   -211       C  
ATOM    823  CG  LYS A 270     -73.687   6.172   6.419  1.00 42.09           C  
ANISOU  823  CG  LYS A 270     4623   5192   6175     -3    456   -192       C  
ATOM    824  CD  LYS A 270     -73.969   5.546   7.763  1.00 56.92           C  
ANISOU  824  CD  LYS A 270     6531   7048   8049    -24    552   -154       C  
ATOM    825  CE  LYS A 270     -74.270   4.037   7.613  1.00 60.98           C  
ANISOU  825  CE  LYS A 270     6961   7552   8656    -40    543   -137       C  
ATOM    826  NZ  LYS A 270     -74.287   3.341   8.923  1.00 56.86           N  
ANISOU  826  NZ  LYS A 270     6478   7014   8114    -66    624    -98       N  
ATOM    827  N   GLU A 271     -70.545   7.649   5.562  1.00 27.83           N  
ANISOU  827  N   GLU A 271     3002   3474   4100    -26    270   -219       N  
ATOM    828  CA  GLU A 271     -69.331   6.952   5.151  1.00 27.63           C  
ANISOU  828  CA  GLU A 271     2993   3478   4025    -54    183   -212       C  
ATOM    829  C   GLU A 271     -68.151   7.229   6.091  1.00 26.48           C  
ANISOU  829  C   GLU A 271     2971   3350   3741    -82    193   -188       C  
ATOM    830  O   GLU A 271     -67.364   6.337   6.361  1.00 25.54           O  
ANISOU  830  O   GLU A 271     2873   3244   3589   -114    168   -165       O  
ATOM    831  CB  GLU A 271     -68.927   7.356   3.754  1.00 28.10           C  
ANISOU  831  CB  GLU A 271     3019   3565   4092    -37     76   -247       C  
ATOM    832  CG  GLU A 271     -69.912   6.897   2.724  1.00 32.25           C  
ANISOU  832  CG  GLU A 271     3422   4077   4753    -14     49   -269       C  
ATOM    833  CD  GLU A 271     -69.458   7.229   1.327  1.00 35.71           C  
ANISOU  833  CD  GLU A 271     3826   4543   5197      1    -60   -303       C  
ATOM    834  OE1 GLU A 271     -68.788   6.351   0.727  1.00 37.44           O  
ANISOU  834  OE1 GLU A 271     4018   4781   5425    -16   -136   -300       O  
ATOM    835  OE2 GLU A 271     -69.770   8.341   0.823  1.00 31.11           O  
ANISOU  835  OE2 GLU A 271     3244   3964   4614     30    -71   -331       O  
ATOM    836  N   LEU A 272     -67.980   8.468   6.523  1.00 26.55           N  
ANISOU  836  N   LEU A 272     3059   3361   3667    -72    222   -195       N  
ATOM    837  CA  LEU A 272     -66.880   8.782   7.466  1.00 22.60           C  
ANISOU  837  CA  LEU A 272     2679   2876   3032    -99    235   -171       C  
ATOM    838  C   LEU A 272     -67.084   8.048   8.779  1.00 24.96           C  
ANISOU  838  C   LEU A 272     3005   3152   3325   -124    325   -133       C  
ATOM    839  O   LEU A 272     -66.137   7.576   9.387  1.00 24.38           O  
ANISOU  839  O   LEU A 272     2996   3092   3175   -157    319   -106       O  
ATOM    840  CB  LEU A 272     -66.817  10.297   7.709  1.00 20.65           C  
ANISOU  840  CB  LEU A 272     2508   2632   2707    -80    259   -186       C  
ATOM    841  CG  LEU A 272     -66.428  11.020   6.434  1.00 30.15           C  
ANISOU  841  CG  LEU A 272     3694   3862   3900    -59    162   -223       C  
ATOM    842  CD1 LEU A 272     -66.598  12.552   6.672  1.00 34.18           C  
ANISOU  842  CD1 LEU A 272     4268   4370   4349    -36    196   -239       C  
ATOM    843  CD2 LEU A 272     -64.998  10.687   6.096  1.00 33.93           C  
ANISOU  843  CD2 LEU A 272     4219   4377   4297    -86     72   -216       C  
ATOM    844  N   GLU A 273     -68.330   7.879   9.205  1.00 27.86           N  
ANISOU  844  N   GLU A 273     3321   3485   3779   -109    409   -128       N  
ATOM    845  CA  GLU A 273     -68.583   7.160  10.454  1.00 28.08           C  
ANISOU  845  CA  GLU A 273     3370   3490   3807   -132    497    -91       C  
ATOM    846  C   GLU A 273     -68.198   5.685  10.276  1.00 28.97           C  
ANISOU  846  C   GLU A 273     3436   3611   3960   -160    457    -73       C  
ATOM    847  O   GLU A 273     -67.629   5.070  11.186  1.00 30.03           O  
ANISOU  847  O   GLU A 273     3624   3746   4042   -192    486    -41       O  
ATOM    848  CB  GLU A 273     -70.077   7.283  10.884  1.00 37.59           C  
ANISOU  848  CB  GLU A 273     4521   4656   5104   -107    594    -91       C  
ATOM    849  CG  GLU A 273     -70.540   8.738  11.112  1.00 52.15           C  
ANISOU  849  CG  GLU A 273     6411   6490   6912    -78    641   -109       C  
ATOM    850  CD  GLU A 273     -72.051   8.894  11.414  1.00 63.58           C  
ANISOU  850  CD  GLU A 273     7799   7900   8458    -51    731   -111       C  
ATOM    851  OE1 GLU A 273     -72.863   8.034  10.977  1.00 66.33           O  
ANISOU  851  OE1 GLU A 273     8046   8234   8923    -44    733   -112       O  
ATOM    852  OE2 GLU A 273     -72.422   9.888  12.088  1.00 56.80           O  
ANISOU  852  OE2 GLU A 273     6996   7028   7558    -37    800   -111       O  
ATOM    853  N   VAL A 274     -68.500   5.120   9.109  1.00 25.65           N  
ANISOU  853  N   VAL A 274     2917   3196   3632   -148    390    -93       N  
ATOM    854  CA  VAL A 274     -68.170   3.733   8.836  1.00 22.39           C  
ANISOU  854  CA  VAL A 274     2453   2790   3264   -172    347    -78       C  
ATOM    855  C   VAL A 274     -66.650   3.582   8.829  1.00 26.20           C  
ANISOU  855  C   VAL A 274     3012   3307   3637   -202    278    -67       C  
ATOM    856  O   VAL A 274     -66.121   2.700   9.465  1.00 26.44           O  
ANISOU  856  O   VAL A 274     3067   3339   3639   -234    289    -38       O  
ATOM    857  CB  VAL A 274     -68.800   3.217   7.501  1.00 25.50           C  
ANISOU  857  CB  VAL A 274     2726   3184   3780   -151    284   -105       C  
ATOM    858  CG1 VAL A 274     -68.137   1.912   7.048  1.00 25.79           C  
ANISOU  858  CG1 VAL A 274     2724   3236   3838   -177    215    -93       C  
ATOM    859  CG2 VAL A 274     -70.307   3.054   7.664  1.00 30.32           C  
ANISOU  859  CG2 VAL A 274     3256   3757   4506   -128    361   -106       C  
ATOM    860  N   LEU A 275     -65.973   4.488   8.147  1.00 24.57           N  
ANISOU  860  N   LEU A 275     2843   3127   3367   -191    209    -91       N  
ATOM    861  CA  LEU A 275     -64.515   4.514   8.159  1.00 26.02           C  
ANISOU  861  CA  LEU A 275     3106   3342   3437   -218    145    -81       C  
ATOM    862  C   LEU A 275     -63.941   4.543   9.566  1.00 26.40           C  
ANISOU  862  C   LEU A 275     3259   3388   3386   -248    210    -46       C  
ATOM    863  O   LEU A 275     -63.027   3.777   9.870  1.00 25.62           O  
ANISOU  863  O   LEU A 275     3194   3304   3238   -281    184    -22       O  
ATOM    864  CB  LEU A 275     -63.995   5.673   7.284  1.00 25.83           C  
ANISOU  864  CB  LEU A 275     3111   3344   3359   -198     72   -113       C  
ATOM    865  CG  LEU A 275     -62.441   5.847   7.215  1.00 25.39           C  
ANISOU  865  CG  LEU A 275     3142   3325   3180   -222     -2   -106       C  
ATOM    866  CD1 LEU A 275     -61.706   4.561   6.682  1.00 24.81           C  
ANISOU  866  CD1 LEU A 275     3030   3270   3125   -248    -77    -94       C  
ATOM    867  CD2 LEU A 275     -62.078   7.088   6.438  1.00 30.78           C  
ANISOU  867  CD2 LEU A 275     3853   4028   3813   -199    -61   -137       C  
ATOM    868  N   SER A 276     -64.456   5.410  10.436  1.00 26.64           N  
ANISOU  868  N   SER A 276     3340   3398   3384   -236    296    -42       N  
ATOM    869  CA  SER A 276     -63.970   5.492  11.815  1.00 23.87           C  
ANISOU  869  CA  SER A 276     3089   3041   2938   -263    364     -8       C  
ATOM    870  C   SER A 276     -64.127   4.163  12.519  1.00 27.58           C  
ANISOU  870  C   SER A 276     3533   3496   3450   -291    408     24       C  
ATOM    871  O   SER A 276     -63.248   3.717  13.283  1.00 25.73           O  
ANISOU  871  O   SER A 276     3368   3272   3138   -325    415     54       O  
ATOM    872  CB  SER A 276     -64.809   6.535  12.591  1.00 34.23           C  
ANISOU  872  CB  SER A 276     4439   4328   4240   -241    460    -11       C  
ATOM    873  OG  SER A 276     -64.429   6.503  13.964  1.00 35.50           O  
ANISOU  873  OG  SER A 276     4690   4480   4319   -268    532     23       O  
ATOM    874  N   GLN A 277     -65.236   3.477  12.245  1.00 28.27           N  
ANISOU  874  N   GLN A 277     3519   3561   3662   -276    436     20       N  
ATOM    875  CA  GLN A 277     -65.448   2.187  12.898  1.00 26.51           C  
ANISOU  875  CA  GLN A 277     3265   3322   3484   -302    479     50       C  
ATOM    876  C   GLN A 277     -64.521   1.129  12.350  1.00 28.28           C  
ANISOU  876  C   GLN A 277     3470   3572   3705   -328    394     59       C  
ATOM    877  O   GLN A 277     -64.069   0.251  13.086  1.00 28.60           O  
ANISOU  877  O   GLN A 277     3536   3612   3720   -361    416     90       O  
ATOM    878  CB  GLN A 277     -66.917   1.747  12.745  1.00 35.36           C  
ANISOU  878  CB  GLN A 277     4282   4411   4742   -278    532     44       C  
ATOM    879  CG  GLN A 277     -67.902   2.619  13.549  1.00 39.39           C  
ANISOU  879  CG  GLN A 277     4815   4891   5259   -256    635     44       C  
ATOM    880  CD  GLN A 277     -67.547   2.717  15.024  1.00 53.61           C  
ANISOU  880  CD  GLN A 277     6715   6684   6972   -281    716     78       C  
ATOM    881  OE1 GLN A 277     -67.406   3.820  15.579  1.00 64.57           O  
ANISOU  881  OE1 GLN A 277     8184   8070   8280   -274    754     76       O  
ATOM    882  NE2 GLN A 277     -67.415   1.562  15.678  1.00 65.19           N  
ANISOU  882  NE2 GLN A 277     8175   8144   8453   -310    744    109       N  
ATOM    883  N   LYS A 278     -64.250   1.138  11.051  1.00 26.08           N  
ANISOU  883  N   LYS A 278     3140   3314   3455   -315    298     31       N  
ATOM    884  CA  LYS A 278     -63.296   0.164  10.554  1.00 26.14           C  
ANISOU  884  CA  LYS A 278     3135   3346   3450   -342    217     40       C  
ATOM    885  C   LYS A 278     -61.917   0.407  11.130  1.00 29.35           C  
ANISOU  885  C   LYS A 278     3654   3778   3719   -372    194     60       C  
ATOM    886  O   LYS A 278     -61.196  -0.531  11.408  1.00 26.05           O  
ANISOU  886  O   LYS A 278     3251   3371   3276   -404    174     85       O  
ATOM    887  CB  LYS A 278     -63.205   0.253   9.025  1.00 32.20           C  
ANISOU  887  CB  LYS A 278     3835   4134   4267   -321    114      6       C  
ATOM    888  CG  LYS A 278     -64.552   0.078   8.328  1.00 38.84           C  
ANISOU  888  CG  LYS A 278     4562   4952   5245   -289    127    -17       C  
ATOM    889  CD  LYS A 278     -64.758  -1.330   7.847  1.00 36.27           C  
ANISOU  889  CD  LYS A 278     4146   4623   5012   -300     95    -10       C  
ATOM    890  CE  LYS A 278     -66.203  -1.477   7.322  1.00 40.61           C  
ANISOU  890  CE  LYS A 278     4586   5145   5698   -269    123    -29       C  
ATOM    891  NZ  LYS A 278     -66.414  -2.727   6.513  1.00 36.62           N  
ANISOU  891  NZ  LYS A 278     3981   4640   5292   -273     70    -31       N  
ATOM    892  N   LEU A 279     -61.532   1.682  11.273  1.00 24.96           N  
ANISOU  892  N   LEU A 279     3214   3230   3039   -234      0    367       N  
ATOM    893  CA  LEU A 279     -60.193   1.993  11.809  1.00 22.57           C  
ANISOU  893  CA  LEU A 279     2974   2955   2646   -224     -8    353       C  
ATOM    894  C   LEU A 279     -60.082   1.534  13.264  1.00 24.41           C  
ANISOU  894  C   LEU A 279     3257   3191   2827   -216     59    347       C  
ATOM    895  O   LEU A 279     -59.071   0.966  13.704  1.00 25.21           O  
ANISOU  895  O   LEU A 279     3416   3315   2849   -210     52    342       O  
ATOM    896  CB  LEU A 279     -59.949   3.495  11.708  1.00 21.13           C  
ANISOU  896  CB  LEU A 279     2782   2772   2473   -211    -18    333       C  
ATOM    897  CG  LEU A 279     -59.797   3.984  10.260  1.00 28.61           C  
ANISOU  897  CG  LEU A 279     3695   3721   3454   -213    -86    341       C  
ATOM    898  CD1 LEU A 279     -59.827   5.549  10.248  1.00 32.36           C  
ANISOU  898  CD1 LEU A 279     4152   4186   3957   -200    -81    325       C  
ATOM    899  CD2 LEU A 279     -58.587   3.411   9.539  1.00 33.06           C  
ANISOU  899  CD2 LEU A 279     4291   4311   3959   -217   -148    347       C  
ATOM    900  N   ARG A 280     -61.151   1.751  14.004  1.00 24.51           N  
ANISOU  900  N   ARG A 280     3248   3180   2886   -213    126    347       N  
ATOM    901  CA  ARG A 280     -61.196   1.300  15.377  1.00 26.28           C  
ANISOU  901  CA  ARG A 280     3517   3403   3065   -200    198    346       C  
ATOM    902  C   ARG A 280     -61.074  -0.200  15.454  1.00 31.11           C  
ANISOU  902  C   ARG A 280     4156   4016   3650   -210    205    369       C  
ATOM    903  O   ARG A 280     -60.343  -0.726  16.276  1.00 30.70           O  
ANISOU  903  O   ARG A 280     4167   3981   3518   -196    225    366       O  
ATOM    904  CB  ARG A 280     -62.501   1.717  16.014  1.00 28.62           C  
ANISOU  904  CB  ARG A 280     3777   3671   3428   -198    269    346       C  
ATOM    905  CG  ARG A 280     -62.550   1.270  17.465  1.00 34.14           C  
ANISOU  905  CG  ARG A 280     4526   4369   4075   -179    349    348       C  
ATOM    906  CD  ARG A 280     -63.806   1.750  18.185  1.00 43.54           C  
ANISOU  906  CD  ARG A 280     5684   5532   5327   -174    425    346       C  
ATOM    907  NE  ARG A 280     -63.911   1.037  19.460  1.00 50.75           N  
ANISOU  907  NE  ARG A 280     6647   6442   6193   -156    505    358       N  
ATOM    908  CZ  ARG A 280     -64.377  -0.212  19.576  1.00 54.58           C  
ANISOU  908  CZ  ARG A 280     7136   6907   6694   -168    544    387       C  
ATOM    909  NH1 ARG A 280     -64.795  -0.878  18.503  1.00 50.71           N  
ANISOU  909  NH1 ARG A 280     6598   6400   6271   -198    507    403       N  
ATOM    910  NH2 ARG A 280     -64.424  -0.804  20.764  1.00 53.22           N  
ANISOU  910  NH2 ARG A 280     7016   6733   6473   -147    621    400       N  
ATOM    911  N   ALA A 281     -61.774  -0.915  14.574  1.00 33.81           N  
ANISOU  911  N   ALA A 281     4448   4340   4058   -232    185    389       N  
ATOM    912  CA  ALA A 281     -61.577  -2.356  14.546  1.00 33.19           C  
ANISOU  912  CA  ALA A 281     4391   4262   3958   -242    183    409       C  
ATOM    913  C   ALA A 281     -60.160  -2.766  14.211  1.00 32.24           C  
ANISOU  913  C   ALA A 281     4323   4178   3751   -240    119    405       C  
ATOM    914  O   ALA A 281     -59.683  -3.809  14.680  1.00 32.51           O  
ANISOU  914  O   ALA A 281     4404   4220   3730   -239    132    416       O  
ATOM    915  CB  ALA A 281     -62.581  -3.041  13.585  1.00 31.55           C  
ANISOU  915  CB  ALA A 281     4114   4028   3847   -263    166    425       C  
ATOM    916  N   LEU A 282     -59.469  -1.992  13.392  1.00 27.01           N  
ANISOU  916  N   LEU A 282     3653   3535   3076   -239     52    390       N  
ATOM    917  CA  LEU A 282     -58.068  -2.293  13.074  1.00 26.82           C  
ANISOU  917  CA  LEU A 282     3676   3544   2969   -238     -8    382       C  
ATOM    918  C   LEU A 282     -57.050  -1.980  14.198  1.00 26.59           C  
ANISOU  918  C   LEU A 282     3720   3537   2848   -215     15    357       C  
ATOM    919  O   LEU A 282     -55.889  -2.411  14.115  1.00 29.29           O  
ANISOU  919  O   LEU A 282     4108   3905   3118   -213    -28    347       O  
ATOM    920  CB  LEU A 282     -57.604  -1.532  11.810  1.00 27.39           C  
ANISOU  920  CB  LEU A 282     3718   3629   3059   -242    -85    375       C  
ATOM    921  CG  LEU A 282     -58.103  -1.992  10.453  1.00 38.70           C  
ANISOU  921  CG  LEU A 282     5094   5055   4553   -257   -139    394       C  
ATOM    922  CD1 LEU A 282     -57.900  -0.841   9.408  1.00 33.12           C  
ANISOU  922  CD1 LEU A 282     4358   4355   3873   -251   -191    387       C  
ATOM    923  CD2 LEU A 282     -57.349  -3.230  10.070  1.00 34.11           C  
ANISOU  923  CD2 LEU A 282     4540   4495   3924   -267   -183    403       C  
ATOM    924  N   MET A 283     -57.477  -1.264  15.230  1.00 27.17           N  
ANISOU  924  N   MET A 283     3801   3598   2922   -196     78    345       N  
ATOM    925  CA  MET A 283     -56.547  -0.815  16.289  1.00 26.39           C  
ANISOU  925  CA  MET A 283     3766   3520   2740   -167     96    313       C  
ATOM    926  C   MET A 283     -57.208  -1.195  17.580  1.00 26.71           C  
ANISOU  926  C   MET A 283     3834   3548   2767   -148    182    321       C  
ATOM    927  O   MET A 283     -57.943  -0.419  18.140  1.00 34.72           O  
ANISOU  927  O   MET A 283     4828   4548   3818   -136    232    315       O  
ATOM    928  CB  MET A 283     -56.373   0.724  16.206  1.00 22.81           C  
ANISOU  928  CB  MET A 283     3290   3069   2309   -156     84    284       C  
ATOM    929  CG  MET A 283     -55.398   1.149  15.101  1.00 25.68           C  
ANISOU  929  CG  MET A 283     3645   3448   2665   -166      4    271       C  
ATOM    930  SD  MET A 283     -55.275   2.977  14.885  1.00 30.08           S  
ANISOU  930  SD  MET A 283     4167   3998   3264   -155     -7    242       S  
ATOM    931  CE  MET A 283     -56.665   3.100  13.884  1.00 30.55           C  
ANISOU  931  CE  MET A 283     4151   4031   3425   -178     -9    277       C  
ATOM    932  N   PRO A 284     -56.986  -2.434  18.025  1.00 30.21           N  
ANISOU  932  N   PRO A 284     4324   3995   3161   -145    201    338       N  
ATOM    933  CA  PRO A 284     -57.729  -2.999  19.155  1.00 34.16           C  
ANISOU  933  CA  PRO A 284     4848   4477   3654   -128    289    356       C  
ATOM    934  C   PRO A 284     -57.522  -2.237  20.458  1.00 36.67           C  
ANISOU  934  C   PRO A 284     5211   4805   3917    -85    341    328       C  
ATOM    935  O   PRO A 284     -58.391  -2.374  21.331  1.00 38.36           O  
ANISOU  935  O   PRO A 284     5430   4999   4145    -71    422    344       O  
ATOM    936  CB  PRO A 284     -57.180  -4.439  19.253  1.00 33.90           C  
ANISOU  936  CB  PRO A 284     4866   4452   3563   -130    282    375       C  
ATOM    937  CG  PRO A 284     -56.648  -4.734  17.865  1.00 39.63           C  
ANISOU  937  CG  PRO A 284     5560   5189   4307   -162    191    377       C  
ATOM    938  CD  PRO A 284     -56.043  -3.394  17.443  1.00 31.33           C  
ANISOU  938  CD  PRO A 284     4495   4157   3253   -157    140    342       C  
ATOM    939  N   TYR A 285     -56.450  -1.434  20.569  1.00 27.12           N  
ANISOU  939  N   TYR A 285     4029   3622   2652    -64    296    286       N  
ATOM    940  CA  TYR A 285     -56.158  -0.628  21.763  1.00 31.82           C  
ANISOU  940  CA  TYR A 285     4663   4229   3196    -17    334    250       C  
ATOM    941  C   TYR A 285     -56.866   0.709  21.748  1.00 35.20           C  
ANISOU  941  C   TYR A 285     5036   4646   3694    -17    351    236       C  
ATOM    942  O   TYR A 285     -56.823   1.475  22.724  1.00 35.71           O  
ANISOU  942  O   TYR A 285     5120   4717   3732     21    386    206       O  
ATOM    943  CB  TYR A 285     -54.659  -0.369  21.815  1.00 33.19           C  
ANISOU  943  CB  TYR A 285     4886   4436   3291      5    273    204       C  
ATOM    944  CG  TYR A 285     -54.122   0.227  20.519  1.00 30.16           C  
ANISOU  944  CG  TYR A 285     4456   4057   2948    -27    192    192       C  
ATOM    945  CD1 TYR A 285     -54.180   1.607  20.283  1.00 31.66           C  
ANISOU  945  CD1 TYR A 285     4602   4242   3186    -25    178    165       C  
ATOM    946  CD2 TYR A 285     -53.567  -0.589  19.544  1.00 31.46           C  
ANISOU  946  CD2 TYR A 285     4621   4228   3102    -56    133    207       C  
ATOM    947  CE1 TYR A 285     -53.703   2.138  19.092  1.00 27.39           C  
ANISOU  947  CE1 TYR A 285     4023   3703   2682    -52    111    159       C  
ATOM    948  CE2 TYR A 285     -53.104  -0.080  18.362  1.00 27.12           C  
ANISOU  948  CE2 TYR A 285     4034   3684   2588    -82     64    200       C  
ATOM    949  CZ  TYR A 285     -53.157   1.288  18.156  1.00 28.56           C  
ANISOU  949  CZ  TYR A 285     4177   3860   2816    -79     56    177       C  
ATOM    950  OH  TYR A 285     -52.670   1.768  16.977  1.00 27.73           O  
ANISOU  950  OH  TYR A 285     4038   3756   2742   -101     -7    173       O  
ATOM    951  N   ALA A 286     -57.501   1.036  20.627  1.00 33.59           N  
ANISOU  951  N   ALA A 286     4761   4424   3580    -57    322    254       N  
ATOM    952  CA  ALA A 286     -58.142   2.343  20.526  1.00 29.69           C  
ANISOU  952  CA  ALA A 286     4212   3916   3153    -58    332    239       C  
ATOM    953  C   ALA A 286     -59.616   2.369  20.948  1.00 33.78           C  
ANISOU  953  C   ALA A 286     4692   4406   3738    -63    406    263       C  
ATOM    954  O   ALA A 286     -60.415   1.599  20.420  1.00 36.16           O  
ANISOU  954  O   ALA A 286     4961   4685   4094    -92    418    298       O  
ATOM    955  CB  ALA A 286     -58.027   2.880  19.074  1.00 33.11           C  
ANISOU  955  CB  ALA A 286     4589   4346   3647    -91    259    241       C  
ATOM    956  N   ASP A 287     -59.978   3.283  21.859  1.00 31.53           N  
ANISOU  956  N   ASP A 287     4405   4119   3455    -35    453    240       N  
ATOM    957  CA  ASP A 287     -61.385   3.445  22.247  1.00 34.89           C  
ANISOU  957  CA  ASP A 287     4790   4517   3950    -40    523    258       C  
ATOM    958  C   ASP A 287     -62.205   3.998  21.112  1.00 41.82           C  
ANISOU  958  C   ASP A 287     5587   5372   4933    -77    492    266       C  
ATOM    959  O   ASP A 287     -63.358   3.611  20.916  1.00 40.15           O  
ANISOU  959  O   ASP A 287     5333   5131   4792    -98    529    291       O  
ATOM    960  CB  ASP A 287     -61.536   4.372  23.459  1.00 45.64           C  
ANISOU  960  CB  ASP A 287     6167   5886   5288      1    574    227       C  
ATOM    961  CG  ASP A 287     -60.876   3.808  24.711  1.00 62.07           C  
ANISOU  961  CG  ASP A 287     8331   7989   7264     49    615    218       C  
ATOM    962  OD1 ASP A 287     -60.773   2.564  24.810  1.00 67.93           O  
ANISOU  962  OD1 ASP A 287     9113   8729   7969     45    634    248       O  
ATOM    963  OD2 ASP A 287     -60.455   4.603  25.590  1.00 65.80           O  
ANISOU  963  OD2 ASP A 287     8830   8481   7690     93    626    179       O  
ATOM    964  N   SER A 288     -61.625   4.936  20.370  1.00 39.27           N  
ANISOU  964  N   SER A 288     5241   5059   4622    -82    426    244       N  
ATOM    965  CA  SER A 288     -62.347   5.534  19.255  1.00 41.40           C  
ANISOU  965  CA  SER A 288     5438   5307   4985   -110    393    251       C  
ATOM    966  C   SER A 288     -61.331   6.085  18.288  1.00 31.21           C  
ANISOU  966  C   SER A 288     4145   4032   3682   -116    312    237       C  
ATOM    967  O   SER A 288     -60.158   6.248  18.641  1.00 30.87           O  
ANISOU  967  O   SER A 288     4149   4014   3568    -97    290    214       O  
ATOM    968  CB  SER A 288     -63.251   6.655  19.735  1.00 39.59           C  
ANISOU  968  CB  SER A 288     5169   5063   4812   -101    434    234       C  
ATOM    969  OG  SER A 288     -62.474   7.662  20.339  1.00 45.74           O  
ANISOU  969  OG  SER A 288     5971   5862   5547    -72    426    197       O  
ATOM    970  N   VAL A 289     -61.755   6.322  17.054  1.00 30.81           N  
ANISOU  970  N   VAL A 289     4041   3967   3700   -140    268    251       N  
ATOM    971  CA  VAL A 289     -60.830   6.947  16.101  1.00 30.75           C  
ANISOU  971  CA  VAL A 289     4029   3971   3684   -143    196    241       C  
ATOM    972  C   VAL A 289     -61.578   8.146  15.554  1.00 30.63           C  
ANISOU  972  C   VAL A 289     3954   3935   3749   -146    188    236       C  
ATOM    973  O   VAL A 289     -62.605   8.037  14.892  1.00 32.04           O  
ANISOU  973  O   VAL A 289     4084   4092   3998   -162    186    254       O  
ATOM    974  CB  VAL A 289     -60.388   5.971  14.999  1.00 36.41           C  
ANISOU  974  CB  VAL A 289     4751   4696   4390   -163    140    266       C  
ATOM    975  CG1 VAL A 289     -59.627   6.735  13.883  1.00 31.18           C  
ANISOU  975  CG1 VAL A 289     4074   4039   3734   -166     71    261       C  
ATOM    976  CG2 VAL A 289     -59.531   4.817  15.590  1.00 32.23           C  
ANISOU  976  CG2 VAL A 289     4284   4187   3773   -158    145    268       C  
ATOM    977  N   ASN A 290     -61.068   9.321  15.862  1.00 27.94           N  
ANISOU  977  N   ASN A 290     3616   3599   3401   -130    184    207       N  
ATOM    978  CA  ASN A 290     -61.724  10.547  15.449  1.00 31.27           C  
ANISOU  978  CA  ASN A 290     3985   4001   3896   -130    179    199       C  
ATOM    979  C   ASN A 290     -61.198  10.925  14.056  1.00 27.68           C  
ANISOU  979  C   ASN A 290     3513   3544   3462   -139    111    211       C  
ATOM    980  O   ASN A 290     -60.000  10.804  13.779  1.00 37.06           O  
ANISOU  980  O   ASN A 290     4734   4749   4598   -136     75    207       O  
ATOM    981  CB  ASN A 290     -61.301  11.578  16.499  1.00 44.45           C  
ANISOU  981  CB  ASN A 290     5668   5677   5544   -105    206    161       C  
ATOM    982  CG  ASN A 290     -61.757  13.002  16.184  1.00 57.72           C  
ANISOU  982  CG  ASN A 290     7299   7339   7293   -101    200    147       C  
ATOM    983  OD1 ASN A 290     -62.597  13.244  15.317  1.00 62.38           O  
ANISOU  983  OD1 ASN A 290     7843   7908   7950   -115    184    165       O  
ATOM    984  ND2 ASN A 290     -61.200  13.954  16.929  1.00 63.91           N  
ANISOU  984  ND2 ASN A 290     8092   8129   8062    -79    211    110       N  
ATOM    985  N   ILE A 291     -62.091  11.303  13.151  1.00 26.68           N  
ANISOU  985  N   ILE A 291     3335   3396   3407   -147     94    227       N  
ATOM    986  CA  ILE A 291     -61.655  11.698  11.838  1.00 24.62           C  
ANISOU  986  CA  ILE A 291     3060   3132   3163   -149     34    240       C  
ATOM    987  C   ILE A 291     -61.749  13.235  11.808  1.00 31.16           C  
ANISOU  987  C   ILE A 291     3861   3944   4035   -137     37    223       C  
ATOM    988  O   ILE A 291     -62.817  13.784  12.055  1.00 29.94           O  
ANISOU  988  O   ILE A 291     3668   3771   3938   -134     64    216       O  
ATOM    989  CB  ILE A 291     -62.590  11.092  10.798  1.00 27.82           C  
ANISOU  989  CB  ILE A 291     3428   3524   3619   -159      8    267       C  
ATOM    990  CG1 ILE A 291     -62.363   9.558  10.754  1.00 34.87           C  
ANISOU  990  CG1 ILE A 291     4346   4432   4469   -171      0    284       C  
ATOM    991  CG2 ILE A 291     -62.395  11.751   9.462  1.00 30.85           C  
ANISOU  991  CG2 ILE A 291     3790   3900   4031   -152    -47    281       C  
ATOM    992  CD1 ILE A 291     -63.087   8.860   9.578  1.00 34.00           C  
ANISOU  992  CD1 ILE A 291     4200   4313   4407   -178    -39    307       C  
ATOM    993  N   THR A 292     -60.656  13.915  11.491  1.00 27.78           N  
ANISOU  993  N   THR A 292     3449   3520   3585   -129      9    214       N  
ATOM    994  CA  THR A 292     -60.675  15.384  11.455  1.00 27.75           C  
ANISOU  994  CA  THR A 292     3418   3498   3626   -117     13    197       C  
ATOM    995  C   THR A 292     -60.456  15.847  10.040  1.00 28.52           C  
ANISOU  995  C   THR A 292     3500   3583   3753   -115    -34    222       C  
ATOM    996  O   THR A 292     -59.499  15.426   9.407  1.00 28.43           O  
ANISOU  996  O   THR A 292     3516   3584   3703   -117    -68    235       O  
ATOM    997  CB  THR A 292     -59.584  15.946  12.348  1.00 34.00           C  
ANISOU  997  CB  THR A 292     4239   4301   4380   -105     28    161       C  
ATOM    998  OG1 THR A 292     -59.963  15.679  13.692  1.00 38.30           O  
ANISOU  998  OG1 THR A 292     4795   4855   4903    -98     76    137       O  
ATOM    999  CG2 THR A 292     -59.477  17.465  12.182  1.00 40.02           C  
ANISOU  999  CG2 THR A 292     4971   5041   5195    -93     27    144       C  
ATOM   1000  N   LEU A 293     -61.282  16.774   9.545  1.00 25.20           N  
ANISOU 1000  N   LEU A 293     3038   3138   3400   -108    -36    228       N  
ATOM   1001  CA  LEU A 293     -61.151  17.196   8.152  1.00 25.90           C  
ANISOU 1001  CA  LEU A 293     3114   3213   3514    -99    -79    256       C  
ATOM   1002  C   LEU A 293     -60.193  18.366   8.141  1.00 31.54           C  
ANISOU 1002  C   LEU A 293     3835   3917   4233    -90    -78    243       C  
ATOM   1003  O   LEU A 293     -60.529  19.425   8.656  1.00 29.98           O  
ANISOU 1003  O   LEU A 293     3612   3701   4076    -83    -52    222       O  
ATOM   1004  CB  LEU A 293     -62.495  17.637   7.550  1.00 24.69           C  
ANISOU 1004  CB  LEU A 293     2915   3037   3430    -91    -85    267       C  
ATOM   1005  CG  LEU A 293     -63.494  16.449   7.421  1.00 36.32           C  
ANISOU 1005  CG  LEU A 293     4373   4515   4911    -99    -89    276       C  
ATOM   1006  CD1 LEU A 293     -64.797  16.852   6.724  1.00 39.07           C  
ANISOU 1006  CD1 LEU A 293     4675   4839   5331    -87   -102    281       C  
ATOM   1007  CD2 LEU A 293     -62.890  15.280   6.743  1.00 27.18           C  
ANISOU 1007  CD2 LEU A 293     3243   3379   3706   -104   -126    299       C  
ATOM   1008  N   MET A 294     -59.013  18.182   7.548  1.00 26.83           N  
ANISOU 1008  N   MET A 294     3268   3328   3598    -89   -105    255       N  
ATOM   1009  CA  MET A 294     -57.995  19.238   7.542  1.00 23.06           C  
ANISOU 1009  CA  MET A 294     2796   2836   3128    -82   -100    240       C  
ATOM   1010  C   MET A 294     -58.026  20.050   6.255  1.00 21.75           C  
ANISOU 1010  C   MET A 294     2614   2646   3005    -68   -122    273       C  
ATOM   1011  O   MET A 294     -58.380  19.557   5.176  1.00 23.44           O  
ANISOU 1011  O   MET A 294     2828   2862   3217    -62   -155    309       O  
ATOM   1012  CB  MET A 294     -56.588  18.651   7.693  1.00 23.92           C  
ANISOU 1012  CB  MET A 294     2947   2966   3175    -88   -112    229       C  
ATOM   1013  CG  MET A 294     -56.423  17.798   8.973  1.00 24.31           C  
ANISOU 1013  CG  MET A 294     3023   3043   3172    -96    -91    196       C  
ATOM   1014  SD  MET A 294     -56.576  18.682  10.542  1.00 33.50           S  
ANISOU 1014  SD  MET A 294     4173   4201   4354    -85    -43    142       S  
ATOM   1015  CE  MET A 294     -55.038  19.579  10.575  1.00 30.30           C  
ANISOU 1015  CE  MET A 294     3779   3784   3949    -75    -49    109       C  
ATOM   1016  N   ASP A 295     -57.592  21.299   6.370  1.00 20.75           N  
ANISOU 1016  N   ASP A 295     2474   2493   2916    -59   -105    258       N  
ATOM   1017  CA  ASP A 295     -57.686  22.216   5.234  1.00 20.65           C  
ANISOU 1017  CA  ASP A 295     2445   2451   2949    -41   -117    290       C  
ATOM   1018  C   ASP A 295     -56.400  22.109   4.418  1.00 18.32           C  
ANISOU 1018  C   ASP A 295     2181   2156   2625    -39   -135    310       C  
ATOM   1019  O   ASP A 295     -55.312  22.286   4.974  1.00 21.70           O  
ANISOU 1019  O   ASP A 295     2623   2584   3037    -47   -121    281       O  
ATOM   1020  CB  ASP A 295     -57.805  23.661   5.820  1.00 23.55           C  
ANISOU 1020  CB  ASP A 295     2782   2788   3379    -34    -84    262       C  
ATOM   1021  CG  ASP A 295     -58.163  24.713   4.757  1.00 29.84           C  
ANISOU 1021  CG  ASP A 295     3558   3548   4232    -13    -90    295       C  
ATOM   1022  OD1 ASP A 295     -57.925  24.495   3.543  1.00 27.14           O  
ANISOU 1022  OD1 ASP A 295     3233   3203   3877     -1   -116    338       O  
ATOM   1023  OD2 ASP A 295     -58.636  25.809   5.145  1.00 44.69           O  
ANISOU 1023  OD2 ASP A 295     5407   5403   6169     -6    -67    278       O  
ATOM   1024  N   ASP A 296     -56.531  21.829   3.119  1.00 20.95           N  
ANISOU 1024  N   ASP A 296     2522   2488   2952    -26   -166    356       N  
ATOM   1025  CA  ASP A 296     -55.391  21.689   2.205  1.00 20.84           C  
ANISOU 1025  CA  ASP A 296     2537   2474   2909    -21   -184    382       C  
ATOM   1026  C   ASP A 296     -54.563  22.980   2.197  1.00 20.16           C  
ANISOU 1026  C   ASP A 296     2444   2352   2865    -14   -155    373       C  
ATOM   1027  O   ASP A 296     -53.351  22.962   1.905  1.00 20.00           O  
ANISOU 1027  O   ASP A 296     2446   2329   2825    -18   -154    375       O  
ATOM   1028  CB  ASP A 296     -55.852  21.391   0.777  1.00 21.44           C  
ANISOU 1028  CB  ASP A 296     2617   2551   2979      3   -220    433       C  
ATOM   1029  CG  ASP A 296     -56.462  19.955   0.602  1.00 25.98           C  
ANISOU 1029  CG  ASP A 296     3198   3161   3511     -3   -256    442       C  
ATOM   1030  OD1 ASP A 296     -56.424  19.130   1.566  1.00 24.34           O  
ANISOU 1030  OD1 ASP A 296     2997   2979   3273    -28   -250    412       O  
ATOM   1031  OD2 ASP A 296     -56.974  19.684  -0.524  1.00 21.00           O  
ANISOU 1031  OD2 ASP A 296     2566   2534   2880     21   -290    477       O  
ATOM   1032  N   VAL A 297     -55.245  24.099   2.422  1.00 18.97           N  
ANISOU 1032  N   VAL A 297     2260   2170   2776     -3   -131    367       N  
ATOM   1033  CA  VAL A 297     -54.577  25.406   2.398  1.00 21.76           C  
ANISOU 1033  CA  VAL A 297     2601   2483   3182      4   -100    359       C  
ATOM   1034  C   VAL A 297     -53.560  25.492   3.528  1.00 20.04           C  
ANISOU 1034  C   VAL A 297     2386   2269   2959    -14    -79    304       C  
ATOM   1035  O   VAL A 297     -52.456  26.041   3.354  1.00 22.40           O  
ANISOU 1035  O   VAL A 297     2689   2545   3276    -13    -63    296       O  
ATOM   1036  CB  VAL A 297     -55.625  26.522   2.540  1.00 21.48           C  
ANISOU 1036  CB  VAL A 297     2528   2418   3215     19    -82    358       C  
ATOM   1037  CG1 VAL A 297     -54.944  27.935   2.792  1.00 25.34           C  
ANISOU 1037  CG1 VAL A 297     2995   2862   3769     24    -45    338       C  
ATOM   1038  CG2 VAL A 297     -56.472  26.539   1.324  1.00 27.53           C  
ANISOU 1038  CG2 VAL A 297     3295   3176   3989     44   -106    410       C  
ATOM   1039  N   THR A 298     -53.891  24.909   4.672  1.00 21.51           N  
ANISOU 1039  N   THR A 298     2570   2483   3118    -27    -77    264       N  
ATOM   1040  CA  THR A 298     -52.952  24.841   5.765  1.00 22.39           C  
ANISOU 1040  CA  THR A 298     2690   2606   3213    -37    -62    207       C  
ATOM   1041  C   THR A 298     -51.767  23.936   5.435  1.00 21.27           C  
ANISOU 1041  C   THR A 298     2588   2484   3012    -47    -82    209       C  
ATOM   1042  O   THR A 298     -50.602  24.267   5.738  1.00 19.72           O  
ANISOU 1042  O   THR A 298     2396   2276   2822    -49    -71    174       O  
ATOM   1043  CB  THR A 298     -53.635  24.312   7.069  1.00 23.85           C  
ANISOU 1043  CB  THR A 298     2871   2820   3372    -44    -54    168       C  
ATOM   1044  OG1 THR A 298     -54.825  25.076   7.291  1.00 27.53           O  
ANISOU 1044  OG1 THR A 298     3299   3268   3891    -36    -38    170       O  
ATOM   1045  CG2 THR A 298     -52.676  24.416   8.270  1.00 21.89           C  
ANISOU 1045  CG2 THR A 298     2630   2580   3110    -44    -38    103       C  
ATOM   1046  N   ALA A 299     -52.052  22.744   4.911  1.00 20.22           N  
ANISOU 1046  N   ALA A 299     2480   2382   2821    -54   -113    242       N  
ATOM   1047  CA  ALA A 299     -50.946  21.843   4.586  1.00 21.58           C  
ANISOU 1047  CA  ALA A 299     2689   2575   2935    -64   -135    243       C  
ATOM   1048  C   ALA A 299     -49.975  22.452   3.588  1.00 20.05           C  
ANISOU 1048  C   ALA A 299     2500   2353   2765    -57   -133    265       C  
ATOM   1049  O   ALA A 299     -48.752  22.369   3.758  1.00 20.47           O  
ANISOU 1049  O   ALA A 299     2569   2405   2803    -65   -131    236       O  
ATOM   1050  CB  ALA A 299     -51.536  20.470   3.998  1.00 17.15           C  
ANISOU 1050  CB  ALA A 299     2149   2050   2316    -70   -173    282       C  
ATOM   1051  N   ALA A 300     -50.507  23.066   2.521  1.00 21.20           N  
ANISOU 1051  N   ALA A 300     2633   2474   2949    -41   -132    316       N  
ATOM   1052  CA  ALA A 300     -49.613  23.624   1.534  1.00 20.98           C  
ANISOU 1052  CA  ALA A 300     2613   2417   2942    -31   -124    343       C  
ATOM   1053  C   ALA A 300     -48.983  24.876   2.098  1.00 20.12           C  
ANISOU 1053  C   ALA A 300     2479   2266   2901    -31    -83    304       C  
ATOM   1054  O   ALA A 300     -47.818  25.156   1.799  1.00 22.15           O  
ANISOU 1054  O   ALA A 300     2744   2502   3169    -33    -70    297       O  
ATOM   1055  CB  ALA A 300     -50.352  23.983   0.227  1.00 23.36           C  
ANISOU 1055  CB  ALA A 300     2911   2701   3263     -6   -132    410       C  
ATOM   1056  N   GLY A 301     -49.725  25.636   2.908  1.00 21.13           N  
ANISOU 1056  N   GLY A 301     2574   2379   3076    -27    -62    277       N  
ATOM   1057  CA  GLY A 301     -49.176  26.880   3.476  1.00 19.78           C  
ANISOU 1057  CA  GLY A 301     2372   2166   2977    -24    -24    236       C  
ATOM   1058  C   GLY A 301     -48.014  26.643   4.442  1.00 20.23           C  
ANISOU 1058  C   GLY A 301     2435   2232   3019    -36    -19    167       C  
ATOM   1059  O   GLY A 301     -47.040  27.425   4.512  1.00 22.46           O  
ANISOU 1059  O   GLY A 301     2703   2479   3353    -34      5    137       O  
ATOM   1060  N   GLN A 302     -48.072  25.537   5.193  1.00 20.27           N  
ANISOU 1060  N   GLN A 302     2462   2284   2954    -46    -43    139       N  
ATOM   1061  CA  GLN A 302     -46.919  25.201   6.027  1.00 18.38           C  
ANISOU 1061  CA  GLN A 302     2237   2057   2691    -52    -45     74       C  
ATOM   1062  C   GLN A 302     -45.704  24.796   5.208  1.00 22.44           C  
ANISOU 1062  C   GLN A 302     2777   2566   3182    -60    -56     85       C  
ATOM   1063  O   GLN A 302     -44.591  25.053   5.649  1.00 24.74           O  
ANISOU 1063  O   GLN A 302     3065   2843   3491    -61    -46     31       O  
ATOM   1064  CB  GLN A 302     -47.255  24.175   7.126  1.00 20.56           C  
ANISOU 1064  CB  GLN A 302     2533   2381   2898    -57    -62     38       C  
ATOM   1065  CG  GLN A 302     -48.265  24.749   8.115  1.00 19.39           C  
ANISOU 1065  CG  GLN A 302     2355   2232   2781    -46    -43     12       C  
ATOM   1066  CD  GLN A 302     -48.586  23.869   9.267  1.00 23.75           C  
ANISOU 1066  CD  GLN A 302     2926   2826   3270    -45    -51    -23       C  
ATOM   1067  OE1 GLN A 302     -47.943  22.856   9.466  1.00 24.34           O  
ANISOU 1067  OE1 GLN A 302     3039   2931   3279    -51    -70    -38       O  
ATOM   1068  NE2 GLN A 302     -49.568  24.266  10.066  1.00 24.06           N  
ANISOU 1068  NE2 GLN A 302     2942   2869   3331    -36    -33    -39       N  
ATOM   1069  N   ALA A 303     -45.886  24.161   4.050  1.00 17.63           N  
ANISOU 1069  N   ALA A 303     2192   1969   2536    -64    -77    151       N  
ATOM   1070  CA  ALA A 303     -44.764  23.908   3.145  1.00 21.69           C  
ANISOU 1070  CA  ALA A 303     2729   2476   3036    -69    -83    168       C  
ATOM   1071  C   ALA A 303     -44.133  25.189   2.599  1.00 25.85           C  
ANISOU 1071  C   ALA A 303     3231   2943   3647    -60    -44    174       C  
ATOM   1072  O   ALA A 303     -42.913  25.374   2.659  1.00 27.05           O  
ANISOU 1072  O   ALA A 303     3384   3076   3819    -66    -31    137       O  
ATOM   1073  CB  ALA A 303     -45.210  22.991   1.974  1.00 18.69           C  
ANISOU 1073  CB  ALA A 303     2378   2124   2600    -69   -116    240       C  
ATOM   1074  N   GLU A 304     -44.982  26.050   2.043  1.00 20.98           N  
ANISOU 1074  N   GLU A 304     2592   2297   3081    -45    -24    221       N  
ATOM   1075  CA  GLU A 304     -44.592  27.378   1.568  1.00 26.77           C  
ANISOU 1075  CA  GLU A 304     3299   2970   3903    -34     20    233       C  
ATOM   1076  C   GLU A 304     -43.853  28.136   2.657  1.00 28.84           C  
ANISOU 1076  C   GLU A 304     3528   3202   4226    -38     48    152       C  
ATOM   1077  O   GLU A 304     -42.707  28.567   2.478  1.00 24.95           O  
ANISOU 1077  O   GLU A 304     3029   2675   3777    -41     72    128       O  
ATOM   1078  CB  GLU A 304     -45.838  28.171   1.080  1.00 23.70           C  
ANISOU 1078  CB  GLU A 304     2891   2558   3556    -15     34    285       C  
ATOM   1079  CG  GLU A 304     -45.651  29.741   1.231  1.00 37.50           C  
ANISOU 1079  CG  GLU A 304     4596   4242   5412     -4     84    269       C  
ATOM   1080  CD  GLU A 304     -46.863  30.600   0.795  1.00 41.82           C  
ANISOU 1080  CD  GLU A 304     5123   4764   6004     16     98    317       C  
ATOM   1081  OE1 GLU A 304     -47.970  30.042   0.558  1.00 39.10           O  
ANISOU 1081  OE1 GLU A 304     4790   4452   5612     23     67    351       O  
ATOM   1082  OE2 GLU A 304     -46.681  31.848   0.680  1.00 49.26           O  
ANISOU 1082  OE2 GLU A 304     6035   5650   7033     27    139    317       O  
ATOM   1083  N   ALA A 305     -44.441  28.230   3.834  1.00 23.98           N  
ANISOU 1083  N   ALA A 305     2893   2605   3615    -38     43    102       N  
ATOM   1084  CA  ALA A 305     -43.766  28.968   4.887  1.00 29.46           C  
ANISOU 1084  CA  ALA A 305     3552   3273   4368    -35     65     20       C  
ATOM   1085  C   ALA A 305     -42.451  28.374   5.323  1.00 30.85           C  
ANISOU 1085  C   ALA A 305     3745   3460   4514    -44     53    -41       C  
ATOM   1086  O   ALA A 305     -41.500  29.104   5.619  1.00 30.10           O  
ANISOU 1086  O   ALA A 305     3623   3326   4487    -40     77    -96       O  
ATOM   1087  CB  ALA A 305     -44.670  29.167   6.099  1.00 33.99           C  
ANISOU 1087  CB  ALA A 305     4103   3866   4945    -28     61    -22       C  
ATOM   1088  N   GLY A 306     -42.354  27.055   5.378  1.00 25.03           N  
ANISOU 1088  N   GLY A 306     3052   2777   3683    -54     15    -38       N  
ATOM   1089  CA  GLY A 306     -41.119  26.490   5.848  1.00 28.13           C  
ANISOU 1089  CA  GLY A 306     3461   3181   4046    -60      1   -102       C  
ATOM   1090  C   GLY A 306     -40.007  26.712   4.860  1.00 28.58           C  
ANISOU 1090  C   GLY A 306     3522   3202   4136    -68     17    -87       C  
ATOM   1091  O   GLY A 306     -38.835  26.885   5.239  1.00 33.29           O  
ANISOU 1091  O   GLY A 306     4108   3778   4761    -69     24   -154       O  
ATOM   1092  N   LEU A 307     -40.348  26.701   3.586  1.00 22.18           N  
ANISOU 1092  N   LEU A 307     2724   2381   3320    -70     22     -1       N  
ATOM   1093  CA  LEU A 307     -39.299  26.829   2.595  1.00 24.69           C  
ANISOU 1093  CA  LEU A 307     3051   2668   3662    -75     40     21       C  
ATOM   1094  C   LEU A 307     -38.858  28.290   2.589  1.00 33.36           C  
ANISOU 1094  C   LEU A 307     4102   3694   4879    -67     94     -1       C  
ATOM   1095  O   LEU A 307     -37.674  28.600   2.464  1.00 32.82           O  
ANISOU 1095  O   LEU A 307     4022   3589   4857    -72    117    -38       O  
ATOM   1096  CB  LEU A 307     -39.812  26.476   1.234  1.00 23.28           C  
ANISOU 1096  CB  LEU A 307     2901   2499   3447    -73     33    119       C  
ATOM   1097  CG  LEU A 307     -40.060  24.951   1.051  1.00 22.62           C  
ANISOU 1097  CG  LEU A 307     2863   2483   3251    -82    -22    142       C  
ATOM   1098  CD1 LEU A 307     -40.640  24.678  -0.334  1.00 29.10           C  
ANISOU 1098  CD1 LEU A 307     3706   3311   4040    -72    -32    237       C  
ATOM   1099  CD2 LEU A 307     -38.765  24.159   1.290  1.00 28.90           C  
ANISOU 1099  CD2 LEU A 307     3681   3296   4005    -98    -43     89       C  
ATOM   1100  N   LYS A 308     -39.828  29.191   2.683  1.00 31.55           N  
ANISOU 1100  N   LYS A 308     3842   3442   4703    -54    116     23       N  
ATOM   1101  CA  LYS A 308     -39.462  30.622   2.672  1.00 29.64           C  
ANISOU 1101  CA  LYS A 308     3552   3128   4580    -45    170      4       C  
ATOM   1102  C   LYS A 308     -38.594  30.947   3.851  1.00 34.73           C  
ANISOU 1102  C   LYS A 308     4163   3758   5274    -46    175   -104       C  
ATOM   1103  O   LYS A 308     -37.681  31.795   3.751  1.00 36.39           O  
ANISOU 1103  O   LYS A 308     4340   3909   5577    -45    215   -138       O  
ATOM   1104  CB  LYS A 308     -40.715  31.493   2.662  1.00 28.44           C  
ANISOU 1104  CB  LYS A 308     3374   2958   4472    -31    187     43       C  
ATOM   1105  CG  LYS A 308     -41.384  31.501   1.300  1.00 32.09           C  
ANISOU 1105  CG  LYS A 308     3863   3415   4916    -22    194    149       C  
ATOM   1106  CD  LYS A 308     -42.707  32.252   1.332  1.00 37.60           C  
ANISOU 1106  CD  LYS A 308     4537   4101   5647     -6    202    183       C  
ATOM   1107  CE  LYS A 308     -43.200  32.591  -0.087  1.00 40.29           C  
ANISOU 1107  CE  LYS A 308     4898   4418   5993     12    220    282       C  
ATOM   1108  NZ  LYS A 308     -44.558  33.204  -0.021  1.00 45.19           N  
ANISOU 1108  NZ  LYS A 308     5500   5034   6638     29    220    310       N  
ATOM   1109  N   GLN A 309     -38.848  30.289   4.971  1.00 35.33           N  
ANISOU 1109  N   GLN A 309     3476   4466   5484   -519    838    279       N  
ATOM   1110  CA  GLN A 309     -38.070  30.530   6.173  1.00 36.00           C  
ANISOU 1110  CA  GLN A 309     3483   4543   5652   -608    823    246       C  
ATOM   1111  C   GLN A 309     -36.591  30.231   5.938  1.00 46.08           C  
ANISOU 1111  C   GLN A 309     4764   5799   6947   -572    863    324       C  
ATOM   1112  O   GLN A 309     -35.722  30.840   6.584  1.00 43.21           O  
ANISOU 1112  O   GLN A 309     4378   5419   6620   -594    842    316       O  
ATOM   1113  CB  GLN A 309     -38.603  29.712   7.344  1.00 40.47           C  
ANISOU 1113  CB  GLN A 309     4063   5173   6142   -694    720    147       C  
ATOM   1114  CG  GLN A 309     -38.192  30.238   8.671  1.00 42.90           C  
ANISOU 1114  CG  GLN A 309     4360   5494   6448   -749    643     97       C  
ATOM   1115  CD  GLN A 309     -38.497  31.728   8.788  1.00 54.60           C  
ANISOU 1115  CD  GLN A 309     5818   6939   7990   -743    651     86       C  
ATOM   1116  OE1 GLN A 309     -39.624  32.157   8.541  1.00 49.26           O  
ANISOU 1116  OE1 GLN A 309     5140   6260   7316   -739    650     54       O  
ATOM   1117  NE2 GLN A 309     -37.471  32.530   9.120  1.00 53.13           N  
ANISOU 1117  NE2 GLN A 309     5612   6721   7852   -739    665    111       N  
ATOM   1118  N   GLN A 310     -36.289  29.336   4.995  1.00 40.81           N  
ANISOU 1118  N   GLN A 310     4146   5134   6227   -504    907    397       N  
ATOM   1119  CA  GLN A 310     -34.877  29.098   4.617  1.00 39.78           C  
ANISOU 1119  CA  GLN A 310     4005   4976   6133   -462    970    490       C  
ATOM   1120  C   GLN A 310     -34.378  29.775   3.334  1.00 43.57           C  
ANISOU 1120  C   GLN A 310     4499   5400   6654   -356   1060    595       C  
ATOM   1121  O   GLN A 310     -33.366  29.367   2.773  1.00 47.09           O  
ANISOU 1121  O   GLN A 310     4964   5830   7097   -300   1109    678       O  
ATOM   1122  CB  GLN A 310     -34.629  27.592   4.514  1.00 46.21           C  
ANISOU 1122  CB  GLN A 310     4892   5834   6832   -445    940    499       C  
ATOM   1123  CG  GLN A 310     -35.132  26.852   5.704  1.00 42.25           C  
ANISOU 1123  CG  GLN A 310     4383   5387   6281   -541    854    400       C  
ATOM   1124  CD  GLN A 310     -34.702  25.389   5.693  1.00 55.44           C  
ANISOU 1124  CD  GLN A 310     6119   7096   7852   -529    832    415       C  
ATOM   1125  OE1 GLN A 310     -34.162  24.886   4.694  1.00 49.33           O  
ANISOU 1125  OE1 GLN A 310     5405   6308   7030   -440    880    497       O  
ATOM   1126  NE2 GLN A 310     -34.934  24.696   6.812  1.00 63.58           N  
ANISOU 1126  NE2 GLN A 310     7137   8173   8848   -616    763    335       N  
ATOM   1127  N   ALA A 311     -35.070  30.803   2.862  1.00 41.41           N  
ANISOU 1127  N   ALA A 311     4220   5097   6417   -326   1083    594       N  
ATOM   1128  CA  ALA A 311     -34.715  31.449   1.594  1.00 49.96           C  
ANISOU 1128  CA  ALA A 311     5323   6128   7531   -220   1168    692       C  
ATOM   1129  C   ALA A 311     -34.561  30.450   0.462  1.00 51.25           C  
ANISOU 1129  C   ALA A 311     5584   6304   7583   -121   1186    759       C  
ATOM   1130  O   ALA A 311     -33.752  30.644  -0.444  1.00 59.17           O  
ANISOU 1130  O   ALA A 311     6600   7269   8615    -40   1260    856       O  
ATOM   1131  CB  ALA A 311     -33.455  32.299   1.722  1.00 47.03           C  
ANISOU 1131  CB  ALA A 311     4909   5704   7255   -215   1197    730       C  
ATOM   1132  N   LEU A 312     -35.338  29.378   0.507  1.00 44.26           N  
ANISOU 1132  N   LEU A 312     4771   5475   6572   -128   1119    708       N  
ATOM   1133  CA  LEU A 312     -35.288  28.415  -0.559  1.00 40.49           C  
ANISOU 1133  CA  LEU A 312     4393   5010   5981    -38   1132    764       C  
ATOM   1134  C   LEU A 312     -36.266  28.830  -1.599  1.00 45.96           C  
ANISOU 1134  C   LEU A 312     5141   5699   6624     38   1144    777       C  
ATOM   1135  O   LEU A 312     -37.470  28.861  -1.364  1.00 43.51           O  
ANISOU 1135  O   LEU A 312     4847   5422   6262      8   1086    702       O  
ATOM   1136  CB  LEU A 312     -35.593  27.020  -0.044  1.00 40.36           C  
ANISOU 1136  CB  LEU A 312     4431   5054   5850    -82   1059    706       C  
ATOM   1137  CG  LEU A 312     -34.537  26.660   0.997  1.00 42.57           C  
ANISOU 1137  CG  LEU A 312     4650   5338   6186   -155   1053    700       C  
ATOM   1138  CD1 LEU A 312     -34.985  25.458   1.793  1.00 38.47           C  
ANISOU 1138  CD1 LEU A 312     4167   4878   5570   -221    972    621       C  
ATOM   1139  CD2 LEU A 312     -33.267  26.339   0.262  1.00 43.94           C  
ANISOU 1139  CD2 LEU A 312     4842   5481   6371    -79   1126    809       C  
ATOM   1140  N   PRO A 313     -35.744  29.171  -2.768  1.00 47.09           N  
ANISOU 1140  N   PRO A 313     5311   5800   6782    141   1222    875       N  
ATOM   1141  CA  PRO A 313     -36.614  29.470  -3.887  1.00 52.02           C  
ANISOU 1141  CA  PRO A 313     5997   6422   7347    227   1237    898       C  
ATOM   1142  C   PRO A 313     -37.219  28.167  -4.296  1.00 45.64           C  
ANISOU 1142  C   PRO A 313     5290   5666   6383    251   1186    876       C  
ATOM   1143  O   PRO A 313     -36.602  27.114  -4.082  1.00 42.57           O  
ANISOU 1143  O   PRO A 313     4934   5296   5946    238   1172    885       O  
ATOM   1144  CB  PRO A 313     -35.637  29.960  -4.951  1.00 55.14           C  
ANISOU 1144  CB  PRO A 313     6396   6759   7797    326   1335   1017       C  
ATOM   1145  CG  PRO A 313     -34.369  29.311  -4.599  1.00 51.84           C  
ANISOU 1145  CG  PRO A 313     5961   6333   7402    308   1355   1056       C  
ATOM   1146  CD  PRO A 313     -34.322  29.269  -3.127  1.00 53.42           C  
ANISOU 1146  CD  PRO A 313     6089   6557   7653    184   1298    972       C  
ATOM   1147  N   TYR A 314     -38.410  28.220  -4.865  1.00 41.48           N  
ANISOU 1147  N   TYR A 314     4816   5167   5777    286   1158    848       N  
ATOM   1148  CA  TYR A 314     -39.024  26.998  -5.293  1.00 36.13           C  
ANISOU 1148  CA  TYR A 314     4238   4540   4949    308   1109    825       C  
ATOM   1149  C   TYR A 314     -40.061  27.324  -6.306  1.00 40.03           C  
ANISOU 1149  C   TYR A 314     4786   5048   5377    380   1111    834       C  
ATOM   1150  O   TYR A 314     -40.487  28.464  -6.395  1.00 46.02           O  
ANISOU 1150  O   TYR A 314     5496   5786   6205    391   1132    833       O  
ATOM   1151  CB  TYR A 314     -39.626  26.284  -4.089  1.00 38.83           C  
ANISOU 1151  CB  TYR A 314     4573   4937   5245    198   1017    717       C  
ATOM   1152  CG  TYR A 314     -40.676  27.102  -3.376  1.00 37.44           C  
ANISOU 1152  CG  TYR A 314     4338   4779   5108    132    971    633       C  
ATOM   1153  CD1 TYR A 314     -41.982  27.110  -3.836  1.00 34.85           C  
ANISOU 1153  CD1 TYR A 314     4057   4489   4694    153    932    594       C  
ATOM   1154  CD2 TYR A 314     -40.351  27.855  -2.242  1.00 38.60           C  
ANISOU 1154  CD2 TYR A 314     4384   4905   5376     47    967    595       C  
ATOM   1155  CE1 TYR A 314     -42.961  27.851  -3.202  1.00 38.82           C  
ANISOU 1155  CE1 TYR A 314     4508   5011   5231     97    891    520       C  
ATOM   1156  CE2 TYR A 314     -41.325  28.613  -1.593  1.00 38.94           C  
ANISOU 1156  CE2 TYR A 314     4377   4964   5455    -11    926    519       C  
ATOM   1157  CZ  TYR A 314     -42.623  28.605  -2.091  1.00 39.42           C  
ANISOU 1157  CZ  TYR A 314     4487   5063   5429     17    890    484       C  
ATOM   1158  OH  TYR A 314     -43.619  29.338  -1.473  1.00 43.99           O  
ANISOU 1158  OH  TYR A 314     5018   5659   6037    -36    850    411       O  
ATOM   1159  N   SER A 315     -40.449  26.350  -7.106  1.00 40.63           N  
ANISOU 1159  N   SER A 315     4963   5157   5319    433   1093    845       N  
ATOM   1160  CA  SER A 315     -41.640  26.490  -7.885  1.00 44.02           C  
ANISOU 1160  CA  SER A 315     5444   5617   5665    482   1073    830       C  
ATOM   1161  C   SER A 315     -42.589  25.432  -7.384  1.00 40.73           C  
ANISOU 1161  C   SER A 315     5079   5270   5128    416    980    738       C  
ATOM   1162  O   SER A 315     -42.212  24.282  -7.131  1.00 41.84           O  
ANISOU 1162  O   SER A 315     5267   5429   5202    390    954    725       O  
ATOM   1163  CB  SER A 315     -41.382  26.353  -9.395  1.00 43.84           C  
ANISOU 1163  CB  SER A 315     5500   5574   5584    608   1134    926       C  
ATOM   1164  OG  SER A 315     -41.357  25.007  -9.820  1.00 62.24           O  
ANISOU 1164  OG  SER A 315     7928   7936   7784    629   1110    930       O  
ATOM   1165  N   ARG A 316     -43.829  25.831  -7.218  1.00 37.74           N  
ANISOU 1165  N   ARG A 316     4689   4930   4722    389    931    672       N  
ATOM   1166  CA  ARG A 316     -44.863  24.895  -6.875  1.00 37.05           C  
ANISOU 1166  CA  ARG A 316     4653   4911   4513    335    844    586       C  
ATOM   1167  C   ARG A 316     -45.403  24.393  -8.179  1.00 42.28           C  
ANISOU 1167  C   ARG A 316     5416   5599   5051    423    850    623       C  
ATOM   1168  O   ARG A 316     -45.748  25.183  -9.086  1.00 43.51           O  
ANISOU 1168  O   ARG A 316     5575   5743   5215    502    889    669       O  
ATOM   1169  CB  ARG A 316     -45.931  25.599  -6.026  1.00 29.99           C  
ANISOU 1169  CB  ARG A 316     3693   4047   3654    260    789    499       C  
ATOM   1170  CG  ARG A 316     -47.285  24.950  -6.074  1.00 38.44           C  
ANISOU 1170  CG  ARG A 316     4820   5192   4594    235    711    425       C  
ATOM   1171  CD  ARG A 316     -48.294  25.655  -5.125  1.00 51.68           C  
ANISOU 1171  CD  ARG A 316     6425   6899   6314    156    656    338       C  
ATOM   1172  NE  ARG A 316     -49.585  24.941  -5.165  1.00 53.76           N  
ANISOU 1172  NE  ARG A 316     6743   7238   6445    129    578    266       N  
ATOM   1173  CZ  ARG A 316     -50.502  24.929  -4.190  1.00 42.11           C  
ANISOU 1173  CZ  ARG A 316     5232   5809   4958     40    506    171       C  
ATOM   1174  NH1 ARG A 316     -51.622  24.233  -4.346  1.00 47.34           N  
ANISOU 1174  NH1 ARG A 316     5951   6540   5495     22    440    115       N  
ATOM   1175  NH2 ARG A 316     -50.300  25.596  -3.059  1.00 37.12           N  
ANISOU 1175  NH2 ARG A 316     4511   5156   4439    -33    499    131       N  
ATOM   1176  N   ARG A 317     -45.464  23.078  -8.286  1.00 36.65           N  
ANISOU 1176  N   ARG A 317     4786   4920   4219    412    812    602       N  
ATOM   1177  CA  ARG A 317     -45.971  22.377  -9.470  1.00 45.47           C  
ANISOU 1177  CA  ARG A 317     6011   6067   5198    485    809    628       C  
ATOM   1178  C   ARG A 317     -47.041  21.381  -9.097  1.00 50.84           C  
ANISOU 1178  C   ARG A 317     6746   6819   5751    419    719    536       C  
ATOM   1179  O   ARG A 317     -46.763  20.413  -8.407  1.00 49.60           O  
ANISOU 1179  O   ARG A 317     6613   6676   5558    355    684    495       O  
ATOM   1180  CB  ARG A 317     -44.833  21.613 -10.157  1.00 44.89           C  
ANISOU 1180  CB  ARG A 317     6005   5958   5093    550    864    710       C  
ATOM   1181  CG  ARG A 317     -43.783  22.558 -10.623  1.00 45.36           C  
ANISOU 1181  CG  ARG A 317     6015   5948   5270    621    955    806       C  
ATOM   1182  CD  ARG A 317     -42.741  21.961 -11.534  1.00 45.09           C  
ANISOU 1182  CD  ARG A 317     6051   5878   5204    706   1020    900       C  
ATOM   1183  NE  ARG A 317     -41.740  22.996 -11.773  1.00 48.02           N  
ANISOU 1183  NE  ARG A 317     6355   6183   5709    758   1104    984       N  
ATOM   1184  CZ  ARG A 317     -40.474  22.758 -12.096  1.00 56.85           C  
ANISOU 1184  CZ  ARG A 317     7484   7254   6862    806   1168   1066       C  
ATOM   1185  NH1 ARG A 317     -40.040  21.502 -12.223  1.00 50.71           N  
ANISOU 1185  NH1 ARG A 317     6786   6488   5995    812   1160   1076       N  
ATOM   1186  NH2 ARG A 317     -39.642  23.775 -12.285  1.00 62.98           N  
ANISOU 1186  NH2 ARG A 317     8193   7972   7764    848   1243   1138       N  
ATOM   1187  N   ASN A 318     -48.272  21.611  -9.528  1.00 49.06           N  
ANISOU 1187  N   ASN A 318     6540   6642   5457    432    682    501       N  
ATOM   1188  CA  ASN A 318     -49.328  20.670  -9.184  1.00 50.31           C  
ANISOU 1188  CA  ASN A 318     6750   6872   5493    366    596    412       C  
ATOM   1189  C   ASN A 318     -49.080  19.390  -9.932  1.00 59.35           C  
ANISOU 1189  C   ASN A 318     8012   8027   6510    404    598    438       C  
ATOM   1190  O   ASN A 318     -48.506  19.423 -11.001  1.00 63.34           O  
ANISOU 1190  O   ASN A 318     8565   8501   7003    499    660    523       O  
ATOM   1191  CB  ASN A 318     -50.716  21.236  -9.496  1.00 45.95           C  
ANISOU 1191  CB  ASN A 318     6189   6374   4897    373    556    372       C  
ATOM   1192  CG  ASN A 318     -51.054  22.443  -8.643  1.00 56.37           C  
ANISOU 1192  CG  ASN A 318     7396   7685   6336    326    548    335       C  
ATOM   1193  OD1 ASN A 318     -50.218  22.946  -7.889  1.00 58.94           O  
ANISOU 1193  OD1 ASN A 318     7649   7962   6784    293    578    345       O  
ATOM   1194  ND2 ASN A 318     -52.279  22.928  -8.766  1.00 63.88           N  
ANISOU 1194  ND2 ASN A 318     8332   8687   7253    323    510    294       N  
ATOM   1195  N   HIS A 319     -49.442  18.262  -9.332  1.00 63.90           N  
ANISOU 1195  N   HIS A 319     8636   8646   6999    328    533    365       N  
ATOM   1196  CA  HIS A 319     -49.456  16.979 -10.026  1.00 66.07           C  
ANISOU 1196  CA  HIS A 319     9031   8941   7132    354    524    374       C  
ATOM   1197  C   HIS A 319     -50.804  16.324  -9.756  1.00 73.38           C  
ANISOU 1197  C   HIS A 319     9997   9944   7939    286    435    278       C  
ATOM   1198  O   HIS A 319     -51.676  16.949  -9.147  1.00 79.91           O  
ANISOU 1198  O   HIS A 319    10757  10806   8799    232    389    216       O  
ATOM   1199  CB  HIS A 319     -48.249  16.090  -9.669  1.00 63.94           C  
ANISOU 1199  CB  HIS A 319     8794   8632   6870    342    551    401       C  
ATOM   1200  CG  HIS A 319     -48.207  15.603  -8.248  1.00 66.19           C  
ANISOU 1200  CG  HIS A 319     9038   8931   7178    228    497    322       C  
ATOM   1201  ND1 HIS A 319     -47.545  16.280  -7.243  1.00 70.11           N  
ANISOU 1201  ND1 HIS A 319     9431   9395   7814    182    511    319       N  
ATOM   1202  CD2 HIS A 319     -48.671  14.464  -7.680  1.00 67.64           C  
ANISOU 1202  CD2 HIS A 319     9276   9157   7265    154    433    247       C  
ATOM   1203  CE1 HIS A 319     -47.638  15.602  -6.111  1.00 64.08           C  
ANISOU 1203  CE1 HIS A 319     8656   8655   7036     85    456    244       C  
ATOM   1204  NE2 HIS A 319     -48.316  14.494  -6.351  1.00 66.22           N  
ANISOU 1204  NE2 HIS A 319     9023   8971   7167     67    409    200       N  
ATOM   1205  N   LYS A 320     -51.015  15.108 -10.243  1.00 76.41           N  
ANISOU 1205  N   LYS A 320    10492  10356   8186    290    412    265       N  
ATOM   1206  CA  LYS A 320     -52.327  14.487 -10.091  1.00 78.59           C  
ANISOU 1206  CA  LYS A 320    10810  10707   8343    229    330    177       C  
ATOM   1207  C   LYS A 320     -52.592  14.219  -8.621  1.00 72.17           C  
ANISOU 1207  C   LYS A 320     9943   9917   7562    109    267     85       C  
ATOM   1208  O   LYS A 320     -51.937  13.368  -8.020  1.00 68.58           O  
ANISOU 1208  O   LYS A 320     9515   9444   7099     65    264     71       O  
ATOM   1209  CB  LYS A 320     -52.428  13.188 -10.892  1.00 87.16           C  
ANISOU 1209  CB  LYS A 320    11962  11784   9370    209    301    170       C  
ATOM   1210  CG  LYS A 320     -52.680  13.394 -12.376  1.00 94.97           C  
ANISOU 1210  CG  LYS A 320    12982  12760  10340    290    325    224       C  
ATOM   1211  CD  LYS A 320     -52.532  12.091 -13.153  1.00 98.47           C  
ANISOU 1211  CD  LYS A 320    13467  13185  10762    269    305    223       C  
ATOM   1212  CE  LYS A 320     -52.428  12.359 -14.647  1.00100.00           C  
ANISOU 1212  CE  LYS A 320    13699  13350  10947    368    346    291       C  
ATOM   1213  NZ  LYS A 320     -53.558  13.199 -15.140  1.00102.00           N  
ANISOU 1213  NZ  LYS A 320    13936  13647  11173    391    327    280       N  
ATOM   1214  N   GLY A 321     -53.538  14.964  -8.047  1.00 64.77           N  
ANISOU 1214  N   GLY A 321     8929   9018   6662     58    220     24       N  
ATOM   1215  CA  GLY A 321     -53.913  14.801  -6.648  1.00 61.15           C  
ANISOU 1215  CA  GLY A 321     8414   8585   6234    -56    157    -67       C  
ATOM   1216  C   GLY A 321     -52.830  15.192  -5.645  1.00 50.15           C  
ANISOU 1216  C   GLY A 321     6939   7136   4978    -90    187    -55       C  
ATOM   1217  O   GLY A 321     -52.826  14.724  -4.489  1.00 44.70           O  
ANISOU 1217  O   GLY A 321     6224   6459   4301   -183    142   -122       O  
ATOM   1218  N   GLY A 322     -51.913  16.057  -6.083  1.00 44.46           N  
ANISOU 1218  N   GLY A 322     6176   6356   4361    -17    263     31       N  
ATOM   1219  CA  GLY A 322     -50.835  16.506  -5.232  1.00 40.53           C  
ANISOU 1219  CA  GLY A 322     5598   5804   3997    -43    297     51       C  
ATOM   1220  C   GLY A 322     -50.197  17.781  -5.691  1.00 41.77           C  
ANISOU 1220  C   GLY A 322     5689   5906   4275     29    371    130       C  
ATOM   1221  O   GLY A 322     -50.541  18.359  -6.732  1.00 34.43           O  
ANISOU 1221  O   GLY A 322     4777   4977   3330    109    401    178       O  
ATOM   1222  N   VAL A 323     -49.264  18.252  -4.875  1.00 30.87           N  
ANISOU 1222  N   VAL A 323     4229   4480   3020     -2    399    144       N  
ATOM   1223  CA  VAL A 323     -48.511  19.428  -5.198  1.00 29.11           C  
ANISOU 1223  CA  VAL A 323     3940   4198   2922     58    473    220       C  
ATOM   1224  C   VAL A 323     -47.073  19.056  -4.887  1.00 31.54           C  
ANISOU 1224  C   VAL A 323     4239   4456   3289     60    519    270       C  
ATOM   1225  O   VAL A 323     -46.815  18.434  -3.856  1.00 28.00           O  
ANISOU 1225  O   VAL A 323     3776   4018   2845    -21    483    219       O  
ATOM   1226  CB  VAL A 323     -48.899  20.621  -4.290  1.00 32.65           C  
ANISOU 1226  CB  VAL A 323     4274   4645   3488      1    456    174       C  
ATOM   1227  CG1 VAL A 323     -48.214  21.882  -4.786  1.00 40.62           C  
ANISOU 1227  CG1 VAL A 323     5224   5592   4618     72    537    256       C  
ATOM   1228  CG2 VAL A 323     -50.389  20.840  -4.318  1.00 48.85           C  
ANISOU 1228  CG2 VAL A 323     6329   6756   5476    -22    396    107       C  
ATOM   1229  N   THR A 324     -46.145  19.440  -5.759  1.00 28.71           N  
ANISOU 1229  N   THR A 324     3889   4045   2977    151    600    370       N  
ATOM   1230  CA  THR A 324     -44.723  19.295  -5.482  1.00 34.31           C  
ANISOU 1230  CA  THR A 324     4573   4703   3760    158    653    427       C  
ATOM   1231  C   THR A 324     -44.133  20.659  -5.357  1.00 34.31           C  
ANISOU 1231  C   THR A 324     4473   4652   3912    177    709    473       C  
ATOM   1232  O   THR A 324     -44.304  21.505  -6.271  1.00 35.41           O  
ANISOU 1232  O   THR A 324     4608   4770   4076    254    754    527       O  
ATOM   1233  CB  THR A 324     -43.983  18.549  -6.595  1.00 36.60           C  
ANISOU 1233  CB  THR A 324     4958   4969   3980    250    707    513       C  
ATOM   1234  OG1 THR A 324     -44.485  17.211  -6.679  1.00 36.86           O  
ANISOU 1234  OG1 THR A 324     5090   5046   3868    229    657    469       O  
ATOM   1235  CG2 THR A 324     -42.490  18.468  -6.250  1.00 31.60           C  
ANISOU 1235  CG2 THR A 324     4289   4286   3433    257    763    575       C  
ATOM   1236  N   PHE A 325     -43.465  20.922  -4.231  1.00 25.09           N  
ANISOU 1236  N   PHE A 325     3222   3465   2847    106    707    452       N  
ATOM   1237  CA  PHE A 325     -42.692  22.155  -4.088  1.00 28.55           C  
ANISOU 1237  CA  PHE A 325     3566   3848   3435    120    768    502       C  
ATOM   1238  C   PHE A 325     -41.319  21.778  -4.570  1.00 32.73           C  
ANISOU 1238  C   PHE A 325     4118   4334   3986    180    837    596       C  
ATOM   1239  O   PHE A 325     -40.634  21.002  -3.911  1.00 31.07           O  
ANISOU 1239  O   PHE A 325     3908   4127   3771    135    825    586       O  
ATOM   1240  CB  PHE A 325     -42.646  22.667  -2.632  1.00 27.63           C  
ANISOU 1240  CB  PHE A 325     3345   3733   3420     12    733    433       C  
ATOM   1241  CG  PHE A 325     -43.927  23.365  -2.214  1.00 32.26           C  
ANISOU 1241  CG  PHE A 325     3893   4351   4014    -35    681    354       C  
ATOM   1242  CD1 PHE A 325     -45.031  22.641  -1.856  1.00 26.85           C  
ANISOU 1242  CD1 PHE A 325     3250   3727   3225    -88    601    269       C  
ATOM   1243  CD2 PHE A 325     -44.022  24.753  -2.251  1.00 33.68           C  
ANISOU 1243  CD2 PHE A 325     3998   4497   4303    -21    717    371       C  
ATOM   1244  CE1 PHE A 325     -46.233  23.261  -1.516  1.00 32.45           C  
ANISOU 1244  CE1 PHE A 325     3926   4469   3936   -126    554    200       C  
ATOM   1245  CE2 PHE A 325     -45.225  25.404  -1.927  1.00 35.95           C  
ANISOU 1245  CE2 PHE A 325     4254   4814   4594    -56    673    304       C  
ATOM   1246  CZ  PHE A 325     -46.342  24.664  -1.568  1.00 30.73           C  
ANISOU 1246  CZ  PHE A 325     3634   4218   3826   -108    591    219       C  
ATOM   1247  N   VAL A 326     -40.904  22.329  -5.708  1.00 32.24           N  
ANISOU 1247  N   VAL A 326     4071   4230   3946    281    910    687       N  
ATOM   1248  CA  VAL A 326     -39.564  22.046  -6.241  1.00 30.17           C  
ANISOU 1248  CA  VAL A 326     3829   3924   3710    346    982    785       C  
ATOM   1249  C   VAL A 326     -38.584  23.116  -5.854  1.00 36.27           C  
ANISOU 1249  C   VAL A 326     4498   4644   4641    339   1040    831       C  
ATOM   1250  O   VAL A 326     -38.654  24.253  -6.359  1.00 36.18           O  
ANISOU 1250  O   VAL A 326     4446   4599   4702    385   1085    869       O  
ATOM   1251  CB  VAL A 326     -39.602  21.906  -7.810  1.00 38.55           C  
ANISOU 1251  CB  VAL A 326     4981   4972   4696    469   1033    866       C  
ATOM   1252  CG1 VAL A 326     -38.205  21.624  -8.363  1.00 47.45           C  
ANISOU 1252  CG1 VAL A 326     6127   6052   5850    539   1111    970       C  
ATOM   1253  CG2 VAL A 326     -40.579  20.826  -8.251  1.00 33.86           C  
ANISOU 1253  CG2 VAL A 326     4495   4431   3940    476    977    821       C  
ATOM   1254  N   ILE A 327     -37.661  22.766  -4.945  1.00 31.78           N  
ANISOU 1254  N   ILE A 327     3883   4068   4124    280   1039    826       N  
ATOM   1255  CA  ILE A 327     -36.650  23.664  -4.491  1.00 32.81           C  
ANISOU 1255  CA  ILE A 327     3914   4153   4401    263   1090    867       C  
ATOM   1256  C   ILE A 327     -35.658  23.756  -5.633  1.00 41.31           C  
ANISOU 1256  C   ILE A 327     5021   5182   5493    372   1179    987       C  
ATOM   1257  O   ILE A 327     -35.402  22.763  -6.319  1.00 42.56           O  
ANISOU 1257  O   ILE A 327     5269   5349   5554    430   1192   1028       O  
ATOM   1258  CB  ILE A 327     -35.967  23.113  -3.243  1.00 31.05           C  
ANISOU 1258  CB  ILE A 327     3643   3945   4211    173   1060    829       C  
ATOM   1259  CG1 ILE A 327     -36.985  23.004  -2.112  1.00 34.93           C  
ANISOU 1259  CG1 ILE A 327     4106   4483   4682     65    970    709       C  
ATOM   1260  CG2 ILE A 327     -34.800  23.983  -2.795  1.00 33.17           C  
ANISOU 1260  CG2 ILE A 327     3808   4168   4628    155   1116    878       C  
ATOM   1261  CD1 ILE A 327     -36.476  22.160  -0.923  1.00 32.76           C  
ANISOU 1261  CD1 ILE A 327     3807   4235   4403    -21    928    663       C  
ATOM   1262  N   GLN A 328     -35.113  24.949  -5.846  1.00 39.29           N  
ANISOU 1262  N   GLN A 328     4694   4876   5359    400   1243   1042       N  
ATOM   1263  CA  GLN A 328     -34.336  25.220  -7.043  1.00 47.45           C  
ANISOU 1263  CA  GLN A 328     5754   5862   6412    511   1331   1156       C  
ATOM   1264  C   GLN A 328     -33.108  25.981  -6.682  1.00 52.95           C  
ANISOU 1264  C   GLN A 328     6356   6511   7250    499   1393   1212       C  
ATOM   1265  O   GLN A 328     -33.183  26.945  -5.943  1.00 48.37           O  
ANISOU 1265  O   GLN A 328     5687   5917   6776    436   1388   1175       O  
ATOM   1266  CB  GLN A 328     -35.119  26.118  -7.964  1.00 51.84           C  
ANISOU 1266  CB  GLN A 328     6326   6402   6970    578   1356   1175       C  
ATOM   1267  CG  GLN A 328     -35.998  25.410  -8.895  1.00 55.10           C  
ANISOU 1267  CG  GLN A 328     6848   6847   7239    640   1332   1171       C  
ATOM   1268  CD  GLN A 328     -37.151  26.278  -9.281  1.00 58.19           C  
ANISOU 1268  CD  GLN A 328     7235   7247   7629    659   1319   1141       C  
ATOM   1269  OE1 GLN A 328     -37.325  27.366  -8.727  1.00 59.98           O  
ANISOU 1269  OE1 GLN A 328     7375   7454   7961    617   1323   1115       O  
ATOM   1270  NE2 GLN A 328     -37.962  25.807 -10.225  1.00 61.98           N  
ANISOU 1270  NE2 GLN A 328     7807   7756   7988    723   1303   1145       N  
ATOM   1271  N   GLY A 329     -31.961  25.574  -7.205  1.00 48.69           N  
ANISOU 1271  N   GLY A 329     5838   5946   6716    560   1453   1303       N  
ATOM   1272  CA  GLY A 329     -30.806  26.434  -7.056  1.00 47.19           C  
ANISOU 1272  CA  GLY A 329     5559   5707   6665    562   1522   1369       C  
ATOM   1273  C   GLY A 329     -29.538  25.644  -6.978  1.00 41.46           C  
ANISOU 1273  C   GLY A 329     4837   4977   5938    576   1554   1431       C  
ATOM   1274  O   GLY A 329     -29.561  24.402  -7.028  1.00 42.48           O  
ANISOU 1274  O   GLY A 329     5042   5141   5956    585   1523   1422       O  
ATOM   1275  N   ALA A 330     -28.426  26.351  -6.828  1.00 41.48           N  
ANISOU 1275  N   ALA A 330     4764   4938   6057    578   1589   1471       N  
ATOM   1276  CA  ALA A 330     -27.129  25.699  -6.786  1.00 45.34           C  
ANISOU 1276  CA  ALA A 330     5256   5422   6549    599   1589   1507       C  
ATOM   1277  C   ALA A 330     -26.805  25.473  -5.320  1.00 58.86           C  
ANISOU 1277  C   ALA A 330     6896   7165   8303    482   1537   1443       C  
ATOM   1278  O   ALA A 330     -25.890  26.092  -4.764  1.00 73.59           O  
ANISOU 1278  O   ALA A 330     8683   9008  10270    447   1534   1442       O  
ATOM   1279  CB  ALA A 330     -26.060  26.568  -7.472  1.00 44.36           C  
ANISOU 1279  CB  ALA A 330     5097   5239   6520    671   1639   1576       C  
ATOM   1280  N   LEU A 331     -27.569  24.585  -4.691  1.00 48.14           N  
ANISOU 1280  N   LEU A 331     5569   5861   6862    421   1494   1385       N  
ATOM   1281  CA  LEU A 331     -27.471  24.385  -3.242  1.00 47.44           C  
ANISOU 1281  CA  LEU A 331     5411   5807   6809    303   1438   1310       C  
ATOM   1282  C   LEU A 331     -26.126  23.771  -2.825  1.00 46.09           C  
ANISOU 1282  C   LEU A 331     5222   5640   6650    299   1428   1334       C  
ATOM   1283  O   LEU A 331     -25.612  22.857  -3.471  1.00 49.43           O  
ANISOU 1283  O   LEU A 331     5717   6067   6999    370   1446   1387       O  
ATOM   1284  CB  LEU A 331     -28.636  23.511  -2.732  1.00 36.14           C  
ANISOU 1284  CB  LEU A 331     4030   4431   5269    247   1371   1226       C  
ATOM   1285  CG  LEU A 331     -30.032  24.179  -2.608  1.00 49.77           C  
ANISOU 1285  CG  LEU A 331     5755   6166   6989    211   1321   1141       C  
ATOM   1286  CD1 LEU A 331     -30.670  24.480  -3.929  1.00 53.07           C  
ANISOU 1286  CD1 LEU A 331     6245   6561   7357    309   1353   1181       C  
ATOM   1287  CD2 LEU A 331     -30.972  23.326  -1.780  1.00 47.55           C  
ANISOU 1287  CD2 LEU A 331     5507   5942   6617    134   1227   1033       C  
ATOM   1288  N   ASP A 332     -25.566  24.241  -1.719  1.00 33.40           N  
ANISOU 1288  N   ASP A 332     3981   4781   3928     -1    282   -352       N  
ATOM   1289  CA  ASP A 332     -24.367  23.583  -1.216  1.00 40.35           C  
ANISOU 1289  CA  ASP A 332     4822   5694   4814     36    284   -359       C  
ATOM   1290  C   ASP A 332     -24.733  22.489  -0.228  1.00 34.76           C  
ANISOU 1290  C   ASP A 332     4104   4994   4109     70    257   -315       C  
ATOM   1291  O   ASP A 332     -25.910  22.207   0.005  1.00 32.97           O  
ANISOU 1291  O   ASP A 332     3901   4743   3881     63    239   -281       O  
ATOM   1292  CB  ASP A 332     -23.395  24.584  -0.585  1.00 43.36           C  
ANISOU 1292  CB  ASP A 332     5153   6138   5184     31    297   -394       C  
ATOM   1293  CG  ASP A 332     -23.909  25.156   0.716  1.00 55.00           C  
ANISOU 1293  CG  ASP A 332     6600   7657   6642     25    280   -378       C  
ATOM   1294  OD1 ASP A 332     -24.970  24.691   1.186  1.00 55.80           O  
ANISOU 1294  OD1 ASP A 332     6719   7741   6743     30    258   -338       O  
ATOM   1295  OD2 ASP A 332     -23.250  26.066   1.282  1.00 64.04           O  
ANISOU 1295  OD2 ASP A 332     7706   8853   7774     15    290   -407       O  
ATOM   1296  N   ASP A 333     -23.717  21.909   0.389  1.00 31.62           N  
ANISOU 1296  N   ASP A 333     3667   4631   3715    105    254   -315       N  
ATOM   1297  CA  ASP A 333     -23.890  20.785   1.295  1.00 36.03           C  
ANISOU 1297  CA  ASP A 333     4215   5197   4277    143    230   -273       C  
ATOM   1298  C   ASP A 333     -24.912  21.081   2.393  1.00 35.50           C  
ANISOU 1298  C   ASP A 333     4145   5149   4194    135    208   -244       C  
ATOM   1299  O   ASP A 333     -25.907  20.329   2.577  1.00 31.65           O  
ANISOU 1299  O   ASP A 333     3686   4629   3711    142    193   -206       O  
ATOM   1300  CB  ASP A 333     -22.531  20.435   1.949  1.00 37.35           C  
ANISOU 1300  CB  ASP A 333     4330   5414   4447    180    229   -281       C  
ATOM   1301  CG  ASP A 333     -21.647  19.554   1.063  1.00 48.24           C  
ANISOU 1301  CG  ASP A 333     5716   6763   5850    206    248   -291       C  
ATOM   1302  OD1 ASP A 333     -22.076  19.146  -0.027  1.00 54.93           O  
ANISOU 1302  OD1 ASP A 333     6612   7551   6709    194    262   -291       O  
ATOM   1303  OD2 ASP A 333     -20.510  19.242   1.475  1.00 57.37           O  
ANISOU 1303  OD2 ASP A 333     6829   7956   7014    237    249   -298       O  
ATOM   1304  N   VAL A 334     -24.658  22.167   3.127  1.00 33.58           N  
ANISOU 1304  N   VAL A 334     3867   4958   3933    118    208   -263       N  
ATOM   1305  CA  VAL A 334     -25.467  22.476   4.308  1.00 38.58           C  
ANISOU 1305  CA  VAL A 334     4492   5616   4550    112    191   -238       C  
ATOM   1306  C   VAL A 334     -26.920  22.827   3.944  1.00 35.98           C  
ANISOU 1306  C   VAL A 334     4204   5242   4224     80    191   -221       C  
ATOM   1307  O   VAL A 334     -27.854  22.459   4.657  1.00 31.31           O  
ANISOU 1307  O   VAL A 334     3623   4642   3631     84    175   -186       O  
ATOM   1308  CB  VAL A 334     -24.775  23.563   5.222  1.00 42.18           C  
ANISOU 1308  CB  VAL A 334     4901   6141   4985     99    194   -264       C  
ATOM   1309  CG1 VAL A 334     -25.068  24.980   4.763  1.00 36.00           C  
ANISOU 1309  CG1 VAL A 334     4125   5358   4195     53    217   -297       C  
ATOM   1310  CG2 VAL A 334     -25.219  23.395   6.637  1.00 42.68           C  
ANISOU 1310  CG2 VAL A 334     4950   6236   5032    110    172   -233       C  
ATOM   1311  N   GLU A 335     -27.108  23.510   2.823  1.00 32.32           N  
ANISOU 1311  N   GLU A 335     3764   4748   3766     49    209   -246       N  
ATOM   1312  CA  GLU A 335     -28.433  23.924   2.385  1.00 31.04           C  
ANISOU 1312  CA  GLU A 335     3638   4546   3610     18    208   -232       C  
ATOM   1313  C   GLU A 335     -29.310  22.760   2.013  1.00 30.27           C  
ANISOU 1313  C   GLU A 335     3577   4395   3527     30    192   -195       C  
ATOM   1314  O   GLU A 335     -30.528  22.760   2.300  1.00 28.87           O  
ANISOU 1314  O   GLU A 335     3418   4197   3354     17    180   -167       O  
ATOM   1315  CB  GLU A 335     -28.312  24.923   1.224  1.00 36.76           C  
ANISOU 1315  CB  GLU A 335     4380   5253   4335    -15    230   -267       C  
ATOM   1316  CG  GLU A 335     -27.602  26.191   1.665  1.00 43.96           C  
ANISOU 1316  CG  GLU A 335     5257   6215   5231    -32    250   -303       C  
ATOM   1317  CD  GLU A 335     -27.227  27.138   0.514  1.00 53.80           C  
ANISOU 1317  CD  GLU A 335     6519   7448   6477    -60    277   -344       C  
ATOM   1318  OE1 GLU A 335     -27.092  26.672  -0.664  1.00 45.81           O  
ANISOU 1318  OE1 GLU A 335     5539   6393   5475    -59    283   -351       O  
ATOM   1319  OE2 GLU A 335     -27.058  28.356   0.814  1.00 47.75           O  
ANISOU 1319  OE2 GLU A 335     5733   6711   5698    -83    296   -369       O  
ATOM   1320  N   ILE A 336     -28.719  21.775   1.349  1.00 29.43           N  
ANISOU 1320  N   ILE A 336     3485   4266   3431     52    194   -197       N  
ATOM   1321  CA  ILE A 336     -29.410  20.511   1.084  1.00 35.22           C  
ANISOU 1321  CA  ILE A 336     4252   4953   4178     67    181   -163       C  
ATOM   1322  C   ILE A 336     -29.809  19.784   2.357  1.00 29.79           C  
ANISOU 1322  C   ILE A 336     3550   4280   3488     94    163   -125       C  
ATOM   1323  O   ILE A 336     -30.933  19.254   2.482  1.00 27.07           O  
ANISOU 1323  O   ILE A 336     3231   3902   3151     90    151    -93       O  
ATOM   1324  CB  ILE A 336     -28.541  19.584   0.215  1.00 36.92           C  
ANISOU 1324  CB  ILE A 336     4482   5143   4403     87    193   -174       C  
ATOM   1325  CG1 ILE A 336     -28.513  20.095  -1.217  1.00 47.72           C  
ANISOU 1325  CG1 ILE A 336     5882   6475   5774     56    210   -203       C  
ATOM   1326  CG2 ILE A 336     -29.056  18.183   0.255  1.00 46.07           C  
ANISOU 1326  CG2 ILE A 336     5667   6264   5573    110    182   -138       C  
ATOM   1327  CD1 ILE A 336     -28.233  19.014  -2.238  1.00 60.14           C  
ANISOU 1327  CD1 ILE A 336     7492   8001   7360     65    219   -203       C  
ATOM   1328  N   LEU A 337     -28.896  19.720   3.320  1.00 26.05           N  
ANISOU 1328  N   LEU A 337     3037   3858   3004    121    160   -128       N  
ATOM   1329  CA  LEU A 337     -29.233  19.015   4.561  1.00 26.33           C  
ANISOU 1329  CA  LEU A 337     3062   3908   3034    148    143    -91       C  
ATOM   1330  C   LEU A 337     -30.351  19.772   5.301  1.00 29.52           C  
ANISOU 1330  C   LEU A 337     3468   4319   3431    121    136    -77       C  
ATOM   1331  O   LEU A 337     -31.297  19.148   5.819  1.00 27.90           O  
ANISOU 1331  O   LEU A 337     3280   4091   3230    127    125    -42       O  
ATOM   1332  CB  LEU A 337     -27.986  18.905   5.474  1.00 25.69           C  
ANISOU 1332  CB  LEU A 337     2935   3886   2940    181    139    -98       C  
ATOM   1333  CG  LEU A 337     -26.866  18.006   4.991  1.00 30.27           C  
ANISOU 1333  CG  LEU A 337     3508   4463   3532    216    145   -104       C  
ATOM   1334  CD1 LEU A 337     -25.710  17.938   6.059  1.00 29.96           C  
ANISOU 1334  CD1 LEU A 337     3417   4488   3480    250    135   -105       C  
ATOM   1335  CD2 LEU A 337     -27.412  16.604   4.655  1.00 34.75           C  
ANISOU 1335  CD2 LEU A 337     4113   4976   4116    239    143    -70       C  
ATOM   1336  N   ARG A 338     -30.265  21.102   5.352  1.00 29.32           N  
ANISOU 1336  N   ARG A 338     3424   4321   3394     91    146   -104       N  
ATOM   1337  CA  ARG A 338     -31.298  21.865   6.014  1.00 30.52           C  
ANISOU 1337  CA  ARG A 338     3577   4476   3541     65    145    -92       C  
ATOM   1338  C   ARG A 338     -32.622  21.677   5.280  1.00 31.17           C  
ANISOU 1338  C   ARG A 338     3699   4499   3644     44    142    -72       C  
ATOM   1339  O   ARG A 338     -33.643  21.509   5.927  1.00 28.69           O  
ANISOU 1339  O   ARG A 338     3395   4172   3336     40    134    -42       O  
ATOM   1340  CB  ARG A 338     -30.972  23.360   6.066  1.00 32.00           C  
ANISOU 1340  CB  ARG A 338     3743   4699   3716     33    161   -126       C  
ATOM   1341  CG  ARG A 338     -29.827  23.668   6.993  1.00 36.57           C  
ANISOU 1341  CG  ARG A 338     4280   5342   4273     47    162   -144       C  
ATOM   1342  CD  ARG A 338     -29.507  25.168   7.024  1.00 47.57           C  
ANISOU 1342  CD  ARG A 338     5653   6768   5652     13    183   -181       C  
ATOM   1343  NE  ARG A 338     -28.287  25.361   7.798  1.00 51.32           N  
ANISOU 1343  NE  ARG A 338     6086   7306   6106     26    182   -202       N  
ATOM   1344  CZ  ARG A 338     -27.289  26.184   7.485  1.00 53.41           C  
ANISOU 1344  CZ  ARG A 338     6326   7605   6363     12    199   -245       C  
ATOM   1345  NH1 ARG A 338     -26.236  26.244   8.290  1.00 50.60           N  
ANISOU 1345  NH1 ARG A 338     5930   7308   5989     26    193   -259       N  
ATOM   1346  NH2 ARG A 338     -27.332  26.941   6.385  1.00 60.00           N  
ANISOU 1346  NH2 ARG A 338     7176   8415   7207    -14    221   -273       N  
ATOM   1347  N   ALA A 339     -32.607  21.680   3.948  1.00 31.37           N  
ANISOU 1347  N   ALA A 339     3749   4489   3681     30    148    -87       N  
ATOM   1348  CA  ALA A 339     -33.858  21.473   3.174  1.00 28.78           C  
ANISOU 1348  CA  ALA A 339     3459   4106   3371      9    141    -68       C  
ATOM   1349  C   ALA A 339     -34.438  20.117   3.500  1.00 28.93           C  
ANISOU 1349  C   ALA A 339     3496   4095   3401     32    126    -32       C  
ATOM   1350  O   ALA A 339     -35.633  19.987   3.781  1.00 30.89           O  
ANISOU 1350  O   ALA A 339     3758   4318   3660     20    118     -4       O  
ATOM   1351  CB  ALA A 339     -33.596  21.571   1.685  1.00 28.26           C  
ANISOU 1351  CB  ALA A 339     3418   4008   3310     -7    148    -91       C  
ATOM   1352  N   ARG A 340     -33.605  19.081   3.487  1.00 26.53           N  
ANISOU 1352  N   ARG A 340     3192   3793   3094     65    126    -30       N  
ATOM   1353  CA  ARG A 340     -34.125  17.756   3.694  1.00 26.83           C  
ANISOU 1353  CA  ARG A 340     3252   3799   3143     87    116      3       C  
ATOM   1354  C   ARG A 340     -34.606  17.537   5.146  1.00 25.10           C  
ANISOU 1354  C   ARG A 340     3018   3600   2919    102    108     32       C  
ATOM   1355  O   ARG A 340     -35.513  16.745   5.408  1.00 28.33           O  
ANISOU 1355  O   ARG A 340     3448   3976   3339    107    102     63       O  
ATOM   1356  CB  ARG A 340     -33.070  16.716   3.255  1.00 28.88           C  
ANISOU 1356  CB  ARG A 340     3517   4053   3404    119    123     -3       C  
ATOM   1357  CG  ARG A 340     -33.598  15.318   3.071  1.00 43.76           C  
ANISOU 1357  CG  ARG A 340     5434   5890   5302    136    120     26       C  
ATOM   1358  CD  ARG A 340     -33.579  14.547   4.365  1.00 42.32           C  
ANISOU 1358  CD  ARG A 340     5238   5725   5114    172    114     56       C  
ATOM   1359  NE  ARG A 340     -32.258  14.029   4.634  1.00 45.66           N  
ANISOU 1359  NE  ARG A 340     5640   6177   5531    213    119     51       N  
ATOM   1360  CZ  ARG A 340     -31.746  12.988   3.989  1.00 41.62           C  
ANISOU 1360  CZ  ARG A 340     5147   5637   5030    235    130     53       C  
ATOM   1361  NH1 ARG A 340     -30.526  12.557   4.288  1.00 43.78           N  
ANISOU 1361  NH1 ARG A 340     5396   5938   5301    274    136     50       N  
ATOM   1362  NH2 ARG A 340     -32.473  12.368   3.054  1.00 46.73           N  
ANISOU 1362  NH2 ARG A 340     5837   6226   5691    218    135     59       N  
ATOM   1363  N   GLN A 341     -33.955  18.179   6.100  1.00 26.24           N  
ANISOU 1363  N   GLN A 341     3127   3797   3045    111    110     23       N  
ATOM   1364  CA  GLN A 341     -34.374  18.117   7.493  1.00 23.36           C  
ANISOU 1364  CA  GLN A 341     2750   3454   2671    121    104     48       C  
ATOM   1365  C   GLN A 341     -35.737  18.788   7.684  1.00 25.18           C  
ANISOU 1365  C   GLN A 341     2992   3663   2912     86    105     60       C  
ATOM   1366  O   GLN A 341     -36.562  18.314   8.485  1.00 21.68           O  
ANISOU 1366  O   GLN A 341     2558   3205   2474     91    101     90       O  
ATOM   1367  CB  GLN A 341     -33.305  18.802   8.415  1.00 23.37           C  
ANISOU 1367  CB  GLN A 341     2712   3522   2647    131    105     30       C  
ATOM   1368  CG  GLN A 341     -32.115  17.893   8.651  1.00 25.78           C  
ANISOU 1368  CG  GLN A 341     3001   3851   2943    175     99     32       C  
ATOM   1369  CD  GLN A 341     -30.893  18.649   9.189  1.00 37.48           C  
ANISOU 1369  CD  GLN A 341     4440   5398   4402    180     99      5       C  
ATOM   1370  OE1 GLN A 341     -30.967  19.844   9.517  1.00 35.38           O  
ANISOU 1370  OE1 GLN A 341     4157   5161   4123    150    105    -14       O  
ATOM   1371  NE2 GLN A 341     -29.780  17.951   9.280  1.00 44.06           N  
ANISOU 1371  NE2 GLN A 341     5255   6255   5232    218     93      4       N  
ATOM   1372  N   PHE A 342     -35.949  19.927   7.019  1.00 22.30           N  
ANISOU 1372  N   PHE A 342     2625   3298   2552     51    113     38       N  
ATOM   1373  CA  PHE A 342     -37.283  20.550   7.027  1.00 21.79           C  
ANISOU 1373  CA  PHE A 342     2570   3206   2504     19    115     51       C  
ATOM   1374  C   PHE A 342     -38.334  19.580   6.433  1.00 23.70           C  
ANISOU 1374  C   PHE A 342     2845   3390   2770     17    105     77       C  
ATOM   1375  O   PHE A 342     -39.436  19.386   6.991  1.00 23.17           O  
ANISOU 1375  O   PHE A 342     2786   3300   2717      9    103    104       O  
ATOM   1376  CB  PHE A 342     -37.320  21.892   6.242  1.00 27.00           C  
ANISOU 1376  CB  PHE A 342     3224   3869   3165    -16    126     24       C  
ATOM   1377  CG  PHE A 342     -38.724  22.341   5.962  1.00 20.93           C  
ANISOU 1377  CG  PHE A 342     2470   3062   2420    -46    126     41       C  
ATOM   1378  CD1 PHE A 342     -39.267  22.238   4.696  1.00 20.74           C  
ANISOU 1378  CD1 PHE A 342     2470   2996   2413    -63    118     42       C  
ATOM   1379  CD2 PHE A 342     -39.560  22.682   7.018  1.00 26.83           C  
ANISOU 1379  CD2 PHE A 342     3208   3812   3173    -55    132     62       C  
ATOM   1380  CE1 PHE A 342     -40.598  22.566   4.485  1.00 22.43           C  
ANISOU 1380  CE1 PHE A 342     2695   3176   2652    -89    114     63       C  
ATOM   1381  CE2 PHE A 342     -40.894  22.959   6.801  1.00 26.82           C  
ANISOU 1381  CE2 PHE A 342     3218   3773   3200    -79    131     82       C  
ATOM   1382  CZ  PHE A 342     -41.396  22.923   5.543  1.00 21.66           C  
ANISOU 1382  CZ  PHE A 342     2583   3081   2564    -95    121     83       C  
ATOM   1383  N   VAL A 343     -38.000  18.941   5.319  1.00 19.51           N  
ANISOU 1383  N   VAL A 343     2336   2834   2245     22    100     69       N  
ATOM   1384  CA  VAL A 343     -38.975  18.104   4.628  1.00 18.56           C  
ANISOU 1384  CA  VAL A 343     2247   2658   2145     13     91     90       C  
ATOM   1385  C   VAL A 343     -39.307  16.955   5.546  1.00 19.28           C  
ANISOU 1385  C   VAL A 343     2346   2739   2240     40     88    120       C  
ATOM   1386  O   VAL A 343     -40.461  16.531   5.708  1.00 21.63           O  
ANISOU 1386  O   VAL A 343     2660   3003   2557     30     83    145       O  
ATOM   1387  CB  VAL A 343     -38.329  17.580   3.323  1.00 21.40           C  
ANISOU 1387  CB  VAL A 343     2630   2998   2505     15     90     72       C  
ATOM   1388  CG1 VAL A 343     -39.173  16.473   2.686  1.00 22.20           C  
ANISOU 1388  CG1 VAL A 343     2767   3044   2623     10     81     92       C  
ATOM   1389  CG2 VAL A 343     -38.226  18.742   2.304  1.00 24.76           C  
ANISOU 1389  CG2 VAL A 343     3055   3423   2928    -17     93     44       C  
ATOM   1390  N   ASP A 344     -38.297  16.403   6.197  1.00 20.86           N  
ANISOU 1390  N   ASP A 344     2534   2968   2423     76     91    120       N  
ATOM   1391  CA  ASP A 344     -38.609  15.258   7.049  1.00 23.24           C  
ANISOU 1391  CA  ASP A 344     2847   3257   2727    104     89    150       C  
ATOM   1392  C   ASP A 344     -39.531  15.679   8.202  1.00 23.93           C  
ANISOU 1392  C   ASP A 344     2926   3351   2817     94     90    170       C  
ATOM   1393  O   ASP A 344     -40.407  14.917   8.613  1.00 22.82           O  
ANISOU 1393  O   ASP A 344     2803   3177   2689     98     90    198       O  
ATOM   1394  CB  ASP A 344     -37.319  14.700   7.710  1.00 25.49           C  
ANISOU 1394  CB  ASP A 344     3115   3579   2990    147     91    149       C  
ATOM   1395  CG  ASP A 344     -36.460  13.850   6.769  1.00 40.03           C  
ANISOU 1395  CG  ASP A 344     4970   5405   4834    169     94    139       C  
ATOM   1396  OD1 ASP A 344     -35.312  13.504   7.183  1.00 45.71           O  
ANISOU 1396  OD1 ASP A 344     5671   6157   5540    204     96    136       O  
ATOM   1397  OD2 ASP A 344     -36.917  13.503   5.650  1.00 37.48           O  
ANISOU 1397  OD2 ASP A 344     4675   5037   4527    150     96    136       O  
ATOM   1398  N   SER A 345     -39.295  16.849   8.760  1.00 24.53           N  
ANISOU 1398  N   SER A 345     2974   3465   2879     80     95    157       N  
ATOM   1399  CA  SER A 345     -40.129  17.349   9.849  1.00 21.58           C  
ANISOU 1399  CA  SER A 345     2594   3097   2508     67    101    173       C  
ATOM   1400  C   SER A 345     -41.556  17.648   9.339  1.00 21.01           C  
ANISOU 1400  C   SER A 345     2536   2979   2468     33    102    185       C  
ATOM   1401  O   SER A 345     -42.567  17.419  10.043  1.00 20.07           O  
ANISOU 1401  O   SER A 345     2425   2837   2363     27    106    209       O  
ATOM   1402  CB  SER A 345     -39.529  18.617  10.394  1.00 31.12           C  
ANISOU 1402  CB  SER A 345     3773   4356   3695     55    109    151       C  
ATOM   1403  OG  SER A 345     -40.454  19.200  11.273  1.00 38.97           O  
ANISOU 1403  OG  SER A 345     4763   5347   4695     35    119    165       O  
ATOM   1404  N   TYR A 346     -41.641  18.155   8.110  1.00 20.14           N  
ANISOU 1404  N   TYR A 346     2429   2854   2368      9     98    167       N  
ATOM   1405  CA  TYR A 346     -42.953  18.368   7.492  1.00 19.46           C  
ANISOU 1405  CA  TYR A 346     2356   2725   2314    -22     93    180       C  
ATOM   1406  C   TYR A 346     -43.769  17.051   7.383  1.00 19.96           C  
ANISOU 1406  C   TYR A 346     2446   2742   2397    -15     86    206       C  
ATOM   1407  O   TYR A 346     -44.957  16.971   7.751  1.00 18.92           O  
ANISOU 1407  O   TYR A 346     2318   2582   2290    -29     87    228       O  
ATOM   1408  CB  TYR A 346     -42.775  19.022   6.113  1.00 20.05           C  
ANISOU 1408  CB  TYR A 346     2434   2793   2392    -45     87    157       C  
ATOM   1409  CG  TYR A 346     -44.124  19.302   5.434  1.00 20.77           C  
ANISOU 1409  CG  TYR A 346     2535   2842   2515    -78     79    172       C  
ATOM   1410  CD1 TYR A 346     -44.811  20.503   5.657  1.00 22.34           C  
ANISOU 1410  CD1 TYR A 346     2716   3044   2728   -104     87    174       C  
ATOM   1411  CD2 TYR A 346     -44.735  18.336   4.680  1.00 18.01           C  
ANISOU 1411  CD2 TYR A 346     2211   2449   2182    -83     64    185       C  
ATOM   1412  CE1 TYR A 346     -46.074  20.760   5.044  1.00 20.81           C  
ANISOU 1412  CE1 TYR A 346     2528   2813   2567   -132     77    191       C  
ATOM   1413  CE2 TYR A 346     -45.978  18.577   4.070  1.00 20.58           C  
ANISOU 1413  CE2 TYR A 346     2544   2740   2537   -114     52    199       C  
ATOM   1414  CZ  TYR A 346     -46.635  19.760   4.251  1.00 22.86           C  
ANISOU 1414  CZ  TYR A 346     2811   3032   2841   -136     57    203       C  
ATOM   1415  OH  TYR A 346     -47.892  19.935   3.690  1.00 17.97           O  
ANISOU 1415  OH  TYR A 346     2195   2379   2255   -164     44    221       O  
ATOM   1416  N   TYR A 347     -43.145  16.017   6.837  1.00 20.45           N  
ANISOU 1416  N   TYR A 347     2526   2793   2451      7     80    203       N  
ATOM   1417  CA  TYR A 347     -43.809  14.733   6.649  1.00 23.03           C  
ANISOU 1417  CA  TYR A 347     2882   3076   2794     13     76    224       C  
ATOM   1418  C   TYR A 347     -44.155  14.064   7.977  1.00 25.01           C  
ANISOU 1418  C   TYR A 347     3134   3325   3045     35     85    250       C  
ATOM   1419  O   TYR A 347     -45.095  13.274   8.043  1.00 24.30           O  
ANISOU 1419  O   TYR A 347     3063   3194   2975     31     86    270       O  
ATOM   1420  CB  TYR A 347     -42.892  13.804   5.875  1.00 23.48           C  
ANISOU 1420  CB  TYR A 347     2957   3125   2839     34     75    213       C  
ATOM   1421  CG  TYR A 347     -42.702  14.114   4.391  1.00 22.05           C  
ANISOU 1421  CG  TYR A 347     2788   2929   2659     10     66    191       C  
ATOM   1422  CD1 TYR A 347     -41.518  13.726   3.749  1.00 23.01           C  
ANISOU 1422  CD1 TYR A 347     2919   3060   2765     28     71    172       C  
ATOM   1423  CD2 TYR A 347     -43.687  14.772   3.636  1.00 21.94           C  
ANISOU 1423  CD2 TYR A 347     2778   2892   2664    -30     55    191       C  
ATOM   1424  CE1 TYR A 347     -41.324  13.950   2.397  1.00 24.01           C  
ANISOU 1424  CE1 TYR A 347     3061   3170   2891      5     66    151       C  
ATOM   1425  CE2 TYR A 347     -43.499  15.013   2.257  1.00 20.28           C  
ANISOU 1425  CE2 TYR A 347     2585   2669   2453    -52     47    172       C  
ATOM   1426  CZ  TYR A 347     -42.325  14.611   1.669  1.00 23.60           C  
ANISOU 1426  CZ  TYR A 347     3016   3095   2854    -36     53    151       C  
ATOM   1427  OH  TYR A 347     -42.126  14.791   0.325  1.00 22.11           O  
ANISOU 1427  OH  TYR A 347     2849   2889   2662    -58     48    132       O  
ATOM   1428  N   ARG A 348     -43.388  14.307   9.032  1.00 21.22           N  
ANISOU 1428  N   ARG A 348     2636   2886   2540     59     93    248       N  
ATOM   1429  CA  ARG A 348     -43.804  13.773  10.357  1.00 23.83           C  
ANISOU 1429  CA  ARG A 348     2972   3214   2869     77    102    274       C  
ATOM   1430  C   ARG A 348     -45.185  14.322  10.781  1.00 27.78           C  
ANISOU 1430  C   ARG A 348     3469   3690   3395     46    109    288       C  
ATOM   1431  O   ARG A 348     -46.015  13.632  11.381  1.00 25.81           O  
ANISOU 1431  O   ARG A 348     3235   3410   3161     49    116    311       O  
ATOM   1432  CB  ARG A 348     -42.702  14.063  11.438  1.00 24.79           C  
ANISOU 1432  CB  ARG A 348     3073   3390   2955    105    106    269       C  
ATOM   1433  CG  ARG A 348     -41.509  13.122  11.336  1.00 35.58           C  
ANISOU 1433  CG  ARG A 348     4445   4773   4302    146    101    267       C  
ATOM   1434  CD  ARG A 348     -40.593  13.154  12.591  1.00 36.91           C  
ANISOU 1434  CD  ARG A 348     4595   4990   4437    177    101    272       C  
ATOM   1435  NE  ARG A 348     -39.968  14.474  12.793  1.00 38.61           N  
ANISOU 1435  NE  ARG A 348     4779   5256   4634    161    100    247       N  
ATOM   1436  CZ  ARG A 348     -38.820  14.845  12.219  1.00 43.92           C  
ANISOU 1436  CZ  ARG A 348     5432   5963   5294    168     94    221       C  
ATOM   1437  NH1 ARG A 348     -38.185  14.011  11.401  1.00 43.33           N  
ANISOU 1437  NH1 ARG A 348     5366   5875   5223    191     90    217       N  
ATOM   1438  NH2 ARG A 348     -38.309  16.051  12.447  1.00 44.47           N  
ANISOU 1438  NH2 ARG A 348     5473   6077   5346    151     95    198       N  
ATOM   1439  N   THR A 349     -45.478  15.578  10.430  1.00 24.70           N  
ANISOU 1439  N   THR A 349     3060   3310   3015     15    108    275       N  
ATOM   1440  CA  THR A 349     -46.793  16.115  10.730  1.00 22.38           C  
ANISOU 1440  CA  THR A 349     2761   2990   2751    -15    116    289       C  
ATOM   1441  C   THR A 349     -47.859  15.774   9.721  1.00 20.24           C  
ANISOU 1441  C   THR A 349     2503   2671   2517    -39    105    298       C  
ATOM   1442  O   THR A 349     -48.957  15.348  10.098  1.00 22.09           O  
ANISOU 1442  O   THR A 349     2745   2869   2778    -48    111    319       O  
ATOM   1443  CB  THR A 349     -46.699  17.681  10.807  1.00 27.74           C  
ANISOU 1443  CB  THR A 349     3413   3699   3427    -39    124    273       C  
ATOM   1444  OG1 THR A 349     -45.883  17.993  11.920  1.00 25.72           O  
ANISOU 1444  OG1 THR A 349     3145   3487   3139    -22    135    267       O  
ATOM   1445  CG2 THR A 349     -48.061  18.348  10.980  1.00 30.89           C  
ANISOU 1445  CG2 THR A 349     3803   4069   3863    -70    134    287       C  
ATOM   1446  N   TRP A 350     -47.558  15.894   8.424  1.00 17.74           N  
ANISOU 1446  N   TRP A 350     2190   2350   2200    -50     89    282       N  
ATOM   1447  CA  TRP A 350     -48.632  15.833   7.426  1.00 18.93           C  
ANISOU 1447  CA  TRP A 350     2349   2459   2384    -80     76    289       C  
ATOM   1448  C   TRP A 350     -48.662  14.562   6.632  1.00 20.86           C  
ANISOU 1448  C   TRP A 350     2623   2672   2631    -75     64    292       C  
ATOM   1449  O   TRP A 350     -49.611  14.323   5.885  1.00 18.67           O  
ANISOU 1449  O   TRP A 350     2355   2358   2379   -100     51    300       O  
ATOM   1450  CB  TRP A 350     -48.432  16.966   6.427  1.00 19.28           C  
ANISOU 1450  CB  TRP A 350     2381   2517   2427   -104     65    270       C  
ATOM   1451  CG  TRP A 350     -48.699  18.273   7.045  1.00 17.83           C  
ANISOU 1451  CG  TRP A 350     2171   2355   2251   -118     79    270       C  
ATOM   1452  CD1 TRP A 350     -47.795  19.157   7.517  1.00 23.72           C  
ANISOU 1452  CD1 TRP A 350     2899   3144   2971   -110     92    251       C  
ATOM   1453  CD2 TRP A 350     -49.996  18.832   7.296  1.00 18.01           C  
ANISOU 1453  CD2 TRP A 350     2180   2353   2311   -142     83    289       C  
ATOM   1454  NE1 TRP A 350     -48.459  20.282   8.049  1.00 19.57           N  
ANISOU 1454  NE1 TRP A 350     2352   2621   2462   -131    107    257       N  
ATOM   1455  CE2 TRP A 350     -49.812  20.096   7.871  1.00 20.38           C  
ANISOU 1455  CE2 TRP A 350     2456   2682   2606   -150    102    281       C  
ATOM   1456  CE3 TRP A 350     -51.305  18.399   7.007  1.00 21.18           C  
ANISOU 1456  CE3 TRP A 350     2585   2710   2751   -161     74    311       C  
ATOM   1457  CZ2 TRP A 350     -50.892  20.906   8.258  1.00 20.15           C  
ANISOU 1457  CZ2 TRP A 350     2409   2637   2611   -172    115    297       C  
ATOM   1458  CZ3 TRP A 350     -52.368  19.186   7.374  1.00 22.42           C  
ANISOU 1458  CZ3 TRP A 350     2721   2853   2943   -183     83    327       C  
ATOM   1459  CH2 TRP A 350     -52.148  20.464   7.966  1.00 22.53           C  
ANISOU 1459  CH2 TRP A 350     2713   2894   2952   -188    105    320       C  
ATOM   1460  N   GLY A 351     -47.572  13.799   6.702  1.00 20.99           N  
ANISOU 1460  N   GLY A 351     2653   2702   2619    -43     68    284       N  
ATOM   1461  CA  GLY A 351     -47.430  12.614   5.853  1.00 23.93           C  
ANISOU 1461  CA  GLY A 351     3056   3045   2990    -38     62    283       C  
ATOM   1462  C   GLY A 351     -46.963  13.091   4.483  1.00 20.79           C  
ANISOU 1462  C   GLY A 351     2663   2651   2585    -57     48    260       C  
ATOM   1463  O   GLY A 351     -46.882  14.320   4.253  1.00 22.86           O  
ANISOU 1463  O   GLY A 351     2904   2936   2846    -74     43    247       O  
ATOM   1464  N   GLY A 352     -46.757  12.175   3.529  1.00 21.27           N  
ANISOU 1464  N   GLY A 352     2754   2686   2643    -58     43    254       N  
ATOM   1465  CA  GLY A 352     -46.232  12.569   2.213  1.00 19.86           C  
ANISOU 1465  CA  GLY A 352     2585   2508   2453    -76     32    231       C  
ATOM   1466  C   GLY A 352     -47.187  12.370   1.035  1.00 22.19           C  
ANISOU 1466  C   GLY A 352     2902   2762   2765   -115     13    233       C  
ATOM   1467  O   GLY A 352     -46.740  12.227  -0.085  1.00 25.44           O  
ANISOU 1467  O   GLY A 352     3337   3163   3165   -127      7    216       O  
ATOM   1468  N   ARG A 353     -48.483  12.383   1.290  1.00 20.95           N  
ANISOU 1468  N   ARG A 353     2740   2583   2637   -137      4    254       N  
ATOM   1469  CA  ARG A 353     -49.464  12.017   0.269  1.00 23.64           C  
ANISOU 1469  CA  ARG A 353     3102   2885   2996   -174    -16    260       C  
ATOM   1470  C   ARG A 353     -50.082  13.188  -0.468  1.00 25.44           C  
ANISOU 1470  C   ARG A 353     3315   3115   3236   -209    -39    258       C  
ATOM   1471  O   ARG A 353     -50.817  12.978  -1.396  1.00 24.42           O  
ANISOU 1471  O   ARG A 353     3201   2958   3117   -241    -61    262       O  
ATOM   1472  CB  ARG A 353     -50.568  11.197   0.909  1.00 23.94           C  
ANISOU 1472  CB  ARG A 353     3142   2892   3060   -177    -13    284       C  
ATOM   1473  CG  ARG A 353     -49.999   9.961   1.676  1.00 25.57           C  
ANISOU 1473  CG  ARG A 353     3367   3093   3255   -140     12    288       C  
ATOM   1474  CD  ARG A 353     -51.146   9.135   2.202  1.00 28.14           C  
ANISOU 1474  CD  ARG A 353     3700   3384   3609   -147     17    310       C  
ATOM   1475  NE  ARG A 353     -51.969   8.523   1.130  1.00 23.16           N  
ANISOU 1475  NE  ARG A 353     3094   2714   2993   -185      1    311       N  
ATOM   1476  CZ  ARG A 353     -51.688   7.343   0.584  1.00 28.16           C  
ANISOU 1476  CZ  ARG A 353     3765   3321   3615   -183      9    305       C  
ATOM   1477  NH1 ARG A 353     -52.494   6.837  -0.356  1.00 26.69           N  
ANISOU 1477  NH1 ARG A 353     3601   3100   3441   -222     -6    305       N  
ATOM   1478  NH2 ARG A 353     -50.597   6.669   0.985  1.00 27.41           N  
ANISOU 1478  NH2 ARG A 353     3684   3233   3495   -143     34    300       N  
ATOM   1479  N   TYR A 354     -49.811  14.421  -0.059  1.00 21.26           N  
ANISOU 1479  N   TYR A 354     2755   2618   2703   -204    -35    253       N  
ATOM   1480  CA  TYR A 354     -50.444  15.553  -0.750  1.00 23.29           C  
ANISOU 1480  CA  TYR A 354     2999   2875   2974   -236    -55    255       C  
ATOM   1481  C   TYR A 354     -49.281  16.422  -1.188  1.00 23.92           C  
ANISOU 1481  C   TYR A 354     3078   2987   3025   -230    -49    228       C  
ATOM   1482  O   TYR A 354     -48.842  16.349  -2.343  1.00 23.92           O  
ANISOU 1482  O   TYR A 354     3103   2978   3007   -243    -59    212       O  
ATOM   1483  CB  TYR A 354     -51.369  16.287   0.221  1.00 21.73           C  
ANISOU 1483  CB  TYR A 354     2765   2682   2807   -240    -50    276       C  
ATOM   1484  CG  TYR A 354     -51.987  17.541  -0.388  1.00 24.01           C  
ANISOU 1484  CG  TYR A 354     3037   2974   3114   -268    -66    280       C  
ATOM   1485  CD1 TYR A 354     -52.660  17.475  -1.626  1.00 21.67           C  
ANISOU 1485  CD1 TYR A 354     2756   2652   2827   -301    -97    285       C  
ATOM   1486  CD2 TYR A 354     -51.883  18.738   0.255  1.00 23.48           C  
ANISOU 1486  CD2 TYR A 354     2938   2932   3050   -263    -50    280       C  
ATOM   1487  CE1 TYR A 354     -53.213  18.612  -2.208  1.00 25.27           C  
ANISOU 1487  CE1 TYR A 354     3195   3109   3297   -324   -114    292       C  
ATOM   1488  CE2 TYR A 354     -52.429  19.931  -0.331  1.00 26.14           C  
ANISOU 1488  CE2 TYR A 354     3259   3269   3402   -287    -62    285       C  
ATOM   1489  CZ  TYR A 354     -53.103  19.832  -1.561  1.00 28.30           C  
ANISOU 1489  CZ  TYR A 354     3548   3517   3687   -316    -95    292       C  
ATOM   1490  OH  TYR A 354     -53.658  21.023  -2.073  1.00 31.99           O  
ANISOU 1490  OH  TYR A 354     3998   3985   4171   -336   -107    302       O  
ATOM   1491  N   VAL A 355     -48.732  17.238  -0.291  1.00 20.67           N  
ANISOU 1491  N   VAL A 355     2637   2610   2605   -210    -29    222       N  
ATOM   1492  CA  VAL A 355     -47.506  17.961  -0.666  1.00 21.01           C  
ANISOU 1492  CA  VAL A 355     2680   2684   2619   -202    -19    194       C  
ATOM   1493  C   VAL A 355     -46.308  17.036  -0.705  1.00 21.87           C  
ANISOU 1493  C   VAL A 355     2808   2800   2702   -175     -7    176       C  
ATOM   1494  O   VAL A 355     -46.076  16.287   0.245  1.00 23.03           O  
ANISOU 1494  O   VAL A 355     2949   2953   2847   -147      5    185       O  
ATOM   1495  CB  VAL A 355     -47.218  19.104   0.330  1.00 22.44           C  
ANISOU 1495  CB  VAL A 355     2826   2903   2799   -191      0    190       C  
ATOM   1496  CG1 VAL A 355     -45.843  19.727   0.111  1.00 21.93           C  
ANISOU 1496  CG1 VAL A 355     2757   2872   2702   -179     14    158       C  
ATOM   1497  CG2 VAL A 355     -48.254  20.209   0.214  1.00 22.20           C  
ANISOU 1497  CG2 VAL A 355     2776   2865   2793   -218     -7    204       C  
ATOM   1498  N   GLN A 356     -45.503  17.120  -1.783  1.00 22.89           N  
ANISOU 1498  N   GLN A 356     2958   2929   2810   -181     -9    152       N  
ATOM   1499  CA  GLN A 356     -44.228  16.429  -1.844  1.00 22.67           C  
ANISOU 1499  CA  GLN A 356     2942   2911   2759   -154      7    133       C  
ATOM   1500  C   GLN A 356     -43.174  17.415  -2.232  1.00 25.89           C  
ANISOU 1500  C   GLN A 356     3341   3349   3146   -152     18    103       C  
ATOM   1501  O   GLN A 356     -43.491  18.589  -2.491  1.00 26.00           O  
ANISOU 1501  O   GLN A 356     3344   3372   3163   -174     13     98       O  
ATOM   1502  CB  GLN A 356     -44.263  15.242  -2.830  1.00 23.82           C  
ANISOU 1502  CB  GLN A 356     3131   3018   2903   -162      0    131       C  
ATOM   1503  CG  GLN A 356     -45.203  14.191  -2.351  1.00 26.17           C  
ANISOU 1503  CG  GLN A 356     3437   3287   3219   -161     -5    158       C  
ATOM   1504  CD  GLN A 356     -45.394  13.129  -3.403  1.00 39.49           C  
ANISOU 1504  CD  GLN A 356     5168   4932   4903   -178    -12    157       C  
ATOM   1505  OE1 GLN A 356     -44.915  13.278  -4.545  1.00 35.38           O  
ANISOU 1505  OE1 GLN A 356     4672   4402   4367   -196    -15    136       O  
ATOM   1506  NE2 GLN A 356     -46.088  12.057  -3.040  1.00 37.76           N  
ANISOU 1506  NE2 GLN A 356     4961   4687   4700   -176    -12    177       N  
ATOM   1507  N   PHE A 357     -41.895  17.013  -2.113  1.00 20.02           N  
ANISOU 1507  N   PHE A 357     2599   2624   2385   -125     35     83       N  
ATOM   1508  CA  PHE A 357     -40.819  17.961  -2.343  1.00 20.22           C  
ANISOU 1508  CA  PHE A 357     2609   2681   2391   -121     49     53       C  
ATOM   1509  C   PHE A 357     -39.785  17.373  -3.289  1.00 25.23           C  
ANISOU 1509  C   PHE A 357     3272   3304   3011   -115     60     29       C  
ATOM   1510  O   PHE A 357     -39.610  16.149  -3.379  1.00 25.19           O  
ANISOU 1510  O   PHE A 357     3287   3277   3008    -99     63     36       O  
ATOM   1511  CB  PHE A 357     -40.080  18.356  -1.052  1.00 19.84           C  
ANISOU 1511  CB  PHE A 357     2522   2682   2335    -92     65     48       C  
ATOM   1512  CG  PHE A 357     -40.972  19.038  -0.006  1.00 22.54           C  
ANISOU 1512  CG  PHE A 357     2836   3038   2689    -98     61     68       C  
ATOM   1513  CD1 PHE A 357     -41.010  20.440   0.113  1.00 23.52           C  
ANISOU 1513  CD1 PHE A 357     2938   3186   2811   -116     68     56       C  
ATOM   1514  CD2 PHE A 357     -41.761  18.281   0.840  1.00 21.34           C  
ANISOU 1514  CD2 PHE A 357     2683   2873   2551    -88     56     98       C  
ATOM   1515  CE1 PHE A 357     -41.837  21.066   1.075  1.00 21.46           C  
ANISOU 1515  CE1 PHE A 357     2655   2937   2564   -123     70     75       C  
ATOM   1516  CE2 PHE A 357     -42.576  18.867   1.808  1.00 22.25           C  
ANISOU 1516  CE2 PHE A 357     2775   2998   2679    -94     57    117       C  
ATOM   1517  CZ  PHE A 357     -42.609  20.287   1.948  1.00 24.33           C  
ANISOU 1517  CZ  PHE A 357     3016   3286   2941   -112     65    105       C  
ATOM   1518  N   ALA A 358     -39.057  18.261  -3.950  1.00 26.45           N  
ANISOU 1518  N   ALA A 358     3426   3472   3152   -125     69     -1       N  
ATOM   1519  CA  ALA A 358     -37.932  17.851  -4.790  1.00 32.10           C  
ANISOU 1519  CA  ALA A 358     4164   4179   3855   -118     85    -28       C  
ATOM   1520  C   ALA A 358     -36.923  18.950  -4.835  1.00 32.42           C  
ANISOU 1520  C   ALA A 358     4182   4255   3882   -116    103    -60       C  
ATOM   1521  O   ALA A 358     -37.263  20.114  -4.589  1.00 30.27           O  
ANISOU 1521  O   ALA A 358     3889   4003   3608   -131    101    -63       O  
ATOM   1522  CB  ALA A 358     -38.397  17.505  -6.186  1.00 31.87           C  
ANISOU 1522  CB  ALA A 358     4184   4103   3824   -150     76    -31       C  
ATOM   1523  N   ILE A 359     -35.664  18.590  -5.120  1.00 30.26           N  
ANISOU 1523  N   ILE A 359     3910   3988   3599    -97    124    -85       N  
ATOM   1524  CA  ILE A 359     -34.602  19.602  -5.271  1.00 28.47           C  
ANISOU 1524  CA  ILE A 359     3665   3794   3361    -97    144   -121       C  
ATOM   1525  C   ILE A 359     -34.072  19.542  -6.695  1.00 35.24           C  
ANISOU 1525  C   ILE A 359     4561   4618   4209   -115    157   -148       C  
ATOM   1526  O   ILE A 359     -33.651  18.482  -7.147  1.00 32.27           O  
ANISOU 1526  O   ILE A 359     4210   4215   3835   -104    166   -150       O  
ATOM   1527  CB  ILE A 359     -33.453  19.390  -4.305  1.00 31.81           C  
ANISOU 1527  CB  ILE A 359     4047   4259   3781    -58    159   -131       C  
ATOM   1528  CG1 ILE A 359     -33.935  19.527  -2.863  1.00 28.40           C  
ANISOU 1528  CG1 ILE A 359     3578   3861   3352    -43    147   -106       C  
ATOM   1529  CG2 ILE A 359     -32.353  20.415  -4.541  1.00 35.23           C  
ANISOU 1529  CG2 ILE A 359     4460   4723   4202    -62    181   -171       C  
ATOM   1530  CD1 ILE A 359     -32.876  19.210  -1.884  1.00 32.06           C  
ANISOU 1530  CD1 ILE A 359     4004   4367   3811     -5    156   -111       C  
ATOM   1531  N   GLU A 360     -34.140  20.652  -7.420  1.00 30.94           N  
ANISOU 1531  N   GLU A 360     4029   4072   3656   -144    161   -168       N  
ATOM   1532  CA  GLU A 360     -33.525  20.697  -8.739  1.00 34.64           C  
ANISOU 1532  CA  GLU A 360     4537   4512   4114   -162    178   -198       C  
ATOM   1533  C   GLU A 360     -32.154  21.356  -8.581  1.00 35.13           C  
ANISOU 1533  C   GLU A 360     4571   4609   4169   -147    209   -236       C  
ATOM   1534  O   GLU A 360     -32.047  22.496  -8.180  1.00 37.48           O  
ANISOU 1534  O   GLU A 360     4840   4939   4462   -153    214   -248       O  
ATOM   1535  CB  GLU A 360     -34.398  21.464  -9.743  1.00 35.63           C  
ANISOU 1535  CB  GLU A 360     4698   4609   4231   -203    164   -196       C  
ATOM   1536  CG  GLU A 360     -35.489  20.614 -10.371  1.00 40.97           C  
ANISOU 1536  CG  GLU A 360     5416   5240   4911   -224    138   -169       C  
ATOM   1537  CD  GLU A 360     -36.334  21.410 -11.362  1.00 45.88           C  
ANISOU 1537  CD  GLU A 360     6071   5837   5524   -264    120   -166       C  
ATOM   1538  OE1 GLU A 360     -37.197  20.804 -12.048  1.00 48.74           O  
ANISOU 1538  OE1 GLU A 360     6471   6162   5885   -287     96   -147       O  
ATOM   1539  OE2 GLU A 360     -36.127  22.632 -11.429  1.00 45.85           O  
ANISOU 1539  OE2 GLU A 360     6055   5854   5513   -273    130   -182       O  
ATOM   1540  N   LEU A 361     -31.104  20.610  -8.889  1.00 28.53           N  
ANISOU 1540  N   LEU A 361     3741   3764   3334   -128    230   -254       N  
ATOM   1541  CA  LEU A 361     -29.734  21.108  -8.799  1.00 27.78           C  
ANISOU 1541  CA  LEU A 361     3618   3700   3238   -114    261   -292       C  
ATOM   1542  C   LEU A 361     -29.309  21.779 -10.103  1.00 34.79           C  
ANISOU 1542  C   LEU A 361     4543   4562   4114   -143    283   -327       C  
ATOM   1543  O   LEU A 361     -29.357  21.190 -11.191  1.00 35.23           O  
ANISOU 1543  O   LEU A 361     4650   4569   4167   -159    289   -332       O  
ATOM   1544  CB  LEU A 361     -28.812  19.967  -8.461  1.00 31.03           C  
ANISOU 1544  CB  LEU A 361     4014   4114   3660    -76    274   -292       C  
ATOM   1545  CG  LEU A 361     -29.085  19.394  -7.077  1.00 35.28           C  
ANISOU 1545  CG  LEU A 361     4513   4685   4208    -44    255   -259       C  
ATOM   1546  CD1 LEU A 361     -28.222  18.166  -6.849  1.00 37.69           C  
ANISOU 1546  CD1 LEU A 361     4809   4986   4525     -5    268   -254       C  
ATOM   1547  CD2 LEU A 361     -28.789  20.444  -6.002  1.00 37.00           C  
ANISOU 1547  CD2 LEU A 361     4676   4963   4420    -36    253   -267       C  
ATOM   1548  N   LYS A 362     -28.910  23.038  -9.989  1.00 37.91           N  
ANISOU 1548  N   LYS A 362     4916   4988   4502   -153    297   -354       N  
ATOM   1549  CA  LYS A 362     -28.585  23.846 -11.139  1.00 39.71           C  
ANISOU 1549  CA  LYS A 362     5179   5194   4717   -183    320   -387       C  
ATOM   1550  C   LYS A 362     -27.118  24.280 -11.071  1.00 39.62           C  
ANISOU 1550  C   LYS A 362     5137   5209   4706   -169    357   -431       C  
ATOM   1551  O   LYS A 362     -26.512  24.265  -9.990  1.00 43.68           O  
ANISOU 1551  O   LYS A 362     5596   5770   5228   -141    360   -433       O  
ATOM   1552  CB  LYS A 362     -29.438  25.117 -11.102  1.00 45.23           C  
ANISOU 1552  CB  LYS A 362     5877   5903   5406   -209    308   -381       C  
ATOM   1553  CG  LYS A 362     -30.932  24.908 -11.140  1.00 51.54           C  
ANISOU 1553  CG  LYS A 362     6698   6679   6206   -225    270   -339       C  
ATOM   1554  CD  LYS A 362     -31.368  24.392 -12.499  1.00 52.31           C  
ANISOU 1554  CD  LYS A 362     6861   6719   6295   -251    262   -335       C  
ATOM   1555  CE  LYS A 362     -32.887  24.513 -12.663  1.00 55.10           C  
ANISOU 1555  CE  LYS A 362     7234   7052   6648   -274    224   -297       C  
ATOM   1556  NZ  LYS A 362     -33.372  23.787 -13.876  1.00 52.39           N  
ANISOU 1556  NZ  LYS A 362     6953   6656   6297   -299    210   -289       N  
ATOM   1557  N   ASP A 363     -26.584  24.608 -12.247  1.00 37.31           N  
ANISOU 1557  N   ASP A 363     4884   4886   4406   -191    385   -464       N  
ATOM   1558  CA  ASP A 363     -25.384  25.408 -12.488  1.00 53.13           C  
ANISOU 1558  CA  ASP A 363     6873   6908   6408   -193    425   -512       C  
ATOM   1559  C   ASP A 363     -24.236  24.651 -13.125  1.00 53.48           C  
ANISOU 1559  C   ASP A 363     6930   6928   6462   -181    457   -540       C  
ATOM   1560  O   ASP A 363     -23.758  25.059 -14.189  1.00 60.55           O  
ANISOU 1560  O   ASP A 363     7863   7792   7349   -203    488   -574       O  
ATOM   1561  CB  ASP A 363     -24.941  26.254 -11.286  1.00 52.57           C  
ANISOU 1561  CB  ASP A 363     6735   6902   6339   -178    429   -524       C  
ATOM   1562  CG  ASP A 363     -25.555  27.611 -11.300  1.00 63.50           C  
ANISOU 1562  CG  ASP A 363     8123   8297   7709   -206    429   -529       C  
ATOM   1563  OD1 ASP A 363     -26.781  27.692 -11.493  1.00 68.01           O  
ANISOU 1563  OD1 ASP A 363     8721   8845   8273   -223    402   -497       O  
ATOM   1564  OD2 ASP A 363     -24.819  28.609 -11.143  1.00 71.40           O  
ANISOU 1564  OD2 ASP A 363     9097   9327   8704   -212    458   -564       O  
TER    1565      ASP A 363                                                      
ATOM   1566  N   GLU B 172       2.731  44.236  33.948  1.00 64.24           N  
ATOM   1567  CA  GLU B 172       2.841  42.855  33.487  1.00 75.37           C  
ATOM   1568  C   GLU B 172       3.752  42.117  34.444  1.00 75.04           C  
ATOM   1569  O   GLU B 172       3.487  40.987  34.868  1.00 78.76           O  
ATOM   1570  CB  GLU B 172       3.445  42.791  32.081  1.00 89.30           C  
ATOM   1571  CG  GLU B 172       2.654  43.512  30.996  1.00103.03           C  
ATOM   1572  CD  GLU B 172       2.892  45.013  30.984  1.00111.41           C  
ATOM   1573  OE1 GLU B 172       4.016  45.444  31.340  1.00110.12           O  
ATOM   1574  OE2 GLU B 172       1.951  45.755  30.618  1.00115.68           O  
ATOM   1575  N   LEU B 173       4.850  42.783  34.760  1.00 74.29           N  
ATOM   1576  CA  LEU B 173       5.834  42.286  35.701  1.00 75.40           C  
ATOM   1577  C   LEU B 173       5.352  42.459  37.147  1.00 64.43           C  
ATOM   1578  O   LEU B 173       5.491  41.549  37.968  1.00 57.68           O  
ATOM   1579  CB  LEU B 173       7.145  43.029  35.460  1.00 86.93           C  
ATOM   1580  CG  LEU B 173       6.978  44.332  34.666  1.00 94.22           C  
ATOM   1581  CD1 LEU B 173       6.575  45.477  35.583  1.00 95.83           C  
ATOM   1582  CD2 LEU B 173       8.238  44.678  33.875  1.00 97.66           C  
ATOM   1583  N   ASP B 174       4.792  43.629  37.442  1.00 67.05           N  
ATOM   1584  CA  ASP B 174       4.119  43.888  38.711  1.00 68.61           C  
ATOM   1585  C   ASP B 174       3.184  42.732  39.066  1.00 63.84           C  
ATOM   1586  O   ASP B 174       3.337  42.087  40.109  1.00 58.11           O  
ATOM   1587  CB  ASP B 174       3.288  45.180  38.610  1.00 77.28           C  
ATOM   1588  CG  ASP B 174       4.022  46.406  39.137  1.00 82.70           C  
ATOM   1589  OD1 ASP B 174       5.024  46.224  39.861  1.00 84.31           O  
ATOM   1590  OD2 ASP B 174       3.578  47.551  38.851  1.00 82.68           O  
ATOM   1591  N   SER B 175       2.218  42.451  38.189  1.00 62.07           N  
ATOM   1592  CA  SER B 175       1.190  41.461  38.530  1.00 60.95           C  
ATOM   1593  C   SER B 175       1.788  40.075  38.599  1.00 54.96           C  
ATOM   1594  O   SER B 175       1.357  39.252  39.414  1.00 54.94           O  
ATOM   1595  CB  SER B 175      -0.008  41.500  37.575  1.00 63.67           C  
ATOM   1596  OG  SER B 175       0.345  41.059  36.281  1.00 65.20           O  
ATOM   1597  N   LEU B 176       2.792  39.825  37.755  1.00 59.88           N  
ATOM   1598  CA  LEU B 176       3.535  38.563  37.827  1.00 71.33           C  
ATOM   1599  C   LEU B 176       4.347  38.402  39.129  1.00 72.12           C  
ATOM   1600  O   LEU B 176       4.668  37.286  39.511  1.00 74.27           O  
ATOM   1601  CB  LEU B 176       4.443  38.360  36.608  1.00 78.71           C  
ATOM   1602  CG  LEU B 176       4.683  36.862  36.371  1.00 81.11           C  
ATOM   1603  CD1 LEU B 176       3.602  36.280  35.454  1.00 81.09           C  
ATOM   1604  CD2 LEU B 176       6.094  36.555  35.872  1.00 79.05           C  
ATOM   1605  N   LEU B 177       4.702  39.498  39.800  1.00 68.00           N  
ATOM   1606  CA  LEU B 177       5.251  39.363  41.155  1.00 71.13           C  
ATOM   1607  C   LEU B 177       4.113  39.298  42.179  1.00 67.02           C  
ATOM   1608  O   LEU B 177       4.142  38.498  43.124  1.00 61.49           O  
ATOM   1609  CB  LEU B 177       6.277  40.463  41.493  1.00 76.86           C  
ATOM   1610  CG  LEU B 177       6.023  41.981  41.508  1.00 82.05           C  
ATOM   1611  CD1 LEU B 177       5.168  42.431  42.695  1.00 82.92           C  
ATOM   1612  CD2 LEU B 177       7.345  42.763  41.493  1.00 85.91           C  
ATOM   1613  N   GLY B 178       3.091  40.121  41.947  1.00 65.87           N  
ATOM   1614  CA  GLY B 178       1.952  40.236  42.841  1.00 64.77           C  
ATOM   1615  C   GLY B 178       1.148  38.965  43.024  1.00 60.40           C  
ATOM   1616  O   GLY B 178       0.752  38.637  44.139  1.00 60.87           O  
ATOM   1617  N   GLN B 179       0.906  38.254  41.930  1.00 59.40           N  
ATOM   1618  CA  GLN B 179       0.095  37.040  41.959  1.00 69.83           C  
ATOM   1619  C   GLN B 179       0.713  35.992  42.906  1.00 76.10           C  
ATOM   1620  O   GLN B 179       0.402  34.795  42.858  1.00 80.33           O  
ATOM   1621  CB  GLN B 179      -0.067  36.507  40.526  1.00 67.71           C  
ATOM   1622  CG  GLN B 179       0.872  35.353  40.076  1.00 90.39           C  
ATOM   1623  CD  GLN B 179       2.365  35.660  40.167  1.00 90.24           C  
ATOM   1624  OE1 GLN B 179       2.821  36.391  41.048  1.00 86.40           O  
ATOM   1625  NE2 GLN B 179       3.139  35.078  39.251  1.00 90.54           N  
ATOM   1626  N   GLU B 182       1.503  29.998  39.520  1.00 86.40           N  
ATOM   1627  CA  GLU B 182       0.938  28.885  38.763  1.00 83.11           C  
ATOM   1628  C   GLU B 182      -0.557  28.721  39.065  1.00 73.25           C  
ATOM   1629  O   GLU B 182      -1.295  28.099  38.302  1.00 78.06           O  
ATOM   1630  CB  GLU B 182       1.734  27.591  38.998  1.00 89.25           C  
ATOM   1631  CG  GLU B 182       2.027  27.237  40.467  1.00 96.76           C  
ATOM   1632  CD  GLU B 182       3.027  28.176  41.145  1.00 98.75           C  
ATOM   1633  OE1 GLU B 182       4.236  27.860  41.180  1.00 99.17           O  
ATOM   1634  OE2 GLU B 182       2.595  29.233  41.652  1.00 98.80           O  
ATOM   1635  N   ARG B 183      -0.991  29.303  40.180  1.00 86.61           N  
ANISOU 1635  N   ARG B 183    10518  11351  11037    316  -1004   -761       N  
ATOM   1636  CA  ARG B 183      -2.408  29.478  40.483  1.00 74.89           C  
ANISOU 1636  CA  ARG B 183     9036   9971   9448    302  -1004   -742       C  
ATOM   1637  C   ARG B 183      -3.041  30.387  39.429  1.00 64.92           C  
ANISOU 1637  C   ARG B 183     7747   8700   8218    296   -951   -720       C  
ATOM   1638  O   ARG B 183      -4.214  30.235  39.090  1.00 66.19           O  
ANISOU 1638  O   ARG B 183     7929   8929   8291    265   -927   -676       O  
ATOM   1639  CB  ARG B 183      -2.549  30.151  41.849  1.00 74.04           C  
ANISOU 1639  CB  ARG B 183     8884   9918   9331    347  -1058   -809       C  
ATOM   1640  CG  ARG B 183      -3.499  29.500  42.826  1.00 72.98           C  
ANISOU 1640  CG  ARG B 183     8775   9897   9057    331  -1093   -796       C  
ATOM   1641  CD  ARG B 183      -3.269  30.113  44.198  1.00 76.15           C  
ANISOU 1641  CD  ARG B 183     9129  10336   9470    385  -1151   -872       C  
ATOM   1642  NE  ARG B 183      -4.295  29.760  45.171  1.00 76.63           N  
ANISOU 1642  NE  ARG B 183     9198  10519   9398    377  -1183   -866       N  
ATOM   1643  CZ  ARG B 183      -4.516  30.438  46.295  1.00 82.16           C  
ANISOU 1643  CZ  ARG B 183     9852  11283  10083    422  -1227   -927       C  
ATOM   1644  NH1 ARG B 183      -3.784  31.516  46.587  1.00 80.94           N  
ANISOU 1644  NH1 ARG B 183     9640  11075  10040    479  -1245  -1001       N  
ATOM   1645  NH2 ARG B 183      -5.481  30.044  47.121  1.00 82.43           N  
ANISOU 1645  NH2 ARG B 183     9895  11435   9989    411  -1252   -915       N  
ATOM   1646  N   PHE B 184      -2.259  31.348  38.939  1.00 53.41           N  
ANISOU 1646  N   PHE B 184     6242   7161   6890    327   -934   -750       N  
ATOM   1647  CA  PHE B 184      -2.736  32.361  38.007  1.00 50.37           C  
ANISOU 1647  CA  PHE B 184     5823   6762   6554    328   -889   -735       C  
ATOM   1648  C   PHE B 184      -1.875  32.379  36.750  1.00 52.15           C  
ANISOU 1648  C   PHE B 184     6049   6890   6875    317   -842   -706       C  
ATOM   1649  O   PHE B 184      -0.705  32.018  36.805  1.00 48.80           O  
ANISOU 1649  O   PHE B 184     5628   6399   6515    328   -854   -723       O  
ATOM   1650  CB  PHE B 184      -2.671  33.745  38.652  1.00 44.14           C  
ANISOU 1650  CB  PHE B 184     4962   5969   5840    382   -918   -803       C  
ATOM   1651  CG  PHE B 184      -3.514  33.881  39.886  1.00 50.66           C  
ANISOU 1651  CG  PHE B 184     5777   6893   6577    400   -964   -839       C  
ATOM   1652  CD1 PHE B 184      -4.894  34.042  39.787  1.00 45.96           C  
ANISOU 1652  CD1 PHE B 184     5187   6386   5888    381   -949   -812       C  
ATOM   1653  CD2 PHE B 184      -2.930  33.877  41.147  1.00 54.41           C  
ANISOU 1653  CD2 PHE B 184     6234   7378   7062    438  -1024   -901       C  
ATOM   1654  CE1 PHE B 184      -5.680  34.181  40.930  1.00 45.94           C  
ANISOU 1654  CE1 PHE B 184     5171   6482   5801    400   -992   -845       C  
ATOM   1655  CE2 PHE B 184      -3.706  34.004  42.292  1.00 50.77           C  
ANISOU 1655  CE2 PHE B 184     5760   7016   6516    457  -1067   -935       C  
ATOM   1656  CZ  PHE B 184      -5.084  34.159  42.183  1.00 48.10           C  
ANISOU 1656  CZ  PHE B 184     5427   6768   6083    438  -1050   -907       C  
ATOM   1657  N   GLN B 185      -2.445  32.805  35.623  1.00 42.76           N  
ANISOU 1657  N   GLN B 185     4854   5697   5696    297   -789   -662       N  
ATOM   1658  CA  GLN B 185      -1.650  33.054  34.433  1.00 41.59           C  
ANISOU 1658  CA  GLN B 185     4693   5462   5648    293   -744   -638       C  
ATOM   1659  C   GLN B 185      -1.926  34.479  33.975  1.00 47.78           C  
ANISOU 1659  C   GLN B 185     5415   6227   6511    314   -722   -648       C  
ATOM   1660  O   GLN B 185      -3.086  34.883  33.892  1.00 51.51           O  
ANISOU 1660  O   GLN B 185     5883   6762   6925    305   -711   -632       O  
ATOM   1661  CB  GLN B 185      -2.005  32.069  33.322  1.00 46.27           C  
ANISOU 1661  CB  GLN B 185     5343   6063   6176    242   -695   -565       C  
ATOM   1662  CG  GLN B 185      -2.110  30.608  33.755  1.00 49.63           C  
ANISOU 1662  CG  GLN B 185     5836   6524   6497    213   -717   -546       C  
ATOM   1663  CD  GLN B 185      -2.329  29.682  32.574  1.00 51.03           C  
ANISOU 1663  CD  GLN B 185     6066   6697   6628    167   -670   -479       C  
ATOM   1664  OE1 GLN B 185      -1.761  29.880  31.507  1.00 62.55           O  
ANISOU 1664  OE1 GLN B 185     7513   8095   8159    165   -628   -458       O  
ATOM   1665  NE2 GLN B 185      -3.149  28.667  32.763  1.00 52.02           N  
ANISOU 1665  NE2 GLN B 185     6246   6886   6632    131   -679   -444       N  
ATOM   1666  N   VAL B 186      -0.871  35.241  33.699  1.00 38.21           N  
ANISOU 1666  N   VAL B 186     4154   4930   5433    343   -719   -673       N  
ATOM   1667  CA  VAL B 186      -1.012  36.587  33.185  1.00 42.51           C  
ANISOU 1667  CA  VAL B 186     4638   5445   6068    362   -700   -678       C  
ATOM   1668  C   VAL B 186      -0.812  36.601  31.673  1.00 49.14           C  
ANISOU 1668  C   VAL B 186     5481   6238   6951    334   -635   -614       C  
ATOM   1669  O   VAL B 186       0.309  36.397  31.203  1.00 52.96           O  
ANISOU 1669  O   VAL B 186     5960   6652   7512    336   -621   -609       O  
ATOM   1670  CB  VAL B 186       0.029  37.519  33.837  1.00 51.10           C  
ANISOU 1670  CB  VAL B 186     5664   6467   7286    412   -741   -745       C  
ATOM   1671  CG1 VAL B 186       0.024  38.872  33.150  1.00 53.55           C  
ANISOU 1671  CG1 VAL B 186     5911   6731   7705    428   -719   -741       C  
ATOM   1672  CG2 VAL B 186      -0.234  37.648  35.357  1.00 49.14           C  
ANISOU 1672  CG2 VAL B 186     5405   6271   6996    446   -808   -813       C  
ATOM   1673  N   LEU B 187      -1.893  36.858  30.924  1.00 40.63           N  
ANISOU 1673  N   LEU B 187     4410   5204   5825    309   -595   -569       N  
ATOM   1674  CA  LEU B 187      -1.949  36.684  29.463  1.00 35.64           C  
ANISOU 1674  CA  LEU B 187     3792   4550   5201    276   -530   -500       C  
ATOM   1675  C   LEU B 187      -2.269  38.008  28.769  1.00 40.66           C  
ANISOU 1675  C   LEU B 187     4370   5164   5916    285   -503   -486       C  
ATOM   1676  O   LEU B 187      -3.393  38.493  28.866  1.00 40.46           O  
ANISOU 1676  O   LEU B 187     4338   5195   5841    283   -502   -482       O  
ATOM   1677  CB  LEU B 187      -3.089  35.703  29.137  1.00 32.82           C  
ANISOU 1677  CB  LEU B 187     3499   4270   4700    232   -506   -450       C  
ATOM   1678  CG  LEU B 187      -2.931  34.356  29.858  1.00 36.01           C  
ANISOU 1678  CG  LEU B 187     3963   4704   5016    218   -537   -459       C  
ATOM   1679  CD1 LEU B 187      -4.059  33.387  29.521  1.00 38.52           C  
ANISOU 1679  CD1 LEU B 187     4343   5095   5196    173   -516   -407       C  
ATOM   1680  CD2 LEU B 187      -1.623  33.730  29.443  1.00 36.48           C  
ANISOU 1680  CD2 LEU B 187     4034   4690   5136    218   -528   -454       C  
ATOM   1681  N   PRO B 188      -1.292  38.612  28.065  1.00 36.75           N  
ANISOU 1681  N   PRO B 188     3831   4588   5544    297   -481   -477       N  
ATOM   1682  CA  PRO B 188      -1.661  39.863  27.364  1.00 38.05           C  
ANISOU 1682  CA  PRO B 188     3941   4733   5782    302   -455   -457       C  
ATOM   1683  C   PRO B 188      -2.558  39.514  26.200  1.00 36.24           C  
ANISOU 1683  C   PRO B 188     3746   4546   5478    261   -395   -384       C  
ATOM   1684  O   PRO B 188      -2.303  38.487  25.565  1.00 34.69           O  
ANISOU 1684  O   PRO B 188     3595   4350   5234    233   -363   -345       O  
ATOM   1685  CB  PRO B 188      -0.330  40.393  26.814  1.00 37.50           C  
ANISOU 1685  CB  PRO B 188     3823   4570   5856    318   -443   -454       C  
ATOM   1686  CG  PRO B 188       0.588  39.164  26.764  1.00 44.81           C  
ANISOU 1686  CG  PRO B 188     4793   5475   6758    306   -437   -449       C  
ATOM   1687  CD  PRO B 188       0.142  38.278  27.927  1.00 41.22           C  
ANISOU 1687  CD  PRO B 188     4389   5080   6193    306   -482   -487       C  
ATOM   1688  N   GLY B 189      -3.562  40.344  25.934  1.00 33.69           N  
ANISOU 1688  N   GLY B 189     3399   4255   5145    259   -383   -370       N  
ATOM   1689  CA  GLY B 189      -4.520  40.128  24.856  1.00 33.27           C  
ANISOU 1689  CA  GLY B 189     3373   4246   5021    222   -328   -303       C  
ATOM   1690  C   GLY B 189      -4.352  41.069  23.677  1.00 35.52           C  
ANISOU 1690  C   GLY B 189     3610   4484   5401    219   -283   -259       C  
ATOM   1691  O   GLY B 189      -3.580  42.048  23.731  1.00 34.37           O  
ANISOU 1691  O   GLY B 189     3403   4272   5383    247   -298   -280       O  
ATOM   1692  N   ARG B 190      -5.057  40.774  22.591  1.00 39.39           N  
ANISOU 1692  N   ARG B 190     4127   5009   5831    185   -228   -194       N  
ATOM   1693  CA  ARG B 190      -4.938  41.586  21.366  1.00 40.09           C  
ANISOU 1693  CA  ARG B 190     4173   5060   6000    177   -181   -142       C  
ATOM   1694  C   ARG B 190      -5.468  43.013  21.544  1.00 44.64           C  
ANISOU 1694  C   ARG B 190     4689   5628   6643    199   -199   -158       C  
ATOM   1695  O   ARG B 190      -5.227  43.869  20.704  1.00 50.15           O  
ANISOU 1695  O   ARG B 190     5340   6283   7433    200   -171   -124       O  
ATOM   1696  CB  ARG B 190      -5.671  40.934  20.182  1.00 41.28           C  
ANISOU 1696  CB  ARG B 190     4367   5257   6060    136   -119    -71       C  
ATOM   1697  CG  ARG B 190      -4.979  39.706  19.611  1.00 46.34           C  
ANISOU 1697  CG  ARG B 190     5054   5889   6666    115    -90    -43       C  
ATOM   1698  CD  ARG B 190      -5.852  39.124  18.518  1.00 53.84           C  
ANISOU 1698  CD  ARG B 190     6045   6891   7520     78    -35     21       C  
ATOM   1699  NE  ARG B 190      -7.162  38.840  19.079  1.00 57.32           N  
ANISOU 1699  NE  ARG B 190     6525   7406   7847     65    -52     12       N  
ATOM   1700  CZ  ARG B 190      -7.466  37.688  19.658  1.00 46.97           C  
ANISOU 1700  CZ  ARG B 190     5275   6139   6431     50    -73     -1       C  
ATOM   1701  NH1 ARG B 190      -6.551  36.736  19.718  1.00 56.99           N  
ANISOU 1701  NH1 ARG B 190     6574   7381   7700     48    -79     -9       N  
ATOM   1702  NH2 ARG B 190      -8.660  37.492  20.180  1.00 42.09           N  
ANISOU 1702  NH2 ARG B 190     4687   5592   5712     38    -89     -7       N  
ATOM   1703  N   ASP B 191      -6.190  43.248  22.630  1.00 44.36           N  
ANISOU 1703  N   ASP B 191     4655   5635   6563    217   -246   -210       N  
ATOM   1704  CA  ASP B 191      -6.742  44.557  22.942  1.00 40.85           C  
ANISOU 1704  CA  ASP B 191     4157   5189   6176    243   -273   -236       C  
ATOM   1705  C   ASP B 191      -5.788  45.348  23.837  1.00 47.15           C  
ANISOU 1705  C   ASP B 191     4898   5920   7095    287   -329   -303       C  
ATOM   1706  O   ASP B 191      -6.165  46.412  24.355  1.00 50.17           O  
ANISOU 1706  O   ASP B 191     5235   6299   7530    316   -367   -342       O  
ATOM   1707  CB  ASP B 191      -8.094  44.386  23.665  1.00 39.59           C  
ANISOU 1707  CB  ASP B 191     4027   5119   5895    241   -296   -260       C  
ATOM   1708  CG  ASP B 191      -7.988  43.531  24.930  1.00 40.76           C  
ANISOU 1708  CG  ASP B 191     4213   5304   5968    252   -343   -315       C  
ATOM   1709  OD1 ASP B 191      -6.857  43.083  25.278  1.00 38.30           O  
ANISOU 1709  OD1 ASP B 191     3905   4946   5702    263   -360   -338       O  
ATOM   1710  OD2 ASP B 191      -9.036  43.303  25.589  1.00 36.11           O  
ANISOU 1710  OD2 ASP B 191     3650   4795   5276    251   -363   -335       O  
ATOM   1711  N   LYS B 192      -4.579  44.800  24.051  1.00 47.58           N  
ANISOU 1711  N   LYS B 192     4958   5927   7193    293   -339   -318       N  
ATOM   1712  CA  LYS B 192      -3.517  45.415  24.868  1.00 48.60           C  
ANISOU 1712  CA  LYS B 192     5037   5988   7439    334   -391   -380       C  
ATOM   1713  C   LYS B 192      -3.813  45.377  26.358  1.00 48.14           C  
ANISOU 1713  C   LYS B 192     4985   5968   7337    365   -457   -459       C  
ATOM   1714  O   LYS B 192      -3.097  45.986  27.179  1.00 51.67           O  
ANISOU 1714  O   LYS B 192     5388   6368   7876    404   -509   -520       O  
ATOM   1715  CB  LYS B 192      -3.176  46.850  24.395  1.00 46.37           C  
ANISOU 1715  CB  LYS B 192     4677   5636   7305    352   -393   -372       C  
ATOM   1716  CG  LYS B 192      -2.470  46.901  23.021  1.00 51.17           C  
ANISOU 1716  CG  LYS B 192     5268   6191   7984    327   -334   -299       C  
ATOM   1717  CD  LYS B 192      -2.024  48.317  22.655  1.00 62.76           C  
ANISOU 1717  CD  LYS B 192     6654   7585   9607    346   -343   -292       C  
ATOM   1718  CE  LYS B 192      -1.718  48.459  21.166  1.00 68.64           C  
ANISOU 1718  CE  LYS B 192     7381   8300  10398    315   -278   -205       C  
ATOM   1719  NZ  LYS B 192      -1.755  49.913  20.743  1.00 69.07           N  
ANISOU 1719  NZ  LYS B 192     7361   8303  10579    327   -285   -187       N  
ATOM   1720  N   MET B 193      -4.846  44.629  26.717  1.00 37.66           N  
ANISOU 1720  N   MET B 193     3712   4728   5868    348   -456   -458       N  
ATOM   1721  CA  MET B 193      -5.180  44.434  28.124  1.00 40.42           C  
ANISOU 1721  CA  MET B 193     4073   5129   6157    374   -515   -527       C  
ATOM   1722  C   MET B 193      -4.449  43.227  28.668  1.00 39.08           C  
ANISOU 1722  C   MET B 193     3949   4960   5939    368   -529   -542       C  
ATOM   1723  O   MET B 193      -4.052  42.373  27.903  1.00 40.92           O  
ANISOU 1723  O   MET B 193     4220   5178   6148    337   -487   -493       O  
ATOM   1724  CB  MET B 193      -6.691  44.217  28.262  1.00 42.55           C  
ANISOU 1724  CB  MET B 193     4376   5498   6293    358   -509   -515       C  
ATOM   1725  CG  MET B 193      -7.260  44.432  29.655  1.00 55.95           C  
ANISOU 1725  CG  MET B 193     6065   7255   7939    391   -571   -587       C  
ATOM   1726  SD  MET B 193      -7.445  46.171  30.168  1.00 75.60           S  
ANISOU 1726  SD  MET B 193     8468   9716  10541    445   -620   -651       S  
ATOM   1727  CE  MET B 193      -7.022  47.084  28.701  1.00 42.79           C  
ANISOU 1727  CE  MET B 193     4269   5472   6519    432   -572   -592       C  
ATOM   1728  N   LEU B 194      -4.278  43.159  29.986  1.00 42.43           N  
ANISOU 1728  N   LEU B 194     4369   5403   6348    400   -589   -612       N  
ATOM   1729  CA  LEU B 194      -3.741  41.966  30.617  1.00 42.71           C  
ANISOU 1729  CA  LEU B 194     4453   5452   6323    394   -607   -627       C  
ATOM   1730  C   LEU B 194      -4.813  41.125  31.279  1.00 43.60           C  
ANISOU 1730  C   LEU B 194     4619   5667   6279    377   -620   -629       C  
ATOM   1731  O   LEU B 194      -5.511  41.597  32.181  1.00 46.62           O  
ANISOU 1731  O   LEU B 194     4983   6105   6627    402   -661   -675       O  
ATOM   1732  CB  LEU B 194      -2.700  42.350  31.679  1.00 56.54           C  
ANISOU 1732  CB  LEU B 194     6166   7154   8163    440   -667   -703       C  
ATOM   1733  CG  LEU B 194      -1.342  42.872  31.216  1.00 56.63           C  
ANISOU 1733  CG  LEU B 194     6133   7059   8326    455   -662   -706       C  
ATOM   1734  CD1 LEU B 194      -0.584  43.280  32.433  1.00 55.86           C  
ANISOU 1734  CD1 LEU B 194     5998   6930   8296    503   -728   -787       C  
ATOM   1735  CD2 LEU B 194      -0.551  41.810  30.466  1.00 53.05           C  
ANISOU 1735  CD2 LEU B 194     5721   6572   7863    423   -620   -657       C  
ATOM   1736  N   TYR B 195      -4.915  39.857  30.871  1.00 36.66           N  
ANISOU 1736  N   TYR B 195     3805   4815   5308    337   -590   -581       N  
ATOM   1737  CA  TYR B 195      -5.893  38.965  31.467  1.00 36.97           C  
ANISOU 1737  CA  TYR B 195     3897   4951   5200    316   -603   -575       C  
ATOM   1738  C   TYR B 195      -5.292  38.049  32.519  1.00 36.90           C  
ANISOU 1738  C   TYR B 195     3917   4951   5151    324   -647   -611       C  
ATOM   1739  O   TYR B 195      -4.266  37.425  32.278  1.00 42.31           O  
ANISOU 1739  O   TYR B 195     4622   5580   5876    317   -641   -602       O  
ATOM   1740  CB  TYR B 195      -6.575  38.144  30.342  1.00 29.70           C  
ANISOU 1740  CB  TYR B 195     3030   4061   4193    263   -544   -495       C  
ATOM   1741  CG  TYR B 195      -7.407  39.072  29.478  1.00 30.42           C  
ANISOU 1741  CG  TYR B 195     3093   4162   4303    256   -506   -463       C  
ATOM   1742  CD1 TYR B 195      -8.728  39.343  29.812  1.00 31.74           C  
ANISOU 1742  CD1 TYR B 195     3261   4413   4384    253   -514   -466       C  
ATOM   1743  CD2 TYR B 195      -6.872  39.678  28.358  1.00 30.15           C  
ANISOU 1743  CD2 TYR B 195     3028   4058   4371    254   -465   -431       C  
ATOM   1744  CE1 TYR B 195      -9.491  40.206  29.040  1.00 34.24           C  
ANISOU 1744  CE1 TYR B 195     3552   4739   4720    248   -482   -438       C  
ATOM   1745  CE2 TYR B 195      -7.630  40.548  27.580  1.00 26.89           C  
ANISOU 1745  CE2 TYR B 195     2587   3653   3977    248   -433   -401       C  
ATOM   1746  CZ  TYR B 195      -8.937  40.801  27.945  1.00 34.23           C  
ANISOU 1746  CZ  TYR B 195     3521   4663   4822    246   -442   -406       C  
ATOM   1747  OH  TYR B 195      -9.711  41.653  27.190  1.00 40.65           O  
ANISOU 1747  OH  TYR B 195     4307   5486   5652    241   -412   -377       O  
ATOM   1748  N   VAL B 196      -5.956  37.937  33.665  1.00 34.22           N  
ANISOU 1748  N   VAL B 196     3584   4689   4730    338   -692   -649       N  
ATOM   1749  CA  VAL B 196      -5.460  37.071  34.704  1.00 41.38           C  
ANISOU 1749  CA  VAL B 196     4518   5613   5592    345   -736   -680       C  
ATOM   1750  C   VAL B 196      -6.398  35.901  34.839  1.00 39.20           C  
ANISOU 1750  C   VAL B 196     4306   5424   5164    303   -730   -637       C  
ATOM   1751  O   VAL B 196      -7.534  36.044  35.292  1.00 38.46           O  
ANISOU 1751  O   VAL B 196     4214   5417   4983    300   -741   -640       O  
ATOM   1752  CB  VAL B 196      -5.320  37.790  36.080  1.00 40.62           C  
ANISOU 1752  CB  VAL B 196     4375   5536   5523    398   -801   -763       C  
ATOM   1753  CG1 VAL B 196      -4.860  36.787  37.144  1.00 41.29           C  
ANISOU 1753  CG1 VAL B 196     4493   5646   5548    401   -845   -789       C  
ATOM   1754  CG2 VAL B 196      -4.360  38.949  35.977  1.00 46.48           C  
ANISOU 1754  CG2 VAL B 196     5052   6187   6421    440   -813   -807       C  
ATOM   1755  N   ALA B 197      -5.931  34.734  34.422  1.00 39.68           N  
ANISOU 1755  N   ALA B 197     4421   5462   5194    269   -712   -597       N  
ATOM   1756  CA  ALA B 197      -6.786  33.554  34.398  1.00 38.87           C  
ANISOU 1756  CA  ALA B 197     4383   5433   4954    224   -704   -548       C  
ATOM   1757  C   ALA B 197      -6.745  32.875  35.748  1.00 44.68           C  
ANISOU 1757  C   ALA B 197     5137   6219   5618    232   -762   -581       C  
ATOM   1758  O   ALA B 197      -5.669  32.506  36.244  1.00 43.79           O  
ANISOU 1758  O   ALA B 197     5028   6059   5553    249   -791   -611       O  
ATOM   1759  CB  ALA B 197      -6.348  32.587  33.301  1.00 42.20           C  
ANISOU 1759  CB  ALA B 197     4854   5807   5374    184   -662   -489       C  
ATOM   1760  N   ALA B 198      -7.924  32.710  36.335  1.00 37.22           N  
ANISOU 1760  N   ALA B 198     4205   5376   4561    220   -777   -574       N  
ATOM   1761  CA  ALA B 198      -8.058  32.147  37.662  1.00 35.96           C  
ANISOU 1761  CA  ALA B 198     4059   5282   4322    228   -832   -602       C  
ATOM   1762  C   ALA B 198      -8.805  30.845  37.538  1.00 42.08           C  
ANISOU 1762  C   ALA B 198     4900   6120   4969    174   -824   -538       C  
ATOM   1763  O   ALA B 198      -9.625  30.670  36.607  1.00 42.62           O  
ANISOU 1763  O   ALA B 198     4993   6210   4990    137   -780   -482       O  
ATOM   1764  CB  ALA B 198      -8.832  33.132  38.538  1.00 42.97           C  
ANISOU 1764  CB  ALA B 198     4897   6245   5186    264   -862   -650       C  
ATOM   1765  N   GLN B 199      -8.580  29.923  38.471  1.00 39.70           N  
ANISOU 1765  N   GLN B 199     4629   5850   4607    167   -868   -544       N  
ATOM   1766  CA  GLN B 199      -9.156  28.594  38.336  1.00 47.99           C  
ANISOU 1766  CA  GLN B 199     5744   6947   5544    113   -864   -480       C  
ATOM   1767  C   GLN B 199     -10.510  28.434  39.016  1.00 43.77           C  
ANISOU 1767  C   GLN B 199     5216   6536   4879     96   -882   -462       C  
ATOM   1768  O   GLN B 199     -11.241  27.505  38.716  1.00 47.98           O  
ANISOU 1768  O   GLN B 199     5798   7114   5317     47   -870   -401       O  
ATOM   1769  CB  GLN B 199      -8.189  27.569  38.921  1.00 59.34           C  
ANISOU 1769  CB  GLN B 199     7214   8349   6982    109   -903   -486       C  
ATOM   1770  CG  GLN B 199      -6.743  27.757  38.485  1.00 68.08           C  
ANISOU 1770  CG  GLN B 199     8309   9340   8220    135   -895   -516       C  
ATOM   1771  CD  GLN B 199      -5.820  26.717  39.104  1.00 74.02           C  
ANISOU 1771  CD  GLN B 199     9094  10062   8969    132   -936   -523       C  
ATOM   1772  OE1 GLN B 199      -5.262  26.930  40.178  1.00 73.89           O  
ANISOU 1772  OE1 GLN B 199     9052  10048   8975    168   -983   -577       O  
ATOM   1773  NE2 GLN B 199      -5.667  25.581  38.430  1.00 74.60           N  
ANISOU 1773  NE2 GLN B 199     9224  10105   9013     89   -920   -471       N  
ATOM   1774  N   ASN B 200     -10.815  29.308  39.969  1.00 46.71           N  
ANISOU 1774  N   ASN B 200     5538   6965   5247    137   -913   -517       N  
ATOM   1775  CA  ASN B 200     -12.097  29.261  40.675  1.00 50.01           C  
ANISOU 1775  CA  ASN B 200     5952   7507   5541    127   -931   -506       C  
ATOM   1776  C   ASN B 200     -12.496  30.624  41.228  1.00 53.67           C  
ANISOU 1776  C   ASN B 200     6348   8013   6030    178   -945   -569       C  
ATOM   1777  O   ASN B 200     -11.779  31.613  41.038  1.00 48.74           O  
ANISOU 1777  O   ASN B 200     5679   7316   5524    221   -942   -619       O  
ATOM   1778  CB  ASN B 200     -12.084  28.209  41.782  1.00 52.45           C  
ANISOU 1778  CB  ASN B 200     6291   7877   5760    112   -981   -498       C  
ATOM   1779  CG  ASN B 200     -11.027  28.490  42.846  1.00 55.76           C  
ANISOU 1779  CG  ASN B 200     6678   8269   6240    163  -1031   -569       C  
ATOM   1780  OD1 ASN B 200     -10.729  29.656  43.192  1.00 50.88           O  
ANISOU 1780  OD1 ASN B 200     6001   7636   5696    217  -1043   -636       O  
ATOM   1781  ND2 ASN B 200     -10.444  27.427  43.358  1.00 56.35           N  
ANISOU 1781  ND2 ASN B 200     6790   8335   6287    146  -1063   -554       N  
ATOM   1782  N   GLU B 201     -13.640  30.677  41.906  1.00 57.92           N  
ANISOU 1782  N   GLU B 201     6877   8670   6461    175   -963   -567       N  
ATOM   1783  CA  GLU B 201     -14.223  31.956  42.294  1.00 61.18           C  
ANISOU 1783  CA  GLU B 201     7227   9132   6886    221   -972   -621       C  
ATOM   1784  C   GLU B 201     -13.403  32.586  43.423  1.00 56.10           C  
ANISOU 1784  C   GLU B 201     6534   8478   6304    284  -1025   -707       C  
ATOM   1785  O   GLU B 201     -13.202  33.806  43.442  1.00 52.48           O  
ANISOU 1785  O   GLU B 201     6019   7988   5932    332  -1030   -766       O  
ATOM   1786  CB  GLU B 201     -15.694  31.781  42.684  1.00 62.74           C  
ANISOU 1786  CB  GLU B 201     7429   9465   6943    199   -975   -592       C  
ATOM   1787  CG  GLU B 201     -16.561  31.114  41.602  1.00 72.40           C  
ANISOU 1787  CG  GLU B 201     8703  10705   8101    135   -924   -506       C  
ATOM   1788  CD  GLU B 201     -17.015  32.075  40.503  1.00 77.16           C  
ANISOU 1788  CD  GLU B 201     9283  11274   8759    139   -875   -501       C  
ATOM   1789  OE1 GLU B 201     -16.712  33.283  40.594  1.00 83.67           O  
ANISOU 1789  OE1 GLU B 201    10052  12065   9673    191   -882   -563       O  
ATOM   1790  OE2 GLU B 201     -17.686  31.624  39.546  1.00 75.35           O  
ANISOU 1790  OE2 GLU B 201     9092  11052   8485     91   -832   -435       O  
ATOM   1791  N   ARG B 202     -12.923  31.732  44.332  1.00 57.29           N  
ANISOU 1791  N   ARG B 202     6706   8651   6411    281  -1066   -711       N  
ATOM   1792  CA  ARG B 202     -12.068  32.135  45.445  1.00 63.71           C  
ANISOU 1792  CA  ARG B 202     7478   9454   7274    337  -1120   -789       C  
ATOM   1793  C   ARG B 202     -10.877  32.929  44.930  1.00 59.31           C  
ANISOU 1793  C   ARG B 202     6891   8766   6877    373  -1111   -834       C  
ATOM   1794  O   ARG B 202     -10.671  34.077  45.312  1.00 53.84           O  
ANISOU 1794  O   ARG B 202     6139   8061   6257    428  -1132   -904       O  
ATOM   1795  CB  ARG B 202     -11.548  30.902  46.202  1.00 78.09           C  
ANISOU 1795  CB  ARG B 202     9341  11292   9039    317  -1156   -770       C  
ATOM   1796  CG  ARG B 202     -12.604  29.862  46.542  1.00 90.44           C  
ANISOU 1796  CG  ARG B 202    10946  12968  10448    267  -1161   -706       C  
ATOM   1797  CD  ARG B 202     -12.023  28.754  47.425  1.00 98.78           C  
ANISOU 1797  CD  ARG B 202    12034  14040  11457    255  -1205   -695       C  
ATOM   1798  NE  ARG B 202     -11.588  29.264  48.726  1.00104.94           N  
ANISOU 1798  NE  ARG B 202    12765  14858  12248    313  -1261   -772       N  
ATOM   1799  CZ  ARG B 202     -12.366  29.335  49.805  1.00107.70           C  
ANISOU 1799  CZ  ARG B 202    13089  15337  12495    329  -1296   -789       C  
ATOM   1800  NH1 ARG B 202     -11.885  29.823  50.942  1.00109.08           N  
ANISOU 1800  NH1 ARG B 202    13218  15541  12687    386  -1346   -863       N  
ATOM   1801  NH2 ARG B 202     -13.628  28.924  49.748  1.00107.45           N  
ANISOU 1801  NH2 ARG B 202    13076  15410  12342    288  -1282   -731       N  
ATOM   1802  N   ASP B 203     -10.099  32.306  44.049  1.00 54.85           N  
ANISOU 1802  N   ASP B 203     6367   8105   6369    341  -1081   -793       N  
ATOM   1803  CA  ASP B 203      -8.897  32.930  43.508  1.00 48.18           C  
ANISOU 1803  CA  ASP B 203     5498   7135   5675    370  -1070   -827       C  
ATOM   1804  C   ASP B 203      -9.238  34.158  42.694  1.00 43.56           C  
ANISOU 1804  C   ASP B 203     4870   6516   5164    387  -1035   -838       C  
ATOM   1805  O   ASP B 203      -8.526  35.154  42.740  1.00 38.21           O  
ANISOU 1805  O   ASP B 203     4142   5772   4604    433  -1047   -895       O  
ATOM   1806  CB  ASP B 203      -8.080  31.911  42.694  1.00 54.50           C  
ANISOU 1806  CB  ASP B 203     6352   7849   6505    329  -1042   -774       C  
ATOM   1807  CG  ASP B 203      -7.487  30.809  43.573  1.00 58.75           C  
ANISOU 1807  CG  ASP B 203     6925   8399   6997    321  -1085   -775       C  
ATOM   1808  OD1 ASP B 203      -7.421  31.016  44.805  1.00 54.09           O  
ANISOU 1808  OD1 ASP B 203     6307   7862   6383    358  -1137   -828       O  
ATOM   1809  OD2 ASP B 203      -7.095  29.744  43.041  1.00 58.24           O  
ANISOU 1809  OD2 ASP B 203     6915   8293   6920    280  -1069   -724       O  
ATOM   1810  N   THR B 204     -10.356  34.099  41.968  1.00 39.30           N  
ANISOU 1810  N   THR B 204     4349   6026   4557    351   -995   -784       N  
ATOM   1811  CA  THR B 204     -10.804  35.264  41.224  1.00 39.35           C  
ANISOU 1811  CA  THR B 204     4316   6012   4625    366   -964   -792       C  
ATOM   1812  C   THR B 204     -11.071  36.448  42.162  1.00 44.61           C  
ANISOU 1812  C   THR B 204     4914   6721   5314    427  -1007   -873       C  
ATOM   1813  O   THR B 204     -10.687  37.583  41.880  1.00 38.15           O  
ANISOU 1813  O   THR B 204     4046   5840   4610    464  -1006   -914       O  
ATOM   1814  CB  THR B 204     -12.118  34.963  40.476  1.00 41.79           C  
ANISOU 1814  CB  THR B 204     4657   6387   4835    318   -920   -724       C  
ATOM   1815  OG1 THR B 204     -11.957  33.789  39.643  1.00 40.87           O  
ANISOU 1815  OG1 THR B 204     4605   6239   4686    261   -883   -650       O  
ATOM   1816  CG2 THR B 204     -12.530  36.167  39.659  1.00 42.49           C  
ANISOU 1816  CG2 THR B 204     4704   6447   4992    333   -887   -730       C  
ATOM   1817  N   LEU B 205     -11.783  36.198  43.254  1.00 48.18           N  
ANISOU 1817  N   LEU B 205     5363   7286   5656    436  -1045   -893       N  
ATOM   1818  CA  LEU B 205     -12.035  37.277  44.209  1.00 53.06           C  
ANISOU 1818  CA  LEU B 205     5916   7953   6290    498  -1091   -975       C  
ATOM   1819  C   LEU B 205     -10.687  37.840  44.750  1.00 50.47           C  
ANISOU 1819  C   LEU B 205     5548   7539   6089    551  -1131  -1049       C  
ATOM   1820  O   LEU B 205     -10.432  39.049  44.717  1.00 52.63           O  
ANISOU 1820  O   LEU B 205     5764   7766   6467    598  -1144  -1106       O  
ATOM   1821  CB  LEU B 205     -12.929  36.753  45.339  1.00 63.55           C  
ANISOU 1821  CB  LEU B 205     7251   9423   7470    497  -1126   -980       C  
ATOM   1822  CG  LEU B 205     -13.216  37.639  46.563  1.00 73.25           C  
ANISOU 1822  CG  LEU B 205     8417  10729   8687    562  -1182  -1068       C  
ATOM   1823  CD1 LEU B 205     -13.673  39.039  46.168  1.00 72.18           C  
ANISOU 1823  CD1 LEU B 205     8226  10579   8622    599  -1175  -1109       C  
ATOM   1824  CD2 LEU B 205     -14.238  36.964  47.492  1.00 72.65           C  
ANISOU 1824  CD2 LEU B 205     8355  10803   8446    548  -1206  -1052       C  
ATOM   1825  N   TRP B 206      -9.824  36.934  45.208  1.00 47.43           N  
ANISOU 1825  N   TRP B 206     5194   7129   5699    543  -1151  -1046       N  
ATOM   1826  CA  TRP B 206      -8.496  37.294  45.682  1.00 47.75           C  
ANISOU 1826  CA  TRP B 206     5203   7085   5854    587  -1187  -1108       C  
ATOM   1827  C   TRP B 206      -7.725  38.181  44.680  1.00 51.54           C  
ANISOU 1827  C   TRP B 206     5654   7437   6491    601  -1158  -1117       C  
ATOM   1828  O   TRP B 206      -7.290  39.292  45.013  1.00 44.76           O  
ANISOU 1828  O   TRP B 206     4735   6538   5733    655  -1188  -1187       O  
ATOM   1829  CB  TRP B 206      -7.721  36.012  45.997  1.00 49.27           C  
ANISOU 1829  CB  TRP B 206     5447   7259   6014    561  -1198  -1081       C  
ATOM   1830  CG  TRP B 206      -6.507  36.228  46.865  1.00 58.35           C  
ANISOU 1830  CG  TRP B 206     6568   8358   7246    610  -1249  -1153       C  
ATOM   1831  CD1 TRP B 206      -6.484  36.384  48.223  1.00 61.21           C  
ANISOU 1831  CD1 TRP B 206     6899   8788   7570    654  -1308  -1218       C  
ATOM   1832  CD2 TRP B 206      -5.144  36.306  46.429  1.00 63.81           C  
ANISOU 1832  CD2 TRP B 206     7255   8921   8068    619  -1243  -1166       C  
ATOM   1833  NE1 TRP B 206      -5.186  36.554  48.659  1.00 65.36           N  
ANISOU 1833  NE1 TRP B 206     7403   9233   8198    691  -1342  -1272       N  
ATOM   1834  CE2 TRP B 206      -4.346  36.511  47.576  1.00 63.53           C  
ANISOU 1834  CE2 TRP B 206     7187   8880   8071    670  -1302  -1241       C  
ATOM   1835  CE3 TRP B 206      -4.520  36.221  45.183  1.00 64.37           C  
ANISOU 1835  CE3 TRP B 206     7345   8886   8226    591  -1195  -1122       C  
ATOM   1836  CZ2 TRP B 206      -2.958  36.632  47.507  1.00 63.27           C  
ANISOU 1836  CZ2 TRP B 206     7141   8736   8162    692  -1314  -1272       C  
ATOM   1837  CZ3 TRP B 206      -3.134  36.350  45.120  1.00 60.98           C  
ANISOU 1837  CZ3 TRP B 206     6901   8350   7919    613  -1206  -1153       C  
ATOM   1838  CH2 TRP B 206      -2.374  36.551  46.272  1.00 58.86           C  
ANISOU 1838  CH2 TRP B 206     6601   8076   7687    662  -1265  -1226       C  
ATOM   1839  N   ALA B 207      -7.566  37.711  43.444  1.00 50.03           N  
ANISOU 1839  N   ALA B 207     5503   7184   6322    552  -1102  -1046       N  
ATOM   1840  CA  ALA B 207      -6.835  38.497  42.444  1.00 49.75           C  
ANISOU 1840  CA  ALA B 207     5440   7031   6431    561  -1072  -1046       C  
ATOM   1841  C   ALA B 207      -7.462  39.879  42.203  1.00 46.85           C  
ANISOU 1841  C   ALA B 207     5015   6669   6118    592  -1070  -1077       C  
ATOM   1842  O   ALA B 207      -6.746  40.911  42.068  1.00 44.71           O  
ANISOU 1842  O   ALA B 207     4691   6315   5983    631  -1083  -1122       O  
ATOM   1843  CB  ALA B 207      -6.696  37.711  41.134  1.00 46.79           C  
ANISOU 1843  CB  ALA B 207     5119   6606   6055    502  -1010   -961       C  
ATOM   1844  N   ARG B 208      -8.796  39.925  42.178  1.00 40.44           N  
ANISOU 1844  N   ARG B 208     4210   5953   5203    577  -1058  -1055       N  
ATOM   1845  CA  ARG B 208      -9.458  41.206  41.949  1.00 41.35           C  
ANISOU 1845  CA  ARG B 208     4273   6077   5363    606  -1057  -1083       C  
ATOM   1846  C   ARG B 208      -9.200  42.205  43.087  1.00 49.81           C  
ANISOU 1846  C   ARG B 208     5277   7157   6490    677  -1123  -1183       C  
ATOM   1847  O   ARG B 208      -8.970  43.391  42.834  1.00 50.46           O  
ANISOU 1847  O   ARG B 208     5305   7179   6689    712  -1132  -1222       O  
ATOM   1848  CB  ARG B 208     -10.959  41.023  41.703  1.00 45.77           C  
ANISOU 1848  CB  ARG B 208     4853   6741   5795    575  -1031  -1040       C  
ATOM   1849  CG  ARG B 208     -11.297  40.834  40.223  1.00 42.07           C  
ANISOU 1849  CG  ARG B 208     4418   6233   5334    522   -961   -957       C  
ATOM   1850  CD  ARG B 208     -12.685  40.225  40.026  1.00 41.65           C  
ANISOU 1850  CD  ARG B 208     4404   6288   5132    479   -934   -901       C  
ATOM   1851  NE  ARG B 208     -12.912  39.901  38.616  1.00 42.53           N  
ANISOU 1851  NE  ARG B 208     4554   6360   5248    428   -868   -821       N  
ATOM   1852  CZ  ARG B 208     -13.924  39.158  38.185  1.00 43.72           C  
ANISOU 1852  CZ  ARG B 208     4751   6581   5280    379   -834   -756       C  
ATOM   1853  NH1 ARG B 208     -14.046  38.900  36.885  1.00 38.98           N  
ANISOU 1853  NH1 ARG B 208     4181   5938   4692    336   -776   -688       N  
ATOM   1854  NH2 ARG B 208     -14.810  38.671  39.060  1.00 40.30           N  
ANISOU 1854  NH2 ARG B 208     4332   6263   4717    373   -860   -761       N  
ATOM   1855  N   GLN B 209      -9.257  41.719  44.327  1.00 51.96           N  
ANISOU 1855  N   GLN B 209     5554   7508   6681    697  -1170  -1223       N  
ATOM   1856  CA  GLN B 209      -8.851  42.508  45.503  1.00 55.12           C  
ANISOU 1856  CA  GLN B 209     5895   7917   7132    766  -1238  -1323       C  
ATOM   1857  C   GLN B 209      -7.429  43.053  45.346  1.00 56.80           C  
ANISOU 1857  C   GLN B 209     6075   7997   7508    796  -1253  -1361       C  
ATOM   1858  O   GLN B 209      -7.193  44.268  45.439  1.00 56.04           O  
ANISOU 1858  O   GLN B 209     5918   7854   7522    844  -1281  -1421       O  
ATOM   1859  CB  GLN B 209      -8.938  41.654  46.771  1.00 54.49           C  
ANISOU 1859  CB  GLN B 209     5834   7933   6935    774  -1280  -1346       C  
ATOM   1860  CG  GLN B 209     -10.303  41.716  47.427  1.00 57.72           C  
ANISOU 1860  CG  GLN B 209     6235   8487   7210    782  -1297  -1357       C  
ATOM   1861  CD  GLN B 209     -10.597  40.514  48.273  1.00 55.70           C  
ANISOU 1861  CD  GLN B 209     6021   8333   6811    760  -1313  -1334       C  
ATOM   1862  OE1 GLN B 209      -9.773  39.613  48.400  1.00 59.66           O  
ANISOU 1862  OE1 GLN B 209     6559   8795   7313    738  -1316  -1312       O  
ATOM   1863  NE2 GLN B 209     -11.792  40.472  48.842  1.00 60.97           N  
ANISOU 1863  NE2 GLN B 209     6682   9133   7352    762  -1326  -1337       N  
ATOM   1864  N   VAL B 210      -6.490  42.142  45.093  1.00 55.85           N  
ANISOU 1864  N   VAL B 210     5997   7817   7407    766  -1236  -1325       N  
ATOM   1865  CA  VAL B 210      -5.110  42.527  44.821  1.00 56.71           C  
ANISOU 1865  CA  VAL B 210     6082   7799   7668    786  -1243  -1349       C  
ATOM   1866  C   VAL B 210      -5.009  43.613  43.740  1.00 57.50           C  
ANISOU 1866  C   VAL B 210     6143   7810   7893    789  -1213  -1337       C  
ATOM   1867  O   VAL B 210      -4.410  44.660  43.964  1.00 56.38           O  
ANISOU 1867  O   VAL B 210     5942   7604   7876    837  -1247  -1398       O  
ATOM   1868  CB  VAL B 210      -4.276  41.319  44.417  1.00 56.40           C  
ANISOU 1868  CB  VAL B 210     6101   7710   7620    742  -1215  -1294       C  
ATOM   1869  CG1 VAL B 210      -2.906  41.766  43.987  1.00 56.64           C  
ANISOU 1869  CG1 VAL B 210     6104   7609   7809    759  -1215  -1312       C  
ATOM   1870  CG2 VAL B 210      -4.216  40.287  45.569  1.00 48.86           C  
ANISOU 1870  CG2 VAL B 210     5178   6830   6556    744  -1253  -1310       C  
ATOM   1871  N   LEU B 211      -5.630  43.380  42.586  1.00 62.71           N  
ANISOU 1871  N   LEU B 211     6835   8470   8521    739  -1151  -1259       N  
ATOM   1872  CA  LEU B 211      -5.611  44.338  41.480  1.00 61.52           C  
ANISOU 1872  CA  LEU B 211     6652   8244   8480    736  -1117  -1236       C  
ATOM   1873  C   LEU B 211      -6.227  45.674  41.884  1.00 64.05           C  
ANISOU 1873  C   LEU B 211     6907   8587   8843    785  -1154  -1298       C  
ATOM   1874  O   LEU B 211      -5.836  46.733  41.391  1.00 67.18           O  
ANISOU 1874  O   LEU B 211     7254   8900   9372    807  -1156  -1315       O  
ATOM   1875  CB  LEU B 211      -6.392  43.780  40.279  1.00 61.41           C  
ANISOU 1875  CB  LEU B 211     6687   8252   8395    674  -1047  -1141       C  
ATOM   1876  CG  LEU B 211      -5.765  42.794  39.288  1.00 56.56           C  
ANISOU 1876  CG  LEU B 211     6126   7581   7784    621   -992  -1065       C  
ATOM   1877  CD1 LEU B 211      -6.516  42.828  37.961  1.00 54.73           C  
ANISOU 1877  CD1 LEU B 211     5914   7350   7531    576   -927   -988       C  
ATOM   1878  CD2 LEU B 211      -4.319  43.114  39.050  1.00 55.20           C  
ANISOU 1878  CD2 LEU B 211     5926   7290   7758    639   -999  -1084       C  
ATOM   1879  N   ALA B 212      -7.215  45.609  42.769  1.00 61.94           N  
ANISOU 1879  N   ALA B 212     6639   8434   8461    803  -1185  -1332       N  
ATOM   1880  CA  ALA B 212      -7.964  46.798  43.159  1.00 68.04           C  
ANISOU 1880  CA  ALA B 212     7354   9244   9254    849  -1220  -1391       C  
ATOM   1881  C   ALA B 212      -7.112  47.687  44.076  1.00 81.38           C  
ANISOU 1881  C   ALA B 212     8979  10884  11057    918  -1289  -1489       C  
ATOM   1882  O   ALA B 212      -7.078  48.909  43.924  1.00 87.56           O  
ANISOU 1882  O   ALA B 212     9704  11616  11950    955  -1311  -1531       O  
ATOM   1883  CB  ALA B 212      -9.271  46.393  43.842  1.00 60.07           C  
ANISOU 1883  CB  ALA B 212     6363   8381   8080    846  -1230  -1396       C  
ATOM   1884  N   ARG B 213      -6.409  47.054  45.009  1.00 83.07           N  
ANISOU 1884  N   ARG B 213     9206  11111  11247    934  -1324  -1526       N  
ATOM   1885  CA  ARG B 213      -5.524  47.744  45.940  1.00 87.63           C  
ANISOU 1885  CA  ARG B 213     9728  11643  11925    998  -1391  -1619       C  
ATOM   1886  C   ARG B 213      -4.402  48.490  45.228  1.00 91.23           C  
ANISOU 1886  C   ARG B 213    10149  11953  12562   1007  -1387  -1622       C  
ATOM   1887  O   ARG B 213      -3.717  49.299  45.843  1.00 94.95           O  
ANISOU 1887  O   ARG B 213    10564  12373  13139   1062  -1442  -1699       O  
ATOM   1888  CB  ARG B 213      -4.900  46.738  46.909  1.00 84.90           C  
ANISOU 1888  CB  ARG B 213     9412  11330  11514   1003  -1419  -1640       C  
ATOM   1889  CG  ARG B 213      -4.807  47.215  48.343  1.00 85.82           C  
ANISOU 1889  CG  ARG B 213     9482  11499  11627   1073  -1497  -1745       C  
ATOM   1890  CD  ARG B 213      -5.713  46.376  49.219  1.00 88.34           C  
ANISOU 1890  CD  ARG B 213     9834  11965  11768   1066  -1509  -1744       C  
ATOM   1891  NE  ARG B 213      -5.355  44.962  49.126  1.00 88.81           N  
ANISOU 1891  NE  ARG B 213     9961  12034  11748   1013  -1479  -1678       N  
ATOM   1892  CZ  ARG B 213      -6.109  43.957  49.566  1.00 87.55           C  
ANISOU 1892  CZ  ARG B 213     9848  11989  11429    984  -1472  -1642       C  
ATOM   1893  NH1 ARG B 213      -7.284  44.192  50.134  1.00 90.48           N  
ANISOU 1893  NH1 ARG B 213    10202  12481  11695   1001  -1490  -1665       N  
ATOM   1894  NH2 ARG B 213      -5.689  42.710  49.430  1.00 86.77           N  
ANISOU 1894  NH2 ARG B 213     9809  11883  11276    937  -1448  -1583       N  
ATOM   1895  N   GLY B 214      -4.201  48.215  43.941  1.00 91.63           N  
ANISOU 1895  N   GLY B 214    10229  11939  12649    954  -1322  -1537       N  
ATOM   1896  CA  GLY B 214      -3.088  48.808  43.218  1.00 90.42           C  
ANISOU 1896  CA  GLY B 214    10044  11651  12662    957  -1312  -1529       C  
ATOM   1897  C   GLY B 214      -3.424  49.483  41.900  1.00 87.14           C  
ANISOU 1897  C   GLY B 214     9613  11180  12315    929  -1264  -1469       C  
ATOM   1898  O   GLY B 214      -2.544  49.611  41.050  1.00 82.87           O  
ANISOU 1898  O   GLY B 214     9066  10538  11883    910  -1235  -1430       O  
ATOM   1899  N   ASP B 215      -4.669  49.950  41.763  1.00 87.67           N  
ANISOU 1899  N   ASP B 215     9672  11315  12323    930  -1258  -1465       N  
ATOM   1900  CA  ASP B 215      -5.269  50.379  40.479  1.00 92.21           C  
ANISOU 1900  CA  ASP B 215    10247  11866  12923    894  -1203  -1396       C  
ATOM   1901  C   ASP B 215      -4.661  49.786  39.185  1.00 91.88           C  
ANISOU 1901  C   ASP B 215    10242  11751  12916    836  -1133  -1302       C  
ATOM   1902  O   ASP B 215      -3.959  50.463  38.430  1.00 93.49           O  
ANISOU 1902  O   ASP B 215    10411  11854  13257    835  -1120  -1283       O  
ATOM   1903  CB  ASP B 215      -5.488  51.915  40.403  1.00130.87           C  
ANISOU 1903  CB  ASP B 215    15070  16718  17939    937  -1239  -1442       C  
ATOM   1904  CG  ASP B 215      -4.202  52.708  40.163  1.00128.63           C  
ANISOU 1904  CG  ASP B 215    14733  16300  17840    960  -1261  -1463       C  
ATOM   1905  OD1 ASP B 215      -3.107  52.209  40.494  1.00128.76           O  
ANISOU 1905  OD1 ASP B 215    14759  16271  17894    964  -1272  -1477       O  
ATOM   1906  OD2 ASP B 215      -4.291  53.843  39.640  1.00126.99           O  
ANISOU 1906  OD2 ASP B 215    14473  16032  17743    974  -1269  -1466       O  
ATOM   1907  N   TYR B 216      -4.935  48.505  38.951  1.00 86.46           N  
ANISOU 1907  N   TYR B 216     9626  11121  12104    789  -1090  -1244       N  
ATOM   1908  CA  TYR B 216      -4.527  47.851  37.717  1.00 79.27           C  
ANISOU 1908  CA  TYR B 216     8755  10159  11204    733  -1021  -1155       C  
ATOM   1909  C   TYR B 216      -5.761  47.672  36.852  1.00 80.17           C  
ANISOU 1909  C   TYR B 216     8900  10334  11225    691   -967  -1086       C  
ATOM   1910  O   TYR B 216      -5.672  47.349  35.663  1.00 77.25           O  
ANISOU 1910  O   TYR B 216     8556   9929  10865    646   -907  -1009       O  
ATOM   1911  CB  TYR B 216      -3.878  46.495  38.010  1.00 74.61           C  
ANISOU 1911  CB  TYR B 216     8221   9579  10546    710  -1013  -1137       C  
ATOM   1912  CG  TYR B 216      -2.499  46.601  38.619  1.00 76.47           C  
ANISOU 1912  CG  TYR B 216     8430   9739  10887    744  -1054  -1191       C  
ATOM   1913  CD1 TYR B 216      -1.402  46.977  37.851  1.00 74.55           C  
ANISOU 1913  CD1 TYR B 216     8161   9384  10783    740  -1035  -1170       C  
ATOM   1914  CD2 TYR B 216      -2.289  46.323  39.965  1.00 79.75           C  
ANISOU 1914  CD2 TYR B 216     8845  10197  11261    780  -1113  -1262       C  
ATOM   1915  CE1 TYR B 216      -0.139  47.078  38.409  1.00 74.90           C  
ANISOU 1915  CE1 TYR B 216     8178   9358  10923    770  -1074  -1219       C  
ATOM   1916  CE2 TYR B 216      -1.029  46.420  40.528  1.00 78.46           C  
ANISOU 1916  CE2 TYR B 216     8655   9962  11192    812  -1152  -1312       C  
ATOM   1917  CZ  TYR B 216       0.038  46.800  39.747  1.00 78.05           C  
ANISOU 1917  CZ  TYR B 216     8579   9798  11280    807  -1132  -1291       C  
ATOM   1918  OH  TYR B 216       1.285  46.903  40.314  1.00 81.78           O  
ANISOU 1918  OH  TYR B 216     9024  10202  11848    838  -1172  -1342       O  
ATOM   1919  N   ASP B 217      -6.913  47.933  37.466  1.00 86.71           N  
ANISOU 1919  N   ASP B 217     9723  11256  11966    708   -992  -1118       N  
ATOM   1920  CA  ASP B 217      -8.225  47.625  36.895  1.00 89.88           C  
ANISOU 1920  CA  ASP B 217    10160  11738  12252    671   -949  -1062       C  
ATOM   1921  C   ASP B 217      -8.543  48.346  35.582  1.00 81.60           C  
ANISOU 1921  C   ASP B 217     9092  10640  11271    649   -901  -1005       C  
ATOM   1922  O   ASP B 217      -9.566  48.086  34.944  1.00 78.04           O  
ANISOU 1922  O   ASP B 217     8672  10247  10732    613   -859   -951       O  
ATOM   1923  CB  ASP B 217      -9.315  47.867  37.942  1.00 98.96           C  
ANISOU 1923  CB  ASP B 217    11298  12998  13305    702   -993  -1119       C  
ATOM   1924  CG  ASP B 217      -9.360  46.768  38.992  1.00105.28           C  
ANISOU 1924  CG  ASP B 217    12139  13879  13982    700  -1017  -1139       C  
ATOM   1925  OD1 ASP B 217      -9.246  45.579  38.610  1.00107.35           O  
ANISOU 1925  OD1 ASP B 217    12464  14155  14170    652   -978  -1078       O  
ATOM   1926  OD2 ASP B 217      -9.505  47.086  40.195  1.00104.21           O  
ANISOU 1926  OD2 ASP B 217    11974  13796  13824    747  -1077  -1217       O  
ATOM   1927  N   LYS B 218      -7.651  49.238  35.177  1.00 69.07           N  
ANISOU 1927  N   LYS B 218     8724   8260   9260   -734   -399   -413       N  
ATOM   1928  CA  LYS B 218      -7.758  49.896  33.888  1.00 71.06           C  
ANISOU 1928  CA  LYS B 218     8922   8455   9624   -656   -402   -374       C  
ATOM   1929  C   LYS B 218      -6.853  49.201  32.868  1.00 65.17           C  
ANISOU 1929  C   LYS B 218     8126   7769   8869   -606   -481   -261       C  
ATOM   1930  O   LYS B 218      -6.956  49.426  31.661  1.00 59.24           O  
ANISOU 1930  O   LYS B 218     7319   6994   8195   -536   -493   -212       O  
ATOM   1931  CB  LYS B 218      -7.358  51.358  34.039  1.00 82.05           C  
ANISOU 1931  CB  LYS B 218    10329   9778  11067   -704   -383   -416       C  
ATOM   1932  CG  LYS B 218      -7.515  52.189  32.797  1.00 93.31           C  
ANISOU 1932  CG  LYS B 218    11695  11139  12618   -632   -382   -376       C  
ATOM   1933  CD  LYS B 218      -8.544  53.265  33.021  1.00104.76           C  
ANISOU 1933  CD  LYS B 218    13151  12483  14169   -632   -289   -460       C  
ATOM   1934  CE  LYS B 218      -9.948  52.688  33.112  1.00109.90           C  
ANISOU 1934  CE  LYS B 218    13797  13117  14843   -583   -226   -494       C  
ATOM   1935  NZ  LYS B 218     -10.986  53.754  32.997  1.00112.70           N  
ANISOU 1935  NZ  LYS B 218    14132  13360  15331   -559   -136   -545       N  
ATOM   1936  N   ASN B 219      -5.961  48.347  33.351  1.00 60.47           N  
ANISOU 1936  N   ASN B 219     7544   7252   8180   -647   -533   -216       N  
ATOM   1937  CA  ASN B 219      -5.024  47.709  32.451  1.00 61.23           C  
ANISOU 1937  CA  ASN B 219     7593   7399   8272   -606   -600   -111       C  
ATOM   1938  C   ASN B 219      -5.149  46.186  32.478  1.00 57.48           C  
ANISOU 1938  C   ASN B 219     7104   6986   7748   -577   -609    -69       C  
ATOM   1939  O   ASN B 219      -4.624  45.492  31.605  1.00 57.40           O  
ANISOU 1939  O   ASN B 219     7050   7009   7750   -529   -645      9       O  
ATOM   1940  CB  ASN B 219      -3.597  48.153  32.774  1.00 73.60           C  
ANISOU 1940  CB  ASN B 219     9172   8998   9797   -674   -659    -67       C  
ATOM   1941  CG  ASN B 219      -2.834  48.602  31.542  1.00 86.29           C  
ANISOU 1941  CG  ASN B 219    10728  10595  11464   -627   -706      5       C  
ATOM   1942  OD1 ASN B 219      -3.414  48.774  30.469  1.00 90.09           O  
ANISOU 1942  OD1 ASN B 219    11166  11040  12023   -553   -691     14       O  
ATOM   1943  ND2 ASN B 219      -1.527  48.789  31.687  1.00 89.82           N  
ANISOU 1943  ND2 ASN B 219    11177  11079  11872   -675   -766     63       N  
ATOM   1944  N   ALA B 220      -5.877  45.672  33.462  1.00 46.00           N  
ANISOU 1944  N   ALA B 220     5687   5546   6245   -607   -572   -124       N  
ATOM   1945  CA  ALA B 220      -5.888  44.244  33.708  1.00 45.26           C  
ANISOU 1945  CA  ALA B 220     5584   5514   6099   -595   -583    -83       C  
ATOM   1946  C   ALA B 220      -7.277  43.767  34.134  1.00 51.05           C  
ANISOU 1946  C   ALA B 220     6337   6234   6827   -575   -524   -151       C  
ATOM   1947  O   ALA B 220      -8.020  44.507  34.784  1.00 55.45           O  
ANISOU 1947  O   ALA B 220     6933   6750   7386   -608   -477   -237       O  
ATOM   1948  CB  ALA B 220      -4.848  43.882  34.768  1.00 41.59           C  
ANISOU 1948  CB  ALA B 220     5139   5116   5548   -683   -627    -44       C  
ATOM   1949  N   ARG B 221      -7.607  42.524  33.784  1.00 44.91           N  
ANISOU 1949  N   ARG B 221     5534   5489   6043   -524   -522   -114       N  
ATOM   1950  CA  ARG B 221      -8.900  41.927  34.132  1.00 40.82           C  
ANISOU 1950  CA  ARG B 221     5030   4965   5515   -500   -471   -167       C  
ATOM   1951  C   ARG B 221      -8.705  40.492  34.564  1.00 42.78           C  
ANISOU 1951  C   ARG B 221     5269   5277   5708   -504   -487   -121       C  
ATOM   1952  O   ARG B 221      -7.847  39.797  34.036  1.00 43.91           O  
ANISOU 1952  O   ARG B 221     5375   5452   5856   -484   -523    -40       O  
ATOM   1953  CB  ARG B 221      -9.799  41.880  32.905  1.00 38.78           C  
ANISOU 1953  CB  ARG B 221     4736   4669   5328   -413   -440   -168       C  
ATOM   1954  CG  ARG B 221     -10.012  43.206  32.255  1.00 51.37           C  
ANISOU 1954  CG  ARG B 221     6320   6201   6998   -396   -426   -190       C  
ATOM   1955  CD  ARG B 221     -11.169  43.140  31.300  1.00 67.51           C  
ANISOU 1955  CD  ARG B 221     8331   8217   9104   -326   -387   -194       C  
ATOM   1956  NE  ARG B 221     -11.111  44.244  30.344  1.00 81.87           N  
ANISOU 1956  NE  ARG B 221    10113   9989  11003   -301   -390   -176       N  
ATOM   1957  CZ  ARG B 221     -11.893  44.346  29.275  1.00 91.44           C  
ANISOU 1957  CZ  ARG B 221    11280  11185  12279   -247   -370   -153       C  
ATOM   1958  NH1 ARG B 221     -11.768  45.384  28.460  1.00 95.95           N  
ANISOU 1958  NH1 ARG B 221    11811  11719  12926   -232   -378   -127       N  
ATOM   1959  NH2 ARG B 221     -12.802  43.409  29.022  1.00 93.50           N  
ANISOU 1959  NH2 ARG B 221    11530  11469  12525   -212   -344   -152       N  
ATOM   1960  N   VAL B 222      -9.530  40.030  35.487  1.00 34.60           N  
ANISOU 1960  N   VAL B 222     4262   4257   4629   -528   -457   -171       N  
ATOM   1961  CA  VAL B 222      -9.433  38.666  35.933  1.00 35.04           C  
ANISOU 1961  CA  VAL B 222     4303   4370   4639   -531   -470   -125       C  
ATOM   1962  C   VAL B 222     -10.578  37.902  35.235  1.00 40.46           C  
ANISOU 1962  C   VAL B 222     4973   5039   5361   -450   -428   -141       C  
ATOM   1963  O   VAL B 222     -11.672  38.430  35.068  1.00 37.98           O  
ANISOU 1963  O   VAL B 222     4676   4681   5073   -424   -385   -207       O  
ATOM   1964  CB  VAL B 222      -9.587  38.619  37.451  1.00 42.52           C  
ANISOU 1964  CB  VAL B 222     5291   5358   5507   -620   -467   -165       C  
ATOM   1965  CG1 VAL B 222      -9.325  37.208  37.977  1.00 48.54           C  
ANISOU 1965  CG1 VAL B 222     6028   6188   6227   -632   -490    -98       C  
ATOM   1966  CG2 VAL B 222      -8.627  39.620  38.083  1.00 37.62           C  
ANISOU 1966  CG2 VAL B 222     4694   4749   4850   -711   -498   -168       C  
ATOM   1967  N   ILE B 223     -10.317  36.669  34.818  1.00 34.93           N  
ANISOU 1967  N   ILE B 223     4238   4370   4666   -414   -438    -77       N  
ATOM   1968  CA  ILE B 223     -11.359  35.894  34.132  1.00 35.47           C  
ANISOU 1968  CA  ILE B 223     4291   4426   4760   -346   -398    -91       C  
ATOM   1969  C   ILE B 223     -11.309  34.515  34.700  1.00 39.52           C  
ANISOU 1969  C   ILE B 223     4792   4985   5241   -352   -400    -54       C  
ATOM   1970  O   ILE B 223     -10.261  34.097  35.221  1.00 40.13           O  
ANISOU 1970  O   ILE B 223     4852   5099   5297   -392   -436      9       O  
ATOM   1971  CB  ILE B 223     -11.093  35.810  32.617  1.00 36.58           C  
ANISOU 1971  CB  ILE B 223     4391   4548   4961   -286   -397    -51       C  
ATOM   1972  CG1 ILE B 223      -9.705  35.193  32.361  1.00 35.83           C  
ANISOU 1972  CG1 ILE B 223     4260   4482   4873   -293   -433     34       C  
ATOM   1973  CG2 ILE B 223     -11.191  37.203  31.975  1.00 39.47           C  
ANISOU 1973  CG2 ILE B 223     4759   4870   5369   -278   -397    -78       C  
ATOM   1974  CD1 ILE B 223      -9.484  34.692  30.920  1.00 40.50           C  
ANISOU 1974  CD1 ILE B 223     4808   5065   5515   -237   -420     72       C  
ATOM   1975  N   ASN B 224     -12.439  33.815  34.649  1.00 32.84           N  
ANISOU 1975  N   ASN B 224     3950   4137   4392   -316   -362    -87       N  
ATOM   1976  CA  ASN B 224     -12.462  32.398  34.971  1.00 31.01           C  
ANISOU 1976  CA  ASN B 224     3697   3940   4145   -308   -357    -47       C  
ATOM   1977  C   ASN B 224     -13.478  31.726  34.064  1.00 30.76           C  
ANISOU 1977  C   ASN B 224     3655   3890   4142   -243   -313    -67       C  
ATOM   1978  O   ASN B 224     -14.238  32.398  33.367  1.00 30.69           O  
ANISOU 1978  O   ASN B 224     3657   3850   4154   -213   -289   -111       O  
ATOM   1979  CB  ASN B 224     -12.791  32.130  36.435  1.00 35.23           C  
ANISOU 1979  CB  ASN B 224     4256   4513   4616   -365   -364    -67       C  
ATOM   1980  CG  ASN B 224     -14.154  32.664  36.857  1.00 39.25           C  
ANISOU 1980  CG  ASN B 224     4809   5003   5101   -364   -328   -160       C  
ATOM   1981  OD1 ASN B 224     -15.219  32.288  36.315  1.00 36.60           O  
ANISOU 1981  OD1 ASN B 224     4475   4648   4785   -310   -290   -189       O  
ATOM   1982  ND2 ASN B 224     -14.134  33.529  37.860  1.00 40.66           N  
ANISOU 1982  ND2 ASN B 224     5025   5189   5236   -431   -336   -205       N  
ATOM   1983  N   GLU B 225     -13.480  30.403  34.069  1.00 30.47           N  
ANISOU 1983  N   GLU B 225     3594   3874   4108   -225   -300    -30       N  
ATOM   1984  CA  GLU B 225     -14.297  29.647  33.118  1.00 31.29           C  
ANISOU 1984  CA  GLU B 225     3686   3966   4238   -171   -256    -44       C  
ATOM   1985  C   GLU B 225     -15.807  29.834  33.291  1.00 32.22           C  
ANISOU 1985  C   GLU B 225     3836   4076   4331   -155   -225   -112       C  
ATOM   1986  O   GLU B 225     -16.529  29.878  32.293  1.00 32.13           O  
ANISOU 1986  O   GLU B 225     3819   4048   4340   -119   -195   -132       O  
ATOM   1987  CB  GLU B 225     -13.898  28.160  33.151  1.00 27.19           C  
ANISOU 1987  CB  GLU B 225     3132   3464   3735   -159   -242     11       C  
ATOM   1988  CG  GLU B 225     -14.881  27.213  32.412  1.00 40.66           C  
ANISOU 1988  CG  GLU B 225     4832   5162   5454   -116   -189    -13       C  
ATOM   1989  CD  GLU B 225     -14.292  25.800  32.114  1.00 51.74           C  
ANISOU 1989  CD  GLU B 225     6193   6566   6899   -101   -162     42       C  
ATOM   1990  OE1 GLU B 225     -13.047  25.659  31.967  1.00 39.23           O  
ANISOU 1990  OE1 GLU B 225     4575   4978   5354   -109   -176    103       O  
ATOM   1991  OE2 GLU B 225     -15.094  24.843  31.979  1.00 50.23           O  
ANISOU 1991  OE2 GLU B 225     6001   6376   6707    -80   -122     24       O  
ATOM   1992  N   ASN B 226     -16.296  29.935  34.529  1.00 33.06           N  
ANISOU 1992  N   ASN B 226     3972   4198   4391   -187   -231   -145       N  
ATOM   1993  CA  ASN B 226     -17.728  30.152  34.757  1.00 37.48           C  
ANISOU 1993  CA  ASN B 226     4562   4748   4930   -173   -199   -209       C  
ATOM   1994  C   ASN B 226     -18.198  31.486  34.178  1.00 29.76           C  
ANISOU 1994  C   ASN B 226     3597   3728   3980   -160   -185   -249       C  
ATOM   1995  O   ASN B 226     -19.169  31.547  33.415  1.00 28.81           O  
ANISOU 1995  O   ASN B 226     3474   3592   3882   -122   -154   -267       O  
ATOM   1996  CB  ASN B 226     -18.096  30.062  36.249  1.00 47.65           C  
ANISOU 1996  CB  ASN B 226     5879   6064   6162   -218   -206   -240       C  
ATOM   1997  CG  ASN B 226     -18.128  28.625  36.768  1.00 61.97           C  
ANISOU 1997  CG  ASN B 226     7674   7918   7953   -219   -209   -203       C  
ATOM   1998  OD1 ASN B 226     -18.254  27.672  35.992  1.00 65.95           O  
ANISOU 1998  OD1 ASN B 226     8153   8420   8486   -176   -190   -174       O  
ATOM   1999  ND2 ASN B 226     -18.032  28.464  38.095  1.00 63.48           N  
ANISOU 1999  ND2 ASN B 226     7876   8149   8092   -274   -231   -205       N  
ATOM   2000  N   GLU B 227     -17.558  32.572  34.579  1.00 31.06           N  
ANISOU 2000  N   GLU B 227     3775   3877   4147   -197   -207   -261       N  
ATOM   2001  CA  GLU B 227     -17.942  33.873  34.061  1.00 30.32           C  
ANISOU 2001  CA  GLU B 227     3688   3738   4094   -185   -191   -294       C  
ATOM   2002  C   GLU B 227     -17.812  34.043  32.547  1.00 34.68           C  
ANISOU 2002  C   GLU B 227     4202   4274   4701   -143   -189   -256       C  
ATOM   2003  O   GLU B 227     -18.624  34.751  31.916  1.00 30.08           O  
ANISOU 2003  O   GLU B 227     3612   3662   4157   -118   -164   -272       O  
ATOM   2004  CB  GLU B 227     -17.100  34.994  34.743  1.00 33.63           C  
ANISOU 2004  CB  GLU B 227     4127   4141   4508   -240   -215   -312       C  
ATOM   2005  CG  GLU B 227     -17.362  35.168  36.224  1.00 37.88           C  
ANISOU 2005  CG  GLU B 227     4708   4693   4991   -298   -208   -366       C  
ATOM   2006  CD  GLU B 227     -16.563  36.352  36.825  1.00 46.26           C  
ANISOU 2006  CD  GLU B 227     5793   5739   6046   -362   -224   -391       C  
ATOM   2007  OE1 GLU B 227     -15.953  37.143  36.057  1.00 44.53           O  
ANISOU 2007  OE1 GLU B 227     5558   5488   5874   -350   -237   -370       O  
ATOM   2008  OE2 GLU B 227     -16.535  36.491  38.066  1.00 49.96           O  
ANISOU 2008  OE2 GLU B 227     6295   6230   6457   -430   -223   -431       O  
ATOM   2009  N   GLU B 228     -16.754  33.471  31.964  1.00 28.58           N  
ANISOU 2009  N   GLU B 228     3401   3522   3935   -140   -215   -201       N  
ATOM   2010  CA  GLU B 228     -16.553  33.611  30.523  1.00 31.06           C  
ANISOU 2010  CA  GLU B 228     3678   3830   4293   -110   -213   -167       C  
ATOM   2011  C   GLU B 228     -17.665  32.851  29.804  1.00 25.25           C  
ANISOU 2011  C   GLU B 228     2930   3107   3557    -77   -175   -172       C  
ATOM   2012  O   GLU B 228     -18.180  33.332  28.805  1.00 24.35           O  
ANISOU 2012  O   GLU B 228     2793   2985   3473    -60   -161   -165       O  
ATOM   2013  CB  GLU B 228     -15.164  33.126  30.111  1.00 25.78           C  
ANISOU 2013  CB  GLU B 228     2982   3179   3633   -117   -242   -112       C  
ATOM   2014  CG  GLU B 228     -14.057  34.129  30.517  1.00 33.23           C  
ANISOU 2014  CG  GLU B 228     3931   4110   4584   -150   -284    -97       C  
ATOM   2015  CD  GLU B 228     -14.205  35.490  29.803  1.00 37.21           C  
ANISOU 2015  CD  GLU B 228     4427   4581   5131   -143   -288   -109       C  
ATOM   2016  OE1 GLU B 228     -14.944  36.367  30.306  1.00 39.13           O  
ANISOU 2016  OE1 GLU B 228     4694   4794   5379   -151   -273   -156       O  
ATOM   2017  OE2 GLU B 228     -13.617  35.672  28.711  1.00 35.13           O  
ANISOU 2017  OE2 GLU B 228     4128   4319   4900   -129   -301    -70       O  
ATOM   2018  N   ASN B 229     -18.065  31.698  30.328  1.00 28.82           N  
ANISOU 2018  N   ASN B 229     3395   3582   3975    -74   -158   -180       N  
ATOM   2019  CA  ASN B 229     -19.191  30.989  29.668  1.00 28.98           C  
ANISOU 2019  CA  ASN B 229     3407   3617   3989    -48   -120   -187       C  
ATOM   2020  C   ASN B 229     -20.445  31.799  29.689  1.00 28.01           C  
ANISOU 2020  C   ASN B 229     3295   3475   3874    -37    -99   -218       C  
ATOM   2021  O   ASN B 229     -21.184  31.804  28.713  1.00 26.56           O  
ANISOU 2021  O   ASN B 229     3089   3300   3704    -22    -78   -206       O  
ATOM   2022  CB  ASN B 229     -19.470  29.635  30.302  1.00 28.47           C  
ANISOU 2022  CB  ASN B 229     3354   3575   3889    -45   -104   -192       C  
ATOM   2023  CG  ASN B 229     -18.696  28.538  29.632  1.00 31.03           C  
ANISOU 2023  CG  ASN B 229     3650   3914   4225    -41    -94   -155       C  
ATOM   2024  OD1 ASN B 229     -19.139  27.984  28.616  1.00 28.79           O  
ANISOU 2024  OD1 ASN B 229     3349   3641   3947    -29    -61   -153       O  
ATOM   2025  ND2 ASN B 229     -17.527  28.202  30.186  1.00 28.70           N  
ANISOU 2025  ND2 ASN B 229     3347   3621   3938    -56   -118   -123       N  
ATOM   2026  N   LYS B 230     -20.693  32.481  30.806  1.00 28.59           N  
ANISOU 2026  N   LYS B 230     3399   3525   3939    -50   -102   -256       N  
ATOM   2027  CA  LYS B 230     -21.894  33.286  30.933  1.00 27.61           C  
ANISOU 2027  CA  LYS B 230     3283   3373   3834    -39    -73   -287       C  
ATOM   2028  C   LYS B 230     -21.900  34.441  29.982  1.00 30.36           C  
ANISOU 2028  C   LYS B 230     3600   3693   4244    -30    -73   -265       C  
ATOM   2029  O   LYS B 230     -22.917  34.723  29.321  1.00 28.35           O  
ANISOU 2029  O   LYS B 230     3322   3431   4018    -10    -47   -251       O  
ATOM   2030  CB  LYS B 230     -22.131  33.756  32.364  1.00 32.46           C  
ANISOU 2030  CB  LYS B 230     3940   3966   4428    -63    -66   -342       C  
ATOM   2031  CG  LYS B 230     -22.522  32.656  33.337  1.00 44.99           C  
ANISOU 2031  CG  LYS B 230     5554   5587   5954    -71    -61   -364       C  
ATOM   2032  CD  LYS B 230     -23.170  33.283  34.565  1.00 56.14           C  
ANISOU 2032  CD  LYS B 230     7003   6977   7349    -94    -39   -426       C  
ATOM   2033  CE  LYS B 230     -23.638  32.226  35.548  1.00 59.56           C  
ANISOU 2033  CE  LYS B 230     7460   7451   7721   -106    -36   -446       C  
ATOM   2034  NZ  LYS B 230     -22.503  31.414  36.053  1.00 58.33           N  
ANISOU 2034  NZ  LYS B 230     7301   7337   7525   -138    -78   -416       N  
ATOM   2035  N   ARG B 231     -20.779  35.128  29.911  1.00 27.62           N  
ANISOU 2035  N   ARG B 231     3247   3330   3919    -47   -103   -253       N  
ATOM   2036  CA  ARG B 231     -20.640  36.284  29.049  1.00 32.35           C  
ANISOU 2036  CA  ARG B 231     3810   3899   4581    -42   -108   -227       C  
ATOM   2037  C   ARG B 231     -20.824  35.906  27.595  1.00 31.67           C  
ANISOU 2037  C   ARG B 231     3675   3847   4509    -26   -108   -174       C  
ATOM   2038  O   ARG B 231     -21.507  36.597  26.841  1.00 29.39           O  
ANISOU 2038  O   ARG B 231     3351   3549   4268    -16    -95   -147       O  
ATOM   2039  CB  ARG B 231     -19.230  36.880  29.233  1.00 35.14           C  
ANISOU 2039  CB  ARG B 231     4167   4240   4943    -67   -148   -220       C  
ATOM   2040  CG  ARG B 231     -18.838  37.878  28.186  1.00 39.81           C  
ANISOU 2040  CG  ARG B 231     4716   4813   5597    -61   -163   -180       C  
ATOM   2041  CD  ARG B 231     -17.595  38.654  28.657  1.00 34.63           C  
ANISOU 2041  CD  ARG B 231     4074   4134   4950    -89   -198   -186       C  
ATOM   2042  NE  ARG B 231     -16.377  37.957  28.299  1.00 30.64           N  
ANISOU 2042  NE  ARG B 231     3558   3668   4415    -98   -237   -147       N  
ATOM   2043  CZ  ARG B 231     -15.838  38.052  27.095  1.00 34.13           C  
ANISOU 2043  CZ  ARG B 231     3956   4126   4884    -89   -257    -97       C  
ATOM   2044  NH1 ARG B 231     -14.707  37.404  26.819  1.00 35.29           N  
ANISOU 2044  NH1 ARG B 231     4095   4305   5011    -96   -285    -63       N  
ATOM   2045  NH2 ARG B 231     -16.419  38.854  26.182  1.00 32.14           N  
ANISOU 2045  NH2 ARG B 231     3665   3861   4687    -75   -248    -75       N  
ATOM   2046  N   ILE B 232     -20.194  34.815  27.178  1.00 30.69           N  
ANISOU 2046  N   ILE B 232     3547   3766   4348    -30   -120   -154       N  
ATOM   2047  CA  ILE B 232     -20.297  34.419  25.783  1.00 32.61           C  
ANISOU 2047  CA  ILE B 232     3747   4048   4597    -30   -115   -112       C  
ATOM   2048  C   ILE B 232     -21.685  33.910  25.490  1.00 24.56           C  
ANISOU 2048  C   ILE B 232     2721   3050   3559    -21    -79   -113       C  
ATOM   2049  O   ILE B 232     -22.231  34.222  24.416  1.00 24.52           O  
ANISOU 2049  O   ILE B 232     2674   3068   3575    -27    -71    -74       O  
ATOM   2050  CB  ILE B 232     -19.197  33.369  25.436  1.00 32.17           C  
ANISOU 2050  CB  ILE B 232     3688   4022   4513    -40   -125    -98       C  
ATOM   2051  CG1 ILE B 232     -17.849  34.090  25.475  1.00 38.24           C  
ANISOU 2051  CG1 ILE B 232     4449   4772   5308    -50   -165    -80       C  
ATOM   2052  CG2 ILE B 232     -19.427  32.732  24.056  1.00 29.15           C  
ANISOU 2052  CG2 ILE B 232     3269   3686   4122    -50   -104    -70       C  
ATOM   2053  CD1 ILE B 232     -16.702  33.177  25.529  1.00 42.08           C  
ANISOU 2053  CD1 ILE B 232     4938   5274   5777    -57   -174    -66       C  
ATOM   2054  N   SER B 233     -22.301  33.167  26.420  1.00 24.78           N  
ANISOU 2054  N   SER B 233     2788   3079   3549    -12    -59   -149       N  
ATOM   2055  CA  SER B 233     -23.678  32.679  26.170  1.00 26.43           C  
ANISOU 2055  CA  SER B 233     2994   3311   3739     -4    -25   -147       C  
ATOM   2056  C   SER B 233     -24.625  33.858  26.024  1.00 25.39           C  
ANISOU 2056  C   SER B 233     2838   3152   3658      6    -13   -130       C  
ATOM   2057  O   SER B 233     -25.573  33.784  25.271  1.00 24.71           O  
ANISOU 2057  O   SER B 233     2721   3093   3575      5      6    -96       O  
ATOM   2058  CB  SER B 233     -24.209  31.811  27.325  1.00 30.64           C  
ANISOU 2058  CB  SER B 233     3571   3843   4226      6     -9   -190       C  
ATOM   2059  OG  SER B 233     -23.598  30.521  27.340  1.00 27.43           O  
ANISOU 2059  OG  SER B 233     3176   3465   3780     -1     -9   -194       O  
ATOM   2060  N   ILE B 234     -24.391  34.955  26.753  1.00 21.60           N  
ANISOU 2060  N   ILE B 234     2370   2617   3222     12    -19   -152       N  
ATOM   2061  CA  ILE B 234     -25.257  36.127  26.484  1.00 21.64           C  
ANISOU 2061  CA  ILE B 234     2341   2586   3297     23      1   -126       C  
ATOM   2062  C   ILE B 234     -25.075  36.647  25.070  1.00 22.98           C  
ANISOU 2062  C   ILE B 234     2443   2779   3507     13    -15    -55       C  
ATOM   2063  O   ILE B 234     -26.068  36.998  24.373  1.00 25.89           O  
ANISOU 2063  O   ILE B 234     2765   3161   3912     14      3     -3       O  
ATOM   2064  CB  ILE B 234     -24.969  37.271  27.493  1.00 29.43           C  
ANISOU 2064  CB  ILE B 234     3351   3500   4331     26      8   -169       C  
ATOM   2065  CG1 ILE B 234     -25.333  36.768  28.896  1.00 32.14           C  
ANISOU 2065  CG1 ILE B 234     3755   3830   4626     26     28   -238       C  
ATOM   2066  CG2 ILE B 234     -25.810  38.532  27.072  1.00 25.96           C  
ANISOU 2066  CG2 ILE B 234     2863   3014   3988     40     37   -133       C  
ATOM   2067  CD1 ILE B 234     -24.812  37.688  30.045  1.00 31.58           C  
ANISOU 2067  CD1 ILE B 234     3722   3702   4577      8     34   -298       C  
ATOM   2068  N   TRP B 235     -23.836  36.692  24.592  1.00 23.09           N  
ANISOU 2068  N   TRP B 235     2448   2808   3519     -3    -50    -44       N  
ATOM   2069  CA  TRP B 235     -23.600  37.133  23.225  1.00 25.38           C  
ANISOU 2069  CA  TRP B 235     2673   3130   3840    -20    -69     24       C  
ATOM   2070  C   TRP B 235     -24.280  36.220  22.211  1.00 25.51           C  
ANISOU 2070  C   TRP B 235     2660   3221   3811    -41    -55     61       C  
ATOM   2071  O   TRP B 235     -24.892  36.672  21.245  1.00 24.80           O  
ANISOU 2071  O   TRP B 235     2510   3162   3751    -58    -54    126       O  
ATOM   2072  CB  TRP B 235     -22.120  37.197  22.932  1.00 28.22           C  
ANISOU 2072  CB  TRP B 235     3032   3495   4194    -34   -107     25       C  
ATOM   2073  CG  TRP B 235     -21.741  37.824  21.609  1.00 27.67           C  
ANISOU 2073  CG  TRP B 235     2895   3457   4162    -55   -131     91       C  
ATOM   2074  CD1 TRP B 235     -21.545  39.153  21.361  1.00 35.42           C  
ANISOU 2074  CD1 TRP B 235     3835   4402   5220    -52   -149    128       C  
ATOM   2075  CD2 TRP B 235     -21.444  37.135  20.380  1.00 26.14           C  
ANISOU 2075  CD2 TRP B 235     2666   3336   3929    -87   -139    127       C  
ATOM   2076  NE1 TRP B 235     -21.168  39.331  20.047  1.00 29.12           N  
ANISOU 2076  NE1 TRP B 235     2975   3657   4432    -80   -174    191       N  
ATOM   2077  CE2 TRP B 235     -21.100  38.106  19.426  1.00 28.01           C  
ANISOU 2077  CE2 TRP B 235     2840   3587   4217   -105   -167    188       C  
ATOM   2078  CE3 TRP B 235     -21.467  35.793  19.986  1.00 28.51           C  
ANISOU 2078  CE3 TRP B 235     2982   3692   4158   -108   -119    111       C  
ATOM   2079  CZ2 TRP B 235     -20.769  37.788  18.117  1.00 33.31           C  
ANISOU 2079  CZ2 TRP B 235     3462   4331   4862   -147   -179    232       C  
ATOM   2080  CZ3 TRP B 235     -21.136  35.473  18.671  1.00 24.91           C  
ANISOU 2080  CZ3 TRP B 235     2482   3303   3680   -150   -123    148       C  
ATOM   2081  CH2 TRP B 235     -20.800  36.464  17.757  1.00 27.36           C  
ANISOU 2081  CH2 TRP B 235     2729   3632   4034   -172   -154    207       C  
ATOM   2082  N   LEU B 236     -24.178  34.929  22.450  1.00 22.03           N  
ANISOU 2082  N   LEU B 236     2261   2811   3300    -46    -44     24       N  
ATOM   2083  CA  LEU B 236     -24.736  33.961  21.525  1.00 18.78           C  
ANISOU 2083  CA  LEU B 236     1830   2470   2837    -75    -25     47       C  
ATOM   2084  C   LEU B 236     -26.246  34.028  21.523  1.00 22.74           C  
ANISOU 2084  C   LEU B 236     2316   2984   3341    -72      1     73       C  
ATOM   2085  O   LEU B 236     -26.872  33.747  20.479  1.00 26.25           O  
ANISOU 2085  O   LEU B 236     2718   3493   3762   -108     11    122       O  
ATOM   2086  CB  LEU B 236     -24.300  32.556  21.968  1.00 21.91           C  
ANISOU 2086  CB  LEU B 236     2276   2879   3170    -75    -10     -6       C  
ATOM   2087  CG  LEU B 236     -22.790  32.295  21.717  1.00 23.03           C  
ANISOU 2087  CG  LEU B 236     2421   3021   3310    -86    -30    -16       C  
ATOM   2088  CD1 LEU B 236     -22.411  30.946  22.409  1.00 21.80           C  
ANISOU 2088  CD1 LEU B 236     2311   2862   3111    -78    -10    -62       C  
ATOM   2089  CD2 LEU B 236     -22.406  32.282  20.192  1.00 24.40           C  
ANISOU 2089  CD2 LEU B 236     2542   3252   3478   -130    -31     26       C  
ATOM   2090  N   ASP B 237     -26.851  34.364  22.662  1.00 24.34           N  
ANISOU 2090  N   ASP B 237     2551   3132   3567    -35     15     42       N  
ATOM   2091  CA  ASP B 237     -28.335  34.446  22.699  1.00 22.87           C  
ANISOU 2091  CA  ASP B 237     2348   2953   3389    -28     44     72       C  
ATOM   2092  C   ASP B 237     -28.837  35.403  21.616  1.00 29.89           C  
ANISOU 2092  C   ASP B 237     3155   3863   4338    -47     40    162       C  
ATOM   2093  O   ASP B 237     -29.941  35.239  21.105  1.00 29.36           O  
ANISOU 2093  O   ASP B 237     3053   3839   4263    -63     57    216       O  
ATOM   2094  CB  ASP B 237     -28.893  35.013  24.019  1.00 29.44           C  
ANISOU 2094  CB  ASP B 237     3214   3712   4261     13     65     31       C  
ATOM   2095  CG  ASP B 237     -28.741  34.085  25.202  1.00 41.42           C  
ANISOU 2095  CG  ASP B 237     4803   5216   5717     28     73    -48       C  
ATOM   2096  OD1 ASP B 237     -28.727  32.852  25.017  1.00 36.14           O  
ANISOU 2096  OD1 ASP B 237     4155   4598   4979     15     74    -60       O  
ATOM   2097  OD2 ASP B 237     -28.670  34.596  26.342  1.00 42.27           O  
ANISOU 2097  OD2 ASP B 237     4947   5266   5849     48     81    -97       O  
ATOM   2098  N   THR B 238     -28.055  36.435  21.313  1.00 25.88           N  
ANISOU 2098  N   THR B 238     2613   3326   3894    -48     16    186       N  
ATOM   2099  CA  THR B 238     -28.493  37.392  20.272  1.00 27.14           C  
ANISOU 2099  CA  THR B 238     2684   3506   4120    -68      8    285       C  
ATOM   2100  C   THR B 238     -28.023  36.975  18.898  1.00 23.70           C  
ANISOU 2100  C   THR B 238     2204   3162   3638   -126    -18    334       C  
ATOM   2101  O   THR B 238     -28.825  36.896  17.959  1.00 30.65           O  
ANISOU 2101  O   THR B 238     3026   4113   4508   -167    -14    411       O  
ATOM   2102  CB  THR B 238     -27.988  38.822  20.590  1.00 30.77           C  
ANISOU 2102  CB  THR B 238     3120   3885   4685    -42     -2    294       C  
ATOM   2103  OG1 THR B 238     -28.625  39.291  21.792  1.00 28.96           O  
ANISOU 2103  OG1 THR B 238     2925   3573   4507      1     35    252       O  
ATOM   2104  CG2 THR B 238     -28.273  39.716  19.473  1.00 31.23           C  
ANISOU 2104  CG2 THR B 238     3081   3970   4814    -66    -15    402       C  
ATOM   2105  N   TYR B 239     -26.743  36.631  18.760  1.00 21.52           N  
ANISOU 2105  N   TYR B 239     1955   2894   3328   -136    -40    291       N  
ATOM   2106  CA  TYR B 239     -26.189  36.376  17.424  1.00 26.81           C  
ANISOU 2106  CA  TYR B 239     2578   3645   3962   -195    -61    334       C  
ATOM   2107  C   TYR B 239     -26.286  34.957  16.873  1.00 30.72           C  
ANISOU 2107  C   TYR B 239     3097   4218   4357   -241    -39    308       C  
ATOM   2108  O   TYR B 239     -26.188  34.766  15.678  1.00 28.18           O  
ANISOU 2108  O   TYR B 239     2728   3977   4002   -304    -44    351       O  
ATOM   2109  CB  TYR B 239     -24.746  36.828  17.390  1.00 22.26           C  
ANISOU 2109  CB  TYR B 239     2008   3040   3411   -188    -93    312       C  
ATOM   2110  CG  TYR B 239     -24.669  38.356  17.425  1.00 24.61           C  
ANISOU 2110  CG  TYR B 239     2254   3284   3812   -166   -116    364       C  
ATOM   2111  CD1 TYR B 239     -25.109  39.100  16.318  1.00 25.15           C  
ANISOU 2111  CD1 TYR B 239     2229   3401   3925   -203   -132    465       C  
ATOM   2112  CD2 TYR B 239     -24.192  39.040  18.551  1.00 25.41           C  
ANISOU 2112  CD2 TYR B 239     2397   3291   3967   -116   -120    315       C  
ATOM   2113  CE1 TYR B 239     -25.029  40.521  16.317  1.00 27.94           C  
ANISOU 2113  CE1 TYR B 239     2527   3699   4387   -182   -150    519       C  
ATOM   2114  CE2 TYR B 239     -24.155  40.438  18.566  1.00 25.01           C  
ANISOU 2114  CE2 TYR B 239     2299   3185   4018   -100   -132    358       C  
ATOM   2115  CZ  TYR B 239     -24.571  41.166  17.441  1.00 35.10           C  
ANISOU 2115  CZ  TYR B 239     3482   4504   5352   -129   -146    461       C  
ATOM   2116  OH  TYR B 239     -24.509  42.576  17.437  1.00 32.60           O  
ANISOU 2116  OH  TYR B 239     3111   4126   5150   -111   -155    510       O  
ATOM   2117  N   TYR B 240     -26.375  33.976  17.746  1.00 28.91           N  
ANISOU 2117  N   TYR B 240     2938   3964   4081   -215    -14    235       N  
ATOM   2118  CA  TYR B 240     -26.585  32.585  17.307  1.00 24.69           C  
ANISOU 2118  CA  TYR B 240     2428   3493   3459   -256     17    206       C  
ATOM   2119  C   TYR B 240     -27.667  31.982  18.161  1.00 20.63           C  
ANISOU 2119  C   TYR B 240     1956   2963   2920   -229     45    178       C  
ATOM   2120  O   TYR B 240     -27.447  30.978  18.882  1.00 24.16           O  
ANISOU 2120  O   TYR B 240     2464   3388   3327   -208     65    110       O  
ATOM   2121  CB  TYR B 240     -25.306  31.752  17.477  1.00 26.04           C  
ANISOU 2121  CB  TYR B 240     2645   3649   3602   -253     23    138       C  
ATOM   2122  CG  TYR B 240     -24.202  32.074  16.462  1.00 26.26           C  
ANISOU 2122  CG  TYR B 240     2631   3706   3638   -292      4    160       C  
ATOM   2123  CD1 TYR B 240     -23.994  31.260  15.366  1.00 27.31           C  
ANISOU 2123  CD1 TYR B 240     2749   3913   3714   -360     30    157       C  
ATOM   2124  CD2 TYR B 240     -23.387  33.203  16.614  1.00 27.71           C  
ANISOU 2124  CD2 TYR B 240     2795   3847   3887   -265    -38    181       C  
ATOM   2125  CE1 TYR B 240     -22.964  31.525  14.453  1.00 26.93           C  
ANISOU 2125  CE1 TYR B 240     2665   3895   3672   -398     16    172       C  
ATOM   2126  CE2 TYR B 240     -22.404  33.530  15.668  1.00 26.33           C  
ANISOU 2126  CE2 TYR B 240     2580   3704   3720   -300    -59    206       C  
ATOM   2127  CZ  TYR B 240     -22.190  32.681  14.597  1.00 33.24           C  
ANISOU 2127  CZ  TYR B 240     3439   4653   4536   -366    -32    201       C  
ATOM   2128  OH  TYR B 240     -21.186  32.916  13.659  1.00 29.52           O  
ANISOU 2128  OH  TYR B 240     2932   4218   4068   -406    -48    219       O  
ATOM   2129  N   PRO B 241     -28.889  32.510  18.043  1.00 22.31           N  
ANISOU 2129  N   PRO B 241     2132   3192   3153   -231     49    239       N  
ATOM   2130  CA  PRO B 241     -29.982  32.154  18.965  1.00 22.49           C  
ANISOU 2130  CA  PRO B 241     2191   3189   3165   -196     73    219       C  
ATOM   2131  C   PRO B 241     -30.456  30.694  18.810  1.00 24.63           C  
ANISOU 2131  C   PRO B 241     2499   3516   3345   -228    103    186       C  
ATOM   2132  O   PRO B 241     -31.054  30.158  19.730  1.00 27.78           O  
ANISOU 2132  O   PRO B 241     2943   3887   3723   -193    121    147       O  
ATOM   2133  CB  PRO B 241     -31.118  33.127  18.545  1.00 26.57           C  
ANISOU 2133  CB  PRO B 241     2639   3722   3735   -204     71    315       C  
ATOM   2134  CG  PRO B 241     -30.816  33.429  17.138  1.00 27.12           C  
ANISOU 2134  CG  PRO B 241     2638   3867   3799   -271     52    386       C  
ATOM   2135  CD  PRO B 241     -29.303  33.503  17.040  1.00 22.57           C  
ANISOU 2135  CD  PRO B 241     2079   3267   3229   -268     30    338       C  
ATOM   2136  N   GLN B 242     -30.149  30.042  17.696  1.00 23.82           N  
ANISOU 2136  N   GLN B 242     2377   3488   3186   -296    113    194       N  
ATOM   2137  CA  GLN B 242     -30.543  28.649  17.591  1.00 27.62           C  
ANISOU 2137  CA  GLN B 242     2896   4012   3585   -328    150    153       C  
ATOM   2138  C   GLN B 242     -29.373  27.692  17.690  1.00 27.06           C  
ANISOU 2138  C   GLN B 242     2869   3921   3490   -330    169     75       C  
ATOM   2139  O   GLN B 242     -29.518  26.493  17.441  1.00 26.94           O  
ANISOU 2139  O   GLN B 242     2881   3940   3415   -365    208     37       O  
ATOM   2140  CB  GLN B 242     -31.295  28.408  16.271  1.00 30.65           C  
ANISOU 2140  CB  GLN B 242     3232   4503   3912   -420    163    215       C  
ATOM   2141  CG  GLN B 242     -32.513  29.300  16.107  1.00 36.64           C  
ANISOU 2141  CG  GLN B 242     3934   5288   4700   -424    147    311       C  
ATOM   2142  CD  GLN B 242     -33.269  29.042  14.819  1.00 39.52           C  
ANISOU 2142  CD  GLN B 242     4245   5771   4999   -527    156    384       C  
ATOM   2143  OE1 GLN B 242     -32.980  29.650  13.791  1.00 47.64           O  
ANISOU 2143  OE1 GLN B 242     5208   6857   6036   -586    136    447       O  
ATOM   2144  NE2 GLN B 242     -34.228  28.136  14.868  1.00 36.20           N  
ANISOU 2144  NE2 GLN B 242     3850   5393   4510   -555    184    378       N  
ATOM   2145  N   LEU B 243     -28.208  28.173  18.089  1.00 21.91           N  
ANISOU 2145  N   LEU B 243     2225   3211   2888   -291    145     52       N  
ATOM   2146  CA  LEU B 243     -27.048  27.283  18.168  1.00 23.11           C  
ANISOU 2146  CA  LEU B 243     2409   3342   3028   -292    165     -8       C  
ATOM   2147  C   LEU B 243     -27.219  26.255  19.298  1.00 24.23           C  
ANISOU 2147  C   LEU B 243     2610   3443   3155   -250    189    -65       C  
ATOM   2148  O   LEU B 243     -27.554  26.611  20.428  1.00 24.22           O  
ANISOU 2148  O   LEU B 243     2632   3393   3176   -195    169    -73       O  
ATOM   2149  CB  LEU B 243     -25.786  28.148  18.426  1.00 19.89           C  
ANISOU 2149  CB  LEU B 243     1993   2883   2682   -258    128     -7       C  
ATOM   2150  CG  LEU B 243     -24.505  27.362  18.335  1.00 20.06           C  
ANISOU 2150  CG  LEU B 243     2031   2886   2703   -263    147    -50       C  
ATOM   2151  CD1 LEU B 243     -24.225  26.961  16.914  1.00 28.83           C  
ANISOU 2151  CD1 LEU B 243     3111   4064   3781   -338    177    -43       C  
ATOM   2152  CD2 LEU B 243     -23.329  28.224  18.878  1.00 22.36           C  
ANISOU 2152  CD2 LEU B 243     2322   3120   3054   -221    104    -46       C  
ATOM   2153  N   ALA B 244     -26.971  24.975  19.008  1.00 25.38           N  
ANISOU 2153  N   ALA B 244     2775   3604   3263   -279    235   -107       N  
ATOM   2154  CA  ALA B 244     -27.103  23.920  20.022  1.00 26.37           C  
ANISOU 2154  CA  ALA B 244     2948   3693   3379   -243    258   -153       C  
ATOM   2155  C   ALA B 244     -25.704  23.652  20.554  1.00 22.57           C  
ANISOU 2155  C   ALA B 244     2478   3154   2942   -211    256   -180       C  
ATOM   2156  O   ALA B 244     -24.871  23.108  19.829  1.00 23.77           O  
ANISOU 2156  O   ALA B 244     2619   3313   3101   -243    289   -196       O  
ATOM   2157  CB  ALA B 244     -27.642  22.608  19.346  1.00 21.24           C  
ANISOU 2157  CB  ALA B 244     2309   3090   2672   -298    320   -180       C  
ATOM   2158  N   TYR B 245     -25.395  24.057  21.770  1.00 21.01           N  
ANISOU 2158  N   TYR B 245     2299   2905   2779   -155    219   -183       N  
ATOM   2159  CA  TYR B 245     -23.998  23.881  22.233  1.00 19.73           C  
ANISOU 2159  CA  TYR B 245     2140   2697   2660   -132    211   -193       C  
ATOM   2160  C   TYR B 245     -23.990  23.474  23.691  1.00 22.64           C  
ANISOU 2160  C   TYR B 245     2540   3026   3037    -88    197   -209       C  
ATOM   2161  O   TYR B 245     -25.073  23.453  24.339  1.00 21.51           O  
ANISOU 2161  O   TYR B 245     2417   2888   2866    -72    192   -217       O  
ATOM   2162  CB  TYR B 245     -23.170  25.178  21.979  1.00 19.58           C  
ANISOU 2162  CB  TYR B 245     2096   2665   2678   -128    165   -164       C  
ATOM   2163  CG  TYR B 245     -23.601  26.345  22.809  1.00 22.66           C  
ANISOU 2163  CG  TYR B 245     2495   3032   3084    -96    119   -152       C  
ATOM   2164  CD1 TYR B 245     -23.063  26.583  24.069  1.00 27.41           C  
ANISOU 2164  CD1 TYR B 245     3120   3589   3707    -61     89   -163       C  
ATOM   2165  CD2 TYR B 245     -24.556  27.228  22.325  1.00 23.75           C  
ANISOU 2165  CD2 TYR B 245     2613   3194   3217   -106    108   -125       C  
ATOM   2166  CE1 TYR B 245     -23.450  27.669  24.810  1.00 27.47           C  
ANISOU 2166  CE1 TYR B 245     3138   3572   3728    -41     57   -162       C  
ATOM   2167  CE2 TYR B 245     -24.966  28.321  23.070  1.00 21.65           C  
ANISOU 2167  CE2 TYR B 245     2352   2896   2978    -76     78   -117       C  
ATOM   2168  CZ  TYR B 245     -24.437  28.524  24.308  1.00 23.49           C  
ANISOU 2168  CZ  TYR B 245     2615   3082   3229    -45     56   -142       C  
ATOM   2169  OH  TYR B 245     -24.893  29.637  25.033  1.00 29.41           O  
ANISOU 2169  OH  TYR B 245     3372   3796   4005    -24     37   -143       O  
ATOM   2170  N   TYR B 246     -22.797  23.143  24.211  1.00 20.17           N  
ANISOU 2170  N   TYR B 246     2224   2677   2761    -73    191   -207       N  
ATOM   2171  CA  TYR B 246     -22.699  22.625  25.547  1.00 20.77           C  
ANISOU 2171  CA  TYR B 246     2321   2727   2844    -43    179   -213       C  
ATOM   2172  C   TYR B 246     -22.003  23.664  26.384  1.00 23.87           C  
ANISOU 2172  C   TYR B 246     2716   3095   3258    -26    123   -196       C  
ATOM   2173  O   TYR B 246     -22.634  24.290  27.212  1.00 24.92           O  
ANISOU 2173  O   TYR B 246     2870   3225   3373    -13     95   -206       O  
ATOM   2174  CB  TYR B 246     -21.905  21.294  25.590  1.00 19.71           C  
ANISOU 2174  CB  TYR B 246     2175   2572   2741    -44    221   -212       C  
ATOM   2175  CG  TYR B 246     -22.775  20.166  24.986  1.00 20.65           C  
ANISOU 2175  CG  TYR B 246     2301   2712   2834    -64    284   -239       C  
ATOM   2176  CD1 TYR B 246     -23.794  19.592  25.731  1.00 22.84           C  
ANISOU 2176  CD1 TYR B 246     2600   2997   3079    -50    288   -253       C  
ATOM   2177  CD2 TYR B 246     -22.561  19.705  23.682  1.00 23.60           C  
ANISOU 2177  CD2 TYR B 246     2658   3098   3210   -102    339   -253       C  
ATOM   2178  CE1 TYR B 246     -24.596  18.580  25.206  1.00 25.77           C  
ANISOU 2178  CE1 TYR B 246     2980   3387   3424    -71    343   -278       C  
ATOM   2179  CE2 TYR B 246     -23.389  18.710  23.132  1.00 21.76           C  
ANISOU 2179  CE2 TYR B 246     2434   2887   2946   -131    400   -284       C  
ATOM   2180  CZ  TYR B 246     -24.411  18.155  23.917  1.00 26.23           C  
ANISOU 2180  CZ  TYR B 246     3025   3459   3482   -113    399   -294       C  
ATOM   2181  OH  TYR B 246     -25.216  17.126  23.426  1.00 24.75           O  
ANISOU 2181  OH  TYR B 246     2849   3293   3262   -144    459   -324       O  
ATOM   2182  N   ARG B 247     -20.708  23.849  26.147  1.00 23.70           N  
ANISOU 2182  N   ARG B 247     2674   3056   3275    -31    111   -174       N  
ATOM   2183  CA  ARG B 247     -19.870  24.658  27.058  1.00 27.81           C  
ANISOU 2183  CA  ARG B 247     3197   3556   3814    -23     59   -155       C  
ATOM   2184  C   ARG B 247     -18.547  25.003  26.421  1.00 29.01           C  
ANISOU 2184  C   ARG B 247     3321   3695   4005    -32     48   -125       C  
ATOM   2185  O   ARG B 247     -18.117  24.313  25.507  1.00 23.62           O  
ANISOU 2185  O   ARG B 247     2617   3015   3344    -41     88   -120       O  
ATOM   2186  CB  ARG B 247     -19.597  23.863  28.372  1.00 34.53           C  
ANISOU 2186  CB  ARG B 247     4056   4397   4665    -14     51   -145       C  
ATOM   2187  CG  ARG B 247     -19.097  24.707  29.532  1.00 42.69           C  
ANISOU 2187  CG  ARG B 247     5103   5424   5694    -20     -4   -134       C  
ATOM   2188  CD  ARG B 247     -19.275  24.039  30.895  1.00 43.65           C  
ANISOU 2188  CD  ARG B 247     5236   5555   5796    -23    -16   -130       C  
ATOM   2189  NE  ARG B 247     -18.897  24.929  31.999  1.00 48.57           N  
ANISOU 2189  NE  ARG B 247     5873   6181   6399    -44    -65   -128       N  
ATOM   2190  CZ  ARG B 247     -19.580  26.014  32.380  1.00 50.18           C  
ANISOU 2190  CZ  ARG B 247     6109   6383   6575    -50    -81   -168       C  
ATOM   2191  NH1 ARG B 247     -20.692  26.400  31.756  1.00 50.29           N  
ANISOU 2191  NH1 ARG B 247     6137   6392   6581    -32    -57   -203       N  
ATOM   2192  NH2 ARG B 247     -19.130  26.745  33.394  1.00 51.60           N  
ANISOU 2192  NH2 ARG B 247     6304   6566   6737    -81   -118   -170       N  
ATOM   2193  N   ILE B 248     -17.903  26.093  26.888  1.00 22.81           N  
ANISOU 2193  N   ILE B 248     2537   2897   3231    -32     -2   -109       N  
ATOM   2194  CA  ILE B 248     -16.532  26.405  26.439  1.00 20.01           C  
ANISOU 2194  CA  ILE B 248     2156   2531   2914    -40    -20    -74       C  
ATOM   2195  C   ILE B 248     -15.574  26.009  27.540  1.00 23.53           C  
ANISOU 2195  C   ILE B 248     2599   2964   3376    -40    -43    -40       C  
ATOM   2196  O   ILE B 248     -15.856  26.249  28.714  1.00 25.18           O  
ANISOU 2196  O   ILE B 248     2832   3176   3559    -44    -72    -47       O  
ATOM   2197  CB  ILE B 248     -16.356  27.923  26.199  1.00 21.07           C  
ANISOU 2197  CB  ILE B 248     2291   2662   3053    -46    -63    -70       C  
ATOM   2198  CG1 ILE B 248     -17.421  28.398  25.222  1.00 31.26           C  
ANISOU 2198  CG1 ILE B 248     3576   3970   4331    -48    -46    -89       C  
ATOM   2199  CG2 ILE B 248     -15.003  28.183  25.598  1.00 27.83           C  
ANISOU 2199  CG2 ILE B 248     3117   3511   3944    -53    -79    -33       C  
ATOM   2200  CD1 ILE B 248     -17.348  29.878  25.055  1.00 36.87           C  
ANISOU 2200  CD1 ILE B 248     4281   4671   5059    -51    -85    -80       C  
ATOM   2201  N   HIS B 249     -14.493  25.317  27.187  1.00 24.57           N  
ANISOU 2201  N   HIS B 249     2700   3085   3551    -41    -24     -2       N  
ATOM   2202  CA  HIS B 249     -13.511  24.888  28.179  1.00 26.53           C  
ANISOU 2202  CA  HIS B 249     2931   3325   3823    -45    -46     50       C  
ATOM   2203  C   HIS B 249     -12.219  25.655  28.051  1.00 27.82           C  
ANISOU 2203  C   HIS B 249     3075   3481   4012    -56    -86     95       C  
ATOM   2204  O   HIS B 249     -11.780  25.870  26.924  1.00 31.93           O  
ANISOU 2204  O   HIS B 249     3578   3996   4559    -53    -70     97       O  
ATOM   2205  CB  HIS B 249     -13.224  23.361  28.058  1.00 26.15           C  
ANISOU 2205  CB  HIS B 249     2853   3263   3821    -35     12     75       C  
ATOM   2206  CG  HIS B 249     -14.409  22.550  28.420  1.00 35.11           C  
ANISOU 2206  CG  HIS B 249     4006   4405   4929    -27     43     39       C  
ATOM   2207  ND1 HIS B 249     -14.921  22.533  29.703  1.00 39.80           N  
ANISOU 2207  ND1 HIS B 249     4620   5015   5488    -31     10     39       N  
ATOM   2208  CD2 HIS B 249     -15.259  21.823  27.653  1.00 35.19           C  
ANISOU 2208  CD2 HIS B 249     4023   4414   4934    -20    103     -3       C  
ATOM   2209  CE1 HIS B 249     -15.995  21.751  29.726  1.00 38.93           C  
ANISOU 2209  CE1 HIS B 249     4523   4910   5359    -20     47      4       C  
ATOM   2210  NE2 HIS B 249     -16.228  21.323  28.495  1.00 32.90           N  
ANISOU 2210  NE2 HIS B 249     3753   4137   4612    -14    104    -22       N  
ATOM   2211  N   PHE B 250     -11.618  26.005  29.194  1.00 28.21           N  
ANISOU 2211  N   PHE B 250     3128   3538   4052    -75   -137    132       N  
ATOM   2212  CA  PHE B 250     -10.466  26.921  29.254  1.00 27.63           C  
ANISOU 2212  CA  PHE B 250     3044   3465   3990    -93   -186    175       C  
ATOM   2213  C   PHE B 250      -9.211  26.282  29.869  1.00 38.75           C  
ANISOU 2213  C   PHE B 250     4413   4875   5436   -106   -200    261       C  
ATOM   2214  O   PHE B 250      -8.377  26.987  30.449  1.00 36.22           O  
ANISOU 2214  O   PHE B 250     4090   4567   5105   -135   -254    303       O  
ATOM   2215  CB  PHE B 250     -10.830  28.195  30.013  1.00 32.58           C  
ANISOU 2215  CB  PHE B 250     3710   4102   4566   -117   -237    142       C  
ATOM   2216  CG  PHE B 250     -11.844  29.027  29.307  1.00 33.23           C  
ANISOU 2216  CG  PHE B 250     3818   4176   4632   -103   -226     78       C  
ATOM   2217  CD1 PHE B 250     -11.454  29.986  28.382  1.00 31.35           C  
ANISOU 2217  CD1 PHE B 250     3570   3928   4414   -101   -242     79       C  
ATOM   2218  CD2 PHE B 250     -13.193  28.825  29.529  1.00 32.11           C  
ANISOU 2218  CD2 PHE B 250     3702   4037   4460    -93   -200     24       C  
ATOM   2219  CE1 PHE B 250     -12.401  30.752  27.680  1.00 28.21           C  
ANISOU 2219  CE1 PHE B 250     3183   3524   4010    -90   -231     35       C  
ATOM   2220  CE2 PHE B 250     -14.141  29.579  28.844  1.00 32.16           C  
ANISOU 2220  CE2 PHE B 250     3721   4036   4460    -80   -188    -20       C  
ATOM   2221  CZ  PHE B 250     -13.743  30.553  27.920  1.00 35.86           C  
ANISOU 2221  CZ  PHE B 250     4175   4495   4954    -80   -204    -12       C  
ATOM   2222  N   ASP B 251      -9.079  24.966  29.706  1.00 33.09           N  
ANISOU 2222  N   ASP B 251     3661   4144   4766    -88   -149    291       N  
ATOM   2223  CA  ASP B 251      -7.887  24.245  30.156  1.00 42.80           C  
ANISOU 2223  CA  ASP B 251     4840   5369   6054    -96   -151    387       C  
ATOM   2224  C   ASP B 251      -6.642  24.946  29.671  1.00 43.46           C  
ANISOU 2224  C   ASP B 251     4901   5446   6165   -104   -180    436       C  
ATOM   2225  O   ASP B 251      -5.683  25.115  30.422  1.00 39.74           O  
ANISOU 2225  O   ASP B 251     4406   4991   5702   -131   -226    515       O  
ATOM   2226  CB  ASP B 251      -7.898  22.822  29.614  1.00 46.23           C  
ANISOU 2226  CB  ASP B 251     5236   5771   6559    -67    -71    401       C  
ATOM   2227  CG  ASP B 251      -9.212  22.159  29.817  1.00 59.38           C  
ANISOU 2227  CG  ASP B 251     6926   7439   8195    -56    -36    340       C  
ATOM   2228  OD1 ASP B 251      -9.466  21.729  30.957  1.00 57.90           O  
ANISOU 2228  OD1 ASP B 251     6734   7271   7993    -69    -57    369       O  
ATOM   2229  OD2 ASP B 251      -9.995  22.099  28.846  1.00 69.30           O  
ANISOU 2229  OD2 ASP B 251     8206   8685   9440    -40     10    268       O  
ATOM   2230  N   GLU B 252      -6.663  25.354  28.408  1.00 36.24           N  
ANISOU 2230  N   GLU B 252     3993   4515   5263    -85   -156    394       N  
ATOM   2231  CA  GLU B 252      -5.610  26.191  27.855  1.00 32.31           C  
ANISOU 2231  CA  GLU B 252     3481   4015   4782    -92   -188    429       C  
ATOM   2232  C   GLU B 252      -6.291  27.484  27.433  1.00 32.87           C  
ANISOU 2232  C   GLU B 252     3595   4098   4797    -97   -221    358       C  
ATOM   2233  O   GLU B 252      -6.927  27.537  26.401  1.00 32.83           O  
ANISOU 2233  O   GLU B 252     3597   4087   4790    -81   -186    304       O  
ATOM   2234  CB  GLU B 252      -4.996  25.548  26.627  1.00 33.75           C  
ANISOU 2234  CB  GLU B 252     3622   4167   5033    -69   -126    444       C  
ATOM   2235  CG  GLU B 252      -4.422  24.181  26.836  1.00 56.56           C  
ANISOU 2235  CG  GLU B 252     6461   7029   7999    -57    -69    507       C  
ATOM   2236  CD  GLU B 252      -3.625  23.722  25.628  1.00 72.76           C  
ANISOU 2236  CD  GLU B 252     8472   9047  10125    -40     -5    522       C  
ATOM   2237  OE1 GLU B 252      -4.028  24.054  24.486  1.00 77.43           O  
ANISOU 2237  OE1 GLU B 252     9081   9640  10697    -39     23    453       O  
ATOM   2238  OE2 GLU B 252      -2.593  23.037  25.825  1.00 77.84           O  
ANISOU 2238  OE2 GLU B 252     9063   9665  10849    -34     19    608       O  
ATOM   2239  N   PRO B 253      -6.153  28.517  28.249  1.00 34.86           N  
ANISOU 2239  N   PRO B 253     3873   4367   5006   -125   -287    364       N  
ATOM   2240  CA  PRO B 253      -6.812  29.798  28.024  1.00 33.28           C  
ANISOU 2240  CA  PRO B 253     3711   4170   4765   -131   -316    302       C  
ATOM   2241  C   PRO B 253      -6.449  30.395  26.682  1.00 31.38           C  
ANISOU 2241  C   PRO B 253     3452   3920   4551   -117   -313    298       C  
ATOM   2242  O   PRO B 253      -7.267  31.098  26.110  1.00 29.37           O  
ANISOU 2242  O   PRO B 253     3215   3666   4279   -111   -311    245       O  
ATOM   2243  CB  PRO B 253      -6.315  30.650  29.179  1.00 36.99           C  
ANISOU 2243  CB  PRO B 253     4200   4654   5198   -172   -379    325       C  
ATOM   2244  CG  PRO B 253      -5.995  29.648  30.264  1.00 47.48           C  
ANISOU 2244  CG  PRO B 253     5514   6002   6525   -192   -380    379       C  
ATOM   2245  CD  PRO B 253      -5.518  28.415  29.579  1.00 44.41           C  
ANISOU 2245  CD  PRO B 253     5075   5596   6201   -159   -330    427       C  
ATOM   2246  N   ARG B 254      -5.254  30.113  26.162  1.00 32.68           N  
ANISOU 2246  N   ARG B 254     3578   4080   4760   -113   -311    358       N  
ATOM   2247  CA  ARG B 254      -4.901  30.619  24.836  1.00 26.72           C  
ANISOU 2247  CA  ARG B 254     2802   3323   4027   -104   -306    354       C  
ATOM   2248  C   ARG B 254      -5.655  29.930  23.703  1.00 27.33           C  
ANISOU 2248  C   ARG B 254     2869   3400   4115    -88   -238    307       C  
ATOM   2249  O   ARG B 254      -5.647  30.412  22.584  1.00 28.27           O  
ANISOU 2249  O   ARG B 254     2973   3529   4238    -91   -234    292       O  
ATOM   2250  CB  ARG B 254      -3.410  30.413  24.600  1.00 31.86           C  
ANISOU 2250  CB  ARG B 254     3412   3968   4724   -106   -316    433       C  
ATOM   2251  CG  ARG B 254      -2.521  31.348  25.431  1.00 23.59           C  
ANISOU 2251  CG  ARG B 254     2371   2930   3661   -132   -392    486       C  
ATOM   2252  CD  ARG B 254      -2.827  32.793  25.134  1.00 29.40           C  
ANISOU 2252  CD  ARG B 254     3132   3670   4366   -142   -439    446       C  
ATOM   2253  NE  ARG B 254      -1.763  33.673  25.662  1.00 26.88           N  
ANISOU 2253  NE  ARG B 254     2814   3359   4041   -170   -506    500       N  
ATOM   2254  CZ  ARG B 254      -1.783  34.996  25.524  1.00 29.71           C  
ANISOU 2254  CZ  ARG B 254     3191   3717   4382   -184   -551    479       C  
ATOM   2255  NH1 ARG B 254      -0.771  35.738  26.005  1.00 29.64           N  
ANISOU 2255  NH1 ARG B 254     3184   3715   4365   -214   -609    529       N  
ATOM   2256  NH2 ARG B 254      -2.829  35.586  24.927  1.00 28.95           N  
ANISOU 2256  NH2 ARG B 254     3108   3611   4280   -170   -537    412       N  
ATOM   2257  N   LYS B 255      -6.203  28.747  23.976  1.00 25.96           N  
ANISOU 2257  N   LYS B 255     2698   3220   3947    -79   -184    290       N  
ATOM   2258  CA  LYS B 255      -6.901  28.011  22.957  1.00 30.72           C  
ANISOU 2258  CA  LYS B 255     3293   3825   4555    -74   -114    243       C  
ATOM   2259  C   LYS B 255      -8.177  27.368  23.584  1.00 30.08           C  
ANISOU 2259  C   LYS B 255     3241   3745   4442    -68    -86    197       C  
ATOM   2260  O   LYS B 255      -8.209  26.158  23.835  1.00 29.52           O  
ANISOU 2260  O   LYS B 255     3161   3659   4396    -60    -34    202       O  
ATOM   2261  CB  LYS B 255      -6.015  26.862  22.427  1.00 39.14           C  
ANISOU 2261  CB  LYS B 255     4319   4870   5683    -68    -49    274       C  
ATOM   2262  CG  LYS B 255      -4.614  27.232  21.984  1.00 56.43           C  
ANISOU 2262  CG  LYS B 255     6473   7051   7915    -70    -68    333       C  
ATOM   2263  CD  LYS B 255      -4.627  28.148  20.750  1.00 62.66           C  
ANISOU 2263  CD  LYS B 255     7256   7866   8684    -85    -83    306       C  
ATOM   2264  CE  LYS B 255      -3.352  27.969  19.911  1.00 62.50           C  
ANISOU 2264  CE  LYS B 255     7193   7836   8717    -88    -58    348       C  
ATOM   2265  NZ  LYS B 255      -3.248  28.983  18.808  1.00 56.47           N  
ANISOU 2265  NZ  LYS B 255     6420   7106   7933   -107    -88    334       N  
ATOM   2266  N   PRO B 256      -9.191  28.171  23.882  1.00 25.87           N  
ANISOU 2266  N   PRO B 256     2741   3227   3861    -71   -118    158       N  
ATOM   2267  CA  PRO B 256     -10.446  27.603  24.421  1.00 23.00           C  
ANISOU 2267  CA  PRO B 256     2406   2868   3465    -65    -92    114       C  
ATOM   2268  C   PRO B 256     -11.064  26.615  23.441  1.00 30.11           C  
ANISOU 2268  C   PRO B 256     3296   3775   4368    -67    -18     80       C  
ATOM   2269  O   PRO B 256     -10.870  26.722  22.217  1.00 26.27           O  
ANISOU 2269  O   PRO B 256     2788   3301   3891    -81      7     72       O  
ATOM   2270  CB  PRO B 256     -11.368  28.824  24.545  1.00 30.07           C  
ANISOU 2270  CB  PRO B 256     3329   3774   4321    -69   -131     80       C  
ATOM   2271  CG  PRO B 256     -10.400  30.036  24.576  1.00 32.40           C  
ANISOU 2271  CG  PRO B 256     3617   4064   4630    -78   -190    113       C  
ATOM   2272  CD  PRO B 256      -9.303  29.619  23.620  1.00 25.91           C  
ANISOU 2272  CD  PRO B 256     2755   3242   3847    -80   -171    150       C  
ATOM   2273  N   VAL B 257     -11.773  25.625  23.980  1.00 23.72           N  
ANISOU 2273  N   VAL B 257     2501   2962   3550    -59     19     59       N  
ATOM   2274  CA  VAL B 257     -12.441  24.625  23.145  1.00 21.78           C  
ANISOU 2274  CA  VAL B 257     2251   2722   3302    -67     94     21       C  
ATOM   2275  C   VAL B 257     -13.948  24.762  23.360  1.00 28.12           C  
ANISOU 2275  C   VAL B 257     3087   3548   4049    -68     92    -24       C  
ATOM   2276  O   VAL B 257     -14.425  24.646  24.500  1.00 26.41           O  
ANISOU 2276  O   VAL B 257     2893   3326   3816    -53     70    -26       O  
ATOM   2277  CB  VAL B 257     -12.017  23.205  23.561  1.00 27.06           C  
ANISOU 2277  CB  VAL B 257     2904   3360   4018    -56    149     38       C  
ATOM   2278  CG1 VAL B 257     -12.712  22.148  22.699  1.00 26.47           C  
ANISOU 2278  CG1 VAL B 257     2829   3288   3941    -71    236    -11       C  
ATOM   2279  CG2 VAL B 257     -10.494  23.051  23.374  1.00 29.72           C  
ANISOU 2279  CG2 VAL B 257     3201   3670   4423    -53    156     93       C  
ATOM   2280  N   PHE B 258     -14.665  25.045  22.280  1.00 23.43           N  
ANISOU 2280  N   PHE B 258     2492   2985   3426    -89    112    -53       N  
ATOM   2281  CA  PHE B 258     -16.116  25.223  22.342  1.00 23.37           C  
ANISOU 2281  CA  PHE B 258     2508   3002   3369    -93    111    -85       C  
ATOM   2282  C   PHE B 258     -16.777  23.903  21.931  1.00 21.40           C  
ANISOU 2282  C   PHE B 258     2263   2763   3105   -108    184   -118       C  
ATOM   2283  O   PHE B 258     -16.583  23.438  20.803  1.00 26.86           O  
ANISOU 2283  O   PHE B 258     2936   3472   3799   -140    236   -132       O  
ATOM   2284  CB  PHE B 258     -16.519  26.300  21.351  1.00 25.09           C  
ANISOU 2284  CB  PHE B 258     2711   3255   3568   -116     90    -82       C  
ATOM   2285  CG  PHE B 258     -17.940  26.818  21.544  1.00 31.76           C  
ANISOU 2285  CG  PHE B 258     3573   4120   4375   -114     76    -96       C  
ATOM   2286  CD1 PHE B 258     -18.643  26.577  22.720  1.00 36.78           C  
ANISOU 2286  CD1 PHE B 258     4241   4738   4995    -88     69   -112       C  
ATOM   2287  CD2 PHE B 258     -18.561  27.529  20.554  1.00 36.86           C  
ANISOU 2287  CD2 PHE B 258     4196   4804   5004   -141     70    -85       C  
ATOM   2288  CE1 PHE B 258     -19.944  27.074  22.885  1.00 36.74           C  
ANISOU 2288  CE1 PHE B 258     4249   4748   4962    -85     61   -122       C  
ATOM   2289  CE2 PHE B 258     -19.844  28.019  20.710  1.00 36.49           C  
ANISOU 2289  CE2 PHE B 258     4155   4773   4934   -139     61    -85       C  
ATOM   2290  CZ  PHE B 258     -20.537  27.803  21.856  1.00 25.15           C  
ANISOU 2290  CZ  PHE B 258     2755   3314   3487   -108     58   -105       C  
ATOM   2291  N   TRP B 259     -17.546  23.284  22.824  1.00 22.43           N  
ANISOU 2291  N   TRP B 259     2418   2886   3217    -90    193   -133       N  
ATOM   2292  CA  TRP B 259     -18.188  21.996  22.487  1.00 21.52           C  
ANISOU 2292  CA  TRP B 259     2309   2779   3090   -105    263   -165       C  
ATOM   2293  C   TRP B 259     -19.563  22.291  21.897  1.00 25.20           C  
ANISOU 2293  C   TRP B 259     2788   3291   3495   -129    269   -190       C  
ATOM   2294  O   TRP B 259     -20.434  22.854  22.588  1.00 23.65           O  
ANISOU 2294  O   TRP B 259     2612   3103   3270   -110    229   -188       O  
ATOM   2295  CB  TRP B 259     -18.395  21.194  23.764  1.00 23.71           C  
ANISOU 2295  CB  TRP B 259     2602   3029   3377    -75    264   -162       C  
ATOM   2296  CG  TRP B 259     -17.156  20.540  24.300  1.00 25.80           C  
ANISOU 2296  CG  TRP B 259     2842   3252   3707    -58    276   -128       C  
ATOM   2297  CD1 TRP B 259     -15.886  20.655  23.823  1.00 30.11           C  
ANISOU 2297  CD1 TRP B 259     3359   3778   4305    -62    283    -99       C  
ATOM   2298  CD2 TRP B 259     -17.101  19.609  25.400  1.00 25.94           C  
ANISOU 2298  CD2 TRP B 259     2858   3246   3752    -37    284   -109       C  
ATOM   2299  NE1 TRP B 259     -15.034  19.850  24.575  1.00 31.48           N  
ANISOU 2299  NE1 TRP B 259     3507   3912   4540    -43    298    -59       N  
ATOM   2300  CE2 TRP B 259     -15.755  19.215  25.552  1.00 32.58           C  
ANISOU 2300  CE2 TRP B 259     3662   4052   4666    -29    296    -61       C  
ATOM   2301  CE3 TRP B 259     -18.075  19.068  26.268  1.00 26.26           C  
ANISOU 2301  CE3 TRP B 259     2920   3296   3764    -25    282   -122       C  
ATOM   2302  CZ2 TRP B 259     -15.349  18.290  26.542  1.00 35.63           C  
ANISOU 2302  CZ2 TRP B 259     4025   4411   5103    -12    305    -18       C  
ATOM   2303  CZ3 TRP B 259     -17.684  18.163  27.256  1.00 27.96           C  
ANISOU 2303  CZ3 TRP B 259     3115   3487   4021     -9    288    -86       C  
ATOM   2304  CH2 TRP B 259     -16.332  17.766  27.376  1.00 27.68           C  
ANISOU 2304  CH2 TRP B 259     3036   3416   4063     -4    300    -31       C  
ATOM   2305  N   LEU B 260     -19.766  21.896  20.643  1.00 22.12           N  
ANISOU 2305  N   LEU B 260     2385   2934   3085   -177    321   -210       N  
ATOM   2306  CA  LEU B 260     -21.040  22.120  19.938  1.00 21.36           C  
ANISOU 2306  CA  LEU B 260     2294   2895   2928   -214    328   -221       C  
ATOM   2307  C   LEU B 260     -21.687  20.732  19.783  1.00 22.36           C  
ANISOU 2307  C   LEU B 260     2437   3029   3029   -238    401   -260       C  
ATOM   2308  O   LEU B 260     -21.001  19.713  19.783  1.00 27.32           O  
ANISOU 2308  O   LEU B 260     3063   3623   3695   -239    456   -281       O  
ATOM   2309  CB  LEU B 260     -20.758  22.666  18.546  1.00 28.29           C  
ANISOU 2309  CB  LEU B 260     3139   3818   3791   -269    336   -212       C  
ATOM   2310  CG  LEU B 260     -21.325  23.953  18.025  1.00 44.34           C  
ANISOU 2310  CG  LEU B 260     5150   5897   5800   -288    284   -176       C  
ATOM   2311  CD1 LEU B 260     -20.882  25.082  18.944  1.00 48.42           C  
ANISOU 2311  CD1 LEU B 260     5669   6372   6358   -231    213   -146       C  
ATOM   2312  CD2 LEU B 260     -20.751  24.121  16.629  1.00 38.48           C  
ANISOU 2312  CD2 LEU B 260     4371   5199   5049   -351    305   -170       C  
ATOM   2313  N   SER B 261     -23.009  20.697  19.654  1.00 21.39           N  
ANISOU 2313  N   SER B 261     2328   2949   2849   -258    403   -267       N  
ATOM   2314  CA  SER B 261     -23.710  19.411  19.359  1.00 20.45           C  
ANISOU 2314  CA  SER B 261     2226   2847   2696   -293    474   -306       C  
ATOM   2315  C   SER B 261     -23.526  19.004  17.904  1.00 28.72           C  
ANISOU 2315  C   SER B 261     3257   3938   3718   -375    539   -331       C  
ATOM   2316  O   SER B 261     -23.717  19.815  16.993  1.00 25.72           O  
ANISOU 2316  O   SER B 261     2854   3615   3303   -421    518   -310       O  
ATOM   2317  CB  SER B 261     -25.225  19.613  19.573  1.00 20.80           C  
ANISOU 2317  CB  SER B 261     2289   2936   2680   -298    452   -296       C  
ATOM   2318  OG  SER B 261     -25.972  18.493  19.003  1.00 23.70           O  
ANISOU 2318  OG  SER B 261     2669   3336   2999   -351    520   -331       O  
ATOM   2319  N   ARG B 262     -23.166  17.756  17.665  1.00 26.15           N  
ANISOU 2319  N   ARG B 262     2939   3587   3412   -398    621   -376       N  
ATOM   2320  CA  ARG B 262     -23.055  17.301  16.288  1.00 25.23           C  
ANISOU 2320  CA  ARG B 262     2810   3513   3264   -488    695   -413       C  
ATOM   2321  C   ARG B 262     -24.448  17.238  15.710  1.00 25.54           C  
ANISOU 2321  C   ARG B 262     2860   3633   3210   -553    703   -418       C  
ATOM   2322  O   ARG B 262     -24.700  17.756  14.636  1.00 28.86           O  
ANISOU 2322  O   ARG B 262     3260   4128   3577   -627    701   -407       O  
ATOM   2323  CB  ARG B 262     -22.412  15.901  16.273  1.00 37.84           C  
ANISOU 2323  CB  ARG B 262     4414   5050   4914   -495    795   -466       C  
ATOM   2324  CG  ARG B 262     -22.181  15.292  14.866  1.00 40.81           C  
ANISOU 2324  CG  ARG B 262     4782   5459   5265   -597    894   -522       C  
ATOM   2325  CD  ARG B 262     -21.329  13.987  14.880  1.00 48.18           C  
ANISOU 2325  CD  ARG B 262     5716   6311   6280   -594   1000   -572       C  
ATOM   2326  NE  ARG B 262     -20.001  14.115  15.507  1.00 56.72           N  
ANISOU 2326  NE  ARG B 262     6771   7313   7468   -521    988   -540       N  
ATOM   2327  CZ  ARG B 262     -18.896  14.585  14.915  1.00 58.46           C  
ANISOU 2327  CZ  ARG B 262     6963   7524   7725   -532    994   -532       C  
ATOM   2328  NH1 ARG B 262     -18.913  15.024  13.650  1.00 57.17           N  
ANISOU 2328  NH1 ARG B 262     6791   7430   7501   -616   1011   -555       N  
ATOM   2329  NH2 ARG B 262     -17.761  14.638  15.606  1.00 59.03           N  
ANISOU 2329  NH2 ARG B 262     7013   7523   7893   -462    977   -492       N  
ATOM   2330  N   GLN B 263     -25.387  16.622  16.433  1.00 25.10           N  
ANISOU 2330  N   GLN B 263     2834   3569   3133   -529    708   -427       N  
ATOM   2331  CA  GLN B 263     -26.689  16.321  15.806  1.00 33.11           C  
ANISOU 2331  CA  GLN B 263     3860   4662   4058   -603    732   -435       C  
ATOM   2332  C   GLN B 263     -27.589  17.522  15.666  1.00 34.52           C  
ANISOU 2332  C   GLN B 263     4021   4907   4186   -610    653   -371       C  
ATOM   2333  O   GLN B 263     -28.403  17.610  14.728  1.00 29.79           O  
ANISOU 2333  O   GLN B 263     3411   4397   3512   -695    665   -357       O  
ATOM   2334  CB  GLN B 263     -27.447  15.239  16.592  1.00 35.82           C  
ANISOU 2334  CB  GLN B 263     4238   4977   4393   -577    764   -463       C  
ATOM   2335  CG  GLN B 263     -26.840  13.854  16.517  1.00 39.33           C  
ANISOU 2335  CG  GLN B 263     4695   5366   4882   -593    863   -527       C  
ATOM   2336  CD  GLN B 263     -25.933  13.539  17.666  1.00 36.13           C  
ANISOU 2336  CD  GLN B 263     4288   4864   4576   -499    854   -521       C  
ATOM   2337  OE1 GLN B 263     -25.356  14.458  18.308  1.00 26.50           O  
ANISOU 2337  OE1 GLN B 263     3053   3618   3396   -434    778   -476       O  
ATOM   2338  NE2 GLN B 263     -25.770  12.234  17.960  1.00 30.62           N  
ANISOU 2338  NE2 GLN B 263     3600   4110   3924   -493    931   -561       N  
ATOM   2339  N   ARG B 264     -27.503  18.454  16.603  1.00 25.05           N  
ANISOU 2339  N   ARG B 264     2818   3671   3029   -525    576   -328       N  
ATOM   2340  CA  ARG B 264     -28.505  19.530  16.607  1.00 25.30           C  
ANISOU 2340  CA  ARG B 264     2833   3753   3028   -523    511   -266       C  
ATOM   2341  C   ARG B 264     -28.091  20.806  15.914  1.00 27.59           C  
ANISOU 2341  C   ARG B 264     3077   4074   3330   -543    465   -216       C  
ATOM   2342  O   ARG B 264     -28.717  21.848  16.082  1.00 26.67           O  
ANISOU 2342  O   ARG B 264     2940   3977   3218   -523    408   -158       O  
ATOM   2343  CB  ARG B 264     -29.003  19.773  18.061  1.00 26.42           C  
ANISOU 2343  CB  ARG B 264     3000   3842   3198   -430    463   -252       C  
ATOM   2344  CG  ARG B 264     -29.720  18.503  18.631  1.00 28.71           C  
ANISOU 2344  CG  ARG B 264     3328   4121   3458   -423    506   -290       C  
ATOM   2345  CD  ARG B 264     -30.126  18.760  20.079  1.00 26.60           C  
ANISOU 2345  CD  ARG B 264     3082   3807   3217   -336    457   -278       C  
ATOM   2346  NE  ARG B 264     -28.935  18.623  20.927  1.00 23.70           N  
ANISOU 2346  NE  ARG B 264     2723   3366   2918   -278    448   -298       N  
ATOM   2347  CZ  ARG B 264     -28.505  19.540  21.778  1.00 24.96           C  
ANISOU 2347  CZ  ARG B 264     2879   3486   3119   -220    391   -277       C  
ATOM   2348  NH1 ARG B 264     -29.186  20.694  21.923  1.00 28.12           N  
ANISOU 2348  NH1 ARG B 264     3271   3904   3511   -206    343   -241       N  
ATOM   2349  NH2 ARG B 264     -27.405  19.278  22.505  1.00 21.96           N  
ANISOU 2349  NH2 ARG B 264     2502   3048   2793   -181    386   -290       N  
ATOM   2350  N   ASN B 265     -27.016  20.731  15.129  1.00 26.61           N  
ANISOU 2350  N   ASN B 265     2935   3953   3222   -583    493   -237       N  
ATOM   2351  CA  ASN B 265     -26.696  21.845  14.255  1.00 29.01           C  
ANISOU 2351  CA  ASN B 265     3190   4305   3526   -622    454   -188       C  
ATOM   2352  C   ASN B 265     -26.456  21.332  12.849  1.00 30.82           C  
ANISOU 2352  C   ASN B 265     3400   4608   3703   -736    513   -213       C  
ATOM   2353  O   ASN B 265     -25.986  20.202  12.650  1.00 29.37           O  
ANISOU 2353  O   ASN B 265     3241   4403   3514   -764    589   -281       O  
ATOM   2354  CB  ASN B 265     -25.415  22.545  14.706  1.00 30.50           C  
ANISOU 2354  CB  ASN B 265     3370   4426   3792   -556    415   -182       C  
ATOM   2355  CG  ASN B 265     -25.536  23.128  16.084  1.00 30.65           C  
ANISOU 2355  CG  ASN B 265     3408   4377   3861   -457    358   -164       C  
ATOM   2356  OD1 ASN B 265     -26.214  24.165  16.294  1.00 25.72           O  
ANISOU 2356  OD1 ASN B 265     2765   3765   3242   -437    306   -112       O  
ATOM   2357  ND2 ASN B 265     -24.832  22.505  17.038  1.00 24.43           N  
ANISOU 2357  ND2 ASN B 265     2654   3515   3115   -398    371   -203       N  
ATOM   2358  N   THR B 266     -26.701  22.194  11.901  1.00 27.89           N  
ANISOU 2358  N   THR B 266     2980   4318   3300   -801    481   -155       N  
ATOM   2359  CA  THR B 266     -26.380  21.852  10.533  1.00 35.78           C  
ANISOU 2359  CA  THR B 266     3982   5361   4251   -881    505   -172       C  
ATOM   2360  C   THR B 266     -25.637  23.025   9.986  1.00 32.18           C  
ANISOU 2360  C   THR B 266     3475   4926   3826   -887    454   -121       C  
ATOM   2361  O   THR B 266     -26.257  24.005   9.571  1.00 38.62           O  
ANISOU 2361  O   THR B 266     4257   5789   4629   -897    392    -42       O  
ATOM   2362  CB  THR B 266     -27.669  21.646   9.758  1.00 34.45           C  
ANISOU 2362  CB  THR B 266     3835   5253   4002   -929    484   -142       C  
ATOM   2363  OG1 THR B 266     -28.430  20.603  10.411  1.00 33.04           O  
ANISOU 2363  OG1 THR B 266     3703   5052   3800   -916    523   -184       O  
ATOM   2364  CG2 THR B 266     -27.332  21.232   8.342  1.00 39.43           C  
ANISOU 2364  CG2 THR B 266     4485   5917   4580   -999    497   -171       C  
ATOM   2365  N   MET B 267     -24.300  22.971  10.070  1.00 33.01           N  
ANISOU 2365  N   MET B 267     3569   4988   3984   -872    480   -160       N  
ATOM   2366  CA  MET B 267     -23.472  24.150   9.727  1.00 37.96           C  
ANISOU 2366  CA  MET B 267     4144   5626   4652   -867    425   -111       C  
ATOM   2367  C   MET B 267     -22.314  23.772   8.817  1.00 36.22           C  
ANISOU 2367  C   MET B 267     3934   5396   4432   -898    459   -152       C  
ATOM   2368  O   MET B 267     -21.718  22.721   8.990  1.00 38.82           O  
ANISOU 2368  O   MET B 267     4297   5676   4777   -894    531   -226       O  
ATOM   2369  CB  MET B 267     -22.912  24.821  10.989  1.00 33.09           C  
ANISOU 2369  CB  MET B 267     3535   4914   4123   -748    371    -95       C  
ATOM   2370  CG  MET B 267     -23.969  25.418  11.875  1.00 34.03           C  
ANISOU 2370  CG  MET B 267     3661   5016   4255   -688    318    -48       C  
ATOM   2371  SD  MET B 267     -23.167  25.878  13.446  1.00 41.64           S  
ANISOU 2371  SD  MET B 267     4658   5852   5309   -553    272    -58       S  
ATOM   2372  CE  MET B 267     -22.352  27.416  12.952  1.00 35.18           C  
ANISOU 2372  CE  MET B 267     3783   5042   4541   -549    202      5       C  
ATOM   2373  N   SER B 268     -22.026  24.621   7.829  1.00 36.69           N  
ANISOU 2373  N   SER B 268     3964   5497   4477   -926    411   -103       N  
ATOM   2374  CA  SER B 268     -20.894  24.342   6.934  1.00 38.13           C  
ANISOU 2374  CA  SER B 268     4154   5676   4659   -957    441   -141       C  
ATOM   2375  C   SER B 268     -19.602  24.643   7.638  1.00 43.08           C  
ANISOU 2375  C   SER B 268     4750   6244   5373   -909    444   -151       C  
ATOM   2376  O   SER B 268     -19.581  25.376   8.651  1.00 40.36           O  
ANISOU 2376  O   SER B 268     4371   5880   5084   -859    399   -116       O  
ATOM   2377  CB  SER B 268     -20.951  25.195   5.678  1.00 44.52           C  
ANISOU 2377  CB  SER B 268     4938   6550   5425  -1000    386    -84       C  
ATOM   2378  OG  SER B 268     -20.882  26.566   6.022  1.00 40.61           O  
ANISOU 2378  OG  SER B 268     4390   6057   4981   -960    308     -4       O  
ATOM   2379  N   LYS B 269     -18.518  24.080   7.098  1.00 41.16           N  
ANISOU 2379  N   LYS B 269     4520   5976   5144   -926    496   -200       N  
ATOM   2380  CA  LYS B 269     -17.176  24.322   7.607  1.00 40.91           C  
ANISOU 2380  CA  LYS B 269     4458   5890   5195   -885    501   -207       C  
ATOM   2381  C   LYS B 269     -16.891  25.828   7.654  1.00 43.40           C  
ANISOU 2381  C   LYS B 269     4716   6232   5540   -864    403   -128       C  
ATOM   2382  O   LYS B 269     -16.317  26.333   8.624  1.00 46.59           O  
ANISOU 2382  O   LYS B 269     5126   6563   6014   -772    354   -105       O  
ATOM   2383  CB  LYS B 269     -16.147  23.574   6.748  1.00 50.29           C  
ANISOU 2383  CB  LYS B 269     5666   7057   6386   -914    568   -260       C  
ATOM   2384  CG  LYS B 269     -14.707  23.705   7.234  1.00 65.32           C  
ANISOU 2384  CG  LYS B 269     7538   8897   8381   -871    583   -265       C  
ATOM   2385  CD  LYS B 269     -13.732  22.927   6.335  1.00 73.44           C  
ANISOU 2385  CD  LYS B 269     8587   9901   9415   -899    657   -315       C  
ATOM   2386  CE  LYS B 269     -12.292  23.406   6.524  1.00 72.27           C  
ANISOU 2386  CE  LYS B 269     8397   9713   9350   -864    647   -293       C  
ATOM   2387  NZ  LYS B 269     -11.337  22.683   5.640  1.00 74.14           N  
ANISOU 2387  NZ  LYS B 269     8650   9925   9596   -890    721   -338       N  
ATOM   2388  N   LYS B 270     -17.331  26.559   6.641  1.00 40.72           N  
ANISOU 2388  N   LYS B 270     4366   5955   5151   -899    351    -75       N  
ATOM   2389  CA  LYS B 270     -17.203  28.004   6.667  1.00 44.39           C  
ANISOU 2389  CA  LYS B 270     4782   6434   5651   -871    257      6       C  
ATOM   2390  C   LYS B 270     -17.973  28.670   7.820  1.00 36.06           C  
ANISOU 2390  C   LYS B 270     3704   5364   4633   -821    205     51       C  
ATOM   2391  O   LYS B 270     -17.466  29.588   8.474  1.00 37.08           O  
ANISOU 2391  O   LYS B 270     3819   5444   4827   -752    142     89       O  
ATOM   2392  CB  LYS B 270     -17.693  28.595   5.342  1.00 52.61           C  
ANISOU 2392  CB  LYS B 270     5819   7539   6632   -916    220     54       C  
ATOM   2393  CG  LYS B 270     -17.605  30.113   5.301  1.00 61.68           C  
ANISOU 2393  CG  LYS B 270     6922   8691   7823   -882    130    139       C  
ATOM   2394  CD  LYS B 270     -18.133  30.663   3.992  1.00 75.15           C  
ANISOU 2394  CD  LYS B 270     8624  10462   9470   -926    100    188       C  
ATOM   2395  CE  LYS B 270     -18.404  32.154   4.085  1.00 80.07           C  
ANISOU 2395  CE  LYS B 270     9206  11077  10139   -884     19    276       C  
ATOM   2396  NZ  LYS B 270     -19.465  32.565   3.113  1.00 84.81           N  
ANISOU 2396  NZ  LYS B 270     9803  11741  10678   -922     -4    333       N  
ATOM   2397  N   GLU B 271     -19.231  28.274   8.024  1.00 33.33           N  
ANISOU 2397  N   GLU B 271     3381   5038   4245   -832    221     49       N  
ATOM   2398  CA  GLU B 271     -20.013  28.815   9.124  1.00 27.80           C  
ANISOU 2398  CA  GLU B 271     2682   4299   3580   -764    176     85       C  
ATOM   2399  C   GLU B 271     -19.317  28.531  10.475  1.00 27.91           C  
ANISOU 2399  C   GLU B 271     2755   4193   3655   -655    176     40       C  
ATOM   2400  O   GLU B 271     -19.262  29.396  11.344  1.00 29.18           O  
ANISOU 2400  O   GLU B 271     2920   4297   3870   -579    118     72       O  
ATOM   2401  CB  GLU B 271     -21.424  28.191   9.078  1.00 28.19           C  
ANISOU 2401  CB  GLU B 271     2745   4398   3566   -807    210     81       C  
ATOM   2402  CG  GLU B 271     -22.261  28.815   8.000  1.00 41.08           C  
ANISOU 2402  CG  GLU B 271     4366   6086   5154   -844    172    149       C  
ATOM   2403  CD  GLU B 271     -23.564  28.079   7.759  1.00 49.52           C  
ANISOU 2403  CD  GLU B 271     5471   7193   6151   -878    202    142       C  
ATOM   2404  OE1 GLU B 271     -23.601  26.844   7.958  1.00 39.51           O  
ANISOU 2404  OE1 GLU B 271     4249   5917   4848   -897    267     68       O  
ATOM   2405  OE2 GLU B 271     -24.537  28.760   7.382  1.00 54.96           O  
ANISOU 2405  OE2 GLU B 271     6142   7916   6824   -884    160    214       O  
ATOM   2406  N   LEU B 272     -18.759  27.342  10.624  1.00 26.48           N  
ANISOU 2406  N   LEU B 272     2614   3977   3469   -654    243    -30       N  
ATOM   2407  CA  LEU B 272     -18.034  27.010  11.850  1.00 28.86           C  
ANISOU 2407  CA  LEU B 272     2960   4175   3829   -562    243    -59       C  
ATOM   2408  C   LEU B 272     -16.762  27.856  11.993  1.00 34.23           C  
ANISOU 2408  C   LEU B 272     3621   4816   4569   -520    191    -30       C  
ATOM   2409  O   LEU B 272     -16.379  28.216  13.102  1.00 30.61           O  
ANISOU 2409  O   LEU B 272     3185   4286   4158   -443    152    -20       O  
ATOM   2410  CB  LEU B 272     -17.674  25.525  11.899  1.00 33.22           C  
ANISOU 2410  CB  LEU B 272     3547   4697   4377   -573    332   -129       C  
ATOM   2411  CG  LEU B 272     -18.922  24.651  12.007  1.00 36.67           C  
ANISOU 2411  CG  LEU B 272     4013   5159   4762   -601    380   -161       C  
ATOM   2412  CD1 LEU B 272     -18.537  23.266  11.706  1.00 37.25           C  
ANISOU 2412  CD1 LEU B 272     4107   5214   4831   -635    478   -230       C  
ATOM   2413  CD2 LEU B 272     -19.477  24.733  13.441  1.00 31.40           C  
ANISOU 2413  CD2 LEU B 272     3382   4429   4120   -513    342   -152       C  
ATOM   2414  N   GLU B 273     -16.124  28.180  10.867  1.00 32.96           N  
ANISOU 2414  N   GLU B 273     3416   4706   4399   -578    192    -14       N  
ATOM   2415  CA  GLU B 273     -14.971  29.081  10.889  1.00 35.37           C  
ANISOU 2415  CA  GLU B 273     3698   4984   4755   -545    137     22       C  
ATOM   2416  C   GLU B 273     -15.342  30.480  11.325  1.00 30.46           C  
ANISOU 2416  C   GLU B 273     3056   4355   4162   -506     50     84       C  
ATOM   2417  O   GLU B 273     -14.673  31.078  12.189  1.00 33.39           O  
ANISOU 2417  O   GLU B 273     3441   4660   4585   -438      3     99       O  
ATOM   2418  CB  GLU B 273     -14.274  29.087   9.520  1.00 46.36           C  
ANISOU 2418  CB  GLU B 273     5045   6443   6127   -624    160     23       C  
ATOM   2419  CG  GLU B 273     -13.544  27.771   9.249  1.00 59.49           C  
ANISOU 2419  CG  GLU B 273     6731   8083   7791   -647    254    -44       C  
ATOM   2420  CD  GLU B 273     -12.651  27.828   8.012  1.00 74.44           C  
ANISOU 2420  CD  GLU B 273     8582  10027   9673   -717    279    -47       C  
ATOM   2421  OE1 GLU B 273     -12.596  28.907   7.368  1.00 77.91           O  
ANISOU 2421  OE1 GLU B 273     8974  10528  10102   -748    214      7       O  
ATOM   2422  OE2 GLU B 273     -12.010  26.792   7.689  1.00 76.91           O  
ANISOU 2422  OE2 GLU B 273     8908  10320   9996   -742    366   -104       O  
ATOM   2423  N   VAL B 274     -16.404  31.040  10.770  1.00 27.43           N  
ANISOU 2423  N   VAL B 274     2637   4036   3749   -548     29    123       N  
ATOM   2424  CA  VAL B 274     -16.850  32.335  11.213  1.00 35.01           C  
ANISOU 2424  CA  VAL B 274     3575   4978   4751   -509    -40    182       C  
ATOM   2425  C   VAL B 274     -17.178  32.370  12.716  1.00 36.44           C  
ANISOU 2425  C   VAL B 274     3810   5071   4964   -424    -52    160       C  
ATOM   2426  O   VAL B 274     -16.865  33.350  13.431  1.00 32.18           O  
ANISOU 2426  O   VAL B 274     3273   4476   4479   -371   -103    184       O  
ATOM   2427  CB  VAL B 274     -18.065  32.803  10.408  1.00 33.72           C  
ANISOU 2427  CB  VAL B 274     3358   4898   4558   -570    -51    238       C  
ATOM   2428  CG1 VAL B 274     -18.592  34.132  10.965  1.00 37.91           C  
ANISOU 2428  CG1 VAL B 274     3863   5392   5150   -520   -112    301       C  
ATOM   2429  CG2 VAL B 274     -17.699  32.901   8.930  1.00 41.91           C  
ANISOU 2429  CG2 VAL B 274     4334   6033   5558   -664    -49    268       C  
ATOM   2430  N   LEU B 275     -17.829  31.318  13.197  1.00 31.42           N  
ANISOU 2430  N   LEU B 275     3219   4425   4295   -418     -3    114       N  
ATOM   2431  CA  LEU B 275     -18.227  31.277  14.616  1.00 25.93           C  
ANISOU 2431  CA  LEU B 275     2574   3658   3621   -347    -11     91       C  
ATOM   2432  C   LEU B 275     -16.962  31.272  15.472  1.00 28.22           C  
ANISOU 2432  C   LEU B 275     2894   3877   3952   -295    -29     72       C  
ATOM   2433  O   LEU B 275     -16.898  31.962  16.512  1.00 26.76           O  
ANISOU 2433  O   LEU B 275     2730   3637   3801   -244    -68     78       O  
ATOM   2434  CB  LEU B 275     -19.064  30.009  14.894  1.00 23.82           C  
ANISOU 2434  CB  LEU B 275     2345   3400   3307   -356     47     46       C  
ATOM   2435  CG  LEU B 275     -19.307  29.614  16.359  1.00 24.28           C  
ANISOU 2435  CG  LEU B 275     2459   3389   3378   -291     50     12       C  
ATOM   2436  CD1 LEU B 275     -20.070  30.765  17.051  1.00 26.16           C  
ANISOU 2436  CD1 LEU B 275     2695   3601   3644   -254      4     42       C  
ATOM   2437  CD2 LEU B 275     -20.082  28.267  16.475  1.00 26.61           C  
ANISOU 2437  CD2 LEU B 275     2785   3699   3625   -306    110    -31       C  
ATOM   2438  N   SER B 276     -15.959  30.508  15.026  1.00 24.62           N  
ANISOU 2438  N   SER B 276     2438   3425   3493   -314      3     51       N  
ATOM   2439  CA  SER B 276     -14.658  30.471  15.729  1.00 30.69           C  
ANISOU 2439  CA  SER B 276     3224   4134   4303   -271    -13     48       C  
ATOM   2440  C   SER B 276     -13.997  31.852  15.812  1.00 34.37           C  
ANISOU 2440  C   SER B 276     3668   4584   4808   -253    -84     92       C  
ATOM   2441  O   SER B 276     -13.462  32.243  16.872  1.00 30.08           O  
ANISOU 2441  O   SER B 276     3150   3986   4295   -208   -119     96       O  
ATOM   2442  CB  SER B 276     -13.715  29.461  15.039  1.00 32.48           C  
ANISOU 2442  CB  SER B 276     3442   4370   4530   -300     42     27       C  
ATOM   2443  OG  SER B 276     -12.405  29.596  15.569  1.00 37.53           O  
ANISOU 2443  OG  SER B 276     4085   4960   5216   -264     18     44       O  
ATOM   2444  N   GLN B 277     -14.074  32.598  14.717  1.00 33.64           N  
ANISOU 2444  N   GLN B 277     3525   4543   4714   -292   -105    128       N  
ATOM   2445  CA  GLN B 277     -13.455  33.936  14.646  1.00 34.72           C  
ANISOU 2445  CA  GLN B 277     3633   4668   4893   -280   -171    174       C  
ATOM   2446  C   GLN B 277     -14.236  34.900  15.484  1.00 32.50           C  
ANISOU 2446  C   GLN B 277     3362   4349   4638   -245   -207    187       C  
ATOM   2447  O   GLN B 277     -13.692  35.840  16.038  1.00 32.78           O  
ANISOU 2447  O   GLN B 277     3400   4340   4714   -216   -253    204       O  
ATOM   2448  CB  GLN B 277     -13.416  34.416  13.190  1.00 38.40           C  
ANISOU 2448  CB  GLN B 277     4033   5207   5349   -338   -182    214       C  
ATOM   2449  CG  GLN B 277     -12.471  33.553  12.329  1.00 48.68           C  
ANISOU 2449  CG  GLN B 277     5325   6543   6629   -378   -142    195       C  
ATOM   2450  CD  GLN B 277     -12.599  33.812  10.824  1.00 61.24           C  
ANISOU 2450  CD  GLN B 277     6852   8225   8191   -456   -140    225       C  
ATOM   2451  OE1 GLN B 277     -13.324  34.709  10.386  1.00 69.48           O  
ANISOU 2451  OE1 GLN B 277     7852   9310   9236   -480   -178    274       O  
ATOM   2452  NE2 GLN B 277     -11.900  33.011  10.030  1.00 64.73           N  
ANISOU 2452  NE2 GLN B 277     7287   8701   8609   -501    -92    197       N  
ATOM   2453  N   LYS B 278     -15.544  34.700  15.567  1.00 27.95           N  
ANISOU 2453  N   LYS B 278     2790   3788   4041   -251   -183    179       N  
ATOM   2454  CA  LYS B 278     -16.347  35.565  16.414  1.00 30.55           C  
ANISOU 2454  CA  LYS B 278     3131   4074   4404   -216   -204    187       C  
ATOM   2455  C   LYS B 278     -16.015  35.332  17.862  1.00 27.30           C  
ANISOU 2455  C   LYS B 278     2781   3594   3997   -169   -205    143       C  
ATOM   2456  O   LYS B 278     -15.844  36.287  18.595  1.00 29.91           O  
ANISOU 2456  O   LYS B 278     3122   3875   4366   -144   -237    146       O  
ATOM   2457  CB  LYS B 278     -17.870  35.339  16.188  1.00 41.18           C  
ANISOU 2457  CB  LYS B 278     4465   5455   5727   -232   -174    194       C  
ATOM   2458  CG  LYS B 278     -18.380  35.733  14.802  1.00 42.17           C  
ANISOU 2458  CG  LYS B 278     4519   5658   5847   -289   -179    255       C  
ATOM   2459  CD  LYS B 278     -18.205  37.213  14.585  1.00 43.30           C  
ANISOU 2459  CD  LYS B 278     4609   5783   6059   -281   -229    315       C  
ATOM   2460  CE  LYS B 278     -18.759  37.631  13.228  1.00 46.24           C  
ANISOU 2460  CE  LYS B 278     4899   6242   6430   -343   -239    391       C  
ATOM   2461  NZ  LYS B 278     -18.586  39.088  13.066  1.00 44.51           N  
ANISOU 2461  NZ  LYS B 278     4622   5997   6291   -330   -287    456       N  
ATOM   2462  N   LEU B 279     -15.931  34.071  18.278  1.00 26.38           N  
ANISOU 2462  N   LEU B 279     2704   3477   3843   -165   -168    103       N  
ATOM   2463  CA  LEU B 279     -15.600  33.746  19.666  1.00 27.29           C  
ANISOU 2463  CA  LEU B 279     2872   3539   3958   -130   -171     69       C  
ATOM   2464  C   LEU B 279     -14.202  34.324  20.006  1.00 32.94           C  
ANISOU 2464  C   LEU B 279     3588   4223   4703   -120   -214     87       C  
ATOM   2465  O   LEU B 279     -13.965  34.912  21.074  1.00 31.59           O  
ANISOU 2465  O   LEU B 279     3446   4010   4547   -102   -242     78       O  
ATOM   2466  CB  LEU B 279     -15.611  32.210  19.834  1.00 27.02           C  
ANISOU 2466  CB  LEU B 279     2863   3515   3888   -131   -122     38       C  
ATOM   2467  CG  LEU B 279     -17.064  31.687  19.709  1.00 32.72           C  
ANISOU 2467  CG  LEU B 279     3592   4263   4576   -140    -84     18       C  
ATOM   2468  CD1 LEU B 279     -16.998  30.216  19.541  1.00 36.02           C  
ANISOU 2468  CD1 LEU B 279     4024   4697   4964   -152    -32    -10       C  
ATOM   2469  CD2 LEU B 279     -17.798  32.022  20.968  1.00 42.52           C  
ANISOU 2469  CD2 LEU B 279     4870   5466   5818   -108    -95     -2       C  
ATOM   2470  N   ARG B 280     -13.282  34.186  19.073  1.00 27.65           N  
ANISOU 2470  N   ARG B 280     2887   3580   4041   -139   -218    112       N  
ATOM   2471  CA  ARG B 280     -11.921  34.757  19.278  1.00 32.16           C  
ANISOU 2471  CA  ARG B 280     3453   4127   4639   -132   -261    138       C  
ATOM   2472  C   ARG B 280     -11.996  36.267  19.464  1.00 33.30           C  
ANISOU 2472  C   ARG B 280     3587   4249   4818   -127   -310    157       C  
ATOM   2473  O   ARG B 280     -11.243  36.877  20.252  1.00 30.97           O  
ANISOU 2473  O   ARG B 280     3311   3916   4540   -117   -347    162       O  
ATOM   2474  CB  ARG B 280     -11.065  34.416  18.059  1.00 31.22           C  
ANISOU 2474  CB  ARG B 280     3293   4045   4523   -157   -252    162       C  
ATOM   2475  CG  ARG B 280      -9.583  34.797  18.141  1.00 41.48           C  
ANISOU 2475  CG  ARG B 280     4584   5327   5851   -151   -291    195       C  
ATOM   2476  CD  ARG B 280      -8.884  34.440  16.817  1.00 43.64           C  
ANISOU 2476  CD  ARG B 280     4814   5641   6126   -179   -272    214       C  
ATOM   2477  NE  ARG B 280      -7.503  34.902  16.736  1.00 43.54           N  
ANISOU 2477  NE  ARG B 280     4785   5617   6142   -175   -311    253       N  
ATOM   2478  CZ  ARG B 280      -7.141  36.055  16.179  1.00 51.05           C  
ANISOU 2478  CZ  ARG B 280     5704   6582   7112   -185   -363    288       C  
ATOM   2479  NH1 ARG B 280      -8.063  36.863  15.673  1.00 54.69           N  
ANISOU 2479  NH1 ARG B 280     6140   7067   7572   -199   -379    294       N  
ATOM   2480  NH2 ARG B 280      -5.862  36.408  16.145  1.00 56.40           N  
ANISOU 2480  NH2 ARG B 280     6369   7250   7812   -180   -398    325       N  
ATOM   2481  N   ALA B 281     -12.910  36.918  18.753  1.00 35.25           N  
ANISOU 2481  N   ALA B 281     3800   4516   5079   -138   -310    173       N  
ATOM   2482  CA  ALA B 281     -12.969  38.370  18.887  1.00 35.38           C  
ANISOU 2482  CA  ALA B 281     3798   4502   5145   -131   -349    196       C  
ATOM   2483  C   ALA B 281     -13.495  38.738  20.249  1.00 34.80           C  
ANISOU 2483  C   ALA B 281     3772   4370   5079   -108   -344    157       C  
ATOM   2484  O   ALA B 281     -13.135  39.773  20.797  1.00 32.54           O  
ANISOU 2484  O   ALA B 281     3494   4040   4829   -103   -372    158       O  
ATOM   2485  CB  ALA B 281     -13.831  39.012  17.753  1.00 38.28           C  
ANISOU 2485  CB  ALA B 281     4101   4905   5537   -150   -349    239       C  
ATOM   2486  N   LEU B 282     -14.367  37.906  20.801  1.00 27.04           N  
ANISOU 2486  N   LEU B 282     2823   3389   4063   -100   -306    121       N  
ATOM   2487  CA  LEU B 282     -14.912  38.131  22.154  1.00 33.31           C  
ANISOU 2487  CA  LEU B 282     3665   4134   4856    -84   -295     77       C  
ATOM   2488  C   LEU B 282     -13.910  37.856  23.269  1.00 29.83           C  
ANISOU 2488  C   LEU B 282     3272   3672   4392    -86   -313     54       C  
ATOM   2489  O   LEU B 282     -14.176  38.194  24.436  1.00 34.27           O  
ANISOU 2489  O   LEU B 282     3875   4197   4949    -86   -310     16       O  
ATOM   2490  CB  LEU B 282     -16.058  37.158  22.440  1.00 27.31           C  
ANISOU 2490  CB  LEU B 282     2928   3390   4059    -76   -251     47       C  
ATOM   2491  CG  LEU B 282     -17.308  37.359  21.594  1.00 32.73           C  
ANISOU 2491  CG  LEU B 282     3574   4100   4760    -78   -227     70       C  
ATOM   2492  CD1 LEU B 282     -18.357  36.227  21.903  1.00 34.11           C  
ANISOU 2492  CD1 LEU B 282     3776   4296   4887    -73   -184     39       C  
ATOM   2493  CD2 LEU B 282     -17.878  38.747  21.809  1.00 35.13           C  
ANISOU 2493  CD2 LEU B 282     3860   4358   5129    -68   -232     81       C  
ATOM   2494  N   MET B 283     -12.826  37.164  22.924  1.00 28.80           N  
ANISOU 2494  N   MET B 283     3134   3566   4244    -93   -327     77       N  
ATOM   2495  CA  MET B 283     -11.847  36.717  23.951  1.00 29.48           C  
ANISOU 2495  CA  MET B 283     3254   3642   4307    -99   -344     73       C  
ATOM   2496  C   MET B 283     -10.442  37.106  23.472  1.00 32.30           C  
ANISOU 2496  C   MET B 283     3586   4004   4684   -109   -384    119       C  
ATOM   2497  O   MET B 283      -9.738  36.289  22.854  1.00 30.25           O  
ANISOU 2497  O   MET B 283     3304   3769   4421   -109   -377    147       O  
ATOM   2498  CB  MET B 283     -11.928  35.189  24.107  1.00 30.46           C  
ANISOU 2498  CB  MET B 283     3388   3789   4398    -93   -309     66       C  
ATOM   2499  CG  MET B 283     -13.226  34.715  24.780  1.00 31.22           C  
ANISOU 2499  CG  MET B 283     3514   3881   4467    -85   -274     22       C  
ATOM   2500  SD  MET B 283     -13.305  32.898  24.903  1.00 37.11           S  
ANISOU 2500  SD  MET B 283     4266   4650   5182    -78   -232     18       S  
ATOM   2501  CE  MET B 283     -13.861  32.480  23.262  1.00 38.67           C  
ANISOU 2501  CE  MET B 283     4426   4883   5386    -79   -193     23       C  
ATOM   2502  N   PRO B 284     -10.062  38.366  23.686  1.00 30.52           N  
ANISOU 2502  N   PRO B 284     3361   3752   4484   -119   -421    125       N  
ATOM   2503  CA  PRO B 284      -8.828  38.898  23.116  1.00 30.64           C  
ANISOU 2503  CA  PRO B 284     3349   3773   4521   -127   -463    172       C  
ATOM   2504  C   PRO B 284      -7.560  38.149  23.560  1.00 30.11           C  
ANISOU 2504  C   PRO B 284     3291   3718   4432   -137   -481    203       C  
ATOM   2505  O   PRO B 284      -6.520  38.271  22.918  1.00 31.49           O  
ANISOU 2505  O   PRO B 284     3436   3905   4623   -140   -507    248       O  
ATOM   2506  CB  PRO B 284      -8.772  40.309  23.701  1.00 31.59           C  
ANISOU 2506  CB  PRO B 284     3485   3853   4666   -140   -493    159       C  
ATOM   2507  CG  PRO B 284     -10.246  40.696  23.877  1.00 34.47           C  
ANISOU 2507  CG  PRO B 284     3857   4192   5047   -129   -456    116       C  
ATOM   2508  CD  PRO B 284     -10.880  39.419  24.339  1.00 33.62           C  
ANISOU 2508  CD  PRO B 284     3776   4104   4894   -121   -418     88       C  
ATOM   2509  N   TYR B 285      -7.659  37.422  24.658  1.00 28.21           N  
ANISOU 2509  N   TYR B 285     3085   3475   4159   -143   -467    185       N  
ATOM   2510  CA  TYR B 285      -6.553  36.557  25.147  1.00 32.28           C  
ANISOU 2510  CA  TYR B 285     3599   4004   4660   -153   -478    228       C  
ATOM   2511  C   TYR B 285      -6.434  35.231  24.422  1.00 33.90           C  
ANISOU 2511  C   TYR B 285     3775   4228   4876   -133   -436    247       C  
ATOM   2512  O   TYR B 285      -5.427  34.523  24.560  1.00 31.78           O  
ANISOU 2512  O   TYR B 285     3491   3966   4618   -135   -437    295       O  
ATOM   2513  CB  TYR B 285      -6.757  36.277  26.632  1.00 28.14           C  
ANISOU 2513  CB  TYR B 285     3116   3477   4098   -175   -480    209       C  
ATOM   2514  CG  TYR B 285      -8.115  35.720  26.968  1.00 33.57           C  
ANISOU 2514  CG  TYR B 285     3826   4163   4766   -162   -436    154       C  
ATOM   2515  CD1 TYR B 285      -9.137  36.549  27.453  1.00 32.97           C  
ANISOU 2515  CD1 TYR B 285     3781   4066   4681   -168   -429     97       C  
ATOM   2516  CD2 TYR B 285      -8.379  34.353  26.828  1.00 32.89           C  
ANISOU 2516  CD2 TYR B 285     3729   4092   4676   -143   -396    160       C  
ATOM   2517  CE1 TYR B 285     -10.396  36.015  27.778  1.00 29.89           C  
ANISOU 2517  CE1 TYR B 285     3410   3674   4271   -154   -388     51       C  
ATOM   2518  CE2 TYR B 285      -9.610  33.828  27.135  1.00 29.38           C  
ANISOU 2518  CE2 TYR B 285     3305   3648   4211   -132   -358    113       C  
ATOM   2519  CZ  TYR B 285     -10.611  34.639  27.596  1.00 29.76           C  
ANISOU 2519  CZ  TYR B 285     3383   3680   4244   -136   -356     61       C  
ATOM   2520  OH  TYR B 285     -11.844  34.082  27.889  1.00 33.53           O  
ANISOU 2520  OH  TYR B 285     3879   4160   4701   -123   -318     19       O  
ATOM   2521  N   ALA B 286      -7.480  34.840  23.685  1.00 29.48           N  
ANISOU 2521  N   ALA B 286     3208   3676   4317   -117   -392    212       N  
ATOM   2522  CA  ALA B 286      -7.427  33.571  22.967  1.00 24.61           C  
ANISOU 2522  CA  ALA B 286     2568   3075   3708   -106   -341    218       C  
ATOM   2523  C   ALA B 286      -6.734  33.781  21.643  1.00 28.58           C  
ANISOU 2523  C   ALA B 286     3028   3593   4236   -110   -342    246       C  
ATOM   2524  O   ALA B 286      -7.112  34.662  20.876  1.00 33.87           O  
ANISOU 2524  O   ALA B 286     3682   4276   4910   -116   -358    239       O  
ATOM   2525  CB  ALA B 286      -8.840  33.061  22.707  1.00 26.68           C  
ANISOU 2525  CB  ALA B 286     2840   3346   3950    -99   -293    168       C  
ATOM   2526  N   ASP B 287      -5.731  32.962  21.354  1.00 25.59           N  
ANISOU 2526  N   ASP B 287     2626   3216   3882   -108   -321    281       N  
ATOM   2527  CA  ASP B 287      -5.026  33.032  20.080  1.00 29.48           C  
ANISOU 2527  CA  ASP B 287     3078   3726   4398   -115   -312    304       C  
ATOM   2528  C   ASP B 287      -5.866  32.332  19.010  1.00 31.99           C  
ANISOU 2528  C   ASP B 287     3381   4068   4705   -126   -247    262       C  
ATOM   2529  O   ASP B 287      -5.884  32.732  17.850  1.00 31.51           O  
ANISOU 2529  O   ASP B 287     3290   4038   4643   -145   -245    261       O  
ATOM   2530  CB  ASP B 287      -3.674  32.324  20.228  1.00 29.26           C  
ANISOU 2530  CB  ASP B 287     3028   3682   4406   -110   -301    357       C  
ATOM   2531  CG  ASP B 287      -2.702  33.113  21.101  1.00 30.32           C  
ANISOU 2531  CG  ASP B 287     3169   3805   4545   -112   -372    411       C  
ATOM   2532  OD1 ASP B 287      -2.793  34.378  21.125  1.00 31.05           O  
ANISOU 2532  OD1 ASP B 287     3272   3903   4623   -121   -429    408       O  
ATOM   2533  OD2 ASP B 287      -1.852  32.450  21.759  1.00 33.93           O  
ANISOU 2533  OD2 ASP B 287     3618   4249   5025   -109   -368    462       O  
ATOM   2534  N   SER B 288      -6.555  31.262  19.393  1.00 37.43           N  
ANISOU 2534  N   SER B 288     4088   4749   5383   -120   -193    229       N  
ATOM   2535  CA  SER B 288      -7.563  30.682  18.496  1.00 36.27           C  
ANISOU 2535  CA  SER B 288     3936   4631   5214   -138   -135    183       C  
ATOM   2536  C   SER B 288      -8.622  29.976  19.331  1.00 32.94           C  
ANISOU 2536  C   SER B 288     3549   4197   4769   -126   -105    147       C  
ATOM   2537  O   SER B 288      -8.454  29.800  20.536  1.00 31.13           O  
ANISOU 2537  O   SER B 288     3342   3939   4545   -105   -124    159       O  
ATOM   2538  CB  SER B 288      -6.959  29.674  17.523  1.00 34.97           C  
ANISOU 2538  CB  SER B 288     3743   4473   5072   -156    -65    178       C  
ATOM   2539  OG  SER B 288      -6.360  28.633  18.240  1.00 39.11           O  
ANISOU 2539  OG  SER B 288     4271   4956   5633   -135    -27    193       O  
ATOM   2540  N   VAL B 289      -9.738  29.596  18.704  1.00 31.61           N  
ANISOU 2540  N   VAL B 289     3384   4057   4571   -144    -63    106       N  
ATOM   2541  CA  VAL B 289     -10.796  28.932  19.461  1.00 28.63           C  
ANISOU 2541  CA  VAL B 289     3039   3671   4169   -132    -36     72       C  
ATOM   2542  C   VAL B 289     -11.171  27.676  18.724  1.00 31.42           C  
ANISOU 2542  C   VAL B 289     3385   4038   4514   -154     46     38       C  
ATOM   2543  O   VAL B 289     -11.483  27.739  17.547  1.00 34.66           O  
ANISOU 2543  O   VAL B 289     3776   4490   4903   -192     72     22       O  
ATOM   2544  CB  VAL B 289     -12.045  29.815  19.528  1.00 33.43           C  
ANISOU 2544  CB  VAL B 289     3660   4298   4742   -135    -67     56       C  
ATOM   2545  CG1 VAL B 289     -13.207  28.980  20.085  1.00 28.42           C  
ANISOU 2545  CG1 VAL B 289     3056   3664   4079   -128    -29     18       C  
ATOM   2546  CG2 VAL B 289     -11.779  31.037  20.410  1.00 26.33           C  
ANISOU 2546  CG2 VAL B 289     2774   3374   3855   -115   -137     77       C  
ATOM   2547  N   ASN B 290     -11.102  26.540  19.399  1.00 27.48           N  
ANISOU 2547  N   ASN B 290     2899   3508   4032   -137     90     29       N  
ATOM   2548  CA  ASN B 290     -11.293  25.273  18.698  1.00 26.44           C  
ANISOU 2548  CA  ASN B 290     2760   3379   3905   -160    180     -7       C  
ATOM   2549  C   ASN B 290     -12.772  24.923  18.803  1.00 26.95           C  
ANISOU 2549  C   ASN B 290     2852   3467   3919   -170    201    -49       C  
ATOM   2550  O   ASN B 290     -13.358  25.121  19.856  1.00 36.50           O  
ANISOU 2550  O   ASN B 290     4088   4666   5114   -142    164    -46       O  
ATOM   2551  CB  ASN B 290     -10.443  24.226  19.394  1.00 32.58           C  
ANISOU 2551  CB  ASN B 290     3530   4104   4743   -134    218     15       C  
ATOM   2552  CG  ASN B 290     -10.544  22.841  18.739  1.00 55.77           C  
ANISOU 2552  CG  ASN B 290     6459   7029   7704   -155    325    -25       C  
ATOM   2553  OD1 ASN B 290     -11.147  22.679  17.678  1.00 60.62           O  
ANISOU 2553  OD1 ASN B 290     7073   7679   8280   -199    371    -72       O  
ATOM   2554  ND2 ASN B 290      -9.916  21.842  19.368  1.00 63.27           N  
ANISOU 2554  ND2 ASN B 290     7395   7926   8720   -130    368     -1       N  
ATOM   2555  N   ILE B 291     -13.388  24.412  17.737  1.00 29.17           N  
ANISOU 2555  N   ILE B 291     3128   3786   4170   -215    261    -88       N  
ATOM   2556  CA  ILE B 291     -14.790  24.014  17.833  1.00 22.15           C  
ANISOU 2556  CA  ILE B 291     2263   2922   3229   -228    282   -122       C  
ATOM   2557  C   ILE B 291     -14.792  22.480  17.747  1.00 30.37           C  
ANISOU 2557  C   ILE B 291     3312   3940   4289   -240    375   -160       C  
ATOM   2558  O   ILE B 291     -14.267  21.921  16.805  1.00 32.10           O  
ANISOU 2558  O   ILE B 291     3511   4162   4523   -278    441   -182       O  
ATOM   2559  CB  ILE B 291     -15.644  24.639  16.738  1.00 27.33           C  
ANISOU 2559  CB  ILE B 291     2907   3648   3830   -280    276   -130       C  
ATOM   2560  CG1 ILE B 291     -15.784  26.140  16.955  1.00 32.38           C  
ANISOU 2560  CG1 ILE B 291     3537   4300   4467   -262    188    -88       C  
ATOM   2561  CG2 ILE B 291     -17.074  24.006  16.730  1.00 31.83           C  
ANISOU 2561  CG2 ILE B 291     3499   4248   4346   -303    311   -162       C  
ATOM   2562  CD1 ILE B 291     -16.640  26.845  15.933  1.00 40.16           C  
ANISOU 2562  CD1 ILE B 291     4497   5353   5408   -311    174    -75       C  
ATOM   2563  N   THR B 292     -15.311  21.805  18.761  1.00 27.81           N  
ANISOU 2563  N   THR B 292     3012   3587   3969   -208    384   -167       N  
ATOM   2564  CA  THR B 292     -15.355  20.354  18.713  1.00 29.41           C  
ANISOU 2564  CA  THR B 292     3217   3762   4197   -217    474   -200       C  
ATOM   2565  C   THR B 292     -16.806  19.933  18.672  1.00 30.77           C  
ANISOU 2565  C   THR B 292     3416   3968   4305   -239    496   -239       C  
ATOM   2566  O   THR B 292     -17.611  20.469  19.437  1.00 31.75           O  
ANISOU 2566  O   THR B 292     3561   4106   4395   -212    436   -226       O  
ATOM   2567  CB  THR B 292     -14.659  19.750  19.930  1.00 35.40           C  
ANISOU 2567  CB  THR B 292     3970   4458   5024   -164    471   -166       C  
ATOM   2568  OG1 THR B 292     -13.268  20.079  19.870  1.00 40.76           O  
ANISOU 2568  OG1 THR B 292     4618   5107   5762   -151    457   -123       O  
ATOM   2569  CG2 THR B 292     -14.803  18.212  19.931  1.00 36.09           C  
ANISOU 2569  CG2 THR B 292     4055   4508   5149   -170    569   -196       C  
ATOM   2570  N   LEU B 293     -17.151  19.015  17.764  1.00 24.30           N  
ANISOU 2570  N   LEU B 293     2598   3165   3469   -292    584   -288       N  
ATOM   2571  CA  LEU B 293     -18.514  18.523  17.668  1.00 30.48           C  
ANISOU 2571  CA  LEU B 293     3408   3986   4189   -320    609   -323       C  
ATOM   2572  C   LEU B 293     -18.643  17.368  18.633  1.00 38.62           C  
ANISOU 2572  C   LEU B 293     4453   4962   5260   -282    648   -333       C  
ATOM   2573  O   LEU B 293     -17.825  16.445  18.610  1.00 39.13           O  
ANISOU 2573  O   LEU B 293     4501   4972   5394   -277    718   -343       O  
ATOM   2574  CB  LEU B 293     -18.795  18.051  16.233  1.00 32.56           C  
ANISOU 2574  CB  LEU B 293     3665   4298   4409   -409    689   -372       C  
ATOM   2575  CG  LEU B 293     -18.673  19.158  15.186  1.00 36.92           C  
ANISOU 2575  CG  LEU B 293     4194   4916   4919   -458    651   -355       C  
ATOM   2576  CD1 LEU B 293     -19.235  18.684  13.844  1.00 44.21           C  
ANISOU 2576  CD1 LEU B 293     5113   5908   5774   -563    724   -402       C  
ATOM   2577  CD2 LEU B 293     -19.370  20.417  15.630  1.00 37.82           C  
ANISOU 2577  CD2 LEU B 293     4308   5064   4996   -429    549   -305       C  
ATOM   2578  N   MET B 294     -19.638  17.416  19.509  1.00 28.16           N  
ANISOU 2578  N   MET B 294     3153   3648   3899   -253    606   -326       N  
ATOM   2579  CA  MET B 294     -19.789  16.374  20.513  1.00 25.16           C  
ANISOU 2579  CA  MET B 294     2782   3221   3555   -215    631   -327       C  
ATOM   2580  C   MET B 294     -21.061  15.639  20.205  1.00 24.42           C  
ANISOU 2580  C   MET B 294     2714   3160   3403   -251    678   -371       C  
ATOM   2581  O   MET B 294     -22.023  16.215  19.768  1.00 25.71           O  
ANISOU 2581  O   MET B 294     2893   3384   3491   -281    651   -378       O  
ATOM   2582  CB  MET B 294     -19.863  16.923  21.939  1.00 22.21           C  
ANISOU 2582  CB  MET B 294     2417   2834   3188   -154    544   -283       C  
ATOM   2583  CG  MET B 294     -18.633  17.774  22.313  1.00 28.15           C  
ANISOU 2583  CG  MET B 294     3147   3562   3987   -126    488   -235       C  
ATOM   2584  SD  MET B 294     -17.124  16.804  22.410  1.00 36.06           S  
ANISOU 2584  SD  MET B 294     4107   4495   5098   -111    547   -207       S  
ATOM   2585  CE  MET B 294     -17.493  15.700  23.749  1.00 40.39           C  
ANISOU 2585  CE  MET B 294     4655   5011   5679    -75    557   -187       C  
ATOM   2586  N   ASP B 295     -21.041  14.342  20.472  1.00 23.95           N  
ANISOU 2586  N   ASP B 295     3043   3162   2895     70    283   -340       N  
ATOM   2587  CA  ASP B 295     -22.192  13.512  20.128  1.00 23.48           C  
ANISOU 2587  CA  ASP B 295     3009   3111   2801     50    273   -314       C  
ATOM   2588  C   ASP B 295     -23.218  13.606  21.269  1.00 21.59           C  
ANISOU 2588  C   ASP B 295     2802   2846   2554     64    248   -257       C  
ATOM   2589  O   ASP B 295     -22.863  13.383  22.429  1.00 22.39           O  
ANISOU 2589  O   ASP B 295     2917   2905   2684     96    219   -268       O  
ATOM   2590  CB  ASP B 295     -21.714  12.057  20.063  1.00 24.54           C  
ANISOU 2590  CB  ASP B 295     3154   3218   2953     62    251   -373       C  
ATOM   2591  CG  ASP B 295     -22.776  11.126  19.523  1.00 26.91           C  
ANISOU 2591  CG  ASP B 295     3480   3529   3215     30    246   -360       C  
ATOM   2592  OD1 ASP B 295     -23.998  11.404  19.658  1.00 27.86           O  
ANISOU 2592  OD1 ASP B 295     3617   3667   3300     11    243   -297       O  
ATOM   2593  OD2 ASP B 295     -22.401  10.092  18.919  1.00 35.83           O  
ANISOU 2593  OD2 ASP B 295     4612   4651   4351     22    249   -415       O  
ATOM   2594  N   ASP B 296     -24.468  13.948  20.957  1.00 23.12           N  
ANISOU 2594  N   ASP B 296     3004   3070   2710     39    260   -195       N  
ATOM   2595  CA  ASP B 296     -25.467  14.052  22.012  1.00 22.96           C  
ANISOU 2595  CA  ASP B 296     3012   3030   2683     51    241   -142       C  
ATOM   2596  C   ASP B 296     -25.628  12.742  22.734  1.00 23.42           C  
ANISOU 2596  C   ASP B 296     3103   3051   2746     64    199   -162       C  
ATOM   2597  O   ASP B 296     -25.989  12.704  23.895  1.00 23.60           O  
ANISOU 2597  O   ASP B 296     3148   3045   2776     83    176   -140       O  
ATOM   2598  CB  ASP B 296     -26.825  14.446  21.426  1.00 24.42           C  
ANISOU 2598  CB  ASP B 296     3195   3260   2823     22    259    -73       C  
ATOM   2599  CG  ASP B 296     -26.826  15.823  20.856  1.00 30.12           C  
ANISOU 2599  CG  ASP B 296     3888   4014   3543     15    300    -35       C  
ATOM   2600  OD1 ASP B 296     -25.889  16.629  21.111  1.00 25.30           O  
ANISOU 2600  OD1 ASP B 296     3264   3382   2965     32    316    -58       O  
ATOM   2601  OD2 ASP B 296     -27.787  16.105  20.112  1.00 26.76           O  
ANISOU 2601  OD2 ASP B 296     3452   3636   3081    -10    317     21       O  
ATOM   2602  N   VAL B 297     -25.409  11.636  22.032  1.00 20.60           N  
ANISOU 2602  N   VAL B 297     2749   2693   2383     49    193   -204       N  
ATOM   2603  CA  VAL B 297     -25.435  10.327  22.715  1.00 24.41           C  
ANISOU 2603  CA  VAL B 297     3264   3129   2880     64    155   -226       C  
ATOM   2604  C   VAL B 297     -24.417  10.174  23.825  1.00 26.01           C  
ANISOU 2604  C   VAL B 297     3470   3283   3131    110    128   -255       C  
ATOM   2605  O   VAL B 297     -24.670   9.552  24.878  1.00 26.20           O  
ANISOU 2605  O   VAL B 297     3523   3269   3164    129     92   -241       O  
ATOM   2606  CB  VAL B 297     -25.319   9.190  21.661  1.00 24.60           C  
ANISOU 2606  CB  VAL B 297     3293   3157   2896     38    162   -273       C  
ATOM   2607  CG1 VAL B 297     -25.268   7.811  22.343  1.00 25.19           C  
ANISOU 2607  CG1 VAL B 297     3404   3171   2994     56    128   -297       C  
ATOM   2608  CG2 VAL B 297     -26.492   9.293  20.773  1.00 28.32           C  
ANISOU 2608  CG2 VAL B 297     3765   3684   3311    -13    181   -235       C  
ATOM   2609  N   THR B 298     -23.270  10.804  23.638  1.00 23.11           N  
ANISOU 2609  N   THR B 298     3070   2921   2791    126    143   -290       N  
ATOM   2610  CA  THR B 298     -22.276  10.820  24.695  1.00 28.81           C  
ANISOU 2610  CA  THR B 298     3784   3609   3552    167    117   -313       C  
ATOM   2611  C   THR B 298     -22.712  11.706  25.868  1.00 25.77           C  
ANISOU 2611  C   THR B 298     3409   3221   3160    174    107   -268       C  
ATOM   2612  O   THR B 298     -22.553  11.323  27.026  1.00 27.90           O  
ANISOU 2612  O   THR B 298     3695   3462   3444    198     71   -264       O  
ATOM   2613  CB  THR B 298     -20.935  11.383  24.156  1.00 31.76           C  
ANISOU 2613  CB  THR B 298     4114   3999   3953    176    140   -363       C  
ATOM   2614  OG1 THR B 298     -20.439  10.506  23.144  1.00 37.69           O  
ANISOU 2614  OG1 THR B 298     4854   4751   4715    172    150   -414       O  
ATOM   2615  CG2 THR B 298     -19.935  11.506  25.273  1.00 31.55           C  
ANISOU 2615  CG2 THR B 298     4074   3950   3962    212    112   -382       C  
ATOM   2616  N   ALA B 299     -23.243  12.891  25.573  1.00 26.05           N  
ANISOU 2616  N   ALA B 299     3436   3286   3175    153    141   -234       N  
ATOM   2617  CA  ALA B 299     -23.674  13.772  26.659  1.00 25.53           C  
ANISOU 2617  CA  ALA B 299     3381   3214   3105    159    140   -197       C  
ATOM   2618  C   ALA B 299     -24.752  13.073  27.489  1.00 26.23           C  
ANISOU 2618  C   ALA B 299     3507   3286   3173    160    110   -158       C  
ATOM   2619  O   ALA B 299     -24.680  13.023  28.718  1.00 24.16           O  
ANISOU 2619  O   ALA B 299     3260   3003   2917    176     83   -152       O  
ATOM   2620  CB  ALA B 299     -24.208  15.101  26.042  1.00 22.25           C  
ANISOU 2620  CB  ALA B 299     2951   2828   2673    138    189   -161       C  
ATOM   2621  N   ALA B 300     -25.763  12.492  26.831  1.00 24.56           N  
ANISOU 2621  N   ALA B 300     3310   3088   2932    138    112   -131       N  
ATOM   2622  CA  ALA B 300     -26.808  11.852  27.617  1.00 25.56           C  
ANISOU 2622  CA  ALA B 300     3471   3202   3037    135     85    -93       C  
ATOM   2623  C   ALA B 300     -26.266  10.569  28.236  1.00 25.65           C  
ANISOU 2623  C   ALA B 300     3504   3173   3069    154     41   -122       C  
ATOM   2624  O   ALA B 300     -26.698  10.153  29.314  1.00 23.15           O  
ANISOU 2624  O   ALA B 300     3215   2836   2746    160     10    -98       O  
ATOM   2625  CB  ALA B 300     -28.058  11.526  26.743  1.00 22.93           C  
ANISOU 2625  CB  ALA B 300     3147   2901   2664    100     99    -56       C  
ATOM   2626  N   GLY B 301     -25.324   9.919  27.548  1.00 26.76           N  
ANISOU 2626  N   GLY B 301     3631   3300   3235    163     38   -172       N  
ATOM   2627  CA  GLY B 301     -24.860   8.604  28.003  1.00 26.58           C  
ANISOU 2627  CA  GLY B 301     3628   3233   3237    184      0   -196       C  
ATOM   2628  C   GLY B 301     -23.980   8.759  29.214  1.00 31.16           C  
ANISOU 2628  C   GLY B 301     4201   3792   3845    220    -30   -203       C  
ATOM   2629  O   GLY B 301     -24.013   7.892  30.091  1.00 28.45           O  
ANISOU 2629  O   GLY B 301     3883   3417   3511    237    -69   -190       O  
ATOM   2630  N   GLN B 302     -23.217   9.859  29.295  1.00 26.02           N  
ANISOU 2630  N   GLN B 302     3516   3163   3205    228    -13   -219       N  
ATOM   2631  CA  GLN B 302     -22.385  10.099  30.490  1.00 30.16           C  
ANISOU 2631  CA  GLN B 302     4031   3680   3750    254    -41   -226       C  
ATOM   2632  C   GLN B 302     -23.233  10.376  31.696  1.00 29.34           C  
ANISOU 2632  C   GLN B 302     3955   3576   3618    245    -59   -180       C  
ATOM   2633  O   GLN B 302     -22.887  10.027  32.819  1.00 30.08           O  
ANISOU 2633  O   GLN B 302     4055   3657   3717    262    -98   -173       O  
ATOM   2634  CB  GLN B 302     -21.408  11.232  30.290  1.00 30.71           C  
ANISOU 2634  CB  GLN B 302     4060   3775   3835    256    -15   -258       C  
ATOM   2635  CG  GLN B 302     -20.334  10.881  29.298  1.00 33.55           C  
ANISOU 2635  CG  GLN B 302     4385   4135   4225    269     -4   -310       C  
ATOM   2636  CD  GLN B 302     -19.081  11.686  29.474  1.00 44.92           C  
ANISOU 2636  CD  GLN B 302     5784   5597   5688    279      3   -345       C  
ATOM   2637  OE1 GLN B 302     -19.019  12.621  30.298  1.00 47.51           O  
ANISOU 2637  OE1 GLN B 302     6108   5939   6005    270      5   -334       O  
ATOM   2638  NE2 GLN B 302     -18.075  11.364  28.670  1.00 40.89           N  
ANISOU 2638  NE2 GLN B 302     5240   5091   5206    293     13   -392       N  
ATOM   2639  N   ALA B 303     -24.390  10.979  31.461  1.00 26.96           N  
ANISOU 2639  N   ALA B 303     3667   3291   3284    218    -31   -145       N  
ATOM   2640  CA  ALA B 303     -25.280  11.257  32.555  1.00 23.51           C  
ANISOU 2640  CA  ALA B 303     3256   2858   2820    208    -41   -103       C  
ATOM   2641  C   ALA B 303     -25.863   9.993  33.057  1.00 26.61           C  
ANISOU 2641  C   ALA B 303     3683   3227   3202    209    -81    -79       C  
ATOM   2642  O   ALA B 303     -25.864   9.728  34.266  1.00 34.03           O  
ANISOU 2642  O   ALA B 303     4638   4156   4134    216   -115    -62       O  
ATOM   2643  CB  ALA B 303     -26.405  12.208  32.072  1.00 28.12           C  
ANISOU 2643  CB  ALA B 303     3840   3467   3376    184      4    -70       C  
ATOM   2644  N   GLU B 304     -26.356   9.184  32.128  1.00 27.47           N  
ANISOU 2644  N   GLU B 304     3805   3328   3307    198    -77    -77       N  
ATOM   2645  CA  GLU B 304     -26.929   7.897  32.500  1.00 26.29           C  
ANISOU 2645  CA  GLU B 304     3692   3148   3148    194   -111    -55       C  
ATOM   2646  C   GLU B 304     -25.893   6.973  33.199  1.00 34.47           C  
ANISOU 2646  C   GLU B 304     4732   4145   4220    228   -156    -73       C  
ATOM   2647  O   GLU B 304     -26.185   6.350  34.227  1.00 31.37           O  
ANISOU 2647  O   GLU B 304     4367   3733   3818    231   -193    -43       O  
ATOM   2648  CB  GLU B 304     -27.500   7.236  31.253  1.00 27.32           C  
ANISOU 2648  CB  GLU B 304     3832   3278   3269    170    -92    -62       C  
ATOM   2649  CG  GLU B 304     -28.043   5.844  31.519  1.00 41.72           C  
ANISOU 2649  CG  GLU B 304     5697   5066   5089    161   -123    -46       C  
ATOM   2650  CD  GLU B 304     -28.841   5.308  30.350  1.00 48.16           C  
ANISOU 2650  CD  GLU B 304     6525   5892   5882    123   -100    -50       C  
ATOM   2651  OE1 GLU B 304     -29.161   6.117  29.438  1.00 48.68           O  
ANISOU 2651  OE1 GLU B 304     6565   6003   5928    103    -63    -50       O  
ATOM   2652  OE2 GLU B 304     -29.118   4.084  30.337  1.00 58.88           O  
ANISOU 2652  OE2 GLU B 304     7916   7212   7243    112   -118    -51       O  
ATOM   2653  N   ALA B 305     -24.700   6.868  32.636  1.00 33.47           N  
ANISOU 2653  N   ALA B 305     4577   4009   4133    254   -152   -119       N  
ATOM   2654  CA  ALA B 305     -23.637   6.010  33.229  1.00 34.06           C  
ANISOU 2654  CA  ALA B 305     4646   4048   4247    293   -193   -134       C  
ATOM   2655  C   ALA B 305     -23.229   6.489  34.622  1.00 36.47           C  
ANISOU 2655  C   ALA B 305     4943   4369   4546    306   -225   -113       C  
ATOM   2656  O   ALA B 305     -23.077   5.688  35.555  1.00 34.53           O  
ANISOU 2656  O   ALA B 305     4713   4100   4307    324   -269    -88       O  
ATOM   2657  CB  ALA B 305     -22.418   5.982  32.301  1.00 34.06           C  
ANISOU 2657  CB  ALA B 305     4607   4045   4290    318   -175   -190       C  
ATOM   2658  N   GLY B 306     -23.055   7.800  34.775  1.00 31.90           N  
ANISOU 2658  N   GLY B 306     4338   3830   3951    294   -201   -122       N  
ATOM   2659  CA  GLY B 306     -22.722   8.381  36.068  1.00 30.70           C  
ANISOU 2659  CA  GLY B 306     4178   3701   3785    295   -224   -109       C  
ATOM   2660  C   GLY B 306     -23.814   8.118  37.101  1.00 35.07           C  
ANISOU 2660  C   GLY B 306     4772   4254   4300    275   -246    -58       C  
ATOM   2661  O   GLY B 306     -23.511   7.706  38.202  1.00 41.77           O  
ANISOU 2661  O   GLY B 306     5625   5101   5143    285   -289    -38       O  
ATOM   2662  N   LEU B 307     -25.087   8.308  36.746  1.00 33.03           N  
ANISOU 2662  N   LEU B 307     4540   3999   4012    247   -219    -35       N  
ATOM   2663  CA  LEU B 307     -26.165   7.947  37.676  1.00 29.11           C  
ANISOU 2663  CA  LEU B 307     4081   3502   3478    226   -239     13       C  
ATOM   2664  C   LEU B 307     -26.074   6.468  38.054  1.00 36.53           C  
ANISOU 2664  C   LEU B 307     5046   4402   4430    241   -288     35       C  
ATOM   2665  O   LEU B 307     -26.136   6.125  39.234  1.00 38.07           O  
ANISOU 2665  O   LEU B 307     5258   4599   4609    240   -326     67       O  
ATOM   2666  CB  LEU B 307     -27.535   8.218  37.087  1.00 29.43           C  
ANISOU 2666  CB  LEU B 307     4139   3554   3489    196   -203     36       C  
ATOM   2667  CG  LEU B 307     -27.762   9.766  36.915  1.00 27.94           C  
ANISOU 2667  CG  LEU B 307     3927   3400   3287    183   -152     27       C  
ATOM   2668  CD1 LEU B 307     -29.055   9.989  36.196  1.00 33.64           C  
ANISOU 2668  CD1 LEU B 307     4659   4136   3985    160   -117     55       C  
ATOM   2669  CD2 LEU B 307     -27.806  10.521  38.263  1.00 28.17           C  
ANISOU 2669  CD2 LEU B 307     3958   3450   3294    174   -156     37       C  
ATOM   2670  N   LYS B 308     -25.937   5.595  37.059  1.00 30.93           N  
ANISOU 2670  N   LYS B 308     4343   3658   3751    253   -285     19       N  
ATOM   2671  CA  LYS B 308     -25.709   4.165  37.345  1.00 36.99           C  
ANISOU 2671  CA  LYS B 308     5135   4376   4542    273   -327     35       C  
ATOM   2672  C   LYS B 308     -24.459   3.906  38.216  1.00 32.03           C  
ANISOU 2672  C   LYS B 308     4485   3741   3944    313   -370     35       C  
ATOM   2673  O   LYS B 308     -24.507   3.093  39.136  1.00 35.26           O  
ANISOU 2673  O   LYS B 308     4916   4128   4351    322   -414     75       O  
ATOM   2674  CB  LYS B 308     -25.660   3.345  36.041  1.00 37.79           C  
ANISOU 2674  CB  LYS B 308     5245   4439   4676    278   -307      5       C  
ATOM   2675  CG  LYS B 308     -26.993   3.152  35.325  1.00 42.08           C  
ANISOU 2675  CG  LYS B 308     5819   4985   5186    234   -278     18       C  
ATOM   2676  CD  LYS B 308     -26.809   2.250  34.073  1.00 54.47           C  
ANISOU 2676  CD  LYS B 308     7395   6515   6786    235   -260    -20       C  
ATOM   2677  CE  LYS B 308     -27.915   2.389  33.025  1.00 55.26           C  
ANISOU 2677  CE  LYS B 308     7507   6641   6850    187   -221    -23       C  
ATOM   2678  NZ  LYS B 308     -29.256   1.841  33.392  1.00 54.57           N  
ANISOU 2678  NZ  LYS B 308     7462   6551   6721    146   -230     22       N  
ATOM   2679  N   GLN B 309     -23.349   4.584  37.947  1.00 38.83           N  
ANISOU 2679  N   GLN B 309     5300   4624   4831    335   -360     -5       N  
ATOM   2680  CA  GLN B 309     -22.126   4.369  38.744  1.00 43.53           C  
ANISOU 2680  CA  GLN B 309     5865   5223   5451    372   -402     -4       C  
ATOM   2681  C   GLN B 309     -22.280   4.855  40.195  1.00 49.06           C  
ANISOU 2681  C   GLN B 309     6567   5964   6108    354   -433     33       C  
ATOM   2682  O   GLN B 309     -21.626   4.326  41.093  1.00 40.97           O  
ANISOU 2682  O   GLN B 309     5533   4941   5092    377   -482     58       O  
ATOM   2683  CB  GLN B 309     -20.894   5.047  38.096  1.00 46.03           C  
ANISOU 2683  CB  GLN B 309     6126   5562   5800    395   -381    -58       C  
ATOM   2684  CG  GLN B 309     -20.549   6.459  38.676  1.00 95.66           C  
ANISOU 2684  CG  GLN B 309    12381  11910  12057    373   -370    -73       C  
ATOM   2685  CD  GLN B 309     -19.788   7.388  37.700  1.00 92.74           C  
ANISOU 2685  CD  GLN B 309    11967  11562  11707    374   -326   -130       C  
ATOM   2686  OE1 GLN B 309     -19.171   6.934  36.730  1.00 93.44           O  
ANISOU 2686  OE1 GLN B 309    12037  11630  11837    400   -315   -161       O  
ATOM   2687  NE2 GLN B 309     -19.836   8.695  37.968  1.00 85.82           N  
ANISOU 2687  NE2 GLN B 309    11078  10728  10802    343   -300   -143       N  
ATOM   2688  N   GLN B 310     -23.118   5.875  40.409  1.00 44.38           N  
ANISOU 2688  N   GLN B 310     5985   5407   5469    313   -403     35       N  
ATOM   2689  CA  GLN B 310     -23.408   6.417  41.746  1.00 41.80           C  
ANISOU 2689  CA  GLN B 310     5666   5123   5096    286   -422     62       C  
ATOM   2690  C   GLN B 310     -24.581   5.683  42.363  1.00 43.77           C  
ANISOU 2690  C   GLN B 310     5964   5356   5311    264   -442    115       C  
ATOM   2691  O   GLN B 310     -25.087   6.095  43.408  1.00 52.50           O  
ANISOU 2691  O   GLN B 310     7082   6496   6371    235   -451    140       O  
ATOM   2692  CB  GLN B 310     -23.785   7.909  41.674  1.00 36.32           C  
ANISOU 2692  CB  GLN B 310     4960   4469   4372    253   -371     35       C  
ATOM   2693  CG  GLN B 310     -22.642   8.842  41.293  1.00 47.20           C  
ANISOU 2693  CG  GLN B 310     6290   5870   5773    262   -349    -17       C  
ATOM   2694  CD  GLN B 310     -21.504   8.750  42.265  1.00 58.33           C  
ANISOU 2694  CD  GLN B 310     7670   7309   7184    274   -395    -19       C  
ATOM   2695  OE1 GLN B 310     -21.606   9.219  43.394  1.00 63.07           O  
ANISOU 2695  OE1 GLN B 310     8272   7947   7743    247   -408     -7       O  
ATOM   2696  NE2 GLN B 310     -20.414   8.110  41.846  1.00 62.78           N  
ANISOU 2696  NE2 GLN B 310     8203   7859   7793    315   -420    -32       N  
ATOM   2697  N   ALA B 311     -25.037   4.627  41.691  1.00 35.32           N  
ANISOU 2697  N   ALA B 311     4923   4236   4263    274   -446    130       N  
ATOM   2698  CA  ALA B 311     -26.219   3.878  42.138  1.00 40.72           C  
ANISOU 2698  CA  ALA B 311     5655   4901   4915    248   -460    179       C  
ATOM   2699  C   ALA B 311     -27.426   4.746  42.512  1.00 48.15           C  
ANISOU 2699  C   ALA B 311     6612   5884   5800    202   -430    193       C  
ATOM   2700  O   ALA B 311     -28.024   4.581  43.579  1.00 42.93           O  
ANISOU 2700  O   ALA B 311     5974   5240   5098    178   -453    233       O  
ATOM   2701  CB  ALA B 311     -25.868   2.917  43.293  1.00 47.41           C  
ANISOU 2701  CB  ALA B 311     6517   5736   5762    262   -522    227       C  
ATOM   2702  N   LEU B 312     -27.795   5.661  41.615  1.00 40.12           N  
ANISOU 2702  N   LEU B 312     5580   4883   4781    191   -377    162       N  
ATOM   2703  CA  LEU B 312     -28.971   6.522  41.809  1.00 35.98           C  
ANISOU 2703  CA  LEU B 312     5065   4393   4213    154   -340    174       C  
ATOM   2704  C   LEU B 312     -30.054   6.141  40.797  1.00 46.39           C  
ANISOU 2704  C   LEU B 312     6404   5697   5526    137   -313    186       C  
ATOM   2705  O   LEU B 312     -29.904   6.369  39.580  1.00 45.12           O  
ANISOU 2705  O   LEU B 312     6225   5529   5389    146   -281    158       O  
ATOM   2706  CB  LEU B 312     -28.582   7.972  41.617  1.00 34.97           C  
ANISOU 2706  CB  LEU B 312     4902   4297   4086    154   -297    136       C  
ATOM   2707  CG  LEU B 312     -27.512   8.460  42.574  1.00 36.60           C  
ANISOU 2707  CG  LEU B 312     5087   4528   4294    162   -319    117       C  
ATOM   2708  CD1 LEU B 312     -26.877   9.733  42.048  1.00 43.56           C  
ANISOU 2708  CD1 LEU B 312     5931   5426   5192    166   -274     69       C  
ATOM   2709  CD2 LEU B 312     -28.121   8.676  43.955  1.00 35.11           C  
ANISOU 2709  CD2 LEU B 312     4916   4370   4053    131   -332    146       C  
ATOM   2710  N   PRO B 313     -31.148   5.553  41.285  1.00 35.25           N  
ANISOU 2710  N   PRO B 313     5026   4287   4080    109   -325    229       N  
ATOM   2711  CA  PRO B 313     -32.220   5.075  40.420  1.00 31.34           C  
ANISOU 2711  CA  PRO B 313     4551   3784   3573     86   -305    244       C  
ATOM   2712  C   PRO B 313     -32.817   6.308  39.724  1.00 36.06           C  
ANISOU 2712  C   PRO B 313     5122   4422   4159     75   -249    233       C  
ATOM   2713  O   PRO B 313     -32.825   7.365  40.346  1.00 32.48           O  
ANISOU 2713  O   PRO B 313     4652   3998   3691     75   -230    230       O  
ATOM   2714  CB  PRO B 313     -33.270   4.577  41.412  1.00 35.16           C  
ANISOU 2714  CB  PRO B 313     5068   4279   4012     53   -326    293       C  
ATOM   2715  CG  PRO B 313     -32.560   4.352  42.680  1.00 36.13           C  
ANISOU 2715  CG  PRO B 313     5198   4398   4132     64   -369    306       C  
ATOM   2716  CD  PRO B 313     -31.500   5.446  42.712  1.00 36.71           C  
ANISOU 2716  CD  PRO B 313     5231   4491   4226     91   -355    265       C  
ATOM   2717  N   TYR B 314     -33.318   6.189  38.505  1.00 32.35           N  
ANISOU 2717  N   TYR B 314     4647   3953   3691     65   -222    228       N  
ATOM   2718  CA  TYR B 314     -33.829   7.393  37.801  1.00 40.35           C  
ANISOU 2718  CA  TYR B 314     5630   5005   4696     59   -170    225       C  
ATOM   2719  C   TYR B 314     -34.888   7.072  36.756  1.00 38.47           C  
ANISOU 2719  C   TYR B 314     5394   4786   4438     32   -149    245       C  
ATOM   2720  O   TYR B 314     -35.021   5.929  36.314  1.00 39.18           O  
ANISOU 2720  O   TYR B 314     5506   4852   4528     16   -169    245       O  
ATOM   2721  CB  TYR B 314     -32.675   8.181  37.130  1.00 31.85           C  
ANISOU 2721  CB  TYR B 314     4519   3925   3658     89   -148    180       C  
ATOM   2722  CG  TYR B 314     -31.998   7.331  36.082  1.00 37.90           C  
ANISOU 2722  CG  TYR B 314     5285   4661   4455     98   -159    151       C  
ATOM   2723  CD1 TYR B 314     -32.486   7.249  34.760  1.00 34.29           C  
ANISOU 2723  CD1 TYR B 314     4819   4218   3993     81   -131    148       C  
ATOM   2724  CD2 TYR B 314     -30.918   6.551  36.427  1.00 36.08           C  
ANISOU 2724  CD2 TYR B 314     5062   4392   4256    122   -197    128       C  
ATOM   2725  CE1 TYR B 314     -31.865   6.422  33.836  1.00 33.23           C  
ANISOU 2725  CE1 TYR B 314     4686   4056   3884     85   -137    114       C  
ATOM   2726  CE2 TYR B 314     -30.311   5.730  35.522  1.00 44.07           C  
ANISOU 2726  CE2 TYR B 314     6074   5371   5299    134   -202     99       C  
ATOM   2727  CZ  TYR B 314     -30.782   5.671  34.226  1.00 41.58           C  
ANISOU 2727  CZ  TYR B 314     5753   5068   4978    113   -171     88       C  
ATOM   2728  OH  TYR B 314     -30.135   4.818  33.352  1.00 51.94           O  
ANISOU 2728  OH  TYR B 314     7067   6346   6321    121   -173     51       O  
ATOM   2729  N   SER B 315     -35.600   8.109  36.323  1.00 31.66           N  
ANISOU 2729  N   SER B 315     4505   3965   3560     25   -106    261       N  
ATOM   2730  CA  SER B 315     -36.544   7.997  35.220  1.00 34.98           C  
ANISOU 2730  CA  SER B 315     4915   4418   3959     -1    -82    281       C  
ATOM   2731  C   SER B 315     -36.087   8.989  34.134  1.00 39.74           C  
ANISOU 2731  C   SER B 315     5479   5038   4584     16    -43    262       C  
ATOM   2732  O   SER B 315     -35.906  10.183  34.416  1.00 35.41           O  
ANISOU 2732  O   SER B 315     4908   4499   4047     37    -14    263       O  
ATOM   2733  CB  SER B 315     -37.938   8.304  35.747  1.00 36.75           C  
ANISOU 2733  CB  SER B 315     5138   4682   4141    -24    -68    331       C  
ATOM   2734  OG  SER B 315     -38.850   8.598  34.711  1.00 44.14           O  
ANISOU 2734  OG  SER B 315     6049   5665   5057    -43    -38    358       O  
ATOM   2735  N   ARG B 316     -35.828   8.490  32.924  1.00 33.58           N  
ANISOU 2735  N   ARG B 316     4692   4257   3810      5    -40    242       N  
ATOM   2736  CA  ARG B 316     -35.428   9.371  31.819  1.00 37.99           C  
ANISOU 2736  CA  ARG B 316     5213   4838   4384     15     -4    228       C  
ATOM   2737  C   ARG B 316     -36.608   9.864  30.988  1.00 38.25           C  
ANISOU 2737  C   ARG B 316     5221   4930   4383     -9     28    274       C  
ATOM   2738  O   ARG B 316     -37.448   9.055  30.538  1.00 40.24           O  
ANISOU 2738  O   ARG B 316     5481   5206   4601    -46     19    293       O  
ATOM   2739  CB  ARG B 316     -34.429   8.655  30.912  1.00 38.23           C  
ANISOU 2739  CB  ARG B 316     5245   4843   4438     16    -14    179       C  
ATOM   2740  CG  ARG B 316     -34.198   9.367  29.578  1.00 32.08           C  
ANISOU 2740  CG  ARG B 316     4428   4098   3662     13     23    169       C  
ATOM   2741  CD  ARG B 316     -33.067   8.707  28.799  1.00 34.78           C  
ANISOU 2741  CD  ARG B 316     4770   4413   4032     17     16    111       C  
ATOM   2742  NE  ARG B 316     -32.799   9.428  27.559  1.00 38.50           N  
ANISOU 2742  NE  ARG B 316     5205   4921   4503     10     52    101       N  
ATOM   2743  CZ  ARG B 316     -31.656   9.358  26.883  1.00 38.69           C  
ANISOU 2743  CZ  ARG B 316     5215   4930   4555     21     59     49       C  
ATOM   2744  NH1 ARG B 316     -31.485  10.079  25.776  1.00 31.58           N  
ANISOU 2744  NH1 ARG B 316     4281   4069   3649     11     93     47       N  
ATOM   2745  NH2 ARG B 316     -30.676   8.592  27.335  1.00 34.99           N  
ANISOU 2745  NH2 ARG B 316     4764   4410   4121     44     33      3       N  
ATOM   2746  N   ARG B 317     -36.670  11.183  30.760  1.00 30.76           N  
ANISOU 2746  N   ARG B 317     4238   4005   3444     10     67    292       N  
ATOM   2747  CA  ARG B 317     -37.694  11.753  29.875  1.00 32.38           C  
ANISOU 2747  CA  ARG B 317     4410   4269   3622     -6     99    342       C  
ATOM   2748  C   ARG B 317     -37.024  12.464  28.708  1.00 37.33           C  
ANISOU 2748  C   ARG B 317     5006   4911   4269      2    128    329       C  
ATOM   2749  O   ARG B 317     -36.091  13.270  28.914  1.00 34.33           O  
ANISOU 2749  O   ARG B 317     4618   4501   3925     33    145    303       O  
ATOM   2750  CB  ARG B 317     -38.606  12.733  30.613  1.00 43.94           C  
ANISOU 2750  CB  ARG B 317     5860   5753   5080     10    127    392       C  
ATOM   2751  CG  ARG B 317     -39.519  12.125  31.666  1.00 53.03           C  
ANISOU 2751  CG  ARG B 317     7037   6910   6204     -6    105    416       C  
ATOM   2752  CD  ARG B 317     -38.846  12.066  33.034  1.00 59.36           C  
ANISOU 2752  CD  ARG B 317     7869   7659   7025     13     86    383       C  
ATOM   2753  NE  ARG B 317     -39.777  11.666  34.098  1.00 62.15           N  
ANISOU 2753  NE  ARG B 317     8242   8023   7348     -2     71    411       N  
ATOM   2754  CZ  ARG B 317     -40.556  12.522  34.762  1.00 66.54           C  
ANISOU 2754  CZ  ARG B 317     8784   8600   7896      9    102    444       C  
ATOM   2755  NH1 ARG B 317     -40.528  13.823  34.473  1.00 65.25           N  
ANISOU 2755  NH1 ARG B 317     8590   8443   7758     37    150    454       N  
ATOM   2756  NH2 ARG B 317     -41.361  12.083  35.720  1.00 71.24           N  
ANISOU 2756  NH2 ARG B 317     9398   9207   8462     -9     88    466       N  
ATOM   2757  N   ASN B 318     -37.475  12.153  27.490  1.00 30.31           N  
ANISOU 2757  N   ASN B 318     4097   4070   3350    -29    134    346       N  
ATOM   2758  CA  ASN B 318     -36.912  12.787  26.289  1.00 24.72           C  
ANISOU 2758  CA  ASN B 318     3356   3385   2651    -28    162    339       C  
ATOM   2759  C   ASN B 318     -37.777  13.899  25.808  1.00 31.39           C  
ANISOU 2759  C   ASN B 318     4161   4283   3483    -24    199    407       C  
ATOM   2760  O   ASN B 318     -38.976  13.736  25.676  1.00 35.40           O  
ANISOU 2760  O   ASN B 318     4656   4840   3953    -45    199    460       O  
ATOM   2761  CB  ASN B 318     -36.740  11.747  25.185  1.00 36.72           C  
ANISOU 2761  CB  ASN B 318     4879   4928   4147    -70    147    308       C  
ATOM   2762  CG  ASN B 318     -35.687  10.699  25.548  1.00 38.20           C  
ANISOU 2762  CG  ASN B 318     5104   5052   4360    -65    117    236       C  
ATOM   2763  OD1 ASN B 318     -34.751  10.992  26.259  1.00 36.05           O  
ANISOU 2763  OD1 ASN B 318     4839   4729   4127    -29    112    204       O  
ATOM   2764  ND2 ASN B 318     -35.863   9.467  25.071  1.00 47.12           N  
ANISOU 2764  ND2 ASN B 318     6252   6184   5466   -103     98    211       N  
ATOM   2765  N   HIS B 319     -37.169  15.042  25.544  1.00 32.43           N  
ANISOU 2765  N   HIS B 319     4271   4405   3647      4    232    410       N  
ATOM   2766  CA  HIS B 319     -37.921  16.170  24.979  1.00 28.68           C  
ANISOU 2766  CA  HIS B 319     3755   3976   3167     13    271    482       C  
ATOM   2767  C   HIS B 319     -37.369  16.493  23.579  1.00 32.72           C  
ANISOU 2767  C   HIS B 319     4237   4522   3675     -2    289    481       C  
ATOM   2768  O   HIS B 319     -36.324  15.968  23.181  1.00 30.29           O  
ANISOU 2768  O   HIS B 319     3940   4193   3374    -15    275    417       O  
ATOM   2769  CB  HIS B 319     -37.763  17.372  25.894  1.00 28.44           C  
ANISOU 2769  CB  HIS B 319     3724   3900   3181     58    304    493       C  
ATOM   2770  CG  HIS B 319     -37.977  17.046  27.340  1.00 37.06           C  
ANISOU 2770  CG  HIS B 319     4850   4953   4280     71    286    474       C  
ATOM   2771  ND1 HIS B 319     -39.191  16.604  27.839  1.00 37.02           N  
ANISOU 2771  ND1 HIS B 319     4847   4975   4242     60    275    515       N  
ATOM   2772  CD2 HIS B 319     -37.117  17.042  28.393  1.00 42.94           C  
ANISOU 2772  CD2 HIS B 319     5625   5638   5053     88    276    420       C  
ATOM   2773  CE1 HIS B 319     -39.066  16.357  29.131  1.00 39.84           C  
ANISOU 2773  CE1 HIS B 319     5238   5291   4609     70    259    486       C  
ATOM   2774  NE2 HIS B 319     -37.816  16.604  29.491  1.00 43.56           N  
ANISOU 2774  NE2 HIS B 319     5726   5710   5116     87    258    429       N  
ATOM   2775  N   LYS B 320     -38.042  17.358  22.815  1.00 37.66           N  
ANISOU 2775  N   LYS B 320     4821   5200   4288     -1    320    552       N  
ATOM   2776  CA  LYS B 320     -37.554  17.643  21.469  1.00 42.43           C  
ANISOU 2776  CA  LYS B 320     5396   5844   4881    -22    335    557       C  
ATOM   2777  C   LYS B 320     -36.160  18.232  21.502  1.00 41.63           C  
ANISOU 2777  C   LYS B 320     5303   5687   4828      1    352    503       C  
ATOM   2778  O   LYS B 320     -35.367  17.919  20.617  1.00 43.01           O  
ANISOU 2778  O   LYS B 320     5472   5877   4994    -24    349    463       O  
ATOM   2779  CB  LYS B 320     -38.493  18.569  20.676  1.00 47.16           C  
ANISOU 2779  CB  LYS B 320     5945   6511   5462    -20    366    655       C  
ATOM   2780  CG  LYS B 320     -38.580  19.941  21.214  1.00 63.14           C  
ANISOU 2780  CG  LYS B 320     7958   8496   7535     32    407    699       C  
ATOM   2781  CD  LYS B 320     -39.426  20.872  20.323  1.00 76.85           C  
ANISOU 2781  CD  LYS B 320     9642  10297   9260     38    439    803       C  
ATOM   2782  CE  LYS B 320     -38.763  21.104  18.971  1.00 82.87           C  
ANISOU 2782  CE  LYS B 320    10380  11100  10007     11    449    806       C  
ATOM   2783  NZ  LYS B 320     -39.776  21.007  17.873  1.00 87.99           N  
ANISOU 2783  NZ  LYS B 320    10980  11856  10598    -22    444    889       N  
ATOM   2784  N   GLY B 321     -35.848  19.064  22.506  1.00 30.46           N  
ANISOU 2784  N   GLY B 321     3903   4211   3462     42    372    497       N  
ATOM   2785  CA  GLY B 321     -34.517  19.655  22.581  1.00 36.46           C  
ANISOU 2785  CA  GLY B 321     4668   4919   4264     58    390    444       C  
ATOM   2786  C   GLY B 321     -33.674  19.392  23.825  1.00 32.10           C  
ANISOU 2786  C   GLY B 321     4152   4298   3745     78    371    373       C  
ATOM   2787  O   GLY B 321     -32.700  20.103  24.069  1.00 25.81           O  
ANISOU 2787  O   GLY B 321     3359   3461   2988     93    391    339       O  
ATOM   2788  N   GLY B 322     -34.013  18.360  24.609  1.00 24.96           N  
ANISOU 2788  N   GLY B 322     3276   3384   2825     73    333    352       N  
ATOM   2789  CA  GLY B 322     -33.246  18.069  25.814  1.00 23.86           C  
ANISOU 2789  CA  GLY B 322     3168   3185   2712     90    311    293       C  
ATOM   2790  C   GLY B 322     -33.676  16.774  26.428  1.00 22.83           C  
ANISOU 2790  C   GLY B 322     3066   3052   2556     78    265    279       C  
ATOM   2791  O   GLY B 322     -34.531  16.084  25.853  1.00 27.49           O  
ANISOU 2791  O   GLY B 322     3652   3684   3109     53    252    309       O  
ATOM   2792  N   VAL B 323     -33.063  16.427  27.567  1.00 21.12           N  
ANISOU 2792  N   VAL B 323     2877   2790   2360     92    241    234       N  
ATOM   2793  CA  VAL B 323     -33.368  15.177  28.245  1.00 26.58           C  
ANISOU 2793  CA  VAL B 323     3598   3469   3031     82    195    222       C  
ATOM   2794  C   VAL B 323     -33.422  15.517  29.730  1.00 25.52           C  
ANISOU 2794  C   VAL B 323     3485   3302   2909    102    191    220       C  
ATOM   2795  O   VAL B 323     -32.596  16.279  30.183  1.00 28.63           O  
ANISOU 2795  O   VAL B 323     3876   3670   3333    119    206    191       O  
ATOM   2796  CB  VAL B 323     -32.190  14.218  28.079  1.00 23.76           C  
ANISOU 2796  CB  VAL B 323     3254   3086   2689     81    163    157       C  
ATOM   2797  CG1 VAL B 323     -32.498  12.872  28.799  1.00 27.20           C  
ANISOU 2797  CG1 VAL B 323     3724   3501   3109     73    116    149       C  
ATOM   2798  CG2 VAL B 323     -31.937  13.982  26.594  1.00 26.13           C  
ANISOU 2798  CG2 VAL B 323     3531   3416   2979     60    175    145       C  
ATOM   2799  N   THR B 324     -34.362  14.951  30.498  1.00 23.93           N  
ANISOU 2799  N   THR B 324     3304   3106   2682     93    170    247       N  
ATOM   2800  CA  THR B 324     -34.369  15.193  31.939  1.00 22.77           C  
ANISOU 2800  CA  THR B 324     3177   2933   2540    106    164    241       C  
ATOM   2801  C   THR B 324     -34.194  13.812  32.559  1.00 24.63           C  
ANISOU 2801  C   THR B 324     3446   3151   2762     95    108    220       C  
ATOM   2802  O   THR B 324     -34.846  12.880  32.145  1.00 27.84           O  
ANISOU 2802  O   THR B 324     3862   3574   3143     74     88    239       O  
ATOM   2803  CB  THR B 324     -35.735  15.704  32.398  1.00 32.32           C  
ANISOU 2803  CB  THR B 324     4384   4167   3729    105    189    296       C  
ATOM   2804  OG1 THR B 324     -35.947  16.994  31.811  1.00 33.25           O  
ANISOU 2804  OG1 THR B 324     4472   4296   3866    120    243    323       O  
ATOM   2805  CG2 THR B 324     -35.763  15.848  33.947  1.00 32.05           C  
ANISOU 2805  CG2 THR B 324     4373   4109   3693    111    181    284       C  
ATOM   2806  N   PHE B 325     -33.245  13.685  33.468  1.00 23.57           N  
ANISOU 2806  N   PHE B 325     3326   2984   2646    108     85    181       N  
ATOM   2807  CA  PHE B 325     -33.188  12.478  34.294  1.00 24.69           C  
ANISOU 2807  CA  PHE B 325     3499   3107   2775    101     34    175       C  
ATOM   2808  C   PHE B 325     -33.758  12.869  35.632  1.00 25.79           C  
ANISOU 2808  C   PHE B 325     3652   3250   2896     99     35    195       C  
ATOM   2809  O   PHE B 325     -33.249  13.799  36.265  1.00 23.47           O  
ANISOU 2809  O   PHE B 325     3352   2950   2617    110     54    175       O  
ATOM   2810  CB  PHE B 325     -31.749  12.000  34.483  1.00 25.98           C  
ANISOU 2810  CB  PHE B 325     3665   3239   2968    118      2    125       C  
ATOM   2811  CG  PHE B 325     -31.128  11.459  33.206  1.00 27.14           C  
ANISOU 2811  CG  PHE B 325     3799   3379   3133    120      0     97       C  
ATOM   2812  CD1 PHE B 325     -30.472  12.301  32.330  1.00 23.98           C  
ANISOU 2812  CD1 PHE B 325     3368   2989   2755    128     34     74       C  
ATOM   2813  CD2 PHE B 325     -31.256  10.111  32.864  1.00 30.56           C  
ANISOU 2813  CD2 PHE B 325     4253   3798   3561    110    -31     95       C  
ATOM   2814  CE1 PHE B 325     -29.922  11.815  31.115  1.00 29.21           C  
ANISOU 2814  CE1 PHE B 325     4017   3652   3431    126     36     46       C  
ATOM   2815  CE2 PHE B 325     -30.713   9.622  31.671  1.00 29.77           C  
ANISOU 2815  CE2 PHE B 325     4141   3692   3477    108    -27     63       C  
ATOM   2816  CZ  PHE B 325     -30.049  10.484  30.797  1.00 28.89           C  
ANISOU 2816  CZ  PHE B 325     3996   3597   3384    116      7     38       C  
ATOM   2817  N   VAL B 326     -34.767  12.111  36.081  1.00 26.35           N  
ANISOU 2817  N   VAL B 326     3745   3332   2933     80     14    230       N  
ATOM   2818  CA  VAL B 326     -35.400  12.371  37.384  1.00 28.45           C  
ANISOU 2818  CA  VAL B 326     4027   3608   3177     72     14    250       C  
ATOM   2819  C   VAL B 326     -34.947  11.293  38.363  1.00 29.47           C  
ANISOU 2819  C   VAL B 326     4187   3715   3295     66    -42    240       C  
ATOM   2820  O   VAL B 326     -35.282  10.119  38.199  1.00 29.17           O  
ANISOU 2820  O   VAL B 326     4171   3670   3244     51    -75    257       O  
ATOM   2821  CB  VAL B 326     -36.928  12.302  37.297  1.00 29.72           C  
ANISOU 2821  CB  VAL B 326     4187   3802   3302     53     31    301       C  
ATOM   2822  CG1 VAL B 326     -37.524  12.639  38.673  1.00 31.17           C  
ANISOU 2822  CG1 VAL B 326     4384   3996   3462     45     37    316       C  
ATOM   2823  CG2 VAL B 326     -37.435  13.360  36.305  1.00 32.73           C  
ANISOU 2823  CG2 VAL B 326     4533   4209   3694     63     86    322       C  
ATOM   2824  N   ILE B 327     -34.188  11.697  39.366  1.00 26.22           N  
ANISOU 2824  N   ILE B 327     3778   3295   2890     74    -51    216       N  
ATOM   2825  CA  ILE B 327     -33.697  10.708  40.335  1.00 28.70           C  
ANISOU 2825  CA  ILE B 327     4117   3593   3194     70   -107    214       C  
ATOM   2826  C   ILE B 327     -34.804  10.380  41.299  1.00 35.24           C  
ANISOU 2826  C   ILE B 327     4970   4441   3979     44   -117    253       C  
ATOM   2827  O   ILE B 327     -35.440  11.300  41.830  1.00 34.36           O  
ANISOU 2827  O   ILE B 327     4851   4354   3848     35    -80    260       O  
ATOM   2828  CB  ILE B 327     -32.534  11.288  41.103  1.00 29.82           C  
ANISOU 2828  CB  ILE B 327     4249   3732   3350     82   -115    177       C  
ATOM   2829  CG1 ILE B 327     -31.361  11.541  40.137  1.00 33.26           C  
ANISOU 2829  CG1 ILE B 327     4658   4150   3830    106   -108    137       C  
ATOM   2830  CG2 ILE B 327     -32.108  10.357  42.281  1.00 29.46           C  
ANISOU 2830  CG2 ILE B 327     4226   3682   3287     76   -175    187       C  
ATOM   2831  CD1 ILE B 327     -30.260  12.459  40.720  1.00 37.45           C  
ANISOU 2831  CD1 ILE B 327     5168   4686   4374    113    -99     96       C  
ATOM   2832  N   GLN B 328     -34.978   9.078  41.575  1.00 27.88           N  
ANISOU 2832  N   GLN B 328     4067   3495   3032     31   -165    276       N  
ATOM   2833  CA  GLN B 328     -36.156   8.566  42.284  1.00 32.26           C  
ANISOU 2833  CA  GLN B 328     4646   4069   3542      0   -176    319       C  
ATOM   2834  C   GLN B 328     -35.822   7.648  43.472  1.00 43.77           C  
ANISOU 2834  C   GLN B 328     6134   5515   4982    -11   -231    334       C  
ATOM   2835  O   GLN B 328     -34.702   7.132  43.580  1.00 41.29           O  
ANISOU 2835  O   GLN B 328     5823   5171   4693      9   -268    318       O  
ATOM   2836  CB  GLN B 328     -37.014   7.777  41.294  1.00 35.34           C  
ANISOU 2836  CB  GLN B 328     5045   4456   3926    -17   -175    344       C  
ATOM   2837  CG  GLN B 328     -37.587   8.656  40.163  1.00 40.34           C  
ANISOU 2837  CG  GLN B 328     5646   5115   4566    -13   -121    344       C  
ATOM   2838  CD  GLN B 328     -38.413   7.859  39.190  1.00 45.34           C  
ANISOU 2838  CD  GLN B 328     6286   5757   5185    -37   -123    368       C  
ATOM   2839  OE1 GLN B 328     -38.069   6.713  38.874  1.00 46.15           O  
ANISOU 2839  OE1 GLN B 328     6411   5827   5295    -45   -158    361       O  
ATOM   2840  NE2 GLN B 328     -39.527   8.438  38.724  1.00 50.78           N  
ANISOU 2840  NE2 GLN B 328     6952   6490   5852    -50    -85    396       N  
ATOM   2841  N   GLY B 329     -36.815   7.425  44.333  1.00 44.26           N  
ANISOU 2841  N   GLY B 329     6216   5602   4998    -43   -236    370       N  
ATOM   2842  CA  GLY B 329     -36.682   6.507  45.454  1.00 44.61           C  
ANISOU 2842  CA  GLY B 329     6292   5641   5018    -60   -288    396       C  
ATOM   2843  C   GLY B 329     -36.036   7.160  46.656  1.00 43.44           C  
ANISOU 2843  C   GLY B 329     6135   5516   4853    -60   -296    380       C  
ATOM   2844  O   GLY B 329     -35.517   8.283  46.566  1.00 37.77           O  
ANISOU 2844  O   GLY B 329     5389   4810   4151    -44   -262    341       O  
ATOM   2845  N   ALA B 330     -36.058   6.461  47.792  1.00 39.92           N  
ANISOU 2845  N   ALA B 330     5715   5080   4374    -82   -340    411       N  
ATOM   2846  CA  ALA B 330     -35.526   7.029  49.021  1.00 44.29           C  
ANISOU 2846  CA  ALA B 330     6261   5668   4900    -93   -350    399       C  
ATOM   2847  C   ALA B 330     -34.040   7.314  48.882  1.00 41.14           C  
ANISOU 2847  C   ALA B 330     5837   5254   4539    -60   -368    362       C  
ATOM   2848  O   ALA B 330     -33.305   6.528  48.305  1.00 41.50           O  
ANISOU 2848  O   ALA B 330     5884   5260   4624    -31   -402    365       O  
ATOM   2849  CB  ALA B 330     -35.783   6.078  50.221  1.00 40.45           C  
ANISOU 2849  CB  ALA B 330     5806   5197   4368   -125   -402    447       C  
ATOM   2850  N   LEU B 331     -33.598   8.456  49.404  1.00 33.77           N  
ANISOU 2850  N   LEU B 331     4881   4354   3595    -66   -341    323       N  
ATOM   2851  CA  LEU B 331     -32.164   8.719  49.490  1.00 38.75           C  
ANISOU 2851  CA  LEU B 331     5488   4984   4252    -44   -363    290       C  
ATOM   2852  C   LEU B 331     -31.805   9.209  50.891  1.00 41.70           C  
ANISOU 2852  C   LEU B 331     5856   5410   4577    -76   -375    281       C  
ATOM   2853  O   LEU B 331     -32.487  10.076  51.467  1.00 35.44           O  
ANISOU 2853  O   LEU B 331     5065   4651   3748   -109   -331    264       O  
ATOM   2854  CB  LEU B 331     -31.752   9.772  48.466  1.00 42.79           C  
ANISOU 2854  CB  LEU B 331     5970   5483   4807    -20   -310    239       C  
ATOM   2855  CG  LEU B 331     -32.239   9.572  47.024  1.00 40.87           C  
ANISOU 2855  CG  LEU B 331     5726   5200   4602      3   -283    243       C  
ATOM   2856  CD1 LEU B 331     -32.243  10.940  46.307  1.00 44.89           C  
ANISOU 2856  CD1 LEU B 331     6209   5713   5134     12   -215    201       C  
ATOM   2857  CD2 LEU B 331     -31.373   8.580  46.293  1.00 37.66           C  
ANISOU 2857  CD2 LEU B 331     5316   4753   4237     36   -325    245       C  
ATOM   2858  N   ASP B 332     -30.724   8.684  51.454  1.00 41.35           N  
ANISOU 2858  N   ASP B 332     5802   5376   4533    -69   -433    290       N  
ATOM   2859  CA  ASP B 332     -30.319   9.207  52.739  1.00 38.80           C  
ANISOU 2859  CA  ASP B 332     5470   5112   4159   -106   -445    277       C  
ATOM   2860  C   ASP B 332     -29.454  10.422  52.524  1.00 42.12           C  
ANISOU 2860  C   ASP B 332     5857   5548   4600   -103   -407    211       C  
ATOM   2861  O   ASP B 332     -29.100  10.784  51.384  1.00 37.62           O  
ANISOU 2861  O   ASP B 332     5270   4941   4085    -69   -378    181       O  
ATOM   2862  CB  ASP B 332     -29.616   8.139  53.590  1.00 49.91           C  
ANISOU 2862  CB  ASP B 332     6880   6538   5547   -107   -526    325       C  
ATOM   2863  CG  ASP B 332     -28.321   7.628  52.963  1.00 53.40           C  
ANISOU 2863  CG  ASP B 332     7295   6949   6047    -56   -566    323       C  
ATOM   2864  OD1 ASP B 332     -27.607   8.410  52.291  1.00 47.33           O  
ANISOU 2864  OD1 ASP B 332     6495   6175   5314    -37   -535    269       O  
ATOM   2865  OD2 ASP B 332     -28.007   6.427  53.165  1.00 52.30           O  
ANISOU 2865  OD2 ASP B 332     7164   6790   5917    -36   -627    377       O  
ATOM   2866  N   ASP B 333     -29.099  11.067  53.617  1.00 34.41           N  
ANISOU 2866  N   ASP B 333     4869   4628   3576   -143   -406    187       N  
ATOM   2867  CA  ASP B 333     -28.400  12.344  53.501  1.00 41.23           C  
ANISOU 2867  CA  ASP B 333     5705   5507   4452   -152   -360    118       C  
ATOM   2868  C   ASP B 333     -27.066  12.243  52.736  1.00 46.67           C  
ANISOU 2868  C   ASP B 333     6360   6177   5195   -113   -385     98       C  
ATOM   2869  O   ASP B 333     -26.676  13.190  52.069  1.00 47.83           O  
ANISOU 2869  O   ASP B 333     6488   6309   5375   -105   -336     46       O  
ATOM   2870  CB  ASP B 333     -28.245  12.986  54.880  1.00 41.58           C  
ANISOU 2870  CB  ASP B 333     5747   5621   4430   -212   -356     92       C  
ATOM   2871  CG  ASP B 333     -29.548  13.572  55.375  1.00 46.03           C  
ANISOU 2871  CG  ASP B 333     6337   6197   4955   -249   -298     83       C  
ATOM   2872  OD1 ASP B 333     -30.482  13.648  54.554  1.00 46.39           O  
ANISOU 2872  OD1 ASP B 333     6397   6198   5032   -225   -256     93       O  
ATOM   2873  OD2 ASP B 333     -29.645  13.990  56.552  1.00 55.45           O  
ANISOU 2873  OD2 ASP B 333     7535   7448   6087   -304   -291     65       O  
ATOM   2874  N   VAL B 334     -26.367  11.113  52.799  1.00 39.03           N  
ANISOU 2874  N   VAL B 334     5384   5207   4239    -86   -457    139       N  
ATOM   2875  CA  VAL B 334     -25.111  11.069  52.043  1.00 40.54           C  
ANISOU 2875  CA  VAL B 334     5537   5381   4484    -46   -474    116       C  
ATOM   2876  C   VAL B 334     -25.379  10.801  50.554  1.00 42.89           C  
ANISOU 2876  C   VAL B 334     5841   5610   4846      1   -447    114       C  
ATOM   2877  O   VAL B 334     -24.649  11.282  49.689  1.00 43.28           O  
ANISOU 2877  O   VAL B 334     5863   5643   4939     25   -423     73       O  
ATOM   2878  CB  VAL B 334     -24.044  10.094  52.621  1.00 46.68           C  
ANISOU 2878  CB  VAL B 334     6291   6185   5259    -28   -556    155       C  
ATOM   2879  CG1 VAL B 334     -23.843  10.339  54.131  1.00 49.52           C  
ANISOU 2879  CG1 VAL B 334     6644   6625   5544    -82   -586    162       C  
ATOM   2880  CG2 VAL B 334     -24.384   8.649  52.334  1.00 49.56           C  
ANISOU 2880  CG2 VAL B 334     6681   6502   5650     11   -603    221       C  
ATOM   2881  N   GLU B 335     -26.442  10.057  50.266  1.00 33.86           N  
ANISOU 2881  N   GLU B 335     4733   4431   3703     10   -448    156       N  
ATOM   2882  CA  GLU B 335     -26.768   9.748  48.890  1.00 33.80           C  
ANISOU 2882  CA  GLU B 335     4731   4365   3745     45   -424    156       C  
ATOM   2883  C   GLU B 335     -27.273  10.996  48.215  1.00 40.26           C  
ANISOU 2883  C   GLU B 335     5546   5179   4574     35   -348    113       C  
ATOM   2884  O   GLU B 335     -26.883  11.274  47.066  1.00 41.50           O  
ANISOU 2884  O   GLU B 335     5684   5307   4777     62   -321     85       O  
ATOM   2885  CB  GLU B 335     -27.837   8.651  48.804  1.00 33.65           C  
ANISOU 2885  CB  GLU B 335     4752   4315   3718     47   -443    211       C  
ATOM   2886  CG  GLU B 335     -27.401   7.321  49.366  1.00 47.17           C  
ANISOU 2886  CG  GLU B 335     6474   6018   5430     62   -516    261       C  
ATOM   2887  CD  GLU B 335     -28.528   6.306  49.347  1.00 53.93           C  
ANISOU 2887  CD  GLU B 335     7374   6842   6274     53   -530    314       C  
ATOM   2888  OE1 GLU B 335     -29.595   6.586  49.958  1.00 44.99           O  
ANISOU 2888  OE1 GLU B 335     6265   5737   5091     13   -511    330       O  
ATOM   2889  OE2 GLU B 335     -28.354   5.239  48.714  1.00 63.33           O  
ANISOU 2889  OE2 GLU B 335     8577   7982   7505     84   -556    336       O  
ATOM   2890  N   ILE B 336     -28.121  11.772  48.907  1.00 34.26           N  
ANISOU 2890  N   ILE B 336     4800   4447   3771     -3   -310    107       N  
ATOM   2891  CA  ILE B 336     -28.702  12.914  48.229  1.00 36.96           C  
ANISOU 2891  CA  ILE B 336     5139   4776   4129     -6   -234     76       C  
ATOM   2892  C   ILE B 336     -27.591  13.922  47.945  1.00 39.34           C  
ANISOU 2892  C   ILE B 336     5408   5084   4458     -3   -207     18       C  
ATOM   2893  O   ILE B 336     -27.613  14.593  46.911  1.00 37.24           O  
ANISOU 2893  O   ILE B 336     5130   4791   4229     13   -158     -5       O  
ATOM   2894  CB  ILE B 336     -29.892  13.536  48.979  1.00 30.88           C  
ANISOU 2894  CB  ILE B 336     4390   4029   3315    -42   -191     81       C  
ATOM   2895  CG1 ILE B 336     -30.779  14.317  47.997  1.00 35.17           C  
ANISOU 2895  CG1 ILE B 336     4933   4546   3885    -30   -120     75       C  
ATOM   2896  CG2 ILE B 336     -29.404  14.447  50.071  1.00 31.89           C  
ANISOU 2896  CG2 ILE B 336     4509   4198   3410    -80   -175     40       C  
ATOM   2897  CD1 ILE B 336     -32.029  14.965  48.664  1.00 32.72           C  
ANISOU 2897  CD1 ILE B 336     4639   4255   3539    -58    -70     81       C  
ATOM   2898  N   LEU B 337     -26.569  13.956  48.811  1.00 37.27           N  
ANISOU 2898  N   LEU B 337     5127   4857   4175    -20   -242     -1       N  
ATOM   2899  CA  LEU B 337     -25.428  14.824  48.558  1.00 36.75           C  
ANISOU 2899  CA  LEU B 337     5029   4802   4134    -22   -222    -55       C  
ATOM   2900  C   LEU B 337     -24.517  14.306  47.430  1.00 35.38           C  
ANISOU 2900  C   LEU B 337     4828   4599   4014     24   -245    -60       C  
ATOM   2901  O   LEU B 337     -24.029  15.096  46.613  1.00 36.67           O  
ANISOU 2901  O   LEU B 337     4971   4749   4212     31   -203   -100       O  
ATOM   2902  CB  LEU B 337     -24.619  15.054  49.852  1.00 40.30           C  
ANISOU 2902  CB  LEU B 337     5462   5310   4539    -60   -253    -76       C  
ATOM   2903  CG  LEU B 337     -25.364  15.985  50.812  1.00 46.65           C  
ANISOU 2903  CG  LEU B 337     6287   6142   5295   -113   -205    -99       C  
ATOM   2904  CD1 LEU B 337     -24.570  16.262  52.088  1.00 46.29           C  
ANISOU 2904  CD1 LEU B 337     6226   6164   5198   -161   -233   -125       C  
ATOM   2905  CD2 LEU B 337     -25.681  17.275  50.110  1.00 49.44           C  
ANISOU 2905  CD2 LEU B 337     6642   6463   5679   -116   -119   -144       C  
ATOM   2906  N   ARG B 338     -24.286  12.995  47.382  1.00 34.14           N  
ANISOU 2906  N   ARG B 338     4673   4432   3867     53   -307    -19       N  
ATOM   2907  CA  ARG B 338     -23.494  12.419  46.307  1.00 42.15           C  
ANISOU 2907  CA  ARG B 338     5665   5416   4934     97   -325    -25       C  
ATOM   2908  C   ARG B 338     -24.210  12.666  44.974  1.00 38.69           C  
ANISOU 2908  C   ARG B 338     5238   4935   4529    113   -272    -30       C  
ATOM   2909  O   ARG B 338     -23.558  12.911  43.956  1.00 38.55           O  
ANISOU 2909  O   ARG B 338     5195   4901   4551    134   -252    -60       O  
ATOM   2910  CB  ARG B 338     -23.248  10.914  46.523  1.00 49.34           C  
ANISOU 2910  CB  ARG B 338     6580   6313   5853    128   -396     23       C  
ATOM   2911  CG  ARG B 338     -22.016  10.570  47.394  1.00 51.09           C  
ANISOU 2911  CG  ARG B 338     6769   6575   6068    133   -455     27       C  
ATOM   2912  CD  ARG B 338     -21.544   9.130  47.120  1.00 58.29           C  
ANISOU 2912  CD  ARG B 338     7677   7454   7017    182   -512     67       C  
ATOM   2913  NE  ARG B 338     -22.662   8.277  46.727  1.00 64.56           N  
ANISOU 2913  NE  ARG B 338     8516   8197   7816    191   -511    106       N  
ATOM   2914  CZ  ARG B 338     -23.222   7.353  47.503  1.00 70.08           C  
ANISOU 2914  CZ  ARG B 338     9247   8891   8490    186   -553    163       C  
ATOM   2915  NH1 ARG B 338     -24.255   6.644  47.044  1.00 71.60           N  
ANISOU 2915  NH1 ARG B 338     9481   9036   8687    188   -545    193       N  
ATOM   2916  NH2 ARG B 338     -22.752   7.129  48.729  1.00 69.31           N  
ANISOU 2916  NH2 ARG B 338     9139   8837   8359    174   -604    192       N  
ATOM   2917  N   ALA B 339     -25.545  12.599  44.995  1.00 32.63           N  
ANISOU 2917  N   ALA B 339     4505   4155   3739    100   -251      0       N  
ATOM   2918  CA  ALA B 339     -26.363  12.990  43.837  1.00 34.99           C  
ANISOU 2918  CA  ALA B 339     4811   4426   4058    107   -197      1       C  
ATOM   2919  C   ALA B 339     -26.099  14.410  43.412  1.00 37.19           C  
ANISOU 2919  C   ALA B 339     5069   4709   4352     98   -135    -42       C  
ATOM   2920  O   ALA B 339     -25.839  14.649  42.248  1.00 32.49           O  
ANISOU 2920  O   ALA B 339     4458   4095   3792    116   -108    -58       O  
ATOM   2921  CB  ALA B 339     -27.836  12.808  44.126  1.00 40.01           C  
ANISOU 2921  CB  ALA B 339     5481   5061   4662     90   -184     42       C  
ATOM   2922  N   ARG B 340     -26.162  15.364  44.342  1.00 33.85           N  
ANISOU 2922  N   ARG B 340     4649   4311   3904     67   -108    -63       N  
ATOM   2923  CA  ARG B 340     -25.967  16.759  43.979  1.00 33.34           C  
ANISOU 2923  CA  ARG B 340     4570   4242   3857     55    -42   -104       C  
ATOM   2924  C   ARG B 340     -24.589  16.951  43.420  1.00 34.91           C  
ANISOU 2924  C   ARG B 340     4733   4442   4087     66    -50   -143       C  
ATOM   2925  O   ARG B 340     -24.387  17.703  42.473  1.00 35.65           O  
ANISOU 2925  O   ARG B 340     4813   4518   4213     73     -3   -165       O  
ATOM   2926  CB  ARG B 340     -26.168  17.702  45.177  1.00 33.20           C  
ANISOU 2926  CB  ARG B 340     4561   4248   3804     15    -12   -128       C  
ATOM   2927  CG  ARG B 340     -26.301  19.177  44.720  1.00 51.77           C  
ANISOU 2927  CG  ARG B 340     6909   6581   6181      5     71   -162       C  
ATOM   2928  CD  ARG B 340     -25.549  20.153  45.630  1.00 52.80           C  
ANISOU 2928  CD  ARG B 340     7032   6733   6296    -36     95   -218       C  
ATOM   2929  NE  ARG B 340     -24.205  19.666  45.919  1.00 59.39           N  
ANISOU 2929  NE  ARG B 340     7841   7600   7126    -41     37   -241       N  
ATOM   2930  CZ  ARG B 340     -23.091  20.166  45.394  1.00 60.90           C  
ANISOU 2930  CZ  ARG B 340     8002   7791   7346    -42     48   -281       C  
ATOM   2931  NH1 ARG B 340     -21.914  19.641  45.716  1.00 57.43           N  
ANISOU 2931  NH1 ARG B 340     7534   7387   6899    -44     -9   -297       N  
ATOM   2932  NH2 ARG B 340     -23.155  21.188  44.548  1.00 65.22           N  
ANISOU 2932  NH2 ARG B 340     8548   8305   7929    -41    115   -303       N  
ATOM   2933  N   GLN B 341     -23.628  16.274  44.027  1.00 34.02           N  
ANISOU 2933  N   GLN B 341     4606   4354   3967     68   -109   -150       N  
ATOM   2934  CA  GLN B 341     -22.239  16.448  43.645  1.00 35.06           C  
ANISOU 2934  CA  GLN B 341     4697   4496   4126     77   -120   -189       C  
ATOM   2935  C   GLN B 341     -22.004  15.902  42.252  1.00 35.48           C  
ANISOU 2935  C   GLN B 341     4737   4519   4223    116   -121   -184       C  
ATOM   2936  O   GLN B 341     -21.268  16.496  41.457  1.00 36.23           O  
ANISOU 2936  O   GLN B 341     4805   4611   4348    120    -92   -220       O  
ATOM   2937  CB  GLN B 341     -21.334  15.733  44.645  1.00 42.38           C  
ANISOU 2937  CB  GLN B 341     5607   5463   5034     75   -189   -186       C  
ATOM   2938  CG  GLN B 341     -21.051  16.570  45.910  1.00 54.52           C  
ANISOU 2938  CG  GLN B 341     7140   7046   6527     25   -182   -215       C  
ATOM   2939  CD  GLN B 341     -20.479  15.741  47.051  1.00 59.44           C  
ANISOU 2939  CD  GLN B 341     7751   7716   7117     19   -256   -193       C  
ATOM   2940  OE1 GLN B 341     -19.896  14.674  46.828  1.00 58.79           O  
ANISOU 2940  OE1 GLN B 341     7650   7631   7056     58   -312   -167       O  
ATOM   2941  NE2 GLN B 341     -20.657  16.220  48.285  1.00 57.83           N  
ANISOU 2941  NE2 GLN B 341     7557   7555   6860    -29   -255   -202       N  
ATOM   2942  N   PHE B 342     -22.609  14.760  41.960  1.00 28.07           N  
ANISOU 2942  N   PHE B 342     3819   3559   3287    140   -152   -143       N  
ATOM   2943  CA  PHE B 342     -22.499  14.249  40.602  1.00 30.07           C  
ANISOU 2943  CA  PHE B 342     4062   3783   3578    171   -146   -143       C  
ATOM   2944  C   PHE B 342     -23.105  15.255  39.603  1.00 26.88           C  
ANISOU 2944  C   PHE B 342     3661   3367   3186    161    -77   -151       C  
ATOM   2945  O   PHE B 342     -22.500  15.567  38.557  1.00 26.94           O  
ANISOU 2945  O   PHE B 342     3644   3369   3223    171    -53   -177       O  
ATOM   2946  CB  PHE B 342     -23.145  12.844  40.450  1.00 31.32           C  
ANISOU 2946  CB  PHE B 342     4247   3917   3735    192   -186   -100       C  
ATOM   2947  CG  PHE B 342     -23.309  12.448  39.024  1.00 28.87           C  
ANISOU 2947  CG  PHE B 342     3934   3579   3454    211   -166   -102       C  
ATOM   2948  CD1 PHE B 342     -24.549  12.525  38.395  1.00 32.03           C  
ANISOU 2948  CD1 PHE B 342     4359   3968   3843    200   -134    -76       C  
ATOM   2949  CD2 PHE B 342     -22.197  12.082  38.284  1.00 31.21           C  
ANISOU 2949  CD2 PHE B 342     4200   3870   3790    236   -177   -134       C  
ATOM   2950  CE1 PHE B 342     -24.678  12.214  37.036  1.00 28.51           C  
ANISOU 2950  CE1 PHE B 342     3908   3507   3418    210   -114    -81       C  
ATOM   2951  CE2 PHE B 342     -22.311  11.765  36.951  1.00 33.34           C  
ANISOU 2951  CE2 PHE B 342     4466   4119   4082    248   -154   -143       C  
ATOM   2952  CZ  PHE B 342     -23.552  11.847  36.310  1.00 31.67           C  
ANISOU 2952  CZ  PHE B 342     4280   3899   3854    232   -123   -117       C  
ATOM   2953  N   VAL B 343     -24.283  15.788  39.916  1.00 24.65           N  
ANISOU 2953  N   VAL B 343     3405   3082   2879    142    -44   -127       N  
ATOM   2954  CA  VAL B 343     -24.930  16.741  38.988  1.00 29.66           C  
ANISOU 2954  CA  VAL B 343     4040   3705   3526    138     21   -123       C  
ATOM   2955  C   VAL B 343     -24.076  17.986  38.818  1.00 32.98           C  
ANISOU 2955  C   VAL B 343     4436   4129   3967    125     64   -168       C  
ATOM   2956  O   VAL B 343     -23.866  18.486  37.696  1.00 29.44           O  
ANISOU 2956  O   VAL B 343     3970   3670   3544    131    100   -177       O  
ATOM   2957  CB  VAL B 343     -26.332  17.108  39.460  1.00 31.55           C  
ANISOU 2957  CB  VAL B 343     4307   3943   3739    124     49    -87       C  
ATOM   2958  CG1 VAL B 343     -26.907  18.216  38.587  1.00 34.35           C  
ANISOU 2958  CG1 VAL B 343     4656   4286   4111    123    119    -80       C  
ATOM   2959  CG2 VAL B 343     -27.228  15.850  39.396  1.00 34.70           C  
ANISOU 2959  CG2 VAL B 343     4728   4338   4118    133     11    -42       C  
ATOM   2960  N   ASP B 344     -23.497  18.449  39.922  1.00 30.02           N  
ANISOU 2960  N   ASP B 344     4058   3772   3578    103     57   -197       N  
ATOM   2961  CA  ASP B 344     -22.617  19.595  39.840  1.00 31.70           C  
ANISOU 2961  CA  ASP B 344     4249   3989   3807     84     97   -244       C  
ATOM   2962  C   ASP B 344     -21.452  19.316  38.911  1.00 31.96           C  
ANISOU 2962  C   ASP B 344     4247   4027   3871    100     82   -270       C  
ATOM   2963  O   ASP B 344     -21.157  20.106  38.039  1.00 33.73           O  
ANISOU 2963  O   ASP B 344     4457   4241   4120     96    127   -289       O  
ATOM   2964  CB  ASP B 344     -22.057  19.924  41.218  1.00 42.02           C  
ANISOU 2964  CB  ASP B 344     5554   5323   5086     52     81   -276       C  
ATOM   2965  CG  ASP B 344     -21.338  21.224  41.233  1.00 48.48           C  
ANISOU 2965  CG  ASP B 344     6357   6144   5917     22    132   -326       C  
ATOM   2966  OD1 ASP B 344     -22.019  22.250  41.341  1.00 53.99           O  
ANISOU 2966  OD1 ASP B 344     7076   6821   6617      3    194   -330       O  
ATOM   2967  OD2 ASP B 344     -20.096  21.232  41.109  1.00 63.18           O  
ANISOU 2967  OD2 ASP B 344     8187   8029   7792     16    112   -362       O  
ATOM   2968  N   SER B 345     -20.792  18.177  39.087  1.00 30.79           N  
ANISOU 2968  N   SER B 345     4084   3893   3723    120     19   -270       N  
ATOM   2969  CA  SER B 345     -19.645  17.874  38.252  1.00 33.46           C  
ANISOU 2969  CA  SER B 345     4385   4238   4092    139      6   -299       C  
ATOM   2970  C   SER B 345     -20.035  17.643  36.798  1.00 30.18           C  
ANISOU 2970  C   SER B 345     3969   3799   3700    158     31   -285       C  
ATOM   2971  O   SER B 345     -19.285  18.008  35.895  1.00 29.86           O  
ANISOU 2971  O   SER B 345     3900   3762   3684    160     54   -314       O  
ATOM   2972  CB  SER B 345     -18.853  16.666  38.798  1.00 33.82           C  
ANISOU 2972  CB  SER B 345     4411   4300   4137    162    -66   -298       C  
ATOM   2973  OG  SER B 345     -19.236  15.493  38.128  1.00 50.80           O  
ANISOU 2973  OG  SER B 345     6572   6426   6302    196    -91   -270       O  
ATOM   2974  N   TYR B 346     -21.205  17.038  36.560  1.00 28.92           N  
ANISOU 2974  N   TYR B 346     3840   3621   3528    169     26   -242       N  
ATOM   2975  CA  TYR B 346     -21.707  16.861  35.186  1.00 29.05           C  
ANISOU 2975  CA  TYR B 346     3856   3623   3558    179     52   -226       C  
ATOM   2976  C   TYR B 346     -21.884  18.208  34.532  1.00 28.60           C  
ANISOU 2976  C   TYR B 346     3792   3565   3509    161    118   -230       C  
ATOM   2977  O   TYR B 346     -21.461  18.392  33.391  1.00 26.56           O  
ANISOU 2977  O   TYR B 346     3512   3309   3269    163    141   -244       O  
ATOM   2978  CB  TYR B 346     -23.043  16.095  35.186  1.00 28.14           C  
ANISOU 2978  CB  TYR B 346     3775   3495   3421    184     39   -177       C  
ATOM   2979  CG  TYR B 346     -23.556  15.901  33.793  1.00 21.35           C  
ANISOU 2979  CG  TYR B 346     2913   2632   2568    187     64   -161       C  
ATOM   2980  CD1 TYR B 346     -23.316  14.697  33.112  1.00 25.57           C  
ANISOU 2980  CD1 TYR B 346     3444   3159   3111    203     34   -168       C  
ATOM   2981  CD2 TYR B 346     -24.269  16.914  33.144  1.00 21.97           C  
ANISOU 2981  CD2 TYR B 346     2991   2714   2642    173    118   -140       C  
ATOM   2982  CE1 TYR B 346     -23.766  14.526  31.813  1.00 24.01           C  
ANISOU 2982  CE1 TYR B 346     3244   2966   2913    197     58   -158       C  
ATOM   2983  CE2 TYR B 346     -24.728  16.755  31.871  1.00 24.30           C  
ANISOU 2983  CE2 TYR B 346     3280   3017   2937    172    138   -122       C  
ATOM   2984  CZ  TYR B 346     -24.456  15.577  31.196  1.00 26.72           C  
ANISOU 2984  CZ  TYR B 346     3583   3323   3247    180    108   -134       C  
ATOM   2985  OH  TYR B 346     -24.921  15.435  29.909  1.00 24.82           O  
ANISOU 2985  OH  TYR B 346     3336   3096   2999    171    131   -120       O  
ATOM   2986  N   TYR B 347     -22.491  19.161  35.252  1.00 25.72           N  
ANISOU 2986  N   TYR B 347     3446   3196   3132    142    151   -219       N  
ATOM   2987  CA  TYR B 347     -22.767  20.481  34.654  1.00 28.76           C  
ANISOU 2987  CA  TYR B 347     3827   3570   3531    128    219   -215       C  
ATOM   2988  C   TYR B 347     -21.484  21.266  34.385  1.00 33.56           C  
ANISOU 2988  C   TYR B 347     4406   4183   4161    113    241   -265       C  
ATOM   2989  O   TYR B 347     -21.434  22.082  33.453  1.00 28.44           O  
ANISOU 2989  O   TYR B 347     3748   3528   3532    106    290   -263       O  
ATOM   2990  CB  TYR B 347     -23.738  21.343  35.502  1.00 27.72           C  
ANISOU 2990  CB  TYR B 347     3722   3424   3386    114    256   -194       C  
ATOM   2991  CG  TYR B 347     -25.220  20.989  35.487  1.00 29.41           C  
ANISOU 2991  CG  TYR B 347     3960   3634   3582    125    259   -137       C  
ATOM   2992  CD1 TYR B 347     -25.988  21.219  36.624  1.00 29.14           C  
ANISOU 2992  CD1 TYR B 347     3950   3595   3527    117    266   -124       C  
ATOM   2993  CD2 TYR B 347     -25.843  20.389  34.376  1.00 26.93           C  
ANISOU 2993  CD2 TYR B 347     3642   3325   3266    140    254    -99       C  
ATOM   2994  CE1 TYR B 347     -27.321  20.920  36.669  1.00 30.54           C  
ANISOU 2994  CE1 TYR B 347     4145   3773   3686    125    269    -74       C  
ATOM   2995  CE2 TYR B 347     -27.214  20.101  34.408  1.00 29.34           C  
ANISOU 2995  CE2 TYR B 347     3964   3632   3550    145    257    -46       C  
ATOM   2996  CZ  TYR B 347     -27.930  20.358  35.562  1.00 28.87           C  
ANISOU 2996  CZ  TYR B 347     3927   3568   3473    139    264    -34       C  
ATOM   2997  OH  TYR B 347     -29.257  20.058  35.638  1.00 26.64           O  
ANISOU 2997  OH  TYR B 347     3659   3294   3170    143    266     17       O  
ATOM   2998  N   ARG B 348     -20.447  21.056  35.204  1.00 30.93           N  
ANISOU 2998  N   ARG B 348     4059   3868   3826    106    207   -306       N  
ATOM   2999  CA  ARG B 348     -19.153  21.727  35.002  1.00 33.63           C  
ANISOU 2999  CA  ARG B 348     4369   4223   4187     87    224   -357       C  
ATOM   3000  C   ARG B 348     -18.476  21.238  33.732  1.00 32.98           C  
ANISOU 3000  C   ARG B 348     4255   4150   4125    104    217   -368       C  
ATOM   3001  O   ARG B 348     -17.758  21.982  33.059  1.00 35.96           O  
ANISOU 3001  O   ARG B 348     4610   4534   4521     88    252   -396       O  
ATOM   3002  CB  ARG B 348     -18.229  21.504  36.216  1.00 40.14           C  
ANISOU 3002  CB  ARG B 348     5178   5075   4997     75    181   -394       C  
ATOM   3003  CG  ARG B 348     -18.844  22.042  37.482  1.00 50.36           C  
ANISOU 3003  CG  ARG B 348     6503   6366   6266     50    192   -390       C  
ATOM   3004  CD  ARG B 348     -17.880  22.167  38.654  1.00 60.16           C  
ANISOU 3004  CD  ARG B 348     7727   7642   7488     22    163   -432       C  
ATOM   3005  NE  ARG B 348     -18.599  22.765  39.778  1.00 73.28           N  
ANISOU 3005  NE  ARG B 348     9422   9300   9122     -7    185   -431       N  
ATOM   3006  CZ  ARG B 348     -18.162  23.779  40.518  1.00 80.58           C  
ANISOU 3006  CZ  ARG B 348    10346  10235  10035    -53    218   -475       C  
ATOM   3007  NH1 ARG B 348     -16.969  24.319  40.286  1.00 80.19           N  
ANISOU 3007  NH1 ARG B 348    10264  10205   9999    -78    229   -522       N  
ATOM   3008  NH2 ARG B 348     -18.926  24.245  41.501  1.00 81.81           N  
ANISOU 3008  NH2 ARG B 348    10535  10385  10166    -79    241   -474       N  
ATOM   3009  N   THR B 349     -18.737  19.991  33.356  1.00 28.24           N  
ANISOU 3009  N   THR B 349     3657   3551   3522    133    176   -349       N  
ATOM   3010  CA  THR B 349     -18.236  19.499  32.083  1.00 27.59           C  
ANISOU 3010  CA  THR B 349     3548   3477   3458    147    176   -361       C  
ATOM   3011  C   THR B 349     -19.097  19.825  30.866  1.00 30.17           C  
ANISOU 3011  C   THR B 349     3885   3795   3783    142    220   -328       C  
ATOM   3012  O   THR B 349     -18.598  20.260  29.831  1.00 31.46           O  
ANISOU 3012  O   THR B 349     4025   3969   3960    133    251   -343       O  
ATOM   3013  CB  THR B 349     -18.119  17.975  32.173  1.00 33.77           C  
ANISOU 3013  CB  THR B 349     4330   4260   4242    179    118   -359       C  
ATOM   3014  OG1 THR B 349     -17.134  17.689  33.161  1.00 37.59           O  
ANISOU 3014  OG1 THR B 349     4794   4759   4730    186     77   -387       O  
ATOM   3015  CG2 THR B 349     -17.727  17.366  30.843  1.00 32.08           C  
ANISOU 3015  CG2 THR B 349     4094   4050   4044    192    122   -375       C  
ATOM   3016  N   TRP B 350     -20.395  19.607  30.979  1.00 22.19           N  
ANISOU 3016  N   TRP B 350     2906   2771   2754    147    220   -279       N  
ATOM   3017  CA  TRP B 350     -21.288  19.672  29.829  1.00 24.53           C  
ANISOU 3017  CA  TRP B 350     3207   3069   3043    145    250   -240       C  
ATOM   3018  C   TRP B 350     -22.167  20.921  29.778  1.00 27.43           C  
ANISOU 3018  C   TRP B 350     3589   3426   3408    131    304   -200       C  
ATOM   3019  O   TRP B 350     -22.853  21.142  28.771  1.00 26.22           O  
ANISOU 3019  O   TRP B 350     3432   3280   3249    128    332   -161       O  
ATOM   3020  CB  TRP B 350     -22.218  18.474  29.893  1.00 22.64           C  
ANISOU 3020  CB  TRP B 350     2991   2828   2783    159    213   -208       C  
ATOM   3021  CG  TRP B 350     -21.502  17.181  29.658  1.00 22.22           C  
ANISOU 3021  CG  TRP B 350     2927   2777   2738    175    168   -240       C  
ATOM   3022  CD1 TRP B 350     -21.099  16.271  30.590  1.00 31.84           C  
ANISOU 3022  CD1 TRP B 350     4153   3985   3960    193    117   -256       C  
ATOM   3023  CD2 TRP B 350     -21.132  16.674  28.400  1.00 22.02           C  
ANISOU 3023  CD2 TRP B 350     2883   2765   2720    175    174   -259       C  
ATOM   3024  NE1 TRP B 350     -20.504  15.178  29.964  1.00 28.77           N  
ANISOU 3024  NE1 TRP B 350     3750   3595   3586    210     93   -282       N  
ATOM   3025  CE2 TRP B 350     -20.522  15.411  28.609  1.00 31.03           C  
ANISOU 3025  CE2 TRP B 350     4021   3896   3874    197    129   -289       C  
ATOM   3026  CE3 TRP B 350     -21.295  17.135  27.092  1.00 23.32           C  
ANISOU 3026  CE3 TRP B 350     3031   2949   2878    157    215   -252       C  
ATOM   3027  CZ2 TRP B 350     -20.030  14.650  27.569  1.00 29.11           C  
ANISOU 3027  CZ2 TRP B 350     3760   3659   3642    202    129   -320       C  
ATOM   3028  CZ3 TRP B 350     -20.825  16.369  26.056  1.00 28.92           C  
ANISOU 3028  CZ3 TRP B 350     3724   3673   3592    157    212   -281       C  
ATOM   3029  CH2 TRP B 350     -20.197  15.129  26.306  1.00 26.63           C  
ANISOU 3029  CH2 TRP B 350     3432   3369   3318    180    171   -318       C  
ATOM   3030  N   GLY B 351     -22.216  21.688  30.862  1.00 28.98           N  
ANISOU 3030  N   GLY B 351     3799   3605   3607    124    319   -205       N  
ATOM   3031  CA  GLY B 351     -23.160  22.810  30.972  1.00 27.49           C  
ANISOU 3031  CA  GLY B 351     3626   3396   3421    117    373   -166       C  
ATOM   3032  C   GLY B 351     -24.578  22.252  31.193  1.00 31.58           C  
ANISOU 3032  C   GLY B 351     4168   3916   3917    131    359   -111       C  
ATOM   3033  O   GLY B 351     -24.771  21.023  31.338  1.00 29.21           O  
ANISOU 3033  O   GLY B 351     3874   3627   3597    140    308   -108       O  
ATOM   3034  N   GLY B 352     -25.576  23.132  31.228  1.00 25.39           N  
ANISOU 3034  N   GLY B 352     3395   3117   3135    132    406    -67       N  
ATOM   3035  CA  GLY B 352     -26.933  22.708  31.573  1.00 29.95           C  
ANISOU 3035  CA  GLY B 352     3990   3699   3690    143    397    -16       C  
ATOM   3036  C   GLY B 352     -27.930  22.944  30.479  1.00 28.11           C  
ANISOU 3036  C   GLY B 352     3746   3480   3453    150    426     47       C  
ATOM   3037  O   GLY B 352     -29.120  23.028  30.749  1.00 27.70           O  
ANISOU 3037  O   GLY B 352     3704   3430   3390    159    438     96       O  
ATOM   3038  N   ARG B 353     -27.467  22.985  29.221  1.00 26.27           N  
ANISOU 3038  N   ARG B 353     3490   3265   3227    145    435     50       N  
ATOM   3039  CA  ARG B 353     -28.352  23.360  28.107  1.00 27.45           C  
ANISOU 3039  CA  ARG B 353     3624   3436   3371    147    466    116       C  
ATOM   3040  C   ARG B 353     -28.989  22.172  27.413  1.00 27.35           C  
ANISOU 3040  C   ARG B 353     3605   3465   3321    143    427    143       C  
ATOM   3041  O   ARG B 353     -29.823  22.341  26.565  1.00 27.05           O  
ANISOU 3041  O   ARG B 353     3552   3456   3269    141    445    200       O  
ATOM   3042  CB  ARG B 353     -27.562  24.163  27.077  1.00 27.06           C  
ANISOU 3042  CB  ARG B 353     3551   3388   3342    137    503    110       C  
ATOM   3043  CG  ARG B 353     -26.871  25.430  27.671  1.00 25.26           C  
ANISOU 3043  CG  ARG B 353     3329   3115   3153    134    549     81       C  
ATOM   3044  CD  ARG B 353     -26.151  26.216  26.571  1.00 24.65           C  
ANISOU 3044  CD  ARG B 353     3230   3042   3095    120    587     82       C  
ATOM   3045  NE  ARG B 353     -27.066  26.763  25.558  1.00 27.34           N  
ANISOU 3045  NE  ARG B 353     3555   3398   3434    126    622    163       N  
ATOM   3046  CZ  ARG B 353     -27.679  27.944  25.667  1.00 33.25           C  
ANISOU 3046  CZ  ARG B 353     4308   4114   4211    139    679    213       C  
ATOM   3047  NH1 ARG B 353     -28.468  28.393  24.693  1.00 31.48           N  
ANISOU 3047  NH1 ARG B 353     4065   3910   3986    148    708    293       N  
ATOM   3048  NH2 ARG B 353     -27.501  28.672  26.760  1.00 30.99           N  
ANISOU 3048  NH2 ARG B 353     4045   3775   3955    143    709    182       N  
ATOM   3049  N   TYR B 354     -28.605  20.961  27.780  1.00 24.64           N  
ANISOU 3049  N   TYR B 354     3274   3125   2963    139    374    102       N  
ATOM   3050  CA  TYR B 354     -29.174  19.794  27.092  1.00 24.48           C  
ANISOU 3050  CA  TYR B 354     3252   3139   2910    129    341    120       C  
ATOM   3051  C   TYR B 354     -29.728  18.819  28.133  1.00 23.47           C  
ANISOU 3051  C   TYR B 354     3153   3001   2763    133    298    118       C  
ATOM   3052  O   TYR B 354     -30.948  18.688  28.285  1.00 25.08           O  
ANISOU 3052  O   TYR B 354     3364   3222   2944    132    299    169       O  
ATOM   3053  CB  TYR B 354     -28.101  19.148  26.177  1.00 22.50           C  
ANISOU 3053  CB  TYR B 354     2986   2901   2660    117    323     70       C  
ATOM   3054  CG  TYR B 354     -28.605  17.909  25.414  1.00 23.19           C  
ANISOU 3054  CG  TYR B 354     3075   3020   2714    101    294     78       C  
ATOM   3055  CD1 TYR B 354     -29.699  17.997  24.546  1.00 23.16           C  
ANISOU 3055  CD1 TYR B 354     3059   3060   2679     84    310    137       C  
ATOM   3056  CD2 TYR B 354     -27.972  16.707  25.555  1.00 26.87           C  
ANISOU 3056  CD2 TYR B 354     3554   3475   3183    101    254     26       C  
ATOM   3057  CE1 TYR B 354     -30.181  16.854  23.855  1.00 26.64           C  
ANISOU 3057  CE1 TYR B 354     3502   3534   3084     59    286    139       C  
ATOM   3058  CE2 TYR B 354     -28.425  15.560  24.871  1.00 27.98           C  
ANISOU 3058  CE2 TYR B 354     3700   3637   3294     81    232     26       C  
ATOM   3059  CZ  TYR B 354     -29.512  15.659  24.011  1.00 25.32           C  
ANISOU 3059  CZ  TYR B 354     3353   3347   2922     57    249     79       C  
ATOM   3060  OH  TYR B 354     -29.945  14.516  23.341  1.00 31.12           O  
ANISOU 3060  OH  TYR B 354     4093   4105   3624     29    230     73       O  
ATOM   3061  N   VAL B 355     -28.855  18.125  28.857  1.00 24.02           N  
ANISOU 3061  N   VAL B 355     3236   3047   2841    138    260     65       N  
ATOM   3062  CA  VAL B 355     -29.351  17.217  29.897  1.00 23.40           C  
ANISOU 3062  CA  VAL B 355     3187   2959   2746    141    219     69       C  
ATOM   3063  C   VAL B 355     -29.603  18.029  31.139  1.00 25.37           C  
ANISOU 3063  C   VAL B 355     3448   3190   3001    149    235     76       C  
ATOM   3064  O   VAL B 355     -28.800  18.902  31.478  1.00 25.76           O  
ANISOU 3064  O   VAL B 355     3491   3222   3075    152    258     45       O  
ATOM   3065  CB  VAL B 355     -28.301  16.142  30.263  1.00 24.49           C  
ANISOU 3065  CB  VAL B 355     3333   3078   2893    147    170     15       C  
ATOM   3066  CG1 VAL B 355     -28.813  15.301  31.453  1.00 25.25           C  
ANISOU 3066  CG1 VAL B 355     3460   3161   2972    149    129     27       C  
ATOM   3067  CG2 VAL B 355     -28.049  15.240  29.045  1.00 21.82           C  
ANISOU 3067  CG2 VAL B 355     2985   2753   2551    138    158      0       C  
ATOM   3068  N   GLN B 356     -30.737  17.775  31.800  1.00 23.50           N  
ANISOU 3068  N   GLN B 356     3231   2959   2741    147    228    115       N  
ATOM   3069  CA  GLN B 356     -30.979  18.374  33.117  1.00 22.00           C  
ANISOU 3069  CA  GLN B 356     3056   2752   2551    150    240    114       C  
ATOM   3070  C   GLN B 356     -31.375  17.295  34.098  1.00 21.90           C  
ANISOU 3070  C   GLN B 356     3070   2740   2511    144    191    117       C  
ATOM   3071  O   GLN B 356     -31.718  16.168  33.684  1.00 27.22           O  
ANISOU 3071  O   GLN B 356     3752   3425   3167    138    156    131       O  
ATOM   3072  CB  GLN B 356     -32.089  19.436  33.007  1.00 29.40           C  
ANISOU 3072  CB  GLN B 356     3985   3697   3489    156    295    164       C  
ATOM   3073  CG  GLN B 356     -31.554  20.718  32.385  1.00 42.67           C  
ANISOU 3073  CG  GLN B 356     5645   5364   5204    163    349    158       C  
ATOM   3074  CD  GLN B 356     -32.634  21.804  32.296  1.00 50.42           C  
ANISOU 3074  CD  GLN B 356     6616   6344   6195    175    407    212       C  
ATOM   3075  OE1 GLN B 356     -33.575  21.706  31.500  1.00 57.87           O  
ANISOU 3075  OE1 GLN B 356     7544   7317   7125    179    416    270       O  
ATOM   3076  NE2 GLN B 356     -32.509  22.823  33.134  1.00 54.56           N  
ANISOU 3076  NE2 GLN B 356     7151   6837   6744    180    449    194       N  
ATOM   3077  N   PHE B 357     -31.321  17.598  35.391  1.00 27.03           N  
ANISOU 3077  N   PHE B 357     3703   3912   2656    378    549   -566       N  
ATOM   3078  CA  PHE B 357     -31.584  16.605  36.411  1.00 24.57           C  
ANISOU 3078  CA  PHE B 357     3309   3478   2547    303    566   -516       C  
ATOM   3079  C   PHE B 357     -32.596  17.159  37.381  1.00 22.51           C  
ANISOU 3079  C   PHE B 357     3198   3261   2093    405    558   -405       C  
ATOM   3080  O   PHE B 357     -32.591  18.350  37.669  1.00 26.21           O  
ANISOU 3080  O   PHE B 357     3897   3744   2317    501    506   -291       O  
ATOM   3081  CB  PHE B 357     -30.314  16.350  37.213  1.00 23.04           C  
ANISOU 3081  CB  PHE B 357     3195   3019   2541    191    504   -373       C  
ATOM   3082  CG  PHE B 357     -29.204  15.739  36.392  1.00 25.03           C  
ANISOU 3082  CG  PHE B 357     3304   3196   3010     76    506   -467       C  
ATOM   3083  CD1 PHE B 357     -29.040  14.346  36.329  1.00 24.46           C  
ANISOU 3083  CD1 PHE B 357     2994   3053   3249    -49    551   -559       C  
ATOM   3084  CD2 PHE B 357     -28.325  16.538  35.705  1.00 25.89           C  
ANISOU 3084  CD2 PHE B 357     3517   3303   3020     91    463   -461       C  
ATOM   3085  CE1 PHE B 357     -28.018  13.797  35.574  1.00 25.56           C  
ANISOU 3085  CE1 PHE B 357     3002   3123   3587   -154    552   -646       C  
ATOM   3086  CE2 PHE B 357     -27.282  15.974  34.952  1.00 24.40           C  
ANISOU 3086  CE2 PHE B 357     3195   3042   3033    -18    464   -548       C  
ATOM   3087  CZ  PHE B 357     -27.162  14.598  34.872  1.00 25.22           C  
ANISOU 3087  CZ  PHE B 357     3059   3083   3440   -138    511   -645       C  
ATOM   3088  N   ALA B 358     -33.400  16.263  37.937  1.00 25.35           N  
ANISOU 3088  N   ALA B 358     3430   3627   2576    377    605   -433       N  
ATOM   3089  CA  ALA B 358     -34.356  16.603  38.998  1.00 23.39           C  
ANISOU 3089  CA  ALA B 358     3305   3397   2186    454    599   -325       C  
ATOM   3090  C   ALA B 358     -34.272  15.492  40.045  1.00 27.00           C  
ANISOU 3090  C   ALA B 358     3677   3681   2902    342    606   -262       C  
ATOM   3091  O   ALA B 358     -33.729  14.434  39.782  1.00 25.52           O  
ANISOU 3091  O   ALA B 358     3305   3409   2982    223    630   -338       O  
ATOM   3092  CB  ALA B 358     -35.752  16.686  38.436  1.00 26.16           C  
ANISOU 3092  CB  ALA B 358     3565   3993   2382    555    664   -456       C  
ATOM   3093  N   ILE B 359     -34.719  15.770  41.266  1.00 30.44           N  
ANISOU 3093  N   ILE B 359     4258   4049   3258    377    578   -114       N  
ATOM   3094  CA  ILE B 359     -34.758  14.773  42.305  1.00 31.83           C  
ANISOU 3094  CA  ILE B 359     4364   4074   3656    281    584    -52       C  
ATOM   3095  C   ILE B 359     -36.182  14.716  42.873  1.00 30.00           C  
ANISOU 3095  C   ILE B 359     4124   3964   3310    358    624    -56       C  
ATOM   3096  O   ILE B 359     -36.659  15.722  43.358  1.00 29.57           O  
ANISOU 3096  O   ILE B 359     4267   3959   3011    465    593     44       O  
ATOM   3097  CB  ILE B 359     -33.771  15.112  43.446  1.00 33.30           C  
ANISOU 3097  CB  ILE B 359     4751   4017   3886    229    500    162       C  
ATOM   3098  CG1 ILE B 359     -32.335  15.124  42.924  1.00 33.43           C  
ANISOU 3098  CG1 ILE B 359     4772   3903   4026    147    460    168       C  
ATOM   3099  CG2 ILE B 359     -33.886  14.043  44.580  1.00 32.22           C  
ANISOU 3099  CG2 ILE B 359     4538   3724   3981    127    507    229       C  
ATOM   3100  CD1 ILE B 359     -31.319  15.568  43.932  1.00 35.93           C  
ANISOU 3100  CD1 ILE B 359     5296   3991   4364    104    377    374       C  
ATOM   3101  N   GLU B 360     -36.872  13.572  42.796  1.00 27.83           N  
ANISOU 3101  N   GLU B 360     3625   3742   3205    306    692   -175       N  
ATOM   3102  CA  GLU B 360     -38.260  13.485  43.344  1.00 29.19           C  
ANISOU 3102  CA  GLU B 360     3785   4034   3271    378    733   -184       C  
ATOM   3103  C   GLU B 360     -38.127  13.402  44.857  1.00 31.85           C  
ANISOU 3103  C   GLU B 360     4256   4182   3664    336    685      4       C  
ATOM   3104  O   GLU B 360     -37.284  12.662  45.353  1.00 29.79           O  
ANISOU 3104  O   GLU B 360     3949   3724   3646    211    662     62       O  
ATOM   3105  CB  GLU B 360     -38.942  12.187  42.953  1.00 38.84           C  
ANISOU 3105  CB  GLU B 360     4730   5338   4689    319    816   -350       C  
ATOM   3106  CG  GLU B 360     -39.592  12.184  41.612  1.00 49.77           C  
ANISOU 3106  CG  GLU B 360     5962   6958   5988    382    883   -549       C  
ATOM   3107  CD  GLU B 360     -40.220  10.841  41.281  1.00 53.37           C  
ANISOU 3107  CD  GLU B 360     6142   7482   6656    315    965   -708       C  
ATOM   3108  OE1 GLU B 360     -40.725  10.710  40.151  1.00 55.71           O  
ANISOU 3108  OE1 GLU B 360     6355   7891   6922    339    961   -802       O  
ATOM   3109  OE2 GLU B 360     -40.218   9.930  42.142  1.00 43.90           O  
ANISOU 3109  OE2 GLU B 360     4872   6150   5658    223    970   -660       O  
ATOM   3110  N   LEU B 361     -38.963  14.115  45.601  1.00 29.43           N  
ANISOU 3110  N   LEU B 361     4107   3932   3142    435    670     97       N  
ATOM   3111  CA  LEU B 361     -38.975  13.989  47.059  1.00 27.19           C  
ANISOU 3111  CA  LEU B 361     3939   3485   2907    396    631    268       C  
ATOM   3112  C   LEU B 361     -40.406  13.549  47.459  1.00 31.73           C  
ANISOU 3112  C   LEU B 361     4426   4188   3440    440    689    212       C  
ATOM   3113  O   LEU B 361     -41.256  14.376  47.819  1.00 30.36           O  
ANISOU 3113  O   LEU B 361     4392   4122   3022    556    683    262       O  
ATOM   3114  CB  LEU B 361     -38.606  15.302  47.713  1.00 27.59           C  
ANISOU 3114  CB  LEU B 361     4282   3467   2735    472    554    452       C  
ATOM   3115  CG  LEU B 361     -37.174  15.856  47.531  1.00 32.18           C  
ANISOU 3115  CG  LEU B 361     4991   3901   3337    433    486    541       C  
ATOM   3116  CD1 LEU B 361     -36.993  17.150  48.256  1.00 29.96           C  
ANISOU 3116  CD1 LEU B 361     4859   3589   2935    463    370    631       C  
ATOM   3117  CD2 LEU B 361     -36.123  14.850  48.033  1.00 34.41           C  
ANISOU 3117  CD2 LEU B 361     5191   3946   3935    272    465    595       C  
ATOM   3118  N   LYS B 362     -40.656  12.242  47.422  1.00 28.88           N  
ANISOU 3118  N   LYS B 362     3838   3813   3322    345    744    111       N  
ATOM   3119  CA  LYS B 362     -41.939  11.684  47.801  1.00 31.98           C  
ANISOU 3119  CA  LYS B 362     4129   4314   3710    369    800     52       C  
ATOM   3120  C   LYS B 362     -41.931  11.123  49.237  1.00 33.07           C  
ANISOU 3120  C   LYS B 362     4309   4270   3986    289    774    192       C  
ATOM   3121  O   LYS B 362     -40.882  11.059  49.870  1.00 29.82           O  
ANISOU 3121  O   LYS B 362     3985   3646   3701    204    715    324       O  
ATOM   3122  CB  LYS B 362     -42.311  10.586  46.789  1.00 35.83           C  
ANISOU 3122  CB  LYS B 362     4327   4919   4369    321    883   -161       C  
ATOM   3123  CG  LYS B 362     -42.753  11.194  45.440  1.00 40.88           C  
ANISOU 3123  CG  LYS B 362     4924   5791   4819    428    923   -311       C  
ATOM   3124  CD  LYS B 362     -43.119  10.115  44.444  1.00 44.04           C  
ANISOU 3124  CD  LYS B 362     5038   6308   5388    380   1006   -521       C  
ATOM   3125  CE  LYS B 362     -43.443  10.714  43.119  1.00 43.93           C  
ANISOU 3125  CE  LYS B 362     5001   6481   5208    469   1025   -644       C  
ATOM   3126  NZ  LYS B 362     -44.588  11.624  43.247  1.00 54.17           N  
ANISOU 3126  NZ  LYS B 362     6467   7839   6277    558    979   -585       N  
ATOM   3127  N   ASP B 363     -43.107  10.758  49.763  1.00 24.81           N  
ANISOU 3127  N   ASP B 363     3210   3310   2905    318    815    168       N  
ATOM   3128  CA  ASP B 363     -43.214  10.285  51.133  1.00 28.58           C  
ANISOU 3128  CA  ASP B 363     3735   3633   3490    251    791    299       C  
ATOM   3129  C   ASP B 363     -42.768   8.831  51.162  1.00 35.74           C  
ANISOU 3129  C   ASP B 363     4424   4418   4738     98    818    237       C  
ATOM   3130  O   ASP B 363     -43.581   7.933  51.100  1.00 37.11           O  
ANISOU 3130  O   ASP B 363     4416   4672   5011     72    880    127       O  
ATOM   3131  CB  ASP B 363     -44.663  10.390  51.628  1.00 27.25           C  
ANISOU 3131  CB  ASP B 363     3577   3611   3163    336    828    283       C  
ATOM   3132  CG  ASP B 363     -44.789  10.135  53.146  1.00 35.33           C  
ANISOU 3132  CG  ASP B 363     4697   4477   4250    282    793    444       C  
ATOM   3133  OD1 ASP B 363     -43.757  10.154  53.875  1.00 38.19           O  
ANISOU 3133  OD1 ASP B 363     5167   4620   4722    201    729    593       O  
ATOM   3134  OD2 ASP B 363     -45.929   9.912  53.614  1.00 40.00           O  
ANISOU 3134  OD2 ASP B 363     5256   5165   4779    319    829    420       O  
ATOM   3135  N   ASP B 364     -41.460   8.624  51.273  1.00 35.35           N  
ANISOU 3135  N   ASP B 364     4398   4171   4864     -2    769    311       N  
ATOM   3136  CA  ASP B 364     -40.870   7.299  51.048  1.00 36.21           C  
ANISOU 3136  CA  ASP B 364     4289   4169   5298   -146    794    233       C  
ATOM   3137  C   ASP B 364     -41.276   6.300  52.124  1.00 38.79           C  
ANISOU 3137  C   ASP B 364     4542   4392   5806   -234    805    280       C  
ATOM   3138  O   ASP B 364     -41.427   6.662  53.287  1.00 36.34           O  
ANISOU 3138  O   ASP B 364     4395   3989   5423   -225    762    437       O  
ATOM   3139  CB  ASP B 364     -39.335   7.438  51.098  1.00 47.87           C  
ANISOU 3139  CB  ASP B 364     5849   5438   6903   -230    727    331       C  
ATOM   3140  CG  ASP B 364     -38.782   8.333  49.997  1.00 44.31           C  
ANISOU 3140  CG  ASP B 364     5459   5070   6305   -161    714    282       C  
ATOM   3141  OD1 ASP B 364     -39.207   8.190  48.823  1.00 40.05           O  
ANISOU 3141  OD1 ASP B 364     4770   4713   5735   -120    773    105       O  
ATOM   3142  OD2 ASP B 364     -37.907   9.172  50.309  1.00 45.21           O  
ANISOU 3142  OD2 ASP B 364     5772   5067   6339   -150    644    421       O  
ATOM   3143  N   TRP B 365     -41.394   5.029  51.759  1.00 36.56           N  
ANISOU 3143  N   TRP B 365     4013   4113   5765   -327    859    149       N  
ATOM   3144  CA  TRP B 365     -41.619   4.006  52.764  1.00 35.54           C  
ANISOU 3144  CA  TRP B 365     3805   3861   5836   -427    864    196       C  
ATOM   3145  C   TRP B 365     -40.535   3.986  53.865  1.00 44.33           C  
ANISOU 3145  C   TRP B 365     5058   4703   7081   -524    784    390       C  
ATOM   3146  O   TRP B 365     -40.872   4.021  55.055  1.00 42.96           O  
ANISOU 3146  O   TRP B 365     4992   4446   6884   -534    756    520       O  
ATOM   3147  CB  TRP B 365     -41.770   2.637  52.084  1.00 32.25           C  
ANISOU 3147  CB  TRP B 365     3095   3483   5674   -518    933     18       C  
ATOM   3148  CG  TRP B 365     -42.188   1.524  53.013  1.00 38.07           C  
ANISOU 3148  CG  TRP B 365     3773   4148   6543   -580    913     34       C  
ATOM   3149  CD1 TRP B 365     -41.389   0.837  53.891  1.00 38.60           C  
ANISOU 3149  CD1 TRP B 365     3936   4061   6668   -616    794    120       C  
ATOM   3150  CD2 TRP B 365     -43.496   0.919  53.104  1.00 41.78           C  
ANISOU 3150  CD2 TRP B 365     4122   4759   6995   -556    974    -61       C  
ATOM   3151  NE1 TRP B 365     -42.126  -0.148  54.537  1.00 34.95           N  
ANISOU 3151  NE1 TRP B 365     3414   3615   6249   -629    791     93       N  
ATOM   3152  CE2 TRP B 365     -43.413  -0.125  54.068  1.00 37.30           C  
ANISOU 3152  CE2 TRP B 365     3584   4073   6515   -603    895    -12       C  
ATOM   3153  CE3 TRP B 365     -44.715   1.158  52.472  1.00 44.78           C  
ANISOU 3153  CE3 TRP B 365     4395   5373   7244   -470   1070   -190       C  
ATOM   3154  CZ2 TRP B 365     -44.513  -0.912  54.419  1.00 40.65           C  
ANISOU 3154  CZ2 TRP B 365     3923   4575   6945   -601    923    -73       C  
ATOM   3155  CZ3 TRP B 365     -45.818   0.357  52.812  1.00 41.22           C  
ANISOU 3155  CZ3 TRP B 365     3876   5007   6780   -460   1079   -252       C  
ATOM   3156  CH2 TRP B 365     -45.707  -0.655  53.776  1.00 42.54           C  
ANISOU 3156  CH2 TRP B 365     4060   5026   7078   -538   1015   -189       C  
ATOM   3157  N   LEU B 366     -39.251   3.942  53.481  1.00 38.19           N  
ANISOU 3157  N   LEU B 366     4302   3835   6373   -562    715    391       N  
ATOM   3158  CA  LEU B 366     -38.150   4.003  54.460  1.00 37.15           C  
ANISOU 3158  CA  LEU B 366     4354   3625   6135   -556    555    492       C  
ATOM   3159  C   LEU B 366     -37.630   5.452  54.643  1.00 49.54           C  
ANISOU 3159  C   LEU B 366     6164   5166   7492   -499    495    613       C  
ATOM   3160  O   LEU B 366     -37.165   6.080  53.680  1.00 50.48           O  
ANISOU 3160  O   LEU B 366     6297   5287   7594   -478    519    598       O  
ATOM   3161  CB  LEU B 366     -36.991   3.087  54.026  1.00 39.52           C  
ANISOU 3161  CB  LEU B 366     4572   3929   6516   -588    493    403       C  
ATOM   3162  CG  LEU B 366     -37.338   1.592  53.941  1.00 44.55           C  
ANISOU 3162  CG  LEU B 366     5028   4599   7299   -614    518    294       C  
ATOM   3163  CD1 LEU B 366     -36.120   0.744  53.586  1.00 50.41           C  
ANISOU 3163  CD1 LEU B 366     5737   5337   8079   -623    459    242       C  
ATOM   3164  CD2 LEU B 366     -37.936   1.172  55.252  1.00 40.77           C  
ANISOU 3164  CD2 LEU B 366     4595   4100   6795   -625    493    359       C  
ATOM   3165  N   LYS B 367     -37.695   5.952  55.877  1.00 47.23           N  
ANISOU 3165  N   LYS B 367     6064   4864   7018   -473    411    709       N  
ATOM   3166  CA  LYS B 367     -37.527   7.375  56.162  1.00 59.72           C  
ANISOU 3166  CA  LYS B 367     7884   6460   8347   -403    345    794       C  
ATOM   3167  C   LYS B 367     -36.147   7.711  56.692  1.00 68.63           C  
ANISOU 3167  C   LYS B 367     9181   7571   9322   -428    227    765       C  
ATOM   3168  O   LYS B 367     -35.832   8.882  56.915  1.00 69.94           O  
ANISOU 3168  O   LYS B 367     9532   7746   9297   -380    166    799       O  
ATOM   3169  CB  LYS B 367     -38.561   7.806  57.202  1.00 63.87           C  
ANISOU 3169  CB  LYS B 367     8524   7013   8732   -358    330    870       C  
ATOM   3170  CG  LYS B 367     -39.926   8.072  56.621  1.00 66.01           C  
ANISOU 3170  CG  LYS B 367     8734   7334   9013   -274    487    926       C  
ATOM   3171  CD  LYS B 367     -39.822   9.271  55.714  1.00 58.33           C  
ANISOU 3171  CD  LYS B 367     7880   6426   7858   -162    522    961       C  
ATOM   3172  CE  LYS B 367     -41.130   9.594  55.023  1.00 52.55           C  
ANISOU 3172  CE  LYS B 367     7098   5933   6935    -37    607    850       C  
ATOM   3173  NZ  LYS B 367     -41.010  10.932  54.309  1.00 50.83           N  
ANISOU 3173  NZ  LYS B 367     7035   5832   6445     90    585    852       N  
ATOM   3174  N   GLY B 368     -35.332   6.681  56.900  1.00 54.99           N  
ATOM   3175  CA  GLY B 368     -34.049   6.830  57.567  1.00 60.20           C  
ATOM   3176  C   GLY B 368     -33.024   7.606  56.773  1.00 64.41           C  
ATOM   3177  O   GLY B 368     -32.667   7.218  55.662  1.00 72.62           O  
ATOM   3178  N   ARG B 369     -32.553   8.712  57.348  1.00 61.65           N  
ATOM   3179  CA  ARG B 369     -31.634   9.606  56.652  1.00 58.01           C  
ATOM   3180  C   ARG B 369     -30.198   9.413  57.129  1.00 51.49           C  
ATOM   3181  O   ARG B 369     -29.271   9.937  56.525  1.00 49.93           O  
ATOM   3182  CB  ARG B 369     -32.059  11.072  56.833  1.00 58.72           C  
ATOM   3183  CG  ARG B 369     -33.521  11.381  56.480  1.00 58.83           C  
ATOM   3184  CD  ARG B 369     -33.944  10.770  55.146  1.00 55.72           C  
ATOM   3185  NE  ARG B 369     -35.224  11.297  54.682  1.00 52.74           N  
ATOM   3186  CZ  ARG B 369     -36.004  10.676  53.801  1.00 55.99           C  
ATOM   3187  NH1 ARG B 369     -35.635   9.499  53.289  1.00 60.01           N  
ATOM   3188  NH2 ARG B 369     -37.156  11.223  53.431  1.00 50.23           N  
TER    3189      ARG B 369                                                      
HETATM 3190  OH2 1PE A 401     -69.364  -2.759   6.385  1.00 53.18           O  
HETATM 3191  C12 1PE A 401     -70.040  -1.554   6.252  1.00 48.78           C  
HETATM 3192  C22 1PE A 401     -69.745  -0.961   4.919  1.00 42.17           C  
HETATM 3193  OH3 1PE A 401     -68.371  -0.896   4.790  1.00 36.86           O  
HETATM 3194  C13 1PE A 401     -66.332  -0.251   3.765  1.00 38.50           C  
HETATM 3195  C23 1PE A 401     -67.808  -0.461   3.599  1.00 35.51           C  
HETATM 3196  OH4 1PE A 401     -65.625  -1.436   3.656  1.00 35.49           O  
HETATM 3197  C14 1PE A 401     -63.639  -2.732   3.751  1.00 38.56           C  
HETATM 3198  C24 1PE A 401     -64.247  -1.374   3.791  1.00 34.82           C  
HETATM 3199  OH5 1PE A 401     -63.773  -3.416   4.941  1.00 35.79           O  
HETATM 3200  C15 1PE A 401     -63.795  -5.779   5.514  1.00 48.88           C  
HETATM 3201  C25 1PE A 401     -63.053  -4.610   4.991  1.00 41.82           C  
HETATM 3202  OH6 1PE A 401     -65.069  -5.453   5.923  1.00 53.94           O  
HETATM 3203  C26 1PE A 401     -65.340  -5.343   7.281  1.00 54.42           C  
HETATM 3204  OH2 1PE A 402     -53.569  -5.340  10.403  1.00 37.55           O  
HETATM 3205  C12 1PE A 402     -54.486  -5.349   9.364  1.00 40.23           C  
HETATM 3206  C22 1PE A 402     -53.873  -4.641   8.193  1.00 33.80           C  
HETATM 3207  OH3 1PE A 402     -52.524  -4.974   8.015  1.00 34.56           O  
HETATM 3208  C13 1PE A 402     -50.486  -5.044   6.814  1.00 30.92           C  
HETATM 3209  C23 1PE A 402     -51.846  -4.442   6.927  1.00 33.29           C  
HETATM 3210  OH4 1PE A 402     -49.555  -4.327   7.545  1.00 34.22           O  
HETATM 3211  C14 1PE A 402     -47.342  -3.743   8.036  1.00 53.28           C  
HETATM 3212  C24 1PE A 402     -48.308  -4.825   7.801  1.00 36.86           C  
HETATM 3213  OH5 1PE A 402     -46.901  -3.741   9.333  1.00 61.28           O  
HETATM 3214  C15 1PE A 402     -45.795  -1.625   9.622  1.00 44.99           C  
HETATM 3215  C25 1PE A 402     -46.933  -2.523   9.992  1.00 61.32           C  
HETATM 3216  OH6 1PE A 402     -44.626  -2.364   9.537  1.00 57.49           O  
HETATM 3217  C26 1PE A 402     -43.397  -1.765   9.356  1.00 42.29           C  
HETATM 3218  P   PO4 A 403     -51.284  22.339  12.391  1.00 80.76           P  
HETATM 3219  O1  PO4 A 403     -49.843  21.912  12.600  1.00 66.42           O  
HETATM 3220  O2  PO4 A 403     -51.633  22.375  10.919  1.00 82.42           O  
HETATM 3221  O3  PO4 A 403     -52.242  21.376  13.039  1.00 83.75           O  
HETATM 3222  O4  PO4 A 403     -51.517  23.703  13.014  1.00 88.01           O  
HETATM 3223  P   PO4 A 404     -56.578  23.118   9.462  1.00 59.02           P  
HETATM 3224  O1  PO4 A 404     -55.806  22.321   8.471  1.00 51.70           O  
HETATM 3225  O2  PO4 A 404     -56.078  22.845  10.873  1.00 69.77           O  
HETATM 3226  O3  PO4 A 404     -58.047  22.720   9.331  1.00 67.77           O  
HETATM 3227  O4  PO4 A 404     -56.366  24.642   9.249  1.00 48.34           O  
HETATM 3228  OH2 1PE B 401     -21.885  38.998  12.837  1.00 66.55           O  
HETATM 3229  C12 1PE B 401     -22.214  39.110  14.171  1.00 63.17           C  
HETATM 3230  C22 1PE B 401     -21.735  40.433  14.668  1.00 60.69           C  
HETATM 3231  OH3 1PE B 401     -20.444  40.275  15.131  1.00 58.77           O  
HETATM 3232  C13 1PE B 401     -18.510  40.750  16.386  1.00 58.56           C  
HETATM 3233  C23 1PE B 401     -19.838  41.243  15.903  1.00 59.35           C  
HETATM 3234  OH4 1PE B 401     -17.656  40.426  15.331  1.00 61.27           O  
HETATM 3235  C14 1PE B 401     -15.317  39.900  14.722  1.00 64.45           C  
HETATM 3236  C24 1PE B 401     -16.323  40.826  15.365  1.00 61.77           C  
HETATM 3237  OH5 1PE B 401     -15.687  39.238  13.553  1.00 65.75           O  
HETATM 3238  C15 1PE B 401     -15.363  37.514  11.848  1.00 55.07           C  
HETATM 3239  C25 1PE B 401     -14.794  38.335  12.972  1.00 56.86           C  
HETATM 3240  OH6 1PE B 401     -16.338  38.199  11.124  1.00 62.31           O  
HETATM 3241  C26 1PE B 401     -17.060  37.594  10.095  1.00 47.58           C  
HETATM 3242  OH2 1PE B 402     -21.470  40.379  27.999  1.00 59.37           O  
HETATM 3243  C12 1PE B 402     -21.976  39.565  26.980  1.00 40.37           C  
HETATM 3244  C22 1PE B 402     -20.929  39.422  25.921  1.00 58.08           C  
HETATM 3245  OH3 1PE B 402     -20.197  40.595  25.791  1.00 63.43           O  
HETATM 3246  C13 1PE B 402     -18.096  41.718  25.840  1.00 76.30           C  
HETATM 3247  C23 1PE B 402     -19.012  40.720  26.485  1.00 62.26           C  
HETATM 3248  OH4 1PE B 402     -17.463  41.219  24.701  1.00 78.01           O  
HETATM 3249  C14 1PE B 402     -15.194  41.942  24.182  1.00 74.43           C  
HETATM 3250  C24 1PE B 402     -16.672  42.058  23.916  1.00 75.80           C  
HETATM 3251  OH5 1PE B 402     -14.907  41.500  25.468  1.00 73.29           O  
HETATM 3252  C15 1PE B 402     -13.311  40.715  27.108  1.00 66.63           C  
HETATM 3253  C25 1PE B 402     -13.705  41.781  26.115  1.00 67.49           C  
HETATM 3254  OH6 1PE B 402     -13.701  40.989  28.414  1.00 66.96           O  
HETATM 3255  C26 1PE B 402     -13.395  40.109  29.444  1.00 62.58           C  
HETATM 3256  P   PO4 B 403     -26.488  22.126  41.066  1.00102.00           P  
HETATM 3257  O1  PO4 B 403     -25.453  22.790  40.186  1.00 97.83           O  
HETATM 3258  O2  PO4 B 403     -27.824  22.818  40.926  1.00100.74           O  
HETATM 3259  O3  PO4 B 403     -26.646  20.687  40.646  1.00105.87           O  
HETATM 3260  O4  PO4 B 403     -26.023  22.163  42.503  1.00104.29           O  
HETATM 3261  P   PO4 B 404     -40.709  16.187  38.478  1.00117.81           P  
HETATM 3262  O1  PO4 B 404     -39.596  17.198  38.265  1.00111.14           O  
HETATM 3263  O2  PO4 B 404     -42.007  16.919  38.716  1.00119.68           O  
HETATM 3264  O3  PO4 B 404     -40.815  15.322  37.243  1.00118.99           O  
HETATM 3265  O4  PO4 B 404     -40.470  15.293  39.678  1.00117.22           O  
HETATM 3266  O   HOH A 501     -54.222  10.158   0.154  1.00 24.49           O  
HETATM 3267  O   HOH A 502     -48.000  15.596   2.187  1.00 23.13           O  
HETATM 3268  O   HOH A 503     -53.379   4.225   1.596  1.00 21.88           O  
HETATM 3269  O   HOH A 504     -55.553   4.750  -0.090  1.00 27.02           O  
HETATM 3270  O   HOH A 505     -50.582  27.008   9.989  1.00 27.18           O  
HETATM 3271  O   HOH A 506     -40.984   5.658  24.061  1.00 38.05           O  
HETATM 3272  O   HOH A 507     -49.475  17.837   2.673  1.00 20.45           O  
HETATM 3273  O   HOH A 508     -53.056  -3.428   0.310  1.00 24.19           O  
HETATM 3274  O   HOH A 509     -51.855  27.505   0.953  1.00 25.38           O  
HETATM 3275  O   HOH A 510     -66.893   4.221   4.503  1.00 27.58           O  
HETATM 3276  O   HOH A 511     -52.869  26.191  -1.469  1.00 31.84           O  
HETATM 3277  O   HOH A 512     -50.024  12.840   3.643  1.00 25.29           O  
HETATM 3278  O   HOH A 513     -59.800  -7.811  -0.203  1.00 29.82           O  
HETATM 3279  O   HOH A 514     -50.668   6.918   6.997  1.00 27.18           O  
HETATM 3280  O   HOH A 515     -44.624   6.939  18.132  1.00 33.88           O  
HETATM 3281  O   HOH A 516     -56.482  26.885   6.476  1.00 40.91           O  
HETATM 3282  O   HOH A 517     -55.181   7.077  -1.258  1.00 26.01           O  
HETATM 3283  O   HOH A 518     -43.420  14.543  -6.139  1.00 38.17           O  
HETATM 3284  O   HOH A 519     -68.716   8.742  -1.538  1.00 31.92           O  
HETATM 3285  O   HOH A 520     -43.479  -5.883  18.860  1.00 34.29           O  
HETATM 3286  O   HOH A 521     -63.346  17.875  11.332  1.00 39.14           O  
HETATM 3287  O   HOH A 522     -49.347  27.898   0.187  1.00 34.91           O  
HETATM 3288  O   HOH A 523     -60.972  11.305  -0.505  1.00 27.94           O  
HETATM 3289  O   HOH A 524     -54.244  11.068  19.500  1.00 34.46           O  
HETATM 3290  O   HOH A 525     -64.019   2.247  -0.491  1.00 42.39           O  
HETATM 3291  O   HOH A 526     -34.183  -9.924  23.141  1.00 47.64           O  
HETATM 3292  O   HOH A 527     -60.147  13.156  -3.933  1.00 38.25           O  
HETATM 3293  O   HOH A 528     -50.169  31.281  -0.470  1.00 37.82           O  
HETATM 3294  O   HOH A 529     -45.203   6.010   8.749  1.00 39.75           O  
HETATM 3295  O   HOH A 530     -35.858  16.739  10.640  1.00 43.82           O  
HETATM 3296  O   HOH A 531     -38.217   8.671  23.783  1.00 47.54           O  
HETATM 3297  O   HOH A 532     -44.166  11.066  -0.507  1.00 36.56           O  
HETATM 3298  O   HOH A 533     -68.112   5.744  -1.580  1.00 38.41           O  
HETATM 3299  O   HOH A 534     -54.030   4.188  -3.446  1.00 46.08           O  
HETATM 3300  O   HOH A 535     -37.881  33.941   1.712  1.00 44.74           O  
HETATM 3301  O   HOH A 536     -64.315   5.142  16.424  1.00 36.85           O  
HETATM 3302  O   HOH A 537     -40.928  14.484  -5.384  1.00 39.35           O  
HETATM 3303  O   HOH A 538     -66.196   8.139  -1.779  1.00 42.72           O  
HETATM 3304  O   HOH A 539     -52.274   4.414  -2.009  1.00 38.41           O  
HETATM 3305  O   HOH A 540     -60.432  10.682  -4.174  1.00 44.27           O  
HETATM 3306  O   HOH A 541     -40.627   6.056  14.604  1.00 50.52           O  
HETATM 3307  O   HOH A 542     -57.343  12.309  20.627  1.00 43.68           O  
HETATM 3308  O   HOH A 543     -61.431  21.983   7.897  1.00 43.47           O  
HETATM 3309  O   HOH A 544     -65.208  -0.983  15.576  1.00 43.46           O  
HETATM 3310  O   HOH A 545     -62.652  19.876  -3.879  1.00 32.98           O  
HETATM 3311  O   HOH A 546     -53.336  23.633  -1.804  1.00 39.91           O  
HETATM 3312  O   HOH A 547     -57.665  21.169  -2.512  1.00 37.59           O  
HETATM 3313  O   HOH A 548     -49.840   4.022   0.541  1.00 36.87           O  
HETATM 3314  O   HOH A 549     -58.376  14.846  -5.569  1.00 50.88           O  
HETATM 3315  O   HOH A 550     -55.607  14.221  20.232  1.00 53.40           O  
HETATM 3316  O   HOH A 551     -61.436   5.002  -2.151  1.00 28.61           O  
HETATM 3317  O   HOH A 552     -62.685   7.424  -0.988  1.00 42.17           O  
HETATM 3318  O   HOH A 553     -40.963 -10.699  28.410  1.00 47.61           O  
HETATM 3319  O   HOH A 554     -41.899 -17.270  26.524  1.00 47.49           O  
HETATM 3320  O   HOH A 555     -55.648  20.811  -3.703  1.00 39.81           O  
HETATM 3321  O   HOH A 556     -59.797  20.302  -4.376  1.00 47.00           O  
HETATM 3322  O   HOH A 557     -56.332   0.336  25.252  1.00 44.57           O  
HETATM 3323  O   HOH A 558     -54.768  -5.887  -2.495  1.00 38.92           O  
HETATM 3324  O   HOH A 559     -43.147   6.674  15.442  1.00 37.76           O  
HETATM 3325  O   HOH A 560     -53.390  11.848  -1.585  1.00 47.83           O  
HETATM 3326  O   HOH A 561     -54.306   1.561  -3.872  1.00 47.59           O  
HETATM 3327  O   HOH A 562     -46.371   6.250   6.588  1.00 47.31           O  
HETATM 3328  O   HOH A 563     -72.956  14.146   4.387  1.00 38.79           O  
HETATM 3329  O   HOH A 564     -40.206  12.393   8.464  1.00 32.53           O  
HETATM 3330  O   HOH A 565     -21.928  23.580   2.928  1.00 43.74           O  
HETATM 3331  O   HOH A 566     -34.299  22.839   8.385  1.00 46.61           O  
HETATM 3332  O   HOH A 567     -40.589  -8.421  21.262  1.00 49.66           O  
HETATM 3333  O   HOH A 568     -63.587  -1.337   0.188  1.00 40.10           O  
HETATM 3334  O   HOH A 569     -41.819   6.131   7.152  1.00 51.40           O  
HETATM 3335  O   HOH A 570     -39.998  35.016   0.230  1.00 54.28           O  
HETATM 3336  O   HOH A 571     -60.479  23.840   9.379  1.00 57.77           O  
HETATM 3337  O   HOH A 572     -38.536  11.764  10.178  1.00 43.97           O  
HETATM 3338  O   HOH A 573     -48.461   7.313   2.952  1.00 42.50           O  
HETATM 3339  O   HOH A 574     -49.470   9.174   5.939  1.00 31.65           O  
HETATM 3340  O   HOH A 575     -48.804  27.162  -2.537  1.00 45.00           O  
HETATM 3341  O   HOH A 576     -38.118  -4.834  15.135  1.00 50.07           O  
HETATM 3342  O   HOH A 577     -47.759   1.674   4.165  1.00 45.00           O  
HETATM 3343  O   HOH A 578     -43.141  17.856  12.525  1.00 50.21           O  
HETATM 3344  O   HOH A 579     -55.860  17.058  15.157  1.00 56.87           O  
HETATM 3345  O   HOH A 580     -38.397   7.372  15.199  1.00 46.45           O  
HETATM 3346  O   HOH A 581     -36.876  18.127 -12.453  1.00 56.12           O  
HETATM 3347  O   HOH A 582     -41.452   1.911  11.291  1.00 63.66           O  
HETATM 3348  O   HOH A 583     -55.777  14.062  -3.878  1.00 51.69           O  
HETATM 3349  O   HOH A 584     -48.038   5.565   4.704  1.00 46.89           O  
HETATM 3350  O   HOH A 585     -54.020  15.339  16.211  1.00 50.12           O  
HETATM 3351  O   HOH A 586     -33.923  14.430   8.334  1.00 42.32           O  
HETATM 3352  O   HOH A 587     -60.575  13.115   2.122  1.00 36.92           O  
HETATM 3353  O   HOH A 588     -62.316   9.813  -2.583  1.00 55.88           O  
HETATM 3354  O   HOH A 589     -43.718  24.842   8.412  1.00 38.85           O  
HETATM 3355  O   HOH A 590     -40.352   1.303  14.073  1.00 57.19           O  
HETATM 3356  O   HOH A 591     -53.729  13.551   0.527  1.00 32.19           O  
HETATM 3357  O   HOH A 592     -58.414  -9.050  -2.246  1.00 45.78           O  
HETATM 3358  O   HOH A 593     -44.315  22.191   8.980  1.00 56.09           O  
HETATM 3359  O   HOH A 594     -41.058  19.401 -11.842  1.00 55.44           O  
HETATM 3360  O   HOH A 595     -48.117 -11.098  17.659  1.00 57.01           O  
HETATM 3361  O   HOH A 596     -38.184  -9.465  29.665  1.00 50.87           O  
HETATM 3362  O   HOH A 597     -45.474  21.511  10.672  1.00 58.81           O  
HETATM 3363  O   HOH A 598     -39.738   4.845  29.640  1.00 44.49           O  
HETATM 3364  O   HOH A 599     -48.532  12.492  16.363  1.00 45.23           O  
HETATM 3365  O   HOH A 600     -74.559  15.643   6.184  1.00 54.87           O  
HETATM 3366  O   HOH A 601     -50.576  -8.506  32.123  1.00 53.69           O  
HETATM 3367  O   HOH A 602     -50.707  -7.332  38.442  1.00 58.52           O  
HETATM 3368  O   HOH A 603     -56.121  10.893  -3.503  1.00 50.58           O  
HETATM 3369  O   HOH A 604     -40.089  10.933  27.001  1.00 40.63           O  
HETATM 3370  O   HOH A 605     -76.575  15.876   5.310  1.00 56.71           O  
HETATM 3371  O   HOH A 606     -67.098   4.493   1.864  1.00 46.46           O  
HETATM 3372  O   HOH A 607     -51.023  26.749  13.399  1.00 49.90           O  
HETATM 3373  O   HOH A 608     -35.069   6.829  17.056  1.00 63.38           O  
HETATM 3374  O   HOH A 609     -52.675  -4.803  15.607  1.00 45.95           O  
HETATM 3375  O   HOH A 610     -55.598  18.666  -5.731  1.00 55.25           O  
HETATM 3376  O   HOH A 611     -60.621  -4.457  17.439  1.00 51.64           O  
HETATM 3377  O   HOH A 612     -57.744  -6.122  14.458  1.00 50.48           O  
HETATM 3378  O   HOH A 613     -53.343  -5.870  13.947  1.00 60.75           O  
HETATM 3379  O   HOH A 614     -65.246  -8.229   6.150  1.00 67.02           O  
HETATM 3380  O   HOH A 615     -42.038  26.285   9.527  1.00 60.83           O  
HETATM 3381  O   HOH A 616     -39.587  31.275  -4.543  1.00 48.18           O  
HETATM 3382  O   HOH A 617     -44.018  28.899  -6.985  1.00 49.23           O  
HETATM 3383  O   HOH A 618     -21.963  25.995 -14.319  1.00 64.50           O  
HETATM 3384  O   HOH A 619     -42.258   9.197  10.801  1.00 51.79           O  
HETATM 3385  O   HOH A 620     -43.386   8.380  29.815  1.00 44.49           O  
HETATM 3386  O   HOH A 621     -42.903   4.583  30.987  1.00 48.72           O  
HETATM 3387  O   HOH A 622     -37.140  23.824 -13.714  1.00 62.21           O  
HETATM 3388  O   HOH A 623     -31.811  24.975   2.732  1.00 50.40           O  
HETATM 3389  O   HOH A 624     -74.579  10.879   5.464  1.00 44.54           O  
HETATM 3390  O   HOH A 625     -44.005   6.932   6.016  1.00 60.20           O  
HETATM 3391  O   HOH A 626     -60.052  27.189   6.774  1.00 46.26           O  
HETATM 3392  O   HOH A 627     -62.588  11.166   2.237  1.00 50.93           O  
HETATM 3393  O   HOH A 628     -56.779  -7.445  -3.151  1.00 57.12           O  
HETATM 3394  O   HOH A 629     -59.140  17.422  -6.187  1.00 53.51           O  
HETATM 3395  O   HOH A 630     -54.248  23.086  12.346  1.00 58.68           O  
HETATM 3396  O   HOH A 631     -42.485  10.365   8.612  1.00 61.50           O  
HETATM 3397  O   HOH A 632     -51.318  30.654  -2.944  1.00 63.66           O  
HETATM 3398  O   HOH A 633     -65.806   5.970  -2.883  1.00 69.88           O  
HETATM 3399  O   HOH B 501     -26.539  19.707  29.838  1.00 26.46           O  
HETATM 3400  O   HOH B 502     -21.347  31.221  11.450  1.00 34.38           O  
HETATM 3401  O   HOH B 503     -27.729  30.673  21.795  1.00 31.18           O  
HETATM 3402  O   HOH B 504     -28.375  30.478  15.337  1.00 29.73           O  
HETATM 3403  O   HOH B 505     -27.295  21.917  23.971  1.00 30.27           O  
HETATM 3404  O   HOH B 506     -24.827  22.678  28.121  1.00 28.80           O  
HETATM 3405  O   HOH B 507     -21.683  28.680  27.815  1.00 34.54           O  
HETATM 3406  O   HOH B 508     -48.447   9.540  52.553  1.00 34.35           O  
HETATM 3407  O   HOH B 509     -26.632  31.162  24.234  1.00 28.27           O  
HETATM 3408  O   HOH B 510     -22.806  26.364  29.001  1.00 35.03           O  
HETATM 3409  O   HOH B 511     -29.508   9.494  23.959  1.00 33.57           O  
HETATM 3410  O   HOH B 512     -29.237  28.515  21.673  1.00 36.39           O  
HETATM 3411  O   HOH B 513     -27.301   8.044  25.413  1.00 32.12           O  
HETATM 3412  O   HOH B 514     -27.787  24.872  12.451  1.00 43.12           O  
HETATM 3413  O   HOH B 515     -11.661  41.571  36.731  1.00 38.39           O  
HETATM 3414  O   HOH B 516     -27.898  39.046  24.199  1.00 30.50           O  
HETATM 3415  O   HOH B 517     -10.299  31.037  16.276  1.00 43.75           O  
HETATM 3416  O   HOH B 518     -35.777  10.647  49.525  1.00 43.39           O  
HETATM 3417  O   HOH B 519     -15.021  17.863  16.212  1.00 44.86           O  
HETATM 3418  O   HOH B 520     -31.994  15.188  21.377  1.00 46.61           O  
HETATM 3419  O   HOH B 521     -33.393  19.666  29.345  1.00 40.98           O  
HETATM 3420  O   HOH B 522     -29.168  12.015  22.926  1.00 36.41           O  
HETATM 3421  O   HOH B 523     -32.344  33.947  21.726  1.00 40.61           O  
HETATM 3422  O   HOH B 524      -4.214  37.004  22.443  1.00 42.15           O  
HETATM 3423  O   HOH B 525     -38.751  10.069  46.758  1.00 35.11           O  
HETATM 3424  O   HOH B 526     -29.669  12.074  19.956  1.00 52.45           O  
HETATM 3425  O   HOH B 527     -35.897  10.798  46.743  1.00 42.69           O  
HETATM 3426  O   HOH B 528     -20.401   8.625  19.214  1.00 34.63           O  
HETATM 3427  O   HOH B 529     -41.384   4.384  49.042  1.00 50.34           O  
HETATM 3428  O   HOH B 530     -30.353  30.574  24.301  1.00 49.64           O  
HETATM 3429  O   HOH B 531     -21.599  32.753   9.172  1.00 39.28           O  
HETATM 3430  O   HOH B 532     -29.389  19.987  13.066  1.00 43.33           O  
HETATM 3431  O   HOH B 533     -33.464   5.808  45.334  1.00 53.01           O  
HETATM 3432  O   HOH B 534     -26.825  28.382  14.588  1.00 45.53           O  
HETATM 3433  O   HOH B 535     -11.137  36.961  15.284  1.00 36.56           O  
HETATM 3434  O   HOH B 536     -19.789  36.853  33.010  1.00 38.24           O  
HETATM 3435  O   HOH B 537     -27.471  25.877  14.566  1.00 43.92           O  
HETATM 3436  O   HOH B 538       2.192  36.045  29.620  1.00 42.80           O  
HETATM 3437  O   HOH B 539     -11.644  28.919  35.609  1.00 44.06           O  
HETATM 3438  O   HOH B 540     -39.254   9.062  44.474  1.00 42.16           O  
HETATM 3439  O   HOH B 541      -3.125  28.342  27.361  1.00 35.62           O  
HETATM 3440  O   HOH B 542     -28.576   7.931  27.636  1.00 42.84           O  
HETATM 3441  O   HOH B 543     -25.096  25.896  30.728  1.00 36.09           O  
HETATM 3442  O   HOH B 544     -29.925  14.595  19.226  1.00 34.42           O  
HETATM 3443  O   HOH B 545     -31.466  22.478  17.126  1.00 39.49           O  
HETATM 3444  O   HOH B 546     -21.461  36.559  35.052  1.00 45.36           O  
HETATM 3445  O   HOH B 547     -25.740  17.656  28.286  1.00 26.51           O  
HETATM 3446  O   HOH B 548     -34.621   3.134  45.545  1.00 61.09           O  
HETATM 3447  O   HOH B 549     -26.059  28.263  29.368  1.00 45.09           O  
HETATM 3448  O   HOH B 550     -23.882  30.470  10.978  1.00 43.57           O  
HETATM 3449  O   HOH B 551     -38.366   3.233  50.873  1.00 42.36           O  
HETATM 3450  O   HOH B 552      -0.865  28.178  22.940  1.00 52.03           O  
HETATM 3451  O   HOH B 553     -25.458  33.531  30.296  1.00 48.13           O  
HETATM 3452  O   HOH B 554     -21.188  11.834  43.687  1.00 49.46           O  
HETATM 3453  O   HOH B 555     -33.576  20.783  36.249  1.00 47.45           O  
HETATM 3454  O   HOH B 556      -6.548  30.357  40.187  1.00 44.62           O  
HETATM 3455  O   HOH B 557     -34.373   1.362  43.113  1.00 51.88           O  
HETATM 3456  O   HOH B 558     -14.973  38.738  41.908  1.00 53.37           O  
HETATM 3457  O   HOH B 559     -11.410  44.531  25.337  1.00 55.96           O  
HETATM 3458  O   HOH B 560     -40.328   6.016  47.491  1.00 52.90           O  
HETATM 3459  O   HOH B 561     -40.676   6.620  44.972  1.00 45.95           O  
HETATM 3460  O   HOH B 562      -8.727  24.919  26.176  1.00 30.46           O  
HETATM 3461  O   HOH B 563      -6.891  23.794  23.474  1.00 38.68           O  
HETATM 3462  O   HOH B 564     -20.175   9.996  34.046  1.00 55.97           O  
HETATM 3463  O   HOH B 565     -31.430  37.360  17.428  1.00 51.70           O  
HETATM 3464  O   HOH B 566     -36.501   2.313  49.701  1.00 49.82           O  
HETATM 3465  O   HOH B 567     -28.166  31.391  27.285  1.00 46.75           O  
HETATM 3466  O   HOH B 568     -31.803  31.514  22.213  1.00 60.80           O  
HETATM 3467  O   HOH B 569     -41.355  12.812  39.247  1.00 51.91           O  
HETATM 3468  O   HOH B 570      -5.240  29.514  36.101  1.00 53.30           O  
HETATM 3469  O   HOH B 571     -33.096  11.624  23.404  1.00 50.13           O  
HETATM 3470  O   HOH B 572     -30.797  31.394  13.789  1.00 61.41           O  
HETATM 3471  O   HOH B 573      -6.929  40.994  50.166  1.00 49.74           O  
HETATM 3472  O   HOH B 574     -31.442  21.882  20.761  1.00 42.11           O  
HETATM 3473  O   HOH B 575     -31.453  22.088  23.122  1.00 60.36           O  
HETATM 3474  O   HOH B 576     -27.852  33.601  29.171  1.00 49.07           O  
HETATM 3475  O   HOH B 577     -26.965   4.996  46.147  1.00 53.76           O  
HETATM 3476  O   HOH B 578     -34.666  -0.096  41.377  1.00 59.94           O  
HETATM 3477  O   HOH B 579      -2.139  46.553  29.410  1.00 60.98           O  
HETATM 3478  O   HOH B 580     -33.600  13.901  22.978  1.00 57.09           O  
HETATM 3479  O   HOH B 581     -24.698  18.026   9.581  1.00 57.33           O  
HETATM 3480  O   HOH B 582     -10.018  44.438  40.749  1.00 59.72           O  
HETATM 3481  O   HOH B 583      -7.198  27.114  50.235  1.00 61.49           O  
HETATM 3482  O   HOH B 584     -15.810  43.644  26.858  1.00 73.40           O  
HETATM 3483  O   HOH B 585     -20.604  14.856  50.884  1.00 57.07           O  
HETATM 3484  O   HOH B 586     -18.347  13.744  17.923  1.00 57.17           O  
HETATM 3485  O   HOH B 587      -7.325  25.554  52.574  1.00 64.61           O  
HETATM 3486  O   HOH B 588      -1.464  29.912  21.034  1.00 38.03           O  
HETATM 3487  O   HOH B 589     -23.174  20.837  11.397  1.00 50.48           O  
HETATM 3488  O   HOH B 590     -27.658  25.525  23.058  1.00 26.46           O  
HETATM 3489  O   HOH B 591     -12.259  24.710  14.864  1.00 53.26           O  
HETATM 3490  O   HOH B 592     -12.396  18.760  23.721  1.00 52.72           O  
HETATM 3491  O   HOH B 593     -39.032   6.771  32.409  1.00 49.10           O  
HETATM 3492  O   HOH B 594     -12.793  22.659  31.618  1.00 53.00           O  
HETATM 3493  O   HOH B 595     -25.185  28.415   4.526  1.00 46.37           O  
HETATM 3494  O   HOH B 596     -18.208  11.003  18.323  1.00 55.29           O  
HETATM 3495  O   HOH B 597     -24.228  30.014  30.435  1.00 64.58           O  
HETATM 3496  O   HOH B 598     -30.010  24.505  23.345  1.00 61.78           O  
HETATM 3497  O   HOH B 599     -17.865  25.791   3.857  1.00 52.78           O  
HETATM 3498  O   HOH B 600     -45.800  10.545  56.125  1.00 49.35           O  
CONECT 3190 3191                                                                
CONECT 3191 3190 3192                                                           
CONECT 3192 3191 3193                                                           
CONECT 3193 3192 3195                                                           
CONECT 3194 3195 3196                                                           
CONECT 3195 3193 3194                                                           
CONECT 3196 3194 3198                                                           
CONECT 3197 3198 3199                                                           
CONECT 3198 3196 3197                                                           
CONECT 3199 3197 3201                                                           
CONECT 3200 3201 3202                                                           
CONECT 3201 3199 3200                                                           
CONECT 3202 3200 3203                                                           
CONECT 3203 3202                                                                
CONECT 3204 3205                                                                
CONECT 3205 3204 3206                                                           
CONECT 3206 3205 3207                                                           
CONECT 3207 3206 3209                                                           
CONECT 3208 3209 3210                                                           
CONECT 3209 3207 3208                                                           
CONECT 3210 3208 3212                                                           
CONECT 3211 3212 3213                                                           
CONECT 3212 3210 3211                                                           
CONECT 3213 3211 3215                                                           
CONECT 3214 3215 3216                                                           
CONECT 3215 3213 3214                                                           
CONECT 3216 3214 3217                                                           
CONECT 3217 3216                                                                
CONECT 3218 3219 3220 3221 3222                                                 
CONECT 3219 3218                                                                
CONECT 3220 3218                                                                
CONECT 3221 3218                                                                
CONECT 3222 3218                                                                
CONECT 3223 3224 3225 3226 3227                                                 
CONECT 3224 3223                                                                
CONECT 3225 3223                                                                
CONECT 3226 3223                                                                
CONECT 3227 3223                                                                
CONECT 3228 3229                                                                
CONECT 3229 3228 3230                                                           
CONECT 3230 3229 3231                                                           
CONECT 3231 3230 3233                                                           
CONECT 3232 3233 3234                                                           
CONECT 3233 3231 3232                                                           
CONECT 3234 3232 3236                                                           
CONECT 3235 3236 3237                                                           
CONECT 3236 3234 3235                                                           
CONECT 3237 3235 3239                                                           
CONECT 3238 3239 3240                                                           
CONECT 3239 3237 3238                                                           
CONECT 3240 3238 3241                                                           
CONECT 3241 3240                                                                
CONECT 3242 3243                                                                
CONECT 3243 3242 3244                                                           
CONECT 3244 3243 3245                                                           
CONECT 3245 3244 3247                                                           
CONECT 3246 3247 3248                                                           
CONECT 3247 3245 3246                                                           
CONECT 3248 3246 3250                                                           
CONECT 3249 3250 3251                                                           
CONECT 3250 3248 3249                                                           
CONECT 3251 3249 3253                                                           
CONECT 3252 3253 3254                                                           
CONECT 3253 3251 3252                                                           
CONECT 3254 3252 3255                                                           
CONECT 3255 3254                                                                
CONECT 3256 3257 3258 3259 3260                                                 
CONECT 3257 3256                                                                
CONECT 3258 3256                                                                
CONECT 3259 3256                                                                
CONECT 3260 3256                                                                
CONECT 3261 3262 3263 3264 3265                                                 
CONECT 3262 3261                                                                
CONECT 3263 3261                                                                
CONECT 3264 3261                                                                
CONECT 3265 3261                                                                
MASTER      589    0    8   12   18    0   13    6 3491    2   76   36          
ENDMDL     
MODEL 2                                                                        
ATOM      1  N   GLU A   1     -11.218  -2.003   6.468  1.00 27.59           N  
ATOM      2  CA  GLU A   1     -10.394  -1.532   5.366  1.00 36.06           C  
ATOM      3  C   GLU A   1     -11.016  -0.345   4.584  1.00 22.34           C  
ATOM      4  O   GLU A   1     -12.226  -0.401   4.352  1.00 23.38           O  
ATOM      5  CB  GLU A   1     -10.185  -2.732   4.466  1.00 27.56           C  
ATOM      6  CG  GLU A   1      -9.364  -2.477   3.209  1.00 46.76           C  
ATOM      7  CD  GLU A   1      -9.408  -3.605   2.172  1.00 78.17           C  
ATOM      8  OE1 GLU A   1     -10.329  -4.438   2.199  1.00 83.62           O  
ATOM      9  OE2 GLU A   1      -8.509  -3.632   1.323  1.00 88.58           O1-
ATOM     10  N   VAL A   2     -10.246   0.639   4.102  1.00 24.91           N  
ATOM     11  CA  VAL A   2     -10.744   1.810   3.375  1.00 26.19           C  
ATOM     12  C   VAL A   2     -10.021   1.924   2.042  1.00 21.63           C  
ATOM     13  O   VAL A   2      -8.802   2.072   2.039  1.00 25.05           O  
ATOM     14  CB  VAL A   2     -10.511   3.143   4.188  1.00 21.80           C  
ATOM     15  CG1 VAL A   2     -11.151   4.291   3.410  1.00 21.14           C  
ATOM     16  CG2 VAL A   2     -11.118   3.094   5.582  1.00 21.61           C  
ATOM     17  N   LYS A   3     -10.687   1.876   0.896  1.00 17.35           N  
ATOM     18  CA  LYS A   3     -10.065   2.040  -0.405  1.00 16.93           C  
ATOM     19  C   LYS A   3     -10.545   3.338  -1.065  1.00 22.75           C  
ATOM     20  O   LYS A   3     -11.664   3.786  -0.810  1.00 24.29           O  
ATOM     21  CB  LYS A   3     -10.432   0.891  -1.342  1.00 20.86           C  
ATOM     22  CG  LYS A   3      -9.889  -0.457  -0.914  1.00 49.31           C  
ATOM     23  CD  LYS A   3      -9.832  -1.385  -2.127  1.00 66.30           C  
ATOM     24  CE  LYS A   3      -8.780  -2.489  -1.889  1.00 91.35           C  
ATOM     25  NZ  LYS A   3      -7.440  -1.978  -1.581  1.00 86.70           N1+
ATOM     26  N   LEU A   4      -9.734   3.891  -1.942  1.00 18.28           N  
ATOM     27  CA  LEU A   4     -10.004   5.099  -2.648  1.00 17.20           C  
ATOM     28  C   LEU A   4     -10.107   4.880  -4.108  1.00 25.71           C  
ATOM     29  O   LEU A   4      -9.358   4.113  -4.700  1.00 22.60           O  
ATOM     30  CB  LEU A   4      -8.905   6.117  -2.453  1.00 17.62           C  
ATOM     31  CG  LEU A   4      -8.676   6.715  -1.056  1.00 25.02           C  
ATOM     32  CD1 LEU A   4      -7.608   7.773  -1.059  1.00 27.49           C  
ATOM     33  CD2 LEU A   4      -9.917   7.441  -0.633  1.00 28.78           C  
ATOM     34  N   SER A   5     -11.034   5.548  -4.750  1.00 18.09           N  
ATOM     35  CA  SER A   5     -11.088   5.604  -6.199  1.00 16.56           C  
ATOM     36  C   SER A   5     -11.610   7.014  -6.536  1.00 21.22           C  
ATOM     37  O   SER A   5     -11.903   7.777  -5.598  1.00 17.63           O  
ATOM     38  CB  SER A   5     -12.025   4.558  -6.748  1.00 15.90           C  
ATOM     39  OG  SER A   5     -13.350   4.586  -6.243  1.00 22.45           O  
ATOM     40  N   GLY A   6     -11.749   7.403  -7.786  1.00 22.36           N  
ATOM     41  CA  GLY A   6     -12.225   8.737  -8.128  1.00 18.52           C  
ATOM     42  C   GLY A   6     -12.542   8.839  -9.576  1.00 20.43           C  
ATOM     43  O   GLY A   6     -12.422   7.894 -10.371  1.00 19.89           O  
ATOM     44  N   ASP A   7     -13.018  10.008  -9.952  1.00 17.75           N  
ATOM     45  CA  ASP A   7     -13.288  10.295 -11.348  1.00 14.63           C  
ATOM     46  C   ASP A   7     -13.193  11.805 -11.547  1.00 17.50           C  
ATOM     47  O   ASP A   7     -13.076  12.565 -10.576  1.00 17.10           O  
ATOM     48  CB  ASP A   7     -14.679   9.774 -11.786  1.00 15.83           C  
ATOM     49  CG  ASP A   7     -15.857  10.205 -10.919  1.00 23.05           C  
ATOM     50  OD1 ASP A   7     -16.070  11.394 -10.738  1.00 20.15           O  
ATOM     51  OD2 ASP A   7     -16.530   9.352 -10.387  1.00 25.78           O1-
ATOM     52  N   ALA A   8     -13.139  12.225 -12.800  1.00 19.52           N  
ATOM     53  CA  ALA A   8     -13.019  13.635 -13.180  1.00 15.71           C  
ATOM     54  C   ALA A   8     -13.467  13.758 -14.625  1.00 19.05           C  
ATOM     55  O   ALA A   8     -13.650  12.737 -15.321  1.00 18.32           O  
ATOM     56  CB  ALA A   8     -11.583  14.157 -13.063  1.00 14.05           C  
ATOM     57  N   ARG A   9     -13.820  14.970 -15.080  1.00 16.33           N  
ATOM     58  CA  ARG A   9     -14.244  15.186 -16.451  1.00 13.95           C  
ATOM     59  C   ARG A   9     -13.987  16.632 -16.791  1.00 17.40           C  
ATOM     60  O   ARG A   9     -13.859  17.468 -15.874  1.00 18.39           O  
ATOM     61  CB  ARG A   9     -15.725  14.830 -16.609  1.00 15.94           C  
ATOM     62  CG  ARG A   9     -16.668  15.816 -15.950  1.00 16.00           C  
ATOM     63  CD  ARG A   9     -18.012  15.181 -15.866  1.00 19.18           C  
ATOM     64  NE  ARG A   9     -18.946  16.193 -15.397  1.00 20.39           N  
ATOM     65  CZ  ARG A   9     -20.195  15.919 -14.989  1.00 23.61           C  
ATOM     66  NH1 ARG A   9     -20.696  14.674 -14.944  1.00 19.92           N1+
ATOM     67  NH2 ARG A   9     -20.949  16.956 -14.580  1.00 23.34           N  
ATOM     68  N   MET A  10     -13.780  16.972 -18.045  1.00 15.77           N  
ATOM     69  CA  MET A  10     -13.564  18.361 -18.450  1.00 19.06           C  
ATOM     70  C   MET A  10     -13.895  18.482 -19.921  1.00 24.44           C  
ATOM     71  O   MET A  10     -13.798  17.498 -20.659  1.00 18.02           O  
ATOM     72  CB  MET A  10     -12.138  18.848 -18.192  1.00 18.72           C  
ATOM     73  CG  MET A  10     -11.052  18.242 -19.030  1.00 25.28           C  
ATOM     74  SD  MET A  10      -9.514  19.095 -18.692  1.00 30.85           S  
ATOM     75  CE  MET A  10      -8.587  17.815 -19.441  1.00 33.80           C  
ATOM     76  N   GLY A  11     -14.441  19.614 -20.388  1.00 17.85           N  
ATOM     77  CA  GLY A  11     -14.833  19.740 -21.785  1.00 18.79           C  
ATOM     78  C   GLY A  11     -15.675  20.979 -21.907  1.00 25.94           C  
ATOM     79  O   GLY A  11     -15.519  21.896 -21.089  1.00 21.22           O  
ATOM     80  N   VAL A  12     -16.551  21.003 -22.896  1.00 22.43           N  
ATOM     81  CA  VAL A  12     -17.454  22.144 -23.186  1.00 22.84           C  
ATOM     82  C   VAL A  12     -18.875  21.664 -23.290  1.00 21.81           C  
ATOM     83  O   VAL A  12     -19.122  20.549 -23.759  1.00 20.69           O  
ATOM     84  CB  VAL A  12     -17.089  22.877 -24.507  1.00 23.09           C  
ATOM     85  CG1 VAL A  12     -15.811  23.644 -24.220  1.00 21.02           C  
ATOM     86  CG2 VAL A  12     -16.893  21.939 -25.689  1.00 22.56           C  
ATOM     87  N   MET A  13     -19.839  22.426 -22.763  1.00 16.86           N  
ATOM     88  CA  MET A  13     -21.214  21.978 -22.727  1.00 18.95           C  
ATOM     89  C   MET A  13     -22.046  23.133 -23.321  1.00 26.49           C  
ATOM     90  O   MET A  13     -21.766  24.300 -23.031  1.00 22.68           O  
ATOM     91  CB  MET A  13     -21.601  21.688 -21.261  1.00 19.57           C  
ATOM     92  CG AMET A  13     -23.084  21.315 -21.065  0.51 33.28           C  
ATOM     93  CG BMET A  13     -23.034  21.203 -20.976  0.49 31.07           C  
ATOM     94  SD AMET A  13     -24.227  22.733 -21.042  0.51 18.59           S  
ATOM     95  SD BMET A  13     -24.139  22.351 -20.081  0.49 33.60           S  
ATOM     96  CE AMET A  13     -23.561  23.506 -19.597  0.51 14.41           C  
ATOM     97  CE BMET A  13     -25.642  21.729 -20.752  0.49 12.77           C  
ATOM     98  N   TYR A  14     -23.060  22.845 -24.106  1.00 23.01           N  
ATOM     99  CA  TYR A  14     -23.884  23.830 -24.799  1.00 25.16           C  
ATOM    100  C   TYR A  14     -25.227  23.775 -24.118  1.00 23.22           C  
ATOM    101  O   TYR A  14     -25.863  22.717 -24.169  1.00 23.70           O  
ATOM    102  CB  TYR A  14     -24.043  23.424 -26.223  1.00 24.00           C  
ATOM    103  CG  TYR A  14     -24.841  24.417 -27.028  1.00 28.72           C  
ATOM    104  CD1 TYR A  14     -24.226  25.611 -27.366  1.00 29.42           C  
ATOM    105  CD2 TYR A  14     -26.119  24.089 -27.445  1.00 27.77           C  
ATOM    106  CE1 TYR A  14     -24.899  26.511 -28.162  1.00 32.13           C  
ATOM    107  CE2 TYR A  14     -26.799  24.987 -28.242  1.00 30.23           C  
ATOM    108  CZ  TYR A  14     -26.176  26.183 -28.591  1.00 32.81           C  
ATOM    109  OH  TYR A  14     -26.853  27.088 -29.397  1.00 50.72           O  
ATOM    110  N   ASN A  15     -25.716  24.879 -23.533  1.00 22.01           N  
ATOM    111  CA  ASN A  15     -26.959  24.849 -22.745  1.00 22.52           C  
ATOM    112  C   ASN A  15     -28.246  25.106 -23.538  1.00 31.39           C  
ATOM    113  O   ASN A  15     -29.354  25.208 -23.001  1.00 32.32           O  
ATOM    114  CB  ASN A  15     -26.878  25.879 -21.583  1.00 24.87           C  
ATOM    115  CG  ASN A  15     -26.702  27.320 -22.054  1.00 23.96           C  
ATOM    116  ND2 ASN A  15     -26.173  28.242 -21.268  1.00 26.01           N  
ATOM    117  OD1 ASN A  15     -26.931  27.633 -23.224  1.00 23.91           O  
ATOM    118  N   GLY A  16     -28.139  25.169 -24.851  1.00 26.28           N  
ATOM    119  CA  GLY A  16     -29.297  25.471 -25.664  1.00 33.32           C  
ATOM    120  C   GLY A  16     -29.017  26.761 -26.393  1.00 30.42           C  
ATOM    121  O   GLY A  16     -29.497  26.944 -27.510  1.00 36.69           O  
ATOM    122  N   ASP A  17     -28.185  27.646 -25.822  1.00 29.56           N  
ATOM    123  CA  ASP A  17     -27.857  28.956 -26.414  1.00 29.65           C  
ATOM    124  C   ASP A  17     -26.363  29.293 -26.443  1.00 32.17           C  
ATOM    125  O   ASP A  17     -25.825  29.861 -27.404  1.00 30.83           O  
ATOM    126  CB  ASP A  17     -28.631  30.081 -25.629  1.00 35.32           C  
ATOM    127  CG  ASP A  17     -30.177  29.930 -25.543  1.00 51.32           C  
ATOM    128  OD1 ASP A  17     -30.864  30.016 -26.578  1.00 59.35           O  
ATOM    129  OD2 ASP A  17     -30.689  29.699 -24.435  1.00 65.43           O1-
ATOM    130  N   ASP A  18     -25.638  28.901 -25.391  1.00 24.80           N  
ATOM    131  CA  ASP A  18     -24.221  29.192 -25.305  1.00 23.22           C  
ATOM    132  C   ASP A  18     -23.432  27.981 -24.812  1.00 26.47           C  
ATOM    133  O   ASP A  18     -23.988  27.089 -24.160  1.00 25.52           O  
ATOM    134  CB  ASP A  18     -23.939  30.302 -24.319  1.00 25.98           C  
ATOM    135  CG  ASP A  18     -24.473  31.589 -24.886  1.00 43.16           C  
ATOM    136  OD1 ASP A  18     -23.846  32.150 -25.775  1.00 41.16           O  
ATOM    137  OD2 ASP A  18     -25.541  31.991 -24.446  1.00 33.11           O1-
ATOM    138  N   TRP A  19     -22.151  28.014 -25.160  1.00 24.02           N  
ATOM    139  CA  TRP A  19     -21.153  27.051 -24.714  1.00 29.52           C  
ATOM    140  C   TRP A  19     -20.565  27.538 -23.390  1.00 34.72           C  
ATOM    141  O   TRP A  19     -20.420  28.749 -23.192  1.00 26.95           O  
ATOM    142  CB  TRP A  19     -20.013  26.922 -25.745  1.00 20.45           C  
ATOM    143  CG  TRP A  19     -20.453  26.144 -26.970  1.00 34.12           C  
ATOM    144  CD1 TRP A  19     -20.863  26.788 -28.104  1.00 38.42           C  
ATOM    145  CD2 TRP A  19     -20.535  24.778 -27.073  1.00 43.20           C  
ATOM    146  CE2 TRP A  19     -21.036  24.623 -28.354  1.00 43.13           C  
ATOM    147  CE3 TRP A  19     -20.266  23.674 -26.282  1.00 27.67           C  
ATOM    148  NE1 TRP A  19     -21.212  25.824 -28.928  1.00 28.98           N  
ATOM    149  CZ2 TRP A  19     -21.276  23.369 -28.865  1.00 37.29           C  
ATOM    150  CZ3 TRP A  19     -20.509  22.414 -26.793  1.00 26.31           C  
ATOM    151  CH2 TRP A  19     -21.006  22.269 -28.073  1.00 34.35           C  
ATOM    152  N   ASN A  20     -20.250  26.639 -22.456  1.00 20.14           N  
ATOM    153  CA  ASN A  20     -19.552  26.967 -21.234  1.00 20.63           C  
ATOM    154  C   ASN A  20     -18.529  25.873 -20.961  1.00 21.59           C  
ATOM    155  O   ASN A  20     -18.780  24.720 -21.338  1.00 20.91           O  
ATOM    156  CB  ASN A  20     -20.472  26.991 -20.031  1.00 19.26           C  
ATOM    157  CG  ASN A  20     -21.101  28.361 -19.780  1.00 16.94           C  
ATOM    158  ND2 ASN A  20     -22.347  28.441 -20.208  1.00 18.90           N  
ATOM    159  OD1 ASN A  20     -20.492  29.236 -19.144  1.00 19.32           O  
ATOM    160  N   PHE A  21     -17.441  26.202 -20.282  1.00 20.31           N  
ATOM    161  CA  PHE A  21     -16.512  25.188 -19.758  1.00 18.80           C  
ATOM    162  C   PHE A  21     -17.247  24.436 -18.645  1.00 29.01           C  
ATOM    163  O   PHE A  21     -18.007  25.052 -17.882  1.00 18.59           O  
ATOM    164  CB  PHE A  21     -15.247  25.838 -19.158  1.00 15.96           C  
ATOM    165  CG  PHE A  21     -14.325  26.649 -20.073  1.00 16.47           C  
ATOM    166  CD1 PHE A  21     -14.286  26.434 -21.443  1.00 18.25           C  
ATOM    167  CD2 PHE A  21     -13.525  27.610 -19.483  1.00 17.20           C  
ATOM    168  CE1 PHE A  21     -13.436  27.205 -22.195  1.00 20.58           C  
ATOM    169  CE2 PHE A  21     -12.677  28.371 -20.258  1.00 18.95           C  
ATOM    170  CZ  PHE A  21     -12.640  28.162 -21.609  1.00 18.40           C  
ATOM    171  N   SER A  22     -17.096  23.112 -18.507  1.00 16.37           N  
ATOM    172  CA  SER A  22     -17.743  22.348 -17.463  1.00 15.71           C  
ATOM    173  C   SER A  22     -16.754  21.261 -17.014  1.00 27.98           C  
ATOM    174  O   SER A  22     -16.289  20.478 -17.839  1.00 18.52           O  
ATOM    175  CB  SER A  22     -18.987  21.733 -18.003  1.00 13.95           C  
ATOM    176  OG  SER A  22     -19.719  21.166 -16.934  1.00 17.49           O  
ATOM    177  N   SER A  23     -16.387  21.193 -15.746  1.00 17.53           N  
ATOM    178  CA  SER A  23     -15.433  20.209 -15.257  1.00 21.71           C  
ATOM    179  C   SER A  23     -15.729  19.843 -13.813  1.00 27.30           C  
ATOM    180  O   SER A  23     -16.510  20.541 -13.155  1.00 18.45           O  
ATOM    181  CB  SER A  23     -14.047  20.804 -15.417  1.00 13.04           C  
ATOM    182  OG  SER A  23     -13.765  21.928 -14.610  1.00 17.20           O  
ATOM    183  N   ARG A  24     -15.241  18.735 -13.265  1.00 16.47           N  
ATOM    184  CA  ARG A  24     -15.405  18.387 -11.865  1.00 18.28           C  
ATOM    185  C   ARG A  24     -14.420  17.262 -11.542  1.00 21.67           C  
ATOM    186  O   ARG A  24     -13.910  16.635 -12.469  1.00 17.72           O  
ATOM    187  CB  ARG A  24     -16.779  17.835 -11.531  1.00 14.39           C  
ATOM    188  CG  ARG A  24     -17.207  16.523 -12.051  1.00 17.95           C  
ATOM    189  CD  ARG A  24     -18.446  16.109 -11.364  1.00 18.22           C  
ATOM    190  NE  ARG A  24     -18.752  14.775 -11.869  1.00 16.16           N  
ATOM    191  CZ  ARG A  24     -19.912  14.135 -11.778  1.00 22.92           C  
ATOM    192  NH1 ARG A  24     -20.994  14.663 -11.218  1.00 23.47           N1+
ATOM    193  NH2 ARG A  24     -19.958  12.870 -12.188  1.00 24.06           N  
ATOM    194  N   SER A  25     -14.162  16.986 -10.284  1.00 19.57           N  
ATOM    195  CA  SER A  25     -13.431  15.800  -9.880  1.00 19.55           C  
ATOM    196  C   SER A  25     -14.085  15.360  -8.593  1.00 22.34           C  
ATOM    197  O   SER A  25     -14.634  16.172  -7.821  1.00 18.07           O  
ATOM    198  CB  SER A  25     -11.925  16.099  -9.692  1.00 15.96           C  
ATOM    199  OG  SER A  25     -11.576  17.211  -8.920  1.00 31.90           O  
ATOM    200  N   ARG A  26     -14.100  14.047  -8.321  1.00 16.42           N  
ATOM    201  CA  ARG A  26     -14.731  13.446  -7.144  1.00 14.69           C  
ATOM    202  C   ARG A  26     -13.822  12.314  -6.616  1.00 18.06           C  
ATOM    203  O   ARG A  26     -13.024  11.770  -7.397  1.00 16.70           O  
ATOM    204  CB  ARG A  26     -16.087  12.834  -7.504  1.00 15.19           C  
ATOM    205  CG  ARG A  26     -16.974  13.864  -8.205  1.00 18.12           C  
ATOM    206  CD  ARG A  26     -18.380  13.367  -8.319  1.00 19.43           C  
ATOM    207  NE  ARG A  26     -18.389  12.150  -9.066  1.00 17.77           N  
ATOM    208  CZ  ARG A  26     -19.464  11.393  -9.217  1.00 29.11           C  
ATOM    209  NH1 ARG A  26     -20.638  11.695  -8.697  1.00 20.54           N1+
ATOM    210  NH2 ARG A  26     -19.358  10.242  -9.876  1.00 23.76           N  
ATOM    211  N   VAL A  27     -13.919  11.963  -5.344  1.00 18.18           N  
ATOM    212  CA  VAL A  27     -13.188  10.850  -4.728  1.00 17.02           C  
ATOM    213  C   VAL A  27     -14.268  10.031  -4.038  1.00 20.98           C  
ATOM    214  O   VAL A  27     -15.195  10.602  -3.427  1.00 18.90           O  
ATOM    215  CB  VAL A  27     -12.150  11.374  -3.714  1.00 13.14           C  
ATOM    216  CG1 VAL A  27     -11.615  10.298  -2.773  1.00 20.80           C  
ATOM    217  CG2 VAL A  27     -10.996  11.920  -4.537  1.00 18.48           C  
ATOM    218  N   LEU A  28     -14.178   8.699  -4.189  1.00 13.21           N  
ATOM    219  CA  LEU A  28     -15.044   7.758  -3.518  1.00 12.34           C  
ATOM    220  C   LEU A  28     -14.273   6.976  -2.440  1.00 16.60           C  
ATOM    221  O   LEU A  28     -13.160   6.491  -2.650  1.00 19.12           O  
ATOM    222  CB  LEU A  28     -15.654   6.814  -4.566  1.00 15.44           C  
ATOM    223  CG  LEU A  28     -16.484   5.635  -4.056  1.00 17.29           C  
ATOM    224  CD1 LEU A  28     -17.804   6.064  -3.421  1.00 19.53           C  
ATOM    225  CD2 LEU A  28     -16.794   4.770  -5.237  1.00 18.79           C  
ATOM    226  N   PHE A  29     -14.802   6.909  -1.231  1.00 14.46           N  
ATOM    227  CA  PHE A  29     -14.259   6.126  -0.128  1.00 19.10           C  
ATOM    228  C   PHE A  29     -15.026   4.824  -0.124  1.00 28.14           C  
ATOM    229  O   PHE A  29     -16.258   4.886  -0.011  1.00 19.55           O  
ATOM    230  CB  PHE A  29     -14.498   6.780   1.216  1.00 14.05           C  
ATOM    231  CG  PHE A  29     -13.830   8.130   1.320  1.00 21.24           C  
ATOM    232  CD1 PHE A  29     -12.469   8.226   1.457  1.00 17.81           C  
ATOM    233  CD2 PHE A  29     -14.595   9.289   1.259  1.00 23.31           C  
ATOM    234  CE1 PHE A  29     -11.872   9.470   1.525  1.00 26.27           C  
ATOM    235  CE2 PHE A  29     -13.998  10.532   1.330  1.00 20.41           C  
ATOM    236  CZ  PHE A  29     -12.634  10.628   1.460  1.00 22.27           C  
ATOM    237  N   THR A  30     -14.402   3.635  -0.265  1.00 18.98           N  
ATOM    238  CA  THR A  30     -15.127   2.360  -0.167  1.00 17.37           C  
ATOM    239  C   THR A  30     -14.585   1.635   1.039  1.00 18.66           C  
ATOM    240  O   THR A  30     -13.373   1.444   1.151  1.00 21.64           O  
ATOM    241  CB  THR A  30     -14.900   1.527  -1.367  1.00 16.98           C  
ATOM    242  CG2 THR A  30     -15.642   0.249  -1.279  1.00 20.20           C  
ATOM    243  OG1 THR A  30     -15.361   2.260  -2.483  1.00 23.49           O  
ATOM    244  N   MET A  31     -15.433   1.283   1.985  1.00 16.66           N  
ATOM    245  CA  MET A  31     -14.989   0.687   3.225  1.00 17.95           C  
ATOM    246  C   MET A  31     -15.552  -0.699   3.299  1.00 20.41           C  
ATOM    247  O   MET A  31     -16.694  -0.918   2.882  1.00 16.53           O  
ATOM    248  CB  MET A  31     -15.471   1.503   4.409  1.00 18.36           C  
ATOM    249  CG  MET A  31     -14.891   2.907   4.308  1.00 28.91           C  
ATOM    250  SD  MET A  31     -15.127   3.857   5.804  1.00 29.44           S  
ATOM    251  CE  MET A  31     -16.803   4.299   5.572  1.00 24.49           C  
ATOM    252  N   SER A  32     -14.777  -1.690   3.769  1.00 18.58           N  
ATOM    253  CA  SER A  32     -15.274  -3.076   3.804  1.00 18.25           C  
ATOM    254  C   SER A  32     -14.664  -3.896   4.933  1.00 17.77           C  
ATOM    255  O   SER A  32     -13.621  -3.489   5.495  1.00 21.99           O  
ATOM    256  CB  SER A  32     -14.995  -3.777   2.458  1.00 21.16           C  
ATOM    257  OG  SER A  32     -13.648  -3.543   2.074  1.00 36.32           O  
ATOM    258  N   GLY A  33     -15.420  -4.940   5.286  1.00 18.75           N  
ATOM    259  CA  GLY A  33     -15.039  -5.841   6.357  1.00 19.45           C  
ATOM    260  C   GLY A  33     -15.843  -7.139   6.272  1.00 19.89           C  
ATOM    261  O   GLY A  33     -16.781  -7.256   5.474  1.00 18.98           O  
ATOM    262  N   THR A  34     -15.476  -8.131   7.110  1.00 20.70           N  
ATOM    263  CA  THR A  34     -16.074  -9.454   7.125  1.00 18.70           C  
ATOM    264  C   THR A  34     -16.104  -9.883   8.574  1.00 15.56           C  
ATOM    265  O   THR A  34     -15.115  -9.676   9.281  1.00 22.55           O  
ATOM    266  CB  THR A  34     -15.219 -10.487   6.352  1.00 23.51           C  
ATOM    267  CG2 THR A  34     -15.906 -11.810   6.131  1.00 21.14           C  
ATOM    268  OG1 THR A  34     -15.010  -9.955   5.070  1.00 25.34           O  
ATOM    269  N   THR A  35     -17.183 -10.479   9.053  1.00 16.89           N  
ATOM    270  CA  THR A  35     -17.224 -10.877  10.437  1.00 19.04           C  
ATOM    271  C   THR A  35     -16.608 -12.290  10.454  1.00 31.99           C  
ATOM    272  O   THR A  35     -16.383 -12.907   9.405  1.00 22.91           O  
ATOM    273  CB  THR A  35     -18.674 -10.912  10.913  1.00 21.23           C  
ATOM    274  CG2 THR A  35     -19.373  -9.537  10.731  1.00 20.86           C  
ATOM    275  OG1 THR A  35     -19.344 -11.913  10.132  1.00 19.46           O  
ATOM    276  N   ASP A  36     -16.439 -12.861  11.639  1.00 26.13           N  
ATOM    277  CA  ASP A  36     -15.876 -14.193  11.842  1.00 25.73           C  
ATOM    278  C   ASP A  36     -16.683 -15.240  11.102  1.00 25.09           C  
ATOM    279  O   ASP A  36     -16.089 -16.150  10.509  1.00 31.82           O  
ATOM    280  CB  ASP A  36     -15.849 -14.461  13.335  1.00 23.29           C  
ATOM    281  CG  ASP A  36     -14.784 -13.664  14.105  1.00 29.35           C  
ATOM    282  OD1 ASP A  36     -13.944 -13.005  13.460  1.00 32.92           O  
ATOM    283  OD2 ASP A  36     -14.818 -13.706  15.351  1.00 36.59           O1-
ATOM    284  N   SER A  37     -18.009 -15.151  10.998  1.00 25.70           N  
ATOM    285  CA  SER A  37     -18.727 -16.157  10.240  1.00 23.90           C  
ATOM    286  C   SER A  37     -18.869 -15.859   8.757  1.00 22.34           C  
ATOM    287  O   SER A  37     -19.558 -16.610   8.054  1.00 24.38           O  
ATOM    288  CB  SER A  37     -20.097 -16.349  10.879  1.00 30.09           C  
ATOM    289  OG  SER A  37     -20.928 -15.200  10.733  1.00 48.00           O  
ATOM    290  N   GLY A  38     -18.267 -14.762   8.256  1.00 21.78           N  
ATOM    291  CA  GLY A  38     -18.344 -14.462   6.844  1.00 18.40           C  
ATOM    292  C   GLY A  38     -19.509 -13.564   6.406  1.00 21.34           C  
ATOM    293  O   GLY A  38     -19.843 -13.551   5.211  1.00 22.81           O  
ATOM    294  N   LEU A  39     -20.186 -12.850   7.324  1.00 21.84           N  
ATOM    295  CA  LEU A  39     -21.128 -11.814   6.882  1.00 23.27           C  
ATOM    296  C   LEU A  39     -20.225 -10.685   6.382  1.00 19.54           C  
ATOM    297  O   LEU A  39     -19.166 -10.395   6.952  1.00 23.50           O  
ATOM    298  CB  LEU A  39     -21.959 -11.265   8.021  1.00 22.31           C  
ATOM    299  CG  LEU A  39     -22.847 -12.265   8.696  1.00 21.30           C  
ATOM    300  CD1 LEU A  39     -23.619 -11.600   9.793  1.00 28.69           C  
ATOM    301  CD2 LEU A  39     -23.747 -12.856   7.687  1.00 25.27           C  
ATOM    302  N   GLU A  40     -20.548 -10.024   5.287  1.00 18.39           N  
ATOM    303  CA  GLU A  40     -19.727  -8.968   4.742  1.00 18.96           C  
ATOM    304  C   GLU A  40     -20.426  -7.650   5.114  1.00 26.64           C  
ATOM    305  O   GLU A  40     -21.659  -7.577   5.176  1.00 22.66           O  
ATOM    306  CB  GLU A  40     -19.667  -9.082   3.238  1.00 21.71           C  
ATOM    307  CG  GLU A  40     -19.133 -10.405   2.669  1.00 36.43           C  
ATOM    308  CD  GLU A  40     -17.665 -10.656   2.992  1.00 58.73           C  
ATOM    309  OE1 GLU A  40     -16.865  -9.720   2.973  1.00 52.82           O  
ATOM    310  OE2 GLU A  40     -17.320 -11.804   3.255  1.00 61.13           O1-
ATOM    311  N   PHE A  41     -19.685  -6.603   5.367  1.00 23.28           N  
ATOM    312  CA  PHE A  41     -20.279  -5.326   5.715  1.00 20.43           C  
ATOM    313  C   PHE A  41     -19.475  -4.242   5.048  1.00 33.11           C  
ATOM    314  O   PHE A  41     -18.335  -4.480   4.609  1.00 17.55           O  
ATOM    315  CB  PHE A  41     -20.294  -5.198   7.234  1.00 17.40           C  
ATOM    316  CG  PHE A  41     -18.976  -5.249   8.012  1.00 19.97           C  
ATOM    317  CD1 PHE A  41     -18.220  -4.115   8.222  1.00 18.79           C  
ATOM    318  CD2 PHE A  41     -18.577  -6.455   8.581  1.00 24.90           C  
ATOM    319  CE1 PHE A  41     -17.076  -4.157   8.998  1.00 18.42           C  
ATOM    320  CE2 PHE A  41     -17.432  -6.499   9.358  1.00 18.53           C  
ATOM    321  CZ  PHE A  41     -16.689  -5.357   9.565  1.00 20.56           C  
ATOM    322  N   GLY A  42     -20.022  -3.042   4.920  1.00 16.60           N  
ATOM    323  CA  GLY A  42     -19.274  -1.993   4.277  1.00 15.94           C  
ATOM    324  C   GLY A  42     -20.048  -0.670   4.345  1.00 18.51           C  
ATOM    325  O   GLY A  42     -21.130  -0.633   4.932  1.00 17.74           O  
ATOM    326  N   ALA A  43     -19.461   0.349   3.753  1.00 19.68           N  
ATOM    327  CA  ALA A  43     -20.052   1.677   3.680  1.00 19.54           C  
ATOM    328  C   ALA A  43     -19.337   2.426   2.564  1.00 25.22           C  
ATOM    329  O   ALA A  43     -18.176   2.126   2.239  1.00 20.81           O  
ATOM    330  CB  ALA A  43     -19.847   2.397   5.009  1.00 16.52           C  
ATOM    331  N   SER A  44     -19.961   3.363   1.845  1.00 17.32           N  
ATOM    332  CA  SER A  44     -19.219   4.206   0.932  1.00 13.95           C  
ATOM    333  C   SER A  44     -19.938   5.556   0.790  1.00 17.36           C  
ATOM    334  O   SER A  44     -21.152   5.618   1.016  1.00 16.29           O  
ATOM    335  CB  SER A  44     -19.109   3.575  -0.449  1.00 18.32           C  
ATOM    336  OG  SER A  44     -20.350   3.198  -0.969  1.00 28.70           O  
ATOM    337  N   PHE A  45     -19.182   6.566   0.423  1.00 18.21           N  
ATOM    338  CA  PHE A  45     -19.708   7.885   0.118  1.00 19.59           C  
ATOM    339  C   PHE A  45     -18.607   8.646  -0.581  1.00 21.25           C  
ATOM    340  O   PHE A  45     -17.437   8.234  -0.499  1.00 19.84           O  
ATOM    341  CB  PHE A  45     -20.137   8.597   1.418  1.00 12.80           C  
ATOM    342  CG  PHE A  45     -19.084   8.904   2.461  1.00 16.76           C  
ATOM    343  CD1 PHE A  45     -18.353  10.079   2.411  1.00 13.03           C  
ATOM    344  CD2 PHE A  45     -18.850   7.994   3.492  1.00 15.77           C  
ATOM    345  CE1 PHE A  45     -17.385  10.337   3.391  1.00 18.11           C  
ATOM    346  CE2 PHE A  45     -17.887   8.263   4.459  1.00 14.29           C  
ATOM    347  CZ  PHE A  45     -17.145   9.432   4.416  1.00 18.49           C  
ATOM    348  N   LYS A  46     -18.925   9.742  -1.286  1.00 14.65           N  
ATOM    349  CA  LYS A  46     -17.931  10.522  -1.984  1.00 13.19           C  
ATOM    350  C   LYS A  46     -17.510  11.677  -1.139  1.00 16.83           C  
ATOM    351  O   LYS A  46     -18.231  12.073  -0.214  1.00 18.21           O  
ATOM    352  CB  LYS A  46     -18.450  11.036  -3.306  1.00 14.48           C  
ATOM    353  CG  LYS A  46     -18.891   9.855  -4.140  1.00 19.35           C  
ATOM    354  CD  LYS A  46     -19.139  10.198  -5.579  1.00 22.07           C  
ATOM    355  CE  LYS A  46     -19.625   8.964  -6.316  1.00 29.45           C  
ATOM    356  NZ  LYS A  46     -20.954   8.593  -5.872  1.00 30.58           N1+
ATOM    357  N   ALA A  47     -16.376  12.276  -1.434  1.00 13.74           N  
ATOM    358  CA  ALA A  47     -15.806  13.263  -0.561  1.00 14.51           C  
ATOM    359  C   ALA A  47     -16.754  14.486  -0.467  1.00 17.84           C  
ATOM    360  O   ALA A  47     -16.894  15.089   0.606  1.00 16.71           O  
ATOM    361  CB  ALA A  47     -14.478  13.743  -1.113  1.00 13.21           C  
ATOM    362  N   HIS A  48     -17.401  14.892  -1.554  1.00 18.81           N  
ATOM    363  CA  HIS A  48     -18.294  16.070  -1.516  1.00 17.50           C  
ATOM    364  C   HIS A  48     -19.565  15.783  -0.733  1.00 22.24           C  
ATOM    365  O   HIS A  48     -20.300  16.718  -0.437  1.00 17.89           O  
ATOM    366  CB  HIS A  48     -18.638  16.519  -2.956  1.00 11.96           C  
ATOM    367  CG  HIS A  48     -19.516  15.579  -3.747  1.00 19.24           C  
ATOM    368  CD2 HIS A  48     -20.865  15.752  -3.921  1.00 18.37           C  
ATOM    369  ND1 HIS A  48     -19.200  14.454  -4.377  1.00 19.50           N  
ATOM    370  CE1 HIS A  48     -20.276  13.943  -4.917  1.00 20.35           C  
ATOM    371  NE2 HIS A  48     -21.286  14.739  -4.637  1.00 20.64           N  
ATOM    372  N   GLU A  49     -19.812  14.523  -0.339  1.00 14.70           N  
ATOM    373  CA  GLU A  49     -20.980  14.095   0.379  1.00 14.46           C  
ATOM    374  C   GLU A  49     -20.617  13.836   1.804  1.00 14.22           C  
ATOM    375  O   GLU A  49     -21.467  13.282   2.520  1.00 15.82           O  
ATOM    376  CB  GLU A  49     -21.553  12.778  -0.056  1.00 15.73           C  
ATOM    377  CG  GLU A  49     -21.780  12.668  -1.526  1.00 24.60           C  
ATOM    378  CD  GLU A  49     -22.283  11.289  -1.941  1.00 32.30           C  
ATOM    379  OE1 GLU A  49     -21.724  10.253  -1.570  1.00 21.35           O  
ATOM    380  OE2 GLU A  49     -23.265  11.257  -2.671  1.00 21.91           O1-
ATOM    381  N   SER A  50     -19.423  14.187   2.282  1.00 14.73           N  
ATOM    382  CA  SER A  50     -19.060  13.770   3.621  1.00 13.74           C  
ATOM    383  C   SER A  50     -19.941  14.332   4.735  1.00 20.29           C  
ATOM    384  O   SER A  50     -20.197  13.610   5.709  1.00 16.11           O  
ATOM    385  CB ASER A  50     -17.639  14.184   3.928  0.60 12.78           C  
ATOM    386  CB BSER A  50     -17.606  14.120   3.898  0.40 12.35           C  
ATOM    387  OG ASER A  50     -16.693  13.801   2.946  0.60 15.12           O  
ATOM    388  OG BSER A  50     -17.272  15.482   3.704  0.40 13.87           O  
ATOM    389  N   VAL A  51     -20.444  15.602   4.650  1.00 15.56           N  
ATOM    390  CA  VAL A  51     -21.358  16.118   5.683  1.00 16.90           C  
ATOM    391  C   VAL A  51     -22.658  15.329   5.752  1.00 10.27           C  
ATOM    392  O   VAL A  51     -23.103  14.953   6.849  1.00 17.77           O  
ATOM    393  CB  VAL A  51     -21.614  17.611   5.373  1.00 16.34           C  
ATOM    394  CG1 VAL A  51     -22.653  18.144   6.337  1.00 18.56           C  
ATOM    395  CG2 VAL A  51     -20.344  18.407   5.553  1.00 16.82           C  
ATOM    396  N   GLY A  52     -23.244  15.037   4.582  1.00 12.24           N  
ATOM    397  CA  GLY A  52     -24.463  14.272   4.483  1.00 13.64           C  
ATOM    398  C   GLY A  52     -24.274  12.836   4.908  1.00 15.14           C  
ATOM    399  O   GLY A  52     -25.156  12.261   5.531  1.00 15.99           O  
ATOM    400  N   ALA A  53     -23.112  12.226   4.616  1.00 18.76           N  
ATOM    401  CA  ALA A  53     -22.889  10.828   4.995  1.00 14.32           C  
ATOM    402  C   ALA A  53     -22.877  10.686   6.490  1.00 10.54           C  
ATOM    403  O   ALA A  53     -23.298   9.657   7.018  1.00 15.30           O  
ATOM    404  CB  ALA A  53     -21.568  10.378   4.421  1.00 14.72           C  
ATOM    405  N   GLU A  54     -22.449  11.708   7.256  1.00 13.35           N  
ATOM    406  CA  GLU A  54     -22.490  11.662   8.689  1.00 13.86           C  
ATOM    407  C   GLU A  54     -23.913  11.722   9.285  1.00 17.54           C  
ATOM    408  O   GLU A  54     -24.043  11.449  10.476  1.00 17.99           O  
ATOM    409  CB  GLU A  54     -21.594  12.791   9.160  1.00 16.36           C  
ATOM    410  CG  GLU A  54     -21.174  12.702  10.648  1.00 19.98           C  
ATOM    411  CD  GLU A  54     -21.994  13.525  11.664  1.00 33.77           C  
ATOM    412  OE1 GLU A  54     -22.638  14.488  11.256  1.00 26.33           O  
ATOM    413  OE2 GLU A  54     -21.996  13.218  12.858  1.00 28.75           O1-
ATOM    414  N   THR A  55     -25.031  12.014   8.585  1.00 19.05           N  
ATOM    415  CA  THR A  55     -26.371  11.984   9.181  1.00 15.96           C  
ATOM    416  C   THR A  55     -27.239  10.920   8.515  1.00 17.46           C  
ATOM    417  O   THR A  55     -28.380  10.728   8.910  1.00 21.17           O  
ATOM    418  CB  THR A  55     -27.058  13.391   9.019  1.00 13.94           C  
ATOM    419  CG2 THR A  55     -26.126  14.562   9.267  1.00 18.93           C  
ATOM    420  OG1 THR A  55     -27.518  13.450   7.673  1.00 16.77           O  
ATOM    421  N   GLY A  56     -26.806  10.212   7.456  1.00 18.11           N  
ATOM    422  CA  GLY A  56     -27.621   9.189   6.796  1.00 14.36           C  
ATOM    423  C   GLY A  56     -28.218   9.671   5.504  1.00 14.53           C  
ATOM    424  O   GLY A  56     -28.863   8.951   4.744  1.00 19.77           O  
ATOM    425  N   GLU A  57     -28.016  10.954   5.212  1.00 17.95           N  
ATOM    426  CA  GLU A  57     -28.598  11.569   4.037  1.00 14.56           C  
ATOM    427  C   GLU A  57     -27.915  11.161   2.740  1.00 19.55           C  
ATOM    428  O   GLU A  57     -28.536  11.142   1.664  1.00 18.74           O  
ATOM    429  CB  GLU A  57     -28.511  13.075   4.228  1.00 15.25           C  
ATOM    430  CG  GLU A  57     -29.069  13.805   3.010  1.00 25.44           C  
ATOM    431  CD  GLU A  57     -29.154  15.321   3.105  1.00 32.41           C  
ATOM    432  OE1 GLU A  57     -28.549  15.899   4.007  1.00 25.94           O  
ATOM    433  OE2 GLU A  57     -29.833  15.913   2.260  1.00 40.55           O1-
ATOM    434  N   ASP A  58     -26.582  10.949   2.806  1.00 16.20           N  
ATOM    435  CA  ASP A  58     -25.809  10.589   1.627  1.00 12.73           C  
ATOM    436  C   ASP A  58     -24.973   9.337   1.968  1.00 13.30           C  
ATOM    437  O   ASP A  58     -24.737   9.075   3.143  1.00 14.77           O  
ATOM    438  CB  ASP A  58     -24.851  11.675   1.252  1.00 14.67           C  
ATOM    439  CG  ASP A  58     -25.532  12.907   0.648  1.00 21.34           C  
ATOM    440  OD1 ASP A  58     -26.461  12.763  -0.146  1.00 21.30           O  
ATOM    441  OD2 ASP A  58     -25.093  13.998   0.979  1.00 23.15           O1-
ATOM    442  N   GLY A  59     -24.538   8.621   0.946  1.00 19.15           N  
ATOM    443  CA  GLY A  59     -23.738   7.407   1.131  1.00 17.18           C  
ATOM    444  C   GLY A  59     -24.599   6.273   1.613  1.00 19.54           C  
ATOM    445  O   GLY A  59     -25.786   6.453   1.923  1.00 19.80           O  
ATOM    446  N   THR A  60     -24.092   5.037   1.653  1.00 16.10           N  
ATOM    447  CA  THR A  60     -24.855   3.899   2.189  1.00 16.20           C  
ATOM    448  C   THR A  60     -24.001   3.026   3.121  1.00 19.22           C  
ATOM    449  O   THR A  60     -22.770   3.127   3.036  1.00 17.59           O  
ATOM    450  CB  THR A  60     -25.402   2.970   1.089  1.00 22.89           C  
ATOM    451  CG2 THR A  60     -26.569   3.599   0.340  1.00 22.82           C  
ATOM    452  OG1 THR A  60     -24.350   2.675   0.186  1.00 24.63           O  
ATOM    453  N   VAL A  61     -24.631   2.280   4.031  1.00 17.23           N  
ATOM    454  CA  VAL A  61     -24.000   1.338   4.949  1.00 19.01           C  
ATOM    455  C   VAL A  61     -24.695  -0.004   4.636  1.00 26.28           C  
ATOM    456  O   VAL A  61     -25.910  -0.020   4.344  1.00 18.85           O  
ATOM    457  CB  VAL A  61     -24.241   1.758   6.418  1.00 17.83           C  
ATOM    458  CG1 VAL A  61     -23.611   0.757   7.383  1.00 18.08           C  
ATOM    459  CG2 VAL A  61     -23.605   3.096   6.658  1.00 17.74           C  
ATOM    460  N   PHE A  62     -24.001  -1.160   4.608  1.00 19.51           N  
ATOM    461  CA  PHE A  62     -24.680  -2.426   4.339  1.00 17.61           C  
ATOM    462  C   PHE A  62     -24.117  -3.580   5.177  1.00 21.17           C  
ATOM    463  O   PHE A  62     -22.998  -3.504   5.717  1.00 17.39           O  
ATOM    464  CB  PHE A  62     -24.579  -2.788   2.865  1.00 17.41           C  
ATOM    465  CG  PHE A  62     -23.206  -3.280   2.395  1.00 22.01           C  
ATOM    466  CD1 PHE A  62     -22.876  -4.637   2.485  1.00 26.08           C  
ATOM    467  CD2 PHE A  62     -22.312  -2.374   1.857  1.00 20.41           C  
ATOM    468  CE1 PHE A  62     -21.648  -5.076   2.025  1.00 24.18           C  
ATOM    469  CE2 PHE A  62     -21.082  -2.833   1.401  1.00 39.24           C  
ATOM    470  CZ  PHE A  62     -20.747  -4.176   1.481  1.00 26.42           C  
ATOM    471  N   LEU A  63     -24.945  -4.616   5.256  1.00 21.61           N  
ATOM    472  CA  LEU A  63     -24.627  -5.891   5.908  1.00 23.98           C  
ATOM    473  C   LEU A  63     -25.172  -6.950   4.989  1.00 24.88           C  
ATOM    474  O   LEU A  63     -26.331  -6.802   4.591  1.00 20.07           O  
ATOM    475  CB  LEU A  63     -25.328  -6.096   7.253  1.00 23.98           C  
ATOM    476  CG  LEU A  63     -25.024  -7.401   8.006  1.00 27.68           C  
ATOM    477  CD1 LEU A  63     -23.569  -7.438   8.457  1.00 22.99           C  
ATOM    478  CD2 LEU A  63     -25.867  -7.455   9.245  1.00 34.32           C  
ATOM    479  N   SER A  64     -24.413  -7.983   4.563  1.00 21.19           N  
ATOM    480  CA  SER A  64     -24.952  -9.046   3.719  1.00 18.57           C  
ATOM    481  C   SER A  64     -24.478 -10.429   4.197  1.00 18.66           C  
ATOM    482  O   SER A  64     -23.518 -10.579   4.946  1.00 22.26           O  
ATOM    483  CB  SER A  64     -24.552  -8.854   2.276  1.00 18.27           C  
ATOM    484  OG  SER A  64     -23.166  -8.724   2.065  1.00 24.76           O  
ATOM    485  N   GLY A  65     -25.263 -11.406   3.859  1.00 21.15           N  
ATOM    486  CA  GLY A  65     -25.011 -12.757   4.255  1.00 24.41           C  
ATOM    487  C   GLY A  65     -25.783 -13.637   3.306  1.00 28.66           C  
ATOM    488  O   GLY A  65     -26.212 -13.255   2.207  1.00 22.09           O  
ATOM    489  N   ALA A  66     -26.039 -14.835   3.792  1.00 26.28           N  
ATOM    490  CA  ALA A  66     -26.764 -15.807   3.010  1.00 25.46           C  
ATOM    491  C   ALA A  66     -28.210 -15.385   2.766  1.00 26.02           C  
ATOM    492  O   ALA A  66     -28.825 -15.796   1.786  1.00 27.00           O  
ATOM    493  CB  ALA A  66     -26.764 -17.121   3.748  1.00 28.91           C  
ATOM    494  N   PHE A  67     -28.702 -14.561   3.696  1.00 33.18           N  
ATOM    495  CA  PHE A  67     -30.038 -13.956   3.680  1.00 33.95           C  
ATOM    496  C   PHE A  67     -30.206 -12.837   2.645  1.00 35.16           C  
ATOM    497  O   PHE A  67     -31.328 -12.426   2.393  1.00 30.66           O  
ATOM    498  CB  PHE A  67     -30.374 -13.386   5.079  1.00 23.01           C  
ATOM    499  CG  PHE A  67     -29.445 -12.276   5.617  1.00 45.98           C  
ATOM    500  CD1 PHE A  67     -29.638 -10.943   5.242  1.00 41.66           C  
ATOM    501  CD2 PHE A  67     -28.386 -12.609   6.459  1.00 34.67           C  
ATOM    502  CE1 PHE A  67     -28.775  -9.970   5.698  1.00 40.95           C  
ATOM    503  CE2 PHE A  67     -27.527 -11.624   6.913  1.00 32.83           C  
ATOM    504  CZ  PHE A  67     -27.723 -10.308   6.532  1.00 35.21           C  
ATOM    505  N   GLY A  68     -29.175 -12.282   2.035  1.00 20.84           N  
ATOM    506  CA  GLY A  68     -29.342 -11.229   1.069  1.00 21.82           C  
ATOM    507  C   GLY A  68     -28.617 -10.041   1.637  1.00 28.92           C  
ATOM    508  O   GLY A  68     -27.761 -10.243   2.510  1.00 24.29           O  
ATOM    509  N   LYS A  69     -28.928  -8.804   1.248  1.00 21.72           N  
ATOM    510  CA  LYS A  69     -28.147  -7.641   1.644  1.00 18.84           C  
ATOM    511  C   LYS A  69     -29.112  -6.560   2.151  1.00 23.51           C  
ATOM    512  O   LYS A  69     -30.132  -6.321   1.504  1.00 20.90           O  
ATOM    513  CB  LYS A  69     -27.399  -7.147   0.424  1.00 16.30           C  
ATOM    514  CG  LYS A  69     -26.510  -5.928   0.676  1.00 16.85           C  
ATOM    515  CD  LYS A  69     -25.979  -5.543  -0.690  1.00 20.17           C  
ATOM    516  CE  LYS A  69     -25.145  -4.307  -0.584  1.00 31.92           C  
ATOM    517  NZ  LYS A  69     -24.527  -4.003  -1.865  1.00 46.73           N1+
ATOM    518  N   ILE A  70     -28.798  -5.925   3.244  1.00 19.45           N  
ATOM    519  CA  ILE A  70     -29.591  -4.839   3.817  1.00 23.74           C  
ATOM    520  C   ILE A  70     -28.724  -3.596   3.698  1.00 25.87           C  
ATOM    521  O   ILE A  70     -27.609  -3.577   4.231  1.00 20.11           O  
ATOM    522  CB  ILE A  70     -29.873  -5.130   5.290  1.00 25.58           C  
ATOM    523  CG1 ILE A  70     -30.724  -6.387   5.411  1.00 43.31           C  
ATOM    524  CG2 ILE A  70     -30.601  -3.939   5.910  1.00 33.44           C  
ATOM    525  CD1 ILE A  70     -30.708  -6.934   6.850  1.00 57.37           C  
ATOM    526  N   GLU A  71     -29.188  -2.525   3.067  1.00 19.38           N  
ATOM    527  CA  GLU A  71     -28.422  -1.307   2.864  1.00 17.37           C  
ATOM    528  C   GLU A  71     -29.235  -0.117   3.434  1.00 24.39           C  
ATOM    529  O   GLU A  71     -30.455  -0.090   3.185  1.00 20.85           O  
ATOM    530  CB  GLU A  71     -28.229  -1.212   1.397  1.00 15.42           C  
ATOM    531  CG  GLU A  71     -27.270  -0.144   0.955  1.00 22.29           C  
ATOM    532  CD  GLU A  71     -27.034  -0.136  -0.554  1.00 23.14           C  
ATOM    533  OE1 GLU A  71     -27.929  -0.552  -1.269  1.00 42.67           O  
ATOM    534  OE2 GLU A  71     -25.951   0.269  -0.999  1.00 53.77           O1-
ATOM    535  N   MET A  72     -28.648   0.854   4.146  1.00 19.50           N  
ATOM    536  CA  MET A  72     -29.409   1.969   4.704  1.00 17.32           C  
ATOM    537  C   MET A  72     -28.641   3.219   4.372  1.00 23.46           C  
ATOM    538  O   MET A  72     -27.398   3.205   4.447  1.00 19.57           O  
ATOM    539  CB  MET A  72     -29.516   1.792   6.184  1.00 18.57           C  
ATOM    540  CG  MET A  72     -30.467   2.815   6.839  1.00 19.11           C  
ATOM    541  SD  MET A  72     -30.736   2.515   8.589  1.00 23.42           S  
ATOM    542  CE  MET A  72     -31.734   1.076   8.475  1.00 18.32           C  
ATOM    543  N   GLY A  73     -29.340   4.286   3.943  1.00 17.35           N  
ATOM    544  CA  GLY A  73     -28.733   5.592   3.694  1.00 14.94           C  
ATOM    545  C   GLY A  73     -29.391   6.155   2.461  1.00 13.51           C  
ATOM    546  O   GLY A  73     -30.597   5.995   2.269  1.00 18.04           O  
ATOM    547  N   ASP A  74     -28.605   6.690   1.548  1.00 15.69           N  
ATOM    548  CA  ASP A  74     -29.109   7.212   0.320  1.00 17.65           C  
ATOM    549  C   ASP A  74     -29.139   6.056  -0.682  1.00 22.75           C  
ATOM    550  O   ASP A  74     -28.314   5.961  -1.583  1.00 21.21           O  
ATOM    551  CB  ASP A  74     -28.197   8.385  -0.104  1.00 14.59           C  
ATOM    552  CG  ASP A  74     -28.627   9.157  -1.356  1.00 19.98           C  
ATOM    553  OD1 ASP A  74     -29.617   8.785  -2.016  1.00 18.00           O  
ATOM    554  OD2 ASP A  74     -27.950  10.141  -1.686  1.00 24.40           O1-
ATOM    555  N   ALA A  75     -30.127   5.178  -0.564  1.00 18.50           N  
ATOM    556  CA  ALA A  75     -30.281   3.973  -1.385  1.00 19.75           C  
ATOM    557  C   ALA A  75     -31.257   4.128  -2.522  1.00 25.86           C  
ATOM    558  O   ALA A  75     -32.122   5.020  -2.511  1.00 24.49           O  
ATOM    559  CB  ALA A  75     -30.756   2.815  -0.505  1.00 15.70           C  
ATOM    560  N   LEU A  76     -31.136   3.278  -3.519  1.00 18.04           N  
ATOM    561  CA  LEU A  76     -32.054   3.230  -4.618  1.00 15.51           C  
ATOM    562  C   LEU A  76     -33.302   2.570  -4.150  1.00 14.71           C  
ATOM    563  O   LEU A  76     -33.302   1.916  -3.115  1.00 17.59           O  
ATOM    564  CB  LEU A  76     -31.516   2.420  -5.765  1.00 16.00           C  
ATOM    565  CG  LEU A  76     -30.215   2.956  -6.344  1.00 22.46           C  
ATOM    566  CD1 LEU A  76     -29.768   1.988  -7.408  1.00 21.79           C  
ATOM    567  CD2 LEU A  76     -30.378   4.380  -6.907  1.00 22.12           C  
ATOM    568  N   GLY A  77     -34.425   2.763  -4.830  1.00 17.76           N  
ATOM    569  CA  GLY A  77     -35.594   2.005  -4.443  1.00 17.10           C  
ATOM    570  C   GLY A  77     -35.501   0.640  -5.145  1.00 17.15           C  
ATOM    571  O   GLY A  77     -34.672   0.498  -6.058  1.00 18.35           O  
ATOM    572  N   ALA A  78     -36.335  -0.336  -4.770  1.00 20.25           N  
ATOM    573  CA  ALA A  78     -36.296  -1.703  -5.299  1.00 16.35           C  
ATOM    574  C   ALA A  78     -36.299  -1.852  -6.796  1.00 23.67           C  
ATOM    575  O   ALA A  78     -35.462  -2.577  -7.346  1.00 22.78           O  
ATOM    576  CB  ALA A  78     -37.450  -2.442  -4.763  1.00 18.71           C  
ATOM    577  N   SER A  79     -37.150  -1.145  -7.553  1.00 18.97           N  
ATOM    578  CA  SER A  79     -37.144  -1.237  -8.994  1.00 20.71           C  
ATOM    579  C   SER A  79     -35.884  -0.695  -9.632  1.00 27.48           C  
ATOM    580  O   SER A  79     -35.316  -1.348 -10.515  1.00 21.54           O  
ATOM    581  CB  SER A  79     -38.341  -0.493  -9.591  1.00 24.34           C  
ATOM    582  OG  SER A  79     -39.520  -0.950  -8.947  1.00 24.45           O  
ATOM    583  N   GLU A  80     -35.399   0.484  -9.240  1.00 20.47           N  
ATOM    584  CA  GLU A  80     -34.200   1.044  -9.815  1.00 18.48           C  
ATOM    585  C   GLU A  80     -33.010   0.123  -9.480  1.00 15.64           C  
ATOM    586  O   GLU A  80     -32.197  -0.068 -10.379  1.00 21.68           O  
ATOM    587  CB  GLU A  80     -33.971   2.409  -9.231  1.00 14.52           C  
ATOM    588  CG  GLU A  80     -32.873   3.074 -10.018  1.00 19.36           C  
ATOM    589  CD  GLU A  80     -32.688   4.560  -9.838  1.00 21.31           C  
ATOM    590  OE1 GLU A  80     -33.487   5.230  -9.193  1.00 23.28           O  
ATOM    591  OE2 GLU A  80     -31.755   5.115 -10.411  1.00 17.31           O1-
ATOM    592  N   ALA A  81     -32.953  -0.434  -8.261  1.00 18.80           N  
ATOM    593  CA  ALA A  81     -31.906  -1.357  -7.795  1.00 19.97           C  
ATOM    594  C   ALA A  81     -31.829  -2.553  -8.770  1.00 25.91           C  
ATOM    595  O   ALA A  81     -30.723  -2.968  -9.138  1.00 26.82           O  
ATOM    596  CB  ALA A  81     -32.231  -1.873  -6.396  1.00 18.56           C  
ATOM    597  N   LEU A  82     -32.936  -3.087  -9.297  1.00 24.81           N  
ATOM    598  CA  LEU A  82     -32.857  -4.167 -10.272  1.00 20.49           C  
ATOM    599  C   LEU A  82     -32.779  -3.745 -11.717  1.00 30.61           C  
ATOM    600  O   LEU A  82     -32.066  -4.421 -12.460  1.00 30.38           O  
ATOM    601  CB  LEU A  82     -34.047  -5.128 -10.119  1.00 18.07           C  
ATOM    602  CG  LEU A  82     -34.256  -5.719  -8.733  1.00 23.91           C  
ATOM    603  CD1 LEU A  82     -35.281  -6.826  -8.773  1.00 21.74           C  
ATOM    604  CD2 LEU A  82     -32.939  -6.227  -8.213  1.00 22.55           C  
ATOM    605  N   PHE A  83     -33.388  -2.650 -12.231  1.00 23.86           N  
ATOM    606  CA  PHE A  83     -33.408  -2.395 -13.679  1.00 18.13           C  
ATOM    607  C   PHE A  83     -32.559  -1.251 -14.153  1.00 21.39           C  
ATOM    608  O   PHE A  83     -32.306  -1.176 -15.357  1.00 24.29           O  
ATOM    609  CB  PHE A  83     -34.869  -2.171 -14.188  1.00 20.46           C  
ATOM    610  CG  PHE A  83     -35.835  -3.232 -13.639  1.00 31.47           C  
ATOM    611  CD1 PHE A  83     -35.563  -4.586 -13.804  1.00 36.76           C  
ATOM    612  CD2 PHE A  83     -36.959  -2.848 -12.924  1.00 29.87           C  
ATOM    613  CE1 PHE A  83     -36.404  -5.514 -13.247  1.00 29.95           C  
ATOM    614  CE2 PHE A  83     -37.792  -3.785 -12.371  1.00 27.18           C  
ATOM    615  CZ  PHE A  83     -37.508  -5.117 -12.531  1.00 28.91           C  
ATOM    616  N   GLY A  84     -32.075  -0.374 -13.246  1.00 21.59           N  
ATOM    617  CA  GLY A  84     -31.218   0.732 -13.643  1.00 19.54           C  
ATOM    618  C   GLY A  84     -31.841   1.755 -14.597  1.00 20.13           C  
ATOM    619  O   GLY A  84     -33.060   1.941 -14.654  1.00 24.79           O  
ATOM    620  N   ASP A  85     -30.988   2.442 -15.342  1.00 18.15           N  
ATOM    621  CA  ASP A  85     -31.353   3.526 -16.239  1.00 22.04           C  
ATOM    622  C   ASP A  85     -31.058   3.200 -17.679  1.00 32.84           C  
ATOM    623  O   ASP A  85     -30.459   2.173 -17.966  1.00 25.86           O  
ATOM    624  CB  ASP A  85     -30.590   4.814 -15.846  1.00 21.66           C  
ATOM    625  CG  ASP A  85     -31.123   5.360 -14.524  1.00 22.97           C  
ATOM    626  OD1 ASP A  85     -32.323   5.304 -14.268  1.00 22.67           O  
ATOM    627  OD2 ASP A  85     -30.320   5.789 -13.715  1.00 22.22           O1-
ATOM    628  N   LEU A  86     -31.435   4.061 -18.620  1.00 21.52           N  
ATOM    629  CA  LEU A  86     -31.192   3.853 -20.031  1.00 19.15           C  
ATOM    630  C   LEU A  86     -29.788   4.371 -20.296  1.00 18.35           C  
ATOM    631  O   LEU A  86     -29.133   4.925 -19.387  1.00 21.62           O  
ATOM    632  CB  LEU A  86     -32.255   4.606 -20.868  1.00 18.02           C  
ATOM    633  CG  LEU A  86     -33.718   4.250 -20.645  1.00 21.20           C  
ATOM    634  CD1 LEU A  86     -34.484   5.026 -21.705  1.00 24.06           C  
ATOM    635  CD2 LEU A  86     -34.036   2.753 -20.795  1.00 22.07           C  
ATOM    636  N   TYR A  87     -29.294   4.185 -21.517  1.00 20.03           N  
ATOM    637  CA  TYR A  87     -27.943   4.588 -21.910  1.00 23.10           C  
ATOM    638  C   TYR A  87     -27.646   6.058 -21.581  1.00 35.01           C  
ATOM    639  O   TYR A  87     -28.363   6.941 -22.017  1.00 21.25           O  
ATOM    640  CB  TYR A  87     -27.758   4.340 -23.430  1.00 22.33           C  
ATOM    641  CG  TYR A  87     -26.350   4.664 -23.923  1.00 24.26           C  
ATOM    642  CD1 TYR A  87     -25.257   3.884 -23.549  1.00 29.11           C  
ATOM    643  CD2 TYR A  87     -26.167   5.767 -24.731  1.00 25.25           C  
ATOM    644  CE1 TYR A  87     -23.991   4.228 -23.991  1.00 24.19           C  
ATOM    645  CE2 TYR A  87     -24.909   6.120 -25.166  1.00 23.60           C  
ATOM    646  CZ  TYR A  87     -23.843   5.347 -24.787  1.00 32.01           C  
ATOM    647  OH  TYR A  87     -22.594   5.745 -25.189  1.00 38.33           O  
ATOM    648  N   GLU A  88     -26.559   6.351 -20.877  1.00 24.04           N  
ATOM    649  CA  GLU A  88     -26.203   7.682 -20.450  1.00 23.00           C  
ATOM    650  C   GLU A  88     -25.495   8.397 -21.548  1.00 28.26           C  
ATOM    651  O   GLU A  88     -24.483   7.947 -22.087  1.00 25.13           O  
ATOM    652  CB  GLU A  88     -25.338   7.570 -19.201  1.00 19.61           C  
ATOM    653  CG  GLU A  88     -24.979   8.918 -18.657  1.00 19.84           C  
ATOM    654  CD  GLU A  88     -24.252   8.897 -17.321  1.00 19.96           C  
ATOM    655  OE1 GLU A  88     -24.734   8.348 -16.340  1.00 22.24           O  
ATOM    656  OE2 GLU A  88     -23.192   9.488 -17.244  1.00 28.96           O1-
ATOM    657  N   VAL A  89     -26.053   9.542 -21.882  1.00 20.98           N  
ATOM    658  CA  VAL A  89     -25.524  10.367 -22.945  1.00 19.79           C  
ATOM    659  C   VAL A  89     -24.834  11.600 -22.396  1.00 21.24           C  
ATOM    660  O   VAL A  89     -25.356  12.225 -21.457  1.00 25.75           O  
ATOM    661  CB  VAL A  89     -26.703  10.742 -23.878  1.00 21.18           C  
ATOM    662  CG1 VAL A  89     -26.249  11.789 -24.895  1.00 20.32           C  
ATOM    663  CG2 VAL A  89     -27.228   9.481 -24.565  1.00 23.18           C  
ATOM    664  N   GLY A  90     -23.707  11.901 -23.072  1.00 18.46           N  
ATOM    665  CA  GLY A  90     -22.834  13.062 -22.916  1.00 17.42           C  
ATOM    666  C   GLY A  90     -21.792  12.938 -21.788  1.00 16.29           C  
ATOM    667  O   GLY A  90     -22.022  12.241 -20.799  1.00 21.52           O  
ATOM    668  N   TYR A  91     -20.634  13.604 -21.869  1.00 15.81           N  
ATOM    669  CA  TYR A  91     -19.639  13.516 -20.814  1.00 16.90           C  
ATOM    670  C   TYR A  91     -20.140  14.134 -19.530  1.00 20.78           C  
ATOM    671  O   TYR A  91     -19.638  13.762 -18.483  1.00 20.06           O  
ATOM    672  CB  TYR A  91     -18.344  14.189 -21.261  1.00 14.86           C  
ATOM    673  CG  TYR A  91     -18.139  15.670 -20.960  1.00 20.42           C  
ATOM    674  CD1 TYR A  91     -17.545  16.044 -19.788  1.00 17.43           C  
ATOM    675  CD2 TYR A  91     -18.526  16.643 -21.860  1.00 21.36           C  
ATOM    676  CE1 TYR A  91     -17.344  17.376 -19.527  1.00 21.64           C  
ATOM    677  CE2 TYR A  91     -18.321  17.989 -21.610  1.00 17.13           C  
ATOM    678  CZ  TYR A  91     -17.734  18.331 -20.438  1.00 16.53           C  
ATOM    679  OH  TYR A  91     -17.538  19.643 -20.134  1.00 19.49           O  
ATOM    680  N   THR A  92     -21.091  15.102 -19.535  1.00 22.98           N  
ATOM    681  CA  THR A  92     -21.599  15.728 -18.299  1.00 20.64           C  
ATOM    682  C   THR A  92     -22.883  15.036 -17.835  1.00 19.15           C  
ATOM    683  O   THR A  92     -23.398  15.398 -16.789  1.00 20.90           O  
ATOM    684  CB  THR A  92     -21.905  17.264 -18.505  1.00 15.66           C  
ATOM    685  CG2 THR A  92     -20.762  18.094 -18.990  1.00 13.61           C  
ATOM    686  OG1 THR A  92     -22.894  17.334 -19.525  1.00 19.23           O  
ATOM    687  N   ASP A  93     -23.399  14.010 -18.544  1.00 18.00           N  
ATOM    688  CA  ASP A  93     -24.675  13.323 -18.335  1.00 18.24           C  
ATOM    689  C   ASP A  93     -25.767  14.352 -18.597  1.00 25.81           C  
ATOM    690  O   ASP A  93     -26.254  15.047 -17.685  1.00 22.47           O  
ATOM    691  CB  ASP A  93     -24.806  12.746 -16.901  1.00 17.88           C  
ATOM    692  CG  ASP A  93     -26.073  11.955 -16.630  1.00 20.65           C  
ATOM    693  OD1 ASP A  93     -26.900  11.667 -17.508  1.00 25.25           O  
ATOM    694  OD2 ASP A  93     -26.306  11.578 -15.486  1.00 20.38           O1-
ATOM    695  N   LEU A  94     -26.103  14.505 -19.880  1.00 23.49           N  
ATOM    696  CA  LEU A  94     -26.997  15.587 -20.329  1.00 22.32           C  
ATOM    697  C   LEU A  94     -28.437  15.313 -19.981  1.00 20.94           C  
ATOM    698  O   LEU A  94     -29.226  14.912 -20.827  1.00 22.40           O  
ATOM    699  CB  LEU A  94     -26.909  15.787 -21.837  1.00 24.80           C  
ATOM    700  CG  LEU A  94     -25.659  16.364 -22.395  1.00 24.83           C  
ATOM    701  CD1 LEU A  94     -25.661  16.181 -23.927  1.00 24.63           C  
ATOM    702  CD2 LEU A  94     -25.544  17.809 -21.975  1.00 23.77           C  
ATOM    703  N   ASP A  95     -28.817  15.535 -18.734  1.00 18.41           N  
ATOM    704  CA  ASP A  95     -30.175  15.295 -18.290  1.00 18.77           C  
ATOM    705  C   ASP A  95     -31.072  16.532 -18.352  1.00 24.15           C  
ATOM    706  O   ASP A  95     -32.226  16.526 -17.948  1.00 20.30           O  
ATOM    707  CB  ASP A  95     -30.169  14.846 -16.888  1.00 17.45           C  
ATOM    708  CG  ASP A  95     -29.704  13.426 -16.699  1.00 24.99           C  
ATOM    709  OD1 ASP A  95     -29.880  12.582 -17.559  1.00 21.65           O  
ATOM    710  OD2 ASP A  95     -29.151  13.132 -15.653  1.00 22.05           O1-
ATOM    711  N   ASP A  96     -30.527  17.603 -18.873  1.00 20.70           N  
ATOM    712  CA  ASP A  96     -31.153  18.914 -18.910  1.00 32.92           C  
ATOM    713  C   ASP A  96     -32.520  18.925 -19.601  1.00 36.10           C  
ATOM    714  O   ASP A  96     -33.360  19.740 -19.226  1.00 35.21           O  
ATOM    715  CB  ASP A  96     -30.187  19.870 -19.620  1.00 30.21           C  
ATOM    716  CG  ASP A  96     -28.780  19.909 -19.042  1.00 59.42           C  
ATOM    717  OD1 ASP A  96     -27.939  19.034 -19.321  1.00 30.49           O  
ATOM    718  OD2 ASP A  96     -28.557  20.843 -18.284  1.00 41.87           O1-
ATOM    719  N   ARG A  97     -32.809  18.073 -20.596  1.00 26.01           N  
ATOM    720  CA  ARG A  97     -34.082  18.051 -21.308  1.00 19.44           C  
ATOM    721  C   ARG A  97     -34.932  16.863 -20.943  1.00 21.06           C  
ATOM    722  O   ARG A  97     -35.931  16.557 -21.613  1.00 27.98           O  
ATOM    723  CB  ARG A  97     -33.799  18.077 -22.819  1.00 19.30           C  
ATOM    724  CG  ARG A  97     -33.157  19.347 -23.360  1.00 23.19           C  
ATOM    725  CD  ARG A  97     -34.107  20.549 -23.211  1.00 30.26           C  
ATOM    726  NE  ARG A  97     -33.431  21.742 -23.683  1.00 30.05           N  
ATOM    727  CZ  ARG A  97     -32.821  22.635 -22.874  1.00 29.77           C  
ATOM    728  NH1 ARG A  97     -32.836  22.491 -21.554  1.00 40.21           N1+
ATOM    729  NH2 ARG A  97     -32.070  23.636 -23.374  1.00 29.73           N  
ATOM    730  N   GLY A  98     -34.588  16.154 -19.866  1.00 22.17           N  
ATOM    731  CA  GLY A  98     -35.319  14.954 -19.451  1.00 19.78           C  
ATOM    732  C   GLY A  98     -34.377  13.847 -18.938  1.00 21.06           C  
ATOM    733  O   GLY A  98     -34.637  13.186 -17.922  1.00 26.48           O  
ATOM    734  N   GLY A  99     -33.341  13.639 -19.752  1.00 26.61           N  
ATOM    735  CA  GLY A  99     -32.268  12.730 -19.409  1.00 26.18           C  
ATOM    736  C   GLY A  99     -32.535  11.267 -19.649  1.00 24.45           C  
ATOM    737  O   GLY A  99     -33.605  10.822 -20.054  1.00 23.54           O  
ATOM    738  N   ASN A 100     -31.545  10.461 -19.330  1.00 25.90           N  
ATOM    739  CA  ASN A 100     -31.576   9.019 -19.607  1.00 19.24           C  
ATOM    740  C   ASN A 100     -32.182   8.246 -18.474  1.00 19.02           C  
ATOM    741  O   ASN A 100     -32.460   7.063 -18.586  1.00 22.88           O  
ATOM    742  CB  ASN A 100     -30.129   8.552 -19.859  1.00 23.30           C  
ATOM    743  CG  ASN A 100     -29.256   8.690 -18.619  1.00 22.39           C  
ATOM    744  ND2 ASN A 100     -28.747   7.587 -18.094  1.00 21.36           N  
ATOM    745  OD1 ASN A 100     -29.044   9.776 -18.075  1.00 24.51           O  
ATOM    746  N   ASP A 101     -32.378   8.839 -17.309  1.00 21.84           N  
ATOM    747  CA  ASP A 101     -32.838   8.128 -16.133  1.00 16.59           C  
ATOM    748  C   ASP A 101     -34.236   7.637 -16.273  1.00 26.25           C  
ATOM    749  O   ASP A 101     -35.069   8.332 -16.832  1.00 24.73           O  
ATOM    750  CB  ASP A 101     -32.765   9.033 -14.911  1.00 17.86           C  
ATOM    751  CG  ASP A 101     -31.390   9.662 -14.666  1.00 18.10           C  
ATOM    752  OD1 ASP A 101     -30.593  10.047 -15.557  1.00 23.14           O  
ATOM    753  OD2 ASP A 101     -31.101   9.747 -13.492  1.00 23.00           O1-
ATOM    754  N   ILE A 102     -34.539   6.447 -15.823  1.00 19.76           N  
ATOM    755  CA  ILE A 102     -35.891   5.969 -15.903  1.00 21.70           C  
ATOM    756  C   ILE A 102     -36.657   6.644 -14.751  1.00 22.28           C  
ATOM    757  O   ILE A 102     -36.086   6.809 -13.665  1.00 20.29           O  
ATOM    758  CB  ILE A 102     -35.855   4.392 -15.818  1.00 19.72           C  
ATOM    759  CG1 ILE A 102     -35.335   3.823 -17.150  1.00 25.08           C  
ATOM    760  CG2 ILE A 102     -37.236   3.812 -15.482  1.00 18.10           C  
ATOM    761  CD1 ILE A 102     -35.223   2.260 -17.122  1.00 22.45           C  
ATOM    762  N   PRO A 103     -37.946   7.034 -14.924  1.00 24.84           N  
ATOM    763  CA  PRO A 103     -38.694   7.813 -13.938  1.00 28.04           C  
ATOM    764  C   PRO A 103     -39.266   6.978 -12.825  1.00 25.87           C  
ATOM    765  O   PRO A 103     -40.481   6.743 -12.766  1.00 26.05           O  
ATOM    766  CB  PRO A 103     -39.746   8.540 -14.778  1.00 21.68           C  
ATOM    767  CG  PRO A 103     -40.032   7.577 -15.908  1.00 24.38           C  
ATOM    768  CD  PRO A 103     -38.662   7.009 -16.220  1.00 21.16           C  
ATOM    769  N   TYR A 104     -38.411   6.489 -11.920  1.00 18.31           N  
ATOM    770  CA  TYR A 104     -38.927   5.710 -10.820  1.00 18.73           C  
ATOM    771  C   TYR A 104     -39.589   6.665  -9.836  1.00 20.07           C  
ATOM    772  O   TYR A 104     -39.153   7.799  -9.652  1.00 21.70           O  
ATOM    773  CB  TYR A 104     -37.799   4.920 -10.108  1.00 20.72           C  
ATOM    774  CG  TYR A 104     -37.152   3.915 -11.068  1.00 20.99           C  
ATOM    775  CD1 TYR A 104     -37.806   2.737 -11.352  1.00 23.25           C  
ATOM    776  CD2 TYR A 104     -35.916   4.173 -11.651  1.00 21.35           C  
ATOM    777  CE1 TYR A 104     -37.211   1.830 -12.219  1.00 23.05           C  
ATOM    778  CE2 TYR A 104     -35.325   3.260 -12.513  1.00 18.76           C  
ATOM    779  CZ  TYR A 104     -35.997   2.096 -12.781  1.00 22.33           C  
ATOM    780  OH  TYR A 104     -35.499   1.171 -13.651  1.00 26.62           O  
ATOM    781  N   LEU A 105     -40.648   6.162  -9.217  1.00 19.68           N  
ATOM    782  CA  LEU A 105     -41.398   6.927  -8.246  1.00 27.46           C  
ATOM    783  C   LEU A 105     -40.697   7.039  -6.900  1.00 24.74           C  
ATOM    784  O   LEU A 105     -40.829   8.075  -6.249  1.00 18.69           O  
ATOM    785  CB  LEU A 105     -42.821   6.281  -8.074  1.00 24.81           C  
ATOM    786  CG  LEU A 105     -43.893   6.954  -7.137  1.00 23.54           C  
ATOM    787  CD1 LEU A 105     -44.300   8.301  -7.738  1.00 22.08           C  
ATOM    788  CD2 LEU A 105     -45.111   6.062  -6.990  1.00 19.57           C  
ATOM    789  N   THR A 106     -39.958   6.024  -6.390  1.00 22.99           N  
ATOM    790  CA  THR A 106     -39.420   6.081  -5.029  1.00 22.98           C  
ATOM    791  C   THR A 106     -37.889   5.922  -5.001  1.00 18.20           C  
ATOM    792  O   THR A 106     -37.294   5.649  -6.057  1.00 21.22           O  
ATOM    793  CB  THR A 106     -40.115   4.981  -4.110  1.00 29.35           C  
ATOM    794  CG2 THR A 106     -41.677   5.028  -4.182  1.00 19.42           C  
ATOM    795  OG1 THR A 106     -39.600   3.695  -4.493  1.00 25.92           O  
ATOM    796  N   GLY A 107     -37.275   6.097  -3.814  1.00 17.26           N  
ATOM    797  CA  GLY A 107     -35.847   5.912  -3.573  1.00 18.97           C  
ATOM    798  C   GLY A 107     -35.102   6.968  -4.325  1.00 27.01           C  
ATOM    799  O   GLY A 107     -35.689   7.902  -4.881  1.00 22.34           O  
ATOM    800  N   ASP A 108     -33.787   6.856  -4.265  1.00 18.09           N  
ATOM    801  CA  ASP A 108     -32.895   7.757  -4.969  1.00 14.02           C  
ATOM    802  C   ASP A 108     -33.241   9.237  -4.731  1.00 16.56           C  
ATOM    803  O   ASP A 108     -33.514  10.025  -5.653  1.00 19.46           O  
ATOM    804  CB  ASP A 108     -32.943   7.481  -6.464  1.00 14.02           C  
ATOM    805  CG  ASP A 108     -31.778   8.070  -7.241  1.00 20.04           C  
ATOM    806  OD1 ASP A 108     -30.777   8.462  -6.645  1.00 22.75           O  
ATOM    807  OD2 ASP A 108     -31.822   8.101  -8.479  1.00 21.20           O1-
ATOM    808  N   GLU A 109     -33.283   9.512  -3.420  1.00 18.15           N  
ATOM    809  CA  GLU A 109     -33.454  10.848  -2.857  1.00 24.76           C  
ATOM    810  C   GLU A 109     -34.879  11.412  -2.957  1.00 28.53           C  
ATOM    811  O   GLU A 109     -35.054  12.615  -2.781  1.00 24.18           O  
ATOM    812  CB  GLU A 109     -32.507  11.848  -3.523  1.00 23.74           C  
ATOM    813  CG  GLU A 109     -31.044  11.490  -3.378  1.00 39.02           C  
ATOM    814  CD  GLU A 109     -30.158  12.516  -4.039  1.00 35.83           C  
ATOM    815  OE1 GLU A 109     -30.159  12.564  -5.267  1.00 42.26           O  
ATOM    816  OE2 GLU A 109     -29.504  13.268  -3.314  1.00 50.54           O1-
ATOM    817  N   ARG A 110     -35.921  10.617  -3.217  1.00 23.57           N  
ATOM    818  CA  ARG A 110     -37.325  11.075  -3.165  1.00 25.84           C  
ATOM    819  C   ARG A 110     -37.647  11.548  -1.743  1.00 30.43           C  
ATOM    820  O   ARG A 110     -38.126  12.671  -1.544  1.00 24.85           O  
ATOM    821  CB  ARG A 110     -38.285   9.935  -3.567  1.00 21.39           C  
ATOM    822  CG  ARG A 110     -39.780  10.288  -3.592  1.00 23.85           C  
ATOM    823  CD  ARG A 110     -39.973  11.342  -4.712  1.00 24.89           C  
ATOM    824  NE  ARG A 110     -39.946  10.666  -6.001  1.00 27.06           N  
ATOM    825  CZ  ARG A 110     -39.469  11.144  -7.147  1.00 24.00           C  
ATOM    826  NH1 ARG A 110     -38.955  12.352  -7.183  1.00 34.29           N1+
ATOM    827  NH2 ARG A 110     -39.525  10.442  -8.278  1.00 26.57           N  
ATOM    828  N   LEU A 111     -37.367  10.757  -0.711  1.00 17.88           N  
ATOM    829  CA  LEU A 111     -37.606  11.144   0.656  1.00 18.66           C  
ATOM    830  C   LEU A 111     -36.368  11.184   1.528  1.00 19.35           C  
ATOM    831  O   LEU A 111     -36.429  11.584   2.698  1.00 18.67           O  
ATOM    832  CB  LEU A 111     -38.609  10.191   1.243  1.00 19.31           C  
ATOM    833  CG  LEU A 111     -40.023  10.302   0.713  1.00 24.75           C  
ATOM    834  CD1 LEU A 111     -40.909   9.242   1.271  1.00 28.02           C  
ATOM    835  CD2 LEU A 111     -40.565  11.631   1.150  1.00 33.78           C  
ATOM    836  N   THR A 112     -35.205  10.774   1.004  1.00 18.03           N  
ATOM    837  CA  THR A 112     -33.984  10.718   1.801  1.00 18.21           C  
ATOM    838  C   THR A 112     -33.622  12.145   2.190  1.00 16.40           C  
ATOM    839  O   THR A 112     -33.673  13.027   1.327  1.00 21.37           O  
ATOM    840  CB  THR A 112     -32.847  10.092   0.958  1.00 20.52           C  
ATOM    841  CG2 THR A 112     -31.636   9.738   1.792  1.00 16.54           C  
ATOM    842  OG1 THR A 112     -33.434   8.972   0.297  1.00 21.48           O  
ATOM    843  N   ALA A 113     -33.205  12.414   3.418  1.00 17.64           N  
ATOM    844  CA  ALA A 113     -32.883  13.760   3.849  1.00 22.16           C  
ATOM    845  C   ALA A 113     -32.027  13.684   5.100  1.00 23.20           C  
ATOM    846  O   ALA A 113     -31.757  12.580   5.593  1.00 21.50           O  
ATOM    847  CB  ALA A 113     -34.201  14.500   4.160  1.00 20.45           C  
ATOM    848  N   GLU A 114     -31.642  14.848   5.648  1.00 17.56           N  
ATOM    849  CA  GLU A 114     -30.848  14.914   6.840  1.00 17.62           C  
ATOM    850  C   GLU A 114     -31.506  14.105   7.923  1.00 20.21           C  
ATOM    851  O   GLU A 114     -32.718  14.149   8.107  1.00 19.38           O  
ATOM    852  CB  GLU A 114     -30.716  16.362   7.213  1.00 21.43           C  
ATOM    853  CG  GLU A 114     -29.928  16.510   8.510  1.00 31.92           C  
ATOM    854  CD  GLU A 114     -29.518  17.922   8.956  1.00 50.58           C  
ATOM    855  OE1 GLU A 114     -29.977  18.896   8.367  1.00 58.25           O  
ATOM    856  OE2 GLU A 114     -28.729  18.045   9.899  1.00 57.25           O1-
ATOM    857  N   ASP A 115     -30.741  13.230   8.572  1.00 18.34           N  
ATOM    858  CA  ASP A 115     -31.224  12.319   9.610  1.00 18.30           C  
ATOM    859  C   ASP A 115     -32.344  11.400   9.189  1.00 14.16           C  
ATOM    860  O   ASP A 115     -33.156  10.894   9.989  1.00 18.02           O  
ATOM    861  CB  ASP A 115     -31.734  13.071  10.833  1.00 19.01           C  
ATOM    862  CG  ASP A 115     -30.720  13.874  11.591  1.00 25.40           C  
ATOM    863  OD1 ASP A 115     -29.531  13.539  11.568  1.00 28.95           O  
ATOM    864  OD2 ASP A 115     -31.132  14.831  12.234  1.00 32.28           O1-
ATOM    865  N   ASN A 116     -32.409  11.168   7.885  1.00 16.08           N  
ATOM    866  CA  ASN A 116     -33.500  10.377   7.392  1.00 21.18           C  
ATOM    867  C   ASN A 116     -32.997   9.488   6.249  1.00 17.53           C  
ATOM    868  O   ASN A 116     -33.206   9.761   5.058  1.00 18.38           O  
ATOM    869  CB  ASN A 116     -34.663  11.320   6.942  1.00 13.57           C  
ATOM    870  CG  ASN A 116     -35.914  10.463   6.803  1.00 13.13           C  
ATOM    871  ND2 ASN A 116     -36.435  10.477   5.565  1.00 17.70           N  
ATOM    872  OD1 ASN A 116     -36.420   9.805   7.771  1.00 22.25           O  
ATOM    873  N   PRO A 117     -32.305   8.374   6.574  1.00 19.89           N  
ATOM    874  CA  PRO A 117     -31.916   7.383   5.585  1.00 22.27           C  
ATOM    875  C   PRO A 117     -33.106   6.544   5.118  1.00 18.54           C  
ATOM    876  O   PRO A 117     -34.104   6.432   5.847  1.00 18.89           O  
ATOM    877  CB  PRO A 117     -30.835   6.597   6.320  1.00 15.27           C  
ATOM    878  CG  PRO A 117     -31.323   6.585   7.753  1.00 17.83           C  
ATOM    879  CD  PRO A 117     -31.841   8.011   7.911  1.00 17.26           C  
ATOM    880  N   VAL A 118     -33.045   5.917   3.927  1.00 16.16           N  
ATOM    881  CA  VAL A 118     -34.054   4.940   3.505  1.00 16.43           C  
ATOM    882  C   VAL A 118     -33.377   3.536   3.483  1.00 25.34           C  
ATOM    883  O   VAL A 118     -32.145   3.421   3.622  1.00 19.32           O  
ATOM    884  CB  VAL A 118     -34.672   5.312   2.078  1.00 18.45           C  
ATOM    885  CG1 VAL A 118     -35.372   6.692   2.357  1.00 15.26           C  
ATOM    886  CG2 VAL A 118     -33.715   5.515   0.884  1.00 15.58           C  
ATOM    887  N   LEU A 119     -34.145   2.468   3.320  1.00 20.33           N  
ATOM    888  CA  LEU A 119     -33.699   1.076   3.389  1.00 20.99           C  
ATOM    889  C   LEU A 119     -33.814   0.307   2.084  1.00 20.18           C  
ATOM    890  O   LEU A 119     -34.822   0.444   1.376  1.00 19.36           O  
ATOM    891  CB  LEU A 119     -34.526   0.430   4.468  1.00 19.83           C  
ATOM    892  CG  LEU A 119     -34.161  -0.964   4.817  1.00 29.38           C  
ATOM    893  CD1 LEU A 119     -32.950  -0.904   5.703  1.00 33.62           C  
ATOM    894  CD2 LEU A 119     -35.271  -1.619   5.557  1.00 28.54           C  
ATOM    895  N   LEU A 120     -32.870  -0.532   1.647  1.00 16.23           N  
ATOM    896  CA  LEU A 120     -33.037  -1.311   0.421  1.00 12.16           C  
ATOM    897  C   LEU A 120     -32.598  -2.720   0.785  1.00 23.81           C  
ATOM    898  O   LEU A 120     -31.553  -2.894   1.408  1.00 18.46           O  
ATOM    899  CB  LEU A 120     -32.147  -0.840  -0.694  1.00 14.54           C  
ATOM    900  CG  LEU A 120     -32.052  -1.680  -1.943  1.00 17.59           C  
ATOM    901  CD1 LEU A 120     -33.420  -1.795  -2.596  1.00 20.38           C  
ATOM    902  CD2 LEU A 120     -31.053  -1.035  -2.909  1.00 15.97           C  
ATOM    903  N   TYR A 121     -33.399  -3.712   0.501  1.00 22.12           N  
ATOM    904  CA  TYR A 121     -33.054  -5.096   0.759  1.00 23.52           C  
ATOM    905  C   TYR A 121     -32.923  -5.765  -0.600  1.00 22.86           C  
ATOM    906  O   TYR A 121     -33.825  -5.568  -1.422  1.00 23.27           O  
ATOM    907  CB  TYR A 121     -34.150  -5.767   1.572  1.00 22.24           C  
ATOM    908  CG  TYR A 121     -34.021  -7.288   1.580  1.00 25.99           C  
ATOM    909  CD1 TYR A 121     -33.042  -7.924   2.331  1.00 34.91           C  
ATOM    910  CD2 TYR A 121     -34.874  -8.002   0.768  1.00 26.29           C  
ATOM    911  CE1 TYR A 121     -32.927  -9.292   2.252  1.00 27.38           C  
ATOM    912  CE2 TYR A 121     -34.766  -9.366   0.677  1.00 35.27           C  
ATOM    913  CZ  TYR A 121     -33.794  -9.994   1.419  1.00 36.17           C  
ATOM    914  OH  TYR A 121     -33.706 -11.368   1.293  1.00 35.43           O  
ATOM    915  N   THR A 122     -31.858  -6.555  -0.898  1.00 22.81           N  
ATOM    916  CA  THR A 122     -31.776  -7.285  -2.150  1.00 19.32           C  
ATOM    917  C   THR A 122     -31.355  -8.719  -1.824  1.00 27.70           C  
ATOM    918  O   THR A 122     -30.737  -9.002  -0.781  1.00 21.98           O  
ATOM    919  CB  THR A 122     -30.757  -6.678  -3.095  1.00 21.37           C  
ATOM    920  CG2 THR A 122     -31.216  -5.392  -3.762  1.00 29.49           C  
ATOM    921  OG1 THR A 122     -29.630  -6.393  -2.287  1.00 27.26           O  
ATOM    922  N   TYR A 123     -31.714  -9.579  -2.757  1.00 26.58           N  
ATOM    923  CA  TYR A 123     -31.406 -10.993  -2.654  1.00 28.58           C  
ATOM    924  C   TYR A 123     -31.366 -11.625  -4.020  1.00 30.09           C  
ATOM    925  O   TYR A 123     -32.253 -11.389  -4.840  1.00 26.30           O  
ATOM    926  CB  TYR A 123     -32.464 -11.659  -1.842  1.00 29.46           C  
ATOM    927  CG  TYR A 123     -32.310 -13.165  -1.772  1.00 31.07           C  
ATOM    928  CD1 TYR A 123     -31.451 -13.662  -0.822  1.00 39.10           C  
ATOM    929  CD2 TYR A 123     -33.018 -13.972  -2.641  1.00 34.75           C  
ATOM    930  CE1 TYR A 123     -31.281 -15.015  -0.720  1.00 35.87           C  
ATOM    931  CE2 TYR A 123     -32.856 -15.327  -2.551  1.00 42.57           C  
ATOM    932  CZ  TYR A 123     -31.989 -15.821  -1.591  1.00 47.35           C  
ATOM    933  OH  TYR A 123     -31.806 -17.182  -1.483  1.00 53.04           O  
ATOM    934  N   SER A 124     -30.382 -12.467  -4.289  1.00 29.07           N  
ATOM    935  CA  SER A 124     -30.397 -13.178  -5.538  1.00 25.74           C  
ATOM    936  C   SER A 124     -30.058 -14.637  -5.247  1.00 32.52           C  
ATOM    937  O   SER A 124     -29.398 -14.959  -4.255  1.00 28.10           O  
ATOM    938  CB  SER A 124     -29.370 -12.670  -6.481  1.00 29.36           C  
ATOM    939  OG  SER A 124     -29.539 -11.305  -6.761  1.00 40.97           O  
ATOM    940  N   ALA A 125     -30.533 -15.520  -6.092  1.00 38.12           N  
ATOM    941  CA  ALA A 125     -30.231 -16.928  -5.998  1.00 28.40           C  
ATOM    942  C   ALA A 125     -30.305 -17.375  -7.444  1.00 30.58           C  
ATOM    943  O   ALA A 125     -31.377 -17.327  -8.062  1.00 39.26           O  
ATOM    944  CB  ALA A 125     -31.291 -17.604  -5.187  1.00 24.99           C  
ATOM    945  N   GLY A 126     -29.195 -17.730  -8.069  1.00 37.02           N  
ATOM    946  CA  GLY A 126     -29.242 -18.206  -9.430  1.00 31.57           C  
ATOM    947  C   GLY A 126     -29.674 -17.155 -10.430  1.00 47.32           C  
ATOM    948  O   GLY A 126     -29.047 -16.114 -10.641  1.00 45.65           O  
ATOM    949  N   ALA A 127     -30.776 -17.480 -11.075  1.00 33.24           N  
ATOM    950  CA  ALA A 127     -31.322 -16.656 -12.138  1.00 42.64           C  
ATOM    951  C   ALA A 127     -32.292 -15.558 -11.679  1.00 33.08           C  
ATOM    952  O   ALA A 127     -32.759 -14.700 -12.437  1.00 40.51           O  
ATOM    953  CB  ALA A 127     -32.032 -17.592 -13.094  1.00 35.42           C  
ATOM    954  N   PHE A 128     -32.604 -15.563 -10.416  1.00 27.81           N  
ATOM    955  CA  PHE A 128     -33.654 -14.745  -9.952  1.00 28.97           C  
ATOM    956  C   PHE A 128     -33.137 -13.725  -8.966  1.00 40.19           C  
ATOM    957  O   PHE A 128     -32.252 -14.010  -8.153  1.00 29.96           O  
ATOM    958  CB  PHE A 128     -34.577 -15.770  -9.428  1.00 27.26           C  
ATOM    959  CG  PHE A 128     -35.661 -15.233  -8.530  1.00 62.21           C  
ATOM    960  CD1 PHE A 128     -36.832 -14.760  -9.102  1.00 68.83           C  
ATOM    961  CD2 PHE A 128     -35.467 -15.240  -7.145  1.00 68.66           C  
ATOM    962  CE1 PHE A 128     -37.823 -14.287  -8.261  1.00 68.63           C  
ATOM    963  CE2 PHE A 128     -36.462 -14.766  -6.312  1.00 72.56           C  
ATOM    964  CZ  PHE A 128     -37.638 -14.294  -6.881  1.00 71.50           C  
ATOM    965  N   SER A 129     -33.760 -12.552  -9.012  1.00 32.05           N  
ATOM    966  CA  SER A 129     -33.441 -11.480  -8.078  1.00 30.97           C  
ATOM    967  C   SER A 129     -34.691 -10.806  -7.532  1.00 26.59           C  
ATOM    968  O   SER A 129     -35.671 -10.668  -8.269  1.00 27.36           O  
ATOM    969  CB  SER A 129     -32.608 -10.425  -8.756  1.00 27.55           C  
ATOM    970  OG  SER A 129     -31.372 -10.889  -9.272  1.00 47.00           O  
ATOM    971  N   VAL A 130     -34.713 -10.468  -6.254  1.00 28.17           N  
ATOM    972  CA  VAL A 130     -35.790  -9.694  -5.670  1.00 29.20           C  
ATOM    973  C   VAL A 130     -35.239  -8.520  -4.876  1.00 40.17           C  
ATOM    974  O   VAL A 130     -34.133  -8.597  -4.323  1.00 25.40           O  
ATOM    975  CB  VAL A 130     -36.639 -10.480  -4.718  1.00 24.69           C  
ATOM    976  CG1 VAL A 130     -37.489 -11.322  -5.586  1.00 34.50           C  
ATOM    977  CG2 VAL A 130     -35.834 -11.241  -3.698  1.00 27.14           C  
ATOM    978  N   ALA A 131     -35.974  -7.408  -4.812  1.00 24.58           N  
ATOM    979  CA  ALA A 131     -35.555  -6.233  -4.032  1.00 21.75           C  
ATOM    980  C   ALA A 131     -36.779  -5.647  -3.311  1.00 27.70           C  
ATOM    981  O   ALA A 131     -37.932  -5.843  -3.759  1.00 27.02           O  
ATOM    982  CB  ALA A 131     -34.928  -5.203  -4.988  1.00 16.82           C  
ATOM    983  N   ALA A 132     -36.609  -5.029  -2.153  1.00 24.98           N  
ATOM    984  CA  ALA A 132     -37.720  -4.419  -1.437  1.00 25.03           C  
ATOM    985  C   ALA A 132     -37.164  -3.185  -0.749  1.00 34.14           C  
ATOM    986  O   ALA A 132     -36.039  -3.213  -0.250  1.00 20.34           O  
ATOM    987  CB  ALA A 132     -38.275  -5.386  -0.390  1.00 23.74           C  
ATOM    988  N   SER A 133     -37.861  -2.059  -0.724  1.00 21.23           N  
ATOM    989  CA  SER A 133     -37.326  -0.844  -0.125  1.00 18.46           C  
ATOM    990  C   SER A 133     -38.413  -0.069   0.634  1.00 24.03           C  
ATOM    991  O   SER A 133     -39.604  -0.284   0.363  1.00 22.23           O  
ATOM    992  CB  SER A 133     -36.759   0.003  -1.225  1.00 14.79           C  
ATOM    993  OG  SER A 133     -37.649   0.084  -2.338  1.00 19.72           O  
ATOM    994  N   MET A 134     -38.097   0.791   1.588  1.00 22.25           N  
ATOM    995  CA  MET A 134     -39.106   1.605   2.255  1.00 21.58           C  
ATOM    996  C   MET A 134     -38.447   2.746   3.000  1.00 33.98           C  
ATOM    997  O   MET A 134     -37.238   2.661   3.276  1.00 19.01           O  
ATOM    998  CB  MET A 134     -39.885   0.747   3.234  1.00 18.41           C  
ATOM    999  CG  MET A 134     -39.041   0.297   4.421  1.00 25.36           C  
ATOM   1000  SD  MET A 134     -39.949  -0.692   5.625  1.00 35.96           S  
ATOM   1001  CE  MET A 134     -41.094   0.500   6.257  1.00 37.35           C  
ATOM   1002  N   SER A 135     -39.171   3.827   3.290  1.00 18.02           N  
ATOM   1003  CA  SER A 135     -38.647   4.886   4.126  1.00 16.76           C  
ATOM   1004  C   SER A 135     -39.355   4.663   5.440  1.00 16.94           C  
ATOM   1005  O   SER A 135     -40.247   3.813   5.524  1.00 20.09           O  
ATOM   1006  CB  SER A 135     -38.965   6.268   3.529  1.00 20.02           C  
ATOM   1007  OG  SER A 135     -40.363   6.467   3.320  1.00 20.86           O  
ATOM   1008  N   ASP A 136     -39.029   5.367   6.506  1.00 16.31           N  
ATOM   1009  CA  ASP A 136     -39.628   5.052   7.767  1.00 16.45           C  
ATOM   1010  C   ASP A 136     -40.905   5.854   8.100  1.00 22.62           C  
ATOM   1011  O   ASP A 136     -41.434   5.627   9.194  1.00 22.11           O  
ATOM   1012  CB  ASP A 136     -38.583   5.262   8.860  1.00 18.28           C  
ATOM   1013  CG  ASP A 136     -38.030   6.657   9.077  1.00 26.65           C  
ATOM   1014  OD1 ASP A 136     -38.602   7.695   8.739  1.00 23.99           O  
ATOM   1015  OD2 ASP A 136     -36.946   6.791   9.634  1.00 20.64           O1-
ATOM   1016  N   GLY A 137     -41.396   6.822   7.294  1.00 24.48           N  
ATOM   1017  CA  GLY A 137     -42.645   7.546   7.582  1.00 23.91           C  
ATOM   1018  C   GLY A 137     -42.531   8.722   8.540  1.00 26.85           C  
ATOM   1019  O   GLY A 137     -43.553   9.346   8.814  1.00 25.96           O  
ATOM   1020  N   LYS A 138     -41.379   9.104   9.087  1.00 17.66           N  
ATOM   1021  CA  LYS A 138     -41.241  10.215  10.008  1.00 18.17           C  
ATOM   1022  C   LYS A 138     -40.138  11.120   9.553  1.00 30.18           C  
ATOM   1023  O   LYS A 138     -39.053  10.663   9.147  1.00 21.24           O  
ATOM   1024  CB  LYS A 138     -40.879   9.803  11.420  1.00 16.38           C  
ATOM   1025  CG  LYS A 138     -41.855   8.815  12.009  1.00 23.82           C  
ATOM   1026  CD  LYS A 138     -43.165   9.521  12.149  1.00 27.64           C  
ATOM   1027  CE  LYS A 138     -44.223   8.643  12.729  1.00 44.82           C  
ATOM   1028  NZ  LYS A 138     -45.057   9.513  13.538  1.00 46.52           N1+
ATOM   1029  N   VAL A 139     -40.377  12.414   9.622  1.00 18.51           N  
ATOM   1030  CA  VAL A 139     -39.436  13.415   9.194  1.00 17.22           C  
ATOM   1031  C   VAL A 139     -38.186  13.330  10.027  1.00 17.48           C  
ATOM   1032  O   VAL A 139     -38.328  13.224  11.243  1.00 19.74           O  
ATOM   1033  CB  VAL A 139     -40.022  14.829   9.347  1.00 22.74           C  
ATOM   1034  CG1 VAL A 139     -39.006  15.865   8.910  1.00 20.52           C  
ATOM   1035  CG2 VAL A 139     -41.197  14.985   8.410  1.00 19.66           C  
ATOM   1036  N   GLY A 140     -36.978  13.361   9.436  1.00 20.23           N  
ATOM   1037  CA  GLY A 140     -35.744  13.246  10.208  1.00 18.19           C  
ATOM   1038  C   GLY A 140     -35.835  12.033  11.134  1.00 15.63           C  
ATOM   1039  O   GLY A 140     -36.387  10.956  10.776  1.00 24.74           O  
ATOM   1040  N   GLU A 141     -35.368  12.282  12.355  1.00 20.17           N  
ATOM   1041  CA  GLU A 141     -35.478  11.319  13.437  1.00 22.48           C  
ATOM   1042  C   GLU A 141     -36.503  11.857  14.413  1.00 27.63           C  
ATOM   1043  O   GLU A 141     -36.416  11.611  15.619  1.00 24.54           O  
ATOM   1044  CB  GLU A 141     -34.129  11.149  14.145  1.00 23.70           C  
ATOM   1045  CG  GLU A 141     -33.235  10.176  13.339  1.00 28.35           C  
ATOM   1046  CD  GLU A 141     -31.745  10.105  13.707  1.00 35.14           C  
ATOM   1047  OE1 GLU A 141     -31.311  10.576  14.759  1.00 29.71           O  
ATOM   1048  OE2 GLU A 141     -30.980   9.583  12.903  1.00 26.87           O1-
ATOM   1049  N   THR A 142     -37.507  12.567  13.890  1.00 24.87           N  
ATOM   1050  CA  THR A 142     -38.512  13.180  14.735  1.00 26.14           C  
ATOM   1051  C   THR A 142     -39.750  12.314  14.745  1.00 26.00           C  
ATOM   1052  O   THR A 142     -39.792  11.238  14.151  1.00 26.49           O  
ATOM   1053  CB  THR A 142     -38.891  14.624  14.229  1.00 22.12           C  
ATOM   1054  CG2 THR A 142     -37.628  15.454  14.009  1.00 22.33           C  
ATOM   1055  OG1 THR A 142     -39.767  14.511  13.083  1.00 23.47           O  
ATOM   1056  N   SER A 143     -40.804  12.764  15.426  1.00 25.41           N  
ATOM   1057  CA  SER A 143     -42.069  12.080  15.355  1.00 24.21           C  
ATOM   1058  C   SER A 143     -43.021  12.722  14.349  1.00 29.13           C  
ATOM   1059  O   SER A 143     -44.165  12.261  14.245  1.00 29.64           O  
ATOM   1060  CB  SER A 143     -42.696  12.069  16.728  1.00 30.36           C  
ATOM   1061  OG  SER A 143     -41.950  11.241  17.604  1.00 34.01           O  
ATOM   1062  N   GLU A 144     -42.610  13.721  13.554  1.00 25.37           N  
ATOM   1063  CA  GLU A 144     -43.531  14.321  12.601  1.00 23.57           C  
ATOM   1064  C   GLU A 144     -43.805  13.389  11.428  1.00 32.22           C  
ATOM   1065  O   GLU A 144     -42.848  12.879  10.835  1.00 26.96           O  
ATOM   1066  CB  GLU A 144     -42.910  15.643  12.147  1.00 30.98           C  
ATOM   1067  CG  GLU A 144     -43.902  16.538  11.387  1.00 55.43           C  
ATOM   1068  CD  GLU A 144     -43.343  17.703  10.557  1.00 68.87           C  
ATOM   1069  OE1 GLU A 144     -42.265  18.217  10.873  1.00 57.51           O  
ATOM   1070  OE2 GLU A 144     -44.001  18.095   9.582  1.00 82.75           O1-
ATOM   1071  N   ASP A 145     -45.067  13.151  11.069  1.00 24.45           N  
ATOM   1072  CA  ASP A 145     -45.433  12.267   9.979  1.00 23.62           C  
ATOM   1073  C   ASP A 145     -44.975  12.750   8.651  1.00 31.40           C  
ATOM   1074  O   ASP A 145     -45.089  13.940   8.353  1.00 27.58           O  
ATOM   1075  CB  ASP A 145     -46.932  12.062   9.830  1.00 27.22           C  
ATOM   1076  CG  ASP A 145     -47.592  11.206  10.918  1.00 43.72           C  
ATOM   1077  OD1 ASP A 145     -46.989  10.238  11.378  1.00 55.35           O  
ATOM   1078  OD2 ASP A 145     -48.732  11.488  11.292  1.00 70.49           O1-
ATOM   1079  N   ASP A 146     -44.468  11.824   7.840  1.00 23.66           N  
ATOM   1080  CA  ASP A 146     -43.935  12.175   6.537  1.00 18.81           C  
ATOM   1081  C   ASP A 146     -44.694  11.309   5.568  1.00 10.77           C  
ATOM   1082  O   ASP A 146     -45.453  10.415   5.949  1.00 22.23           O  
ATOM   1083  CB  ASP A 146     -42.388  11.869   6.493  1.00 21.54           C  
ATOM   1084  CG  ASP A 146     -41.576  12.595   5.422  1.00 31.62           C  
ATOM   1085  OD1 ASP A 146     -42.155  13.265   4.571  1.00 34.30           O  
ATOM   1086  OD2 ASP A 146     -40.350  12.524   5.414  1.00 26.76           O1-
ATOM   1087  N   ALA A 147     -44.578  11.606   4.268  1.00 16.46           N  
ATOM   1088  CA  ALA A 147     -45.027  10.671   3.233  1.00 23.36           C  
ATOM   1089  C   ALA A 147     -44.169   9.397   3.415  1.00 25.54           C  
ATOM   1090  O   ALA A 147     -43.045   9.505   3.934  1.00 21.29           O  
ATOM   1091  CB  ALA A 147     -44.744  11.220   1.844  1.00 18.36           C  
ATOM   1092  N   GLN A 148     -44.623   8.218   3.060  1.00 20.67           N  
ATOM   1093  CA  GLN A 148     -43.792   7.049   3.249  1.00 21.13           C  
ATOM   1094  C   GLN A 148     -43.707   6.326   1.940  1.00 28.17           C  
ATOM   1095  O   GLN A 148     -44.761   6.116   1.342  1.00 24.20           O  
ATOM   1096  CB  GLN A 148     -44.420   6.218   4.267  1.00 21.13           C  
ATOM   1097  CG  GLN A 148     -43.564   4.994   4.464  1.00 25.80           C  
ATOM   1098  CD  GLN A 148     -44.012   4.201   5.654  1.00 34.87           C  
ATOM   1099  NE2 GLN A 148     -45.265   4.264   6.089  1.00 47.02           N  
ATOM   1100  OE1 GLN A 148     -43.210   3.535   6.299  1.00 38.87           O  
ATOM   1101  N   GLU A 149     -42.525   5.936   1.454  1.00 17.81           N  
ATOM   1102  CA  GLU A 149     -42.440   5.268   0.168  1.00 17.51           C  
ATOM   1103  C   GLU A 149     -42.131   3.801   0.405  1.00 20.63           C  
ATOM   1104  O   GLU A 149     -41.650   3.464   1.502  1.00 18.55           O  
ATOM   1105  CB  GLU A 149     -41.353   5.852  -0.694  1.00 19.12           C  
ATOM   1106  CG  GLU A 149     -39.971   5.844  -0.028  1.00 18.36           C  
ATOM   1107  CD  GLU A 149     -38.868   6.533  -0.793  1.00 20.39           C  
ATOM   1108  OE1 GLU A 149     -39.126   7.138  -1.838  1.00 21.55           O  
ATOM   1109  OE2 GLU A 149     -37.729   6.472  -0.316  1.00 21.49           O1-
ATOM   1110  N   MET A 150     -42.460   2.983  -0.586  1.00 18.17           N  
ATOM   1111  CA  MET A 150     -42.210   1.533  -0.532  1.00 20.14           C  
ATOM   1112  C   MET A 150     -42.192   0.996  -1.930  1.00 28.58           C  
ATOM   1113  O   MET A 150     -42.900   1.507  -2.797  1.00 27.20           O  
ATOM   1114  CB  MET A 150     -43.287   0.712   0.123  1.00 27.78           C  
ATOM   1115  CG  MET A 150     -43.453   0.910   1.586  1.00 64.16           C  
ATOM   1116  SD  MET A 150     -45.203   0.695   1.972  1.00 78.93           S  
ATOM   1117  CE  MET A 150     -44.967   0.632   3.732  1.00 70.32           C  
ATOM   1118  N   ALA A 151     -41.438  -0.063  -2.208  1.00 21.76           N  
ATOM   1119  CA  ALA A 151     -41.444  -0.665  -3.531  1.00 22.34           C  
ATOM   1120  C   ALA A 151     -40.965  -2.112  -3.374  1.00 22.98           C  
ATOM   1121  O   ALA A 151     -40.352  -2.489  -2.343  1.00 20.23           O  
ATOM   1122  CB  ALA A 151     -40.499   0.042  -4.471  1.00 15.31           C  
ATOM   1123  N   VAL A 152     -41.360  -2.920  -4.337  1.00 21.53           N  
ATOM   1124  CA  VAL A 152     -40.965  -4.321  -4.382  1.00 23.07           C  
ATOM   1125  C   VAL A 152     -40.692  -4.577  -5.874  1.00 29.71           C  
ATOM   1126  O   VAL A 152     -41.323  -3.966  -6.752  1.00 27.21           O  
ATOM   1127  CB  VAL A 152     -42.115  -5.287  -3.786  1.00 25.13           C  
ATOM   1128  CG1AVAL A 152     -42.356  -4.980  -2.314  0.53 28.48           C  
ATOM   1129  CG2AVAL A 152     -43.411  -5.128  -4.563  0.53 23.43           C  
ATOM   1130  CG1BVAL A 152     -41.654  -6.731  -3.914  0.26 24.20           C  
ATOM   1131  CG2BVAL A 152     -42.404  -5.002  -2.319  0.26 29.11           C  
ATOM   1132  CG1CVAL A 152     -43.404  -5.208  -4.593  0.21 26.31           C  
ATOM   1133  CG2CVAL A 152     -41.578  -6.708  -3.756  0.21 24.18           C  
ATOM   1134  N   ALA A 153     -39.700  -5.400  -6.242  1.00 27.54           N  
ATOM   1135  CA  ALA A 153     -39.434  -5.715  -7.643  1.00 23.02           C  
ATOM   1136  C   ALA A 153     -38.821  -7.126  -7.736  1.00 25.00           C  
ATOM   1137  O   ALA A 153     -38.202  -7.592  -6.762  1.00 23.08           O  
ATOM   1138  CB  ALA A 153     -38.460  -4.696  -8.229  1.00 20.58           C  
ATOM   1139  N   ALA A 154     -38.992  -7.822  -8.845  1.00 25.22           N  
ATOM   1140  CA  ALA A 154     -38.408  -9.145  -9.037  1.00 31.60           C  
ATOM   1141  C   ALA A 154     -37.923  -9.223 -10.446  1.00 28.50           C  
ATOM   1142  O   ALA A 154     -38.463  -8.553 -11.323  1.00 28.42           O  
ATOM   1143  CB  ALA A 154     -39.410 -10.231  -8.852  1.00 24.29           C  
ATOM   1144  N   ALA A 155     -36.863  -9.964 -10.737  1.00 26.24           N  
ATOM   1145  CA  ALA A 155     -36.374 -10.092 -12.094  1.00 31.59           C  
ATOM   1146  C   ALA A 155     -35.916 -11.544 -12.283  1.00 32.78           C  
ATOM   1147  O   ALA A 155     -35.635 -12.284 -11.333  1.00 27.08           O  
ATOM   1148  CB  ALA A 155     -35.163  -9.188 -12.355  1.00 29.48           C  
ATOM   1149  N   TYR A 156     -35.867 -11.930 -13.533  1.00 27.28           N  
ATOM   1150  CA  TYR A 156     -35.442 -13.242 -13.927  1.00 27.65           C  
ATOM   1151  C   TYR A 156     -34.610 -13.137 -15.202  1.00 25.30           C  
ATOM   1152  O   TYR A 156     -34.991 -12.539 -16.217  1.00 31.37           O  
ATOM   1153  CB  TYR A 156     -36.705 -14.081 -14.102  1.00 40.64           C  
ATOM   1154  CG  TYR A 156     -36.389 -15.511 -14.536  1.00 72.25           C  
ATOM   1155  CD1 TYR A 156     -35.757 -16.378 -13.652  1.00 68.07           C  
ATOM   1156  CD2 TYR A 156     -36.697 -15.913 -15.838  1.00 78.75           C  
ATOM   1157  CE1 TYR A 156     -35.427 -17.648 -14.087  1.00 70.03           C  
ATOM   1158  CE2 TYR A 156     -36.371 -17.185 -16.273  1.00 76.52           C  
ATOM   1159  CZ  TYR A 156     -35.733 -18.038 -15.387  1.00 81.42           C  
ATOM   1160  OH  TYR A 156     -35.379 -19.309 -15.810  1.00 98.25           O  
ATOM   1161  N   THR A 157     -33.410 -13.701 -15.144  1.00 33.54           N  
ATOM   1162  CA  THR A 157     -32.553 -13.720 -16.302  1.00 41.02           C  
ATOM   1163  C   THR A 157     -32.621 -15.096 -16.973  1.00 45.31           C  
ATOM   1164  O   THR A 157     -32.578 -16.121 -16.295  1.00 47.36           O  
ATOM   1165  CB  THR A 157     -31.145 -13.393 -15.847  1.00 31.49           C  
ATOM   1166  CG2 THR A 157     -30.192 -13.175 -17.021  1.00 34.86           C  
ATOM   1167  OG1 THR A 157     -31.253 -12.205 -15.063  1.00 47.00           O  
ATOM   1168  N   PHE A 158     -32.792 -15.168 -18.285  1.00 40.52           N  
ATOM   1169  CA  PHE A 158     -32.794 -16.383 -19.068  1.00 46.68           C  
ATOM   1170  C   PHE A 158     -32.058 -16.040 -20.348  1.00 44.70           C  
ATOM   1171  O   PHE A 158     -32.472 -15.331 -21.273  1.00 50.08           O  
ATOM   1172  CB  PHE A 158     -34.228 -16.854 -19.365  1.00 40.11           C  
ATOM   1173  CG  PHE A 158     -35.205 -15.881 -20.021  1.00 60.39           C  
ATOM   1174  CD1 PHE A 158     -35.813 -14.886 -19.269  1.00 73.87           C  
ATOM   1175  CD2 PHE A 158     -35.491 -15.999 -21.378  1.00 75.24           C  
ATOM   1176  CE1 PHE A 158     -36.695 -14.018 -19.876  1.00 73.60           C  
ATOM   1177  CE2 PHE A 158     -36.380 -15.122 -21.977  1.00 79.76           C  
ATOM   1178  CZ  PHE A 158     -36.979 -14.133 -21.224  1.00 79.46           C  
ATOM   1179  N   GLY A 159     -30.814 -16.458 -20.289  1.00 54.47           N  
ATOM   1180  CA  GLY A 159     -29.941 -16.286 -21.419  1.00 53.05           C  
ATOM   1181  C   GLY A 159     -29.571 -14.827 -21.505  1.00 50.28           C  
ATOM   1182  O   GLY A 159     -29.108 -14.237 -20.517  1.00 60.39           O  
ATOM   1183  N   ASN A 160     -29.881 -14.283 -22.690  1.00 40.08           N  
ATOM   1184  CA  ASN A 160     -29.576 -12.889 -23.021  1.00 58.74           C  
ATOM   1185  C   ASN A 160     -30.513 -11.878 -22.379  1.00 49.02           C  
ATOM   1186  O   ASN A 160     -30.221 -10.679 -22.423  1.00 47.25           O  
ATOM   1187  CB  ASN A 160     -29.681 -12.570 -24.519  1.00 63.82           C  
ATOM   1188  CG  ASN A 160     -29.140 -13.586 -25.520  1.00 89.40           C  
ATOM   1189  ND2 ASN A 160     -28.148 -13.258 -26.348  1.00 92.23           N  
ATOM   1190  OD1 ASN A 160     -29.642 -14.714 -25.584  1.00107.52           O  
ATOM   1191  N   TYR A 161     -31.610 -12.399 -21.827  1.00 38.38           N  
ATOM   1192  CA  TYR A 161     -32.745 -11.654 -21.343  1.00 39.40           C  
ATOM   1193  C   TYR A 161     -32.897 -11.571 -19.868  1.00 45.36           C  
ATOM   1194  O   TYR A 161     -32.694 -12.571 -19.199  1.00 41.06           O  
ATOM   1195  CB  TYR A 161     -34.032 -12.248 -21.832  1.00 34.37           C  
ATOM   1196  CG  TYR A 161     -33.928 -12.420 -23.319  1.00 57.59           C  
ATOM   1197  CD1 TYR A 161     -34.214 -11.348 -24.137  1.00 69.71           C  
ATOM   1198  CD2 TYR A 161     -33.466 -13.610 -23.847  1.00 70.14           C  
ATOM   1199  CE1 TYR A 161     -34.024 -11.449 -25.505  1.00 73.90           C  
ATOM   1200  CE2 TYR A 161     -33.273 -13.718 -25.213  1.00 73.04           C  
ATOM   1201  CZ  TYR A 161     -33.551 -12.632 -26.033  1.00 78.64           C  
ATOM   1202  OH  TYR A 161     -33.330 -12.707 -27.399  1.00 85.47           O  
ATOM   1203  N   THR A 162     -33.236 -10.402 -19.355  1.00 30.45           N  
ATOM   1204  CA  THR A 162     -33.706 -10.323 -18.003  1.00 27.25           C  
ATOM   1205  C   THR A 162     -35.022  -9.647 -18.191  1.00 35.32           C  
ATOM   1206  O   THR A 162     -35.134  -8.718 -18.995  1.00 33.92           O  
ATOM   1207  CB  THR A 162     -32.868  -9.465 -17.130  1.00 31.07           C  
ATOM   1208  CG2 THR A 162     -33.451  -9.361 -15.716  1.00 29.14           C  
ATOM   1209  OG1 THR A 162     -31.580 -10.064 -17.140  1.00 39.71           O  
ATOM   1210  N   VAL A 163     -36.026 -10.187 -17.560  1.00 27.12           N  
ATOM   1211  CA  VAL A 163     -37.283  -9.487 -17.575  1.00 37.49           C  
ATOM   1212  C   VAL A 163     -37.647  -9.264 -16.118  1.00 30.21           C  
ATOM   1213  O   VAL A 163     -37.138  -9.955 -15.232  1.00 33.78           O  
ATOM   1214  CB  VAL A 163     -38.441 -10.272 -18.322  1.00 34.36           C  
ATOM   1215  CG1 VAL A 163     -38.016 -10.437 -19.778  1.00 32.38           C  
ATOM   1216  CG2 VAL A 163     -38.781 -11.590 -17.642  1.00 43.54           C  
ATOM   1217  N   GLY A 164     -38.455  -8.264 -15.789  1.00 28.78           N  
ATOM   1218  CA  GLY A 164     -38.834  -8.067 -14.404  1.00 30.23           C  
ATOM   1219  C   GLY A 164     -40.028  -7.130 -14.251  1.00 28.31           C  
ATOM   1220  O   GLY A 164     -40.504  -6.535 -15.231  1.00 28.35           O  
ATOM   1221  N   LEU A 165     -40.485  -7.000 -13.009  1.00 24.05           N  
ATOM   1222  CA  LEU A 165     -41.541  -6.072 -12.695  1.00 31.20           C  
ATOM   1223  C   LEU A 165     -41.362  -5.520 -11.320  1.00 23.08           C  
ATOM   1224  O   LEU A 165     -40.730  -6.101 -10.448  1.00 27.04           O  
ATOM   1225  CB  LEU A 165     -42.916  -6.717 -12.797  1.00 40.23           C  
ATOM   1226  CG  LEU A 165     -43.469  -7.858 -11.993  1.00 55.61           C  
ATOM   1227  CD1 LEU A 165     -44.688  -7.380 -11.203  1.00 64.27           C  
ATOM   1228  CD2 LEU A 165     -43.916  -8.972 -12.950  1.00 58.44           C  
ATOM   1229  N   GLY A 166     -41.889  -4.325 -11.162  1.00 28.71           N  
ATOM   1230  CA  GLY A 166     -41.755  -3.616  -9.922  1.00 24.37           C  
ATOM   1231  C   GLY A 166     -43.037  -2.863  -9.641  1.00 22.71           C  
ATOM   1232  O   GLY A 166     -43.827  -2.589 -10.546  1.00 23.22           O  
ATOM   1233  N   TYR A 167     -43.236  -2.588  -8.386  1.00 22.54           N  
ATOM   1234  CA  TYR A 167     -44.376  -1.878  -7.954  1.00 21.68           C  
ATOM   1235  C   TYR A 167     -43.856  -0.994  -6.859  1.00 22.97           C  
ATOM   1236  O   TYR A 167     -43.290  -1.405  -5.848  1.00 25.70           O  
ATOM   1237  CB  TYR A 167     -45.356  -2.862  -7.457  1.00 19.60           C  
ATOM   1238  CG  TYR A 167     -46.521  -2.126  -6.887  1.00 30.51           C  
ATOM   1239  CD1 TYR A 167     -47.434  -1.490  -7.716  1.00 31.48           C  
ATOM   1240  CD2 TYR A 167     -46.607  -2.065  -5.514  1.00 35.86           C  
ATOM   1241  CE1 TYR A 167     -48.456  -0.772  -7.125  1.00 34.71           C  
ATOM   1242  CE2 TYR A 167     -47.621  -1.345  -4.921  1.00 45.09           C  
ATOM   1243  CZ  TYR A 167     -48.531  -0.707  -5.736  1.00 45.63           C  
ATOM   1244  OH  TYR A 167     -49.526   0.024  -5.121  1.00 43.91           O  
ATOM   1245  N   GLU A 168     -44.228   0.252  -7.040  1.00 25.32           N  
ATOM   1246  CA  GLU A 168     -43.824   1.318  -6.152  1.00 22.85           C  
ATOM   1247  C   GLU A 168     -44.998   2.157  -5.653  1.00 23.46           C  
ATOM   1248  O   GLU A 168     -45.940   2.421  -6.413  1.00 21.97           O  
ATOM   1249  CB  GLU A 168     -42.899   2.239  -6.877  1.00 23.96           C  
ATOM   1250  CG  GLU A 168     -41.734   1.657  -7.677  1.00 18.08           C  
ATOM   1251  CD  GLU A 168     -40.792   2.753  -8.113  1.00 17.37           C  
ATOM   1252  OE1 GLU A 168     -39.998   3.218  -7.302  1.00 19.97           O  
ATOM   1253  OE2 GLU A 168     -40.823   3.163  -9.255  1.00 21.50           O1-
ATOM   1254  N   LYS A 169     -44.961   2.610  -4.418  1.00 21.91           N  
ATOM   1255  CA  LYS A 169     -45.990   3.513  -3.938  1.00 26.98           C  
ATOM   1256  C   LYS A 169     -45.525   4.530  -2.899  1.00 33.90           C  
ATOM   1257  O   LYS A 169     -44.519   4.329  -2.196  1.00 21.78           O  
ATOM   1258  CB  LYS A 169     -47.125   2.697  -3.386  1.00 22.39           C  
ATOM   1259  CG  LYS A 169     -46.716   1.884  -2.217  1.00 33.73           C  
ATOM   1260  CD  LYS A 169     -48.027   1.409  -1.716  1.00 55.00           C  
ATOM   1261  CE  LYS A 169     -47.924   1.523  -0.211  1.00 70.05           C  
ATOM   1262  NZ  LYS A 169     -49.259   1.454   0.366  1.00 76.45           N1+
ATOM   1263  N   ILE A 170     -46.201   5.702  -2.852  1.00 24.31           N  
ATOM   1264  CA  ILE A 170     -45.951   6.738  -1.838  1.00 26.64           C  
ATOM   1265  C   ILE A 170     -47.295   7.004  -1.132  1.00 22.64           C  
ATOM   1266  O   ILE A 170     -48.301   7.280  -1.773  1.00 26.39           O  
ATOM   1267  CB  ILE A 170     -45.407   8.083  -2.451  1.00 22.23           C  
ATOM   1268  CG1 ILE A 170     -44.111   7.891  -3.259  1.00 18.13           C  
ATOM   1269  CG2 ILE A 170     -45.180   9.048  -1.279  1.00 20.59           C  
ATOM   1270  CD1 ILE A 170     -43.570   9.161  -3.907  1.00 22.57           C  
ATOM   1271  N   ASP A 171     -47.366   6.799   0.163  1.00 21.42           N  
ATOM   1272  CA  ASP A 171     -48.488   7.131   0.999  1.00 22.65           C  
ATOM   1273  C   ASP A 171     -48.318   8.504   1.582  1.00 24.81           C  
ATOM   1274  O   ASP A 171     -47.340   8.817   2.262  1.00 25.52           O  
ATOM   1275  CB  ASP A 171     -48.627   6.206   2.163  1.00 24.09           C  
ATOM   1276  CG  ASP A 171     -48.917   4.787   1.723  1.00 37.12           C  
ATOM   1277  OD1 ASP A 171     -49.480   4.591   0.640  1.00 39.08           O  
ATOM   1278  OD2 ASP A 171     -48.553   3.887   2.475  1.00 63.64           O1-
ATOM   1279  N   SER A 172     -49.336   9.308   1.303  1.00 28.50           N  
ATOM   1280  CA  SER A 172     -49.413  10.689   1.722  1.00 29.34           C  
ATOM   1281  C   SER A 172     -49.721  10.769   3.193  1.00 19.80           C  
ATOM   1282  O   SER A 172     -50.577  10.020   3.653  1.00 27.09           O  
ATOM   1283  CB  SER A 172     -50.519  11.409   0.991  1.00 25.55           C  
ATOM   1284  OG  SER A 172     -50.488  12.741   1.467  1.00 28.00           O  
ATOM   1285  N   PRO A 173     -49.141  11.663   3.986  1.00 23.04           N  
ATOM   1286  CA  PRO A 173     -49.563  11.866   5.354  1.00 24.44           C  
ATOM   1287  C   PRO A 173     -50.914  12.578   5.347  1.00 46.59           C  
ATOM   1288  O   PRO A 173     -51.604  12.435   6.343  1.00 45.87           O  
ATOM   1289  CB  PRO A 173     -48.474  12.680   5.974  1.00 21.93           C  
ATOM   1290  CG  PRO A 173     -48.053  13.568   4.845  1.00 24.05           C  
ATOM   1291  CD  PRO A 173     -48.214  12.702   3.573  1.00 23.65           C  
ATOM   1292  N   ASP A 174     -51.353  13.316   4.303  1.00 32.74           N  
ATOM   1293  CA  ASP A 174     -52.634  14.015   4.327  1.00 29.56           C  
ATOM   1294  C   ASP A 174     -53.116  14.097   2.901  1.00 19.81           C  
ATOM   1295  O   ASP A 174     -52.614  14.924   2.116  1.00 27.36           O  
ATOM   1296  CB  ASP A 174     -52.450  15.419   4.897  1.00 37.96           C  
ATOM   1297  CG  ASP A 174     -53.741  16.226   5.161  1.00 44.06           C  
ATOM   1298  OD1 ASP A 174     -54.800  15.951   4.604  1.00 35.40           O  
ATOM   1299  OD2 ASP A 174     -53.679  17.164   5.947  1.00 47.06           O1-
ATOM   1300  N   THR A 175     -54.112  13.255   2.582  1.00 25.91           N  
ATOM   1301  CA  THR A 175     -54.618  13.196   1.218  1.00 31.18           C  
ATOM   1302  C   THR A 175     -55.512  14.380   0.782  1.00 37.44           C  
ATOM   1303  O   THR A 175     -55.851  14.468  -0.411  1.00 34.89           O  
ATOM   1304  CB  THR A 175     -55.337  11.828   0.994  1.00 35.52           C  
ATOM   1305  CG2 THR A 175     -54.326  10.659   0.981  1.00 30.09           C  
ATOM   1306  OG1 THR A 175     -56.306  11.671   2.017  1.00 41.72           O  
ATOM   1307  N   ALA A 176     -55.847  15.319   1.703  1.00 36.77           N  
ATOM   1308  CA  ALA A 176     -56.447  16.604   1.328  1.00 34.55           C  
ATOM   1309  C   ALA A 176     -55.359  17.445   0.692  1.00 34.09           C  
ATOM   1310  O   ALA A 176     -55.619  18.217  -0.240  1.00 32.18           O  
ATOM   1311  CB  ALA A 176     -56.933  17.423   2.507  1.00 29.40           C  
ATOM   1312  N   LEU A 177     -54.115  17.272   1.185  1.00 25.68           N  
ATOM   1313  CA  LEU A 177     -52.994  18.030   0.664  1.00 24.25           C  
ATOM   1314  C   LEU A 177     -52.165  17.379  -0.454  1.00 30.49           C  
ATOM   1315  O   LEU A 177     -51.642  18.098  -1.319  1.00 25.58           O  
ATOM   1316  CB  LEU A 177     -52.118  18.374   1.838  1.00 34.03           C  
ATOM   1317  CG  LEU A 177     -52.745  19.324   2.847  1.00 41.02           C  
ATOM   1318  CD1 LEU A 177     -51.784  19.524   3.976  1.00 40.73           C  
ATOM   1319  CD2 LEU A 177     -53.007  20.676   2.226  1.00 41.14           C  
ATOM   1320  N   MET A 178     -52.023  16.048  -0.505  1.00 27.88           N  
ATOM   1321  CA  MET A 178     -51.218  15.370  -1.540  1.00 24.64           C  
ATOM   1322  C   MET A 178     -51.827  14.007  -1.700  1.00 15.20           C  
ATOM   1323  O   MET A 178     -52.045  13.330  -0.703  1.00 22.04           O  
ATOM   1324  CB  MET A 178     -49.753  15.229  -1.086  1.00 24.97           C  
ATOM   1325  CG  MET A 178     -48.899  14.715  -2.247  1.00 37.40           C  
ATOM   1326  SD  MET A 178     -47.182  14.385  -1.752  1.00 34.16           S  
ATOM   1327  CE  MET A 178     -47.425  12.938  -0.740  1.00 28.69           C  
ATOM   1328  N   ALA A 179     -52.228  13.630  -2.899  1.00 18.97           N  
ATOM   1329  CA  ALA A 179     -52.833  12.343  -3.163  1.00 21.25           C  
ATOM   1330  C   ALA A 179     -51.787  11.240  -2.983  1.00 32.90           C  
ATOM   1331  O   ALA A 179     -50.583  11.466  -3.154  1.00 23.82           O  
ATOM   1332  CB  ALA A 179     -53.313  12.236  -4.607  1.00 19.86           C  
ATOM   1333  N   ASP A 180     -52.209  10.053  -2.628  1.00 25.51           N  
ATOM   1334  CA  ASP A 180     -51.344   8.873  -2.687  1.00 29.77           C  
ATOM   1335  C   ASP A 180     -50.909   8.583  -4.117  1.00 35.87           C  
ATOM   1336  O   ASP A 180     -51.669   8.861  -5.061  1.00 25.57           O  
ATOM   1337  CB  ASP A 180     -52.069   7.661  -2.208  1.00 22.82           C  
ATOM   1338  CG  ASP A 180     -52.396   7.642  -0.743  1.00 19.28           C  
ATOM   1339  OD1 ASP A 180     -51.770   8.363   0.023  1.00 24.24           O  
ATOM   1340  OD2 ASP A 180     -53.276   6.871  -0.372  1.00 34.46           O1-
ATOM   1341  N   MET A 181     -49.726   7.990  -4.329  1.00 21.42           N  
ATOM   1342  CA  MET A 181     -49.246   7.756  -5.678  1.00 19.55           C  
ATOM   1343  C   MET A 181     -48.827   6.279  -5.805  1.00 26.26           C  
ATOM   1344  O   MET A 181     -48.517   5.638  -4.789  1.00 23.03           O  
ATOM   1345  CB  MET A 181     -48.041   8.650  -5.969  1.00 20.30           C  
ATOM   1346  CG  MET A 181     -48.237  10.152  -5.680  1.00 22.93           C  
ATOM   1347  SD  MET A 181     -46.998  11.259  -6.352  1.00 27.32           S  
ATOM   1348  CE  MET A 181     -46.625  11.940  -4.790  1.00 22.23           C  
ATOM   1349  N   GLU A 182     -48.834   5.699  -6.997  1.00 23.25           N  
ATOM   1350  CA  GLU A 182     -48.335   4.352  -7.191  1.00 28.22           C  
ATOM   1351  C   GLU A 182     -47.911   4.225  -8.620  1.00 22.99           C  
ATOM   1352  O   GLU A 182     -48.313   5.042  -9.463  1.00 23.60           O  
ATOM   1353  CB  GLU A 182     -49.361   3.300  -6.905  1.00 27.70           C  
ATOM   1354  CG  GLU A 182     -50.584   3.395  -7.772  1.00 39.91           C  
ATOM   1355  CD  GLU A 182     -51.467   2.157  -7.724  1.00 49.50           C  
ATOM   1356  OE1 GLU A 182     -51.758   1.649  -6.633  1.00 46.27           O  
ATOM   1357  OE2 GLU A 182     -51.842   1.706  -8.810  1.00 81.45           O1-
ATOM   1358  N   GLN A 183     -47.038   3.252  -8.919  1.00 23.57           N  
ATOM   1359  CA  GLN A 183     -46.565   3.033 -10.279  1.00 20.27           C  
ATOM   1360  C   GLN A 183     -46.170   1.565 -10.374  1.00 24.71           C  
ATOM   1361  O   GLN A 183     -45.599   1.021  -9.423  1.00 25.60           O  
ATOM   1362  CB  GLN A 183     -45.366   3.930 -10.548  1.00 21.67           C  
ATOM   1363  CG  GLN A 183     -44.851   3.892 -11.956  1.00 22.57           C  
ATOM   1364  CD  GLN A 183     -43.791   4.946 -12.111  1.00 34.59           C  
ATOM   1365  NE2 GLN A 183     -42.492   4.738 -12.210  1.00 26.73           N  
ATOM   1366  OE1 GLN A 183     -44.129   6.104 -12.162  1.00 33.27           O  
ATOM   1367  N   LEU A 184     -46.534   0.945 -11.477  1.00 25.90           N  
ATOM   1368  CA  LEU A 184     -46.193  -0.431 -11.765  1.00 25.47           C  
ATOM   1369  C   LEU A 184     -45.243  -0.393 -12.933  1.00 30.93           C  
ATOM   1370  O   LEU A 184     -45.488   0.375 -13.863  1.00 29.59           O  
ATOM   1371  CB  LEU A 184     -47.405  -1.224 -12.169  1.00 30.36           C  
ATOM   1372  CG  LEU A 184     -47.133  -2.680 -12.617  1.00 53.58           C  
ATOM   1373  CD1 LEU A 184     -47.054  -3.652 -11.419  1.00 41.36           C  
ATOM   1374  CD2 LEU A 184     -48.238  -3.082 -13.569  1.00 61.50           C  
ATOM   1375  N   GLU A 185     -44.156  -1.171 -12.955  1.00 24.93           N  
ATOM   1376  CA  GLU A 185     -43.212  -1.167 -14.069  1.00 21.56           C  
ATOM   1377  C   GLU A 185     -42.985  -2.592 -14.611  1.00 20.96           C  
ATOM   1378  O   GLU A 185     -43.007  -3.553 -13.823  1.00 25.62           O  
ATOM   1379  CB  GLU A 185     -41.814  -0.676 -13.676  1.00 28.40           C  
ATOM   1380  CG  GLU A 185     -41.611   0.754 -13.196  1.00 33.30           C  
ATOM   1381  CD  GLU A 185     -41.548   0.966 -11.698  1.00 31.54           C  
ATOM   1382  OE1 GLU A 185     -41.251   0.067 -10.924  1.00 27.29           O  
ATOM   1383  OE2 GLU A 185     -41.796   2.079 -11.287  1.00 25.85           O1-
ATOM   1384  N   LEU A 186     -42.756  -2.693 -15.920  1.00 24.15           N  
ATOM   1385  CA  LEU A 186     -42.314  -3.918 -16.584  1.00 28.00           C  
ATOM   1386  C   LEU A 186     -41.047  -3.461 -17.255  1.00 28.26           C  
ATOM   1387  O   LEU A 186     -41.020  -2.388 -17.874  1.00 29.09           O  
ATOM   1388  CB  LEU A 186     -43.209  -4.414 -17.712  1.00 30.48           C  
ATOM   1389  CG  LEU A 186     -44.602  -4.699 -17.272  1.00 49.76           C  
ATOM   1390  CD1 LEU A 186     -45.446  -4.920 -18.505  1.00 56.71           C  
ATOM   1391  CD2 LEU A 186     -44.595  -5.852 -16.294  1.00 41.46           C  
ATOM   1392  N   ALA A 187     -39.978  -4.233 -17.133  1.00 23.92           N  
ATOM   1393  CA  ALA A 187     -38.731  -3.854 -17.743  1.00 23.34           C  
ATOM   1394  C   ALA A 187     -38.161  -5.103 -18.414  1.00 27.75           C  
ATOM   1395  O   ALA A 187     -38.420  -6.226 -17.979  1.00 26.70           O  
ATOM   1396  CB  ALA A 187     -37.784  -3.358 -16.662  1.00 24.93           C  
ATOM   1397  N   ALA A 188     -37.412  -4.924 -19.467  1.00 25.88           N  
ATOM   1398  CA  ALA A 188     -36.774  -6.011 -20.167  1.00 34.01           C  
ATOM   1399  C   ALA A 188     -35.365  -5.546 -20.471  1.00 33.31           C  
ATOM   1400  O   ALA A 188     -35.197  -4.377 -20.836  1.00 29.55           O  
ATOM   1401  CB  ALA A 188     -37.493  -6.294 -21.486  1.00 26.52           C  
ATOM   1402  N   ILE A 189     -34.327  -6.376 -20.337  1.00 36.39           N  
ATOM   1403  CA  ILE A 189     -32.960  -6.008 -20.726  1.00 27.67           C  
ATOM   1404  C   ILE A 189     -32.393  -7.185 -21.542  1.00 37.92           C  
ATOM   1405  O   ILE A 189     -32.623  -8.339 -21.182  1.00 33.44           O  
ATOM   1406  CB  ILE A 189     -32.081  -5.775 -19.495  1.00 29.72           C  
ATOM   1407  CG1 ILE A 189     -32.664  -4.695 -18.625  1.00 39.00           C  
ATOM   1408  CG2 ILE A 189     -30.701  -5.344 -19.946  1.00 33.27           C  
ATOM   1409  CD1 ILE A 189     -32.518  -5.009 -17.141  1.00 38.17           C  
ATOM   1410  N   ALA A 190     -31.681  -6.926 -22.627  1.00 34.42           N  
ATOM   1411  CA  ALA A 190     -31.194  -7.926 -23.542  1.00 33.15           C  
ATOM   1412  C   ALA A 190     -29.832  -7.520 -23.981  1.00 43.94           C  
ATOM   1413  O   ALA A 190     -29.608  -6.344 -24.315  1.00 36.50           O  
ATOM   1414  CB  ALA A 190     -32.001  -8.007 -24.817  1.00 29.97           C  
ATOM   1415  N   LYS A 191     -28.900  -8.466 -23.940  1.00 49.78           N  
ATOM   1416  CA  LYS A 191     -27.596  -8.223 -24.551  1.00 48.56           C  
ATOM   1417  C   LYS A 191     -27.477  -9.171 -25.705  1.00 51.68           C  
ATOM   1418  O   LYS A 191     -27.762 -10.360 -25.570  1.00 65.27           O  
ATOM   1419  CB  LYS A 191     -26.404  -8.488 -23.635  1.00 49.42           C  
ATOM   1420  CG  LYS A 191     -26.600  -9.632 -22.649  1.00 75.96           C  
ATOM   1421  CD  LYS A 191     -26.218  -9.111 -21.267  1.00 86.39           C  
ATOM   1422  CE  LYS A 191     -27.264  -8.136 -20.722  1.00 88.43           C  
ATOM   1423  NZ  LYS A 191     -26.678  -7.247 -19.733  1.00 91.69           N1+
ATOM   1424  N   PHE A 192     -27.140  -8.650 -26.869  1.00 57.59           N  
ATOM   1425  CA  PHE A 192     -26.943  -9.428 -28.078  1.00 49.63           C  
ATOM   1426  C   PHE A 192     -25.509  -9.151 -28.488  1.00 55.22           C  
ATOM   1427  O   PHE A 192     -25.200  -8.440 -29.459  1.00 60.13           O  
ATOM   1428  CB  PHE A 192     -27.891  -8.976 -29.178  1.00 52.90           C  
ATOM   1429  CG  PHE A 192     -29.349  -9.160 -28.825  1.00 55.44           C  
ATOM   1430  CD1 PHE A 192     -29.763 -10.319 -28.197  1.00 63.13           C  
ATOM   1431  CD2 PHE A 192     -30.229  -8.148 -29.140  1.00 62.68           C  
ATOM   1432  CE1 PHE A 192     -31.085 -10.461 -27.875  1.00 71.79           C  
ATOM   1433  CE2 PHE A 192     -31.552  -8.303 -28.813  1.00 64.06           C  
ATOM   1434  CZ  PHE A 192     -31.975  -9.453 -28.184  1.00 66.40           C  
ATOM   1435  N   GLY A 193     -24.605  -9.659 -27.651  1.00 53.26           N  
ATOM   1436  CA  GLY A 193     -23.199  -9.444 -27.910  1.00 64.96           C  
ATOM   1437  C   GLY A 193     -22.767  -8.016 -27.569  1.00 72.86           C  
ATOM   1438  O   GLY A 193     -22.926  -7.578 -26.425  1.00 83.89           O  
ATOM   1439  N   ALA A 194     -22.265  -7.264 -28.558  1.00 65.54           N  
ATOM   1440  CA  ALA A 194     -21.766  -5.909 -28.334  1.00 58.81           C  
ATOM   1441  C   ALA A 194     -22.877  -4.869 -28.095  1.00 53.68           C  
ATOM   1442  O   ALA A 194     -22.573  -3.715 -27.761  1.00 41.71           O  
ATOM   1443  CB  ALA A 194     -20.945  -5.500 -29.552  1.00 56.03           C  
ATOM   1444  N   THR A 195     -24.137  -5.289 -28.324  1.00 51.68           N  
ATOM   1445  CA  THR A 195     -25.374  -4.518 -28.217  1.00 43.81           C  
ATOM   1446  C   THR A 195     -26.216  -4.749 -26.970  1.00 45.19           C  
ATOM   1447  O   THR A 195     -26.547  -5.879 -26.617  1.00 37.22           O  
ATOM   1448  CB  THR A 195     -26.207  -4.817 -29.465  1.00 33.57           C  
ATOM   1449  CG2 THR A 195     -27.502  -4.025 -29.579  1.00 33.82           C  
ATOM   1450  OG1 THR A 195     -25.328  -4.508 -30.552  1.00 41.80           O  
ATOM   1451  N   ASN A 196     -26.609  -3.677 -26.298  1.00 33.40           N  
ATOM   1452  CA  ASN A 196     -27.438  -3.778 -25.113  1.00 34.17           C  
ATOM   1453  C   ASN A 196     -28.769  -3.134 -25.456  1.00 26.07           C  
ATOM   1454  O   ASN A 196     -28.765  -2.098 -26.144  1.00 31.07           O  
ATOM   1455  CB  ASN A 196     -26.789  -3.023 -23.997  1.00 34.94           C  
ATOM   1456  CG  ASN A 196     -25.464  -3.636 -23.582  1.00 37.97           C  
ATOM   1457  ND2 ASN A 196     -24.341  -2.996 -23.878  1.00 35.68           N  
ATOM   1458  OD1 ASN A 196     -25.418  -4.709 -22.978  1.00 38.93           O  
ATOM   1459  N   VAL A 197     -29.898  -3.703 -25.069  1.00 27.67           N  
ATOM   1460  CA  VAL A 197     -31.179  -3.103 -25.356  1.00 27.06           C  
ATOM   1461  C   VAL A 197     -31.875  -3.083 -24.013  1.00 32.58           C  
ATOM   1462  O   VAL A 197     -31.768  -4.050 -23.262  1.00 35.46           O  
ATOM   1463  CB  VAL A 197     -31.970  -3.945 -26.365  1.00 26.96           C  
ATOM   1464  CG1 VAL A 197     -33.337  -3.331 -26.609  1.00 31.44           C  
ATOM   1465  CG2 VAL A 197     -31.276  -3.919 -27.708  1.00 30.72           C  
ATOM   1466  N   LYS A 198     -32.530  -1.990 -23.635  1.00 28.97           N  
ATOM   1467  CA  LYS A 198     -33.250  -1.910 -22.372  1.00 23.59           C  
ATOM   1468  C   LYS A 198     -34.552  -1.203 -22.761  1.00 20.72           C  
ATOM   1469  O   LYS A 198     -34.552  -0.290 -23.612  1.00 25.42           O  
ATOM   1470  CB  LYS A 198     -32.449  -1.082 -21.359  1.00 22.91           C  
ATOM   1471  CG  LYS A 198     -33.157  -1.136 -20.014  1.00 31.46           C  
ATOM   1472  CD  LYS A 198     -32.450  -0.400 -18.890  1.00 27.19           C  
ATOM   1473  CE  LYS A 198     -31.150  -1.110 -18.564  1.00 27.71           C  
ATOM   1474  NZ  LYS A 198     -30.470  -0.546 -17.404  1.00 22.82           N1+
ATOM   1475  N   ALA A 199     -35.654  -1.662 -22.184  1.00 23.92           N  
ATOM   1476  CA  ALA A 199     -36.972  -1.099 -22.456  1.00 29.51           C  
ATOM   1477  C   ALA A 199     -37.829  -1.197 -21.215  1.00 31.31           C  
ATOM   1478  O   ALA A 199     -37.612  -2.106 -20.397  1.00 27.54           O  
ATOM   1479  CB  ALA A 199     -37.689  -1.864 -23.544  1.00 29.98           C  
ATOM   1480  N   TYR A 200     -38.788  -0.287 -20.990  1.00 24.08           N  
ATOM   1481  CA  TYR A 200     -39.652  -0.415 -19.823  1.00 25.77           C  
ATOM   1482  C   TYR A 200     -41.014   0.195 -20.196  1.00 19.77           C  
ATOM   1483  O   TYR A 200     -41.106   0.963 -21.155  1.00 25.09           O  
ATOM   1484  CB  TYR A 200     -39.075   0.337 -18.597  1.00 21.68           C  
ATOM   1485  CG  TYR A 200     -39.130   1.868 -18.750  1.00 27.89           C  
ATOM   1486  CD1 TYR A 200     -38.178   2.561 -19.491  1.00 23.60           C  
ATOM   1487  CD2 TYR A 200     -40.205   2.569 -18.176  1.00 26.80           C  
ATOM   1488  CE1 TYR A 200     -38.299   3.942 -19.669  1.00 21.78           C  
ATOM   1489  CE2 TYR A 200     -40.333   3.943 -18.353  1.00 21.58           C  
ATOM   1490  CZ  TYR A 200     -39.384   4.622 -19.098  1.00 29.96           C  
ATOM   1491  OH  TYR A 200     -39.551   5.991 -19.271  1.00 24.28           O  
ATOM   1492  N   TYR A 201     -42.012  -0.110 -19.412  1.00 22.60           N  
ATOM   1493  CA  TYR A 201     -43.294   0.505 -19.534  1.00 24.74           C  
ATOM   1494  C   TYR A 201     -43.701   0.723 -18.083  1.00 26.88           C  
ATOM   1495  O   TYR A 201     -43.523  -0.165 -17.237  1.00 24.56           O  
ATOM   1496  CB  TYR A 201     -44.227  -0.452 -20.266  1.00 25.19           C  
ATOM   1497  CG  TYR A 201     -45.657   0.054 -20.178  1.00 34.01           C  
ATOM   1498  CD1 TYR A 201     -46.049   1.035 -21.067  1.00 36.14           C  
ATOM   1499  CD2 TYR A 201     -46.510  -0.445 -19.198  1.00 34.68           C  
ATOM   1500  CE1 TYR A 201     -47.324   1.536 -20.978  1.00 36.17           C  
ATOM   1501  CE2 TYR A 201     -47.786   0.060 -19.105  1.00 35.36           C  
ATOM   1502  CZ  TYR A 201     -48.172   1.045 -20.004  1.00 36.59           C  
ATOM   1503  OH  TYR A 201     -49.452   1.567 -19.934  1.00 56.03           O  
ATOM   1504  N   ALA A 202     -44.278   1.887 -17.760  1.00 27.52           N  
ATOM   1505  CA  ALA A 202     -44.712   2.193 -16.394  1.00 25.10           C  
ATOM   1506  C   ALA A 202     -46.106   2.827 -16.479  1.00 25.08           C  
ATOM   1507  O   ALA A 202     -46.402   3.570 -17.412  1.00 25.54           O  
ATOM   1508  CB  ALA A 202     -43.785   3.217 -15.692  1.00 22.21           C  
ATOM   1509  N   ASP A 203     -46.929   2.573 -15.496  1.00 24.00           N  
ATOM   1510  CA  ASP A 203     -48.285   3.046 -15.496  1.00 28.68           C  
ATOM   1511  C   ASP A 203     -48.705   3.292 -14.056  1.00 29.57           C  
ATOM   1512  O   ASP A 203     -48.376   2.476 -13.174  1.00 32.82           O  
ATOM   1513  CB  ASP A 203     -49.124   1.957 -16.171  1.00 37.41           C  
ATOM   1514  CG  ASP A 203     -50.566   2.337 -16.345  1.00 48.02           C  
ATOM   1515  OD1 ASP A 203     -50.901   3.045 -17.293  1.00 75.41           O  
ATOM   1516  OD2 ASP A 203     -51.352   1.938 -15.503  1.00 67.85           O1-
ATOM   1517  N   GLY A 204     -49.435   4.370 -13.736  1.00 32.61           N  
ATOM   1518  CA  GLY A 204     -49.913   4.519 -12.369  1.00 28.05           C  
ATOM   1519  C   GLY A 204     -50.656   5.826 -12.182  1.00 28.93           C  
ATOM   1520  O   GLY A 204     -51.306   6.327 -13.117  1.00 27.42           O  
ATOM   1521  N   GLU A 205     -50.525   6.400 -10.994  1.00 23.03           N  
ATOM   1522  CA  GLU A 205     -51.130   7.696 -10.769  1.00 27.54           C  
ATOM   1523  C   GLU A 205     -50.280   8.513  -9.840  1.00 28.34           C  
ATOM   1524  O   GLU A 205     -49.588   7.992  -8.966  1.00 25.57           O  
ATOM   1525  CB  GLU A 205     -52.529   7.570 -10.188  1.00 27.61           C  
ATOM   1526  CG  GLU A 205     -52.621   6.938  -8.833  1.00 43.67           C  
ATOM   1527  CD  GLU A 205     -54.049   6.661  -8.371  1.00 51.38           C  
ATOM   1528  OE1 GLU A 205     -54.868   6.237  -9.195  1.00 51.17           O  
ATOM   1529  OE2 GLU A 205     -54.309   6.855  -7.173  1.00 66.67           O1-
ATOM   1530  N   LEU A 206     -50.333   9.817 -10.089  1.00 21.41           N  
ATOM   1531  CA  LEU A 206     -49.519  10.803  -9.413  1.00 19.79           C  
ATOM   1532  C   LEU A 206     -50.398  11.859  -8.754  1.00 33.84           C  
ATOM   1533  O   LEU A 206     -51.542  12.037  -9.171  1.00 26.21           O  
ATOM   1534  CB  LEU A 206     -48.625  11.499 -10.405  1.00 20.83           C  
ATOM   1535  CG  LEU A 206     -47.570  10.680 -11.135  1.00 25.89           C  
ATOM   1536  CD1 LEU A 206     -46.800  11.593 -12.075  1.00 25.84           C  
ATOM   1537  CD2 LEU A 206     -46.657  10.004 -10.101  1.00 21.85           C  
ATOM   1538  N   ASP A 207     -49.907  12.559  -7.728  1.00 24.31           N  
ATOM   1539  CA  ASP A 207     -50.586  13.697  -7.155  1.00 26.55           C  
ATOM   1540  C   ASP A 207     -50.626  14.745  -8.267  1.00 29.31           C  
ATOM   1541  O   ASP A 207     -49.638  14.962  -8.986  1.00 22.97           O  
ATOM   1542  CB  ASP A 207     -49.803  14.222  -5.981  1.00 22.03           C  
ATOM   1543  CG  ASP A 207     -50.326  15.569  -5.491  1.00 23.24           C  
ATOM   1544  OD1 ASP A 207     -51.407  15.581  -4.899  1.00 24.98           O  
ATOM   1545  OD2 ASP A 207     -49.662  16.578  -5.719  1.00 24.03           O1-
ATOM   1546  N   ARG A 208     -51.763  15.445  -8.375  1.00 26.76           N  
ATOM   1547  CA  ARG A 208     -51.967  16.482  -9.382  1.00 22.68           C  
ATOM   1548  C   ARG A 208     -50.902  17.543  -9.376  1.00 17.48           C  
ATOM   1549  O   ARG A 208     -50.302  17.826 -10.415  1.00 22.76           O  
ATOM   1550  CB  ARG A 208     -53.321  17.205  -9.187  1.00 24.59           C  
ATOM   1551  CG  ARG A 208     -53.603  18.344 -10.196  1.00 26.44           C  
ATOM   1552  CD  ARG A 208     -54.754  19.225  -9.677  1.00 20.80           C  
ATOM   1553  NE  ARG A 208     -54.353  19.965  -8.489  1.00 20.58           N  
ATOM   1554  CZ  ARG A 208     -55.063  19.883  -7.364  1.00 17.56           C  
ATOM   1555  NH1 ARG A 208     -56.173  19.152  -7.262  1.00 22.76           N1+
ATOM   1556  NH2 ARG A 208     -54.618  20.521  -6.298  1.00 19.37           N  
ATOM   1557  N   ASP A 209     -50.674  18.163  -8.219  1.00 16.79           N  
ATOM   1558  CA  ASP A 209     -49.732  19.250  -8.219  1.00 17.98           C  
ATOM   1559  C   ASP A 209     -48.277  18.778  -8.335  1.00 25.82           C  
ATOM   1560  O   ASP A 209     -47.453  19.489  -8.902  1.00 23.17           O  
ATOM   1561  CB  ASP A 209     -49.970  20.071  -6.954  1.00 24.37           C  
ATOM   1562  CG  ASP A 209     -51.318  20.834  -6.997  1.00 28.77           C  
ATOM   1563  OD1 ASP A 209     -51.843  21.118  -8.071  1.00 22.89           O  
ATOM   1564  OD2 ASP A 209     -51.834  21.124  -5.932  1.00 27.21           O1-
ATOM   1565  N   PHE A 210     -47.944  17.576  -7.889  1.00 24.91           N  
ATOM   1566  CA  PHE A 210     -46.608  16.997  -8.126  1.00 27.45           C  
ATOM   1567  C   PHE A 210     -46.428  16.813  -9.662  1.00 21.30           C  
ATOM   1568  O   PHE A 210     -45.422  17.257 -10.253  1.00 22.41           O  
ATOM   1569  CB  PHE A 210     -46.571  15.672  -7.307  1.00 24.74           C  
ATOM   1570  CG  PHE A 210     -45.380  14.745  -7.530  1.00 36.77           C  
ATOM   1571  CD1 PHE A 210     -45.400  13.825  -8.571  1.00 36.73           C  
ATOM   1572  CD2 PHE A 210     -44.279  14.825  -6.702  1.00 48.62           C  
ATOM   1573  CE1 PHE A 210     -44.320  12.989  -8.785  1.00 42.01           C  
ATOM   1574  CE2 PHE A 210     -43.198  13.982  -6.921  1.00 38.96           C  
ATOM   1575  CZ  PHE A 210     -43.221  13.071  -7.959  1.00 34.54           C  
ATOM   1576  N   ALA A 211     -47.431  16.257 -10.365  1.00 18.70           N  
ATOM   1577  CA  ALA A 211     -47.401  16.129 -11.807  1.00 17.41           C  
ATOM   1578  C   ALA A 211     -47.246  17.440 -12.536  1.00 21.61           C  
ATOM   1579  O   ALA A 211     -46.467  17.557 -13.490  1.00 23.50           O  
ATOM   1580  CB  ALA A 211     -48.686  15.445 -12.229  1.00 20.52           C  
ATOM   1581  N   ARG A 212     -47.945  18.503 -12.118  1.00 24.46           N  
ATOM   1582  CA  ARG A 212     -47.829  19.798 -12.774  1.00 21.96           C  
ATOM   1583  C   ARG A 212     -46.434  20.365 -12.599  1.00 20.18           C  
ATOM   1584  O   ARG A 212     -45.889  20.990 -13.512  1.00 23.86           O  
ATOM   1585  CB  ARG A 212     -48.850  20.791 -12.188  1.00 19.67           C  
ATOM   1586  CG  ARG A 212     -50.322  20.377 -12.464  1.00 22.71           C  
ATOM   1587  CD  ARG A 212     -51.395  21.356 -11.817  1.00 23.65           C  
ATOM   1588  NE  ARG A 212     -51.182  22.715 -12.293  1.00 20.64           N  
ATOM   1589  CZ  ARG A 212     -51.713  23.179 -13.424  1.00 19.45           C  
ATOM   1590  NH1 ARG A 212     -52.532  22.439 -14.149  1.00 22.61           N1+
ATOM   1591  NH2 ARG A 212     -51.460  24.395 -13.847  1.00 22.43           N  
ATOM   1592  N   ALA A 213     -45.827  20.163 -11.428  1.00 22.64           N  
ATOM   1593  CA  ALA A 213     -44.457  20.647 -11.170  1.00 24.94           C  
ATOM   1594  C   ALA A 213     -43.429  19.946 -12.077  1.00 28.90           C  
ATOM   1595  O   ALA A 213     -42.443  20.583 -12.440  1.00 28.23           O  
ATOM   1596  CB  ALA A 213     -44.081  20.415  -9.714  1.00 18.67           C  
ATOM   1597  N   VAL A 214     -43.641  18.690 -12.533  1.00 27.53           N  
ATOM   1598  CA  VAL A 214     -42.781  18.030 -13.523  1.00 24.66           C  
ATOM   1599  C   VAL A 214     -42.703  18.917 -14.740  1.00 28.81           C  
ATOM   1600  O   VAL A 214     -41.614  19.066 -15.291  1.00 36.46           O  
ATOM   1601  CB  VAL A 214     -43.320  16.652 -14.025  1.00 28.48           C  
ATOM   1602  CG1 VAL A 214     -42.521  16.067 -15.208  1.00 34.90           C  
ATOM   1603  CG2 VAL A 214     -43.264  15.717 -12.862  1.00 30.97           C  
ATOM   1604  N   PHE A 215     -43.833  19.524 -15.169  1.00 30.95           N  
ATOM   1605  CA  PHE A 215     -43.862  20.356 -16.375  1.00 22.46           C  
ATOM   1606  C   PHE A 215     -43.695  21.833 -16.082  1.00 22.21           C  
ATOM   1607  O   PHE A 215     -43.865  22.697 -16.953  1.00 31.72           O  
ATOM   1608  CB  PHE A 215     -45.172  20.109 -17.156  1.00 25.11           C  
ATOM   1609  CG  PHE A 215     -45.240  18.744 -17.852  1.00 24.68           C  
ATOM   1610  CD1 PHE A 215     -44.739  18.611 -19.129  1.00 29.63           C  
ATOM   1611  CD2 PHE A 215     -45.763  17.649 -17.193  1.00 33.02           C  
ATOM   1612  CE1 PHE A 215     -44.757  17.376 -19.734  1.00 29.05           C  
ATOM   1613  CE2 PHE A 215     -45.776  16.418 -17.804  1.00 34.93           C  
ATOM   1614  CZ  PHE A 215     -45.273  16.286 -19.068  1.00 28.48           C  
ATOM   1615  N   ASP A 216     -43.286  22.102 -14.843  1.00 21.70           N  
ATOM   1616  CA  ASP A 216     -43.001  23.428 -14.374  1.00 28.43           C  
ATOM   1617  C   ASP A 216     -44.244  24.326 -14.402  1.00 31.75           C  
ATOM   1618  O   ASP A 216     -44.159  25.507 -14.780  1.00 34.20           O  
ATOM   1619  CB  ASP A 216     -41.885  23.973 -15.251  1.00 30.70           C  
ATOM   1620  CG  ASP A 216     -40.968  24.913 -14.523  1.00 58.07           C  
ATOM   1621  OD1 ASP A 216     -40.803  24.742 -13.313  1.00 71.62           O  
ATOM   1622  OD2 ASP A 216     -40.428  25.804 -15.176  1.00 83.68           O1-
ATOM   1623  N   LEU A 217     -45.393  23.756 -14.017  1.00 27.44           N  
ATOM   1624  CA  LEU A 217     -46.674  24.460 -14.070  1.00 27.84           C  
ATOM   1625  C   LEU A 217     -47.064  24.805 -12.647  1.00 27.78           C  
ATOM   1626  O   LEU A 217     -46.768  24.003 -11.743  1.00 26.69           O  
ATOM   1627  CB  LEU A 217     -47.742  23.571 -14.710  1.00 22.43           C  
ATOM   1628  CG  LEU A 217     -47.506  23.133 -16.149  1.00 21.31           C  
ATOM   1629  CD1 LEU A 217     -48.598  22.188 -16.535  1.00 20.93           C  
ATOM   1630  CD2 LEU A 217     -47.428  24.311 -17.067  1.00 24.17           C  
ATOM   1631  N   THR A 218     -47.624  26.007 -12.393  1.00 24.26           N  
ATOM   1632  CA  THR A 218     -48.068  26.363 -11.024  1.00 27.38           C  
ATOM   1633  C   THR A 218     -49.129  25.382 -10.526  1.00 19.15           C  
ATOM   1634  O   THR A 218     -49.901  24.841 -11.340  1.00 25.68           O  
ATOM   1635  CB  THR A 218     -48.690  27.852 -10.902  1.00 30.12           C  
ATOM   1636  CG2 THR A 218     -47.613  28.823 -10.533  1.00 61.20           C  
ATOM   1637  OG1 THR A 218     -49.312  28.263 -12.099  1.00 46.14           O  
ATOM   1638  N   PRO A 219     -49.247  25.149  -9.221  1.00 21.50           N  
ATOM   1639  CA  PRO A 219     -50.278  24.295  -8.659  1.00 23.92           C  
ATOM   1640  C   PRO A 219     -51.691  24.893  -8.767  1.00 32.60           C  
ATOM   1641  O   PRO A 219     -51.809  26.116  -8.978  1.00 29.02           O  
ATOM   1642  CB  PRO A 219     -49.819  24.102  -7.240  1.00 26.19           C  
ATOM   1643  CG  PRO A 219     -49.066  25.357  -6.913  1.00 25.43           C  
ATOM   1644  CD  PRO A 219     -48.353  25.683  -8.197  1.00 20.73           C  
ATOM   1645  N   VAL A 220     -52.740  24.061  -8.649  1.00 33.44           N  
ATOM   1646  CA  VAL A 220     -54.082  24.613  -8.615  1.00 28.14           C  
ATOM   1647  C   VAL A 220     -54.517  24.659  -7.150  1.00 37.97           C  
ATOM   1648  O   VAL A 220     -54.192  23.785  -6.329  1.00 26.48           O  
ATOM   1649  CB  VAL A 220     -55.138  23.816  -9.534  1.00 32.32           C  
ATOM   1650  CG1 VAL A 220     -54.403  23.043 -10.584  1.00 24.32           C  
ATOM   1651  CG2 VAL A 220     -56.080  22.977  -8.768  1.00 34.39           C  
ATOM   1652  N   ALA A 221     -55.222  25.740  -6.795  1.00 25.77           N  
ATOM   1653  CA  ALA A 221     -55.652  25.964  -5.429  1.00 22.75           C  
ATOM   1654  C   ALA A 221     -56.937  25.232  -5.167  1.00 34.19           C  
ATOM   1655  O   ALA A 221     -58.022  25.821  -5.197  1.00 35.48           O  
ATOM   1656  CB  ALA A 221     -55.846  27.454  -5.210  1.00 25.04           C  
ATOM   1657  N   ALA A 222     -56.818  23.926  -4.940  1.00 25.99           N  
ATOM   1658  CA  ALA A 222     -57.930  23.013  -4.684  1.00 20.53           C  
ATOM   1659  C   ALA A 222     -57.379  21.854  -3.885  1.00 27.31           C  
ATOM   1660  O   ALA A 222     -56.153  21.737  -3.765  1.00 32.70           O  
ATOM   1661  CB  ALA A 222     -58.519  22.395  -5.955  1.00 17.91           C  
ATOM   1662  N   ALA A 223     -58.242  21.041  -3.284  1.00 27.27           N  
ATOM   1663  CA  ALA A 223     -57.842  19.818  -2.589  1.00 33.28           C  
ATOM   1664  C   ALA A 223     -57.217  18.841  -3.611  1.00 43.31           C  
ATOM   1665  O   ALA A 223     -57.605  18.768  -4.804  1.00 26.72           O  
ATOM   1666  CB  ALA A 223     -59.046  19.133  -1.958  1.00 24.82           C  
ATOM   1667  N   ALA A 224     -56.210  18.117  -3.109  1.00 32.68           N  
ATOM   1668  CA  ALA A 224     -55.412  17.217  -3.921  1.00 27.30           C  
ATOM   1669  C   ALA A 224     -56.246  16.175  -4.612  1.00 25.24           C  
ATOM   1670  O   ALA A 224     -57.217  15.634  -4.074  1.00 29.56           O  
ATOM   1671  CB  ALA A 224     -54.413  16.486  -3.056  1.00 25.05           C  
ATOM   1672  N   THR A 225     -55.880  15.903  -5.840  1.00 24.13           N  
ATOM   1673  CA  THR A 225     -56.523  14.843  -6.590  1.00 25.61           C  
ATOM   1674  C   THR A 225     -55.398  14.026  -7.223  1.00 36.20           C  
ATOM   1675  O   THR A 225     -54.256  14.528  -7.281  1.00 26.28           O  
ATOM   1676  CB  THR A 225     -57.454  15.443  -7.702  1.00 32.35           C  
ATOM   1677  CG2 THR A 225     -58.550  16.272  -7.042  1.00 42.70           C  
ATOM   1678  OG1 THR A 225     -56.717  16.290  -8.599  1.00 30.23           O  
ATOM   1679  N   ALA A 226     -55.668  12.814  -7.711  1.00 30.91           N  
ATOM   1680  CA  ALA A 226     -54.653  12.035  -8.420  1.00 36.76           C  
ATOM   1681  C   ALA A 226     -54.871  12.087  -9.937  1.00 34.85           C  
ATOM   1682  O   ALA A 226     -56.025  12.194 -10.352  1.00 40.82           O  
ATOM   1683  CB  ALA A 226     -54.727  10.608  -7.967  1.00 25.21           C  
ATOM   1684  N   VAL A 227     -53.846  12.098 -10.808  1.00 31.55           N  
ATOM   1685  CA  VAL A 227     -53.959  12.040 -12.274  1.00 25.98           C  
ATOM   1686  C   VAL A 227     -53.329  10.734 -12.768  1.00 37.72           C  
ATOM   1687  O   VAL A 227     -52.377  10.259 -12.147  1.00 30.25           O  
ATOM   1688  CB  VAL A 227     -53.236  13.208 -12.987  1.00 26.42           C  
ATOM   1689  CG1 VAL A 227     -54.149  14.400 -12.842  1.00 35.42           C  
ATOM   1690  CG2 VAL A 227     -51.841  13.504 -12.420  1.00 24.43           C  
ATOM   1691  N   ASP A 228     -53.783  10.089 -13.835  1.00 28.65           N  
ATOM   1692  CA  ASP A 228     -53.184   8.838 -14.303  1.00 30.27           C  
ATOM   1693  C   ASP A 228     -52.021   9.149 -15.168  1.00 27.49           C  
ATOM   1694  O   ASP A 228     -52.034  10.177 -15.848  1.00 27.44           O  
ATOM   1695  CB  ASP A 228     -54.162   8.003 -15.137  1.00 29.18           C  
ATOM   1696  CG  ASP A 228     -55.367   7.564 -14.300  1.00 36.93           C  
ATOM   1697  OD1 ASP A 228     -55.186   7.017 -13.205  1.00 60.99           O  
ATOM   1698  OD2 ASP A 228     -56.497   7.804 -14.727  1.00 67.40           O1-
ATOM   1699  N   HIS A 229     -51.003   8.300 -15.211  1.00 27.81           N  
ATOM   1700  CA  HIS A 229     -49.856   8.583 -16.068  1.00 27.57           C  
ATOM   1701  C   HIS A 229     -49.319   7.281 -16.638  1.00 22.47           C  
ATOM   1702  O   HIS A 229     -49.595   6.185 -16.121  1.00 25.44           O  
ATOM   1703  CB  HIS A 229     -48.689   9.278 -15.300  1.00 24.81           C  
ATOM   1704  CG  HIS A 229     -48.044   8.408 -14.188  1.00 25.52           C  
ATOM   1705  CD2 HIS A 229     -46.701   8.039 -14.165  1.00 26.80           C  
ATOM   1706  ND1 HIS A 229     -48.591   7.881 -13.086  1.00 26.06           N  
ATOM   1707  CE1 HIS A 229     -47.665   7.230 -12.412  1.00 31.27           C  
ATOM   1708  NE2 HIS A 229     -46.542   7.338 -13.075  1.00 24.74           N  
ATOM   1709  N   LYS A 230     -48.576   7.457 -17.715  1.00 25.04           N  
ATOM   1710  CA  LYS A 230     -47.833   6.360 -18.232  1.00 31.02           C  
ATOM   1711  C   LYS A 230     -46.509   6.878 -18.718  1.00 29.49           C  
ATOM   1712  O   LYS A 230     -46.368   8.061 -19.002  1.00 24.54           O  
ATOM   1713  CB  LYS A 230     -48.608   5.710 -19.333  1.00 26.28           C  
ATOM   1714  CG  LYS A 230     -48.734   6.344 -20.680  1.00 47.78           C  
ATOM   1715  CD  LYS A 230     -49.849   5.513 -21.361  1.00 73.52           C  
ATOM   1716  CE  LYS A 230     -51.191   5.598 -20.577  1.00 89.17           C  
ATOM   1717  NZ  LYS A 230     -52.166   4.565 -20.898  1.00101.19           N1+
ATOM   1718  N   ALA A 231     -45.507   6.010 -18.736  1.00 28.59           N  
ATOM   1719  CA  ALA A 231     -44.169   6.356 -19.181  1.00 23.31           C  
ATOM   1720  C   ALA A 231     -43.612   5.091 -19.842  1.00 23.75           C  
ATOM   1721  O   ALA A 231     -43.932   3.959 -19.434  1.00 27.95           O  
ATOM   1722  CB  ALA A 231     -43.324   6.722 -17.972  1.00 23.08           C  
ATOM   1723  N   TYR A 232     -42.853   5.216 -20.908  1.00 23.45           N  
ATOM   1724  CA  TYR A 232     -42.207   4.060 -21.523  1.00 32.26           C  
ATOM   1725  C   TYR A 232     -40.991   4.535 -22.308  1.00 29.25           C  
ATOM   1726  O   TYR A 232     -40.900   5.721 -22.663  1.00 27.46           O  
ATOM   1727  CB  TYR A 232     -43.192   3.280 -22.444  1.00 28.02           C  
ATOM   1728  CG  TYR A 232     -44.049   4.148 -23.347  1.00 27.17           C  
ATOM   1729  CD1 TYR A 232     -45.253   4.614 -22.846  1.00 35.93           C  
ATOM   1730  CD2 TYR A 232     -43.621   4.488 -24.619  1.00 30.56           C  
ATOM   1731  CE1 TYR A 232     -46.034   5.439 -23.622  1.00 40.00           C  
ATOM   1732  CE2 TYR A 232     -44.408   5.310 -25.411  1.00 39.00           C  
ATOM   1733  CZ  TYR A 232     -45.611   5.781 -24.898  1.00 38.48           C  
ATOM   1734  OH  TYR A 232     -46.406   6.636 -25.658  1.00 56.10           O  
ATOM   1735  N   GLY A 233     -39.990   3.687 -22.570  1.00 22.51           N  
ATOM   1736  CA  GLY A 233     -38.803   4.111 -23.286  1.00 24.02           C  
ATOM   1737  C   GLY A 233     -37.939   2.920 -23.680  1.00 26.25           C  
ATOM   1738  O   GLY A 233     -38.172   1.762 -23.324  1.00 24.83           O  
ATOM   1739  N   LEU A 234     -36.916   3.254 -24.402  1.00 25.95           N  
ATOM   1740  CA  LEU A 234     -36.065   2.242 -24.956  1.00 24.03           C  
ATOM   1741  C   LEU A 234     -34.685   2.817 -25.152  1.00 28.04           C  
ATOM   1742  O   LEU A 234     -34.598   4.015 -25.491  1.00 28.24           O  
ATOM   1743  CB  LEU A 234     -36.640   1.868 -26.276  1.00 31.10           C  
ATOM   1744  CG  LEU A 234     -35.750   1.130 -27.225  1.00 41.38           C  
ATOM   1745  CD1 LEU A 234     -35.694  -0.338 -26.811  1.00 34.15           C  
ATOM   1746  CD2 LEU A 234     -36.252   1.351 -28.615  1.00 42.03           C  
ATOM   1747  N   SER A 235     -33.613   2.026 -24.944  1.00 26.13           N  
ATOM   1748  CA  SER A 235     -32.316   2.494 -25.384  1.00 25.83           C  
ATOM   1749  C   SER A 235     -31.556   1.344 -26.019  1.00 25.93           C  
ATOM   1750  O   SER A 235     -31.815   0.169 -25.689  1.00 28.39           O  
ATOM   1751  CB  SER A 235     -31.430   3.054 -24.251  1.00 32.71           C  
ATOM   1752  OG  SER A 235     -31.011   2.189 -23.225  1.00 30.62           O  
ATOM   1753  N   VAL A 236     -30.639   1.741 -26.905  1.00 24.17           N  
ATOM   1754  CA  VAL A 236     -29.804   0.801 -27.617  1.00 35.92           C  
ATOM   1755  C   VAL A 236     -28.398   1.374 -27.596  1.00 30.98           C  
ATOM   1756  O   VAL A 236     -28.225   2.561 -27.914  1.00 29.40           O  
ATOM   1757  CB  VAL A 236     -30.248   0.635 -29.114  1.00 37.21           C  
ATOM   1758  CG1 VAL A 236     -29.377  -0.429 -29.785  1.00 36.84           C  
ATOM   1759  CG2 VAL A 236     -31.665   0.133 -29.227  1.00 26.11           C  
ATOM   1760  N   ASP A 237     -27.378   0.589 -27.232  1.00 32.91           N  
ATOM   1761  CA  ASP A 237     -26.004   1.037 -27.419  1.00 25.51           C  
ATOM   1762  C   ASP A 237     -25.198  -0.144 -27.943  1.00 35.12           C  
ATOM   1763  O   ASP A 237     -25.531  -1.298 -27.620  1.00 26.89           O  
ATOM   1764  CB  ASP A 237     -25.370   1.512 -26.129  1.00 18.52           C  
ATOM   1765  CG  ASP A 237     -25.303   0.540 -24.983  1.00 30.05           C  
ATOM   1766  OD1 ASP A 237     -26.265   0.410 -24.236  1.00 32.68           O  
ATOM   1767  OD2 ASP A 237     -24.255  -0.069 -24.822  1.00 32.21           O1-
ATOM   1768  N   SER A 238     -24.172   0.115 -28.726  1.00 26.63           N  
ATOM   1769  CA  SER A 238     -23.363  -0.952 -29.261  1.00 37.70           C  
ATOM   1770  C   SER A 238     -21.933  -0.508 -29.315  1.00 32.20           C  
ATOM   1771  O   SER A 238     -21.629   0.661 -29.600  1.00 31.51           O  
ATOM   1772  CB  SER A 238     -23.807  -1.312 -30.664  1.00 41.15           C  
ATOM   1773  OG  SER A 238     -23.270  -2.592 -31.002  1.00 71.90           O  
ATOM   1774  N   THR A 239     -21.064  -1.474 -29.052  1.00 36.96           N  
ATOM   1775  CA  THR A 239     -19.636  -1.217 -29.077  1.00 32.71           C  
ATOM   1776  C   THR A 239     -18.909  -1.904 -30.227  1.00 36.75           C  
ATOM   1777  O   THR A 239     -19.033  -3.114 -30.413  1.00 49.53           O  
ATOM   1778  CB  THR A 239     -19.054  -1.671 -27.752  1.00 32.24           C  
ATOM   1779  CG2 THR A 239     -17.590  -1.318 -27.637  1.00 43.12           C  
ATOM   1780  OG1 THR A 239     -19.755  -1.006 -26.709  1.00 37.41           O  
ATOM   1781  N   PHE A 240     -18.145  -1.145 -30.989  1.00 32.39           N  
ATOM   1782  CA  PHE A 240     -17.287  -1.637 -32.066  1.00 34.60           C  
ATOM   1783  C   PHE A 240     -15.858  -1.120 -31.826  1.00 35.95           C  
ATOM   1784  O   PHE A 240     -15.483   0.031 -32.133  1.00 35.29           O  
ATOM   1785  CB  PHE A 240     -17.715  -1.145 -33.467  1.00 44.97           C  
ATOM   1786  CG  PHE A 240     -18.898  -0.188 -33.539  1.00 76.78           C  
ATOM   1787  CD1 PHE A 240     -20.191  -0.684 -33.409  1.00 80.80           C  
ATOM   1788  CD2 PHE A 240     -18.667   1.160 -33.747  1.00 80.91           C  
ATOM   1789  CE1 PHE A 240     -21.264   0.172 -33.491  1.00 68.89           C  
ATOM   1790  CE2 PHE A 240     -19.750   2.010 -33.828  1.00 82.55           C  
ATOM   1791  CZ  PHE A 240     -21.038   1.514 -33.699  1.00 81.89           C  
ATOM   1792  N   GLY A 241     -15.042  -1.974 -31.216  1.00 34.25           N  
ATOM   1793  CA  GLY A 241     -13.678  -1.613 -30.925  1.00 33.96           C  
ATOM   1794  C   GLY A 241     -13.609  -0.715 -29.689  1.00 29.52           C  
ATOM   1795  O   GLY A 241     -14.049  -1.073 -28.588  1.00 42.22           O  
ATOM   1796  N   ALA A 242     -13.020   0.458 -29.898  1.00 36.46           N  
ATOM   1797  CA  ALA A 242     -12.916   1.463 -28.853  1.00 38.95           C  
ATOM   1798  C   ALA A 242     -14.159   2.376 -28.822  1.00 32.64           C  
ATOM   1799  O   ALA A 242     -14.273   3.167 -27.887  1.00 34.81           O  
ATOM   1800  CB  ALA A 242     -11.665   2.295 -29.123  1.00 29.62           C  
ATOM   1801  N   THR A 243     -15.087   2.296 -29.789  1.00 28.72           N  
ATOM   1802  CA  THR A 243     -16.234   3.173 -29.948  1.00 32.77           C  
ATOM   1803  C   THR A 243     -17.530   2.598 -29.475  1.00 38.01           C  
ATOM   1804  O   THR A 243     -17.931   1.534 -29.945  1.00 34.60           O  
ATOM   1805  CB  THR A 243     -16.432   3.555 -31.418  1.00 29.34           C  
ATOM   1806  CG2 THR A 243     -17.447   4.662 -31.636  1.00 36.27           C  
ATOM   1807  OG1 THR A 243     -15.174   4.034 -31.874  1.00 38.80           O  
ATOM   1808  N   THR A 244     -18.191   3.280 -28.551  1.00 27.70           N  
ATOM   1809  CA  THR A 244     -19.557   2.917 -28.212  1.00 21.95           C  
ATOM   1810  C   THR A 244     -20.425   4.052 -28.756  1.00 38.04           C  
ATOM   1811  O   THR A 244     -20.019   5.230 -28.742  1.00 29.47           O  
ATOM   1812  CB  THR A 244     -19.695   2.817 -26.742  1.00 27.11           C  
ATOM   1813  CG2 THR A 244     -21.134   2.549 -26.303  1.00 22.16           C  
ATOM   1814  OG1 THR A 244     -18.764   1.797 -26.363  1.00 30.63           O  
ATOM   1815  N   VAL A 245     -21.568   3.670 -29.318  1.00 32.84           N  
ATOM   1816  CA  VAL A 245     -22.566   4.579 -29.882  1.00 23.59           C  
ATOM   1817  C   VAL A 245     -23.877   4.114 -29.271  1.00 30.46           C  
ATOM   1818  O   VAL A 245     -24.078   2.908 -29.066  1.00 28.97           O  
ATOM   1819  CB  VAL A 245     -22.615   4.464 -31.418  1.00 26.50           C  
ATOM   1820  CG1 VAL A 245     -23.753   5.279 -32.012  1.00 42.06           C  
ATOM   1821  CG2 VAL A 245     -21.345   5.074 -31.982  1.00 29.56           C  
ATOM   1822  N   GLY A 246     -24.734   5.063 -28.881  1.00 30.97           N  
ATOM   1823  CA  GLY A 246     -26.000   4.698 -28.279  1.00 28.37           C  
ATOM   1824  C   GLY A 246     -26.979   5.860 -28.144  1.00 31.52           C  
ATOM   1825  O   GLY A 246     -26.599   7.026 -28.340  1.00 29.24           O  
ATOM   1826  N   GLY A 247     -28.221   5.556 -27.778  1.00 26.92           N  
ATOM   1827  CA  GLY A 247     -29.212   6.589 -27.628  1.00 25.58           C  
ATOM   1828  C   GLY A 247     -30.412   6.020 -26.938  1.00 36.99           C  
ATOM   1829  O   GLY A 247     -30.461   4.810 -26.710  1.00 25.32           O  
ATOM   1830  N   TYR A 248     -31.398   6.864 -26.627  1.00 23.62           N  
ATOM   1831  CA  TYR A 248     -32.582   6.411 -25.930  1.00 20.94           C  
ATOM   1832  C   TYR A 248     -33.747   7.315 -26.350  1.00 20.63           C  
ATOM   1833  O   TYR A 248     -33.502   8.424 -26.870  1.00 21.90           O  
ATOM   1834  CB  TYR A 248     -32.380   6.505 -24.401  1.00 21.56           C  
ATOM   1835  CG  TYR A 248     -32.172   7.930 -23.876  1.00 25.21           C  
ATOM   1836  CD1 TYR A 248     -33.288   8.700 -23.583  1.00 27.92           C  
ATOM   1837  CD2 TYR A 248     -30.914   8.506 -23.762  1.00 24.90           C  
ATOM   1838  CE1 TYR A 248     -33.148  10.023 -23.189  1.00 26.26           C  
ATOM   1839  CE2 TYR A 248     -30.768   9.840 -23.365  1.00 31.70           C  
ATOM   1840  CZ  TYR A 248     -31.902  10.608 -23.073  1.00 26.70           C  
ATOM   1841  OH  TYR A 248     -31.836  11.948 -22.674  1.00 25.24           O  
ATOM   1842  N   VAL A 249     -34.979   6.892 -26.102  1.00 24.77           N  
ATOM   1843  CA  VAL A 249     -36.128   7.781 -26.279  1.00 27.74           C  
ATOM   1844  C   VAL A 249     -37.118   7.351 -25.211  1.00 28.50           C  
ATOM   1845  O   VAL A 249     -37.261   6.165 -24.877  1.00 24.37           O  
ATOM   1846  CB  VAL A 249     -36.711   7.674 -27.727  1.00 30.76           C  
ATOM   1847  CG1 VAL A 249     -37.290   6.307 -28.007  1.00 36.77           C  
ATOM   1848  CG2 VAL A 249     -37.798   8.730 -27.880  1.00 29.16           C  
ATOM   1849  N   GLN A 250     -37.730   8.333 -24.550  1.00 22.78           N  
ATOM   1850  CA  GLN A 250     -38.664   8.051 -23.493  1.00 23.77           C  
ATOM   1851  C   GLN A 250     -39.850   8.983 -23.715  1.00 25.06           C  
ATOM   1852  O   GLN A 250     -39.693  10.057 -24.326  1.00 21.33           O  
ATOM   1853  CB  GLN A 250     -38.128   8.387 -22.113  1.00 23.22           C  
ATOM   1854  CG  GLN A 250     -36.748   7.905 -21.837  1.00 24.76           C  
ATOM   1855  CD  GLN A 250     -36.502   7.854 -20.358  1.00 18.99           C  
ATOM   1856  NE2 GLN A 250     -35.484   8.495 -19.827  1.00 20.19           N  
ATOM   1857  OE1 GLN A 250     -37.245   7.230 -19.618  1.00 23.92           O  
ATOM   1858  N   VAL A 251     -41.028   8.550 -23.279  1.00 29.03           N  
ATOM   1859  CA  VAL A 251     -42.139   9.470 -23.261  1.00 26.98           C  
ATOM   1860  C   VAL A 251     -42.813   9.309 -21.927  1.00 25.15           C  
ATOM   1861  O   VAL A 251     -42.883   8.246 -21.285  1.00 26.27           O  
ATOM   1862  CB  VAL A 251     -43.186   9.291 -24.463  1.00 33.15           C  
ATOM   1863  CG1 VAL A 251     -42.636   8.362 -25.496  1.00 26.27           C  
ATOM   1864  CG2 VAL A 251     -44.539   8.908 -23.963  1.00 32.70           C  
ATOM   1865  N   LEU A 252     -43.246  10.495 -21.487  1.00 23.70           N  
ATOM   1866  CA  LEU A 252     -43.987  10.590 -20.247  1.00 21.27           C  
ATOM   1867  C   LEU A 252     -45.301  11.242 -20.655  1.00 26.27           C  
ATOM   1868  O   LEU A 252     -45.268  12.262 -21.345  1.00 26.01           O  
ATOM   1869  CB  LEU A 252     -43.239  11.463 -19.291  1.00 22.83           C  
ATOM   1870  CG  LEU A 252     -43.931  11.833 -17.998  1.00 32.44           C  
ATOM   1871  CD1 LEU A 252     -44.323  10.613 -17.182  1.00 25.21           C  
ATOM   1872  CD2 LEU A 252     -42.983  12.780 -17.287  1.00 28.50           C  
ATOM   1873  N   ASP A 253     -46.413  10.647 -20.267  1.00 25.12           N  
ATOM   1874  CA  ASP A 253     -47.733  11.100 -20.657  1.00 34.71           C  
ATOM   1875  C   ASP A 253     -48.618  11.231 -19.416  1.00 25.50           C  
ATOM   1876  O   ASP A 253     -49.068  10.205 -18.877  1.00 26.91           O  
ATOM   1877  CB  ASP A 253     -48.243  10.057 -21.646  1.00 31.51           C  
ATOM   1878  CG  ASP A 253     -49.546  10.329 -22.395  1.00 52.04           C  
ATOM   1879  OD1 ASP A 253     -50.294  11.213 -21.979  1.00 49.77           O  
ATOM   1880  OD2 ASP A 253     -49.803   9.647 -23.399  1.00 67.89           O1-
ATOM   1881  N   ILE A 254     -48.916  12.436 -18.913  1.00 24.18           N  
ATOM   1882  CA  ILE A 254     -49.735  12.554 -17.727  1.00 23.34           C  
ATOM   1883  C   ILE A 254     -51.053  13.165 -18.161  1.00 30.07           C  
ATOM   1884  O   ILE A 254     -51.128  14.280 -18.703  1.00 29.61           O  
ATOM   1885  CB  ILE A 254     -49.120  13.458 -16.680  1.00 20.78           C  
ATOM   1886  CG1 ILE A 254     -47.666  12.994 -16.385  1.00 23.54           C  
ATOM   1887  CG2 ILE A 254     -50.004  13.391 -15.427  1.00 20.01           C  
ATOM   1888  CD1 ILE A 254     -46.868  13.847 -15.387  1.00 30.48           C  
ATOM   1889  N   ASP A 255     -52.052  12.357 -17.880  1.00 27.10           N  
ATOM   1890  CA  ASP A 255     -53.428  12.649 -18.202  1.00 37.11           C  
ATOM   1891  C   ASP A 255     -53.851  13.957 -17.531  1.00 34.48           C  
ATOM   1892  O   ASP A 255     -53.587  14.208 -16.350  1.00 33.20           O  
ATOM   1893  CB  ASP A 255     -54.295  11.502 -17.710  1.00 36.96           C  
ATOM   1894  CG  ASP A 255     -55.767  11.581 -18.120  1.00 61.77           C  
ATOM   1895  OD1 ASP A 255     -56.055  11.881 -19.283  1.00 63.74           O  
ATOM   1896  OD2 ASP A 255     -56.627  11.335 -17.276  1.00 54.70           O1-
ATOM   1897  N   THR A 256     -54.484  14.762 -18.389  1.00 38.04           N  
ATOM   1898  CA  THR A 256     -55.021  16.083 -18.107  1.00 27.79           C  
ATOM   1899  C   THR A 256     -53.890  17.091 -17.965  1.00 45.76           C  
ATOM   1900  O   THR A 256     -54.215  18.274 -17.891  1.00 49.10           O  
ATOM   1901  CB  THR A 256     -55.925  16.197 -16.795  1.00 37.48           C  
ATOM   1902  CG2 THR A 256     -56.921  15.067 -16.657  1.00 36.65           C  
ATOM   1903  OG1 THR A 256     -55.095  16.193 -15.663  1.00 37.65           O  
ATOM   1904  N   ILE A 257     -52.580  16.776 -17.938  1.00 46.16           N  
ATOM   1905  CA  ILE A 257     -51.544  17.804 -17.776  1.00 36.33           C  
ATOM   1906  C   ILE A 257     -50.870  17.899 -19.110  1.00 45.12           C  
ATOM   1907  O   ILE A 257     -51.196  18.802 -19.869  1.00 39.40           O  
ATOM   1908  CB  ILE A 257     -50.466  17.454 -16.690  1.00 30.69           C  
ATOM   1909  CG1 ILE A 257     -51.139  17.090 -15.367  1.00 26.95           C  
ATOM   1910  CG2 ILE A 257     -49.463  18.600 -16.599  1.00 28.34           C  
ATOM   1911  CD1 ILE A 257     -52.152  18.060 -14.787  1.00 47.06           C  
ATOM   1912  N   ASP A 258     -49.986  16.970 -19.476  1.00 26.70           N  
ATOM   1913  CA  ASP A 258     -49.267  17.071 -20.726  1.00 20.95           C  
ATOM   1914  C   ASP A 258     -48.478  15.755 -20.966  1.00 21.68           C  
ATOM   1915  O   ASP A 258     -48.530  14.857 -20.127  1.00 25.33           O  
ATOM   1916  CB  ASP A 258     -48.311  18.275 -20.661  1.00 24.31           C  
ATOM   1917  CG  ASP A 258     -47.987  18.910 -22.029  1.00 39.02           C  
ATOM   1918  OD1 ASP A 258     -48.441  18.431 -23.091  1.00 36.22           O  
ATOM   1919  OD2 ASP A 258     -47.263  19.913 -22.039  1.00 49.23           O1-
ATOM   1920  N   ASP A 259     -47.806  15.659 -22.111  1.00 32.03           N  
ATOM   1921  CA  ASP A 259     -46.945  14.561 -22.495  1.00 35.51           C  
ATOM   1922  C   ASP A 259     -45.660  15.169 -23.018  1.00 29.00           C  
ATOM   1923  O   ASP A 259     -45.625  16.347 -23.386  1.00 29.90           O  
ATOM   1924  CB  ASP A 259     -47.559  13.686 -23.592  1.00 29.16           C  
ATOM   1925  CG  ASP A 259     -48.013  14.401 -24.866  1.00 32.42           C  
ATOM   1926  OD1 ASP A 259     -47.186  14.792 -25.676  1.00 53.80           O  
ATOM   1927  OD2 ASP A 259     -49.215  14.563 -25.045  1.00 66.04           O1-
ATOM   1928  N   VAL A 260     -44.568  14.416 -23.012  1.00 23.61           N  
ATOM   1929  CA  VAL A 260     -43.310  14.884 -23.561  1.00 21.31           C  
ATOM   1930  C   VAL A 260     -42.586  13.612 -24.033  1.00 25.64           C  
ATOM   1931  O   VAL A 260     -42.772  12.521 -23.476  1.00 25.09           O  
ATOM   1932  CB  VAL A 260     -42.534  15.664 -22.438  1.00 21.65           C  
ATOM   1933  CG1 VAL A 260     -42.261  14.810 -21.191  1.00 22.43           C  
ATOM   1934  CG2 VAL A 260     -41.262  16.200 -23.064  1.00 23.25           C  
ATOM   1935  N   THR A 261     -41.853  13.771 -25.127  1.00 26.37           N  
ATOM   1936  CA  THR A 261     -40.946  12.772 -25.651  1.00 29.83           C  
ATOM   1937  C   THR A 261     -39.575  13.441 -25.568  1.00 28.17           C  
ATOM   1938  O   THR A 261     -39.377  14.578 -26.024  1.00 27.71           O  
ATOM   1939  CB  THR A 261     -41.298  12.418 -27.117  1.00 28.09           C  
ATOM   1940  CG2 THR A 261     -40.219  11.547 -27.801  1.00 25.84           C  
ATOM   1941  OG1 THR A 261     -42.582  11.777 -27.062  1.00 29.64           O  
ATOM   1942  N   TYR A 262     -38.616  12.744 -24.963  1.00 29.21           N  
ATOM   1943  CA  TYR A 262     -37.279  13.277 -24.748  1.00 24.79           C  
ATOM   1944  C   TYR A 262     -36.306  12.163 -25.139  1.00 23.96           C  
ATOM   1945  O   TYR A 262     -36.616  10.965 -25.049  1.00 24.24           O  
ATOM   1946  CB  TYR A 262     -37.134  13.703 -23.267  1.00 24.82           C  
ATOM   1947  CG  TYR A 262     -37.637  12.802 -22.133  1.00 25.17           C  
ATOM   1948  CD1 TYR A 262     -38.984  12.509 -21.906  1.00 21.56           C  
ATOM   1949  CD2 TYR A 262     -36.702  12.303 -21.241  1.00 32.68           C  
ATOM   1950  CE1 TYR A 262     -39.379  11.746 -20.808  1.00 28.66           C  
ATOM   1951  CE2 TYR A 262     -37.089  11.544 -20.133  1.00 24.26           C  
ATOM   1952  CZ  TYR A 262     -38.421  11.271 -19.919  1.00 29.01           C  
ATOM   1953  OH  TYR A 262     -38.771  10.553 -18.801  1.00 26.50           O  
ATOM   1954  N   TYR A 263     -35.175  12.555 -25.668  1.00 22.32           N  
ATOM   1955  CA  TYR A 263     -34.274  11.582 -26.237  1.00 30.67           C  
ATOM   1956  C   TYR A 263     -32.839  12.116 -26.246  1.00 32.19           C  
ATOM   1957  O   TYR A 263     -32.587  13.307 -26.040  1.00 24.76           O  
ATOM   1958  CB  TYR A 263     -34.795  11.247 -27.657  1.00 25.45           C  
ATOM   1959  CG  TYR A 263     -34.708  12.440 -28.573  1.00 36.72           C  
ATOM   1960  CD1 TYR A 263     -33.490  12.654 -29.204  1.00 42.51           C  
ATOM   1961  CD2 TYR A 263     -35.773  13.323 -28.675  1.00 40.64           C  
ATOM   1962  CE1 TYR A 263     -33.274  13.777 -29.943  1.00 50.49           C  
ATOM   1963  CE2 TYR A 263     -35.564  14.460 -29.420  1.00 36.33           C  
ATOM   1964  CZ  TYR A 263     -34.315  14.671 -30.031  1.00 50.61           C  
ATOM   1965  OH  TYR A 263     -34.044  15.851 -30.714  1.00 80.92           O  
ATOM   1966  N   GLY A 264     -31.858  11.284 -26.557  1.00 25.91           N  
ATOM   1967  CA  GLY A 264     -30.460  11.664 -26.603  1.00 21.27           C  
ATOM   1968  C   GLY A 264     -29.699  10.599 -27.390  1.00 23.07           C  
ATOM   1969  O   GLY A 264     -30.144   9.449 -27.530  1.00 25.86           O  
ATOM   1970  N   LEU A 265     -28.569  11.042 -27.884  1.00 23.56           N  
ATOM   1971  CA  LEU A 265     -27.733  10.269 -28.777  1.00 26.65           C  
ATOM   1972  C   LEU A 265     -26.297  10.684 -28.436  1.00 27.04           C  
ATOM   1973  O   LEU A 265     -25.961  11.890 -28.402  1.00 23.67           O  
ATOM   1974  CB  LEU A 265     -28.046  10.652 -30.239  1.00 27.27           C  
ATOM   1975  CG  LEU A 265     -28.305   9.644 -31.340  1.00 60.41           C  
ATOM   1976  CD1 LEU A 265     -27.141   8.656 -31.468  1.00 50.33           C  
ATOM   1977  CD2 LEU A 265     -29.609   8.923 -31.016  1.00 66.28           C  
ATOM   1978  N   GLY A 266     -25.418   9.720 -28.158  1.00 24.66           N  
ATOM   1979  CA  GLY A 266     -24.030  10.067 -27.890  1.00 28.90           C  
ATOM   1980  C   GLY A 266     -23.051   8.952 -28.218  1.00 30.41           C  
ATOM   1981  O   GLY A 266     -23.436   7.816 -28.524  1.00 27.92           O  
ATOM   1982  N   ALA A 267     -21.782   9.286 -28.127  1.00 24.95           N  
ATOM   1983  CA  ALA A 267     -20.746   8.320 -28.390  1.00 33.88           C  
ATOM   1984  C   ALA A 267     -19.609   8.488 -27.429  1.00 31.63           C  
ATOM   1985  O   ALA A 267     -19.424   9.578 -26.879  1.00 24.94           O  
ATOM   1986  CB  ALA A 267     -20.160   8.509 -29.762  1.00 24.74           C  
ATOM   1987  N   SER A 268     -18.832   7.427 -27.262  1.00 29.24           N  
ATOM   1988  CA  SER A 268     -17.581   7.542 -26.550  1.00 25.82           C  
ATOM   1989  C   SER A 268     -16.513   6.747 -27.268  1.00 31.52           C  
ATOM   1990  O   SER A 268     -16.804   5.766 -27.955  1.00 28.68           O  
ATOM   1991  CB  SER A 268     -17.716   7.037 -25.112  1.00 24.92           C  
ATOM   1992  OG  SER A 268     -18.579   5.930 -24.945  1.00 39.59           O  
ATOM   1993  N   TYR A 269     -15.298   7.175 -27.055  1.00 26.59           N  
ATOM   1994  CA  TYR A 269     -14.152   6.549 -27.621  1.00 25.66           C  
ATOM   1995  C   TYR A 269     -13.198   6.260 -26.487  1.00 25.81           C  
ATOM   1996  O   TYR A 269     -12.698   7.171 -25.825  1.00 25.05           O  
ATOM   1997  CB  TYR A 269     -13.572   7.509 -28.604  1.00 23.54           C  
ATOM   1998  CG  TYR A 269     -12.408   6.853 -29.294  1.00 33.37           C  
ATOM   1999  CD1 TYR A 269     -12.647   5.990 -30.345  1.00 29.64           C  
ATOM   2000  CD2 TYR A 269     -11.134   7.071 -28.819  1.00 39.37           C  
ATOM   2001  CE1 TYR A 269     -11.581   5.327 -30.925  1.00 52.56           C  
ATOM   2002  CE2 TYR A 269     -10.071   6.407 -29.389  1.00 51.57           C  
ATOM   2003  CZ  TYR A 269     -10.300   5.538 -30.441  1.00 58.86           C  
ATOM   2004  OH  TYR A 269      -9.224   4.871 -31.009  1.00 61.25           O  
ATOM   2005  N   ASP A 270     -12.869   5.010 -26.259  1.00 22.56           N  
ATOM   2006  CA  ASP A 270     -11.983   4.653 -25.173  1.00 20.61           C  
ATOM   2007  C   ASP A 270     -10.509   4.881 -25.532  1.00 29.68           C  
ATOM   2008  O   ASP A 270     -10.026   4.335 -26.524  1.00 34.39           O  
ATOM   2009  CB  ASP A 270     -12.283   3.188 -24.839  1.00 24.95           C  
ATOM   2010  CG  ASP A 270     -11.661   2.632 -23.564  1.00 33.53           C  
ATOM   2011  OD1 ASP A 270     -10.800   3.287 -22.989  1.00 33.68           O  
ATOM   2012  OD2 ASP A 270     -12.056   1.548 -23.123  1.00 54.40           O1-
ATOM   2013  N   LEU A 271      -9.769   5.672 -24.763  1.00 24.09           N  
ATOM   2014  CA  LEU A 271      -8.351   5.919 -24.974  1.00 21.32           C  
ATOM   2015  C   LEU A 271      -7.505   4.932 -24.158  1.00 23.96           C  
ATOM   2016  O   LEU A 271      -6.285   4.976 -24.202  1.00 23.54           O  
ATOM   2017  CB  LEU A 271      -7.959   7.313 -24.520  1.00 19.85           C  
ATOM   2018  CG  LEU A 271      -8.637   8.530 -25.152  1.00 23.59           C  
ATOM   2019  CD1 LEU A 271      -8.130   9.813 -24.516  1.00 24.13           C  
ATOM   2020  CD2 LEU A 271      -8.354   8.541 -26.609  1.00 25.97           C  
ATOM   2021  N   GLY A 272      -8.119   4.124 -23.322  1.00 21.11           N  
ATOM   2022  CA  GLY A 272      -7.462   3.204 -22.441  1.00 20.61           C  
ATOM   2023  C   GLY A 272      -6.982   3.853 -21.158  1.00 23.49           C  
ATOM   2024  O   GLY A 272      -6.926   5.078 -21.043  1.00 26.07           O  
ATOM   2025  N   GLY A 273      -6.663   3.072 -20.125  1.00 16.10           N  
ATOM   2026  CA  GLY A 273      -6.027   3.601 -18.943  1.00 15.88           C  
ATOM   2027  C   GLY A 273      -7.021   4.304 -18.014  1.00 23.40           C  
ATOM   2028  O   GLY A 273      -6.618   4.770 -16.957  1.00 24.50           O  
ATOM   2029  N   GLY A 274      -8.320   4.321 -18.343  1.00 27.38           N  
ATOM   2030  CA  GLY A 274      -9.358   4.975 -17.542  1.00 27.44           C  
ATOM   2031  C   GLY A 274      -9.836   6.285 -18.194  1.00 31.13           C  
ATOM   2032  O   GLY A 274     -10.561   7.026 -17.538  1.00 26.17           O  
ATOM   2033  N   ALA A 275      -9.464   6.610 -19.432  1.00 21.61           N  
ATOM   2034  CA  ALA A 275      -9.841   7.847 -20.081  1.00 21.23           C  
ATOM   2035  C   ALA A 275     -10.632   7.571 -21.339  1.00 31.65           C  
ATOM   2036  O   ALA A 275     -10.389   6.577 -22.031  1.00 22.67           O  
ATOM   2037  CB  ALA A 275      -8.604   8.651 -20.454  1.00 16.02           C  
ATOM   2038  N   SER A 276     -11.630   8.406 -21.635  1.00 19.43           N  
ATOM   2039  CA  SER A 276     -12.425   8.297 -22.840  1.00 19.76           C  
ATOM   2040  C   SER A 276     -12.866   9.697 -23.300  1.00 25.83           C  
ATOM   2041  O   SER A 276     -12.920  10.634 -22.488  1.00 23.50           O  
ATOM   2042  CB  SER A 276     -13.645   7.385 -22.581  1.00 21.87           C  
ATOM   2043  OG  SER A 276     -14.358   7.658 -21.384  1.00 34.39           O  
ATOM   2044  N   ILE A 277     -13.071   9.888 -24.594  1.00 22.23           N  
ATOM   2045  CA  ILE A 277     -13.562  11.134 -25.164  1.00 22.99           C  
ATOM   2046  C   ILE A 277     -15.045  10.841 -25.297  1.00 28.21           C  
ATOM   2047  O   ILE A 277     -15.417   9.768 -25.802  1.00 23.58           O  
ATOM   2048  CB  ILE A 277     -12.901  11.369 -26.527  1.00 26.04           C  
ATOM   2049  CG1 ILE A 277     -11.438  11.608 -26.349  1.00 28.06           C  
ATOM   2050  CG2 ILE A 277     -13.500  12.598 -27.213  1.00 24.61           C  
ATOM   2051  CD1 ILE A 277     -10.740  11.567 -27.721  1.00 28.49           C  
ATOM   2052  N   VAL A 278     -15.950  11.706 -24.812  1.00 24.26           N  
ATOM   2053  CA  VAL A 278     -17.399  11.425 -24.775  1.00 25.14           C  
ATOM   2054  C   VAL A 278     -18.133  12.686 -25.249  1.00 25.78           C  
ATOM   2055  O   VAL A 278     -17.758  13.802 -24.877  1.00 23.74           O  
ATOM   2056  CB  VAL A 278     -17.890  11.099 -23.336  1.00 22.54           C  
ATOM   2057  CG1 VAL A 278     -19.289  10.562 -23.416  1.00 18.27           C  
ATOM   2058  CG2 VAL A 278     -17.003  10.092 -22.652  1.00 24.97           C  
ATOM   2059  N   GLY A 279     -19.177  12.567 -26.043  1.00 22.69           N  
ATOM   2060  CA  GLY A 279     -19.933  13.716 -26.515  1.00 23.27           C  
ATOM   2061  C   GLY A 279     -21.350  13.257 -26.768  1.00 25.33           C  
ATOM   2062  O   GLY A 279     -21.598  12.049 -26.880  1.00 26.35           O  
ATOM   2063  N   GLY A 280     -22.335  14.143 -26.857  1.00 22.79           N  
ATOM   2064  CA  GLY A 280     -23.710  13.713 -27.055  1.00 23.14           C  
ATOM   2065  C   GLY A 280     -24.613  14.912 -27.302  1.00 20.25           C  
ATOM   2066  O   GLY A 280     -24.181  16.061 -27.213  1.00 22.34           O  
ATOM   2067  N   ILE A 281     -25.841  14.589 -27.605  1.00 18.86           N  
ATOM   2068  CA  ILE A 281     -26.848  15.549 -27.981  1.00 27.28           C  
ATOM   2069  C   ILE A 281     -28.090  15.095 -27.229  1.00 24.01           C  
ATOM   2070  O   ILE A 281     -28.306  13.886 -27.063  1.00 25.84           O  
ATOM   2071  CB  ILE A 281     -26.866  15.451 -29.555  1.00 34.33           C  
ATOM   2072  CG1 ILE A 281     -26.675  16.837 -29.973  1.00 32.29           C  
ATOM   2073  CG2 ILE A 281     -28.084  14.857 -30.243  1.00 32.21           C  
ATOM   2074  CD1 ILE A 281     -25.189  17.130 -30.108  1.00 41.67           C  
ATOM   2075  N   ALA A 282     -28.927  15.997 -26.695  1.00 25.05           N  
ATOM   2076  CA  ALA A 282     -30.160  15.580 -26.038  1.00 21.98           C  
ATOM   2077  C   ALA A 282     -31.220  16.681 -26.222  1.00 30.82           C  
ATOM   2078  O   ALA A 282     -30.912  17.881 -26.350  1.00 25.28           O  
ATOM   2079  CB  ALA A 282     -29.970  15.370 -24.537  1.00 19.90           C  
ATOM   2080  N   ASP A 283     -32.486  16.272 -26.245  1.00 29.24           N  
ATOM   2081  CA  ASP A 283     -33.595  17.198 -26.404  1.00 27.15           C  
ATOM   2082  C   ASP A 283     -34.926  16.606 -26.022  1.00 28.94           C  
ATOM   2083  O   ASP A 283     -35.040  15.445 -25.601  1.00 25.65           O  
ATOM   2084  CB  ASP A 283     -33.650  17.641 -27.843  1.00 25.99           C  
ATOM   2085  CG  ASP A 283     -34.266  19.014 -28.054  1.00 44.57           C  
ATOM   2086  OD1 ASP A 283     -34.699  19.714 -27.115  1.00 33.69           O  
ATOM   2087  OD2 ASP A 283     -34.273  19.364 -29.224  1.00 35.12           O1-
ATOM   2088  N   ASN A 284     -35.960  17.430 -26.094  1.00 25.13           N  
ATOM   2089  CA  ASN A 284     -37.290  16.891 -25.944  1.00 24.84           C  
ATOM   2090  C   ASN A 284     -38.115  17.710 -26.920  1.00 32.53           C  
ATOM   2091  O   ASN A 284     -37.645  18.678 -27.515  1.00 27.71           O  
ATOM   2092  CB  ASN A 284     -37.837  17.052 -24.515  1.00 22.73           C  
ATOM   2093  CG  ASN A 284     -37.904  18.473 -24.021  1.00 35.10           C  
ATOM   2094  ND2 ASN A 284     -37.435  18.727 -22.821  1.00 26.62           N  
ATOM   2095  OD1 ASN A 284     -38.347  19.394 -24.706  1.00 32.48           O  
ATOM   2096  N   ASP A 285     -39.346  17.301 -27.094  1.00 26.45           N  
ATOM   2097  CA  ASP A 285     -40.255  17.992 -28.000  1.00 41.39           C  
ATOM   2098  C   ASP A 285     -41.095  19.126 -27.391  1.00 38.31           C  
ATOM   2099  O   ASP A 285     -42.107  19.540 -27.963  1.00 41.71           O  
ATOM   2100  CB  ASP A 285     -41.190  16.948 -28.632  1.00 22.77           C  
ATOM   2101  CG  ASP A 285     -42.174  16.240 -27.707  1.00 23.18           C  
ATOM   2102  OD1 ASP A 285     -42.159  16.433 -26.477  1.00 33.04           O  
ATOM   2103  OD2 ASP A 285     -42.970  15.464 -28.241  1.00 41.33           O1-
ATOM   2104  N   LEU A 286     -40.818  19.627 -26.199  1.00 31.53           N  
ATOM   2105  CA  LEU A 286     -41.629  20.712 -25.688  1.00 25.13           C  
ATOM   2106  C   LEU A 286     -41.329  21.942 -26.550  1.00 41.07           C  
ATOM   2107  O   LEU A 286     -40.302  21.986 -27.256  1.00 43.63           O  
ATOM   2108  CB  LEU A 286     -41.285  20.969 -24.241  1.00 27.21           C  
ATOM   2109  CG  LEU A 286     -41.779  19.862 -23.377  1.00 27.72           C  
ATOM   2110  CD1 LEU A 286     -41.297  20.188 -22.011  1.00 35.20           C  
ATOM   2111  CD2 LEU A 286     -43.289  19.696 -23.432  1.00 33.80           C  
ATOM   2112  N   PRO A 287     -42.261  22.929 -26.566  1.00 72.08           N  
ATOM   2113  CA  PRO A 287     -42.173  24.150 -27.372  1.00 57.25           C  
ATOM   2114  C   PRO A 287     -40.890  24.993 -27.336  1.00 55.50           C  
ATOM   2115  O   PRO A 287     -40.313  25.317 -28.381  1.00 64.32           O  
ATOM   2116  CB  PRO A 287     -43.418  24.922 -26.932  1.00 64.34           C  
ATOM   2117  CG  PRO A 287     -43.805  24.335 -25.586  1.00 69.23           C  
ATOM   2118  CD  PRO A 287     -43.578  22.875 -25.905  1.00 60.19           C  
ATOM   2119  N   ASN A 288     -40.455  25.403 -26.133  1.00 54.09           N  
ATOM   2120  CA  ASN A 288     -39.240  26.228 -25.976  1.00 73.15           C  
ATOM   2121  C   ASN A 288     -37.915  25.523 -26.330  1.00 74.10           C  
ATOM   2122  O   ASN A 288     -37.105  26.086 -27.078  1.00 75.41           O  
ATOM   2123  CB  ASN A 288     -39.196  26.783 -24.490  1.00 81.36           C  
ATOM   2124  CG  ASN A 288     -37.857  26.837 -23.702  1.00 97.42           C  
ATOM   2125  ND2 ASN A 288     -37.746  26.111 -22.588  1.00101.92           N  
ATOM   2126  OD1 ASN A 288     -36.888  27.536 -24.033  1.00 97.46           O  
ATOM   2127  N   SER A 289     -37.747  24.303 -25.787  1.00 69.19           N  
ATOM   2128  CA  SER A 289     -36.544  23.500 -25.819  1.00 50.17           C  
ATOM   2129  C   SER A 289     -35.627  23.536 -27.021  1.00 43.85           C  
ATOM   2130  O   SER A 289     -35.966  23.118 -28.138  1.00 46.69           O  
ATOM   2131  CB  SER A 289     -36.955  22.064 -25.545  1.00 52.12           C  
ATOM   2132  OG  SER A 289     -37.582  22.054 -24.259  1.00 71.82           O  
ATOM   2133  N   ASP A 290     -34.439  24.097 -26.748  1.00 38.06           N  
ATOM   2134  CA  ASP A 290     -33.348  24.041 -27.724  1.00 44.01           C  
ATOM   2135  C   ASP A 290     -32.530  22.827 -27.245  1.00 33.18           C  
ATOM   2136  O   ASP A 290     -32.512  22.510 -26.053  1.00 32.33           O  
ATOM   2137  CB  ASP A 290     -32.381  25.216 -27.693  1.00 56.50           C  
ATOM   2138  CG  ASP A 290     -32.935  26.544 -27.208  1.00 77.24           C  
ATOM   2139  OD1 ASP A 290     -32.933  26.793 -25.985  1.00 84.59           O  
ATOM   2140  OD2 ASP A 290     -33.334  27.313 -28.087  1.00 73.57           O1-
ATOM   2141  N   MET A 291     -31.847  22.170 -28.173  1.00 36.97           N  
ATOM   2142  CA  MET A 291     -31.023  21.000 -27.921  1.00 34.70           C  
ATOM   2143  C   MET A 291     -29.787  21.361 -27.104  1.00 26.12           C  
ATOM   2144  O   MET A 291     -29.130  22.381 -27.421  1.00 28.32           O  
ATOM   2145  CB  MET A 291     -30.607  20.461 -29.247  1.00 33.14           C  
ATOM   2146  CG  MET A 291     -29.838  19.162 -29.264  1.00 52.66           C  
ATOM   2147  SD  MET A 291     -29.216  18.958 -30.950  1.00 48.22           S  
ATOM   2148  CE  MET A 291     -27.977  20.226 -30.976  1.00 41.88           C  
ATOM   2149  N   VAL A 292     -29.526  20.530 -26.068  1.00 30.89           N  
ATOM   2150  CA  VAL A 292     -28.283  20.632 -25.294  1.00 28.79           C  
ATOM   2151  C   VAL A 292     -27.250  19.662 -25.923  1.00 27.78           C  
ATOM   2152  O   VAL A 292     -27.600  18.713 -26.646  1.00 23.47           O  
ATOM   2153  CB  VAL A 292     -28.497  20.283 -23.776  1.00 21.26           C  
ATOM   2154  CG1 VAL A 292     -29.377  21.370 -23.222  1.00 24.54           C  
ATOM   2155  CG2 VAL A 292     -29.112  18.923 -23.529  1.00 17.97           C  
ATOM   2156  N   ALA A 293     -25.963  19.887 -25.738  1.00 24.90           N  
ATOM   2157  CA  ALA A 293     -24.927  19.051 -26.324  1.00 28.34           C  
ATOM   2158  C   ALA A 293     -23.669  19.186 -25.481  1.00 31.62           C  
ATOM   2159  O   ALA A 293     -23.544  20.160 -24.714  1.00 21.58           O  
ATOM   2160  CB  ALA A 293     -24.581  19.517 -27.734  1.00 21.46           C  
ATOM   2161  N   ASP A 294     -22.699  18.259 -25.551  1.00 20.79           N  
ATOM   2162  CA  ASP A 294     -21.417  18.492 -24.897  1.00 18.22           C  
ATOM   2163  C   ASP A 294     -20.321  17.696 -25.582  1.00 23.81           C  
ATOM   2164  O   ASP A 294     -20.651  16.816 -26.401  1.00 21.81           O  
ATOM   2165  CB  ASP A 294     -21.506  18.115 -23.427  1.00 16.80           C  
ATOM   2166  CG  ASP A 294     -21.669  16.651 -23.049  1.00 28.79           C  
ATOM   2167  OD1 ASP A 294     -21.300  15.730 -23.770  1.00 23.51           O  
ATOM   2168  OD2 ASP A 294     -22.168  16.418 -21.962  1.00 20.09           O1-
ATOM   2169  N   LEU A 295     -19.073  17.985 -25.250  1.00 22.29           N  
ATOM   2170  CA  LEU A 295     -17.953  17.261 -25.804  1.00 23.66           C  
ATOM   2171  C   LEU A 295     -16.823  17.412 -24.825  1.00 20.00           C  
ATOM   2172  O   LEU A 295     -16.407  18.533 -24.511  1.00 18.17           O  
ATOM   2173  CB  LEU A 295     -17.553  17.847 -27.149  1.00 22.86           C  
ATOM   2174  CG  LEU A 295     -16.323  17.132 -27.807  1.00 36.71           C  
ATOM   2175  CD1 LEU A 295     -16.653  15.675 -28.127  1.00 28.60           C  
ATOM   2176  CD2 LEU A 295     -15.953  17.801 -29.098  1.00 32.46           C  
ATOM   2177  N   GLY A 296     -16.290  16.309 -24.297  1.00 17.67           N  
ATOM   2178  CA  GLY A 296     -15.187  16.432 -23.368  1.00 17.33           C  
ATOM   2179  C   GLY A 296     -14.543  15.078 -23.127  1.00 21.99           C  
ATOM   2180  O   GLY A 296     -14.715  14.155 -23.925  1.00 20.73           O  
ATOM   2181  N   VAL A 297     -13.816  14.955 -22.029  1.00 23.91           N  
ATOM   2182  CA  VAL A 297     -13.127  13.711 -21.656  1.00 24.04           C  
ATOM   2183  C   VAL A 297     -13.553  13.273 -20.268  1.00 27.04           C  
ATOM   2184  O   VAL A 297     -13.814  14.129 -19.417  1.00 20.84           O  
ATOM   2185  CB  VAL A 297     -11.565  13.893 -21.707  1.00 20.97           C  
ATOM   2186  CG1 VAL A 297     -11.156  14.060 -23.155  1.00 27.35           C  
ATOM   2187  CG2 VAL A 297     -11.065  15.120 -20.999  1.00 23.73           C  
ATOM   2188  N   LYS A 298     -13.705  11.987 -19.986  1.00 18.69           N  
ATOM   2189  CA  LYS A 298     -14.080  11.491 -18.668  1.00 16.67           C  
ATOM   2190  C   LYS A 298     -12.916  10.639 -18.181  1.00 23.47           C  
ATOM   2191  O   LYS A 298     -12.308   9.961 -19.013  1.00 24.58           O  
ATOM   2192  CB  LYS A 298     -15.308  10.618 -18.735  1.00 19.12           C  
ATOM   2193  CG  LYS A 298     -16.560  11.452 -18.919  1.00 21.33           C  
ATOM   2194  CD  LYS A 298     -17.680  10.528 -19.195  1.00 18.34           C  
ATOM   2195  CE  LYS A 298     -17.992   9.837 -17.930  1.00 21.34           C  
ATOM   2196  NZ  LYS A 298     -19.101   8.932 -18.162  1.00 30.35           N1+
ATOM   2197  N   PHE A 299     -12.552  10.656 -16.907  1.00 18.24           N  
ATOM   2198  CA  PHE A 299     -11.404   9.940 -16.366  1.00 17.66           C  
ATOM   2199  C   PHE A 299     -11.851   9.122 -15.185  1.00 26.51           C  
ATOM   2200  O   PHE A 299     -12.735   9.546 -14.423  1.00 22.18           O  
ATOM   2201  CB  PHE A 299     -10.368  10.923 -15.894  1.00 14.69           C  
ATOM   2202  CG  PHE A 299      -9.811  11.877 -16.929  1.00 21.01           C  
ATOM   2203  CD1 PHE A 299      -9.418  11.438 -18.181  1.00 22.78           C  
ATOM   2204  CD2 PHE A 299      -9.658  13.206 -16.606  1.00 20.84           C  
ATOM   2205  CE1 PHE A 299      -8.877  12.314 -19.100  1.00 23.54           C  
ATOM   2206  CE2 PHE A 299      -9.110  14.068 -17.537  1.00 22.22           C  
ATOM   2207  CZ  PHE A 299      -8.718  13.635 -18.782  1.00 21.26           C  
ATOM   2208  N   LYS A 300     -11.321   7.938 -14.974  1.00 17.76           N  
ATOM   2209  CA  LYS A 300     -11.615   7.149 -13.789  1.00 17.46           C  
ATOM   2210  C   LYS A 300     -10.267   6.912 -13.119  1.00 24.16           C  
ATOM   2211  O   LYS A 300      -9.236   6.791 -13.823  1.00 26.46           O  
ATOM   2212  CB  LYS A 300     -12.212   5.835 -14.166  1.00 22.55           C  
ATOM   2213  CG  LYS A 300     -13.557   5.977 -14.793  1.00 34.41           C  
ATOM   2214  CD  LYS A 300     -14.407   4.731 -14.541  1.00 54.10           C  
ATOM   2215  CE  LYS A 300     -14.025   3.500 -15.364  1.00 75.73           C  
ATOM   2216  NZ  LYS A 300     -14.954   2.404 -15.105  1.00 84.85           N1+
ATOM   2217  N   PHE A 301     -10.224   6.873 -11.788  1.00 19.50           N  
ATOM   2218  CA  PHE A 301      -8.983   6.813 -11.045  1.00 18.21           C  
ATOM   2219  C   PHE A 301      -9.075   5.777  -9.954  1.00 22.86           C  
ATOM   2220  O   PHE A 301     -10.180   5.359  -9.597  1.00 17.64           O  
ATOM   2221  CB  PHE A 301      -8.594   8.122 -10.339  1.00 18.80           C  
ATOM   2222  CG  PHE A 301      -8.442   9.267 -11.313  1.00 24.96           C  
ATOM   2223  CD1 PHE A 301      -7.316   9.382 -12.099  1.00 18.68           C  
ATOM   2224  CD2 PHE A 301      -9.432  10.235 -11.398  1.00 23.97           C  
ATOM   2225  CE1 PHE A 301      -7.152  10.451 -12.972  1.00 19.16           C  
ATOM   2226  CE2 PHE A 301      -9.258  11.303 -12.274  1.00 19.39           C  
ATOM   2227  CZ  PHE A 301      -8.128  11.423 -13.061  1.00 20.43           C  
ATOM   2228  OXT PHE A 301      -8.004   5.364  -9.483  1.00 28.38           O1-
TER    2229      PHE A 301 
HETATM 2230 CA    CA A 302     -32.798   7.360 -10.359  1.00 21.26          CA  
HETATM 2231 CA    CA A 303     -28.562  10.852 -16.087  1.00 18.82          CA  
HETATM 2232 CA    CA A 304     -37.073   9.172   9.734  1.00 19.02          CA  
HETATM 2233  O   HOH A 305     -35.079   7.955  -9.785  1.00 20.83           O  
HETATM 2234  O   HOH A 306     -16.401  13.960  -4.253  1.00 16.79           O  
HETATM 2235  O   HOH A 307     -30.926   7.613 -11.712  1.00 20.86           O  
HETATM 2236  O   HOH A 308     -39.347  10.153   6.281  1.00 19.18           O  
HETATM 2237  O   HOH A 309     -15.586  16.467  -5.094  1.00 17.25           O  
HETATM 2238  O   HOH A 310     -25.218   9.428  -1.677  1.00 19.05           O  
HETATM 2239  O   HOH A 311     -36.836   7.084   6.116  1.00 18.03           O  
HETATM 2240  O   HOH A 312     -33.625   6.626 -12.358  1.00 18.77           O  
HETATM 2241  O   HOH A 313     -27.714  11.154 -20.323  1.00 19.97           O  
HETATM 2242  O   HOH A 314     -34.789   8.787  10.123  1.00 16.16           O  
HETATM 2243  O   HOH A 315     -40.880   8.470   5.086  1.00 22.41           O  
HETATM 2244  O   HOH A 316     -35.160   4.426  -7.063  1.00 19.18           O  
HETATM 2245  O   HOH A 317     -24.967 -11.875   0.352  1.00 26.78           O  
HETATM 2246  O   HOH A 318     -29.294  12.519 -22.078  1.00 23.41           O  
HETATM 2247  O   HOH A 319     -18.160  23.148 -14.248  1.00 17.66           O  
HETATM 2248  O   HOH A 320     -37.154   2.415  -7.622  1.00 19.10           O  
HETATM 2249  O   HOH A 321     -26.131   5.727   5.978  1.00 17.80           O  
HETATM 2250  O   HOH A 322     -21.879  14.216  -8.145  1.00 21.07           O  
HETATM 2251  O   HOH A 323     -31.701  15.740 -21.496  1.00 21.64           O  
HETATM 2252  O   HOH A 324     -36.892   7.911  -7.732  1.00 23.75           O  
HETATM 2253  O   HOH A 325     -19.039  19.049 -15.228  1.00 23.49           O  
HETATM 2254  O   HOH A 326     -16.520  13.273 -12.713  1.00 21.15           O  
HETATM 2255  O   HOH A 327     -28.551  10.730 -13.847  1.00 26.61           O  
HETATM 2256  O   HOH A 328     -32.107   7.699  -1.608  1.00 17.22           O  
HETATM 2257  O   HOH A 329     -39.007   2.462  -2.025  1.00 18.42           O  
HETATM 2258  O   HOH A 330     -34.611   2.617  -0.685  1.00 21.28           O  
HETATM 2259  O   HOH A 331     -27.501   8.725 -15.823  1.00 20.17           O  
HETATM 2260  O   HOH A 332     -29.328  -4.028  -0.751  1.00 23.35           O  
HETATM 2261  O   HOH A 333     -24.156   7.405   5.292  1.00 20.95           O  
HETATM 2262  O   HOH A 334     -28.670   1.609  -3.339  1.00 19.73           O  
HETATM 2263  O   HOH A 335     -13.363   3.603  -3.628  1.00 21.76           O  
HETATM 2264  O   HOH A 336     -37.138   3.820  -0.513  1.00 21.38           O  
HETATM 2265  O   HOH A 337     -22.731  16.170   9.131  1.00 20.97           O  
HETATM 2266  O   HOH A 338     -38.117  13.407   4.152  1.00 24.59           O  
HETATM 2267  O   HOH A 339     -32.952   9.554 -11.256  1.00 22.54           O  
HETATM 2268  O   HOH A 340     -23.309  16.247   1.821  1.00 30.10           O  
HETATM 2269  O   HOH A 341     -21.842 -13.512   3.216  1.00 27.64           O  
HETATM 2270  O   HOH A 342     -33.257  14.309 -23.099  1.00 24.28           O  
HETATM 2271  O   HOH A 343     -19.831  12.264 -16.156  1.00 28.57           O  
HETATM 2272  O   HOH A 344     -26.996  15.765   6.199  1.00 31.66           O  
HETATM 2273  O   HOH A 345     -17.596  11.602 -14.625  1.00 27.53           O  
HETATM 2274  O   HOH A 346     -37.378   9.525 -10.940  1.00 33.44           O  
HETATM 2275  O   HOH A 347     -12.521  -1.512   0.967  1.00 28.72           O  
HETATM 2276  O   HOH A 348     -52.759  17.736  -5.903  1.00 24.32           O  
HETATM 2277  O   HOH A 349     -27.753   6.727 -13.918  1.00 32.87           O  
HETATM 2278  O   HOH A 350     -22.221 -11.398   1.493  1.00 25.47           O  
HETATM 2279  O   HOH A 351     -35.878   8.337  -1.059  1.00 20.42           O  
HETATM 2280  O   HOH A 352     -36.837  13.795   6.605  1.00 23.31           O  
HETATM 2281  O   HOH A 353     -23.591  26.048 -21.536  1.00 28.26           O  
HETATM 2282  O   HOH A 354     -10.085   3.326 -20.392  1.00 31.00           O  
HETATM 2283  O   HOH A 355     -21.234  21.985 -12.977  1.00 28.25           O  
HETATM 2284  O   HOH A 356     -22.488  10.172 -24.972  1.00 29.65           O  
HETATM 2285  O   HOH A 357     -12.942  -7.226   8.614  1.00 31.85           O  
HETATM 2286  O   HOH A 358     -29.601   3.762 -11.685  1.00 29.74           O  
HETATM 2287  O   HOH A 359     -13.454   6.900 -18.952  1.00 26.75           O  
HETATM 2288  O   HOH A 360     -21.379  30.472 -26.760  1.00 42.24           O  
HETATM 2289  O   HOH A 361     -19.252  21.426   3.454  0.33 48.27           O  
HETATM 2290  O   HOH A 362     -47.213  22.395  -9.214  1.00 32.73           O  
HETATM 2291  O   HOH A 363     -54.496  20.160 -13.359  1.00 37.66           O  
HETATM 2292  O   HOH A 364     -19.400 -13.353  13.081  1.00 40.03           O  
HETATM 2293  O   HOH A 365     -20.186  17.556   2.230  1.00 29.16           O  
HETATM 2294  O   HOH A 366     -21.582  10.578 -15.197  1.00 43.77           O  
HETATM 2295  O   HOH A 367     -15.580   9.315 -15.301  1.00 34.97           O  
HETATM 2296  O   HOH A 368     -55.164   9.966  -2.499  1.00 37.84           O  
HETATM 2297  O   HOH A 369     -22.790  20.181 -16.676  1.00 35.39           O  
HETATM 2298  O   HOH A 370     -24.885  11.325  13.323  1.00 36.44           O  
HETATM 2299  O   HOH A 371     -21.496  10.188 -19.241  1.00 36.57           O  
HETATM 2300  O   HOH A 372     -49.970  21.069  -3.694  1.00 43.83           O  
HETATM 2301  O   HOH A 373     -49.687  18.250  -3.642  1.00 33.68           O  
HETATM 2302  O   HOH A 374     -22.084   7.964  -2.982  1.00 35.76           O  
HETATM 2303  O   HOH A 375     -25.406   6.532  -2.089  1.00 32.10           O  
HETATM 2304  O   HOH A 376     -29.061   0.420 -24.034  1.00 27.51           O  
HETATM 2305  O   HOH A 377     -35.823  10.660  -7.184  1.00 40.21           O  
HETATM 2306  O   HOH A 378     -23.461  13.461 -10.378  1.00 47.68           O  
HETATM 2307  O   HOH A 379     -24.893  18.782 -18.350  1.00 34.03           O  
HETATM 2308  O   HOH A 380     -15.115   5.733  -8.274  1.00 43.15           O  
HETATM 2309  O   HOH A 381     -32.200 -11.791 -12.531  1.00 41.20           O  
HETATM 2310  O   HOH A 382     -34.164  15.081  13.003  1.00 36.40           O  
HETATM 2311  O   HOH A 383      -6.842   2.761  -2.126  1.00 39.85           O  
HETATM 2312  O   HOH A 384     -30.632  24.247 -20.399  1.00 48.67           O  
HETATM 2313  O   HOH A 385     -52.236   8.047   2.841  1.00 47.58           O  
HETATM 2314  O   HOH A 386     -25.729 -15.555   6.476  1.00 40.32           O  
HETATM 2315  O   HOH A 387     -54.708  21.755  -1.399  1.00 38.71           O  
HETATM 2316  O   HOH A 388     -22.572  18.011  -0.855  1.00 38.73           O  
HETATM 2317  O   HOH A 389     -23.582  15.216 -13.783  1.00 39.55           O  
HETATM 2318  O   HOH A 390     -16.104   2.862 -25.994  1.00 44.19           O  
HETATM 2319  O   HOH A 391     -61.266  21.908  -3.269  1.00 44.93           O  
HETATM 2320  O   HOH A 392     -32.314  17.503   4.366  1.00 41.01           O  
HETATM 2321  O   HOH A 393     -22.254  -1.507 -26.207  1.00 37.42           O  
HETATM 2322  O   HOH A 394     -54.702   8.657  -4.868  1.00 49.33           O  
HETATM 2323  O   HOH A 395     -22.040   5.483  -2.146  1.00 53.49           O  
HETATM 2324  O   HOH A 396     -26.360  18.025   7.406  1.00 46.06           O  
HETATM 2325  O   HOH A 397     -51.062  21.815 -19.329  1.00 50.52           O  
HETATM 2326  O   HOH A 398     -28.172 -17.568  -3.219  1.00 44.63           O  
HETATM 2327  O   HOH A 399     -17.230   6.756 -21.001  1.00 46.80           O  
HETATM 2328  O   HOH A 400     -24.621  -9.370  -2.177  1.00 56.53           O  
HETATM 2329  O   HOH A 401     -27.991   1.785 -15.352  1.00 41.82           O  
HETATM 2330  O   HOH A 402     -52.814  23.239  -3.950  1.00 40.08           O  
HETATM 2331  O   HOH A 403     -43.318  12.716  -2.420  1.00 51.56           O  
HETATM 2332  O   HOH A 404     -22.122  26.715 -31.535  1.00 54.32           O  
HETATM 2333  O   HOH A 405     -39.922  17.426  12.281  1.00 44.63           O  
HETATM 2334  O   HOH A 406     -27.553   1.955 -11.483  1.00 75.55           O  
HETATM 2335  O   HOH A 407     -23.176  20.802   0.096  1.00 49.18           O  
HETATM 2336  O   HOH A 408     -53.039  22.371 -17.463  1.00 57.48           O  
HETATM 2337  O   HOH A 409     -29.047  -0.309 -10.870  1.00 42.07           O  
HETATM 2338  O   HOH A 410     -14.042   5.277 -10.686  1.00 48.26           O  
HETATM 2339  O   HOH A 411     -26.729 -10.615  -1.324  1.00 48.76           O  
HETATM 2340  O   HOH A 412     -21.463 -12.836  11.659  1.00 61.69           O  
HETATM 2341  O   HOH A 413     -24.726  15.402  12.797  1.00 45.17           O  
HETATM 2342  O   HOH A 414     -27.032  25.302 -17.789  1.00 42.63           O  
HETATM 2343  O   HOH A 415     -28.062  -9.266  -3.210  1.00 53.03           O  
HETATM 2344  O   HOH A 416     -29.573  12.413  -0.473  1.00 39.48           O  
HETATM 2345  O   HOH A 417     -21.862   0.606   0.150  1.00 46.65           O  
HETATM 2346  O   HOH A 418     -45.629  25.735 -20.820  1.00 48.30           O  
HETATM 2347  O   HOH A 419     -17.135  -6.615   2.649  1.00 53.86           O  
HETATM 2348  O   HOH A 420     -42.358  15.076  -2.357  1.00 68.06           O  
HETATM 2349  O   HOH A 421     -24.711   3.769 -20.071  1.00 49.89           O  
HETATM 2350  O   HOH A 422     -22.523   0.784 -22.543  1.00 61.39           O  
HETATM 2351  O   HOH A 423     -28.964   7.657  -8.750  1.00 57.43           O  
HETATM 2352  O   HOH A 424     -36.119  11.030 -16.580  1.00 41.42           O  
HETATM 2353  O   HOH A 425     -51.728   8.946 -19.291  1.00 50.68           O  
HETATM 2354  O   HOH A 426     -22.030  20.035   2.414  1.00 45.66           O  
HETATM 2355  O   HOH A 427     -15.718   7.046 -17.440  1.00 51.14           O  
HETATM 2356  O   HOH A 428     -26.103  20.753 -16.726  1.00 40.22           O  
HETATM 2357  O   HOH A 429     -27.217   3.733 -17.525  1.00 42.31           O  
HETATM 2358  O   HOH A 430     -35.661  14.564  -0.085  1.00 46.27           O  
HETATM 2359  O   HOH A 431     -25.676  23.382 -16.085  1.00 49.31           O  
HETATM 2360  O   HOH A 432     -27.799  15.719  -0.460  1.00 51.14           O  
HETATM 2361  O   HOH A 433     -46.158  18.135  -4.263  1.00 61.72           O  
HETATM 2362  O   HOH A 434     -35.722  10.322 -12.907  1.00 54.50           O  
HETATM 2363  O   HOH A 435     -25.110  11.969 -13.236  1.00 48.27           O  
HETATM 2364  O   HOH A 436     -31.572  14.445   0.318  1.00 44.09           O  
HETATM 2365  O   HOH A 437     -24.855  22.387 -31.224  1.00 52.83           O  
HETATM 2366  O   HOH A 438     -16.453   6.360 -11.649  1.00 60.95           O  
HETATM 2367  O   HOH A 439     -43.983  28.127 -13.784  1.00 57.64           O  
HETATM 2368  O   HOH A 440      -7.467   0.158   5.042  1.00 55.03           O  
HETATM 2369  O   HOH A 441     -27.817  -2.691  -2.749  1.00 47.33           O  
HETATM 2370  O   HOH A 442     -52.707  20.141  -3.429  1.00 42.38           O  
HETATM 2371  O   HOH A 443     -57.046  16.157 -11.116  1.00 47.66           O  
HETATM 2372  O   HOH A 444     -29.272   7.521  -4.622  1.00 44.53           O  
HETATM 2373  O   HOH A 445     -34.740  25.505 -24.069  1.00 62.40           O  
HETATM 2374  O   HOH A 446     -26.557   3.981  -7.262  1.00 74.18           O  
HETATM 2375  O   HOH A 447     -47.153  15.038  12.608  1.00 50.06           O  
HETATM 2376  O   HOH A 448     -24.781  18.048   9.594  1.00 39.51           O  
HETATM 2377  O   HOH A 449      -7.796   3.633  -7.222  1.00 53.63           O  
HETATM 2378  O   HOH A 450     -27.684  17.718 -16.534  1.00 37.68           O  
HETATM 2379  O   HOH A 451     -18.121   1.383  -3.638  1.00 53.20           O  
HETATM 2380  O   HOH A 452     -20.625   4.750 -23.495  1.00 47.15           O  
HETATM 2381  O   HOH A 453     -45.334  23.395  -7.643  1.00 58.11           O  
HETATM 2382  O   HOH A 454     -12.598   1.621 -32.663  1.00 66.31           O  
HETATM 2383  O   HOH A 455     -30.997 -20.540 -11.224  1.00 70.96           O  
HETATM 2384  O   HOH A 456     -44.792  13.552 -26.828  1.00 51.90           O  
HETATM 2385  O   HOH A 457     -23.693 -16.026   9.759  1.00 76.94           O  
HETATM 2386  O   HOH A 458     -22.895  29.177 -29.997  1.00 75.09           O  
HETATM 2387  O   HOH A 459     -22.719  18.825  -3.319  1.00 56.50           O  
HETATM 2388  O   HOH A 460     -56.336  11.299 -14.604  1.00 45.95           O  
HETATM 2389  O   HOH A 461      -6.319   0.260 -20.862  1.00 59.14           O  
HETATM 2390  O   HOH A 462     -18.046  -1.616   0.417  1.00 52.16           O  
HETATM 2391  O   HOH A 463     -34.944  15.948   7.945  1.00 35.27           O  
HETATM 2392  O   HOH A 464     -44.249   5.122  10.088  1.00 67.65           O  
HETATM 2393  O   HOH A 465     -29.355 -20.196 -14.868  1.00 73.43           O  
HETATM 2394  O   HOH A 466     -56.229  17.314 -13.482  1.00 57.98           O  
HETATM 2395  O   HOH A 467     -54.564  20.473 -16.200  1.00 72.32           O  
HETATM 2396  O   HOH A 468     -23.154  19.949 -13.890  1.00 70.17           O  
HETATM 2397  O   HOH A 469     -19.358  20.088 -12.809  1.00 36.34           O  
HETATM 2398  O   HOH A 470     -22.379   5.320 -20.531  1.00 56.33           O  
HETATM 2399  O   HOH A 471     -28.328 -17.419 -15.243  1.00 75.50           O  
HETATM 2400  O   HOH A 472     -27.524  12.852 -12.294  1.00 66.81           O  
HETATM 2401  O   HOH A 473     -43.340  26.814 -17.333  1.00 54.10           O  
HETATM 2402  O   HOH A 474     -52.163  14.310 -21.416  1.00 58.95           O  
HETATM 2403  O   HOH A 475     -35.317  13.951  -6.234  1.00 64.71           O  
HETATM 2404  O   HOH A 476     -26.936  15.143 -14.824  1.00 53.66           O  
HETATM 2405  O   HOH A 477     -30.411  21.139 -16.020  1.00 74.59           O  
HETATM 2406  O   HOH A 478     -29.430 -13.363 -10.375  1.00 52.60           O  
HETATM 2407  O   HOH A 479     -11.885  -6.998   4.908  1.00 73.28           O  
HETATM 2408  O   HOH A 480     -33.119  19.008   9.017  1.00 79.45           O  
HETATM 2409  O   HOH A 481     -16.212  -5.005 -30.147  1.00 79.74           O  
HETATM 2410  O   HOH A 482     -44.397  23.419 -19.737  1.00 55.45           O  
HETATM 2411  O   HOH A 483     -40.514  15.156  17.372  1.00 62.96           O  
HETATM 2412  O   HOH A 484     -24.411   9.349 -13.887  1.00 54.07           O  
HETATM 2413  O   HOH A 485     -25.135   4.830 -15.694  1.00 69.32           O  
HETATM 2414  O   HOH A 486     -25.103  18.960   3.850  1.00 70.03           O  
HETATM 2415  O   HOH A 487     -27.923  -1.724  -8.589  1.00 66.77           O  
HETATM 2416  O   HOH A 488     -15.493   1.213  -6.297  1.00 58.10           O  
HETATM 2417  O   HOH A 489     -31.226  13.548 -13.651  1.00 65.27           O  
HETATM 2418  O   HOH A 490     -18.923  31.174 -24.174  1.00 56.86           O  
HETATM 2419  O   HOH A 491     -29.334  -6.943  -7.297  1.00 56.42           O  
HETATM 2420  O   HOH A 492     -52.733   4.874 -15.288  1.00 56.25           O  
HETATM 2421  O   HOH A 493     -12.688   4.545 -20.087  1.00 49.66           O  
HETATM 2422  O   HOH A 494     -40.535  15.522   3.354  1.00 62.01           O  
HETATM 2423  O   HOH A 495     -44.076   9.777 -29.092  1.00 61.29           O  
HETATM 2424  O   HOH A 496     -28.319  -1.093  -5.462  1.00 61.82           O  
HETATM 2425  O   HOH A 497      -7.126   3.480 -27.418  1.00 81.82           O  
HETATM 2426  O   HOH A 498     -28.933  -0.424 -21.370  1.00 52.03           O  
HETATM 2427  O   HOH A 499     -24.423  16.195  -2.021  1.00 55.91           O  
HETATM 2428  O   HOH A 500     -30.025 -10.145 -19.639  1.00 54.60           O  
HETATM 2429  O   HOH A 501     -29.833  23.924 -29.863  1.00 62.48           O  
HETATM 2430  O   HOH A 502     -46.513  21.900 -20.338  1.00 56.15           O  
HETATM 2431  O   HOH A 503     -21.994   8.017 -23.589  1.00 47.52           O  
HETATM 2432  O   HOH A 504     -28.092 -17.610  -0.494  1.00 66.96           O  
HETATM 2433  O   HOH A 505     -29.721  23.878 -15.788  1.00 88.14           O  
HETATM 2434  O   HOH A 506     -24.888  13.493  -3.314  1.00 70.57           O  
HETATM 2435  O   HOH A 507     -56.625   6.986   1.775  1.00 77.52           O  
HETATM 2436  O   HOH A 508     -52.754   6.270 -17.703  1.00 68.06           O  
HETATM 2437  O   HOH A 509     -27.539   1.420 -19.269  1.00 60.83           O  
HETATM 2438  O   HOH A 510      -6.582   5.464 -13.953  1.00 43.72           O  
HETATM 2439  O   HOH A 511     -22.270  23.443   0.813  1.00 64.23           O  
HETATM 2440  O   HOH A 512     -18.144   2.113  -7.187  1.00 67.86           O  
HETATM 2441  O   HOH A 513     -16.410   8.244  -7.756  1.00 48.46           O  
HETATM 2442  O   HOH A 514     -44.360  24.436  -9.991  1.00 58.53           O  
HETATM 2443  O   HOH A 515     -56.399  12.558  -2.604  1.00 49.61           O  
HETATM 2444  O   HOH A 516     -34.057  15.513  15.861  1.00 63.03           O  
HETATM 2445  O   HOH A 517     -46.694  14.008  15.375  1.00 70.54           O  
HETATM 2446  O   HOH A 518     -17.158   7.634 -13.883  1.00 71.25           O  
HETATM 2447  O   HOH A 519     -46.368   8.456   8.287  1.00 49.95           O  
HETATM 2448  O   HOH A 520     -47.395   8.497   5.652  1.00 48.64           O  
HETATM 2449  O   HOH A 521     -20.355   4.859  -6.320  1.00 66.81           O  
HETATM 2450  O   HOH A 522     -30.535  28.408 -29.875  1.00 77.42           O  
HETATM 2451  O   HOH A 523     -60.255  19.296  -6.748  1.00 76.39           O  
HETATM 2452  O   HOH A 524     -40.913  13.090  19.366  1.00 73.03           O  
HETATM 2453  O   HOH A 525     -22.204   8.694 -11.819  1.00 77.39           O  
HETATM 2454  O   HOH A 526     -20.302 -10.102  -0.287  1.00 67.58           O  
HETATM 2455  O   HOH A 527     -27.184  -6.756  -4.438  1.00 62.67           O  
HETATM 2456  O   HOH A 528     -49.004  23.316 -20.347  1.00 67.32           O  
HETATM 2457  O   HOH A 529     -27.968   5.632 -10.380  1.00 76.35           O  
HETATM 2458  O   HOH A 530     -27.561  15.748  12.670  1.00 66.81           O  
HETATM 2459  O   HOH A 531     -49.199   9.219   7.916  1.00 71.46           O  
HETATM 2460  O   HOH A 532     -34.006  17.129   1.202  1.00 79.97           O  
HETATM 2461  O   HOH A 533     -32.492  12.003  -7.623  1.00 65.18           O  
HETATM 2462  O   HOH A 534     -37.491  18.913  12.216  1.00 66.98           O  
HETATM 2463  O   HOH A 535     -28.168  23.486 -19.585  1.00 57.49           O  
HETATM 2464  O   HOH A 536     -12.503   0.771  -4.667  1.00 63.19           O  
HETATM 2465  O   HOH A 537      -9.197  -0.172 -22.143  1.00 61.09           O  
HETATM 2466  O   HOH A 538     -56.821   8.413  -0.587  1.00 71.51           O  
HETATM 2467  O   HOH A 539     -28.283  -2.989 -20.604  1.00 65.27           O  
HETATM 2468  O   HOH A 540     -25.278   8.513  -4.822  1.00 66.67           O  
HETATM 2469  O   HOH A 541     -22.278  -7.611  -0.214  1.00 57.15           O  
HETATM 2470  O   HOH A 542     -22.475  11.531 -12.580  1.00 73.37           O  
HETATM 2471  O   HOH A 543     -17.586  17.799   1.935  1.00 57.28           O  
HETATM 2472  O   HOH A 544     -28.158  -5.270 -22.033  1.00 64.62           O  
HETATM 2473  C1  C8E A 545     -43.456   9.067 -11.956  0.88 42.96           C  
HETATM 2474  C2  C8E A 545     -42.660  10.228 -11.414  0.88 41.67           C  
HETATM 2475  C3  C8E A 545     -42.010  10.854 -12.600  0.88 42.57           C  
HETATM 2476  C4  C8E A 545     -41.167  11.941 -11.998  0.88 43.55           C  
HETATM 2477  C5  C8E A 545     -39.923  12.236 -12.827  0.88 44.03           C  
HETATM 2478  C6  C8E A 545     -40.192  12.601 -14.284  0.88 42.16           C  
HETATM 2479  C7  C8E A 545     -38.973  13.238 -14.978  0.88 39.75           C  
HETATM 2480  C8  C8E A 545     -39.435  13.507 -16.385  0.88 37.75           C  
HETATM 2481  O9  C8E A 545     -38.732  14.376 -17.248  0.88 38.94           O  
HETATM 2482  C10 C8E A 545     -39.595  15.344 -17.837  0.88 40.72           C  
HETATM 2483  C11 C8E A 545     -38.934  16.024 -18.988  0.88 45.43           C  
HETATM 2484  O12 C8E A 545     -39.289  17.358 -19.315  0.88 54.18           O  
HETATM 2485  C13 C8E A 545     -38.441  18.328 -18.688  0.88 63.79           C  
HETATM 2486  C14 C8E A 545     -39.120  19.390 -17.813  0.88 72.45           C  
HETATM 2487  O15 C8E A 545     -40.188  20.180 -18.379  0.88 79.05           O  
HETATM 2488  C16 C8E A 545     -39.971  21.609 -18.353  0.88 84.79           C  
HETATM 2489  C17 C8E A 545     -39.737  22.335 -19.703  0.88 88.54           C  
HETATM 2490  O18 C8E A 545     -39.940  23.753 -19.958  0.88 91.31           O  
HETATM 2491  C19 C8E A 545     -41.325  24.085 -20.272  0.88 93.11           C  
HETATM 2492  C20 C8E A 545     -41.640  24.723 -21.644  0.88 93.71           C  
HETATM 2493  O21 C8E A 545     -40.685  24.275 -22.617  0.88 93.34           O  
HETATM 2494  C1  C8E A 546     -23.141  12.689 -31.427  0.83 50.61           C  
HETATM 2495  C2  C8E A 546     -21.940  12.940 -30.492  0.83 51.77           C  
HETATM 2496  C3  C8E A 546     -21.186  14.267 -30.676  0.83 50.98           C  
HETATM 2497  C4  C8E A 546     -21.845  15.539 -30.127  0.83 51.13           C  
HETATM 2498  C5  C8E A 546     -20.840  16.666 -30.329  0.83 52.63           C  
HETATM 2499  C6  C8E A 546     -21.403  18.048 -30.054  0.83 55.60           C  
HETATM 2500  C7  C8E A 546     -20.589  19.130 -30.786  0.83 60.07           C  
HETATM 2501  C8  C8E A 546     -19.362  19.668 -30.035  0.83 64.27           C  
HETATM 2502  O9  C8E A 546     -18.281  20.302 -30.766  0.83 66.21           O  
HETATM 2503  C10 C8E A 546     -18.229  21.750 -30.816  0.83 66.45           C  
HETATM 2504  C11 C8E A 546     -17.271  22.605 -29.963  0.83 65.91           C  
HETATM 2505  O12 C8E A 546     -17.091  23.966 -30.397  0.83 65.26           O  
HETATM 2506  C13 C8E A 546     -17.757  24.979 -29.616  0.83 65.04           C  
HETATM 2507  C14 C8E A 546     -17.039  26.252 -29.103  0.83 64.60           C  
HETATM 2508  O15 C8E A 546     -16.142  26.267 -27.970  0.83 63.35           O  
HETATM 2509  C16 C8E A 546     -16.555  27.198 -26.954  0.83 61.87           C  
HETATM 2510  C17 C8E A 546     -15.575  27.621 -25.872  0.83 60.37           C  
HETATM 2511  O18 C8E A 546     -15.992  28.549 -24.873  0.83 60.64           O  
HETATM 2512  C19 C8E A 546     -15.101  29.665 -24.853  0.83 62.75           C  
HETATM 2513  C20 C8E A 546     -15.573  30.984 -25.458  0.83 65.74           C  
HETATM 2514  O21 C8E A 546     -14.564  31.991 -25.523  0.83 68.59           O  
HETATM 2515  C1  C8E A 547     -11.425  27.797 -26.416  0.69 53.41           C  
HETATM 2516  C2  C8E A 547     -11.957  26.345 -26.444  0.69 52.85           C  
HETATM 2517  C3  C8E A 547     -11.346  25.574 -25.294  0.69 51.32           C  
HETATM 2518  C4  C8E A 547     -11.808  24.129 -25.290  0.69 50.00           C  
HETATM 2519  C5  C8E A 547     -11.133  23.419 -24.124  0.69 48.73           C  
HETATM 2520  C6  C8E A 547     -11.430  21.929 -24.112  0.69 49.05           C  
HETATM 2521  C7  C8E A 547     -10.820  21.300 -22.877  0.69 50.17           C  
HETATM 2522  C8  C8E A 547     -11.094  19.809 -22.761  0.69 51.75           C  
HETATM 2523  O9  C8E A 547     -10.401  18.884 -23.599  0.69 53.80           O  
HETATM 2524  C10 C8E A 547     -11.258  17.911 -24.230  0.69 55.39           C  
HETATM 2525  C11 C8E A 547     -11.994  18.176 -25.559  0.69 57.31           C  
HETATM 2526  O12 C8E A 547     -12.579  17.067 -26.270  0.69 59.43           O  
HETATM 2527  C13 C8E A 547     -11.795  16.619 -27.400  0.69 62.71           C  
HETATM 2528  C14 C8E A 547     -10.724  15.505 -27.324  0.69 66.12           C  
HETATM 2529  O15 C8E A 547      -9.549  15.662 -26.496  0.69 68.53           O  
HETATM 2530  C16 C8E A 547      -8.753  14.466 -26.359  0.69 69.38           C  
HETATM 2531  C17 C8E A 547      -7.247  14.401 -26.694  0.69 69.19           C  
HETATM 2532  O18 C8E A 547      -6.757  14.387 -28.037  0.69 69.55           O  
HETATM 2533  C19 C8E A 547      -6.689  13.053 -28.554  0.69 71.17           C  
HETATM 2534  C20 C8E A 547      -5.328  12.389 -28.809  0.69 73.02           C  
HETATM 2535  O21 C8E A 547      -5.435  11.029 -29.239  0.69 74.35           O  
HETATM 2536  C1  C8E A 548     -41.997  -4.497 -21.282  0.66 38.33           C  
HETATM 2537  C2  C8E A 548     -41.316  -3.467 -22.178  0.66 39.82           C  
HETATM 2538  C3  C8E A 548     -42.255  -2.817 -23.181  0.66 42.86           C  
HETATM 2539  C4  C8E A 548     -41.621  -1.541 -23.786  0.66 46.04           C  
HETATM 2540  C5  C8E A 548     -42.416  -0.955 -24.961  0.66 48.47           C  
HETATM 2541  C6  C8E A 548     -42.077   0.475 -25.396  0.66 49.60           C  
HETATM 2542  C7  C8E A 548     -40.721   0.684 -26.049  0.66 50.98           C  
HETATM 2543  C8  C8E A 548     -40.832   1.749 -27.144  0.66 53.35           C  
HETATM 2544  O9  C8E A 548     -41.237   3.107 -26.874  0.66 56.73           O  
HETATM 2545  C10 C8E A 548     -40.334   4.100 -27.417  0.66 60.75           C  
HETATM 2546  C11 C8E A 548     -40.767   5.539 -27.800  0.66 64.78           C  
HETATM 2547  O12 C8E A 548     -41.707   5.838 -28.849  0.66 68.03           O  
HETATM 2548  C13 C8E A 548     -41.108   6.080 -30.132  0.66 70.92           C  
HETATM 2549  C14 C8E A 548     -41.590   7.287 -30.960  0.66 73.54           C  
HETATM 2550  O15 C8E A 548     -41.211   8.647 -30.668  0.66 75.50           O  
HETATM 2551  C16 C8E A 548     -40.588   9.291 -31.808  0.66 77.12           C  
HETATM 2552  C17 C8E A 548     -40.110  10.776 -31.869  0.66 78.17           C  
HETATM 2553  O18 C8E A 548     -38.949  11.300 -31.168  0.66 78.30           O  
HETATM 2554  C19 C8E A 548     -37.831  11.661 -31.993  0.66 78.18           C  
HETATM 2555  C20 C8E A 548     -36.617  10.744 -31.991  0.66 78.11           C  
HETATM 2556  O21 C8E A 548     -35.558  11.270 -32.784  0.66 79.53           O  
HETATM 2557  O   HOH A 549     -16.715  10.903 -29.722  1.00 45.08           O  
HETATM 2558  O   HOH A 550     -42.548  -3.293   1.298  1.00 57.73           O  
HETATM 2559  O   HOH A 551     -34.516 -15.569   1.919  1.00 54.12           O  
HETATM 2560  O   HOH A 552     -37.922  -4.542   3.532  1.00 49.12           O  
HETATM 2561  O   HOH A 553     -24.201  24.884 -31.873  1.00 53.13           O  
HETATM 2562  O   HOH A 554     -46.524   1.700 -26.380  1.00 65.70           O  
HETATM 2563  O   HOH A 555     -32.970   7.005 -30.497  1.00 51.43           O  
HETATM 2564  O   HOH A 556     -15.340   7.264 -34.289  1.00 74.75           O  
HETATM 2565  O   HOH A 557     -40.163  -3.610   2.339  1.00 58.01           O  
HETATM 2566  O   HOH A 558     -50.133  -5.892 -10.342  1.00 76.00           O  
HETATM 2567  O   HOH A 559     -36.376 -14.397  -0.005  1.00 63.30           O  
HETATM 2568  O   HOH A 560     -30.872 -17.578   5.608  1.00 78.96           O  
HETATM 2569  O   HOH A 561     -32.590   4.439 -30.002  1.00 56.46           O  
HETATM 2570  O   HOH A 562     -27.460  -1.565 -33.609  1.00 74.14           O  
HETATM 2571  O   HOH A 563     -48.600   2.741 -24.937  1.00 72.99           O  
HETATM 2572  O   HOH A 564     -28.626   4.253 -31.972  1.00 62.33           O  
HETATM 2573  O   HOH A 565     -19.441   8.706 -34.462  1.00 72.81           O  
HETATM 2574  O   HOH A 566     -40.037 -12.298 -12.354  1.00 60.73           O  
HETATM 2575  O   HOH A 567     -23.600  20.091 -31.540  1.00 60.68           O  
HETATM 2576  O   HOH A 568     -49.063  -7.756 -13.759  1.00 66.66           O  
HETATM 2577  O   HOH A 569     -46.243  -6.559  -8.384  1.00 69.04           O  
HETATM 2578  O   HOH A 570     -31.063   1.326 -34.991  1.00 71.01           O  
HETATM 2579  O   HOH A 571     -47.461  -2.898 -23.048  1.00 69.97           O  
HETATM 2580  O   HOH A 572     -30.458  -1.218 -33.862  1.00 83.29           O  
HETATM 2581  O   HOH A 573     -16.360  15.858 -33.103  1.00 74.27           O  
HETATM 2582  O   HOH A 574     -31.441  -3.426 -32.367  1.00 69.37           O  
HETATM 2583  O   HOH A 575     -43.634  -7.639  -7.641  1.00 58.19           O  
HETATM 2584  O   HOH A 576     -27.103   1.854 -32.038  1.00 74.36           O  
HETATM 2585  O   HOH A 577     -17.779   3.416 -35.703  1.00 89.58           O  
HETATM 2586  O   HOH A 578     -48.051  -6.339  -5.959  1.00 75.72           O  
HETATM 2587  O   HOH A 579     -44.968  -2.460  -1.304  1.00 68.59           O  
HETATM 2588  O   HOH A 580     -33.013   9.573 -31.639  1.00 58.90           O  
HETATM 2589  O   HOH A 581     -45.547  -0.126 -24.684  1.00 69.01           O  
HETATM 2590  O   HOH A 582     -10.358  10.735 -31.641  1.00 82.74           O  
CONECT 2473 2474
CONECT 2474 2473 2475
CONECT 2475 2474 2476
CONECT 2476 2475 2477
CONECT 2477 2476 2478
CONECT 2478 2477 2479
CONECT 2479 2478 2480
CONECT 2480 2479 2481
CONECT 2481 2480 2482
CONECT 2482 2481 2483
CONECT 2483 2482 2484
CONECT 2484 2483 2485
CONECT 2485 2484 2486
CONECT 2486 2485 2487
CONECT 2487 2486 2488
CONECT 2488 2487 2489
CONECT 2489 2488 2490
CONECT 2490 2489 2491
CONECT 2491 2490 2492
CONECT 2492 2491 2493
CONECT 2493 2492
CONECT 2494 2495
CONECT 2495 2494 2496
CONECT 2496 2495 2497
CONECT 2497 2496 2498
CONECT 2498 2497 2499
CONECT 2499 2498 2500
CONECT 2500 2499 2501
CONECT 2501 2500 2502
CONECT 2502 2501 2503
CONECT 2503 2502 2504
CONECT 2504 2503 2505
CONECT 2505 2504 2506
CONECT 2506 2505 2507
CONECT 2507 2506 2508
CONECT 2508 2507 2509
CONECT 2509 2508 2510
CONECT 2510 2509 2511
CONECT 2511 2510 2512
CONECT 2512 2511 2513
CONECT 2513 2512 2514
CONECT 2514 2513
CONECT 2515 2516
CONECT 2516 2515 2517
CONECT 2517 2516 2518
CONECT 2518 2517 2519
CONECT 2519 2518 2520
CONECT 2520 2519 2521
CONECT 2521 2520 2522
CONECT 2522 2521 2523
CONECT 2523 2522 2524
CONECT 2524 2523 2525
CONECT 2525 2524 2526
CONECT 2526 2525 2527
CONECT 2527 2526 2528
CONECT 2528 2527 2529
CONECT 2529 2528 2530
CONECT 2530 2529 2531
CONECT 2531 2530 2532
CONECT 2532 2531 2533
CONECT 2533 2532 2534
CONECT 2534 2533 2535
CONECT 2535 2534
CONECT 2536 2537
CONECT 2537 2536 2538
CONECT 2538 2537 2539
CONECT 2539 2538 2540
CONECT 2540 2539 2541
CONECT 2541 2540 2542
CONECT 2542 2541 2543
CONECT 2543 2542 2544
CONECT 2544 2543 2545
CONECT 2545 2544 2546
CONECT 2546 2545 2547
CONECT 2547 2546 2548
CONECT 2548 2547 2549
CONECT 2549 2548 2550
CONECT 2550 2549 2551
CONECT 2551 2550 2552
CONECT 2552 2551 2553
CONECT 2553 2552 2554
CONECT 2554 2553 2555
CONECT 2555 2554 2556
CONECT 2556 2555
ENDMDL
END